# Patent

## Title
Production of carotenoids in oleaginous yeast and fungi

## Abstract

The present invention provides systems for producing engineered oleaginous yeast or fungi that express retinolic compounds.

## Background
CROSS-REFERENCE TO RELATED APPLICATIONS
This application is a divisional of application Ser. No. 12/443,362, filed Mar. 27, 2009, which is a national phase application under 35 U.S.C. §371 of International Application No. PCT/US2007/021092, filed Sep. 28, 2007, which claims the benefit of U.S. provisional patent application No. 60/848,062, filed Sep. 28, 2006, and which claims the benefit of U.S. provisional patent application No. 60/902,145, filed Feb. 16, 2007. The entire contents of each of these applications are hereby incorporated by reference.


SEQUENCE LISTING
In accordance with 37 CFR 1.52(e)(5), a Sequence Listing in the form of a text file (entitled “2005862-0073_SL.txt,” created on Feb. 18, 2014, and is 329,074 bytes in size) is incorporated herein by reference in its entirety.
BACKGROUND OF THE INVENTION
Carotenoids are organic pigments ranging in color from yellow to red that are naturally produced by certain organisms, including photosynthetic organisms (e.g., plants, algae, cyanobacteria), and some fungi. Carotenoids are responsible for the orange color of carrots, as well as the pink in flamingos and salmon, and the red in lobsters and shrimp. Animals, however, cannot produce carotenoids and must receive them through their diet.
Carotenoid pigments (e.g., β-carotene and astaxanthin) are used industrially as ingredients for food and feed stocks, both serving a nutritional function and enhancing consumer acceptability. For example, astaxanthin is widely used in salmon aquaculture to provide the orange coloration characteristic of their wild counterparts. Some carotenoids are also precursors of vitamin A. Also, carotenoids have antioxidant properties, and may have various health benefits (see, for example, Jyonouchi et al., Nutr. Cancer 16:93, 1991; Giovannucci et al., J. Natl. Cancer Inst. 87:1767, 1995; Miki, Pure Appl. Chem 63:141, 1991; Chew et al., Anticancer Res. 19:1849, 1999; Wang et al., Antimicrob. Agents Chemother. 44:2452, 2000). Some carotenoids such as β-carotene, lycopene, and lutein are currently sold as nutritional supplements.
In general, the biological systems that produce carotenoids are industrially intractable and/or produce the compounds at such low levels that commercial scale isolation is not practicable. Thus, most carotenoids used in industry are produced by chemical synthesis. There is a need for improved biological systems that produce carotenoids. Some efforts have previously been made to genetically engineer certain bacteria or fungi to produce higher levels of carotenoids (see, for example, Misawa et al., J. Biotechnol. 59:169, 1998; Visser et al., FEMS Yeast Research 4:221, 2003). However, improved systems, allowing higher levels of production and greater ease of isolation, are needed.
SUMMARY OF THE INVENTION
The present invention provides improved systems for the biological production of carotenoids and/or retinolic compounds. In one aspect, the invention encompasses the discovery that it is desirable to produce carotenoids and/or retinolic compounds in oleaginous organisms. Without wishing to be bound by any particular theory, the present inventors propose that biological systems may be able to accumulate higher levels of carotenoids and/or retinolic compounds if the compounds are sequestered in lipid bodies. Regardless of whether absolute levels are higher, however, carotenoids and/or retinolic compounds that are accumulated within lipid bodies in oleaginous organisms are readily isolatable through isolation of the lipid bodies.
The present invention therefore provides oleaginous fungi (including, for example, yeast) that produce one or more carotenoids and/or retinolic compounds. The present invention also provides methods of constructing such yeast and fungi, methods of using such yeast and fungi to produce carotenoids and/or retinolic compounds, and methods of preparing carotenoid-containing compositions and/or retinolic compound-containing compositions, such as food or feed additives, or nutritional supplements, using carotenoids and/or retinolic compounds produced in such oleaginous yeast or fungi. In particular, the present invention provides systems and methods for generating yeast and fungi containing one or more oleaginic and/or carotenogenic and/or retinologenic modifications that increase the oleaginicity and/or alter their carotenoid-producing and/or retinolic compound-producing capabilities as compared with otherwise identical organisms that lack the modification(s).
The present invention further encompasses the general recognition that lipid-accumulating systems are useful for the production and/or isolation of lipophilic agents (such as, but not limited to isoprenoids, or isoprenoid-derived compounds such as retinolic compounds, carotenoids, ubiquinones, lanosterol, zymosterol, ergosterol, vitamins (e.g., vitamins A, E, D, K, specifically 7-dehydrocholesterol (provitamin D3), sterols (e.g., squalene), etc.). According to the present invention, it is desirable to engineer organisms to produce such lipophilic agents and/or to accumulate lipid.
Indeed, one aspect of the present invention is the recognition that host cells can be engineered to accumulate in lipid bodies any of a variety of hydrophilic and/or fat soluble compounds (e.g., retinolic compounds, carotenoids, ubiquinones, vitamins, squalene, etc.) having negligible solubility in water (whether hot or cold) and an appropriate solubility in oil. In some embodiments of the invention, modified host cells are engineered to produce one or more lipophilic agents characterized by negligible solubility in water and detectable solubility in one or more oils. In some embodiments, such lipophilic agents (including, but not limited to carotenoids and/or retinolic compounds) have a solubility in oil below about 0.2%. In some embodiments, such lipophilic agents have a solubility in oil within the range of about <0.001%-0.2%.
The present invention therefore provides engineered host cells (and methods of making and using them) that contain lipid bodies and that further contain one or more compounds accumulated in the lipid bodies, where the compounds are characterized by a negligible solubility in water and a solubility in oil within the range of about <0.001%-0.2%; 0.004%-0.15%; 0.005-0.1%; or 0.005-0.5%. For example, in some embodiments, such lipophilic agents have a solubility in oil below about 0.15%, 0.14%, 0.13%, 0.12%, 0.11%, 0.10%. 0.09, 0.08%, 0.07%, 0.06%, 0.05%, 0.04%, 0.03%, 0.02%, 0.01%, 0.05%, or less. In some embodiments, the lipophilic agents show such solubility in an oil selected from the group consisting of sesame; soybean; apricot kernel; palm; peanut; safflower; coconut; olive; cocoa butter; palm kernel; shea butter; sunflower; almond; avocado; borage; carnauba; hazel nut; castor; cotton seed; evening primrose; orange roughy; rapeseed; rice bran; walnut; wheat germ; peach kernel; babassu; mango seed; black current seed; jojoba; macademia nut; sea buckthorn; sasquana; tsubaki; mallow; meadowfoam seed; coffee; emu; mink; grape seed; thistle; tea tree; pumpkin seed; kukui nut; and mixtures thereof.
In some embodiments, the present invention provides a recombinant fungus. In certain embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one carotenoid and/or retinolic compound, and can accumulate the produced carotenoid and/or retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, which parental fungus both is not oleaginous and does not accumulate the carotenoid and/or retinolic compound to at least about 1% of its dry cell weight, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid and/or retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid and/or retinolic compound which the parental fungus does not produce.
In other embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one carotenoid selected from the group consisting of antheraxanthin, adonirubin, adonixanthin, astaxanthin, canthaxanthin, capsorubrin, β-cryptoxanthin, α-carotene, β,ψ-carotene, δ-carotene, ε-carotene, echinenone, 3-hydroxyechinenone, 3′-hydroxyechinenone, γ-carotene, ψ-carotene, 4-keto-γ-carotene, ζ-carotene, α-cryptoxanthin, deoxyflexixanthin, diatoxanthin, 7,8-didehydroastaxanthin, didehydrolycopene, fucoxanthin, fucoxanthinol, isorenieratene, β-isorenieratene, lactucaxanthin, lutein, lycopene, myxobactone, neoxanthin, neurosporene, hydroxyneurosporene, peridinin, phytoene, rhodopin, rhodopin glucoside, 4-keto-rubixanthin, siphonaxanthin, spheroidene, spheroidenone, spirilloxanthin, torulene, 4-keto-torulene, 3-hydroxy-4-keto-torulene, uriolide, uriolide acetate, violaxanthin, zeaxanthin-β-diglucoside, zeaxanthin, a C30 carotenoid, and combinations thereof, and can accumulate the produced carotenoid to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid which the parental fungus does not naturally produce.
In other embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, and combinations thereof, and can accumulate the produced retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one retinolic compound which the parental fungus does not naturally produce.
In some embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one carotenoid and/or retinolic compound, and can accumulate the produced carotenoid and/or retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus is a member of a genus selected from the group consisting of: Aspergillus, Blakeslea, Botrytis, Candida, Cercospora, Cryptococcus, Cunninghamella, Fusarium (Gibberella), Kluyveromyces, Lipomyces, Mortierella, Mucor, Neurospora, Penicillium, Phycomyces, Pichia (Hansenula), Puccinia, Pythium, Rhodosporidium, Rhodotorula, Saccharomyces, Sclerotium, Trichoderma, Trichosporon, Xanthophyllomyces (Phaffia), and Yarrowia; or is a species selected from the group consisting of: Aspergillus terreus, Aspergillus nidulans, Aspergillus niger, Blakeslea trispora, Botrytis cinerea, Candida japonica, Candida pulcherrima, Candida revkaufi, Candida tropicalis, Candida utilis, Cercospora nicotianae, Cryptococcus curvatus, Cunninghamella echinulata, Cunninghamella elegans, Fusarium fujikuroi (Gibberella zeae), Kluyveromyces lactis, Lipomyces starkeyi, Lipomyces lipoferus, Mortierella alpina, Mortierella ramanniana, Mortierella isabellina, Mortierella vinacea, Mucor circinelloides, Neurospora crassa, Phycomyces blakesleanus, Pichia pastoris, Puccinia distincta, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, Rhodotorula graminis, Rhodotorula mucilaginosa, Rhodotorula pinicola, Rhodotorula gracilis, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, Trichosporon cutaneum, Trichosporon pullans, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), and Yarrowia lipolytica, wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid and/or retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid and/or retinolic compound which the parental fungus does not naturally produce.
In other embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one carotenoid selected from the group consisting of antheraxanthin, adonirubin, adonixanthin, astaxanthin, canthaxanthin, capsorubrin, β-cryptoxanthin, α-carotene, β,ψ-carotene, δ-carotene, ε-carotene, echinenone, 3-hydroxyechinenone, 3′-hydroxyechinenone, γ-carotene, ψ-carotene, 4-keto-γ-carotene, ζ-carotene, α-cryptoxanthin, deoxyflexixanthin, diatoxanthin, 7,8-didehydroastaxanthin, didehydrolycopene, fucoxanthin, fucoxanthinol, isorenieratene, β-isorenieratene, lactucaxanthin, lutein, lycopene, myxobactone, neoxanthin, neurosporene, hydroxyneurosporene, peridinin, phytoene, rhodopin, rhodopin glucoside, 4-keto-rubixanthin, siphonaxanthin, spheroidene, spheroidenone, spirilloxanthin, torulene, 4-keto-torulene, 3-hydroxy-4-keto-torulene, uriolide, uriolide acetate, violaxanthin, zeaxanthin-β-diglucoside, zeaxanthin, a C30 carotenoid, and combinations thereof, and can accumulate the produced carotenoid to at least about 1% of its dry cell weight; wherein the recombinant fungus is a member of a genus selected from the group consisting of: Aspergillus, Blakeslea, Botrytis, Candida, Cercospora, Cryptococcus, Cunninghamella, Fusarium (Gibberella), Kluyveromyces, Lipomyces, Mortierella, Mucor, Neurospora, Penicillium, Phycomyces, Pichia (Hansenula), Puccinia, Pythium, Rhodosporidium, Rhodotorula, Saccharomyces, Sclerotium, Trichoderma, Trichosporon, Xanthophyllomyces (Phaffia), and Yarrowia, or is of a species selected from the group consisting of Aspergillus terreus, Aspergillus nidulans, Aspergillus niger, Blakeslea trispora, Botrytis cinerea, Candida japonica, Candida pulcherrima, Candida revkaufi, Candida tropicalis, Candida utilis, Cercospora nicotianae, Cryptococcus curvatus, Cunninghamella echinulata, Cunninghamella elegans, Fusarium fujikuroi (Gibberella zeae), Kluyveromyces lactis, Lipomyces starkeyi, Lipomyces lipoferus, Mortierella alpina, Mortierella ramanniana, Mortierella isabellina, Mortierella vinacea, Mucor circinelloides, Neurospora crassa, Phycomyces blakesleanus, Pichia pastoris, Puccinia distincta, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, Rhodotorula graminis, Rhodotorula mucilaginosa, Rhodotorula pinicola, Rhodotorula gracilis, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, Trichosporon cutaneum, Trichosporon pullans, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), and Yarrowia lipolytica, wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid which the parental fungus does not naturally produce.
In other embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, and combinations thereof, and can accumulate the produced retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus is a member of a genus selected from the group consisting of: Aspergillus, Blakeslea, Botrytis, Candida, Cercospora, Cryptococcus, Cunninghamella, Fusarium (Gibberella), Kluyveromyces, Lipomyces, Mortierella, Mucor, Neurospora, Penicillium, Phycomyces, Pichia (Hansenula), Puccinia, Pythium, Rhodosporidium, Rhodotorula, Saccharomyces, Sclerotium, Trichoderma, Trichosporon, Xanthophyllomyces (Phaffia), and Yarrowia, or is of a species selected from the group consisting of Aspergillus terreus, Aspergillus nidulans, Aspergillus niger, Blakeslea trispora, Botrytis cinerea, Candida japonica, Candida pulcherrima, Candida revkaufi, Candida tropicalis, Candida utilis, Cercospora nicotianae, Cryptococcus curvatus, Cunninghamella echinulata, Cunninghamella elegans, Fusarium fujikuroi (Gibberella zeae), Kluyveromyces lactis, Lipomyces starkeyi, Lipomyces lipoferus, Mortierella alpina, Mortierella ramanniana, Mortierella isabellina, Mortierella vinacea, Mucor circinelloides, Neurospora crassa, Phycomyces blakesleanus, Pichia pastoris, Puccinia distincta, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, Rhodotorula graminis, Rhodotorula mucilaginosa, Rhodotorula pinicola, Rhodotorula gracilis, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, Trichosporon cutaneum, Trichosporon pullans, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), and Yarrowia lipolytica, wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one retinolic compound which the parental fungus does not naturally produce.
In certain embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and the recombinant fungus produces at least one small molecule lipophilic agent selected from the group consisting of retinolic compounds, carotenoids, ubiquinone, vitamin K, vitamin E, squalene, lanosterol, zymosterol, ergosterol, 7-dehydrocholesterol (provitamin D3), and combinations thereof and can accumulate the produced carotenoid and/or retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid and/or retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid and/or retinolic compound which the parental fungus does not naturally produce.
In some embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and the recombinant fungus produces at least one small molecule lipophilic agent characterized by a negligible solubility in water and solubility in oil within the range of about <0.001%-0.2%; 0.004%-0.15%; 0.005-0.1%; or 0.005-0.5%, and combinations thereof and can accumulate the produced small molecule lipophilic agent to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one small molecule lipophilic agent to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one small molecule lipophilic agent which the parental fungus does not naturally produce.
In other embodiments the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and the recombinant fungus produces at least one small molecule lipophilic agent selected from the group consisting of retinolic compounds, carotenoids, ubiquinone, vitamin K, vitamin E, squalene, lanosterol, zymosterol, ergosterol, 7-dehydrocholesterol (provitamin D3), and can accumulate the produced small molecule lipophilic agent to at least about 1% of its dry cell weight; wherein the recombinant fungus is a member of a genus selected from the group consisting of Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodosporidium, Rhodotorula, Trichosporon, Yarrowia, Aspergillus, Botrytis, Cercospora, Fusarium (Gibberella), Kluyveromyces, Neurospora, Penicillium, Pichia (Hansenula), Puccinia, Saccharomyces, Schizosaccharomyces, Sclerotium, Trichoderms, Ustilago, and Xanthophyllomyces (Phaffia) and comprises at least one genetic modification as compared with a parental fungus, wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one small molecule lipophilic agent to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one small molecule lipophilic agent which the parental fungus does not naturally produce.
In some embodiments, the present invention provides a strain of Yarrowia lipolytica comprising one or more modifications selected from the group consisting of an oleaginic modification, a carotenogenic modification, and combinations thereof, such that the strain accumulates from 1% to 15% of its dry cell weight as at least one carotenoid. In some embodiments, the present invention provides a strain of Yarrowia lipolytica comprising one or more modifications selected from the group consisting of an oleaginic modification, a retinologenic modification, and combinations thereof, such that the strain accumulates from 1% to 15% of its dry cell weight as at least one retinolic compound.
In some embodiments, the present invention provides an engineered Y. lipolytica strain that produces β-carotene, the strain containing one or more carotenogenic modifications selected from the group consisting of: increased expression or activity of a Y. lipolytica GGPP synthase polypeptide; expression or activity of a truncated HMG CoA reductase polypeptide; expression or activity of a phytoene dehydrogenase polypeptide; expression or activity of a phytoene synthase/lycopene cyclase polypeptide; increased expression or activity of an FPP synthase polypeptide; increased expression or activity of an IPP isomerase polypeptide; increased expression or activity of an HMG synthase polypeptide; increased expression or activity of a mevalonate kinase polypeptide; increased expression or activity of a phosphomevalonate kinase polypeptide; increased expression or activity of a mevalonate pyrophosphate decarboxylate polypeptide; increased expression or activity of a malic enzyme polypeptide; increased expression or activity of a malate dehydrogenase polypeptide; increased expression or activity of an AMP deaminase polypeptide; increased expression or activity of a glucose 6 phosphate dehydrogenase polypeptide; increased expression or activity of a malate dehydrogenase homolog2 polypeptide; increased expression or activity of a GND1-6-phosphogluconate dehydrogenase polypeptide; increased expression or activity of a isocitrate dehydrogenase polypeptide; increased expression or activity of a IDH2-isocitrate dehydrogenase polypeptide; increased expression or activity of a fructose 1,6 bisphosphatase polypeptide; increased expression or activity of a Erg10-acetoacetyl CoA thiolase polypeptide; increased expression or activity of a ATP citrate lyase subunit 2 polypeptide; increased expression or activity of a ATP citrate lyase subunit 1 polypeptide; decreased expression or activity of a squalene synthase polypeptide; decreased expression or activity of a prenyldiphosphate synthase polypeptide; or decreased expression or activity of a PHB polyprenyltransferase polypeptide; and combinations thereof.
In some embodiments, the present invention provides an engineered Y. lipolytica strain that produces Vitamin A, the strain containing one or more retinologenic modifications selected from the group consisting of: increased expression or activity of a beta-carotene 15,15′-monooxygenase polypeptide; increased expression or activity of a retinol dehydrogenase polypeptide; and combinations thereof.
In some embodiments, the present invention provides an engineered Y. lipolytica strain containing a truncated HMG CoA reductase polypeptide. In some embodiments, the present invention provides an engineered Y. lipolytica strain having increased expression or activity of a GGPP synthase gene. In some embodiments, the present invention provides an engineered Y. lipolytica strain having decreased expression or activity of a squalene synthase polypeptide. In some embodiments, the present invention provides an engineered Y. lipolytica strain containing a heterologous phytoene dehydrogenase (carB) polypeptide and a heterologous phytoene synthase/lycopene cyclase (carRP) polypeptide.
In some embodiments, the present invention provides a genetically modified Y. lipolytica strain comprising an altered activity or expression of one or more enzymes when compared to an unmodified strain, wherein the altered activity or expression of one or more enzymes is selected from the group consisting of: increased activity or expression of a beta-carotene 15,15′-monooxygenase polypeptide; increased activity or expression of a retinol dehydrogenase polypeptide; increased activity or expression of acetyl-CoA thiolase, increased activity or expression of HMG-CoA synthase, increased activity or expression of HMG-CoA reductase, increased activity or expression of mevalonate kinase, increased activity or expression of phosphomevalonate kinase, increased activity or expression of mevalonate PP decarboxylase, decreased activity or expression of acetyl-CoA carboxylase, increased activity or expression of IPP isomerase, increased activity or expression of GPP synthase, increased activity or expression of FPP synthase, increased activity or expression of squalene synthase, decreased activity or expression of squalene synthase, increased activity or expression of GGPP synthase, decreased activity or expression of GGPP synthase, increased activity or expression of glucose-6-phosphate dehydrogenase, increased activity or expression of 6-phosphogluconate dehydrogenase, increased activity or expression of fructose 1,6 bisphosphatase, increased activity or expression of NADH kinase, increased activity or expression of transhydrogenase, and combinations thereof.
In certain embodiments, the present invention provides a genetically modified Candida utilis strain comprising an altered activity or expression of one or more enzymes when compared to an unmodified strain, wherein the altered activity or expression of one or more enzymes is selected from the group consisting of: increased activity or expression of a beta-carotene 15,15′-monooxygenase polypeptide; increased activity or expression of a retinol dehydrogenase polypeptide; increased activity or expression of acetyl-CoA thiolase, increased activity or expression of HMG-CoA synthase, increased activity or expression of HMG-CoA reductase, increased activity or expression of mevalonate kinase, increased activity or expression of phosphomevalonate kinase, increased activity or expression of mevalonate PP decarboxylase, decreased activity or expression of acetyl-CoA carboxylase, increased activity or expression of IPP isomerase, increased activity or expression of GPP synthase, increased activity or expression of FPP synthase, increased activity or expression of squalene synthase, decreased activity or expression of squalene synthase, increased activity or expression of GGPP synthase, decreased activity or expression of GGPP synthase, increased activity or expression of glucose-6-phosphate dehydrogenase, increased activity or expression of 6-phosphogluconate dehydrogenase, increased activity or expression of fructose 1,6 bisphosphatase, increased activity or expression of NADH kinase, increased activity or expression of transhydrogenase, and combinations thereof.
In other embodiments, the present invention provides a genetically modified Saccharomyces cerevisiae strain comprising an altered activity or expression of one or more enzymes when compared to an unmodified strain, wherein the altered activity or expression of one or more enzymes is selected from the group consisting of: increased activity or expression of a beta-carotene 15,15′-monooxygenase polypeptide; increased activity or expression of a retinol dehydrogenase polypeptide; increased activity or expression of acetyl-CoA thiolase, increased activity or expression of HMG-CoA synthase, increased activity or expression of HMG-CoA reductase, increased activity or expression of mevalonate kinase, increased activity or expression of phosphomevalonate kinase, increased activity or expression of mevalonate PP decarboxylase, decreased activity or expression of acetyl-CoA carboxylase, increased activity or expression of IPP isomerase, increased activity or expression of GPP synthase, increased activity or expression of FPP synthase, increased activity or expression of squalene synthase, decreased activity or expression of squalene synthase, increased activity or expression of GGPP synthase, decreased activity or expression of GGPP synthase, increased activity or expression of glucose-6-phosphate dehydrogenase, increased activity or expression of 6-phosphogluconate dehydrogenase, increased activity or expression of fructose 1,6 bisphosphatase, increased activity or expression of NADH kinase, increased activity or expression of transhydrogenase, and combinations thereof.
In some embodiments, the present invention provides a genetically modified Xanthophyllomyces dendrorhous (Phaffia rhodozyma) strain comprising an altered activity or expression of one or more enzymes when compared to an unmodified strain, wherein the altered activity or expression of one or more enzymes is selected from the group consisting of: increased activity or expression of a beta-carotene 15,15′-monooxygenase polypeptide; increased activity or expression of a retinol dehydrogenase polypeptide; increased activity or expression of acetyl-CoA thiolase, increased activity or expression of HMG-CoA synthase, increased activity or expression of HMG-CoA reductase, increased activity or expression of mevalonate kinase, increased activity or expression of phosphomevalonate kinase, increased activity or expression of mevalonate PP decarboxylase, decreased activity or expression of acetyl-CoA carboxylase, increased activity or expression of IPP isomerase, increased activity or expression of GPP synthase, increased activity or expression of FPP synthase, increased activity or expression of squalene synthase, decreased activity or expression of squalene synthase, increased activity or expression of GGPP synthase, decreased activity or expression of GGPP synthase, increased activity or expression of glucose-6-phosphate dehydrogenase, increased activity or expression of 6-phosphogluconate dehydrogenase, increased activity or expression of fructose 1,6 bisphosphatase, increased activity or expression of NADH kinase, increased activity or expression of transhydrogenase, and combinations thereof.
In other embodiments, the present invention provides a method of producing a carotenoid, the method comprising steps of cultivating a fungus under conditions that allow production of the carotenoid; and isolating the produced carotenoid. In other embodiments, the present invention provides a method of producing a retinolic compound, the method comprising steps of cultivating a fungus under conditions that allow production of the retinolic compound; and isolating the produced retinolic compound.
In certain embodiments, the present invention provides an isolated carotenoid composition, prepared by a method comprising steps of cultivating the fungus under conditions that allow production of a carotenoid; and isolating the produced carotenoid. In certain embodiments, the present invention provides an isolated retinolic compound composition, prepared by a method comprising steps of cultivating the fungus under conditions that allow production of a retinolic compound; and isolating the produced retinolic compound.
In other embodiments, the present invention provides a composition comprising lipid bodies; at least one carotenoid compound; and intact fungal cells. In other embodiments, the present invention provides a composition comprising lipid bodies; at least one retinolic compound; and intact fungal cells.
In some embodiments, the present invention provides a composition comprising: an oil suspension comprising: lipid bodies; at least one carotenoid compound; intact fungal cells; and a binder or filler. In some embodiments, the present invention provides a composition comprising: an oil suspension comprising: lipid bodies; at least one retinolic compound; intact fungal cells; and a binder or filler.
In certain embodiments, the present invention provides a composition comprising: an oil suspension comprising: lipid bodies; at least one carotenoid compound; intact fungal cells; and one or more other agents selected from the group consisting of chelating agents, pigments, salts, surfactants, moisturizers, viscosity modifiers, thickeners, emollients, fragrances, preservatives, and combinations thereof. In certain embodiments, the present invention provides a composition comprising: an oil suspension comprising: lipid bodies; at least one retinolic compound; intact fungal cells; and one or more other agents selected from the group consisting of chelating agents, pigments, salts, surfactants, moisturizers, viscosity modifiers, thickeners, emollients, fragrances, preservatives, and combinations thereof.
In some embodiments, the present invention provides a feedstuff comprising a carotenoid in lipid bodies. In other embodiments, the present invention provides a feedstuff comprising a carotenoid in lipid bodies; wherein the carotenoid is selected from the group consisting of astaxanthin, β-carotene, canthaxanthin, zeaxanthin, lutein, lycopene, echinenone, β-cryptoxanthin and combinations thereof. In some embodiments, the present invention provides a feedstuff comprising a retinolic compound in lipid bodies. In other embodiments, the present invention provides a feedstuff comprising a retinolic compound in lipid bodies; wherein the retinolic compound is selected from the group consisting of retinol, retainal, retinoic acid, and combinations thereof.
In certain embodiments, the present invention provides a carotenoid composition comprising a Y. lipolytica cell containing at least 1% carotenoids by weight. In other embodiments, the present invention provides a carotenoid composition comprising Y. lipolytica lipid bodies; and at least one carotenoid compound, wherein the at least one carotenoid compound is present at a level that is at least 1% by weight of the lipid bodies. In certain embodiments, the present invention provides a retinolic compound composition comprising a Y. lipolytica cell containing at least 1% retinolic compounds by weight. In other embodiments, the present invention provides a retinolic compound composition comprising Y. lipolytica lipid bodies; and at least one retinolic compound, wherein the at least one retinolic compound is present at a level that is at least 1% by weight of the lipid bodies.
Additional aspects of the present invention will be apparent to those of ordinary skill in the art from the present description, including the appended claims.



BRIEF DESCRIPTION OF THE DRAWING
FIG. 1A-1D depicts certain common carotenoids.
FIG. 2 depicts how sufficient levels of acetyl-CoA and NADPH may be accumulated in the cytosol of oleaginous organisms to allow for production of significant levels of cytosolic lipids. Enzymes: 1, pyruvate decarboxylase; 2, malate dehydrogenase; 3, malic enzyme; 4, pyruvate dehydrogenase; 5, citrate synthase; 6, ATP-citrate lyase; 7, citrate/malate translocase.
FIGS. 3A and 3B depict the mevalonate isoprenoid biosynthesis pathway, which typically operates in eukaryotes, including fungi.
FIG. 4 depicts the mevalonate-independent isoprenoid biosynthesis pathway, also known as the DXP pathway, which typically operates in bacteria and in the plastids of plants.
FIG. 5 depicts intermediates in the isoprenoid biosynthesis pathway and how they feed into biosynthetic pathways of other biomolecules, including carotenoids as well as non-carotenoid compounds such as sterols, steroids, and vitamins, such as vitamin E or vitamin K.
FIGS. 6A-6D illustrate various carotenoid biosynthetic pathways. FIG. 6A highlights branches leading to various cyclic and acyclic xanthophylls; FIG. 6B shows certain X dendrorhous pathways that generate dicyclic and monocyclic carotenoids, including astaxanthin; FIG. 6C shows interconnecting pathways for converting β-carotene into any of a variety of other carotenoids, including astaxanthin; FIG. 6D depicts possible routes of synthesis of cyclic carotenoids and common plant and algal xanthophylls from neurosporene.
FIG. 7 and subparts FIGS. 7A-7I show an alignment of certain representative fungal HMG-CoA reductase polypeptides (SEQ ID NOs 176-182, respectively, in order of appearance). As can be seen, these polypeptides show very high identity across the catalytic region, and also have complex membrane spanning domains. In some embodiments of the invention, these membrane-spanning domains are disrupted or are removed, so that, for example, a hyperactive version of the polypeptide may be produced.
FIGS. 8A-8P depict schematic representations of plasmids generated and described in detail in the exemplification.
FIGS. 9A-E show production characteristics of certain engineered cells according to the present invention. Specifically, Panel A shows β-Carotene and phytoene production by Strain MF760 when grown in glycerol, glucose or olive oil; Panel B shows dry cell weight accumulation of strain MF760 when grown in glycerol, glucose or olive oil; Panel C shows β-Carotene and dry cell weight analysis of strain MF760 when grown in the presence of a combination of olive oil and glucose; Panel D shows canthaxanthin, echinenone and β-carotene production of strain MF840; and Panel E shows canthaxanthin and echinenone production of strain MF838 in a 2 phase feeding protocol.
FIG. 10 is a Table listing certain Y. lipolytica genes representing various polypeptides (e.g., oleaginic and isoprenoid biosynthesis peptides) useful in engineering cells in accordance with the present invention. FIG. 10 discloses SEQ ID NOs 183-218, respectively, in order of appearance.
FIG. 11 depicts the all-trans-retinol (Vitamin A) biosynthesis pathway, starting with beta-carotene as a substrate.
FIGS. 12a-e depict various characteristics of strain ML1011 (MF740 transformed with multiple integrated copies of the X. autotrophicus crtZ gene) grown under different pH conditions. FIG. 12a depicts accumulation of total carotenoid (absorbance units per unit dry cell weight) over the course of the fermentation. FIG. 12b depicts accumulation of zeaxanthin (absorbance units per dry cell weight; AU) over the course of the fermentation. FIG. 12c depicts the fraction of carotenoid as zeaxanthin (AU zeaxanthin/AU total carotenoid) over the course of the fermentation. FIG. 12d depicts carbon dioxide evolution over the course of the fermentation. FIG. 12e depicts biomass accumulation over the course of the fermentation.



DEFINITIONS
Aromatic amino acid biosynthesis polypeptide: The term “aromatic amino acid biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of aromatic amino acids in yeast and/or bacteria through chorismate and the shikimate pathway. For example, as discussed herein, anthranilate synthase, enzymes of the shikimate pathway, chorismate mutase, chorismate synthase, DAHP synthase, and transketolase are all aromatic amino acid biosynthesis polypeptides. Each of these polypeptides is also a ubiquinone biosynthesis polypeptide or a ubiquinone biosynthesis competitor for purposes of the present invention, as production of chorismate is a precursor in the synthesis of para-hydroxybenzoate for the biosynthesis of ubiquinone.
Biosynthesis polypeptide: The term “biosynthesis polypeptide” as used herein (typically in reference to a particular compound or class of compounds), refers to polypeptides involved in the production of the compound or class of compounds. In some embodiments of the invention, biosynthesis polypeptides are synthetic enzymes that catalyze particular steps in a synthesis pathway that ultimately produces a relevant compound. In some embodiments, the term “biosynthesis polypeptide” may also encompass polypeptides that do not themselves catalyze synthetic reactions, but that regulate expression and/or activity of other polypeptides that do so. Biosynthesis polypeptides include, for example, aromatic amino acid biosynthesis polypeptides, C5-9 quinone biosynthesis polypeptides, carotenoid biosynthesis polypeptides, retinolic compound biosynthesis polypeptides, FPP biosynthesis polypeptides, isoprenoid biosynthesis polypeptides, PHB biosynthesis polypeptides, quinone biosynthesis polypeptides, sterol biosynthesis polypeptides, ubiquinone biosynthesis polypeptides, Vitamin D biosynthesis polypeptides, Vitamin E biosynthesis polypeptides, and Vitamin K biosynthesis polypeptides.
C5-9 quinone biosynthesis polypeptide: The term “C5-9 quinone biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of a C5-9 quinone, for example a polyprenyldiphosphate synthase polypeptide. To mention but a few, these include, for example, pentaprenyl, hexaprenyl, heptaprenyl, octaprenyl, and/or solanesyl (nonaprenyl) diphosphate synthase polypeptides (i.e., polypeptides that perform the chemical reactions performed by the pentaprenyl, hexaprenyl, heptaprenyl, octaprenyl, and solanesyl (nonaprenyl) polypeptides, respectively (see also Okada et al., Biochim. Biophys. Acta 1302:217, 1996; Okada et al., J. Bacteriol. 179:5992, 1997). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, C5-9 quinone biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other C5-9 quinone biosynthesis polypeptides.
Carotenogenic modification: The term “carotenogenic modification”, as used herein, refers to a modification of a host organism that adjusts production of one or more carotenoids, as described herein. For example, a carotenogenic modification may increase the production level of one or more carotenoids, and/or may alter relative production levels of different carotenoids. In principle, an inventive carotenogenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of one or more carotenoids in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the carotenogenic modification will comprise a genetic modification, typically resulting in increased production of one or more selected carotenoids. In some embodiments, the carotenogenic modification comprises at least one chemical, physiological, genetic, or other modification; in other embodiments, the carotenogenic modification comprises more than one chemical, physiological, genetic, or other modification. In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic, chemical, and/or physiological modification(s)). In some embodiments, the selected carotenoid is one or more of astaxanthin, β-carotene, canthaxanthin, lutein, lycopene, phytoene, zeaxanthin, and/or modifications of zeaxanthin or astaxanthin (e.g., glucoside, esterified zeaxanthin or astaxanthin). In some embodiments, the selected carotenoid is one or more xanthophylls, and/or a modification thereof (e.g., glucoside, esterified xanthophylls). In certain embodiments, the selected xanthophyll is selected from the group consisting of astaxanthin, lutein, zeaxanthin, lycopene, and modifications thereof. In some embodiments, the selected carotenoid is one or more of astaxanthin, β-carotene, canthaxanthin, lutein, lycopene, and zeaxanthin and/or modifications of zeaxanthin or astaxanthin. In some embodiments, the carotenoid is β-carotene. In some embodiments, the selected carotenoid is astaxanthin. In some embodiments, the selected carotenoid is other than β-carotene.
Carotenogenic polypeptide: The term “carotenogenic polypeptide”, as used herein, refers to any polypeptide that is involved in the process of producing carotenoids in a cell, and may include polypeptides that are involved in processes other than carotenoid production but whose activities affect the extent or level of production of one or more carotenoids, for example by scavenging a substrate or reactant utilized by a carotenoid polypeptide that is directly involved in carotenoid production. Carotenogenic polypeptides include isoprenoid biosynthesis polypeptides, carotenoid biosynthesis polypeptides, and isoprenoid biosynthesis competitor polypeptides, as those terms are defined herein. The term also encompasses polypeptides that may affect the extent to which carotenoids are accumulated in lipid bodies.
Carotenoid: The term “carotenoid” is understood in the art to refer to a structurally diverse class of pigments derived from isoprenoid pathway intermediates. The commitment step in carotenoid biosynthesis is the formation of phytoene from geranylgeranyl pyrophosphate. Carotenoids can be acyclic or cyclic, and may or may not contain oxygen, so that the term carotenoids include both carotenes and xanthophylls. In general, carotenoids are hydrocarbon compounds having a conjugated polyene carbon skeleton formally derived from the five-carbon compound IPP, including triterpenes (C30 diapocarotenoids) and tetraterpenes (C40 carotenoids) as well as their oxygenated derivatives and other compounds that are, for example, C35, C50, C60, C70, C80 in length or other lengths. Many carotenoids have strong light absorbing properties and may range in length in excess of C200. C30 diapocarotenoids typically consist of six isoprenoid units joined in such a manner that the arrangement of isoprenoid units is reversed at the center of the molecule so that the two central methyl groups are in a 1,6-positional relationship and the remaining non-terminal methyl groups are in a 1,5-positional relationship. Such C30 carotenoids may be formally derived from the acyclic C30H42 structure, having a long central chain of conjugated double bonds, by: (i) hydrogenation (ii) dehydrogenation, (iii) cyclization, (iv) oxidation, (v) esterification/glycosylation, or any combination of these processes. C40 carotenoids typically consist of eight isoprenoid units joined in such a manner that the arrangement of isoprenoid units is reversed at the center of the molecule so that the two central methyl groups are in a 1,6-positional relationship and the remaining non-terminal methyl groups are in a 1,5-positional relationship. Such C40 carotenoids may be formally derived from the acyclic C40H56 structure, having a long central chain of conjugated double bonds, by (i) hydrogenation, (ii) dehydrogenation, (iii) cyclization, (iv) oxidation, (v) esterification/glycosylation, or any combination of these processes. The class of C40 carotenoids also includes certain compounds that arise from rearrangements of the carbon skeleton, or by the (formal) removal of part of this structure. More than 600 different carotenoids have been identified in nature; certain common carotenoids are depicted in FIG. 1. Carotenoids include but are not limited to: antheraxanthin, adonirubin, adonixanthin, astaxanthin, canthaxanthin, capsorubrin, β-cryptoxanthin, α-carotene, β-carotene, β,ψ-carotene, δ-carotene, ε-carotene, echinenone, 3-hydroxyechinenone, 3′-hydroxyechinenone, γ-carotene, ψ-carotene, 4-keto-γ-carotene, ζ-carotene, α-cryptoxanthin, deoxyflexixanthin, diatoxanthin, 7,8-didehydroastaxanthin, didehydrolycopene, fucoxanthin, fucoxanthinol, isorenieratene, β-isorenieratene, lactucaxanthin, lutein, lycopene, myxobactone, neoxanthin, neurosporene, hydroxyneurosporene, peridinin, phytoene, rhodopin, rhodopin glucoside, 4-keto-rubixanthin, siphonaxanthin, spheroidene, spheroidenone, spirilloxanthin, torulene, 4-keto-torulene, 3-hydroxy-4-keto-torulene, uriolide, uriolide acetate, violaxanthin, zeaxanthin-β-diglucoside, zeaxanthin, and C30 carotenoids. Additionally, carotenoid compounds include derivatives of these molecules, which may include hydroxy-, methoxy-, oxo-, epoxy-, carboxy-, or aldehydic functional groups. Further, included carotenoid compounds include ester (e.g., glycoside ester, fatty acid ester) and sulfate derivatives (e.g., esterified xanthophylls).
Carotenoid biosynthesis polypeptide: The term “carotenoid biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of one or more carotenoids. To mention but a few, these carotenoid biosynthesis polypeptides include, for example, polypeptides of phytoene synthase, phytoene dehydrogenase (or desaturase), lycopene cyclase, carotenoid ketolase, carotenoid hydroxylase, astaxanthin synthase, carotenoid epsilon hydroxylase, lycopene cyclase (beta and epsilon subunits), carotenoid glucosyltransferase, and acyl CoA:diacylglycerol acyltransferase. In some instances, a single gene may encode a protein with multiple carotenoid biosynthesis polypeptide activities. Representative examples of carotenoid biosynthesis polypeptide sequences are presented in Tables 17a-25. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, carotenoid biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other carotenoid biosynthesis polypeptides.
FPP biosynthesis polypeptides: The term “FPP biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of farnesyl pyrophosphate. As discussed herein, farnesyl pyrophosphate represents the branchpoint between the sterol biosynthesis pathway and the carotenoid and other biosynthesis pathways. One specific example of an FPP biosynthesis polypeptide is FPP synthase. Representative examples of FPP synthase polypeptide sequences are presented in Table 14. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, FPP biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other FPP biosynthesis polypeptides.
Gene: The term “gene”, as used herein, generally refers to a nucleic acid encoding a polypeptide, optionally including certain regulatory elements that may affect expression of one or more gene products (i.e., RNA or protein).
Heterologous: The term “heterologous”, as used herein to refer to genes or polypeptides, refers to a gene or polypeptide that does not naturally occur in the organism in which it is being expressed. It will be understood that, in general, when a heterologous gene or polypeptide is selected for introduction into and/or expression by a host cell, the particular source organism from which the heterologous gene or polypeptide may be selected is not essential to the practice of the present invention. Relevant considerations may include, for example, how closely related the potential source and host organisms are in evolution, or how related the source organism is with other source organisms from which sequences of other relevant polypeptides have been selected. Where a plurality of different heterologous polypeptides are to be introduced into and/or expressed by a host cell, different polypeptides may be from different source organisms, or from the same source organism. To give but one example, in some cases, individual polypeptides may represent individual subunits of a complex protein activity and/or may be required to work in concert with other polypeptides in order to achieve the goals of the present invention. In some embodiments, it will often be desirable for such polypeptides to be from the same source organism, and/or to be sufficiently related to function appropriately when expressed together in a host cell. In some embodiments, such polypeptides may be from different, even unrelated source organisms. It will further be understood that, where a heterologous polypeptide is to be expressed in a host cell, it will often be desirable to utilize nucleic acid sequences encoding the polypeptide that have been adjusted to accommodate codon preferences of the host cell and/or to link the encoding sequences with regulatory elements active in the host cell. For example, when the host cell is a Yarrowia strain (e.g., Yarrowia lipolytica), it will often be desirable to alter the gene sequence encoding a given polypeptide such that it conforms more closely with the codon preferences of such a Yarrowia strain. In certain embodiments, a gene sequence encoding a given polypeptide is altered to conform more closely with the codon preference of a species related to the host cell. For example, when the host cell is a Yarrowia strain (e.g., Yarrowia lipolytica), it will often be desirable to alter the gene sequence encoding a given polypeptide such that it conforms more closely with the codon preferences of a related fungal strain. Such embodiments are advantageous when the gene sequence encoding a given polypeptide is difficult to optimize to conform to the codon preference of the host cell due to experimental (e.g., cloning) and/or other reasons. In certain embodiments, the gene sequence encoding a given polypeptide is optimized even when such a gene sequence is derived from the host cell itself (and thus is not heterologous). For example, a gene sequence encoding a polypeptide of interest may not be codon optimized for expression in a given host cell even though such a gene sequence is isolated from the host cell strain. In such embodiments, the gene sequence may be further optimized to account for codon preferences of the host cell. Those of ordinary skill in the art will be aware of host cell codon preferences and will be able to employ inventive methods and compositions disclosed herein to optimize expression of a given polypeptide in the host cell.
Host cell: As used herein, the “host cell” is a fungal cell or yeast cell that is manipulated according to the present invention to accumulate lipid and/or to express one or more carotenoids as described herein. A “modified host cell”, as used herein, is any host cell which has been modified, engineered, or manipulated in accordance with the present invention as compared with a parental cell. In some embodiments, the modified host cell has at least one carotenogenic and/or at least one oleaginic modification. In some embodiments, the modified host cell containing at least one oleaginic modification and/or one carotenogenic modification further has at least one sterologenic modification and/or at least one quinonogenic modification. In some embodiments, the parental cell is a naturally occurring parental cell.
Isolated: The term “isolated”, as used herein, means that the isolated entity has been separated from at least one component with which it was previously associated. When most other components have been removed, the isolated entity is “purified” or “concentrated”. Isolation and/or purification and/or concentration may be performed using any techniques known in the art including, for example, fractionation, extraction, precipitation, or other separation.
Isoprenoid biosynthesis competitor: The term “isoprenoid biosynthesis competitor”, as used herein, refers to an agent whose presence or activity in a cell reduces the level of geranylgeranyl diphosphate (GGPP) available to enter the carotenoid biosynthesis pathway. The term “isoprenoid biosynthesis competitor” encompasses both polypeptide and non-polypeptide (e.g., small molecule) inhibitor agents. Those of ordinary skill in the art will appreciate that certain competitor agents that do not act as inhibitors of isoprenoid biosynthesis generally can nonetheless act as inhibitors of biosynthesis of a particular isoprenoid compound. Particular examples of isoprenoid biosynthesis competitor agents act on isoprenoid intermediates prior to GGPP, such that less GGPP is generated (see, for example, FIG. 5). Squalene synthase is but one isoprenoid biosynthesis competitor polypeptide according to the present invention; representative squalene synthase sequences are presented in Table 16. Prenyldiphosphate synthase enzymes and para-hydroxybenzoate (PHB) polyprenyltransferase are yet additional isoprenoid biosynthesis competitor polypeptides according to the present invention; representative prenyldiphosphate synthase enzymes and PHB polyprenyltransferase polypeptides are presented in Tables 29 and 30, respectively. In certain embodiments, one or more polypeptide components of the SAGA complex are isoprenoid biosynthesis competitors according to the present invention. Genes encoding SAGA complex polypeptides are presented in Table 69. In certain embodiments, a polypeptide encoded by these and other SAGA complex genes is an isoprenoid biosynthesis competitor polypeptide according to the present invention. Those of ordinary skill in the art, considering the known metabolic pathways relating to isoprenoid production and/or metabolism (see, for example, FIGS. 3-6 and other Figures and references herein) will readily appreciate a variety of other particular isoprenoid biosynthesis competitors, including isoprenoid biosynthesis polypeptides.
Isoprenoid biosynthesis polypeptide: The term “isoprenoid biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of isoprenoids. For example, as discussed herein, acetoacetyl-CoA thiolase, HMG-CoA synthase, HMG-CoA reductase, mevalonate kinase, phosphomevalonate kinase, mevalonate pyrophosphate decarboxylase, IPP isomerase, FPP synthase, and GGPP synthase, are all involved in the mevalonate pathway for isoprenoid biosynthesis. Each of these proteins is also an isoprenoid biosynthesis polypeptide for purposes of the present invention, and sequences of representative examples of these enzymes are provided in Tables 7-15. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, isoprenoid biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other isoprenoid biosynthesis polypeptides (e.g., of one or more enzymes that participates in isoprenoid synthesis). Thus, for instance, transcription factors that regulate expression of isoprenoid biosynthesis enzymes can be isoprenoid biosynthesis polypeptides for purposes of the present invention. To give but a couple of examples, the S. cerevisae Upc2 and YLR228c genes, and the Y. lipolytica YALI0B00660g gene encode transcription factors that are isoprenoid biosynthesis polypeptides according to certain embodiments of the present invention. For instance, the semidominant upc2-1 point mutant (G888D) exhibits increases sterol levels (Crowley et al. J Bacteriol. 180: 4177-4183, 1998). Corresponding YLR228c mutants have been made and tested (Shianna et al. J Bacteriology 183:830-834, 2001); such mutants may be useful in accordance with the present invention, as may be YALI0B00660g derivatives with corresponding upc2-1 mutation(s).
Isoprenoid pathway: The term “isoprenoid pathway” is understood in the art to refer to a metabolic pathway that either produces or utilizes the five-carbon metabolite isopentyl pyrophosphate (IPP). As discussed herein, two different pathways can produce the common isoprenoid precursor IPP—the “mevalonate pathway” and the “non-mevalonate pathway”. The term “isoprenoid pathway” is sufficiently general to encompass both of these types of pathway. Biosynthesis of isoprenoids from IPP occurs by polymerization of several five-carbon isoprene subunits. Isoprenoid metabolites derived from IPP are of varying size and chemical structure, including both cyclic and acyclic molecules. Isoprenoid metabolites include, but are not limited to, monoterpenes, sesquiterpenes, diterpenes, sterols, and polyprenols such as carotenoids.
Oleaginic modification: The term “oleaginic modification”, as used herein, refers to a modification of a host organism that adjusts the desirable oleaginy of that host organism, as described herein. In some cases, the host organism will already be oleaginous in that it will have the ability to accumulate lipid to at least about 20% of its dry cell weight. It may nonetheless be desirable to apply an oleaginic modification to such an organism, in accordance with the present invention, for example to increase (or, in some cases, possibly to decrease) its total lipid accumulation, or to adjust the types or amounts of one or more particular lipids it accumulates (e.g., to increase relative accumulation of triacylglycerol). In other cases, the host organism may be non-oleaginous (though may contain some enzymatic and regulatory components used in other organisms to accumulate lipid), and may require oleaginic modification in order to become oleaginous in accordance with the present invention. The present invention also contemplates application of oleaginic modification to non-oleaginous host strains such that their oleaginicity is increased even though, even after being modified, they may not be oleaginous as defined herein. In principle, the oleaginic modification may be any chemical, physiological, genetic, or other modification that appropriately alters oleaginy of a host organism as compared with an otherwise identical organism not subjected to the oleaginic modification. In most embodiments, however, the oleaginic modification will comprise a genetic modification, typically resulting in increased production and/or activity of one or more oleaginic polypeptides. In some embodiments, the oleaginic modification comprises at least one chemical, physiological, genetic, or other modification; in other embodiments, the oleaginic modification comprises more than one chemical, physiological, genetic, or other modification. In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic, chemical and/or physiological modification(s)).
Oleaginic polypeptide: The term “oleaginic polypeptide”, as used herein, refers to any polypeptide that is involved in the process of lipid accumulation in a cell and may include polypeptides that are involved in processes other than lipid biosynthesis but whose activities affect the extent or level of accumulation of one or more lipids, for example by scavenging a substrate or reactant utilized by an oleaginic polypeptide that is directly involved in lipid accumulation. For example, as discussed herein, acetyl-CoA carboxylase, pyruvate decarboxylase, isocitrate dehydrogenase, ATP-citrate lyase, malic enzyme, malate dehydrogenase, and AMP deaminase, among other proteins, are all involved in lipid accumulation in cells. In general, reducing the activity of pyruvate decarboxylase or isocitrate dehydrogenase, and/or increasing the activity of acetyl CoA carboxylase, ATP-citrate lyase, malic enzyme, malate dehydrogenase, and/or AMP deaminase is expected to promote oleaginy. Each of these proteins is an oleaginic peptide for the purposes of the present invention, and sequences of representative examples of these enzymes are provided in Tables 1-6, and 30. Other peptides that can be involved in regenerating NADPH may include, for example, 6-phosphogluconate dehydrogenase (gnd); Fructose 1,6 bisphosphatase (fbp); Glucose 6 phosphate dehydrogenase (g6pd); NADH kinase (EC 2.7.1.86); and/or transhydrogenase (EC 1.6.1.1 and 1.6.1.2). Alternative or additional strategies to promote oleaginy may include one or more of the following: (1) increased or heterologous expression of one or more of acyl-CoA:diacylglycerol acyltransferase (e.g., DGA1; YALI0E32769g); phospholipid:diacylglycerol acyltransferase (e.g., LRO1; YALI0E16797g); and acyl-CoA:cholesterol acyltransferase (e.g., ARE genes such as ARE1, ARE2, YALI0F06578g), which are involved in triglyceride synthesis (Kalscheuer et al. Appl Environ Microbiol p. 7119-7125, 2004; Oelkers et al. J Biol Chem 277:8877-8881, 2002; and Sorger et al. J Biol Chem 279:31190-31196, 2004), (2) decreased expression of triglyceride lipases (e.g., TGL3 and/or TGL4; YALI0D17534g and/or YALI0F10010g (Kurat et al. J Biol Chem 281:491-500, 2006); and (3) decreased expression of one or more acyl-coenzyme A oxidase activities, for example encoded by POX genes (e.g. POX1, POX2, POX3, POX4, POX5; YALI0C23859g, YALI0D24750g, YALI0E06567g, YALI0E27654g, YALI0E32835g, YALI0F10857g; see, for example, Mlickova et al. Appl Environ Microbiol 70: 3918-3924, 2004; Binns et al. J Cell Biol 173:719, 2006). Each of these proteins is an oleaginic peptide for the purposes of the present invention, and sequences of representative examples of these enzymes are provided in Tables 31-43 and 45-47.
Oleaginous: The term “oleaginous”, refers to the ability of an organism to accumulate lipid to at least about 20% of its dry cell weight. In certain embodiments of the invention, oleaginous yeast or fungi accumulate lipid to at least about 25% of their dry cell weight. In other embodiments, inventive oleaginous yeast or fungi accumulate lipid within the range of about 20-45% (e.g., about 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, or more) of their dry cell weight. In some embodiments, oleaginous organisms may accumulate lipid to as much as about 70% of their dry cell weight. In some embodiments of the invention, oleaginous organisms may accumulate a large fraction of total lipid accumulation in the form of triacylglycerol. In certain embodiments, the majority of the accumulated lipid is in the form of triacylglycerol. Alternatively or additionally, the lipid may accumulate in the form of intracellular lipid bodies, or oil bodies. In certain embodiments, the present invention utilizes yeast or fungi that are naturally oleaginous. In some aspects, naturally oleaginous organisms are manipulated (e.g., genetically, chemically, or otherwise) so as to further increase the level of accumulated lipid in the organism. In other embodiments, yeast or fungi that are not naturally oleaginous are manipulated (e.g., genetically, chemically, or otherwise) to accumulate lipid as described herein. For example, for the purposes of the present invention, Saccharomyces cerevisiae, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), and Candida utilis are not naturally oleaginous fungi.
PHB polypeptide or PHB biosynthesis polypeptide: The terms “PHB polypeptide” or “PHB biosynthesis polypeptide” as used herein refers to a polypeptide that is involved in the synthesis of para-hydroxybenzoate from chorismate. In prokaryotes and lower eukaryotes, synthesis of para-hydroxybenzoate occurs by the action of chorismate pyruvate lyase. Biosynthesis of para-hydroxybenzoate from tyrosine or phenylalanine occurs through a five-step process in mammalian cells. Lower eukaryotes such as yeast can utilize either method for production of para-hydroxybenzoate. For example, enzymes of the shikimate pathway, chorismate synthase, DAHP synthase, and transketolase are all PHB biosynthesis polypeptides. Each of these polypeptides is also a ubiquinone biosynthesis polypeptide or a ubiquinone biosynthesis competitor polypeptide for purposes of the present invention.
Polypeptide: The term “polypeptide”, as used herein, generally has its art-recognized meaning of a polymer of at least three amino acids. However, the term is also used to refer to specific functional classes of polypeptides, such as, for example, oleaginic polypeptides, carotenogenic polypeptides, isoprenoid biosynthesis polypeptides, carotenoid biosynthesis polypeptides, etc. For each such class, the present specification provides several examples of known sequences of such polypeptides. Those of ordinary skill in the art will appreciate, however, that the term “polypeptide” is intended to be sufficiently general as to encompass not only polypeptides having the complete sequence recited herein (or in a reference or database specifically mentioned herein), but also to encompass polypeptides that represent functional fragments (i.e., fragments retaining at least one activity) of such complete polypeptides. Moreover, those of ordinary skill in the art understand that protein sequences generally tolerate some substitution without destroying activity. Thus, any polypeptide that retains activity and shares at least about 30-40% overall sequence identity, often greater than about 50%, 60%, 70%, or 80%, and further usually including at least one region of much higher identity, often greater than 90% or even 95%, 96%, 97%, 98%, or 99% in one or more highly conserved regions (e.g., isocitrate dehydrogenase polypeptides often share a conserved AMP-binding motif; HMG-CoA reductase polypeptides typically include a highly conserved catalytic domain (see, for example, FIG. 7); acetyl coA carboxylase typically has a carboxyl transferase domain; see, for example, Downing et al., Chem. Abs. 93:484, 1980; Gil et al., Cell 41:249, 1985; Jitrapakdee et al. Curr Protein Pept Sci. 4:217, 2003; U.S. Pat. No. 5,349,126, each of which is incorporated herein by reference in its entirety), usually encompassing at least 3-4 and often up to 20 or more amino acids, with another polypeptide of the same class, is encompassed within the relevant term “polypeptide” as used herein. Other regions of similarity and/or identity can be determined by those of ordinary skill in the art by analysis of the sequences of various polypeptides presented in the Tables herein.
Quinone biosynthesis polypeptide: A “quinone biosynthesis polypeptide”, as that term is used herein, refers to any polypeptide involved in the synthesis of one or more quinone derived compound, as described herein. In particular, quinone biosynthesis polypeptides include ubiquinone biosynthesis polypeptides, C5-9 quinone biosynthesis polypeptides, vitamin K biosynthesis polypeptides, and vitamin E biosynthesis polypeptides.
Quinonogenic modification: The term “quinonogenic modification, as used herein, refers to a modification of a host organism that adjusts production of one or more quinone derived compounds (e.g., ubiquinone, vitamin K compounds, vitamin E compounds, etc.), as described herein. For example, a quinonogenic modification may increase the production level of a particular quinone derived compound, or of a variety of different quinone derived compounds. In some embodiments of the invention, production of a particular quinone derived compound may be increased while production of other quinone derived compounds is decreased. In some embodiments of the invention, production of a plurality of different quinone derived compounds is increased. In principle, an inventive quinonogenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of one or more quinone derived compounds in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the quinonogenic modification will comprise a genetic modification, typically resulting in increased production of one or more quinone derived compounds (e.g., ubiquinone, vitamin K compounds, vitamin E compounds). In some embodiments, the quinonogenic modification comprises at least one chemical, physiological, genetic, or other modification; in other embodiments, the quinonogenic modification comprises more than one chemical, physiological, genetic, or other modification. In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic, chemical and/or physiological modification(s)).
Retinologenic modification: The term “retinologenic modification”, as used herein, refers to a modification of a host organism that adjusts production of one or more retinolic compounds, as described herein. For example, a retinologenic modification may increase the production level of one or more retinolic compounds, and/or may alter relative production levels of different retinolic compounds. In principle, an inventive retinologenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of one or more retinolic compounds in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the retinologenic modification will comprise a genetic modification, typically resulting in increased production of one or more selected retinolic compounds. In some embodiments, the retinologenic modification comprises at least one chemical, physiological, genetic, or other modification; in other embodiments, the retinologenic modification comprises more than one chemical, physiological, genetic, or other modification. In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic, chemical, and/or physiological modification(s)). In some embodiments, the selected retinolic compound is one or more of retinol, retinal, and retinoic acid. In some embodiments, the selected retinolic compound is retinol or esters of retinol, including but not limited to retinyl palmitate or retinyl acetate. In some embodiments, the selected retinolic compound is retinoic acid. In some embodiments, the selected retinolic compound is other than retinol.
Retinologenic polypeptide: The term “retinologenic polypeptide”, as used herein, refers to any polypeptide that is involved in the process of producing retinolic compounds in a cell, and may include polypeptides that are involved in processes other than retinolic compound production but whose activities affect the extent or level of production of one or more retinolic compounds, for example by scavenging a substrate or reactant utilized by a retinologenic polypeptide that is directly involved in retinolic compound production. Retinologenic polypeptides include retinolic compound biosynthesis polypeptides, isoprenoid biosynthesis polypeptides, carotenoid biosynthesis polypeptides, and isoprenoid biosynthesis competitor polypeptides, as those terms are defined herein. The term also encompasses polypeptides that may affect the extent to which retinolic compounds are accumulated in lipid bodies.
Retinolic compounds: The term “retinolic compound” is understood in the art to refer to a structurally similar class of compounds derived from certain carotenoids, collectively referred to as Vitamin A. All forms of Vitamin A have a beta-ionone ring to which an isoprenoid chain is attached. Retinolic compounds include, for example, retinol (the alcohol form), retinal (the aldehyde form), and retinoic acid (the acid form). Many different geometric isomers of retinol, retinal and retinoic acid are possible as a result of either a trans or cis configuration of four of the five double bonds found in the polyene chain. The cis isomers are less stable and can readily convert to the all-trans configuration. Nevertheless, some cis isomers are found naturally and carry out essential functions. For example, the 11-cis-retinal isomer is the chromophore of rhodopsin, the vertebrate photoreceptor molecule. The term retinolic compound also includes esters of retinol such as retinyl palmitate or retinyl acetate. Hydrolysis of retinyl esters results in retinol. Retinal, also known as retinaldehyde, can be reversibly reduced to produce retinol or it can be irreversibly oxidized to produce retinoic acid. The best described active retinoid metabolites are 11-cis-retinal and the all-trans and 9-cis-isomers of retinoic acid.
Retinolic compound biosynthesis polypeptides: The term “retinolic compound biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of one or more retinolic compounds. To mention but a few, these retinolic compound biosynthesis polypeptides include, for example, polypeptides of beta-carotene 15,15′-monooxygenase (also known as beta-carotene dioxygenase) and/or beta-carotene retinol dehydrogenase. In some instances, a single gene may encode a protein with multiple retinolic compound biosynthesis polypeptide activities. Representative examples of retinolic compound biosynthesis polypeptide sequences are presented in Tables 67 and 68. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, retinolic compound biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other retinolic compound biosynthesis polypeptides.
Small Molecule: In general, a small molecule is understood in the art to be an organic molecule that is less than about 5 kilodaltons (Kd) in size. In some embodiments, the small molecule is less than about 3 Kd, 2 Kd, or 1 Kd. In some embodiments, the small molecule is less than about 800 daltons (D), 600 D, 500 D, 400 D, 300 D, 200 D, or 100 D. In some embodiments, small molecules are non-polymeric. In some embodiments, small molecules are not proteins, peptides, or amino acids. In some embodiments, small molecules are not nucleic acids or nucleotides. In some embodiments, small molecules are not saccharides or polysaccharides.
Source organism: The term “source organism”, as used herein, refers to the organism in which a particular polypeptide sequence can be found in nature. Thus, for example, if one or more heterologous polypeptides is/are being expressed in a host organism, the organism in which the polypeptides are expressed in nature (and/or from which their genes were originally cloned) is referred to as the “source organism”. Where multiple heterologous polypeptides are being expressed in a host organism, one or more source organism(s) may be utilized for independent selection of each of the heterologous polypeptide(s). It will be appreciated that any and all organisms that naturally contain relevant polypeptide sequences may be used as source organisms in accordance with the present invention. Representative source organisms include, for example, animal, mammalian, insect, plant, fungal, yeast, algal, bacterial, cyanobacterial, archaebacterial and protozoal source organisms.
Sterol biosynthesis polypeptide: The term “sterol biosynthesis polypeptide”, as used herein, refers to any polypeptide that is involved in the synthesis of one or more sterol compounds. Thus, sterol biosynthesis polypeptides can include isoprenoid biosynthesis polypeptides to the extent that they are involved in production of isopentyl pyrophosphate. Moreover, the term refers to any polypeptide that acts downstream of farnesyl pyrophosphate and in involved in the production of one or more sterol compounds. For example, sterol biosynthesis polypeptides include squalene synthase, which catalyses conversion of farnesyl pyrophosphate to presqualene pyrophosphate, and further catalyzes conversion of presqualene pyrophosphate to squalene, e.g., the enzyme with EC number 2.5.1.21. In some embodiments of the invention, sterol biosynthesis polypeptides further include one or more polypeptides involved in metabolizing squalene into a vitamin D compound. Thus, sterol biosynthesis polypeptides can include one or more of the polypeptides designated by EC number 1.14.99.7, 5.4.99.7, 5.4.99.8, 5.3.3.5, 1.14.21.6, 1.14.15.-, and/or 1.14.13.13, as well as other enzyme polypeptides involved in the sterol biosynthesis pathways. Furthermore, sterol biosynthesis polypeptides can include one or more enzyme polypeptides including, for example, C-14 demethylase (ERG9), squalene monooxygenase (ERG1), 2,3-oxidosqualene-lanosterol synthase (ERG7), C-1 demethylase (ERG11), C-14 reductase (ERG24), C-4 methyloxidase (ERG25), C-4 decarboxylase (ERG26), 3-ketoreductase (ERG27), C-24 methyltransferase (ERG6), Δ8-7 isomerase (ERG2), C-5 desaturase (ERG3), C-22 desaturase (ERG5) and/or C-24 reductase (ERG4) polypeptides, and/or other polypeptides involved in producing one or more vitamin D compounds (e.g., vitamin D2, vitamin D3, or a precursor thereof). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, sterol biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other sterol biosynthesis polypeptides. Thus, for instance, transcription factors that regulate expression of sterol biosynthesis enzymes can be sterol biosynthesis polypeptides for purposes of the present invention. To give but a couple of examples, the S. cerevisiae Upc2 and YLR228c genes, and the Y. lipolytica YALI0B00660g gene encode transcription factors that are sterol biosynthesis polypeptides according to certain embodiments of the present invention. For instance, the semidominant upc2-1 point mutation (G888D) exhibits increased sterol levels (Crowley et al., J. Bacteriol 180:4177-4183, 1998). Corresponding YLR228c mutants have been made and tested (Shianna et al., J Bacteriol 183:830, 2001); such mutants may be useful in accordance with the present invention, as may be YALI0B00660g derivatives with corresponding upc2-1 mutation(s). Representative examples of sterol biosynthesis polypeptide sequences are presented in Tables 53-66. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, sterol biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other sterol biosynthesis polypeptides.
Sterologenic modification: The term “sterologenic modification”, as used herein, refers to a modification of a host organism that adjusts production of one or more sterol compounds (e.g., squalene, lanosterol, zymosterol, ergosterol, 7-dehydrocholesterol (provitamin D3), vitamin D compound(s), etc.), as described herein. For example, a sterologenic modification may increase the production level of a particular sterol compound, or of a variety of different sterol compounds. In some embodiments of the invention, production of a particular sterol compound may be increased while production of other sterol compounds is decreased. In some embodiments of the invention, production of a plurality of different sterol compounds is increased. In principle, an inventive sterologenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of one or more sterol compounds in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the sterologenic modification will comprise a genetic modification, typically resulting in increased production of one or more sterol compounds (e.g., squalene, lanosterol, zymosterol, ergosterol, 7-dehydrocholesterol (provitamin D3) or vitamin D compound(s)). In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic modification and chemical or physiological modification).
Ubiquinone biosynthesis polypeptide: The term “ubiquinone biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of ubiquinone. To mention but a few, these ubiquinone biosynthesis polypeptides include, for example, polypeptides of prenyldiphosphate synthase, PHB-polyprenyltransferase, and O-methyltransferase, as well as C5-9 quinone biosynthesis polypeptides. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, ubiquinone biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other ubiquinone biosynthesis polypeptides.
Ubiquinogenic modification: The term “ubiquinogenic modification”, as used herein, refers to a modification of a host organism that adjusts production of ubiquinone (e.g., CoQ10), as described herein. For example, a ubiquinogenic modification may increase the production level of ubiquinone (e.g., CoQ10), and/or may alter relative levels of ubiquinone and/or ubiquinol. In principle, an inventive ubiquinogenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of ubiquinone (e.g., CoQ10) in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the ubiquinogenic modification will comprise a genetic modification, typically resulting in increased production of ubiquinone (CoQ10).
Vitamin D biosynthesis polypeptide: The term “vitamin D biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of one or more vitamin D compounds. To mention but a few, these include, for example, polypeptides enzymes with EC numbers the 1.14.99.7, 5.4.99.7, 5.4.99.8, 5.3.3.5, and/or 1.14.21.6. They further can include the hydroxylases that convert vitamin D3 to calcitriol (e.g., polypeptides enzymes with EC numbers 1.14.15.- and 1.14.13.13). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, vitamin D biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other vitamin D biosynthesis polypeptides.
Vitamin E biosynthesis polypeptide: The term “vitamin E biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of vitamin E. To mention but a few, these include, for example, tyrA, pds1(hppd), VTE1, HPT1(VTE2), VTE3, VTE4, and/or GGH polypeptides (i.e., polypeptides that perform the chemical reactions performed by tyrA, pds1(hppd), VTE1, HPT1(VTE2), VTE3, VTE4, and/or GGH, respectively). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, vitamin E biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other vitamin E biosynthesis polypeptides.
Vitamin K biosynthesis polypeptide: The term “vitamin K biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of vitamin K. To mention but a few, these include, for example, MenF, MenD, MenC, MenE, MenB, MenA, UbiE, and/or MenG polypeptides (i.e., polypeptides that perform the chemical reactions performed by MenF, MenD, MenC, MenE, MenB, MenA, UbiE, and/or MenG, respectively). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, vitamin K biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other carotenoid biosynthesis polypeptides.
DETAILED DESCRIPTION OF CERTAIN PREFERRED EMBODIMENTS OF THE INVENTION
As noted above, the present invention encompasses the discovery that carotenoids and/or retinolic compounds can desirably be produced in oleaginous yeast and fungi. According to the present invention, strains that both (i) accumulate lipid, often in the form of cytoplasmic oil bodies and typically to at least about 20% of their dry cell weight; and (ii) produce carotenoid(s) and/or retinolic compound(s) at a level at least about 1%, and in some embodiments at least about 3-20%, of their dry cell weight, are generated through manipulation of host cells (i.e., strains, including, e.g., naturally-occurring strains, strains which have been previously modified, etc.). These manipulated host cells are then used to produce carotenoids and/or retinolic compounds, so that carotenoids and/or retinolic compounds that partition into the lipid bodies can readily be isolated.
In general, it will be desirable to balance oleaginy and carotenoid production in inventive cells such that, as soon as a minimum desirable level of oleaginy is achieved, substantially all further carbon which is capable of being utilized and diverted into biosynthesis of products is diverted into a carotenoid and/or retinolic compounds production pathway. In some embodiments of the invention, this strategy involves engineering cells to be oleaginous; in other embodiments, it involves engineering cells to accumulate a higher level of lipid, particularly cytoplasmic lipid, than they would accumulate in the absence of such engineering even though the engineered cells may not become “oleaginous” as defined herein. In other embodiments, the extent to which an oleaginous host cell accumulates lipid is actually reduced so that remaining carbon can be utilized in carotenoid and/or retinolic compound production. According to the present invention, the extent of lipid accumulation in a host cell can be adjusted by modifying the level and/or activity of one or more polypeptides involved in lipid accumulation. Such modification can take the form of genetic engineering and/or exposure to particular growth conditions that induce or inhibit lipid accumulation.
To give but one example of adjustments that could be made to achieve a desired balance between oleaginy and carotenoid and/or retinolic compound production, we note that, while increasing acetyl CoA carboxylase expression (and/or activity) promotes oleaginy, decreasing its expression and/or activity can promote carotenoid and/or retinolic compound production. Those of ordinary skill in the art will appreciate that the expression and/or activity of acetyl CoA carboxylase, or of other polypeptides may be adjusted up or down as desired according to the characteristics of a particular host cell of interest.
We note that engineered cells and processes of using them as described herein may provide one or more advantages as compared with unmodified cells. Such advantages may include, but are not limited to: increased yield (e.g., carotenoid and/or retinolic compound content expressed as either % dry cell weight (mg/mg) or parts per million), titer (g carotenoid/L and/or g retinolic compound/L), specific productivity (mg carotenoid g−1 biomass hour−1 and/or mg retinolic compound g−1 biomass hour−1), and/or volumetric productivity (g carotenoid liter−1 hour−1 and/or g retinolic compound liter−1 hour−1)) of the desired carotenoid and/or retinolic compound (and/or intermediates thereof), and/or decreased formation of undesirable side products (for example, undesirable intermediates).
Thus, for example, the specific productivity for one or more desired carotenoids (e.g. β-carotene, astaxanthin), retinolic compound (e.g., retinol, retinal, retinoic acid), total carotenoids and/or total retinolic compounds may be at or about 0.1, at or about 0.11, at or about 0.12, at or about 0.13, at or about 0.14, at or about 0.15, at or about 0.16, at or about 0.17, at or about 0.18, at or about 0.19, at or about 0.2, at or about 0.21, at or about 0.22, at or about 0.23, at or about 0.24, at or about 0.25, at or about 0.26, at or about 0.27, at or about 0.28, at or about 0.29, at or about 0.3, at or about 0.31, at or about 0.32, at or about 0.33, at or about 0.34, at or about 0.35, at or about 0.36, at or about 0.37, at or about 0.38, at or about 0.39, at or about 0.4, at or about 0.41, at or about 0.42, at or about 0.43, at or about 0.44, at or about 0.45, at or about 0.46, at or about 0.47, at or about 0.48, at or about 0.49, at or about 0.5, at or about 0.51, at or about 0.52, at or about 0.53, at or about 0.54, at or about 0.55, at or about 0.56, at or about 0.57, at or about 0.58, at or about 0.59, at or about 0.6, at or about 0.61, at or about 0.62, at or about 0.63, at or about 0.64, at or about 0.65, at or about 0.66, at or about 0.67, at or about 0.68, at or about 0.69, at or about 0.7, at or about 0.71, at or about 0.72, at or about 0.73, at or about 0.74, at or about 0.75, at or about 0.76, at or about 0.77, at or about 0.78, at or about 0.79, at or about 0.8, at or about 0.81, at or about 0.82, at or about 0.83, at or about 0.84, at or about 0.85, at or about 0.86, at or about 0.87, at or about 0.88, at or about 0.89, at or about 0.9, at or about 0.91, at or about 0.92, at or about 0.93, at or about 0.94, at or about 0.95, at or about 0.96, at or about 0.97, at or about 0.98, at or about 0.99, at or about 1, 1.05, at or about 1.1, at or about 1.15, at or about 1.2, at or about 1.25, at or about 1.3, at or about 1.35, at or about 1.4, at or about 1.45, at or about 1.5, at or about 1.55, at or about 1.6, at or about 1.65, at or about 1.7, at or about 1.75, at or about 1.8, at or about 1.85, at or about 1.9, at or about 1.95, at or about 2 mg g−1 hour−1 or more.
Thus, for example, the volumetric productivity for one or more desired carotenoids (e.g. β-carotenoid, astaxanthin), retinolic compound (e.g., retinol, retinal, retinoic acid), total carotenoids and/or total retinolic compounds may be at or about 0.01, at or about 0.011, at or about 0.012, at or about 0.013, at or about 0.014, at or about 0.015, at or about 0.016, at or about 0.017, at or about 0.018, at or about 0.019, at or about 0.02, at or about 0.021, at or about 0.022, at or about 0.023, at or about 0.024, at or about 0.025, at or about 0.026, at or about 0.027, at or about 0.028, at or about 0.029, at or about 0.03, at or about 0.031, at or about 0.032, at or about 0.033, at or about 0.034, at or about 0.035, at or about 0.036, at or about 0.037, at or about 0.038, at or about 0.039, at or about 0.04, at or about 0.041, at or about 0.042, at or about 0.043, at or about 0.044, at or about 0.045, at or about 0.046, at or about 0.047, at or about 0.048, at or about 0.049, at or about 0.05, at or about 0.051, at or about 0.052, at or about 0.053, at or about 0.054, at or about 0.055, at or about 0.056, at or about 0.057, at or about 0.058, at or about 0.059, at or about 0.06, at or about 0.061, at or about 0.062, at or about 0.063, at or about 0.064, at or about 0.065, at or about 0.066, at or about 0.067, at or about 0.068, at or about 0.069, at or about 0.07, at or about 0.071, at or about 0.072, at or about 0.073, at or about 0.074, at or about 0.075, at or about 0.076, at or about 0.077, at or about 0.078, at or about 0.079, at or about 0.08, at or about 0.081, at or about 0.082, at or about 0.083, at or about 0.084, at or about 0.085, at or about 0.086, at or about 0.087, at or about 0.088, at or about 0.089, at or about 0.09, at or about 0.091, at or about 0.092, at or about 0.093, at or about 0.094, at or about 0.095, at or about 0.096, at or about 0.097, at or about 0.098, at or about 0.099, at or about 0.1, 0.105, at or about 0.110, at or about 0.115, at or about 0.120, at or about 0.125, at or about 0.130, at or about 0.135, at or about 0.14, at or about 0.145, at or about 0.15, at or about 0.155, at or about 0.16, at or about 0.165, at or about 0.17, at or about 0.175, at or about 0.18, at or about 0.185, at or about 0.19, at or about 0.195, at or about 0.20 grams liter−1 hour−1 or more.
Host Cells
Those of ordinary skill in the art will readily appreciate that a variety of yeast and fungal strains exist that are naturally oleaginous or that naturally produce carotenoids. Yeast and fungal strains do not naturally produce retinolic compounds. Any of such strains may be utilized as host strains according to the present invention, and may be engineered or otherwise manipulated to generate inventive oleaginous, carotenoid-producing strains and/or oleaginous, retinolic acid compound-producing strains. Alternatively, strains that naturally are neither oleaginous nor: i) carotenoid-producing and/or ii) retinolic compound-producing may be employed. Furthermore, even when a particular strain has a natural capacity for oleaginy or for carotenoid production, its natural capabilities may be adjusted as described herein, so as to change the production level of lipid, carotenoid and/or retinolic compound. In certain embodiments engineering or manipulation of a strain results in modification of a type of lipid, carotenoid and/or retinolic compound which is produced. For example, a strain may be naturally oleaginous and/or carotenogenic, however engineering or modification of the strain may be employed so as to change the type of lipid which is accumulated and or to change the type of carotenoid which is produced. Additionally or alternatively, naturally oleaginous strain may be engineered to permit retinolic compound production. Moreover, further engineering or modification of the strain may be employed so as to change the type of lipid which is accumulated and/or to change the type of retinolic compound which is produced.
When selecting a particular yeast or fungal strain for use in accordance with the present invention, it will generally be desirable to select one whose cultivation characteristics are amenable to commercial scale production. For example, it will generally (though not necessarily always) be desirable to avoid filamentous organisms, or organisms with particularly unusual or stringent requirements for growth conditions. However, where conditions for commercial scale production can be applied which allow for utilization of filamentous organisms, these may be selected as host cells. In some embodiments of the invention, it will be desirable to utilize edible organisms as host cells, as they may optionally be formulated directly into food or feed additives, or into nutritional supplements, as desired. For ease of production, some embodiments of the invention utilize host cells that are genetically tractable, amenable to molecular genetics (e.g., can be efficiently transformed, especially with established or available vectors; optionally can incorporate and/or integrate multiple genes, for example sequentially; and/or have known genetic sequence; etc), devoid of complex growth requirements (e.g., a necessity for light), mesophilic (e.g., prefer growth temperatures with in the range of about 20-32° C.) (e.g. 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32° C.), able to assimilate a variety of carbon and nitrogen sources and/or capable of growing to high cell density. Alternatively or additionally, various embodiments of the invention utilize host cells that grow as single cells rather than multicellular organisms (e.g., as mycelia).
In general, when it is desirable to utilize a naturally oleaginous organism in accordance with the present invention, any modifiable and cultivatable oleaginous organism may be employed. In certain embodiments of the invention, yeast or fungi of genera including, but not limited to, Blakeslea, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodosporidium, Rhodotorula, Trichosporon, and Yarrowia are employed. In certain particular embodiments, organisms of species that include, but are not limited to, Blakeslea trispora, Candida pulcherrima, C. revkaufi, C. tropicalis, Cryptococcus curvatus, Cunninghamella echinulata, C. elegans, C. japonica, Lipomyces starkeyi, L. lipoferus, Mortierella alpina, M. isabellina, M. ramanniana, M. vinacea, Mucor circinelloides, Phycomyces blakesleanus, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, R. gracilis, R. graminis, R. mucilaginosa, R. pinicola, Trichosporon pullans, T. cutaneum, and Yarrowia lipolytica are used.
Of these naturally oleaginous strains, some also naturally produce carotenoids and some do not; these strains do not naturally produced retinolic compounds. In most cases, only low levels (less than about 0.05% dry cell weight) of carotenoids are produced by naturally-occurring carotenogenic, oleaginous yeast or fungi. Higher levels of β-carotene are sometimes produced, but high levels of other carotenoids are generally not observed.
In general, any organism that is naturally oleaginous and non-carotenoid-producing (e.g., produce less than about 0.05% dry cell weight, do not produce the carotenoid of interest) may be utilized as a host cell in accordance with the present invention. Additionally or alternatively, any organism that is naturally oleaginous and non-retinolic compound-producing (e.g., produce less than about 0.05% dry cell weight, do not produce the retinolic compound of interest) may be utilized as a host cell in accordance with the present invention. For example, introduction of one or more retinologenic modifications (e.g., increased expression of one or more endogenous or heterologous retinologenic polypeptides), in accordance with the present invention, can achieve the goals for retinolic compound production. In some embodiments, the organism is a yeast or fungus from a genus such as, but not limited to, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Pythium, Trichosporon, and Yarrowia; in some embodiments, the organism is of a species including, but not limited to, Mortierella alpina and Yarrowia lipolytica. 
Comparably, the present invention may utilize any naturally oleaginous, carotenoid-producing organism as a host cell. In general, the present invention may be utilized to increase carbon flow into the isoprenoid pathway in naturally carotenoid-producing organisms (particularly for organisms other than Blakeslea and Phycomyces), and/or to shift production from one carotenoid (e.g., β-carotene) to another (e.g., astaxanthin). Introduction of one or more carotenogenic modifications (e.g., increased expression of one or more endogenous or heterologous carotenogenic polypeptides), in accordance with the present invention, can achieve these goals. Additionally or alternatively, the present invention may be utilized to introduce the ability to produce one or more retinolic compounds in such naturally carotenoid-producing host cells.
In certain embodiments of the invention, the utilized oleaginous, carotenoid-producing organism is a yeast or fungus, for example of a genus such as, but not limited to, Blakeslea, Mucor, Phycomyces, Rhodosporidium, and Rhodotorula; in some embodiments, the organism is of a species such as, Mucor circinelloides and Rhodotorula glutinis. 
When it is desirable to utilize strains that are naturally non-oleaginous as host cells in accordance with the present invention, genera of non-oleaginous yeast or fungi include, but are not limited to, Aspergillus, Botrytis, Cercospora, Fusarium (Gibberella), Kluyveromyces, Neurospora, Penicillium, Pichia (Hansenula), Puccinia, Saccharomyces, Sclerotium, Trichoderma, and Xanthophyllomyces (Phaffia); in some embodiments, the organism is of a species including, but not limited to, Candida utilis, Aspergillus nidulans, A. niger, A. terreus, Botrytis cinerea, Cercospora nicotianae, Fusarium fujikuroi (Gibberella zeae), Kluyveromyces lactis, K. lactis, Neurospora crassa, Pichia pastoris, Puccinia distincta, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, and Xanthophyllomyces dendrorhous (Phaffia rhodozyma).
It will be appreciated that the term “non-oleaginous”, as used herein, encompasses both strains that naturally have some ability to accumulate lipid, especially cytoplasmically, but do not do so to a level sufficient to qualify as “oleaginous” as defined herein, as well as strains that do not naturally have any ability to accumulate extra lipid, e.g., extra-membranous lipid. It will further be appreciated that, in some embodiments of the invention, it will be sufficient to increase the natural level of oleaginy of a particular host cell, even if the modified cell does not qualify as oleaginous as defined herein. In some embodiments, the cell will be modified to accumulate at least about 19%, 18%, 17%, 16%, 15%, 14%, 13%, 12%, 11%, 10%, 9%, 8%, 7%, 6%, or 5% in dry cell weight as lipid, so long as the accumulation level is more than that observed in the unmodified parental cell.
As with the naturally oleaginous organisms, some of the naturally non-oleaginous fungi naturally produce carotenoids, whereas others do not; these strains do not naturally produced retinolic compounds. Genera of naturally non-oleaginous fungi that do not naturally produce carotenoids (e.g., produce less than about 0.05% dry cell weight, do not produce a carotenoid or retinolic compound of interest) may desirably be used as host cells in accordance with the present invention include, but are not limited to, Aspergillus, Kluyveromyces, Penicillium, Saccharomyces, and Pichia; species include, but are not limited to, Candida utilis, Aspergillus niger and Saccharomyces cerevisiae. Genera of naturally non-oleaginous fungi that do naturally produce carotenoids or retinolic compounds and that may desirably be used as host cells in accordance with the present invention include, but are not limited to, Botrytis, Cercospora, Fusarium (Gibberella), Neurospora, Puccinia, Sclerotium, Trichoderma, and Xanthophyllomyces (Phaffia); species include, but are not limited to, Xanthophyllomyces dendrorhous (Phaffia rhodozyma).
As discussed above, any of a variety of organisms may be employed as host cells in accordance with the present invention. In certain embodiments of the invention, host cells will be Yarrowia lipolytica cells. Advantages of Y. lipolytica include, for example, tractable genetics and molecular biology, availability of genomic sequence (see, for example. Sherman et al. Nucleic Acids Res. 32 (Database issue):D315-8, 2004), suitability to various cost-effective growth conditions, and ability to grow to high cell density. In addition, Y. lipolytica is naturally oleaginous, such that fewer manipulations may be required to generate an oleaginous, carotenoid-producing and/or retinolic compound-producing Y. lipolytica strain than might be required for other organisms. Furthermore, there is already extensive commercial experience with Y. lipolytica. 
Saccharomyces cerevisiae is also a useful host cell in accordance with the present invention, particularly due to its experimental tractability and the extensive experience that researchers have accumulated with the organism. Although cultivation of Saccharomyces under high carbon conditions may result in increased ethanol production, this can generally be managed by process and/or genetic alterations.
Additional useful hosts include Xanthophyllomyces dendrorhous (Phaffia rhodozyma), which is experimentally tractable and naturally carotenogenic. Xanthophyllomyces dendrorhous (Phaffia rhodozyma) strains can produce several carotenoids, including astaxanthin.
Aspergillus niger and Mortierella alpina accumulate large amounts of citric acid and fatty acid, respectively; Mortierella alpina is also oleaginous.
Neurospora or Gibberella are also useful. They are not naturally oleaginous and tend to produce very low levels of carotenoids, thus extensive modification may be required in accordance with the present invention. Neurospora and Gibberella are considered relatively tractable from an experimental standpoint. Both are filamentous fungi, such that production at commercial scales can be a challenge necessary to overcome in utilization of such strains.
Mucor circinelloides is another available useful species. While its molecular genetics are generally less accessible than are those of some other organisms, it naturally produces β-carotene, thus may require less modification than other species available.
Candida utilis is a further useful species. Although it is not naturally oleaginous and produces little or no carotenoids, it is amenable to genetic manipulation (for example, see Iwakiri et al. (2006) Yeast 23:23-34, Iwakiri et al. (2005) Yeast 2005 22:1079-87, Iwakiri et al. (2005) Yeast 22:1049-60, Rodriquez et al. (1998) Yeast 14:1399-406, Rodriquez et al. (1998) FEMS Microbiol Lett. 165:335-40, and Kondo et al. (1995) J Bacteriol. 177:7171-7) and furthermore is edible.
Molecular genetics can be performed in Blakeslea, though significant effort may be required. Furthermore, cost-effective fermentation conditions can be challenging, as, for example, it may be required that the two mating types are mixed. Fungi of the genus Phycomyces are also possible sources which have the potential to pose fermentation process challenges, and these fungi may be less amenable to manipulate than several other potential host organisms.
Additional useful hosts include strains such as Schizosaccharomyces pombe, Saitoella complicata, and Sporidiobolus ruineniae. 
Those of ordinary skill in the art will appreciate that the selection of a particular host cell for use in accordance with the present invention will also affect, for example, the selection of expression sequences utilized with any heterologous polypeptide to be introduced into the cell, codon bias that can optionally be engineered into any nucleic acid to be expressed in the cell, and will also influence various aspects of culture conditions, etc. Much is known about the different gene regulatory requirements, protein targeting sequence requirements, and cultivation requirements, of different host cells to be utilized in accordance with the present invention (see, for example, with respect to Yarrowia, Barth et al. FEMS Microbiol Rev. 19:219, 1997; Madzak et al. J Biotechnol. 109:63, 2004; see, for example, with respect to Xanthophyllomyces, Verdoes et al. Appl Environ Microbiol 69: 3728-38, 2003; Visser et al. FEMS Yeast Res 4: 221-31, 2003; Martinez et al. Antonie Van Leeuwenhoek. 73(2):147-53, 1998; Kim et al. Appl Environ Microbiol. 64(5):1947-9, 1998; Wery et al. Gene. 184(1):89-97, 1997; see, for example, with respect to Saccharomyces, Guthrie and Fink Methods in Enzymology 194:1-933, 1991). In certain aspects, for example, targeting sequences of the host cell (or closely related analogs) may be useful to include for directing heterologous proteins to subcellular localization. Thus, such useful targeting sequences can be added to heterologous sequence for proper intracellular localization of activity. In other aspects (e.g., addition of mitochondrial targeting sequences), heterologous targeting sequences may be eliminated or altered in the selected heterologous sequence (e.g., alteration or removal of source organism plant chloroplast targeting sequences).
To give but a few specific examples, of promoters and/or regulatory sequences that may be employed in expression of polypeptides according to the present invention, useful promoters include, but are not limited to, the Leu2 promoter and variants thereof (see, for example, see U.S. Pat. No. 5,786,212); the EF1alpha protein and ribosomal protein S7 gene promoters (see, for example, PCT Application WO 97/44470); the Gpm (see US20050014270), Xpr2 (see U.S. Pat. No. 4,937,189), Tef1, Gpd1 (see, for example, US Application 2005-0014270A1), Cam1 (YALI0C24420g), YALI0D16467g, Tef4 (YALI0B12562g), Yef3 (YALI0E13277g), Pox2, Yat1 (see, for example US Application 2005-0130280; PCT Application WO 06/052754), Fba1 (see, for example WO05049805), and/or Gpat (see WO06031937) promoters; the sequences represented by SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, and SEQ ID NO: 12, subsequences thereof, and hybrid and tandem derivatives thereof (e.g., as disclosed in US Application 2004-0146975); the sequences represented by SEQ ID NO: 1, 2, or 3 including fragments (e.g. by 462-1016 and by 197-1016 of SEQ ID NO: 1; by 5-523 of SEQ ID NO:3) and complements thereof (e.g., as disclosed in US patent number http://patft.uspto.gov/netacgi/nph-Parser?Sect1=PTO1&Sect2=HITOFF&d=PALL&p=1&u=%2Fnetahtml%2FPTO%2Fsrchnum.htm&r=1&f=G&1=50&s1=5952195.PN.&OS=PN/5952195&RS=PN/5952195-h0#h0http://patft.uspto.gov/netacgi/nph-Parser?Sect1=PTO1&Sect2=HITOFF&d=PALL&p=1&u=%2Fnetahtml%2FPTO%2Fsrchnum.htm&r=1&f=G&1=50&s1=5952195.PN.&OS=PN/5952195&RS=PN/5952195-h2#h25,952,195); CYP52A2A (see, for example, US Application 2002-0034788); promoter sequences from fungal (e.g., C. tropicalis) catalase, citrate synthase, 3-ketoacyl-CoA thiolase A, citrate synthase, O-acetylhornserine sulphydrylase, protease, carnitine O-acetyltransferase, hydratase-dehydrogenase, epimerase genes; promoter sequences from Pox4 genes (see, for example, US application 2004-0265980); and/or promoter sequences from Met2, Met3, Met6, Met25 and YALI0D12903g genes. Any such promoters can be used in conjunction with endogenous genes and/or heterologous genes for modification of expression patterns of endogenous polypeptides and/or heterologous polypeptides in accordance with the present invention.
Alternatively or additionally, regulatory sequences useful in accordance with the present invention may include one or more Xpr2 promoter fragments, for example as described in US patent http://patft.uspto.gov/netacgi/nph-Parser?Sect1=PTO1&Sect2=HITOFF&d=PALL&p=1&u=%2Fnetahtml%2FPTO%2Fsrchnum.htm&r=1&f=G&1=50&s1=6083717.PN.&OS=PN/6083717&RS=PN/6083717-h0#h0http://patft.uspto.gov/netacgi/nph-Parser?Sect1=PTO1&Sect2=HITOFF&d=PALL&p=1&u=%2Fnetahtml%2FPTO%2Fsrchnum.htm&r=1&f=G&1=50&s1=6083717.PN.&OS=PN/6083717&RS=PN/6083717-h2#h26,083,717 (e.g. SEQ ID NOS: 1-4 also including sequences with 80% or more identity to these SEQ ID NOs) (e.g., see Example 11) in one or more copies either in single or in tandem. Similarly, exemplary terminator sequences include, but are not limited to, Y. lipolytica Xpr2 (see U.S. Pat. No. 4,937,189) and Pox2 (YALI0F10857g) terminator sequences.
In some embodiments of this invention, it may be desirable to fused sequences encoding specific targeting signals to bacterial source genes. For example, in certain embodiments mitochondrial signal sequences are useful in conjunction with, e.g., bacterial polypeptides for effective targeting of polypeptides for proper functioning. Mitochondrial signal sequences are known in the art, and include, but are not limited to example, mitochondrial signal sequences provided in Table 52 below. In other embodiments, it may be desirable to utilize genes from other source organisms such as animals, plants, alga, or microalgae, fungi, yeast, insect, protozoa, and mammals.







TABLE 52







Examples of mitochondrial targeting sequences.











Protein




Species
(residues)
GI
Sequence





Yarrowia
NUAM
6689648
MLSRNLSKFARAGLIRPATTSTHTRLFSVSARRL


lipoylitica
(AA 1-34)

(SEQ ID NO: 171)


 


Yarrowia
NUHM
50549567
MLRLIRPRLAALARPTTRAPQALNARTHIVSV


lipoylitica
(AA 1-32)

(SEQ ID NO: 172)


 


Saccharomyces
Coq1
536190
MFQRSGAAHHIKLISSRRCRFKSSFAVALNAA


cerevisiae
(AA 1-53)

SKLVTPKILWNNPISLVSKEM 





(SEQ ID NO: 173)


 


Yarrowia
Coq1
60389562
MLRVGRIGTKTLASSSLRFVAGARPKSTLTEA


lipoylitica
(AA 1-77)

VLETTGLLKTTPQNPEWSGAVKQASRLVETD













TPIRDPFSIVSQEM (SEQ ID NO: 174)









Engineering Oleaginy

All living organisms synthesize lipids for use in their membranes and various other structures. However, most organisms do not accumulate in excess of about 10% of their dry cell weight as total lipid, and most of this lipid generally resides within cellular membranes.
Significant biochemical work has been done to define the metabolic enzymes necessary to confer oleaginy on microorganisms (primarily for the purpose of engineering single cell oils as commercial sources of arachidonic acid and docosahexaenoic acid; see for example Ratledge Biochimie 86:807, 2004, the entire contents of which are incorporated herein by reference). Although this biochemical work is compelling, there only have been a limited number of reports of de novo oleaginy being established through genetic engineering with the genes encoding the key metabolic enzymes. It should be noted that oleaginous organisms typically accumulate lipid only when grown under conditions of carbon excess and nitrogen limitation. The present invention further establishes that the limitation of other nutrients (e.g. phosphate and/or magnesium) can also induce lipid accumulation. The present invention establishes, for example, that limitation of nutrients such as phosphate and/or magnesium can induce lipid accumulation, much as is observed under conditions of nitrogen limitation. Under these conditions, the organism readily depletes the limiting nutrient but continues to assimilate the carbon source. The “excess” carbon is channeled into lipid biosynthesis so that lipids (usually triacylglycerols) accumulate in the cytosol, typically in the form of bodies. It should be noted that oleaginous organisms typically only accumulate lipid when grown under conditions of carbon excess and nitrogen or other nutrient limitation (e.g. phosphate or magnesium). Under these conditions, the organism readily depletes the limiting nutrient but continues to assimilate the carbon source. The “excess” carbon is channeled into lipid biosynthesis so that lipids (usually triacylglycerols) accumulate in the cytosol, typically in the form of bodies.
In general, it is thought that, in order to be oleaginous, an organism must produce both acetyl-CoA and NADPH in the cytosol, which can then be utilized by the fatty acid synthase machinery to generate lipids. In at least some oleaginous organisms, acetyl-CoA is generated in the cytosol through the action of ATP-citrate lyase, which catalyzes the reaction:

citrate+CoA+ATP→acetyl-CoA+oxaloacetate+ADP+Pi.  (1)

Of course, in order for ATP-citrate lyase to generate appropriate levels of acetyl-CoA in the cytosol, it must first have an available pool of its substrate citric acid. Citric acid is generated in the mitochondria of all eukaryotic cells through the tricarboxylic acid (TCA) cycle, and can be moved into the cytosol (in exchange for malate) by citrate/malate translocase.
In most oleaginous organisms, and in some non-oleaginous organisms, the enzyme isocitrate dehydrogenase, which operates as part of the TCA cycle in the mitochondria, is strongly AMP-dependent. Thus, when AMP is depleted from the mitochondria, this enzyme is inactivated. When isocitrate dehydrogenase is inactive, isocitrate accumulates in the mitochondria. This accumulated isocitrate is then equilibrated with citric acid, presumably through the action of aconitase. Therefore, under conditions of low AMP, citrate accumulates in the mitochondria. As noted above, mitochondrial citrate is readily transported into the cytosol.
AMP depletion, which in oleaginous organisms is believed to initiate the cascade leading to accumulation of citrate (and therefore acetyl-CoA) in the cytoplasm, occurs as a result of the nutrient depletion mentioned above. When oleaginous cells are grown in the presence of excess carbon source but under conditions limiting for nitrogen or some other nutrient(s) (e.g., phosphate or magnesium), the activity of AMP deaminase, which catalyzes the reaction:

AMP→inosine 5′-monophosphate+NH3  (2)

is strongly induced. The increased activity of this enzyme depletes cellular AMP in both the cytosol and the mitochondria. Depletion of AMP from the mitochondria is thought to inactivate the AMP-dependent isocitrate dehydrogenase, resulting in accumulation of citrate in the mitochondria and, therefore, the cytosol. This series of events is depicted diagrammatically in FIG. 2.

As noted above, oleaginy requires both cytosolic acetyl-CoA and cytosolic NADPH. It is believed that, in many oleaginous organisms, appropriate levels of cytosolic NADPH are provided through the action of malic enzyme (Enzyme 3 in FIG. 2). Some oleaginous organisms (e.g., Lipomyces and some Candida) do not appear to have malic enzymes, however, so apparently other enzymes can provide comparable activity, although it is expected that a dedicated source of NADPH is probably required for fatty acid synthesis (see, for example, Wynn et al., Microbiol 145:1911, 1999; Ratledge Adv. Appl. Microbiol. 51:1, 2002, each of which is incorporated herein by reference in its entirety).
Other activities which can be involved in regenerating NADPH include, for example, 6-phosphogluconate dehydrogenase (gnd); Fructose 1,6 bisphosphatase (fbp); Glucose 6 phosphate dehydrogenase (g6pd); NADH kinase (EC 2.7.1.86); and/or transhydrogenase (EC 1.6.1.1 and 1.6.1.2).
Gnd is part of the pentose phosphate pathway and catalyses the reaction:

6-phospho-D-gluconate+NADP+→D-ribulose 5-phosphate+CO2+NADPH

    Fbp is a hydrolase that catalyses the gluconeogenic reaction:

D-fructose 1,6-bisphosphate+H2O→D-fructose 6-phosphate+phosphate

Fbp redirects carbon flow from glycolysis towards the pentose phosphate pathway. The oxidative portion of the pentose phosphate pathway, which includes glucose 6 phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, enables the regeneration of NADPH. G6pd is part of the pentose phosphate pathway and catalyses the reaction:

D-glucose 6-phosphate+NADP+→D-glucono-1,5-lactone 6-phosphate+NADPH+H+NADH

    kinase catalyzes the reaction:

ATP+NADH→ADP+NADPH



Transhydrogenase catalyzes the reaction:

NADPH+NAD+⇄NADP++NADH

Thus, enhancing the expression and/or activity of any of these enzymes can increase NADPH levels and promote anabolic pathways requiring NADPH.

Alternative or additional strategies to promote oleaginy may include one or more of the following: (1) increased or heterologous expression of one or more of acyl-CoA:diacylglycerol acyltransferase (e.g., DGA1; YALI0E32769g); phospholipid:diacylglycerol acyltransferase (e.g., LRO1; YALI0E16797g); and acyl-CoA:cholesterol acyltransferase (e.g., ARE genes such as ARE1, ARE2, YALI0F06578g), which are involved in triglyceride synthesis (Kalscheuer et al. Appl Environ Microbiol p. 7119-7125, 2004; Oelkers et al. J Biol Chem 277:8877-8881, 2002; and Sorger et al. J Biol Chem 279:31190-31196, 2004), (2) decreased expression of triglyceride lipases (e.g., TGL3 and/or TGL4; YALI0D17534g and/or YALI0F10010g (Kurat et al. J Biol Chem 281:491-500, 2006); and (3) decreased expression of one or more acyl-coenzyme A oxidase activities, for example encoded by POX genes (e.g. POX1, POX2, POX3, POX4, POX5; YALI0C23859g, YALI0D24750g, YALI0E06567g, YALI0E27654g, YALI0E32835g, YALI0F10857g; see for example Mlickova et al. Appl Environ Microbiol 70: 3918-3924, 2004; Binns et al. J Cell Biol 173:719, 2006).
Thus, according to the present invention, the oleaginy of a host organism may be enhanced by modifying the expression or activity of one or more polypeptides involved in generating cytosolic acetyl-CoA and/or NADPH and/or altering lipid levels through other mechanisms. For example, modification of the expression or activity of one or more of acetyl-CoA carboxylase, pyruvate decarboxylase, isocitrate dehydrogenase, ATP-citrate lyase, malic enzyme, AMP-deaminase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, fructose 1,6 bisphosphatase, NADH kinase, transhydrogenase, acyl-CoA:diacylglycerol acyltransferase, phospholipid:diacylglycerol acyltransferase, acyl-CoA:cholesterol acyltransferase, triglyceride lipase, acyl-coenzyme A oxidase can enhance oleaginy in accordance with the present invention. Exemplary polypeptides which can be utilized or derived so as to enhance oleaginy in accordance with the present invention include, but are not limited to those acetyl-CoA carboxylase, pyruvate decarboxylase, isocitrate dehydrogenase, ATP-citrate lyase, malic enzyme, AMP-deaminase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, fructose 1,6 bisphosphatase, NADH kinase, transhydrogenase, acyl-CoA:diacylglycerol acyltransferase, phospholipid:diacylglycerol acyltransferase, acyl-CoA:cholesterol acyltransferase, triglyceride lipase, acyl-coenzyme A oxidase polypeptides provided in Tables 1-6, and 31-47, respectively.
In some embodiments of the invention, where an oleaginous host cell is employed, enzymes and regulatory components relevant to oleaginy are already in place but could be modified, if desired, by for example altering expression or activity of one or more oleaginic polypeptides and/or by introducing one or more heterologous oleaginic polypeptides. In those embodiments of the invention where a non-oleaginous host cell is employed, it is generally expected that at least one or more heterologous oleaginic polypeptides will be introduced.
The present invention contemplates not only introduction of heterologous oleaginous polypeptides, but also adjustment of expression or activity levels of heterologous or endogenous oleaginic polypeptides, including, for example, alteration of constitutive or inducible expression patterns. In some embodiments of the invention, expression patterns are adjusted such that growth in nutrient-limiting conditions is not required to induce oleaginy. For example, genetic modifications comprising alteration and/or addition of regulatory sequences (e.g., promoter elements, terminator elements) and/or regulatory factors (e.g., polypeptides that modulate transcription, splicing, translation, modification, etc.) may be utilized to confer particular regulation of expression patterns. Such genetic modifications may be utilized in conjunction with endogenous genes (e.g., for regulation of endogenous oleaginic polypeptide(s)); alternatively, such genetic modifications may be included so as to confer regulation of expression of at least one heterologous polypeptide (e.g., oleaginic polypeptide(s)).
In some embodiments, at least one oleaginic polypeptide is introduced into a host cell. In some embodiments of the invention, a plurality (e.g., two or more) of different oleaginic polypeptides is introduced into the same host cell. In some embodiments, the plurality of oleaginic polypeptides contains polypeptides from the same source organism; in other embodiments, the plurality includes polypeptides independently selected from different source organisms.
Representative examples of a variety of oleaginic polypeptides that may be introduced into or modified within host cells according to the present invention, include, but are not limited to, those provided in Tables 1-6, and Tables 31-47. As noted above, it is expected that at least some of these polypeptides (e.g., malic enzyme and ATP-citrate lyase) should desirably act in concert, and possibly together with one or more components of fatty acid synthase, such that, in some embodiments of the invention, it will be desirable to utilize two or more oleaginic polypeptides from the same source organism.
In certain embodiments, the oleaginy of a host organism is enhanced by growing the organism on a carbon source comprising one or more oils. For example, an organism may be grown on a carbon source comprising one or more oils selected from the group consisting of, for example, olive, canola, corn, sunflower, soybean, cottonseed, rapeseed, etc., and combinations thereof. In certain embodiments, the oleaginy of a host organism is enhanced by growing the organism on a carbon source comprising one or more oils in combination with modifying the expression or activity of one or more polypeptides such as any of those described above (e.g., oleaginic polypeptides such as polypeptides involved in generating cytosolic acetyl-CoA and/or NADPH) and/or altering lipid levels through other mechanisms.
In general, source organisms for oleaginic polypeptides to be used in accordance with the present invention include, but are not limited to, Blakeslea, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodosporidium, Rhodotorula, Trichosporon, Yarrowia, Aspergillus, Botrytis, Cercospora, Fusarium (Gibberella), Kluyveromyces, Neurospora, Penicillium, Pichia (Hansenula), Puccinia, Saccharomyces, Sclerotium, Trichoderma, and Xanthophyllomyces (Phaffia). In some embodiments, the source species for acetyl CoA carboxylase, ATP-citrate lyase, malice enzyme and/or AMP deaminase polypeptides include, but are not limited to, Aspergillus nidulans, Cryptococcus neoformans, Fusarium fujikuroi, Kluyveromyces lactis, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Ustilago maydis, and Yarrowia lipolytica; in some embodiments, source species for pyruvate decarboxylase or isocitrate dehydrogenase polypeptides include, but are not limited to Neurospora crassa, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), Aspergillus niger, Saccharomyces cerevisiae, Mucor circinelloides, Rhodotorula glutinis, Candida utilis, Mortierella alpina, and Yarrowia lipolytica. 
Aspergillus niger accumulates large amounts of citric acid, whereas Mortierella alpina and Thraustochytrium sp. accumulate large amounts of fatty acid, respectively; Mortierella alpina and Thraustochytrium are also oleaginous.
To give but one particular example of a host cell engineered to be oleaginous (or at least to accumulate increased levels of lipid) in accordance with the present invention, S. cerevisiae can be engineered to express one or more oleaginic polypeptides, e.g., from heterologous source organisms. In some embodiments, a plurality of different oleaginic polypeptides are expressed, optionally from different source organisms. For instance, in some embodiments, S. cerevisiae cells are engineered to express (and/or to increase expression of) ATP-citrate lyase (e.g., from N. crassa), AMP deaminase (e.g., from S. cerevisiae), and/or malic enzyme (e.g., from M. circinelloides). In other embodiments, Candida utilis and Phaffia rhodozyma can be similarly modified. Modified S. cerevisiae, C. utilis, and P. rhodozyma strains can be further modified as described herein to increase production of one or more carotenoids.
In certain embodiments, host cells are engineered to be oleaginous by introducing one or more oleaginic polypeptides. In general, any oleaginic polypeptide can be introduced into any host cell of the present invention. In certain embodiments, such oleaginic polypeptides are codon-optimized to accommodate the codon preferences of the host cell. In certain embodiments, an oleaginic polypeptide introduced into a host cell is from the same organism as the host cell and/or a related organism. For example, without limitation, the present invention encompasses the recognition that it may be desirable to introduce a fungal oleaginic polypeptide into a fungal host cell (e.g., from the same and/or a related fungal species). In certain embodiments, the host cell is a Y. lipolytica host cell. In certain aspects of such embodiments, a Y. lipolytica oleaginic polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, a S. cerevisiae oleaginic polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, any of a variety of fungal oleaginic polypeptides is introduced into the Y. lipolytica host cell.
Engineering Carotenoid Production
Carotenoids are synthesized from isoprenoid precursors, some of which are also involved in the production of steroids and sterols. The most common isoprenoid biosynthesis pathway, sometimes referred to as the “mevalonate pathway”, is generally depicted in FIG. 3. As shown, acetyl-CoA is converted, via hydroxymethylglutaryl-CoA (HMG-CoA), into mevalonate. Mevalonate is then phosphorylated and converted into the five-carbon compound isopentenyl pyrophosphate (IPP). Following isomerization of IPP into dimethylallyl pyrophosphate (DMAPP), three sequential condensation reactions with additional molecules of IPP generate the ten-carbon molecule geranyl pyrophosphate (GPP), followed by the fifteen-carbon molecule farnesyl pyrophosphate (FPP), and finally the twenty-carbon compound geranylgeranyl pyrophosphate (GGPP).
An alternative isoprenoid biosynthesis pathway, that is utilized by some organisms (particularly bacteria) and is sometimes called the “mevalonate-independent pathway”, is depicted in FIG. 4. This pathway is initiated by the synthesis of 1-deoxy-D-xyloglucose-5-phosphate (DOXP) from pyruvate and glyceraldehyde-3-phosphate. DOXP is then converted, via a series of reactions shown in FIG. 4, into IPP, which isomerizes into DMAPP and is then converted, via GPP and FPP, into GGPP as shown in FIG. 3 and discussed above.
Various proteins involved in isoprenoid biosynthesis have been identified and characterized in a number of organisms. Moreover, various aspects of the isoprenoid biosynthesis pathway are conserved throughout the fungal, bacterial, plant and animal kingdoms. For example, polypeptides corresponding to the acetoacetyl-CoA thiolase, HMG-CoA synthase, HMG-CoA reductase, mevalonate kinase, phosphomevalonate kinase, mevalonate pyrophosphate decarboxylase, IPP isomerase, FPP synthase, and GGPP synthase shown in FIG. 3 have been identified in and isolated from a wide variety of organisms and cells. Representative examples of a wide variety of such polypeptides are provided in Tables 7-15. One or more of the polypeptides selected from those provided in any one of Tables 7-15 may be utilized or derived for use in the methods and compositions in accordance with the present invention.
Alternatively or additionally, modified mevalonate kinase polypeptides that exhibit decreased feedback inhibition properties (e.g. to farnesyl pyrophosphate (FPP)) may be utilized in accordance with the present invention. Such modified mevalonate kinase polypeptides may be of eukaryotic or prokaryotic origin. For example, modified versions of mevalonate kinase polypeptides from animals (including humans), plants, algae, fungi (including yeast), and/or bacteria may be employed; for instance, modified versions of mevalonate kinase polypeptides disclosed in Table 10 herein may be utilized.
Particular examples of modified mevalonate kinase polypeptides include “feedback-resistant mevalonate kinases” disclosed in PCT Application WO 2006/063752. Thus, for example, a modified mevalonate kinase polypeptide may include one or more mutation (s) at one or more amino acid position (s) selected from the group consisting of amino acid positions corresponding to positions 17, 47, 93, 94, 132, 167, 169, 204, and 266 of the amino acid sequence of Paracoccus zeaxanthinifaciens mevalonate kinase as shown in SEQ ID NO: 1 of PCT Application WO 2004/111214. For example, the modified mevalonate kinase polypeptide may contain one or more substitutions at positions corresponding to one or more of I17T, G47D, K93E, V94I, R204H and C266S.
To give but a few specific examples, when a modified mevalonate kinase polypeptide comprises 2 amino acid changes as compared with a parent mevalonate kinase polypeptide, it may comprise changes at positions corresponding to the following positions 132/375,167/169, 17/47 and/or 17/93 of SEQ ID NO: 1 of WO/2004/111214 (e.g. P132A/P375R, R167W/K169Q, I17T/G47D or I17T/K93E); when a modified mevalonate kinase polypeptide comprises 3 amino acid changes as compared with a parent mevalonate kinase, it may comprise changes at positions corresponding to the following positions 17/167/169, 17/132/375, 93/132/375, and/or 17/47/93 of SEQ ID NO: 1 of WO/2004/111214 (e.g., I17T/R167W/K169Q, I17T/P132A/P375R, K93E/P132A/P375R, I17T/R167W/K169H, I17T/R167T/K169M, I17T/R167T/K169Y, I17T/R167F/K169Q, I17T/R167I/K169N, I17T/R167H/K169Y, I17T/G47D/K93E or I17T/G47D/K93Q).
Thus, for example, a modified mevalonate kinase polypeptide may include one or more mutation(s) (particularly substitutions), as compared with a parent mevalonate kinase polypeptide, at one or more amino acid position (s) selected from the group consisting of amino acid positions corresponding to positions 55, 59, 66, 83, 106, 111, 117, 142, 152, 158, 218, 231, 249, 367 and 375 of the amino acid sequence of Saccharomyces cerevisiae mevalonate kinase as shown in SEQ ID NO: 1 of PCT application WO 2006/063752. For example, such corresponding substitutions may comprise one or more of P55L, F59S, N66K, C117S, or I152M. A modified mevalonate kinase may comprise a substitution corresponding to F59S substitution. A modified mevalonate kinase polypeptide comprising 2 amino acid changes as compared with its parent mevalonate kinase polypeptide may, for example, comprise changes at positions corresponding to the following positions 55/117, 66/152, 83/249, 111/375 or 106/218 of to SEQ ID NO: 1 of WO2006/063752 (e.g. P55L/C117S, N66K/1152M, K83E/S249P, H111N/K375N or L106P/S218P). A modified mevalonate kinase may comprise a substitution corresponding to N66K/I152M. A modified mevalonate kinase polypeptide comprising 4 amino acid changes as compared with its parent mevalonate kinase polypeptide may have changes at positions corresponding to one or more of the following positions 42/158/231/367 of SEQ ID NO:1 of WO2006/063752 (e.g. I142N/L158S/L231I/T367S).
According to the present invention, carotenoid production in a host organism may be adjusted by modifying the expression or activity of one or more proteins involved in isoprenoid biosynthesis. In some embodiments, such modification involves introduction of one or more heterologous isoprenoid biosynthesis polypeptides into the host cell; alternatively or additionally, modifications may be made to the expression or activity of one or more endogenous or heterologous isoprenoid biosynthesis polypeptides. Given the considerable conservation of components of the isoprenoid biosynthesis polypeptides, it is expected that heterologous isoprenoid biosynthesis polypeptides will often function even in significantly divergent organisms. Furthermore, should it be desirable to introduce more than one heterologous isoprenoid biosynthesis polypeptide (e.g., more than one version of the same polypeptide and/or more that one different polypeptides), in many cases polypeptides from different source organisms will function together. In some embodiments of the invention, a plurality of different heterologous isoprenoid biosynthesis polypeptides is introduced into the same host cell. In some embodiments, this plurality contains only polypeptides from the same source organism (e.g., two or more sequences of, or sequences derived from, the same source organism); in other embodiments the plurality includes polypeptides independently selected from from different source organisms (e.g., two or more sequences of, or sequences derived from, at least two independent source organisms).
In some embodiments of the present invention that utilize heterologous isoprenoid biosynthesis polypeptides, the source organisms include, but are not limited to, fungi of the genera Blakeslea, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodosporidium, Rhodotorula, Trichosporon, Yarrowia, Aspergillus, Botrytis, Cercospora, Fusarium (Gibberella), Kluyveromyces, Neurospora, Penicillium, Pichia (Hansenula), Puccinia, Saccharomyces, Schizosaccharomyces, Sclerotium, Trichoderms, Ustilago, and Xanthophyllomyces (Phaffia). In certain embodiments, the source organisms are of a species including, but not limited to, Cryptococcus neoformans, Fusarium fujikuroi, Kluyveromyces lactis, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Ustilago maydis, and Yarrowia lipolytica. 
As noted above, the isoprenoid biosynthesis pathway is also involved in the production of non-carotenoid compounds, such as sterols, steroids, and vitamins, such as vitamin E or vitamin K. Proteins that act on isoprenoid biosynthesis pathway intermediates, and divert them into biosynthesis of non-carotenoid compounds are therefore indirect inhibitors of carotenoid biosynthesis (see, for example, FIG. 5, which illustrates points at which isoprenoid intermediates are channeled into other biosynthesis pathways). Such proteins are therefore considered isoprenoid biosynthesis competitor polypeptides. Reductions of the level or activity of such isoprenoid biosynthesis competitor polypeptides are expected to increase carotenoid production in host cells according to the present invention. Additionally or alternatively, since disruption of the SAGA complex component SPT-8 increases carotenoid production (see e.g., Example 16), increased expression or activity of one or more components of the SAGA complex such as, without limitation, the SPT8 gene, may decrease production of carotenoids and/or retinolic compounds. Thus, polypeptides that comprise the SAGA complex can be considered competitor polypeptides in the situation where they decrease production of carotenoids and/or retinolic compounds. Without wishing to be bound by theory, the present invention encompasses the recognition that increased expression or activity of one or more components of the SAGA complex may act as isoprenoid biosynthesis competitors, thus reducing the amount of carotenoid produced. For example, one or more components of the SAGA complex may act on isoprenoid intermediates prior to GGPP, such that less GGPP is generated and available for the carotenoid generation pathway. In such embodiments, it will be understood that the SAGA polypeptide(s) components whose activity or expression is increased functions as isoprenoid biosynthesis competitor polypeptide(s). Thus, for example, one or more of the polypeptides encoded by the genes listed in Table 69 may function as isoprenoid biosynthesis competitor polypeptides. Such SAGA polypeptides can be expressed individually or in combination with one another. In certain embodiments, SAGA isoprenoid biosynthesis competitor polypeptides are expressed (and/or their activity increased) in combination with an increase in expression and/or activity of one or more additional isoprenoid biosynthesis competitor polypeptides, such as, without limitation, those isoprenoid biosynthesis competitor polypeptides listed in Tables 7-15.
In some embodiments of the present invention, production or activity of endogenous isoprenoid biosynthesis competitor polypeptides may be reduced or eliminated in host cells. In some embodiments, this reduction or elimination of the activity of an isoprenoid biosynthesis competitor polypeptide can be achieved by treatment of the host organism with small molecule inhibitors of enzymes of the ergosterol biosynthetic pathway. Enzymes of the ergosterol biosynthetic pathway include, for example, squalene synthase (Erg9), squalene epoxidase (Erg1), 2,3-oxidosqualene-lanosterol cyclase (Erg7), cytochrome P450 lanosterol 14α-demethylase (Erg11), C-14 sterol reductase (Erg24), C-4 sterol methyl oxidase (Erg25), SAM:C-24 sterol methyltransferase (Erg6), C-8 sterol isomerase (Erg2), C-5 sterol desaturase (Erg3), C-22 sterol desaturase (Erg5), and C-24 sterol reductase (Erg4) polypeptides. Each of these enzymes is considered an isoprenoid biosynthesis competitor polypeptide. Regulators of these enzymes may also be considered isoprenoid biosynthesis competitor polypeptides (e.g., the yeast proteins Sut1 (Genbank Accession JC4374 GI:2133159) and Mot3 (Genbank Accession NP_013786 GI:6323715), which may or may not have homologs in other organisms.
In other embodiments, reduction or elimination of the activity of an isoprenoid biosynthesis competitor polypeptide can be achieved by decreasing activity of the ubiquinone biosynthetic pathway. The commitment step in ubiquinone biosynthesis is the formation of para-hydroxybenzoate (PHB) from tyrosine or phenylalanine in mammals or chorismate in bacteria, followed by condensation of PHB and isoprene precursor, resulting in addition of the prenyl group. This reaction is catalyzed by PHB-polyprenyltransferase. The isoprenoid side chain of ubiquinone, which can be of varying length in different organisms, is determined by the prenyldiphosphate synthase enzyme. In organisms that produce the coenzyme Q10 form of ubiquinone, the 3-decaprenyl-4-hydroxybenzoic acid resulting from the condensation of PHB and decaprenyldiphosphate reaction undergoes further modifications, which include hydroxylation, methylation and decarboxylation, in order to form ubiquinone (CoQ10). Thus, reducing the activity of prenyldiphosphate synthase leading from farnesyldiphosphate to extended isoprenoids, or reducing the activity of PHB polyprenyltransferase may be useful in increasing the amount of isoprenoid available for carotenoid biosynthesis. (Examples of prenyldiphosphate synthase and PHB-polyprenyltransferase enzymes are depicted in Tables 29 and 30, respectively).
Known small molecule inhibitors of isoprenoid biosynthesis competitor enzymes include, but are not limited to, zaragosic acid (including analogs thereof such as TAN1607A (Biochem Biophys Res Commun 1996 Feb. 15; 219(2):515-520)), RPR 107393 (3-hydroxy-3-[4-(quinolin-6-yl)phenyl]-1-azabicyclo[2-2-2]octane dihydrochloride; J Pharmacol Exp Ther. 1997 May; 281(2):746-52), ER-28448 (5-{N-[2-butenyl-3-(2-methoxyphenyl)]-N-methylamino}-1,1-pentylidenebis(phosphonic acid) trisodium salt; Journal of Lipid Research, Vol. 41, 1136-1144, July 2000), BMS-188494 (The Journal of Clinical Pharmacology, 1998; 38:1116-1121), TAK-475 (1-[2-[(3R,5S)-1-(3-acetoxy-2,2-dimethylpropyl)-7-chloro-1,2,3,5-tetrahydro-2-oxo-5-(2,3-dimethoxyphenyl)-4,1-benzoxazepine-3-yl]acetyl]piperidin-4-acetic acid; Eur J Pharmacol. 2003 Apr. 11; 466(1-2):155-61), YM-53601 ((E)-2-[2-fluoro-2-(quinuclidin-3-ylidene)ethoxy]-9H-carbazole monohydrochloride; Br J Pharmacol. 2000 September; 131(1):63-70), or squalestatin I that inhibit squalene synthase; terbinafine (e.g., LAMISIL®), naftifine (NAFTIN®), S-allylcysteine, garlic, resveratrol, NB-598 (e.g., from Banyu Pharmaceutical Co), and/or green tea phenols that inhibit squalene epoxidase (see, for example, J. Biol Chem 265:18075, 1990; Biochem. Biophys. Res. Commun. 268:767, 2000); various azoles that inhibit cytochrome P450 lanosterol 14α-demethylase; and fenpropimorph that inhibits the C-14 sterol reductase and the C-8 sterol isomerase. In other embodiments, heterologous isoprenoid biosynthesis competitor polypeptides may be utilized (whether functional or non-functional; in some embodiments, dominant negative mutants are employed).
One particular isoprenoid biosynthesis competitor polypeptide useful according to the present invention is squalene synthase which has been identified and characterized from a variety of organisms; representative examples of squalene synthase polypeptide sequences are included in Table 16. In some embodiments of the invention that utilize squalene synthase (or modifications of squalene synthase) source organisms include, but are not limited to, Neurospora crassa, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), Aspergillus niger, Saccharomyces cerevisiae, Mucor circinelloides, Rhotorula glutinis, Candida utilis, Mortierella alpina, and Yarrowia lipolytica. 
The carotenoid biosynthesis pathway branches off from the isoprenoid biosynthesis pathway at the point where GGPP is formed. The commitment step in carotenoid biosynthesis is the formation of phytoene by the head-to-head condensation of two molecules of GGPP, catalyzed by phytoene synthase (often called crtB; see FIG. 6). A series of dehydrogenation reactions, each of which increases the number of conjugated double bonds by two, converts phytoene into lycopene via neurosporene. The pathway branches at various points, both before and after lycopene production, so that a wide range of carotenoids can be generated. For example, action of a cyclase enzyme on lycopene generates γ-carotene; action of a desaturase instead produces 3,4-didehydrolycopene. γ-carotene is converted to β-carotene through the action of a cyclase. β-carotene can be processed into any of a number of products (see, for example, FIG. 6C), including astaxanthin (via echinenone, hydroxyechinenone, and phoenicoxanthin).
According to the present invention, carotenoid production in a host organism may be adjusted by modifying the expression or activity of one or more proteins involved in carotenoid biosynthesis. As indicated, in some embodiments, it will be desirable to utilize as host cells organisms that naturally produce one or more carotenoids. In some such cases, the focus will be on increasing production of a naturally-produced carotenoid, for example by increasing the level and/or activity of one or more proteins involved in the synthesis of that carotenoid and/or by decreasing the level or activity of one or more proteins involved in a competing biosynthetic pathway. Alternatively or additionally, in some embodiments it will be desirable to generate production of one or more carotenoids not naturally produced by the host cell.
According to some embodiments of the invention, it will be desirable to introduce one or more heterologous carotenogenic polypeptides into a host cell. As will be apparent to those of ordinary skill in the art, any of a variety of heterologous polypeptides may be employed; selection will consider, for instance, the particular carotenoid whose production is to be enhanced. The present invention contemplates not only introduction of heterologous carotenogenic polypeptides, but also adjustment of expression or activity levels of heterologous or endogenous carotenogenic polypeptides, including, for example, alteration of constitutive or inducible expression patterns. In some embodiments of the invention, expression patterns are adjusted such that growth in nutrient-limiting conditions is not required to induce oleaginy. For example, genetic modifications comprising alteration and/or addition of regulatory sequences (e.g., promoter elements, terminator elements) may be utilized to confer particular regulation of expression patterns. Such genetic modifications may be utilized in conjunction with endogenous genes (e.g., for regulation of endogenous carotenogenic); alternatively, such genetic modifications may be included so as to confer regulation of expression of at least one heterologous polypeptide (e.g., carotenogenic polypeptide(s)). For example, promoters including, but not limited to those described herein, such as Tef1, Gpd1 promoters can be used in conjunction with endogenous genes and/or heterolous genes for modification of expression patterns of endogenous carotenogenic polypeptide(s) and/or heterologous carotenogenic polypeptide(s). Similarly, exemplary terminator sequences include, but are not limited to, use of Y. lipolytica XPR2 terminator sequences.
As indicated in FIG. 6 and in the literature, proteins involved in carotenoid biosynthesis include, but are not limited to, phytoene synthase, phytoene dehydrogenase, lycopene cyclase, carotenoid ketolase, carotenoid hydroxylase, astaxanthin synthase (a single multifunctional enzyme found in some source organisms that typically has both ketolase and hydroxylase activities), carotenoid epsilon hydroxylase, lycopene cyclase (beta and epsilon subunits), carotenoid glucosyltransferase, and acyl CoA:diacyglycerol acyltransferase. Representative example sequences for these carotenoid biosynthesis polypeptides are provided in Tables 17a-25.
Alternatively or additionally, modified carotenoid ketolase polypeptides that exhibit improved carotenoid production activity may be utilized in accordance with the present invention. For example, carotenoid ketolase polypeptides comprising one more mutations to corresponding to those identified Sphingomonas sp. DC18 which exhibited improved astaxanthin production (Tao et al. 2006 Metab Eng. 2006 Jun. 27) and Paracoccus sp. strain N81106 which exhibited altered carotenoid production (Ye et al. 2006 Appl Environ Microbiol 72:5829-37).
Xanthophylls can be distinguished from other carotenoids by the presence of oxygen containing functional groups on their cyclic end groups. For instance, lutein and zeaxanthin contain a single hydroxyl group on each of their terminal ring structures, while astaxanthin contains both a keto group and a hydroxyl on each terminal ring. This property makes xanthophylls more polar than carotenes such as beta-carotene and lycopene, and thus dramatically reduces their solubility in fats and lipids. Naturally occurring xanthophylls are often found as esters of the terminal hydroxyl groups, both mono- and diesters of fatty acids. They also occur as glucosides in certain species of bacteria. The solubility and dispersibility of xanthophylls can be greatly modified by the addition of ester moieties, and it is known that esterification can also affect the absorbability and/or bioavailability of a given carotenoid. It is an objective of this invention to maximize the amount of a particular xanthophyll accumulating within the intracellular triacylglyceride fraction of oleaginous yeasts, and one mechanism for achieving this goal is to increase the hydrophobic nature of the xanthophyll product that accumulates. One way of achieving this is to engineer the production of fatty-acyl mono- and/or diesters of the target xanthophyll compound.
A variety of enzymes can function to esterify carotenoids. For example, carotenoid glucosyltransferases have been identified in several bacterial species (see, e.g., Table 24). In addition, acyl CoA:diacyglycerol acyltransferase (DGAT) and acyl CoA:monoacylglycerol acyltransferases (MGAT), which function in the final steps of triacylglycerol biosynthesis, are likely to serve an additional role in the esterification of xanthophylls. Representative DGAT polypeptides are shown in Table 25. Furthermore, other enzymes may specifically modify carotenoids and molecules of similar structure (e.g. sterols) and be available for modification and ester production.
In some embodiments of the invention, potential source organisms for carotenoid biosynthesis polypeptides include, but are not limited to, genera of naturally oleaginous or non-oleaginous fungi that naturally produce carotenoids. These include, but are not limited to, Botrytis, Cercospora, Fusarium (Gibberella), Mucor, Neurospora, Phycomyces, Puccina, Rhodotorula, Sclerotium, Trichoderma, and Xanthophyllomyces. Exemplary species include, but are not limited to, Neurospora crassa, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), Mucor circinelloides, and Rhodotorula glutinis. Of course, carotenoids are produced by a wide range of diverse organisms such as plants, algae, yeast, fungi, bacteria, cyanobacteria, etc. Any such organisms may be source organisms for carotenoid biosynthesis polypeptides according to the present invention.
In certain embodiments of the invention, carotenoid production in a host organism may be adjusted by modifying the activity of one or more endogenous genes that affect carotenoid biosynthesis. For example, as shown in Example 16, disruption of the endogenous SPT8 gene (YALI0E23804g) in Yarrowia lipolytica results in increased carotenoid production. SPT8 functions as part of the SAGA histone acetyltransferase complex, which is required for normal expression of some fungal genes and is thought to function as a coactivator complex in a multistep pathway leading to gene activation. Thus, without wishing to be bound by theory, the present invention encompasses the recognition that alteration of the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex result in increased carotenoid production. Additionally, it will be appreciated by those of ordinary skill in the art that by increasing production of carotenoid(s) in a host organism by altering the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex, production of a retinolic compound(s) in a host organism able to utilize such a carotenoid(s) as a substrate may also be increased since more of the cartenoid substrate will be available.
In Saccharomyces cerevisiae, the SAGA complex is a 1.8-MDa complex comprising a variety of components including distinct classes of transcription factors, such as Ada proteins (Ada1p, Ada2p, Ngg1p/Ada3p, and Ada4p/Gcn5p), TATA-binding protein (TBP)-related SPT proteins (Spt3p, Spt7p, Spt8p, and Spt20p/Ada5p), and TBP-associated factors or (TAFIIs) (TAFII90, TAFII68/61, TAFII60, TAFII25/23, and TAFII17). The SAGA complex also comprises the DNA-dependent protein kinase related molecule Tra1p, acetyltransferase and ubiquitin protease activities. The SAGA complex core comprises Ada and Spt subunits, a subset of Tafs, acetyltransferase and ubiquitin protease activities, the essential factor Tra1p, and two factors related to TBP function, Spt3 and Spt8. Several components of the Saccharomyces cerevisiae SAGA complex and their corresponding Yarrowia lipolytica homologs, are listed in Table 69. Each of these SAGA complex components is encompassed by the recombinant fungal strains, methods and compositions of the present invention. Those of ordinary skill in the art will be aware of these and other SAGA components, and will be able to modify such components in accordance with the present invention.
Certain SAGA components are essential. For example, in Saccharomyces cerevisiae, the TRA1 gene is essential. Thus, in certain embodiments, production of a carotenoid is increased by altering expression and/or activity of the TRA1 such that the host organism remains viable. For example, the expression and/or activity of the TRA1 gene or gene product may be decreased to a level below the expression and/or activity of wild type TRA1, but not to such an extent as to result in lethality. Those of ordinary skill in the art will be aware of tra1 mutations that result in decreased expression and/or activity but that do not result in lethality. Furthermore, it will be within the capability of one of ordinary skill in the art to identify such mutations without undue experimentation, for example by employing standard mutagenesis/screening techniques.
In certain embodiments of the present invention, production of one or more carotenoids is increased by alteration of the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in one or more of the following host organisms: Aspergillus, Blakeslea, Botrytis, Candida, Cercospora, Cryptococcus, Cunninghamella, Fusarium (Gibberella), Kluyveromyces, Lipomyces, Mortierella, Mucor, Neurospora, Penicillium, Phycomyces, Pichia (Hansenula), Puccinia, Pythium, Rhodosporidium, Rhodotorula, Saccharomyces, Sclerotium, Trichoderma, Trichosporon, Xanthophyllomyces (Phaffia), and Yarrowia; or is a species selected from the group consisting of: Aspergillus terreus, Aspergillus nidulans, Aspergillus niger, Blakeslea trispora, Botrytis cinerea, Candida japonica, Candida pulcherrima, Candida revkaufi, Candida tropicalis, Candida utilis, Cercospora nicotianae, Cryptococcus curvatus, Cunninghamella echinulata, Cunninghamella elegans, Fusarium fujikuroi (Gibberella zeae), Kluyveromyces lactis, Lipomyces starkeyi, Lipomyces lipoferus, Mortierella alpina, Mortierella ramanniana, Mortierella isabellina, Mortierella vinacea, Mucor circinelloides, Neurospora crassa, Phycomyces blakesleanus, Pichia pastoris, Puccinia distincta, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, Rhodotorula graminis, Rhodotorula mucilaginosa, Rhodotorula pinicola, Rhodotorula gracilis, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, Trichosporon cutaneum, Trichosporon pullans, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), and/or Yarrowia lipolytica. 
In certain embodiments, production of one or more carotenoids is increased by altering expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in a host organism, in combination with one or more additional carotenogenic modifications as described herein. For example, such one or more additional carotenogenic modifications may comprise heterologous expression of one or more carotenogenic polypeptides, isoprenoid biosynthesis polypeptides, carotenoid biosynthesis polypeptides, etc.
In certain embodiments, production of one or more carotenoids is increased by altering expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in a host organism, in combination with one or more oleaginic modifications, as described herein. In certain embodiments, production of one or more carotenoids is increased by altering expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in a host organism that is not naturally oleaginous. In certain embodiments, production of one or more carotenoids is increased by altering expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in a host organism that is naturally oleaginous.
It will be appreciated that the particular carotenogenic modification to be applied to a host cell in accordance with the present invention will be influenced by which carotenoid(s) is desired to be produced. For example, isoprenoid biosynthesis polypeptides are relevant to the production of most carotenoids. Carotenoid biosynthesis polypeptides are also broadly relevant. Carotenoid ketolase activity is particularly relevant for production of canthaxanthin, as carotenoid hydroxylase activity is for production of lutein and zeaxanthin, among others. Both carotenoid hydroxylase and ketolase activities (and astaxanthin synthase) are particularly useful for production of astaxanthin.
In certain embodiments, host cells are engineered to produce carotenoids by introducing one or more carotenoid biosynthesis polypeptides. In general, any carotenoid biosynthesis polypeptide can be introduced into any host cell of the present invention. In certain embodiments, such carotenoid biosynthesis polypeptides are codon-optimized to accommodate the codon preferences of the host cell. In certain embodiments, a carotenoid biosynthesis polypeptide introduced into a host cell is from the same organism as the host cell and/or a related organism. For example, without limitation, the present invention encompasses the recognition that it may be desirable to introduce a fungal carotenoid biosynthesis polypeptide into a fungal host cell (e.g., from the same and/or a related fungal species). In certain embodiments, the host cell is a Y. lipolytica host cell. In certain aspects of such embodiments, a Y. lipolytica carotenoid biosynthesis polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, a S. cerevisiae carotenoid biosynthesis polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, any of a variety of fungal carotenoid biosynthesis polypeptides is introduced into the Y. lipolytica host cell.
Engineering Retinolic Compound Production
Retinolic compounds are synthesized from certain carotenoid precursors, which are themselves synthesized from isoprenoid precursors, some of which are also involved in the production of steroids and sterols (see description under section entitled “Engineering Carotenoid Production”). Thus, any carotenogenic modification that results in the increased production of a carotenoid from which a retinolic compound can be produced may similarly result in an increased production of a retinolic compound. Retinolic compounds comprise retinol, retinal, and retinoic acid, which together are collectively referred to as “Vitamin A”. In certain embodiments, the retinolic compound retinol is synthesized from the carotenoid precursor beta-carotene. Other carotenoid compounds that contain at least one beta-ionone ring structure, such as alpha-carotene and beta-cryptoxanthin, can be precursor compounds for synthesis of retinolic compounds.
According to the present invention, retinolic compound production in a host organism may be adjusted by modifying the expression or activity of one or more proteins involved in retinolic compound biosynthesis. As indicated, in some embodiments, it will be desirable to utilize as host cells organisms that naturally produce one or more retinolic compounds. In some such cases, the focus will be on increasing production of a naturally-produced retinolic compound, for example by increasing the level and/or activity of one or more proteins involved in the synthesis of that retinolic compound and/or by decreasing the level or activity of one or more proteins involved in a competing biosynthetic pathway. Alternatively or additionally, in some embodiments it will be desirable to generate production of one or more retinolic compounds not naturally produced by the host cell.
According to some embodiments of the invention, it will be desirable to introduce one or more heterologous retinologenic polypeptides into a host cell. As will be apparent to those of ordinary skill in the art, any of a variety of heterologous polypeptides may be employed; selection will consider, for instance, the particular retinolic compound whose production is to be enhanced. The present invention contemplates not only introduction of heterologous retinologenic polypeptides, but also adjustment of expression or activity levels of heterologous retinologenic polypeptides, including, for example, alteration of constitutive or inducible expression patterns. In some embodiments of the invention, expression patterns are adjusted such that growth in nutrient-limiting conditions is not required to induce oleaginy. For example, genetic modifications comprising alteration and/or addition of regulatory sequences (e.g., promoter elements, terminator elements) may be utilized to confer particular regulation of expression patterns. Such genetic modifications may be utilized in conjunction with endogenous genes (e.g., for regulation of endogenous carotenogenic); alternatively, such genetic modifications may be included so as to confer regulation of expression of at least one heterologous polypeptide (e.g., retinologenic polypeptide(s)). For example, promoters including, but not limited to those described herein, such as Tef1, Gpd1 promoters can be used in conjunction with endogenous genes and/or heterolous genes for modification of expression patterns of endogenous retinologenic polypeptide(s) and/or heterologous retinologenic polypeptide(s). Similarly, exemplary terminator sequences include, but are not limited to, use of Y. lipolytica XPR2 terminator sequences.
As indicated in FIG. 11 and in the literature, proteins involved in retinologenic biosynthesis include, but are not limited to, beta-carotene 15,15′-monooxygenase (also known as beta-carotene dioxygenase) and beta carotene retinol dehydrogenase. Representative example sequences for these retinolic compound biosynthesis polypeptides are provided in Tables 67-68.
In some embodiments of the invention, potential source organisms for retinolic compound biosynthesis polypeptides include, but are not limited to, genera of naturally oleaginous or non-oleaginous fungi that naturally produce carotenoids. These include, but are not limited to, Botrytis, Cercospora, Fusarium (Gibberella), Mucor, Neurospora, Phycomyces, Puccina, Rhodotorula, Sclerotium, Trichoderma, and Xanthophyllomyces. Exemplary species include, but are not limited to, Neurospora crassa, Xanthophyllomyces dendrorhous (Phaffia rhodozyma), Mucor circinelloides, and Rhodotorula glutinis. Of course, retinolic compounds are produced by a wide range of diverse organisms such as mammals, bacteria, cyanobacteria, etc. Any such organisms may be source organisms for retinolic compound biosynthesis polypeptides according to the present invention.
In certain embodiments of the invention, retinolic compound production in a host organism that is able to produce retinolic compounds from carotenoid substrates is adjusted by modifying the activity of one or more endogenous genes that affect carotenoid biosynthesis. For example, as shown in Example 16, disruption of the endogenous SPT8 gene (YALI0E23804g) in Yarrowia lipolytica results in increased carotenoid production. As will be appreciated by those of ordinary skill in the art, increasing production of a carotenoid(s) in a host organism by altering the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex will result in a greater abundance of such a carotenoid(s); hence, production of a retinolic compound(s) in a host organism able to utilize such a carotenoid(s) as a substrate may similarly be increased.
Without wishing to be bound by theory, the present invention contemplates that alteration of the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex may result in increased retinolic compound production. In certain embodiments, retinolic compound production is increased in a host organism by altering the expression and/or activity of one or more of: Ada proteins (Ada1p, Ada2p, Ngg1p/Ada3p, and Ada4p/Gcn5p), TATA-binding protein (TBP)-related SPT proteins (Spt3p, Spt7p, Spt8p, and Spt20p/Ada5p), TBP-associated factors or (TAFIIs) (TAFII90, TAFII68/61, TAFII60, TAFII25/23, and TAFII17), Tra1p, and/or proteins encoding the acetyltransferase and/or ubiquitin protease activities. In certain embodiments, retinolic compound production is increased in a host organism by altering the expression and/or activity of one or more polypeptides listed in Table 69. Those of ordinary skill in the art will be aware of these and other SAGA components, and will be able to modify such components in accordance with the present invention.
In certain embodiments, host cells are engineered to produce retinolic compounds by introducing one or more carotenoid biosynthesis polypeptides. In general, any retinolic compound biosynthesis polypeptide can be introduced into any host cell of the present invention. In certain embodiments, such retinolic compound biosynthesis polypeptides are codon-optimized to accommodate the codon preferences of the host cell. In certain embodiments, a retinolic compound biosynthesis polypeptide introduced into a host cell is from the same organism as the host cell and/or a related organism. For example, without limitation, the present invention encompasses the recognition that it may be desirable to introduce a fungal retinolic compound biosynthesis polypeptide into a fungal host cell (e.g., from the same and/or a related fungal species). In certain embodiments, the host cell is a Y. lipolytica host cell. In certain aspects of such embodiments, a Y. lipolytica retinolic compound biosynthesis polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, a S. cerevisiae retinolic compound biosynthesis polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, any of a variety of fungal retinolic compound biosynthesis polypeptides is introduced into the Y. lipolytica host cell.
Production and Isolation of Carotenoids and/or Retinolic Compounds
As discussed above, accumulation of lipid bodies in oleaginous organisms is generally induced by growing the relevant organism in the presence of excess carbon source and limiting nitrogen and/or other nutrients (eg. phosphate and magnesium). Specific conditions for inducing such accumulation have previously been established for a number of different oleaginous organisms (see, for example, Wolf (ed.) Nonconventional yeasts in biotechnology Vol. 1, Springer-Verlag, Berlin, Germany, pp. 313-338; Lipids 18(9):623, 1983; Indian J. Exp. Biol. 35(3):313, 1997; J. Ind. Microbiol. Biotechnol. 30(1):75, 2003; Bioresour Technol. 95(3):287, 2004, each of which is incorporated herein by reference in its entirety).
In general, it will be desirable to cultivate inventive modified host cells under conditions that allow accumulation of at least about 20% of their dry cell weight as lipid. In other embodiments, the inventive modified host cells are grown under conditions that permit accumulation of at least about 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, or even 80% or more of their dry cell weight as lipid. In certain embodiments, the host cells utilized are cells which are naturally oleaginous, and induced to produce lipid to the desired levels. In other embodiments, the host cells are cells which naturally produce lipid, but have been engineered to increase production of lipid such that desired levels of lipid production and accumulation are achieved.
In certain embodiments, the host cells of the invention are not naturally oleaginous, but have been engineered to produce lipid such that desired levels of lipid production are obtained. Those of ordinary skill in the art will appreciate that, in general, growth conditions that are effective for inducing lipid accumulation in a source organism, may well also be useful for inducing lipid accumulation in a host cell into which the source organism's oleaginic polypeptides have been introduced. Of course, modifications may be required in light of characteristics of the host cell, which modifications are within the skill of those of ordinary skill in the art.
It will also be appreciated by those of ordinary skill in the art that it will often be desirable to ensure that production of the desired carotenoid and/or retinolic compound by the inventive modified host cell occurs at an appropriate time in relation to the induction of oleaginy such that the carotenoid(s) and/or retinolic compound(s) accumulate(s) in the lipid bodies. In some embodiments, it will be desirable to induce production of the carotenoid(s) and/or retinolic compound(s) in a host cell which does not naturally produce the carotenoid(s) and/or retinolic compound(s), such that detectable levels of the carotenoid(s) and/or retinolic compound(s) is/are produced. In certain aspects the host cells which do not naturally produce a certain carotenoid(s) and/or retinolic compound(s) are capable of production of other carotenoid(s) (e.g. certain host cells may, for example, naturally produce β-carotene but may not naturally produce astaxanthin) and/or retinolic compound(s), (e.g. certain host cells may, for example, naturally produce retinal but may not naturally produce retinol); in other aspects the host cells do not naturally produce any carotenoid(s) and/or retinolic compound(s). In other embodiments, it will be desirable to increase production levels of carotenoid(s) and/or retinolic compound(s) in a host cell which does naturally produce low levels of the carotenoid(s) and/or retinolic compound(s), such that increased detectable levels of the carotenoid(s) and/or retinolic compound(s) are produced. In certain aspects, the host cells which do naturally produce the carotenoid(s) (e.g., β-carotene) also produce additional carotenoid(s) (e.g., astaxanthin, etc.) and/or retinolic compound(s) (e.g., retinal); in still other aspects, the cells which naturally produce the carotenoid(s) (e.g., β-carotene) do not produce additional carotenoid(s) and/or retinolic compound(s).
In certain embodiments of the invention, it will be desirable to accumulate carotenoids and/or retinolic compounds to levels (i.e., considering the total amount of all produced carotenoids and/or retinolic compounds together or considering a particular carotenoid and/or retinolic compound) that are greater than at least about 1% of the dry weight of the cells. In some embodiments, the total carotenoid and/or retinolic compound accumulation will be to a level at least about 1.5%, at least about 2%, at least about 2.5%, at least about 3%, at least about 3.5%, at least about 4%, at least about 4.5%, at least about 5%, at least about 5.5%, at least about 6%, at least about 6.5%, at least about 7%, at least about 7.5%, at least about 8%, at least about 8.5%, at least about 9%, at least about 9.5%, at least about 10%, at least about 10.5%, at least about 11%, at least about 11.5%, at least about 12%, at least about 12.5%, at least about 13%, at least about 13.5%, at least about 14%, at least about 14.5%, at least about 15%, at least about 15.5%, at least about 16%, at least about 16.5%, at least about 17%, at least about 17.5%, at least about 18%, at least about 18.5%, at least about 19%, at least about 19.5%, at least about 20% or more of the total dry weight of the cells.
In some embodiments of the invention, a particular carotenoid and/or retinolic compound may not accumulate to a level as high as 1% of the total dry weight of the cells; appropriately engineered cells according to the present invention, and any lipid bodies, carotenoids and/or retinolic compounds they produce, remain within the scope of the present invention. Thus, in some embodiments, the cells accumulate a given carotenoid and/or retinolic compound to a level below about 1% of the dry weight of the cells. In some embodiments, the carotenoid and/or retinolic compound accumulates to a level below about 0.9%, 0.8%, 0.7%, 0.6%, 0.5%, 0.4%, 0.3%, 0.2%, 0.1%, 0.05%, or lower, of the dry cell weight of the cells.
In some embodiments of the invention, carotenoids and/or retinolic compounds accumulate both within lipid bodies and elsewhere in the cells. In some embodiments, carotenoids and/or retinolic compounds accumulate primarily within lipid bodies. In some embodiments, carotenoids and/or retinolic compounds accumulate substantially exclusively within lipid bodies. In some embodiments, at least about 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or more of a desired produced carotenoid and/or retinolic compound accumulates in lipid bodies.
In some embodiments of the invention, modified host cells are engineered to produce one or more carotenoid compound(s) and/or retinolic compound(s) characterized by negligible solubility in water (whether hot or cold) and detectable solubility in one or more oils. In some embodiments, such compounds have a solubility in oil below about 0.2%. In some embodiments, such compounds have a solubility in oil within the range of about <0.001%-0.2%.
The present invention therefore provides engineered host cells (and methods of making and using them) that contain lipid bodies and that further contain one or more carotenoid compounds and/or retinolic compounds accumulated in the lipid bodies, where the compounds are characterized by a negligible solubility in water and a solubility in oil within the range of about <0.001%-0.2%; 0.004%-0.15%; 0.005-0.1%; or 0.005-0.5%. For example, in some embodiments, such compounds have a solubility in oil below about 0.15%, 0.14%, 0.13%, 0.12%, 0.11%, 0.10%. 0.09, 0.08%, 0.07%, 0.06%, 0.05%, 0.04%, 0.03%, 0.02%, 0.01%, 0.05%, or less. In some embodiments, the compounds show such solubility in an oil selected from the group consisting of sesame; soybean; apricot kernel; palm; peanut; safflower; coconut; olive; cocoa butter; palm kernel; shea butter; sunflower; almond; avocado; borage; carnauba; hazel nut; castor; cotton seed; evening primrose; orange roughy; rapeseed; rice bran; walnut; wheat germ; peach kernel; babassu; mango seed; black current seed; jojoba; macademia nut; sea buckthorn; sasquana; tsubaki; mallow; meadowfoam seed; coffee; emu; mink; grape seed; thistle; tea tree; pumpkin seed; kukui nut; and mixtures thereof.
Bacterial carotenogenic genes have already been demonstrated to be transferable to other organisms, and are therefore particularly useful in accordance with the present invention (see, for example, Miura et al., Appl. Environ. Microbiol. 64:1226, 1998). In other embodiments, it may be desirable to utilize genes from other source organisms such as plant, alga, or microalgae; these organisms provide a variety of potential sources for ketolase and hydroxylase polypeptides. Still additional useful source organisms include fungal, yeast, insect, protozoal, and mammalian sources of polypeptides.
In some embodiments of the present invention, isoprenoid production is increased in host cells (e.g., in Y. lipolytica cells) through expression of a truncated variant of a hydroxymethylglutaryl-CoA (HMG CoA) reductase polypeptide. In some embodiments, the truncated variant is a truncated variant of a Y. lipolytica HMG CoA reductase polypeptide. According to the present invention, expression of such a truncated HMG CoA reductase polypeptide can result in increased isoprenoid and/or carotenoid production in host cells (e.g., Y. lipolytica cells).
Alternatively or additionally, in some embodiments of the present invention, isoprenoid production is increased in host cells (e.g., in Y. lipolytica cells) through application of one or more carotenogenic modification(s) that increase(s) level and/or activity of a polypeptide selected from the group consisting of farnesyl pyrophosphate synthase polypeptides, geranylgeranylpyrophosphate synthase polypeptides, and combinations thereof. In some embodiments, the source organism for the selected polypeptide is Y. lipolytica. 
Alternatively or additionally, in some embodiments of the present invention, isoprenoid production is increased in host cells (e.g., in Y. lipolytica cells) through application of one or more carotenogenic modification(s) that decrease(s) expression or activity of an isoprenoid biosynthesis competitor polypeptide (e.g., of a squalene synthase polypeptide), for example thereby reducing diversion of one or more intermediates away from the isoprenoid and/or carotenoid biosynthesis pathways. In some embodiments, the polypeptide whose expression or activity is reduced is endogenous to the host cell.
In some embodiments of the present invention, more than one carotenogenic modification is applied to the same host cell. For example, isoprenoid production may be increased in host cells (e.g., Y. lipolytica cells) through application of at least two or more carotenogenic modifications selected from the group consisting of: expression of a truncated HMG CoA reductase polypeptide, increase in expression and/or activity of farnesyl pyrophosphate synthase polypeptide, increase in expression and/or activity of a geranylgeranylpyrophosphate synthase polypeptide, decrease in expression and/or activity of a squalene synthase polypeptide, and combinations thereof.
Furthermore, in some embodiments of the invention, carotenoid production (e.g., production of β-carotene) is increased in host cells (e.g., in Y. lipolytica cells) through application of one or more carotenogenic modification(s) that increase(s) expression and/or activity of a polypeptide selected from the group consisting of phytoene synthase, lycopene cyclase, phytoene dehydrogenase, and combinations thereof. In some embodiments, such increase in expression comprises introduction of one or more genes encoding heterologous polypeptides. In some embodiments, phytoene synthase and lycopene cyclase activities are provided in a single polypeptide or complex (e.g., by the Mucor circinelloides or Neurospora crassa multifunctional phytoene synthase/lycopene cyclase). In some embodiments, phytoene dehydrogenase from Mucor circinelloides or Neurospora crassa is utilized.
In some embodiments, production of one or more carotenoids downstream of β-carotene (e.g., of one or more hydroxylated xanthophylls) is increased in host cells that produce β-carotene (including host cells that have been engineered to produce β-carotene, e.g., through application of one or more carotenogenic modifications as described herein) through application of one or more carotenogenic modifications that increase(s) level and/or activity of one or more carotenoid ketolase polypeptides (e.g., from Parvularcula bermudensis and/or Aurantimonase sp. SI85-9A1) to produce one or more ketone-containing carotenoids (e.g., canthaxanthin, echinenone, astaxanthin, and combinations thereof).
In some embodiments, production of one or more hydroxylated carotenoids is increased in host cells that produce (including having been engineered to produce) β-carotene and/or one or more ketone-containing carotenoids though application of one or more carotenogenic modifications that increase(s) the level and/or activity of one or more carotenoid hydroxylase polypeptides (e.g., from Xanthobacter autotrophicus and/or Erythrobacter litoralis) to increase production of one or more hydroxylated carotenoids (e.g., zeaxanthin, lutein, β-cryptoxanthin, astaxanthin, and combinations thereof).
Similar approaches to enhance carotenoid production may be employed in other oleaginous or non-oleaginous host organisms (e.g. S. cerevisiae, C. utilis, P. rhodozyma) can be undertaken, using the same, homologous, or functionally similar carotogenic polypeptides.
In some embodiments, the present invention provides modified Y. lipolytica strains that have been engineered to express one or more carotenoid biosynthesis polypeptides and/or isoprenoid biosynthesis polypeptides. For example, in some embodiments, a modified Y. lipolytica strain is engineered to increase expression and/or activity of one or more of phytoene synthase, phytoene dehydrogenase, lycopene cyclase, and GGPP synthase, and/or to decrease expression and/or activity of squalene synthase. In some embodiments, a modified Y. lipolytica strain is engineered to express all of these polypeptides. Such a modified Y. lipolytica strain produces β-carotene (see, for example, Example 2).
In some embodiments, inventive modified Y. lipolytica strains that have been engineered to produce β-carotene are further engineered to express a truncated HMG CoA reductase; in some such embodiments, the strains are engineered so that expression of the truncated HMG CoA reductase increases β-carotene several fold (for example, 3-4 fold or more).
In some embodiments, inventive modified Y. lipolytica strains that have been engineered to produce β-carotene are further engineered to express a beta-carotene 15,15′-monooxygenase and/or a retinol dehydrogenase to increase retinolic compound production.
In some embodiments, inventive modified Y. lipolytica strains that have been engineered to produce β-carotene are further engineered to express carotenoid hydroxylase (to achieve production of zeaxanthin and/or β-cryptoxanthin), carotenoid ketolase (to achieve production of canthaxanthin and/or echinenone), or both (to achieve production of astaxanthin).
In some embodiments, inventive modified Y. lipolytica strains that have been engineered to produce, for example, β-carotene, zeaxanthin, canthaxanthin, echinenone, and/or astaxanthin are also engineered to have increased expression of, for example, malic enzyme, mevalonate kinase, etc.
It will be appreciated that, in some embodiments of the invention, it may be desirable to engineer a particular host cell by expressing more than one version of a given polypeptide (e.g., isoprenoid biosynthesis polypeptide, carotenoid biosynthesis polypeptide, oleaginic polypeptide, isoprenoid biosynthesis competitor polypeptides, retinolic compound biosynthesis polypeptide, etc.). For example, a given host cell may be engineered to express versions of a given polypeptide from two or more different sources. Where a particular enzyme may be comprised of more than one polypeptide chains, it will often be desirable to utilize all chains from a single source, although this is not required so long as activity is achieved. Also, whenever a host cell is engineered to express a polypeptide from a different source, it may be desirable to alter the gene sequence encoding the polypeptide to account for codon preferences of the host cell.
To give but a few specific examples, the present invention provides modified Y. lipolytica strains that have been engineered to express the phytoene synthase/lycopene cyclase bifunctional (carB) polypeptide from M. circinelloides (see, for example, Example 1B), and also to express the phytoene dehydrogenase (carRP) polypeptide from M. circinelloides (see, for example, Example 1A). In some embodiments, the present invention provides such carB+carRP-expressing Y. lipolytica strains that have been engineered to modify expression and/or activity of a truncated HMG-CoA reductase polypeptide from Y. lipolytica and/or one or more Y. lipolytica polypeptides selected from the group consisting of GGPP synthase, FPP synthase (Erg20), IPP isomerase (IDI), HMG synthase (Erg13), mevalonate kinase (Erg12), squalene synthase (Erg9), phosphimevalonate kinase (Erg8), mevalonate pyrophosphate decarboxylase (MVD1), malic enzyme, malate dehydrogenase, glucose 6 phosphate dehydrogenase, malate dehydrogenase homolog 2,6-phosphogluconate dehydrogenase (GND1), isocitrate dehydrogenase, fructose 1,6 bisphosphatase, acetoacetyl CoA thiolase (Erg10), ATP citrate lyase subunit 1, ATP citrate lyase subunit 2, and combinations thereof. The present invention therefore specifically provides Y. lipolytica strains that have been engineered to produce β-carotene.
The present invention also specifically provides modified Y. lipolytica strains that have been engineered to express at least one carotenoid ketolase (e.g., crtO/crtW) polypeptide, and in some embodiments more than one, for example from a source selected from the group consisting of Parvularcula bermudensis (see, for example, Example 1H), Aurantimonas (see, for example, Example 1G), and/or an environmental isolate identified from the Sargasso Sea (see, for example, Example 1F). The present invention therefore specifically provides Y. lipolytica strains that have been engineered to produce canthaxanthin, astaxanthin, and/or echinenone.
The present invention further specifically provides modified Y. lipolytica strains that have been engineered to express at least one carotenoid hydroxylase (e.g., crtZ) polypeptide, and in some embodiments more than one, from Erythrobacter litoralis (see, for example, Examples 1J and 1L), Novosphingobium aromaticivarans (see, for example, Example 1E), Parvularcula bermudensis (see, for example, Example 1I), Xanthobacter autotrophicus (see, for example, Example 1O), Sphingopyxis alaskensis (see, for example, Example 1M), Chlamydomonas rheinhardtii, Erythrobacter longus, Robiginitalea biformata (see, or example, Example 1N) and/or Pseudomonas putida (see, for example, Example 1P). The present invention therefore specifically provides Y. lipolytica strains that have been engineered to produce zeaxanthin, lutein, β-cryptoxanthin, and/or astaxanthin.
The present invention further specifically provides modified Y. lipolytica strains that have been engineered to express at least one carotenoid ketolase (e.g., crtO/crtW) polypeptide in combination with at least one carotenoid hydroxylase (e.g., crtZ) polypeptide. In certain embodiments, the at least one carotenoid ketolatse polypeptide and at least one carotenoid hydroxylase polypeptide are encoded by nucleic acid sequences present in separate nucleic acid molecules. In certain embodiments, the at least one carotenoid ketolatse polypeptide and at least one carotenoid hydroxylase polypeptide are encoded by nucleic acid sequences present in the same nucleic acid molecule. For example, a host organism may be transformed or transfected with a single expression vector, which expression vector comprises both a carotenoid ketolatse polypeptide and a carotenoid hydroxylase polypeptide, each of which comprises sequences sufficient to direct their expression in the host organism.
In certain embodiments, the at least one carotenoid ketolase (e.g., crtO/crtW) polypeptide and the at least one carotenoid hydroxylase (e.g., crtZ) polypeptide are expressed as a fusion protein. A representative example of such embodiments is presented in Example 17. In certain embodiments, such a fusion polypeptide is designed such that the carotenoid ketolatse polypeptide is positioned N-terminal to the carotenoid hydroxylase polypeptide. In certain embodiments, such a fusion polypeptide is designed such that the carotenoid ketolatse polypeptide is positioned C-terminal to the carotenoid hydroxylase polypeptide.
In embodiments in which the carotenoid ketolatse polypeptide and the carotenoid hydroxylase polypeptide are expressed concurrently (whether from separate nucleic acid molecules or from the same nucleic acid molecule), the polypeptides may be selected from any of a variety of source organisms. As non-limiting examples, the carotenoid hydroxylase polypeptide may be selected from an organism such as Erythrobacter litoralis (see, for example, Examples 1J and 1L), Novosphingobium aromaticivarans (see, for example, Example 1E), Parvularcula bermudensis (see, for example, Example 1I), Xanthobacter autotrophicus (see, for example, Example 1O), Sphingopyxis alaskensis (see, for example, Example 1M), Chlamydomonas rheinhardtii, Erythrobacter longus, Robiginitalea biformata (see, or example, Example 1N) and/or Pseudomonas putida (see, for example, Example 1P). As further non-limiting examples, the carotenoid ketolase polypeptide may be selected from an organism such as Parvularcula bermudensis (see, for example, Example 1H), Aurantimonas (see, for example, Example 1G), and/or an environmental isolate identified from the Sargasso Sea (see, for example, Example 1F).
It should be noted that, for inventive organisms that produce more than one carotenoid, it will sometimes be possible to adjust the relative amounts of individual carotenoids produced by adjusting growth conditions. For example, it has been reported that controlling the concentration of dissolved oxygen in a culture during cultivation can regulate relative production levels of certain carotenoids such as β-carotene, echinenone, β-cryptoxanthin, 3-hydroxyechinenone, asteroidenone, canthaxanthin, zeaxanthin, adonirubin, adonixanthin and astaxanthin (see, for example, U.S. Pat. No. 6,825,002 to Tsubokura et al., the entire contents of which are incorporated herein by reference). Additionally or alternatively, the present invention encompasses the recognition that controlling the pH in a culture during cultivation can regulate relative production levels of these and/or other carotenoids (see e.g., Example 18).
Particularly for embodiments of the present invention directed toward production of astaxanthin, it will often be desirable to utilize one or more genes from a natural astaxanthin-producing organism. Where multiple heterologous polypeptides are to be expressed, it may be desirable to utilize the same source organism for all, or to utilize closely related source organisms.
Inventive modified cells, that have been engineered to produce carotenoids and/or to accumulate lipid (including to be oleaginous), can be cultured under conditions that achieve carotenoid production and/or oleaginy. In some embodiments, it will be desirable to control growth conditions so in order to maximize production of a particular carotenoid or set of carotenoids (including all carotenoids) and/or to optimize accumulation of the particular carotenoid(s) in lipid bodies. In some embodiments it will be desirable to control growth conditions to adjust the relative amounts of different carotenoid products produced.
Inventive modified cells, that have been engineered to produce retinolic compounds and/or to accumulate lipid (including to be oleaginous), can be cultured under conditions that achieve retinolic compound production and/or oleaginy. In some embodiments, it will be desirable to control growth conditions so in order to maximize production of a particular retinolic compound or set of retinolic compounds (including all retinolic compounds) and/or to optimize accumulation of the particular retinolic compound (s) in lipid bodies. In some embodiments it will be desirable to control growth conditions to adjust the relative amounts of different retinolic compound products produced.
In some embodiments, it will be desirable to limit accumulation of a particular intermediate, for example ensuring that substantially all of a particular intermediate compound is converted so that accumulation is limited. For example, particularly in situations where a downstream enzyme may be less efficient than an upstream enzyme and it is desirable to limit accumulation of the product of the upstream enzyme (e.g., to avoid its being metabolized via a competitive pathway and/or converted into an undesirable product), it may be desirable to grow cells under conditions that control (e.g., slow) activity of the upstream enzyme so that the downstream enzyme can keep pace.
Those of ordinary skill in the art will appreciate that any of a variety of growth parameters, including for example amount of a particular nutrient, pH, temperature, pressure, oxygen concentration, timing of feeds, content of feeds, etc can be adjusted as is known in the art to control growth conditions as desired.
To give but a few examples, in some embodiments, growth and/or metabolism is/are limited by limiting the amount of biomass accumulation. For example, growth and/or metabolism can be limited by growing cells under conditions that are limiting for a selected nutrient. The selected limiting nutrient can then be added in a regulated fashion, as desired. In some embodiments, the limiting nutrient is carbon, nitrogen (e.g., via limiting ammonium or protein), phosphate, magnesium, one or more trace metals, or combinations thereof. In some embodiments, the limiting nutrient is carbon. In some embodiments, the limiting nutrient is one or more trace metals.
In some embodiments, use of a limiting nutrient can by utilized to control metabolism of a particular intermediate and/or to adjust relative production of particular carotenoid compounds and/or retinolic compounds. In some embodiments, this result can be achieved by controlling metabolism of a particular intermediate as discussed above; in some embodiments, it can be achieved, for example, by limiting progress through the carotenoid and/or retinolic compound biosynthesis pathway so that a desired carotenoid product (e.g., β-carotene, canthaxanthin, astaxanthin, etc.) or retinolic compound (e.g., retinal) is not converted to a downstream compound. To give but one example, phosphate limitation can slow the overall rate of clux through the carotenoid biosynthesis pathway and can be utilized to change the ratio of canthaxanthin to echinenone produced.
In some embodiments, cells are grown in the presence of excess carbon source and limiting nitrogen, phosphate, and/or magnesium to induce oleaginy. In some embodiments cells are grown in the presence of excess carbon source and limiting nitrogen. In some embodiments, the carbon:nitrogen ratio is within the range of about 200:1, 150:1, 125:1, 100:1, 95:1, 90:1, 85:1, 80:1, 75:1, 70:1, 65:1, 60:1, 55:1, 50:1, 45:1, 40:1, 35:1, 30:1, 25:1, 20:1, 15:1, 10:1, or less. Those of ordinary skill in the art are aware of a wide variety of carbon sources, including, for example, glycerol, glucose, galactose, dextrose, any of a variety of oils (e.g., olive, canola, corn, sunflower, soybean, cottonseed, rapeseed, etc., and combinations thereof) that may be utilized in accordance with the present invention. Combinations of such may also be utilized. For example, common carbon source compositions contain oil:glucose in a ratio within the range of about 5:95 to 50:50 (e.g. about 5:95, about 10:90, about 15:85, about 20:80, about 25:75, about 30:70, about 35:65, about 40:60, about 45:55, about 50:50).
Those of ordinary skill in the art are also aware of a variety of different nitrogen sources (e.g., ammonium sulfate, proline, sodium glutamate, soy acid hydrolysate, yeast extract-peptone, yeast nitrogen base, corn steep liquor, etc, and combinations thereof) that can be utilized in accordance with the present invention.
In some embodiments, cultures are grown at a selected oxygen concentration (e.g., within a selected range of oxygen concentrations). In some embodiments, oxygen concentration may be varied during culture. In some embodiments, oxygen concentration may be controlled during some periods of culture and not controlled, or controlled at a different point, during others. In some embodiments, oxygen concentration is not controlled. In some embodiments, cultures are grown at an oxygen concentration within the range of about 5-30%, 5-20%, 10-25%, 10-30%, 15-25%, 15-30%, including at about 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, or more. In some embodiments, oxygen concentration is maintained above about 20%, at least for some period of the culture.
In some embodiments, cells are grown via fed-batch fermentation. In some embodiments, feed is continued until feed exhaustion and/or the feed is controlled to initiate or increase once a certain level of dissolved oxygen is detected in the culture medium (e.g., about 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, or more dissolved oxygen). The feed rate can be modulated to maintain the dissolved oxygen at a specific level (e.g., about 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, or more dissolved oxygen).
In some embodiments, inventive modified cells are grown in a two-phase feeding protocol in which the first phase is designed to maintain conditions of excess carbon and limiting oxygen, and the second phase results in conditions of excess oxygen and limiting carbon. The carbon sources in each phase can be the same (e.g., both glucose) or different (e.g., glucose then glucose-oil mixture, oil then glucose, or glucose-oil mixture then glucose). The present invention demonstrates that such conditions can achieve high levels of carotenoid production (see, for example, Example 5D). Additionally or alternatively, such conditions also result in high levels of retinolic compound production. For example, high levels of retinolic compound(s) production may be achieved by increasing the levels of a particular carotenoid that is used as a substrate for the production of such a retinolic compound(s).
In some embodiments, inventive modified cells are cultivated at constant temperature (e.g., between about 20-40, or 20-30 degrees, including for example at about 20, 20.5, 21, 21.5, 22, 22.5, 23, 23.5, 24, 24.5, 25, 25.5, 26, 26.5, 27, 27.5, 28, 28.5, 29, 29.5, 30° C. or above) and/or pH (e.g., within a range of about 4-7.5, or 4-6.5, 3.5-7, 3.5-4, 4-4.5, 4.5-5, 5-5.5, 5.5-6, 6-6.5, 6.5-7, 7-7.5, 7-8, etc., including at about 4.0, 4.1, 4.2, 4.3, 4.4, 4.5, 4.6, 4.7, 4.8, 4.9, 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, 8.0, 8.1, 8.2, 8.3, 8.4, 8.5 or above); in other embodiments, temperature and/or pH may be varied during the culture period, either gradually or in a stepwise fashion.
For example, in some embodiments, the pH is 7.0 at inoculation and is increased to pH 8.0 during the course of the fermentation. The pH may be increased either continuously or in discrete steps. For example, in Example 19, the pH of the culture in increased continuously. In certain embodiments, the pH in increased continuously by increasing the pH at a rate of 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.010, 0.011, 0.012, 0.013, 0.014, 0.015, 0.016, 0.017, 0.018, 0.019, 0.020, 0.021, 0.022, 0.023, 0.024, 0.025, 0.026, 0.027, 0.028, 0.029, 0.030, 0.031, 0.032, 0.033, 0.034, 0.035, 0.036, 0.037, 0.038, 0.039, 0.040, 0.041, 0.042, 0.043, 0.044, 0.045, 0.046, 0.047, 0.048, 0.049, 0.050 or more units/hour.
In certain embodiments, the pH in increased in discrete steps by increasing the pH by 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.010, 0.011, 0.012, 0.013, 0.014, 0.015, 0.016, 0.017, 0.018, 0.019, 0.020, 0.021, 0.022, 0.023, 0.024, 0.025, 0.026, 0.027, 0.028, 0.029, 0.030, 0.031, 0.032, 0.033, 0.034, 0.035, 0.036, 0.037, 0.038, 0.039, 0.040, 0.041, 0.042, 0.043, 0.044, 0.045, 0.046, 0.047, 0.048, 0.049, 0.050 or more at each step.
In certain embodiments, the pH is increased employing a combination of continuous increase and discrete steps.
In certain embodiments, increasing the pH during the course of fermentation results in one or more beneficial effects such as, without limitation, an increase in total biomass accumulation, an increase in the percentage of biomass representing carotenoid accumulation, and, in the case of zeaxanthin production, an increase in the hydroxylation of beta-carotene to zeaxanthin. Those of ordinary skill in the art will be able to select without undue experimentation an appropriate rate of increase, an appropriate type of increase (e.g. continuous, discrete steps or a combination of the two), and/or an optimum pH within the selected range to maximize these and/or other beneficial effects.
In some embodiments, the temperature at which inventive cells are cultivated is selected so that production of one or more particular carotenoid compound(s) and/or retinolic compound(s) is adjusted (e.g., so that production of one or more particular compound(s) is increased and/or production of one or more other compound(s) is decreased). In some embodiments, the temperature at which inventive cells are cultivated is selected so that the ratio of one carotenoid compound and/or retinolic compound to another, is adjusted. To give but one example, in some embodiments, a temperature is selected to be sufficiently low that β-carotene levels are reduced and the level of at least one other carotenoid compound(s) (e.g., zeaxanthin) is increased.
In some embodiments, cultures are grown at about pH 5.5, at about pH 7.0, and or at a temperature between about 28-30° C. In some embodiments, it may be desirable to grow inventive modified cells under low pH conditions, in order to minimize growth of other cells. In some embodiments, it will be desirable to grow inventive modified cells under relatively higher temperature conditions in order to slow growth rate and/or increase the ultimate dry cell weight output of carotenoids and/or retinolic compounds. In some embodiments, it will be desirable to grow inventive modified cells under conditions in which the pH in increased (e.g. continuously, in discrete steps, or both) during the course of fermentation (e.g. increased from pH 7.0 to pH 8.0). In some embodiments, it will be desirable to grow inventive modified cells under two or more of these conditions. For example, inventive modified cells can be grown under relatively higher temperature conditions while simultaneously increasing the pH over the course of the fermentation. Those of ordinary skill in the art will be able to select appropriate growth conditions to achieve their experimental, production and/or other cell culture goals.
One advantage provided by the present invention is that, in addition to allowing the production of high levels of carotenoids and/or retinolic compounds, certain embodiments of the present invention allow produced compounds to be readily isolated because they accumulate in the lipid bodies within oleaginous organisms. Methods and systems for isolating lipid bodies have been established for a wide variety of oleaginous organisms (see, for example, U.S. Pat. Nos. 5,164,308; 5,374,657; 5,422,247; 5,550,156; 5,583,019; 6,166,231; 6,541,049; 6,727,373; 6,750,048; and 6,812,001, each of which is incorporated herein by reference in its entirety). In brief, cells are typically recovered from culture, often by spray drying, filtering or centrifugation.
Of course, it is not essential that lipid bodies be specifically isolated in order to collect carotenoid compounds and/or retinolic compounds produced according to the present invention. Any of a variety of approaches can be utilized to isolate and/or purify carotenoids and/or retinolic compounds. Many useful extraction and/or purification procedures for particular carotenoid compounds, and/or for carotenoids generally, are known in the art (see, for example, EP670306, EP719866, U.S. Pat. No. 4,439,629, U.S. Pat. No. 4,680,314, U.S. Pat. No. 5,310,554, U.S. Pat. No. 5,328,845, U.S. Pat. No. 5,356,810, U.S. Pat. No. 5,422,247, U.S. Pat. No. 5,591,343, U.S. Pat. No. 6,166,231, U.S. Pat. No. 6,750,048, U.S. Pat. No. 6,812,001, U.S. Pat. No. 6,818,239, U.S. Pat. No. 7,015,014, US2003/0054070, US2005/0266132, each of which is incorporated herein by reference).
In many typical isolation procedures, cells are disrupted (e.g., mechanically (for example using a bead mill, mashing), enzymatically (e.g. using zymolyase or a β-1,3 glucanase such as Glucanex 200G (Novozyme), chemically (e.g., by exposure to a mild caustic agent such as a detergent or 0.1 N NaOH, for example at room temperature or at elevated temperature), using a reducing agent (e.g. dithiothreitol, β-mercaptoethanol), using high pressure homogenization/shearing, by changing pH, etc. and combinations thereof) to allow access of intracellular carotenoid and/or retinolic compound(s) to an extraction solvent, and are then extracted one or more times. In certain embodiments, cells are disrupted mechanically using a bead mill/mashing at high pressure (e.g. at 25K, 10K-30K, 15K-25K, or 20-25K, pound-force per square inch (psi)). Cells may optionally be concentrated (e.g., to at least about 100 g/L or more, including to at least about 120 g/l, 150 g/l, 175 g/L, 200 g/L or more) and/or dried (e.g., with a spray dryer, double drum dryer (e.g. Blaw Knox double drum dryer), single drum vacuum dryer, etc.), prior to exposure to extraction solvent (and/or prior to disruption or homogenization). Disruption can, of course, be performed prior to and/or during exposure to extraction solvent. After extraction, solvent is typically removed (e.g., by evaporation, for example by application of vacuum, change of temperature, etc.).
In some instances, cells are disrupted and then subjected to supercritical liquid extraction or solvent extraction. Typical liquids or solvents utilized in such extractions include, for example, organic or non-organic liquids or solvents. To give but a few specific examples, such liquids or solvents may include acetone, supercritical fluids (e.g. carbon dioxide, propane, xenon, ethane, propylene, methane, ethylene, ethanol), carbon dioxide, chloroform, ethanol, ethyl acetate, heptane, hexane, isopropanol, methanol, methylene chloride, octane, tetrahydrofuran (THF), cyclohexane, isobutyl acetate, methyl ketone, ethyl ketone, toluene, cyclohexanone, benzene, propylene glycol, vegetable oils (e.g. soybeen soybean oil, rapeseed oil, corn oil, cottonseed oil, canola oil, etc.) and combinations thereof (e.g. hexane:ethyl acetate, combination of a polar and non-polar solvent, combination of an alcohol with either hexane or ethyl acetate). Particular solvents may be selected, for example, based on their ability to solubilize particular carotenoid compounds and/or retinolic compounds, or sets of carotenoid compounds (e.g., all carotenoids) and/or retinolic compounds (e.g., all retinolic compounds), and/or based on regulatory or other considerations (e.g., toxicity, cost, ease of handling, ease of removal, ease of disposal, etc.). For example, more polar carotenoids (e.g., xanthophylls) are known to be extracted more efficiently into extraction solvents with increased polarity. Craft (1992) J. Agric. Food Chem 40, 431-434 which is herein incorporated by reference discusses the relative solubility of two carotenoids, lutein and β-carotene in different solvents.
In some embodiments, combinations of solvents may be utilized. In some embodiments, combinations of a relatively polar solvent (e.g., alcohols, acetone, chloroform, methylene chloride, ethyl acetate, etc.) and a relatively non-polar solvent (e.g., hexane, cyclohexane, oils, etc.) are utilized for extraction. Those of ordinary skill in the art will readily appreciate that different ratios of polar to non-polar solvent may be employed as appropriate in a particular situation. Just to give a few examples, common ratios include 1:1, 2:1, 3:1, 3:2, 95:5, 90:10, 85:15, 80:20, 75:25, 70:30, 65:45, 60:40, 55:45, and 50:50. It will be appreciated that solvents or solvent mixtures of different polarities may be more effective at extracting particular carotenoids (e.g., based on their polarities and/or as a function of other attributes of the host cell material from which they are being extracted). Those of ordinary skill in the art are well able to adjust the overall polarity of the extracting solvent, for instance by adjusting the relative amounts of polar and non-polar solvents in a solvent blend, in order to achieve more efficient extraction.
Extraction may be performed under any of a variety of environmental conditions, including any of a variety of temperatures. For example, extraction may be performed on ice (for example at 4° C., 0° C., less than 0° C.), at room temperature, or at any of a variety of other temperatures. For example, a solvent may be maintained at a selected temperature (e.g., about less than 0, 0, 4, 25, 28, 30, 37, 68, 70, 75, 80, 85, 90, 95, or 100° C.) in order to improve or adjust extraction of a particular desired carotenoid.
Extraction typically yields a crude oil suspension. In some embodiments, the crude oil suspension contains some intact host cells but is at least about 95% free of intact host cells. In some embodiments, the crude oil suspension is at least about 96%, 97%, 98%, or 99% or more free of intact host cells. In some embodiments, the suspension is substantially free of water-soluble cell components (e.g., nucleic acids, cell wall or storage carbohydrates, etc.). In some embodiments, the suspension contains less than about 5%, 4%, 3%, 2%, or 1% or less water-soluble cell components.
Extraction conditions that yield a crude oil suspension will enrich for lipophilic components that accumulate in the lipid bodies within oleaginous organisms. In general, the major components of the lipid bodies consist of triacylglycerols, ergosteryl esters, other steryl esters, free ergosterol, phospholipids, and some proteins, which often function in the synthesis or regulation of the levels of other lipid body components. C16 and C18 (e.g. C16:0, C16:1, C18:0, C18:1, and C18:2) are generally the major fatty acids present in lipid bodies, mainly as components of triacylglycerol and steryl esters.
In some embodiments of the invention, the crude oil suspension contains at least about 2.5% by weight carotenoid compound(s) and/or retinolic compound(s); in some embodiments, the crude oil suspension contains at least about 5% by weight carotenoid compound(s) and/or retinolic compound(s), at least about 10% by weight carotenoid compound(s) and/or retinolic compound(s), at least about 20% by weight carotenoid compound(s) and/or retinolic compound(s), at least about 30% by weight carotenoid compound(s) and/or retinolic compound(s), at least about 40% by weight carotenoid compound(s) and/or retinolic compound(s), or at least about 50% by weight carotenoid compound(s) and/or retinolic compound(s).
The crude oil suspension may optionally be refined as known in the art. Refined oils may be used directly as feed or food additives. Alternatively or additionally, carotenoids and/or retinolic compound can be isolated from the oil using conventional techniques.
Given the sensitivity of carotenoids and retinolic compounds generally to oxidation, many embodiments of the invention employ oxidative stabilizers (e.g., ascorbyl palmitate, tocopherols, vitamin C (e.g. sodium ascorbate), ethoxyquin, vitamin E, BHT, BHA, TBHQ, etc., or combinations thereof) during and/or after carotenoid isolation. Alternatively or additionally, nitrogen or an inert gas can be utilized to purge oxygen from the process lines of any tanks or equipment. Alternatively or additionally, microencapsulation, (for example with a microencapsulation ingredients such as proteins, carbohydrates (e.g. maltodextrin, gum acacia, xanthan gum, starches/sugars like sucrose), or gelatins, or any other substance which creates a physical barrier to air and/or light) may be employed to add a physical barrier to oxidation and/or to improve handling (see, for example, U.S. Patent Applications 2004/0191365 and 2005/0169999). For example, carotenoids and/or retinolic compounds produced according to the present invention may be microencapsulated after isolation during the formulation of commercial products (e.g. pharmaceuticals, food supplements, electro-optic applications, animal feed additives, cosmetics, etc.) to minimize or eliminate oxidation during production, storage, transport, etc.
Extracted carotenoids and/or retinolic compounds may be further isolated and/or purified, for example, by crystallization, washing, recrystallization, and/or other purification strategies. In some embodiments, carotenoid and/or retinolic compound crystals are collected by filtration and/or centrifugation. Isolated or purified carotenoids and/or retinolic compound may be dried and/or formulated for storage, transport, sale, and/or ultimate use. To give but a few specific examples, carotenoids and/or retinolic compounds may be prepared as a water (e.g. cold water) dispersible powder (e.g. 1%-20% carotenoid: microencapsulation ingredient), as a suspension of crystals in oil (e.g., vegetable oil, e.g., about 1%-30%, 5%-30%, 10%-30% w/w), etc.
Uses
Carotenoids and/or retinolic compounds produced according to the present invention can be utilized in any of a variety of applications, for example exploiting their biological or nutritional properties (e.g., anti-oxidant, anti-proliferative, etc.) and/or their pigment properties. For example, according to the present invention, carotenoids may be used in pharmaceuticals (see, for example, Bertram, Nutr. Rev. 57:182, 1999; Singh et al., Oncology 12:1643, 1998; Rock, Pharmacol. Ther. 75:185, 1997; Edge et al, J. Photochem Photobiol 41:189, 1997; U.S. Patent Application 2004/0116514; U.S. Patent Application 2004/0259959), food supplements (see, for example, Koyama et al, J. Photochem Photobiol 9:265, 1991; Bauernfeind, Carotenoids as colorants and vitamin A precursors, Academic Press, NY, 1981; U.S. Patent Application 2004/0115309; U.S. Patent Application 2004/0234579), electro-optic applications, animal feed additives (see, for example, Krinski, Pure Appl. Chem. 66:1003, 1994; Polazza et al., Meth. Enzymol. 213:403, 1992), cosmetics (as anti-oxidants and/or as cosmetics, including fragrances; see for example U.S. Patent Application 2004/0127554), etc. Carotenoids produced in accordance with the present invention may also be used as intermediates in the production of other compounds (e.g., steroids, etc.).
For example, astaxanthin and/or esters thereof may be useful in a variety of pharmaceutical applications and health foods including treatment of inflammatory diseases, asthma, atopic dermatitis, allergies, multiple myeloma, arteriosclerosis, cardiovascular disease, liver disease, cerebrovascular disease, thrombosis, neoangiogenesis-related diseases, including cancer, rheumatism, diabetic retinopathy; macular degeneration and brain disorder, hyperlipidemia, kidney ischemia, diabetes, hypertension, tumor proliferation and metastasis; and metabolic disorders. Additionally, carotenoids and astaxanthin may be useful in the prevention and treatment of fatigue, for improving kidney function in nephropathy from inflammatory diseases, as well as prevention and treatment of other life habit-related diseases. Still further, astaxanthin has been found to play a role as inhibitors of various biological processes, including interleukin inhibitors, phosphodiesterase inhibitors, phospholipase A2 inhibitors, cyclooxygenase-2 inhibitors, matrix metalloproteinase inhibitors, capillary endothelium cell proliferation inhibitors, lipoxygenase inhibitors. See, e.g., Japanese Publication No. 2006022121, published 20060126 (JP Appl No. 2005-301156 filed 20051017); Japanese Publication No. 2006016408, published 20060119 (JP Appl No. 2005-301155 filed 20051017); Japanese Publication No. 2006016409, published 20060119 (JP Appl No. 2005-301157 filed 20051017); Japanese Publication No. 2006016407, published 20060119 (JP Appl No. 2005-301153 filed 20051017); Japanese Publication No. 2006008717, published 20060112 (JP Appl No. 2005-301151 filed 20051017); Japanese Publication No. 2006008716, published 20060112 (JP Appl No. 2005-301150 filed 20051017); Japanese Publication No. 2006008720, published 20060112 (JP Appl No. 2005-301158 filed 20051017); Japanese Publication No. 2006008719, published 20060112 (JP Appl No. 2005-301154 filed 20051017); Japanese Publication No. 2006008718, published 20060112 (JP Appl No. 2005-301152 filed 20051017); Japanese Publication No. 2006008713, published 20060112 (JP Appl No. 2005-301147 filed 20051017); Japanese Publication No. 2006008715, published 20060112 (JP Appl No. 2005-301149 filed 20051017); Japanese Publication No. 2006008714, published 20060112 (JP Appl No. 2005-301148 filed 20051017); and Japanese Publication No. 2006008712, published 20060112 (JP Appl No. 2005-301146 filed 20051017).
As other non-limiting examples, retinolic compounds produced according to the present invention may be used in pharmaceuticals, foodstuff, dietary supplements, electro-optic applications, animal feed additives, cosmetics, etc.
It will be appreciated that, in some embodiments of the invention, carotenoids and/or retinolic compounds produced by manipulated host cells as described herein are incorporated into a final product (e.g., food or feed supplement, pharmaceutical, cosmetic, dye-containing item, etc.) in the context of the host cell. For example, host cells may be lyophilized, freeze dried, frozen or otherwise inactivated, and then whole cells may be incorporated into or used as the final product. The host cell may also be processed prior to incorporation in the product to increase bioavailability (e.g., via lysis). Alternatively or additionally, a final product may incorporate only a portion of the host cell (e.g., fractionated by size, solubility), separated from the whole. For example, in some embodiments of the invention, lipid droplets are isolated from the host cells and are incorporated into or used as the final product. For instance, inventive carotenoid-containing and/or retinolic compound-containing lipid bodies (e.g., from engineered cells, and particularly from engineered fungal cells) may be substituted for the plant oil bodies described in U.S. Pat. No. 6,599,513 (the entire contents of which are hereby incorporated by reference) and incorporated into emulsion or emulsion formulations, as described therein. In other embodiments, the carotenoids and/or retinolic compounds themselves, or individual carotenoid and/or retinolic compounds are isolated and reformulated into a final product.
As stated above, fatty acid and glucoside esters are the predominant carotenoid esters found in nature, whereas additional esters (e.g. with organic acids or inorganic phosphate) can be synthesized to generate useful product forms. For delivery, carotenoid esters can also be formulated as salts of the ester form. See, e.g., US Publication No. 20050096477.
The amount of carotenoid and/or retinolic compound incorporated into a given product may vary dramatically depending on the product, and the particular carotenoid(s) and/or retinolic compound(s) involved. Amounts may range, for example, from less than 0.01% by weight of the product, to more than 1%, 10%, 20%, 30% or more; in some cases the carotenoid and/or retinolic compound may comprise 100% of the product. Thus, amount of carotenoid and/or retinolic compound incorporated into a given product may be, for example, 0.01%, 0.02%, 0.03%, 0.04%, 0.05%, 0.06%, 0.07%, 0.08%, 0.09%, 0.1%, 0.2%, 0.3%, 0.4%, 0.5%, 0.6%, 0.7%, 0.8%, 0.9%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%.
In some embodiments of the invention, one or more produced carotenoids and/or retinolic compounds is incorporated into a component of food or feed (e.g., a food supplement). Types of food products into which carotenoids and/or retinolic compounds can be incorporated according to the present invention are not particularly limited, and include beverages such as milk, water, sports drinks, energy drinks, teas, juices, and liquors; confections such as jellies and biscuits; fat-containing foods and beverages such as dairy products; processed food products such as rice and soft rice (or porridge); infant formulas; breakfast cereals; or the like. In some embodiments, one or more produced carotenoids and/or retinolic compounds is incorporated into a dietary supplements, such as for example a multivitamin. In certain embodiments, beta-carotene produced according to the present invention is included in a dietary supplement. In certain embodiments, lutein produced according to the present invention is included in a dietary supplement. In certain embodiments, retinol, retinal, retinyl palmitate, retinyl acetate, and/or retinoic acid produced according to the present invention is included in a dietary supplement. In some embodiments of this aspect of the invention, it may be useful to incorporate the carotenoids and/or retinolic compounds within bodies of edible lipids as it may facilitate incorporation into certain fat-containing food products. Thus, for example, when the edible fungus, Candida utilis is used as a host, its' carotenoid and/or retinolic compound containing lipids may be directly incorporated into a component of food or feed (e.g., a food supplement).
Examples of feedstuffs into which carotenoids and/or retinolic compounds produced in accordance with the present invention may be incorporated include, for instance, pet foods such as cat foods, dog foods and the like, feeds for aquarium fish, cultured fish or crustaceans, etc., feed for farm-raised animals (including livestock and further including fish or crustaceans raised in aquaculture). Food or feed material into which the carotenoid(s) and/or retinolic compound(s) produced in accordance with the present invention is incorporated is preferably palatable to the organism which is the intended recipient. This food or feed material may have any physical properties currently known for a food material (e.g., solid, liquid, soft).
In some embodiments, feedstuffs containing carotenoids and/or retinolic compounds produced in accordance with the present invention are substantially free of intact host cells. For example, feedstuffs of the present invention may be at least about 95% free of intact host cells. In some embodiments, feedstuffs of the present invention are at least about 96%, 97%, 98%, or 99% or more free of intact host cells. Such embodiments are typical when the carotenoids and/or retinolic compounds are highly purified away from the host cell in which they were produced (see section entitled “Production and Isolation of Carotenoids and/or Retinolic Compounds”).
In some embodiments, feedstuffs containing carotenoids and/or retinolic compounds produced in accordance with the present invention are not substantially free of intact host cells. For example, feedstuffs of the present invention may comprise greater than about 95% intact host cells. In certain embodiments, feedstuffs of the present invention comprise greater than about 70%, 75%, 85%, or 90% intact host cells. In certain embodiments, feedstuffs of the present invention comprise nearly intact host cells. For example, feedstuffs of the present invention may comprise greater than about 70%, 75%, 85%, 90%, or 95% nearly intact host cells. As will be appreciated by those of ordinary skill in the art, carotenoid and/or retinolic compound-containing feedstuffs of the present invention that contain intact cells and/or nearly intact cells will have great utility in providing the carotenoids and/or retinolic compounds of interest present in such host cells to an animal. Such embodiments are advantageous when host cells that produce the carotenoids and/or retinolic compounds of interest contain additional vitamins, nutrients, etc. that benefit the animal.
In some embodiments of the invention, one or more produced carotenoids and/or retinolic compounds is incorporated into a cosmetic product. Examples of such cosmetics include, for instance, skin cosmetics (e.g., lotions, emulsions, creams and the like), lipsticks, anti-sunburn cosmetics, makeup cosmetics, fragrances, products for daily use (e.g., toothpastes, mouthwashes, bad breath preventive agents, solid soaps, liquid soaps, shampoos, conditioners), etc.
In some embodiments, one or more produced carotenoids and/or retinolic compounds is incorporated into a pharmaceutical. Examples of such pharmaceuticals include, for instance, various types of tablets, capsules, drinkable agents, troches, gargles, etc. In some embodiments, the pharmaceutical is suitable for topical application. Dosage forms are not particularly limited, and include capsules, oils, granula, granula subtilae, pulveres, tabellae, pilulae, trochisci, or the like. Oils and oil-filled capsules may provide additional advantages both because of their lack of ingredient decomposition during manufacturing, and because inventive carotenoid-containing and/or retinolic compound-containing lipid droplets may be readily incorporated into oil-based formulations.
Pharmaceuticals according to the present invention may be prepared according to techniques established in the art including, for example, the common procedure as described in the United States Pharmacopoeia, for example.
Carotenoids and/or retinolic compounds produced according to the present invention may be incorporated into any pigment-containing product including, for example, fabric, paint, etc. They may also be incorporated into a product which is an environmental indicator, or an instrument such as a biosensor for use as a detection agent.
Carotenoids and/or retinolic compounds produced according to the present invention (whether isolated or in the context of lipid droplets or of cells, e.g., fungal cells) may be incorporated into products as described herein by combinations with any of a variety of agents. For instance, such carotenoids and/or retinolic compounds may be combined with one or more binders or fillers. In some embodiments, inventive products will include one or more chelating agents, pigments, salts, surfactants, moisturizers, viscosity modifiers, thickeners, emollients, fragrances, preservatives, etc., and combinations thereof.
Useful surfactants include, for example, anionic surfactants such as branched and unbranched alkyl and acyl hydrocarbon compounds, sodium dodecyl sulfate (SDS); sodium lauryl sulfate (SLS); sodium lauryl ether sulfate (SLES); sarconisate; fatty alcohol sulfates, including sodium, potassium, ammonium or triethanolamine salts of C10 to C18 saturated or unsaturated forms thereof; ethoxylated fatty alcohol sulfates, including alkyl ether sulfates; alkyl glyceryl ether sulfonate, alpha sulpho fatty acids and esters; fatty acid esters of isethionic acid, including Igepon A; acyl (fatty) N-methyltaurides, including Igepon T; dialkylsulfo succinate esters, including C8, C10 and C12 forms thereof; Miranot BT also referred to as lauroamphocarboxyglycinate and sodium tridecath sulfate; N-acylated amino acids, such as sodium N-lauroyl sarconisate or gluconate; sodium coconut monoglyceride sulfonate; and fatty acid soaps, including sodium, potassium, DEA or TEA soaps.
Among the cationic surfactants that are useful are monoalkyl trimethyl quartenary salts; dialkyl dimethyl quartenary salts; ethoxylated or propoxylated alkyl quaternary ammonium salts, also referred to in the art as ethoquats and propoquats; cetyl benzylmethylalkyl ammonium chloride; quaternized imidazolines, which are generally prepared by reacting a fat or fatty acid with diethylenetriamine followed by quaternization, and non-fat derived cationic polymers such as the cellulosic polymer, Polymer JR (Union Carbide).
Further useful cationic surfactants include lauryl trimethyl ammonium chloride; cetyl pyridinium chloride; and alkyltrimethylammonium bromide. Cationic surfactants are particularly useful in the formulation of hair care products, such as shampoos, rinses and conditioners.
Useful nonionic surfactants include polyethoxylated compounds and polypropoxylated products. Examples of ethoxylated and propoxylated non-ionic surfactants include ethoxylated anhydrohexitol fatty esters, for example Tween 20; mono- and diethanolamides; Steareth-20, also known as Volpo20; polyethylene glycol fatty esters (PEGs), such as PEG-8-stearate, PEG-8 distearate; block co-polymers, which are essentially combinations of hydrophylic polyethoxy chains and lipophilic polypropoxy chains and generically known as Poloaxamers.
Still other useful non-ionic surfactants include fatty esters of polyglycols or polyhydric alcohols, such as mono and diglyceride esters; mono- and di-ethylene glycol esters; diethylene glycol esters; sorbitol esters also referred to as Spans; sucrose esters; glucose esters; sorbitan monooleate, also referred to as Span80; glyceryl monostearate; and sorbitan monolaurate, Span20 or Arlacel 20.
Yet other useful nonionic surfactants include polyethylene oxide condensates of alkyl phenols and polyhydroxy fatty acid amide surfactants which may be prepared as for example disclosed in U.S. Pat. No. 2,965,576.
Examples of amphoteric surfactants which can be used in accordance with the present invention include betaines, which can be prepared by reacting an alkyldimethyl tertiary amine, for example lauryl dimethylamine with chloroacetic acid. Betaines and betaine derivatives include higher alkyl betaine derivatives including coco dimethyl carboxymethyl betaine; sulfopropyl betaine; alkyl amido betaines; and cocoamido propyl betaine. Sulfosultaines which may be used include for example, cocoamidopropyl hydroxy sultaine. Still other amphoteric surfactants include imidazoline derivatives and include the products sold under the trade name “Miranol” described in U.S. Pat. No. 2,528,378 which is incorporated herein by reference in its entirety. Still other amphoterics include phosphates for example, cocamidopropyl PG-dimonium chloride phosphate and alkyldimethyl amine oxides.
Suitable moisturizers include, for example, polyhydroxy alcohols, including butylene glycol, hexylene glycol, propylene glycol, sorbitol and the like; lactic acid and lactate salts, such as sodium or ammonium salts; C3 and C6 diols and triols including hexylene glycol, 1,4 dihydroxyhexane, 1,2,6-hexane triol; aloe vera in any of its forms, for example aloe vera gel; sugars and starches; sugar and starch derivatives, for example alkoxylated glucose; hyaluronic acid; lactamide monoethanolamine; acetamide monoethanolamine; glycolic acid; alpha and beta hydroxy acids (e.g. lactic, glycolic salicylic acid); glycerine; pantheol; urea; vaseline; natural oils; oils and waxes (see: the emollients section herein) and mixtures thereof.)
Viscosity modifiers that may be used in accordance with the present invention include, for example, cetyl alcohol; glycerol, polyethylene glycol (PEG); PEG-stearate; and/or Keltrol.
Appropriate thickeners for use in inventive products include, for example, gelling agents such as cellulose and derivatives; Carbopol and derivatives; carob; carregeenans and derivatives; xanthane gum; sclerane gum; long chain alkanolamides; bentone and derivatives; Kaolin USP; Veegum Ultra; Green Clay; Bentonite NFBC; etc.
Suitable emollients include, for example, natural oils, esters, silicone oils, polyunsaturated fatty acids (PUFAs), lanoline and its derivatives and petrochemicals.
Natural oils which may be used in accordance with the present invention may be obtained from sesame; soybean; apricot kernel; palm; peanut; safflower; coconut; olive; cocoa butter; palm kernel; shea butter; sunflower; almond; avocado; borage; carnauba; hazel nut; castor; cotton seed; evening primrose; orange roughy; rapeseed; rice bran; walnut; wheat germ; peach kernel; babassu; mango seed; black current seed; jojoba; macademia nut; sea buckthorn; sasquana; tsubaki; mallow; meadowfoam seed; coffee; emu; mink; grape seed; thistle; tea tree; pumpkin seed; kukui nut; and mixtures thereof.
Esters which may be used include, for example, C8-C30 alkyl esters of C8-C30 carboxylic acids; C1-C6 diol monoesters and diesters of C8-C30 carboxylic acids; C10-C20 alcohol monosorbitan esters, C10-C20 alcohol sorbitan di- and tri-esters; C10-C20 alcohol sucrose mono-, di-, and tri-esters and C10-C20 fatty alcohol esters of C2-C6 2-hydroxy acids and mixtures thereof. Examples of these materials include isopropyl palmitate; isopropyl myristate; isopropyl isononate; C12/C14 benzoate ester (also known as Finesolve); sorbitan palmitate, sorbitan oleate; sucrose palmitate; sucrose oleate; isostearyl lactate; sorbitan laurate; lauryl pyrrolidone carboxylic acid; panthenyl triacetate; and mixtures thereof.
Further useful emollients include silicone oils, including non-volatile and volatile silicones. Examples of silicone oils that may be used in the compositions of the present invention are dimethicone; cyclomethycone; dimethycone-copolyol; aminofunctional silicones; phenyl modified silicones; alkyl modified silicones; dimethyl and diethyl polysiloxane; mixed C1-C30 alkyl polysiloxane; and mixtures thereof. Additionally useful silicones are described in U.S. Pat. No. 5,011,681 to Ciotti et al., incorporated by reference herein.
A yet further useful group of emollients includes lanoline and lanoline derivatives, for example lanoline esters.
Petrochemicals which may be used as emollients in the compositions of the present invention include mineral oil; petrolatum; isohexdecane; permethyl 101; isododecanol; C11-C12 Isoparrafin, also known as Isopar H.
Among the waxes which may be included in inventive products are animal waxes such as beeswax; plant waxes such as carnauba wax, candelilla wax, ouricurry wax, Japan wax or waxes from cork fibres or sugar cane. Mineral waxes, for example paraffin wax, lignite wax, microcrystalline waxes or ozokerites and synthetic waxes may also be included.
Exemplary fragrances for use in inventive products include, for instance, linear and cyclic alkenes (i.e. terpenes); primary, secondary and tertiary alcohols; ethers; esters; ketones; nitrites; and saturated and unsaturated aldehydes; etc.
Examples of synthetic fragrances that may be used in accordance with the present invention include without limitation acetanisole; acetophenone; acetyl cedrene; methyl nonyl acetaldehyde; musk anbrette; heliotropin; citronellol; sandella; methoxycitranellal; hydroxycitranellal; phenyl ethyl acetate; phenylethylisobutarate; gamma methyl ionone; geraniol; anethole; benzaldehyde; benzyl acetate; benzyl salicate; linalool; cinnamic alcohol; phenyl acetaldehyde; amyl cinnamic aldehyde; caphore; p-tertiary butyl cyclohexyl acetate; citral; cinnamyl acetate; citral diethyl acetal; coumarin; ethylene brasslate; eugenol; l-menthol; vanillin; etc.
Examples of natural fragrances of use herein include without limitation lavandin; heliotropin; sandlewood oil; oak moss; pathouly; ambergris tincture; ambrette seed absolute; angelic root oil; bergamont oil; benzoin Siam resin; buchu leaf oil; cassia oil; cedarwood oil; cassia oil; castoreum; civet absolute; chamomile oil; geranium oil; lemon oil; lavender oil; Ylang Ylang oil; etc.
A list of generally used fragrance materials can be found in various reference sources, for example, “Perfume and Flavor Chemicals”, Vols. I and II; Steffen Arctander Allured Pub. Co. (1994) and “Perfumes: Art, Science and Technology”; Muller, P. M. and Lamparsky, D., Blackie Academic and Professional (1994) both incorporated herein by reference.
Suitable preservatives include, among others, (e.g., sodium metabisulfite; Glydant Plus; Phenonip; methylparaben; Germall 115; Germaben II; phytic acid; sodium lauryl sulfate (SLS); sodium lauryl ether sulfate (SLES); Neolone; Kathon; Euxyl and combinations thereof), anti-oxidants (e.g., butylated hydroxytoluened (BHT); butylated hydroxyanisol (BHA); ascorbic acid (vitamin C); tocopherol; tocopherol acetate; phytic acid; citric acid; pro-vitamin A.
In some embodiments, inventive products will comprise an emulsion (e.g., containing inventive lipid bodies), and may include one or more emulsifying agents (e.g., Arlacel, such as Alacel 165; Glucamate; and combinations thereof) and/or emulsion stabilizing agents.
In some embodiments, inventive products will include one or more biologically active agents other than the carotenoid(s). To give but a few examples, inventive cosmetic or pharmaceutical products may include one or more biologically active agents such as, for example, sunscreen actives, anti-wrinkle actives, anti-aging actives, whitening actives, bleaching actives, sunless tanning actives, anti-microbial actives, anti-acne actives, anti-psoriasis actices, anti-eczema actives, antioxidants, anesthetics, vitamins, protein actives, etc.
EXEMPLIFICATION
Table 26 below describes certain Yarrowia lipolytica strains used in the following exemplification:







TABLE 26





Yarrowia lipolytica strains.

















NRRL Y-1095
Wild type diploid



ATCC76861
MATB ura2-21 lyc1-5 LYS1-5B



ATCC76982
MATB ade1 leu2-35 lyc1-5 xpr2



ATCC201249
MATA ura3-302 leu2-270 lys8-




11 PEX17-HA



MF346
MATA ura2-21
ATCC76861 × 




ATCC201249


MF350
MATB ura2-21 leu2-35 ade1
ATCC76982 ×




MF346









(The genotypes at LYC1, LYS1, XPR2, and PEX17 were not determined in crosses nor verified for ATCC strains.)
All basic molecular biology and DNA manipulation procedures described herein are generally performed according to Sambrook et al. or Ausubel et al. (Sambrook J, Fritsch E F, Maniatis T (eds). 1989. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press: New York; Ausubel F M, Brent R, Kingston R E, Moore D D, Seidman J G, Smith J A, Struhl K (eds). 1998. Current Protocols in Molecular Biology. Wiley: New York).
Example 1
Production of Plasmids for Carotenoid Strain Construction
Plasmids were generated for construction of carotenoid producing strains. The following subparts describe production of plasmids encoding carotenogenic polypeptides. Plasmids used in these studies and details of their construction are described in Table 27. Additional plasmid construction details and descriptions of their use are found in the text of the relevant subsection. All PCR amplifications used NRRL Y-1095 genomic DNA as template unless otherwise specified. The URA5 gene described below is allelic with the ura2-21 auxotrophy above. The GPD1 and TEF1 promoters are from Y. lipolytica as is the XPR2 terminator.
GGS1 is the gene encoding the Y. lipolytica gene encoding geranylgeranylpyrophosphate synthase. The nucleic acid coding sequence, and encoded Ggs1 protein of pMB4591 and pMB4683 are as follows:







(SED ID NO: 1)


atggattataacagcgcggatttcaaggagatatggggcaaggccgccga


caccgcgctgctgggaccgtacaactacctcgccaacaaccggggccaca


acatcagagaacacttgatcgcagcgttcggagcggttatcaaggtggac


aagagcgatctcgagaccatttcgcacatcaccaagattttgcataactc


gtcgctgcttgttgatgacgtggaagacaactcgatgctccgacgaggcc


tgccggcagcccattgtctgtttggagtcccccaaaccatcaactccgcc


aactacatgtactttgtggctctgcaggaggtgctcaagctcaagtctta


tgatgccgtctccattttcaccgaggaaatgatcaacttgcatagaggtc


agggtatggatctctactggagagaaacactcacttgcccctcggaagac


gagtatctggagatggtggtgcacaagaccggtggactgtttcggctggc


tctgagacttatgctgtcggtggcatcgaaacaggaggaccatgaaaaga


tcaactttgatctcacacaccttaccgacacactgggagtcatttaccag


attctggatgattacctcaacctgcagtccacggaattgaccgagaacaa


gggattctgcgaagatatcagcgaaggaaagttttcgtttccgctgattc


acagcatacgcaccaacccggataaccacgagattctcaacattctcaaa


cagcgaacaagcgacgcttcactcaaaaagtacgccgtggactacatgag


aacagaaaccaagagtttcgactactgcctcaagaggatacaggccatgt


cactcaaggcaagttcgtacattgatgatctagcagcagctggccacgat


gtctccaagctacgagccattttgcattattttgtgtccacctctgactg


tgaggagagaaagtactttgaggatgcgcagtga


 


(SEQ ID NO: 2)


mdynsadfkeiwgkaadtallgpynylannrghnirehliaafgavikvd


ksdletishitkilhnssllvddvednsmlrrglpaahclfgvpqtinsa


nymyfvalqevlklksydavsifteeminlhrgqgmdlywretltcpsed


eylemvvhktgglfrlalrlmlsvaskqedhekinfdlthltdtlgviyq


ilddylnlqsteltenkgfcedisegkfsfplihsirtnpdnheilnilk


qrtsdaslkkyavdymrtetksfdyclkriqamslkassyiddlaaaghd


vsklrailhyfvstsdceerkyfedaq













TABLE 27







Plasmids













Oligos 


Plasmid
Backbone
Insert
or source





pMB4529
PCR2.1
3.4 kb ADE1 PCR
MO4475 &




product
MO4476


pMB4534
PCR2.1
2.1 kb LEU2 PCR
MO4477 &




product
MO4478


pMB4535
PCR2.1
1.2 kb URA5 PCR
MO4471 &




product
MO4472


pMB4589
pMB4535 
1.2 kb GPD1 promoter
MO4568 &



(KpnI + SpeI)
(KpnI + NotI); 0.14 kb
MO4591;




XPR2 terminator (NotI +
MO4566 &




SpeI)
MO4593


pMB4590
pMB4535 
0.4 kb TEF1 promoter
MO4571 &



(KpnI + SpeI)
(KpnI + NotI); 0.14 kb
MO4592;




XPR2 terminator (NotI +
MO4566 &




SpeI)
MO4593


pMB4591
pMB4590 
1.0 kb GGS1 ORF (XbaI
MO4534 &



(NheI + MluI)
+ MluI)
MO4544


pMB4597
pMB4534 
GPD1 promoter & XPR2
From 



(Acc65I +SpeI)
terminator (Acc65I +
pMB4589




SpeI)



pMB4603
pMB4597 
Residual backbone
From 



(RsrII + MluI)
& TEF1 promoter (RsrII +
pMB4590




MluI)



pMB4616
pMB4529 
Residual backbone
From 



(RsrII + SpeI)
& GPD1 promoter &
pMB4589




XPR2 terminator (RsrII +





SpeI)



pMB4629
pMB4616 
Residual backbone
From 



(RsrII + MluI)
& TEF1 promoter (RsrII +
pMB4590




MluI)



pMB4631
pMB4603 
1.2 kb GPD1 promoter
MO4568 &



(KpnI + NheI)
(KpnI + NheI);
MO4659


pMB4628
pMB4603
carRP
See 1A


pMB4637
pMB4629 
1.5 kb hmg1trunc ORF
See 1D



(NheI + MluI)
(XbaI + MluI)



pMB4714
pMB4691 
1.5 kb hmg1trunc ORF
See 1D



(NheI + MluI)
(XbaI + MluI)



pMB4638
pMB4629
carB(i−)
See 1B


pMB4660
pMB4638 (+URA 3)
carB(i−)
See 1C


pMB4662
pMB4631 
1.8 kb URA3 fragment
See 1C



(SpeI + XhoI)
(SpeI + BsaI



pMB4683
pMB4662 (Acc65I +
1.4 kb tef1p-GGS1
From 



MluI)
fragment (Acc65I +
pMB4591




MluI)



pMB4692
pMB4662 (Acc65I +
0.4 kb TEF1 promoter
See 1E



MluI)
(Acc65I + NheI); 0.55 kb





crtZ ORF (XbaI + MluI)



pMB4698
pMB4629 
0.9 kb crtW ORF (XbaI +
See 1F



(NheI + MluI)
MluI)



pMB4599
pBluescriptSKII-
1.9 kb carRP gene
See 1A



(EcoRV)




pMB4606
pBluescriptSKII-
1.9 kb carB gene
See 1A



(EcoRV)




pMB4613
pMB4599 (Acc65I +
carRP(i−)
See 1A



PpuMI)




pMB4619
pBluescriptSKII- 
carB(i−)
See 1A



(BamHI + Acc65I))




pMB4705
pMB4603 
carRP(i−)
See 1A



(NheI + MluI)




pMB4691
pMB4662 
0.4 kb TEF1 promoter
From 



(Acc65I + MluI)
(Acc65I + MluI)
pMB4629


pMB4751
pMB4691
0.75 kb YALI0D12903g
Inserted 




promoter + 0.45 Y.
between




lipoltyica HIS3
TEF1p/




terminator
XPRt and





URA3


pMB4719
pMB4691
crtZ (E. litoralis)
See 1J



(NheI + MluI)




pMB4778
pMB4751 
crtZ (P. bermudensis)
See 1I



(NheI + MluI)




pMB4741
pMB4629
crtW (Aurantimonas)
See 1G



(NheI + MluI)




pMB4735
pMB4629 
crtW (P. bermudensis)
See 1H



(NheI + MluI)




pMB4812
pMB4603 
al-2 (N. crassa)
See 1K



(NheI + MluI)




pMB4846
pMB4691 
crtZ (Erythrobacter sp.
See 1L



(NheI + MluI)
NAP1)



pMB4835
pMB4691 
S. alaskensis)
See 1M



(NheI + MluI)




pMB4845
pMB4691
crtZ (R. biformata)
See 1N



(NheI + MluI)




pMB4837
pMB4691 
crtZ (X. autrophicus)
See 1O



(NheI + MluI)




pMB4850
pMB4691
crtZ (P. putida)
See 1P



(NheI + MluI)









Certain oligonucleotides referred to in Table 27 above are as follows:









MO4471







(SEQ ID NO: 3)









5′-CTGGGTGACCTGGAAGCCTT


 



MO4472







(SEQ ID NO: 4)









5′-AAGATCAATCCGTAGAAGTTCAG


 



MO4475







(SEQ ID NO: 5)









5′-AAGCGATTACAATCTTCCTTTGG


 



MO4476







(SEQ ID NO: 6)









5′-CCAGTCCATCAACTCAGTCTCA


 



MO4477







(SEQ ID NO: 7)









5′-GCATTGCTTATTACGAAGACTAC


 



MO4478







(SEQ ID NO: 8)









5′-CCACTGTCCTCCACTACAAACAC


 



MO4534







(SEQ ID NO: 9)









5′-CACAAACGCGTTCACTGCGCATCCTCAAAGT


 



MO4544







(SEQ ID NO: 10)









5′-CACAATCTAGACACAAATGGATTATAACAGCGCGGAT


 



MO4566







(SEQ ID NO: 11)









5′-CACAAACTAGTTTGCCACCTACAAGCCAGAT


 



MO4568







(SEQ ID NO: 12)









5′-CACAAGGTACCAATGTGAAAGTGCGCGTGAT


 



MO4571







(SEQ ID NO: 13)









5′-CACAAGGTACCAGAGACCGGGTTGGCGG


 



MO4591







(SEQ ID NO: 14)









5′-CACAAGCGGCCGCGCTAGCATGGGGATCGATCTCTTATAT


 



MO4592







(SEQ ID NO: 15)









5′-CACAAGCGGCCGCGCTAGCGAATGATTCTTATACTCAGAAG


 



MO4593







(SEQ ID NO: 16)









5′-CACAAGCGGCCGCACGCGTGCAATTAACAGATAGTTTGCC


 



MO4659







(SEQ ID NO: 17)









5′-CACAAGCTAGCTGGGGATGCGATCTCTTATATC






1A: Production of pMB4628 (tef1p-carRP LEU2) and pMB4705 (tef1p-carRP[i−] LEU2) Encoding Phytoene Synthase/Lycopene Cyclase:

Intron-containing carRP was amplified from M. circinelloides (ATCC 90680) genomic DNA using MO4525 and MO4541:









MO4525







(SEQ ID NO: 18)









5′-CACAAACGCGTTTAAATGGTATTTAGATTTCTCATT


 



MO4541







(SEQ ID NO: 19)









5′-CACAATCTAGACACAAATGCTGCTCACCTACATGGA






and the resulting 1.9 kb fragment was phosphorylated with T4 polynucleotide kinase. The resulting fragment was blunt-end ligated into pBluescriptSKII-cleaved with EcoRV, yielding pMB4599. The 1.9 kb XbaI-MluI fragment from pMB4599 was inserted into NheI- and MluI-cleaved pMB4603, yielding pMB4628. The intron containing nucleic acid coding sequence, and encoded CarRP protein (assuming correctly predicted splicing) of pMB4628 are as follows:








(SEQ ID NO: 20)







atgctgctcacctacatggaagtccacctctactacacgctgcctgtgct


gggcgtcctgtcctggctgtcgcggccgtactacacagccaccgatgcgc


tcaaattcaaatttctgacactggttgccttcacgaccgcctccgcctgg


gacaactacattgtctaccacaaggcgtggtcctactgccccacctgcgt


caccgctgtcattggctacgtgcccttggaggagtacatgttcttcatca


tcatgactctgttgaccgtggcattcaccaatctggtgatgcgctggcac


ctgcacagcttctttatcaggcctgaaacgcccgtcatgcagtccgtcct


ggtccgtcttgtccccataacagccttattaatcactgcatacaaggctt


gggtaagcaaacaaacaaatgatgtgccgcatcgcattttaatattaacc


attgcatacacagcatttggcggtccctggaaagccactgttctacggat


catgcattttgtggtacgcctgtccggttttggccttattgtggtttggt


gctggcgagtacatgatgcgtcgtccgctggcggtgctcgtctccattgc


gctgcccacgctgtttctctgctgggtcgatgtcgtcgctattggcgccg


gcacatgggacatttcgctggccacaagcaccggcaagttcgtcgtgccc


cacctgcccgtggaggaattcatgttctttgcgctaattaataccgtttt


ggtatttggtacgtgtgcgatcgatcgcacgatggcgatcctccacctgt


tcaaaaacaagagtccttatcagcgcccataccagcacagcaagtcgttc


ctccaccagatcctcgagatgacctgggccttctgtttacccgaccaagt


gctgcattcagacacattccacgacctgtccgtcagctgggacatcctgc


gcaaggcctccaagtccttttacacggcctctgctgtctttcccggcgac


gtgcgccaagagctcggtgtgctatacgccttttgcagagccacggacga


tctctgcgacaacgagcaggtccctgtgcagacgcgaaaggagcagctga


tactgacacatcagttcgtcagcgatctgtttggccaaaagacaagcgcg


ccgactgccattgactgggacttttacaacgaccaactgcctgcctcgtg


catctctgccttcaagtcgttcacccgtttgcgccatgtgctggaagctg


gagccatcaaggaactgctcgacgggtacaagtgggatttggagcgtcgc


tccatcagggatcaggaggatctcagatattactcagcttgtgtcgccag


cagtgttggtgaaatgtgcactcgcatcatactggcccacgccgacaagc


ccgcctcccgccagcaaacacagtggatcattcagcgtgcgcgtgaaatg


ggtctggtactccaatatacaaacattgcaagagacattgtcaccgacag


cgaggaactgggcagatgctacctgcctcaggattggcttaccgagaagg


aggtggcgctgattcaaggcggccttgcccgagaaattggcgaggagcga


ttgctctcactgtcgcatcgcctcatctaccaggcagacgagctcatggt


ggttgccaacaagggcatcgacaagctgcccagccattgtcaaggcggcg


tgcgtgcggcctgcaacgtctatgcttccattggcaccaagctcaagtct


tacaagcaccactatcccagcagagcacatgtcggcaattcgaaacgagt


ggaaattgctcttcttagcgtatacaacctttacaccgcgccaattgcga


ctagtagtaccacacattgcagacagggaaaaatgagaaatctaaatacc


atttaa


 







(SEQ ID NO: 21)







mlltymevhlyytlpvlgvlswlsrpyytatdalkfkfltlvafttasaw


dnyivyhkawsycptcvtavigyvpleeymffiimtlltvaftnlvmrwh


lhsffirpetpvmqsvlvrlvpitallitaykawhlavpgkplfygscil


wyacpvlallwfgageymmrrplavlvsialptlflcwvdvvaigagtwd


islatstgkfvvphlpveefmffalintvlvfgtcaidrtmailhlfknk


spyqrpyqhsksflhqilemtwafclpdqvlhsdtfhdlsvswdilrkas


ksfytasavfpgdvrqelgvlyafcratddlcdneqvpvqtrkeqlilth


qfvsdlfgqktsaptaidwdfyndqlpascisafksftrlrhvleagaik


elldgykwdlerrsirdqedlryysacvassvgemctriilahadkpasr


qqtqwiiqraremglvlqytniardivtdseelgrcylpqdwltekeval


iqgglareigeerllslshrliyqadelmvvankgidklpshcqggvraa


cnvyasigtklksykhhypsrahvgnskrveiallsvynlytapiatsst


thcrqgkmrnlnti






Alternatively, pMB4599 was also used as a template for PCR amplification using MO4318, MO4643, MO4644, and MO4639:









MO4318







(SEQ ID NO: 22)









5′-GTAAAACGACGGCCAGT



 



MO4643







(SEQ ID NO: 23)









5′-CACACGGTCTCATGCCAAGCCTTGTATGCAGTGATTAA



 



MO4639







(SEQ ID NO: 24)









5′-CCACTGTGTTTGCTGGCGG



 



MO4644







(SEQ ID NO: 25)









5′-CACACGGTCTCTGGCATTTGGCGGTCCCTGGAAA






producing fragments of 0.5 and 0.95 kb, that were subsequently cleaved with Acc65I and BsaI, and BsaI and PpuMI, respectively. These fragments were ligated to pMB4599 that had been digested with Acc65I and PpuMI, yielding pMB4613, harboring intronless carRP. The 1.85 kb XbaI-MluI fragment from pMB4613 was inserted into NheI- and MluI-cleaved pMB4603 to yield pMB4705.

The intronless nucleic acid coding sequence of pMB4705 is as follows, and encodes the same CarRP protein as above:







(SEQ ID NO: 26)







atgctgctcacctacatggaagtccacctctactacacgctgcctgtgct


 


gggcgtcctgtcctggctgtcgcggccgtactacacagccaccgatgcgc


 


tcaaattcaaatttctgacactggttgccttcacgaccgcctccgcctgg


 


gacaactacattgtctaccacaaggcgtggtcctactgccccacctgcgt


 


caccgctgtcattggctacgtgcccttggaggagtacatgttcttcatca


 


tcatgactctgttgaccgtggcattcaccaatctggtgatgcgctggcac


 


ctgcacagcttctttatcaggcctgaaacgcccgtcatgcagtccgtcct


 


ggtccgtcttgtccccataacagccttattaatcactgcatacaaggctt


 


ggcatttggcggtccctggaaagccactgttctacggatcatgcattttg


 


tggtacgcctgtccggttttggccttattgtggtttggtgctggcgagta


 


catgatgcgtcgtccgctggcggtgctcgtctccattgcgctgcccacgc


 


tgtttctctgctgggtcgatgtcgtcgctattggcgccggcacatgggac


 


atttcgctggccacaagcaccggcaagttcgtcgtgccccacctgcccgt


 


ggaggaattcatgttctttgcgctaattaataccgttttggtatttggta


 


cgtgtgcgatcgatcgcacgatggcgatcctccacctgttcaaaaacaag


 


agtccttatcagcgcccataccagcacagcaagtcgttcctccaccagat


 


cctcgagatgacctgggccttctgtttacccgaccaagtgctgcattcag


 


acacattccacgacctgtccgtcagctgggacatcctgcgcaaggcctcc


 


aagtccttttacacggcctctgctgtctttcccggcgacgtgcgccaaga


 


gctcggtgtgctatacgccttttgcagagccacggacgatctctgcgaca


 


acgagcaggtccctgtgcagacgcgaaaggagcagctgatactgacacat


 


cagttcgtcagcgatctgtttggccaaaagacaagcgcgccgactgccat


 


tgactgggacttttacaacgaccaactgcctgcctcgtgcatctctgcct


 


tcaagtcgttcacccgtttgcgccatgtgctggaagctggagccatcaag


 


gaactgctcgacgggtacaagtgggatttggagcgtcgctccatcaggga


 


tcaggaggatctcagatattactcagcttgtgtcgccagcagtgttggtg


 


aaatgtgcactcgcatcatactggcccacgccgacaagcccgcctcccgc


 


cagcaaacacagtggatcattcagcgtgcgcgtgaaatgggtctggtact


 


ccaatatacaaacattgcaagagacattgtcaccgacagcgaggaactgg


 


gcagatgctacctgcctcaggattggcttaccgagaaggaggtggcgctg


 


attcaaggcggccttgcccgagaaattggcgaggagcgattgctctcact


 


gtcgcatcgcctcatctaccaggcagacgagctcatggtggttgccaaca


 


agggcatcgacaagctgcccagccattgtcaaggcggcgtgcgtgcggcc


 


tgcaacgtctatgcttccattggcaccaagctcaagtcttacaagcacca


 


ctatcccagcagagcacatgtcggcaattcgaaacgagtggaaattgctc


 


ttcttagcgtatacaacctttacaccgcgccaattgcgactagtagtacc


 


acacattgcagacagggaaaaatgagaaatctaaataccatttaa






1B: Production of pMB4638 (tef1p-carB ADE1), Encoding Phytoene Dehydrogenase:

Intron-containing carB was amplified from M. circinelloides (ATCC 90680) genomic DNA using MO4530 and MO4542:









MO4530







(SEQ ID NO: 27)









5′-CACAAACGCGTTTAAATGACATTAGAGTTATGAAC



 



MO4542







(SEQ ID NO: 28)









5′-CACAATCTAGACACAAATGTCCAAGAAACACATTGTC






and the resulting 1.9 kb fragment was phosphorylated with T4 polynucleotide kinase and blunt-end ligated into pBS-SKII-cleaved with EcoRV, yielding pMB4606. pMB4606 was then used as a template for PCR amplification using MO4318 and MO4648, and MO4646 and MO4647, and MO4343 and MO4645:










MO4318







(SEQ ID NO: 29)









5′-GTAAAACGACGGCCAGT



 



MO4648







(SEQ ID NO: 30)









5′-CACAAGGTCTCAAGCACGCATCCCGGAACTG



 



MO4646







(SEQ ID NO: 31)









5′-CACACGGTCTCAGGCATGTCGCCCTACGATGC



 



MO4647







(SEQ ID NO: 32)









5′-CACACGGTCTCATGCTTGCACCCACAAAGAATAGG



 



MO4343







(SEQ ID NO: 33)









5′-CAGGAAACAGCTATGAC



 



MO4645







(SEQ ID NO: 34)









5′-CACACGGTCTCTTGCCCATATACATGGTCTGAAACG






producing fragments of 0.4 and 0.85 and 0.7 kb, that were subsequently cleaved with Acc65I and BsaI, and BsaI, and BsaI and BamHI, respectively. These fragments were ligated to pBS-SKII- that had been cut with Acc65I and BamHI, yielding pMB4619, harboring intronless carB. The 1.75 kb XbaI-MluI fragment from pMB4619 was inserted into NheI- and MluI-cleaved pMB4629, yielding pMB4638. The resulting nucleic acid coding sequence and encoded CarB protein of pMB4638 are as follows:








(SEQ ID NO: 35)







atgtccaagaaacacattgtcattatcggtgctggcgtgggtggcacggc


tacagctgctcgtttggcccgcgaaggcttcaaggtcactgtggtggaga


aaaacgactttggtggcggccgctgctccttgatccatcaccagggccat


cgctttgatcagggcccgtcgctctacctgatgcccaagtactttgagga


cgcctttgccgatctggacgagcgcattcaagaccacctggagctgctgc


gatgcgacaacaactacaaggtgcactttgacgacggtgagtcgatccag


ctgtcgtctgacttgacacgcatgaaggctgaattggaccgcgtggaggg


cccccttggttttggccgattcctggatttcatgaaagagacacacatcc


actacgaaagcggcaccctgattgcgctcaagaagaatttcgaatccatc


tgggacctgattcgcatcaagtacgctccagagatctttcgcttgcacct


gtttggcaagatctacgaccgcgcttccaagtacttcaagaccaagaaga


tgcgcatggcattcacgtttcagaccatgtatatgggcatgtcgccctac


gatgcgcctgctgtctacagcctgttgcagtacaccgagttcgctgaagg


catctggtatccccgtggcggcttcaacatggtggttcagaagctagagg


cgattgcaaagcaaaagtacgatgccgagtttatctacaatgcgcctgtt


gccaagattaacaccgatgatgccaccaaacaagtgacaggtgtaacctt


ggaaaatggccacatcatcgatgccgatgcggttgtgtgtaacgcagatc


tggtctatgcttatcacaatctgttgcctccctgccgatggacgcaaaac


acactggcttccaagaaattgacgtcttcttccatttccttctactggtc


catgtccaccaaggtgcctcaattggacgtgcacaacatctttttggccg


aggcttatcaggagagctttgacgaaatcttcaaggactttggcctgcct


tctgaagcctccttctacgtcaatgtgccctctcgcatcgatccttctgc


tgctcccgacggcaaggactctgtcattgtcttggtgcctattggtcata


tgaagagcaagacgggcgatgcttccaccgagaactacccggccatggtg


gacaaggcacgcaagatggtgctggctgtgattgagcgtcgtctgggcat


gtcgaatttcgccgacttgattgagcatgagcaagtcaatgatcccgctg


tatggcagagcaagttcaatctgtggagaggctcaattctgggtttgtct


catgatgtgcttcaggtgctgtggttccgtcccagcacaaaggattctac


cggtcgttatgataacctattctttgtgggtgcaagcacgcatcccggaa


ctggtgttcccattgtccttgcaggaagcaagctcacctctgaccaagtt


gtcaagagctttggaaagacgcccaagccaagaaagatcgagatggagaa


cacgcaagcacctttggaggagcctgatgctgaatcgacattccctgtgt


ggttctggttgcgcgctgccttttgggtcatgtttatgttcttttacttc


ttccctcaatccaatggccaaacgcccgcatcttttatcaataatttgtt


acctgaagtattccgcgttcataactctaatgtcatttaa


 







(SEQ ID NO: 36)







mskkhiviigagvggtataarlaregfkvtvvekndfgggrcslihhqgh


rfdqgpslylmpkyfedafadlderiqdhlellrcdnnykvhfddgesiq


lssdltrmkaeldrvegplgfgrfldfmkethihyesgtlialkknfesi


wdlirikyapeifrlhlfgkiydraskyfktkkmrmaftfqtmymgmspy


dapavysllqytefaegiwyprggfnmvvqkleaiakqkydaefiynapv


akintddatkqvtgvtlenghiidadavvcnadlvyayhnllppcrwtqn


tlaskkltsssisfywsmstkvpqldvhniflaeayqesfdeifkdfglp


seasfyvnvpsridpsaapdgkdsvivlvpighmksktgdastenypamv


dkarkmvlavierrlgmsnfadlieheqvndpavwqskfnlwrgsilgls


hdvlqvlwfrpstkdstgrydnlffvgasthpgtgvpivlagskltsdqv


vksfgktpkprkiementqapleepdaestfpvwfwlraafwvmfmffyf


fpqsngqtpasfinnllpevfrvhnsnvi






1C. Production of pMB4660 (tef1p-carB URA3) Encoding Phytoene Dehydrogenase:

The 4.3 kb XhoI-NotI fragment and the 1.8 kb NotI-SpeI fragment from pMB4638 were ligated to the 1.9 kb BsaI- and SpeI-cleaved URA3 gene generated by PCR amplification of Y. lipolytica genomic DNA using MO4684 and MO4685 to create pMB4660:









MO4684







(SEQ ID NO: 37)









5′-CATTCACTAGTGGTGTGTTCTGTGGAGCATTC



 



MO4685







(SEQ ID NO: 38)









5′-CACACGGTCTCATCGAGGTGTAGTGGTAGTGCAGTG






The resulting nucleic acid coding sequence and encoded CarB(i) protein of pMB4660 are as follows:








(SEQ ID NO: 39)







atgtccaagaaacacattgtcattatcggtgctggcgtgggtggcacggc


tacagctgctcgtttggcccgcgaaggcttcaaggtcactgtggtggaga


aaaacgactttggtggcggccgctgctccttgatccatcaccagggccat


cgctttgatcagggcccgtcgctctacctgatgcccaagtactttgagga


cgcctttgccgatctggacgagcgcattcaagaccacctggagctgctgc


gatgcgacaacaactacaaggtgcactttgacgacggtgagtcgatccag


ctgtcgtctgacttgacacgcatgaaggctgaattggaccgcgtggaggg


cccccttggttttggccgattcctggatttcatgaaagagacacacatcc


actacgaaagcggcaccctgattgcgctcaagaagaatttcgaatccatc


tgggacctgattcgcatcaagtacgctccagagatctttcgcttgcacct


gtttggcaagatctacgaccgcgcttccaagtacttcaagaccaagaaga


tgcgcatggcattcacgtttcagaccatgtatatgggcatgtcgccctac


gatgcgcctgctgtctacagcctgttgcagtacaccgagttcgctgaagg


catctggtatccccgtggcggcttcaacatggtggttcagaagctagagg


cgattgcaaagcaaaagtacgatgccgagtttatctacaatgcgcctgtt


gccaagattaacaccgatgatgccaccaaacaagtgacaggtgtaacctt


ggaaaatggccacatcatcgatgccgatgcggttgtgtgtaacgcagatc


tggtctatgcttatcacaatctgttgcctccctgccgatggacgcaaaac


acactggcttccaagaaattgacgtcttcttccatttccttctactggtc


catgtccaccaaggtgcctcaattggacgtgcacaacattctttttggcc


gaggcttatcaggagagctttgacgaaatcttcaaggactttggcctgcc


ttctgaagcctccttctacgtcaatgtgccctctcgcatcgatccttctg


ctgctcccgacggcaaggactctgtcattgtcttggtgcctattggtcat


atgaagagcaagacgggcgatgcttccaccgagaactacccggccatggt


ggacaaggcacgcaagatggtgctggctgtgattgagcgtcgtctgggca


tgtcgaatttcgccgacttgattgagcatgagcaagtcaatgatcccgct


gtatggcagagcaagttcaatctgtggagaggctcaattctgggtttgtc


tcatgatgtgcttcaggtgctgtggttccgtcccagcacaaaggattcta


ccggtcgttatgataacctattctttgtgggtgcaagcacgcatcccgga


actggtgttcccattgtccttgcaggaagcaagctcacctctgaccaagt


tgtcaagagctttggaaagacgcccaagccaagaaagatcgagatggaga


acacgcaagcacctttggaggagcctgatgctgaatcgacattccctgtg


tggttctggttgcgcgctgccttttgggtcatgtttatgttcttttactt


cttccctcaatccaatggccaaacgcccgcatcttttatcaataatttgt


tacctgaagtattccgcgttcataactctaatgtcatttaa


 







(SEQ ID NO: 40)







mskkhiviigagvggtataarlaregfkvtvvekndfgggrcslihhqgh


rfdqgpslylmpkyfedafadlderiqdhlellrcdnnykvhfddgesiq


lssdltrmkaeldrvegplgfgrfldfmkethihyesgtlialkknfesi


wdlirikyapeifrlhlfgkiydraskyfktkkmrmaftfqtmymgmspy


dapavysllqytefaegiwyprggfnmvvqkleaiakqkydaefiynapv


akintddatkqvtgvtlenghiidadavvcnadlvyayhnllppcrwtqn


tlaskkltsssisfywsmstkvpqldvhniflaeayqesfdeifkdfglp


seasfyvnvpsridpsaapdgkdsvivlvpighmksktgdastenypamv


dkarkmvlavierrlgmsnfadlieheqvndpavwqskfnlwrgsilgls


hdvlqvlwfrpstkdstgrydnlffvgasthpgtgvpivlagskltsdqv


vksfgktpkprkiementqapleepdaestfpvwfwlraafwvmfmffyf


fpqsngqtpasfinnllpevfrvhnsnvi






1D. Production of pMB4637, pMB4714 and pTef-HMG Encoding a Truncated HMG1.

For production of a truncated variant of the HMG-CoA reductase gene, which also encodes a 77 amino acid leader sequence derived from S. cerevisiae, the following oligonucleotides are synthesized:









PRIMER O







(SEQ ID NO: 41)









5′-TTCTAGACACAAAAATGGCTGCAGACCAATTGGTGA



 



PRIMER P







(SEQ ID NO: 42)









5′-CATTAATTCTTCTAAAGGACGTATTTTCTTATC



 



PRIMER Q







(SEQ ID NO: 43)









5′-GTTCTCTGGACGACCTAGAGG



 



MO4658







(SEQ ID NO: 44)









5′-CACACACGCGTACACCTATGACCGTATGCAAAT






Primers O and P are used to amplify a 0.23 kb fragment encoding Met-Ala followed by residues 530 to 604 of the Hmg1 protein of S. cerevisiae, using genomic DNA as template. Primers Q and MO4658 are used to amplify a 1.4 kb fragment encoding the C-terminal 448 residues of the Hmg1 protein of Y. lipolytica, using genomic DNA as template. These fragments are ligated to the appropriate cloning vector, and the resultant plasmids, designated pOP and pQMO4658, are verified by sequencing. The OP fragment is liberated with XbaI and AseI, and the QMO4658 fragment is liberated with MaeI and MluI. These fragments are then ligated to the ADE1 TEF1p expression vector pMB4629 cut with XbaI and MluI to produce pTefHMG.
Alternatively, the native HMG1 gene from Y. lipolytica was amplified without S. cerevisiae sequences using primers MO4658 (described above) and MO4657 (5′-CACACTCTAGACACAAAAATGACCCAGTCTGTGAAGGTGG (SEQ ID NO:45)). The 1.5 kb product was phosphorylated and ligated to pBluescriptSK− that had been cleaved with EcoRV to create pMB4623. The XbaI-MluI fragment containing hmg1trunc was ligated both to NheI-MluI-cleaved MB4629 and to NheI-MluI-cleaved pMB4691 to create pMB4637 and pMB4714, respectively.
The resulting nucleic acid coding sequence and encoded Hmg1trunc protein of pMB4637 and pMB4714 are as follows:







(SEQ ID NO: 46)







atgacccagtctgtgaaggtggttgagaagcacgttcctatcgtcattga


gaagcccagcgagaaggaggaggacacctcttctgaagactccattgagc


tgactgtcggaaagcagcccaagcccgtgaccgagacccgttctctggac


gacctagaggctatcatgaaggcaggtaagaccaagcttctggaggacca


cgaggttgtcaagctctctctcgagggcaagcttcctttgtatgctcttg


agaagcagcttggtgacaacacccgagctgttggcatccgacgatctatc


atctcccagcagtctaataccaagactttagagacctcaaagcttcctta


cctgcactacgactacgaccgtgtttttggagcctgttgcgagaacgtta


ttggttacatgcctctccccgttggtgttgctggccccatgaacattgat


ggcaagaactaccacattcctatggccaccactgagggttgtcttgttgc


ctcaaccatgcgaggttgcaaggccatcaacgccggtggcggtgttacca


ctgtgcttactcaggacggtatgacacgaggtccttgtgtttccttcccc


tctctcaagcgggctggagccgctaagatctggcttgattccgaggaggg


tctcaagtccatgcgaaaggccttcaactccacctctcgatttgctcgtc


tccagtctcttcactctacccttgctggtaacctgctgtttattcgattc


cgaaccaccactggtgatgccatgggcatgaacatgatctccaagggcgt


cgaacactctctggccgtcatggtcaaggagtacggcttccctgatatgg


acattgtgtctgtctcgggtaactactgcactgacaagaagcccgcagcg


atcaactggatcgaaggccgaggcaagagtgttgttgccgaagccaccat


ccctgctcacattgtcaagtctgttctcaaaagtgaggttgacgctcttg


ttgagctcaacatcagcaagaatctgatcggtagtgccatggctggctct


gtgggaggtttcaatgcacacgccgcaaacctggtgaccgccatctacct


tgccactggccaggatcctgctcagaatgtcgagtcttccaactgcatca


cgctgatgagcaacgtcgacggtaacctgctcatctccgtttccatgcct


tctatcgaggtcggtaccattggtggaggtactattttggagccccaggg


ggctatgctggagatgcttggcgtgcgaggtcctcacatcgagacccccg


gtgccaacgcccaacagcttgctcgcatcattgcttctggagttcttgca


gcggagctttcgctgtgttctgctcttgctgccggccatcttgtgcaaag


tcatatgacccacaaccggtcccaggctcctactccggccaagcagtctc


aggccgatctgcagcgtctacaaaacggttcgaatatttgcatacggtca


tag


 







(SEQ ID NO: 47)







mtqsvkvvekhvpiviekpsekeedtssedsieltvgkqpkpvtetrsld


dleaimkagktklledhevvklslegklplyalekqlgdntravgirrsi


isqqsntktletsklpylhydydrvfgaccenvigymplpvgvagpmnid


gknyhipmattegclvastmrgckainagggvttvltqdgmtrgpcvsfp


slkragaakiwldseeglksmrkafnstsrfarlqslhstlagnllfirf


rtttgdamgmnmiskgvehslavmvkeygfpdmdivsvsgnyctdkkpaa


inwiegrgksvvaeatipahivksvlksevdalvelnisknligsamags


vggfnahaanlvtaiylatgqdpaqnvessncitlmsnvdgnllisvsmp


sievgtigggtilepqgamlemlgvrgphietpganaqqlariiasgvla


aelslcsalaaghlvqshmthnrsqaptpakqsqadlqrlqngsnicirs






1E. Production of pMB4692 (URA3 tef1p-crtZ) Encoding N. aromaticovans Carotene Hydroxylase.

The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Novosphingobium aromaticivorans, using Y. lipolytica codon bias:







(SEQ ID NO: 48)







5′-ttctagacacaaaaatgggtggagccatgcagaccctc


 


gctgctatcctgatcgtcctcggtacagtgctcgctatggagtttgtcgc


 


ttggtcttctcataagtatatcatgcatggcttcggatggggatggcata


 


gagaccatcacgagccccatgagggatttcttgagaagaatgacttatac


 


gccatcgttggcgctgccctctcgatactcatgtttgccctcggctctcc


 


catgatcatgggcgctgacgcctggtggcccggaacctggatcggactcg


 


gtgtcctcttctatggtgtcatctataccctcgtgcacgacggtctggtg


 


caccaacgatggtttagatgggtgcctaaacgaggttacgccaaacgact


 


cgtgcaggcccataagctgcaccacgccaccattggcaaggaaggaggcg


 


tctcattcggtttcgtgttcgcccgagatcccgccgttctgaagcaggag


 


cttcgagctcaacgagaagcaggtatcgccgtgctgcgagaggctgtgga


 


cggctagacgcgt






This sequence was cleaved using XbaI and MluI and ligated, along with an Acc65I-NheI EF1 promoter fragment from pMB4629, to pMB4662 cut with Acc65I and MIA to produce pMB4692. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4692 is as follows:







(SEQ ID NO: 49)







mggamqtlaailivlgtvlamefvawsshkyimhgfgwgwhrdhhepheg


 


flekindlyaivgaalsilmfalgspmimgadawwpgtwiglgvlfygvi


 


ytlvhdglvhqrwfrwvpkirgyakirlvqahklhhatigkeggvsfgfv


 


fardpavlkqelraqreagiavlreavdg






1F. Production of pMB4698 (ADE1 tef1p-crtW), Encoding Carotene Ketolase Derived from an Environmental Sample.

The following carotene ketolase (CrtW) ORF sequence was synthesized de novo, based on protein sequence of an environmental sequence isolated from the Sargasso Sea (Genbank accession AACY01034193.1):







(SEQ ID NO: 50)







5′-ttctagacacaaaaatgactcgatctatttcctggcct


 


tccacctactggcacctccagccctcctgttcttcttgggtcgcaaacga


 


attctctcctcaagcccgaaaaggtctcgtcctcgctggtctcattggtt


 


ccgcttggctgcttactctcggacttggcttttcccttcccctccatcaa


 


acgagctggcttctcatcggttgtctcgttctccttagatctttcctgca


 


caccggactttttatcgttgcccatgacgctatgcacgcttctcttgttc


 


ctgaccaccctggccttaaccgttggattggacgtgtctgtcttctcatg


 


tatgctggactctcctacaaaagatgctgccgaaatcaccgtcgacacca


 


ccaagcccctgaaacagttgaagaccctgactaccaacgatgcactaaca


 


acaatatcctcgactggtacgttcactttatgggaaattacctcggatgg


 


caacaattgcttaatctctcttgcgtttggctcgctctcaccttccgtgt


 


ttctgactactctgctcaattcttccacctgctccttttctctgtccttc


 


ctctcatcgtctcctcctgtcaactcttcctcgtgggaacctggctgcca


 


caccgacgaggcgctactactcgacccggcgttaccactcgatccctgaa


 


cttccaccctgctctttccttcgctgcttgctaccacttcggttaccacc


 


gtgaacaccatgaatctccctctactccttggttccaacttcctaaactc


 


cgagaaggttctctcatctaaacgcgt






This sequence was cleaved using XbaI and MluI and ligated to pMB4629 cut with NheI and MluI to produce pMB4698. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtW protein of pMB4698 is as follows:







(SEQ ID NO: 51)







mtrsiswpstywhlqpscsswvanefspqarkglvlagligsawlltlgl


 


gfslplhqtswlligclvllrsflhtglfivahdamhaslvpdhpglnrw


 


igrvcllmyaglsykrccrnhrrhhqapetvedpdyqrctnnnildwyvh


 


fmgnylgwqqllnlscvwlaltfrvsdysaqffhlllfsvlplivsscql


 


flvgtwlphrrgattrpgvttrslnfhpalsfaacyhfgyhrehhespst


 


pwfqlpklregsli






Mutant alleles of this protein (e.g. L200M, F238L/I/V, including combinations thereof) can also be constructed and tested.
1G. Production of pMB4741 (ADE1 tef-crtW), Encoding Aurantimonas Carotene Ketolase.
The following carotene ketolase (CrtW) ORF sequence was synthesized de novo based on protein sequence of Aurantimonas sp. S185-9A1, using Y. lipolytica codon bias:







(SEQ ID NO: 52)







ctctagacacaaaaatgtcttcctttgcccctatgaatgatgttgctatt


 


cctgccggtcaagctcctttctctgcctgtactagaaaacctgtcctgag


 


accttttcaagctgccatcggtcttacactcgccggatgtgttatctctg


 


cttggattgcaatccacgttggagctgtctttttcctcgatgtcggttgg


 


cgaacccttcctgttgttcctgtcctcattgccgttcagtgctggctcac


 


ggtcggtctttttattgtcgcacacgatgctatgcacggctccctcgctc


 


ctggttggccacgacttaacgctcgaattggtgccttcatcctcaccatc


 


tacgctggattcgcttggagacgtgtccgaggagctcacatggcccatca


 


cgacgcccctggtactgccgatgaccctgacttctttgttgatgaacctg


 


accgattttggccttggtttcgagctttcttccttagatattttggacgt


 


cgatctattctctttgtttgcacagttgtcaccgtttacattctggtcct


 


tggagcccctgttcttaatgttgttctcttttacggtcttccttcccttc


 


tgtcttctcttcaactcttttactttggaacttttcgtcctcaccgtcat


 


gaagaagatgatttcgttgacgcccataatgcccgatctaatgaatttgg


 


ttacatcgcctccctcctttcttgctttcactttggataccatcacgaac


 


atcatgccgagccgtgggtcccttggtggggtcttccttctcaatggcgc


 


cagagacaagcctcttcttcccgacaggtcccgggcggccgagacgctgc


 


tgacgccgctggagcatctcgacaacctgccggacgataccgatctgttt


 


cttctcgaggtcgaaatcaggcccgttctcccgcttctggtcgaaacgaa


 


caaatgagataaacgcgt






This sequence was cleaved using XbaI and MluI and ligated to pMB4629 cut with NheI and MluI to produce pMB4741. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtW protein of pMB4741 is as follows:







(SEQ ID NO: 53)







mssfapmndvaipagqapfsactrkpvlrpfqaaigltlagcvisawia


 


ihvgavffldvgwrtlpvvpvliavqcwltvglfivahdamhgslapgw


 


prlnarigafiltiyagfawrrvrgahmahhdapgtaddpdffvdepdr


 


fwpwfrafflryfgrrsilfvctvvtvyilvlgapvlnvvlfyglpsll


 


sslqlfyfgtfrphrheeddfvdahnarsnefgyiasllscfhfgyhhe


 


hhaepwvpwwglpsqwrqrqasssrqvpggrdaadaagasrqpagryrs


 


vssrgrnqarspasgrneqmr






Mutant alleles of this protein (e.g. L201M, A232V/I/L, F240L/I/V, including combinations thereof) can also be constructed and tested.
1H. Production of pMB4735 (ADE1 tef-crtW), Encoding P. bermudensis Carotene Ketolase.
The following carotene ketolase (CrtW) ORF sequence was synthesized de novo based on protein sequence of Parvularcula bermudensis, using Y. lipolytica codon bias:







(SEQ ID NO: 54)







ctctagacacaaaaatggaccctaccggagacgttactgctagccctcg


 


acctcaaaccaccattcctgtccgacaagcactctggggacttagcctt


 


gctggagccatcatcgccgcatgggtttttatgcacattggtttcgttt


 


tttttgccccccttgatcctatcgttctcgccctcgccccagttattat


 


tcttcttcaatcctggctttctgttggtctttttattatttctcacgac


 


gcaattcacggttccctcgcccctggacgacccgcctttaatagagcca


 


tgggacgactctgcatgacactttacgccggtttcgactttgaccgtat


 


ggccgctgcacatcaccgacatcacagatcccctggaaccgccgctgac


 


cccgatttttctgttgactcccctgatcgacctctcccttggtttggag


 


ctttcttccgacgttactttggctggagaccttttcttaccgttaacgc


 


tgtcgtctttacctactggcttgttcttggagctaaccctgttaatatt


 


gttctcttttatggcgttcctgcactcctttccgccggacagctctttt


 


actttggtacatttctccctcaccgacacgaacgacaaggctttgctga


 


tcaccaccgagcacgatccgtccgatccccttacatgctttctcttgtt


 


acttgttaccactttggaggctatcatcacgaacatcatctctttccac


 


acgaaccctggtggcgcctgcctcaacgaggaggttgggaacgtgacag


 


acgaaagagaaccggcccttaacgcgt






This sequence was cleaved using XbaI and MluI and ligated to pMB4629 cut with NheI and MluI to produce pMB4735. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtW protein of pMB4735 is as follows:







(SEQ ID NO: 55)







mdptgdvtasprpqttipvrqalwglslagaiiaawvfmhigfvffapl


 


dpivlalapviillqswlsvglfiishdaihgslapgrpafnramgrlc


 


mtlyagfdfdrmaaahhrhhrspgtaadpdfsvdspdrplpwfgaffrr


 


yfgwrpfltvnavvftywlvlganpvnivlfygvpallsagqlfyfgtf


 


lphrherqgfadhhrarsvrspymlslvtcyhfggyhhehhlfphepww


 


rlpqrggwerdrrkrtgp






Mutant alleles of this protein (e.g. L190M, M110I/V/L, F229L/I/V, including combinations thereof) can also be constructed and tested.
1I. Production of pMB4778 (URA3 tef-crtZ), Encoding P. bermudensis Carotene Hydroxylase.
The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Parvularcula bermudensis, using Y. lipolytica codon bias:







(SEQ ID NO: 56)







ctctagacacaaaaatgactctcgctctctggcaaaagatcaccctcgt


 


ccttggttccgctgctctgatggaaggatttgcttggtgggcccataga


 


tatattatgcacggttggggatgggcttggcatagagatcatcatgaac


 


ctcacgacaaagtttttgaaaaaaatgacctgtttgctgtggtttttgg


 


ctcgttcgcatttggtttgttcatcgtcggttacctttattggccacct


 


gtttggtacgttgctgctggcatcactctttacggacttctttacgcat


 


ttgttcatgacggtttggttcatcaacgttggccctggcatttcatgcc


 


taaacgaggatacctccgaagactggttcaagctcacaaacttcatcat


 


gctgttacaacacaaggcggaaatgtttcgtttggattcgtccttgccc


 


ctgaccctagacatcttagagaaaaacttagacaatttcgtgctgaaag


 


acatcgtgcccttgccgccgaaggtgcttcctcctctgaccctcgtgtt


 


cccccttttcgaaaagttcaagacgtttaaacgcgt






This sequence was cleaved using XbaI and MluI and ligated to pMB4751 cut with NheI and MluI to produce pMB4778. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4778 is as follows:







(SEQ ID NO: 57)







mtlalwqkitlvlgsaalmegfawwahryimhgwgwawhrdhhephdkv


 


fekndlfavvfgsfafglfivgylywppywyvaagitlygllyafvhdg


 


lvhqrwpwhfmpkrgylrrlvqahklhhavttqggnvsfgfvlapdprh


 


lreklrqfraerhralaaegasssdprvppfrkvqdv






1J. Production of pMB4719 (URA3 tef-crtZ), Encoding E. litoralis Carotene Hydroxylase.

The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Erythrobacter litoralis, using Y. lipolytica codon bias:







(SEQ ID NO: 58)







ctctagacacaaaaatgagctggtgggctatcgctcttattgtctttgg


 


tgctgtcgttggaatggaattttttgcttggttcgctcataagtacatt


 


atgcatggttggggatggagctggcaccgagatcatcacgaacctcacg


 


ataatactcttgaaaaaaacgaccttttcgccgttgtctttggctcggt


 


tgccgcacttctgtttgttattggagctctctggtctgatcctctctgg


 


tgggcagcagttggtattacattgtatggcgtcatttacactctggttc


 


acgacggacttgttcatcaacgttactggcgttggacccctaagcgagg


 


ttatgctaagagacttgtccaggcccatcgacttcatcacgctactgtt


 


ggaaaggaaggaggtgtttcttttggttttgtgttcgcccgagatcctg


 


ctaagttgaaagccgaattgaaacaacaaagagaacagggacttgccgt


 


cgttcgagattctatgggagcataaacgcgt






This sequence was cleaved using XbaI and MluI and ligated to pMB4691 cut with NheI and MluI to produce pMB4719. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4719 is as follows:







(SEQ ID NO: 59)







mswwaialivfgavvgmeffawfahkyimhgwgwswhrdhhephdntle


 


kindlfavvfgsvaallfvigalwsdplwwaavgitlygviytlvhdgl


 


vhqrywrwtpkrgyakrlvqahrlhhatvgkeggvsfgfvfardpaklk


 


aelkqqreqglavvrdsmga






1K. Production of pMB4812, Encoding N. crassa Phytoene Synthase/Lycopene Cyclase, al-2.

Exon 1 of al-2 was synthesized by annealing the following oligonucleotides:









MO5017:







(SEQ ID NO: 60)









5′-CTAGACACAAAAATGTACGACTACGCCTTCGT;



 



MO5018:







(SEQ ID NO: 61)









5′-GCACCTGAAGTTCACCGTGCCCGCGGTTCCAA;



 



MO5019:







(SEQ ID NO: 62)









5′-GTGCACGAAGGCGTAGTCGTACATTTTTGTGT;



 



MO5020:







(SEQ ID NO: 63)









5′-CGCGTTGGAACCGCGGGCACGGTGAACTTCAG,






and ligating them to pMB4603 that had been cleaved with NheI and MluI, to create pMB4811. Exon2 was amplified from N. crassa (Fungal Genetic Stock Center #3200) genomic DNA, using MO5016 (5′-CCCGCGGCGGTACTTCT (SEQ ID NO:64)) and MO5013 (5′-CCGTCTCTACAGCAGGATCAGGTCAATGC (SEQ ID NO:65)), and inserted into pCR-TOPO (Invitrogen), to create pMB4809. Exon 3 was similarly amplified with MO5014 (5′-CCGTCTCACTGTACTCCTTCTGTCGCCTG (SEQ ID NO:66)) and MO5015 (5′-CACGCGTCTACTGCTCATACAACGCCCT (SEQ ID NO:67)), and cloned into the same vector to create pMB4810. The 0.9 kb SacII-BsmBI fragment from pMB4809 was ligated together with the 0.9 kb BsmBI-MluI fragment from pMB4810 into SacII-MluI-cleaved pMB4811, to create pMB4812, which expresses al-2 from the TEF1 promoter. The resulting nucleic acid coding sequence and encoded al-2 protein of pMB4812 are as follows:








(SEQ ID NO: 68)







atgtacgactacgccttcgtgcacctgaagttcaccgtgcccgcggcgg


tacttctcaccgctatcgcctaccccattctcaacaggatacatctcat


ccaaacaggcttcctcgtcgtcgtcgcctttaccgccgctctgccatgg


gatgcctacttgattaagcacaaagtatggtcttacccaccagaagcca


ttgttgggccgcgtttgcttggaattccctttgaagagctgttcttctt


tgtgatacagacttacatcacggcgctcgtatacatcctcttcaacaag


ccggtgctgcacgcgttgcacctcaacaatcaacaaaacccgccagcat


ggatgagggttgtcaaggttaccggccaggtagtcctcgtagccttgtc


ggtatggggatggaatgccgctcaggttcatcaggaaacaagctatctc


ggcttgatccttgtttgggcttgtccgttcttactggctatctggaccc


tcgctgggcgcttcattctcagcctaccctggtacgcgacggtgctccc


gatgttcctacccaccttctatctttgggcggtagacgagtttgccttg


cacaggggtacttggtccatcggatcggggacgaagctcgatttttgtc


tgtttggcaagttggacattgaagaagccacgttcttcctggtgaccaa


catgctcatcgttggcggtatggccgcgttcgatcaatatctggccgtc


atttacgctttcccaactctgttccccaaggtcaaccggtatccgacaa


ctcatatgcttcttcaaagccgtcttatcaacacttccaggtacgatct


tgagcgcattgagggcctgagagaagcggtcgagagactgcgcctgaag


agcaggagtttttacctggccaattcgctcttttctggtcgactccgca


ttgacctgatcctgctgtactccttctgtcgcctggctgatgatctagt


cgacgacgccaaatctcgccgtgaggtcttgtcctggaccgcgaagctg


aaccacttccttgatctgcactacaaggacgcggacgccaccgaggacc


ccaagaaaaaggcggagcgaatcgacgcctacatcaagacagcgttccc


tccctgtgcctaccaagccctccacctcctgcccactcacattcttcct


cccaagcctctttacgatctcatcaagggtttcgagatggactctcaat


tcaccttccacggtacttccgactctacggatctccaataccccatcgc


cgacgacaaggaccttgagaactacgctatctatgtcgccggtaccgtc


ggcgagctctgcatcgccctcatcatctaccactgcctgccagacatgt


cggacactcagaagcgcgagctcgagaccgccgcgtgccggatgggcat


cgcgctgcagtacgtcaacatcgctcgtgacatcgtcgtcgacgcacgt


atcgggcgcgtttacttgcctaccacctggctcaagaaggaagggttga


cgcacaagatggtcttggagaaccccgagggtcccgaggtcattgagcg


gatgagaagacggcttttggaaaatgcgtttgagctgtatgggggcgcg


aggcctgagatgcaacggataccgagcgaggctaggggcccgatgattg


gtgccgttgaaaattacatggcgattggaagggtgttgagggagaggaa


ggaggggacggtgtttgtgaggatggaggggagggctacggtcccgaag


cgaaggaggttgagcacgctgttgagggcgttgtatgagcagtag;


 







(SEQ ID NO: 69)







mydyafvhlkftvpaavlltaiaypilnrihliqtgflvvvaftaalpw


daylikhkvwsyppeaivgprllgipfeelfffviqtyitalvyilfnk


pvlhalhlnnqqnppawmrvvkvtgqvvlvalsvwgwnaaqvhqetsyl


glilvwacpfllaiwtlagrfilslpwyatvlpmflptfylwavdefal


hrgtwsigsgtkldfclfgkldieeatfflvtnmlivggmaafdqylav


iyafptlfpkvnryptthmllqsrlintsrydlerieglreaverlrlk


srsfylanslfsgrlridlillysfcrladdlvddaksrrevlswtakl


nhfldlhykdadatedpkkkaeridayiktafppcayqalhllpthilp


pkplydlikgfemdsqftfhgtsdstdlqypiaddkdlenyaiyvagtv


gelcialiiyhclpdmsdtqkreletaacrmgialqyvniardivvdar


igrvylpttwlkkeglthkmvlenpegpeviermrrrllenafelygga


rpemqripseargpmigavenymaigrvlrerkegtvfvrmegratvpk


rrrlstllralyeq






1L. Production of pMB4846 (URA3 tef-crtZ), Encoding an Erythrobacter Carotene Hydroxylase.

The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Erythrobacter sp. NAP1, using Y. lipolytica codon bias:







(SEQ ID NO: 70)







ctctagacacaaaaatgtcttggcctgccgctattgcagttacacttgg


 


tgcccttatttttatggaattctttgcttggtacgctcacaaatacatt


 


atgcatggatggggatggggttggcacagagaccatcacgaacctcacg


 


acaacaaactggaaaaaaatgacctgttcgctgtggttttcggaacaat


 


taacgctggtatgtatatttttggtgctctttattgggatgctttgtgg


 


tgggctgcacttggagttaatctttacggagtgatttacgcccttgttc


 


atgacggactggttcatcaaagatttggaagatacgtccctaaaaacgc


 


atacgctaaacgacttgttcaagcacacagattgcatcacgctactatc


 


ggtaaagaaggaggagtgtccttcggattcgttcttgctcgagaccctg


 


ctaaacttaaagccgaacttaaacgacaatctcaatccggagaagctat


 


tgttcgagaatccgccggagcctaaacgcgt






This sequence was cleaved using XbaI and MluI and ligated to pMB4691 cut with NheI and MluI to produce pMB4846. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4846 is as follows:







(SEQ ID NO: 71)







mswpaaiavtlgalifmeffawyahkyimhgwgwgwhrdhhephdnkle


 


kndlfavvfgtinagmyifgalywdalwwaalgvnlygviyalvhdglv


 


hqrfgryvpknayakrlvqahrlhhatigkeggvsfgfvlardpaklka


 


elkrqsqsgeaivresaga






1M. Production of pMB4835 (URA3 tef-crtZ), Encoding an S. alaskensis Carotene Hydroxylase.

The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Sphingopyxis alaskensis, using Y. lipolytica codon bias:







(SEQ ID NO: 72)







ctctagacacaaaaatgagccaccgaagagatccaggacttagaagaga


 


cgacgcacgatctatggcctcctgtctcagacgagcttacaacccccac


 


atgtccctgcctgcaattttgtttttggttcttgctactgtcattgcaa


 


tggaaggagtcgcctgggcatcccacaaatacatcatgcacggatttgg


 


atgggcctggcacagagaccaccatgaaccccacgacaatcgactcgag


 


aaaaacgacctgtttgccctgttcggagccgctatgtctatttctgcct


 


tcgctattggttctcctatgattatgggtgcagctgcctggaagcctgg


 


aacttggattggacttggtattcttctttacggtattatctacacactc


 


gttcacgacggccttgtgcaccaaagatactttcgatgggtcccacgac


 


gaggttacgcaaaacgacttgttcaagcacacaaacttcatcacgctac


 


aatcggaaaagagggaggagtttctttcggatttgtttttgctcgtgac


 


cctgctaaacttaaagccgaactgaaagcacaacgagaagctggtattg


 


cagtcgtcagagaagcccttgctgactaaacgcgt






This sequence was cleaved using XbaI and MluI and ligated to pMB4691 cut with NheI and MluI to produce pMB4835. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4835 is as follows:







(SEQ ID NO: 73)







mshrrdpglrrddarsmasclrraynphmslpailflvlatviamegva


 


washkyimhgfgwawlirdhhephdnrlekndlfalfgaamsisafaig


 


spmimgaaawkpgtwiglgillygiiytlvhdglvhqryfrwvprrgya


 


krlvqahklhhatigkeggvsfgfvfardpaklkaelkaqreagiavvr


 


ealad






1N. Production of pMB4845 (URA3 tef-crtZ), Encoding an R. biformata Carotene Hydroxylase.

The following carotene hydroxylase (CrtZ) ORF sequence was amplified from genomic DNA extracted from Robiginitalea biformata:







(SEQ ID NO: 74)







cacaatctagacacaaaaatgacagtcttgatttggatcgcaattttcc


 


tggccaccttctgcttcatggaattcatggcctggtttacgcataaata


 


tatcatgcacggtttcctctggagccttcataaggaccaccataaaaag


 


gaccacgacagttggtttgagcgaaacgacgccttctttctattttatg


 


cgatagtctccatgtcctttatcggggccgccgtgaacacgggattctg


 


gcaggggtggcccatcggcctgggcatcctcgcttacgggattgcctac


 


tttatcgtacacgatatctttatccatcagcggttcaagctctttcgca


 


atgcgaataactggtacgcgcggggtatccgcagggcccataaaatcca


 


ccacaagcacctgggaaaagaggaaggggaatgcttcgggatgctgttt


 


gtcccatttaagtacttccggaagacctgaacgcgtttgtg






This sequence was phosphorylated and ligated to pBluescriptSK− that had been cleaved with EcoRV and dephosphorylated, to create pMB4824. The XbaI-MluI fragment from pMB4824 that contains crtZ was ligated to pMB4691 cut with NheI and MluI to produce pMB4845. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4845 is as follows:







(SEQ ID NO: 75)







mtvliwiaiflatfcfmefmawfthkyimhgflwslhkdhhkkdhdswf


 


erndafflfyaivsmsfigaavntgfwqgwpiglgilaygiayfivhdi


 


fihqrfklfrnannwyargirrahkihhkhlgkeegecfgmlfvpfkyf


 


rkt






1O. Production of pMB4837 (URA3 tef-crtZ), Encoding an X. autotrophicus Carotene Hydroxylase.

The following carotene hydroxylase (CrtZ) ORF sequence was amplified from genomic DNA extracted from Xanthobacter autotrophicus:







(SEQ ID NO: 76)







cacaatctagacacaaaaatgtccaccagcctcgccttcctcgtcaacg


 


cgctcatcgtgatcgccacggtcgccgccatggaaggggtggcctggg


 


ccgcgcacaaatatgtcatgcacggcttcggctggggctggcacaagtc


 


ccaccacgagccgcgcgagggcgtgttcgagcgcaacgacctttatgc


 


gctgctgttcgcaggcatcgccatcgccctcatctacgcgttccgcaat


 


ggcggcgcgctgctgtgggtgggcgtggggatgacggtctacggcttcc


 


tttatttcttcgtgcacgacggcatcacccaccagcgctggccgttcc


 


gctacgtgccgcgcaacggctatctcaagcgcctggtgcaggcccacc


 


ggctgcaccatgcggtggatggcaaggagggctgcgtctccttcggctt


 


catctatgccccgccgcctgccgacctgaaggccaagctgaagaagct


 


gcacggcggcagcctgaagcagaacgaggcggcggaatagacgcgt


 


ttgtg






This sequence was phosphorylated and ligated to pBluescriptSK− that had been cleaved with EcoRV and dephosphorylated, to create pMB4823. The XbaI-HindIII (filled in with Klenow) fragment from pMB4823 that contains crtZ was ligated to pMB4691 cut with NheI and MluI (filled in with Klenow) to produce pMB4837. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4837 is as follows:







(SEQ ID NO: 77)







mstslaflvnaliviatvaamegvawaahkyvmhgfgwgwhkshhepr


 


egvferndlyallfagiaialiyafrnggallwvgvgmtvygflyffvh


 


dgithqrwpfryvprngylkrlvqahrlhhavdgkegcvsfgfiyappp


 


adlkaklkklhggslkqneaae






1P. Production of pMB4850 (URA3 tef-crtZ), Encoding a P. putida Carotene Hydroxylase.

The following carotene hydroxylase (CrtZ) ORF sequence was amplified from genomic DNA extracted from Pseudomonas putida (this sequence encodes a valine rather than a leucine at the second position, due to N-end rule considerations):







(SEQ ID NO: 78)







tctctctagacacaaaaatggtgttcaatctcgccatattgttcggcac


 


cctggtggccatggagggcgttggtacgctggctcacaagtacatcatg


 


catggctggggctggtggctgcaccgatcgcaccatgagccacacctg


 


ggcatgctcgaaaccaacgacctgtacctggtggccctggggctgatc


 


gccacggcgctggtggcgctgggcaaaagtggttatgcgcctttgcagt


 


gggtgggcggtggtgtggcaggctatggagcactgtatgtactggccca


 


cgacggtttctttcaccggcactggccgcgcaagccgcggccggtcaa


 


ccgctacctgaaacgcttgcaccgcgcgcaccgcttgcaccatgcggt


 


gaaggggcgcacggggagcgtgtcgttcgggttcttctatgcgccgccg


 


ctgaaggtgttgaagcagcaattgcgcagcaggcgcagccaatcgtgaa


 


cgcgtgagacgttgtg






This sequence was phosphorylated and ligated to pBluescriptSK− that had been cleaved with EcoRV and dephosphorylated, to create pMB4847. The XbaI-MluI fragment from pMB4847 that contains crtZ was ligated to pMB4691 cut with NheI and MluI to produce pMB4850. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4850 is as follows:







(SEQ ID NO: 79)







mvfnlailfgtlvamegvgtlahkyimhgwgwwlhrshhephlgmletn


 


dlylvalgliatalvalgksgyaplqwvgggvagygalyvlahdgffhr


 


hwprkprpvnrylkrlhrahrlhhavkgrtgsvsfgffyapplkvlkqq


 


lrsrrsqs






Example 2
Engineering Yarrowia lipolytica for Increased Carotenoid Production
2A. Production of Y. Lipolytica Expressing Geranylgeranylpyrophosphate Synthase and Phytoene Dehydrogenase:
MF350 (MATB ura2-21 leu2-35 ade1) was transformed with pMB4591 (tef1p-GGS1) that had been cleaved upstream of URA5 with SspI; a Ura− transformant carrying the plasmid at the ura2 locus was identified and named MF364. It was subsequently transformed with pMB4638 (tef1p-carB) that had been cleaved at ADE1 with SspI and a prototrophic transformant was chosen that harbored the plasmid at the ade1 locus. This strain was named MF502.
2B. Production of Y. Lipolytica Expressing Geranylgeranylpyrophosphate Synthase, Phytoene Dehydrogenase and Phytoene Synthase/Lycopene Cyclase
MF502 was transformed with pMB4705 (tef1p-carRP[i−]) that had been treated with SspI. Ninety percent of the prototrophic transformants were very orange on YPD agar plates, and one, MF719, produced greater than 10 mg carotene per g dry cell weight (DCW) after four days of growth in YPD at 30° C.
2C. Production of Y. Lipolytica Expressing Phytoene Synthase/Lycopene Cyclase and Phytoene Dehydrogenase:
ATCC201249 (HATA ura3-302 leu2-270 lys8-11) was transformed with SspI-cleaved pMB4628. Hundreds of Leu+ colonies were pooled, re-grown, and transformed with pMB4660 (tef1p-carB) that had been cleaved upstream of URA3 with SalI. One colony that was noticeably yellow after 5 days at 30° C. on YNBglut media (per liter: 1.7 g yeast nitrogen base, 1 g monosodium glutamate, 1% glucose) plus 0.6 mM lysine was selected, named MF447, and found to produce 0.2 mg carotene per gram dry cell weight after 4 days of growth in YPD.
MF447 was challenged with 1 g/L 5-fluoroorotic acid and Ura− segregants selected. Surprisingly, they were all found to retain the identical yellow appearance of their parent, implying that the loss of a functional URA3 gene did not coincide with the loss of a functional CarB enzyme. Southern analysis demonstrates that two fragments from a KpnI-HindIII digest of MF447 DNA contain URA3p-hybridizing sequences, only one of which also hybridizes to carB. The other is absent in MF578, the Ura3− segregant chosen for further manipulation. Plasmid rescue and analysis of the DNA sequence surrounding tef-carB in MF578 confirmed the absence of nearby URA3 sequences. Plasmid rescue and analysis of the DNA sequence encompassing the carRP intron in MF447 revealed that exons 1 and 2 were contiguous and were each separated by an intron sequence that lacked the original internal SspI site (present in pMB4628). The sequence of this region shows a seven-base pair deletion (AATATTA) that would restore the proper frame to an unspliced message. Partial intron sequence comprising the sequence where the deletion occurred is shown as follows:







(SEQ ID NO: 80)







ACAAACAAATGATGTGCCGCATCGCATTTTAATATTAACCATTGCATACA


 


CAG.






Predicted partial amino acid sequence comprising this intron, if unspliced, is as follows:







(SEQ ID NO: 219)







KAWVSKQTNDVPHRILIPLHTQHLA . . .


 


(VSKQTNDVPHRILIPLHTQ (SEQ ID NO: 81) is intron


encoded)






2D. Production of Y. Lipolytica Expressing Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase:

MF578 was transformed with pMB4683 (tef1p-GGS1) that had been cleaved with SalI (upstream of URA3) or with StuI (within the GGS1 ORF). Ura+ Leu+ colonies in both cases appeared bright orange on YNBglut+Lysine and on YPD, and several produced greater than 4 mg carotene per gram of dry cell weight when grown as above. One, MF633, contained a single copy of the plasmid at the GGS1 locus, as inferred from Southern analysis. The others arose by non-homologous or more complex integrations.
2E. Production of Y. Lipolytica Expressing Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase:
MF364 was crossed with MF578, and spores from the resulting diploid were plated on YPD for two to three days at 30° C. White Leu− Ade− Ura− colonies were screened for the presence of tefp-carB and tefp-GGS1 and for the absence of tefp-carRP by PCR. Thirteen colonies meeting these criteria, as well as displaying resistance to 5-fluorootic acid, an indication that they harbor the ura3-302 allele, were chosen as hosts for further modifications.
One such strain, MF731, was transformed with pMB4705 cut with BbvCI, and one Leu+ orange colony, MF740, produced 6 mg of β-carotene per g DCW after four days of growth in YPD at 30° C.
Another tefp-carB tefp-GGS1 strain from the same cross, MF739, was transformed with pMB4705 cut with BbvCI, and one Leu+ orange colony, MF746, produced 8 mg of β-carotene per g DCW after four days of growth in YPD at 30° C. When this strain was transformed with pMB4812 (expressing N. crassa al-2 protein) treated with SspI, the Leu+ transformants were less orange than parallel pMB4705 Leu+ transformants, and after 4 days of growth in YPD, produced about half the amount of β-carotene as pMB4705 transformants. In addition, the pMB4812 transformants produced significant amounts of γ-carotene ( ̃40% of total carotene.).
2F. Expression of a Truncated Form of HMG-CoA Reductase Results in Increased Carotenoid Production in Y. Lipolytica Expressing Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase, and Geranylgeranylpyrophosphate Synthase:
In order to increase carotenoid production, carbon flow through the isoprenoid pathway is enhanced by introducing a truncated variant of the HMG-CoA reductase gene.
MF740 was transformed with pMB4637 treated with SnaBI, and Ade+ colonies were selected. One such colony, MF760, was shown to produce about 20 mg β-carotene per g DCW after four days of growth in YPD at 30° C. This strain was also the subject of several fermentor studies outlined in Example 5. In addition, MF740 was also transformed with MB4714 treated with AflII and Ura+ colonies, were selected. One such colony was designated MF779 (see Example 2G). MF746 was also transformed with pMB4637 treated with SnaBI, and Ade+ colonies were selected. One such colony, MF946, was shown to produce greater than 35 mg β-carotene per g DCW after four days of growth in YPD at 30° C.
MF760 was also transformed with pMB4691 (empty vector) cut with SalI, creating the prototroph MF858.
2G. Production of Y. Lipolytica Expressing Carotene Ketolase, a Truncated Form of HMG-CoA Reductase, Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase:
MF779 was transformed with either pMB4735 or pMB4741 cleaved with SnaBI., and a red prototrophic colony was chosen from each transformation: MF838 (pMB4735) and MF840 (pMB4741). After 4 days of growth in YPD, MF838 produced 25 mg canthaxanthin per g DCW, and MF840 produced 14 mg canthaxanthin and 30 mg echinenone per g DCW. Only trace levels of β-carotene were produced. These strains are the subject of fermentor studies described in Example 5.
In addition, MF740 was transformed with pMB4735 cleaved with SnaBI, and a red Ade+ colony was chosen for further manipulation and designated MF889 (See example 2I).
2H. Manipulation of the Y. Lipolytica ERG9 Gene to Enhance Carotenoid Production.
In order to decrease the expression of Erg9 (squalene synthase) in a carotenoid-producing yeast, pMB4789, containing the following cassette, was constructed using standard molecular techniques. The 4.8 kb fragment contains the Y. lipolytica URA3 gene flanked by the ERG9 ORF and the ERG9 terminator.
Thus this fragment comprises the sequence: GATCtcgttctgctcgggtagatc (SEQ ID NO:82)-ERG9 (promoter and ORF)-gtgctctgcggtaagatcgACTAGTggtgtgttctgtggagcattc (SEQ ID NO:83) URA3 (promoter, ORF, and terminator) ccaccactgcactaccactacacCTCGAGCATGCATcaggaaggactctccctgtggt (SEQ ID NO:84)-ERG9terminator-gtgttatggctctacgtgaagGGGCCC (SEQ ID NO:85). (Capital letters: restriction sites [engineered for assembly]) In addition, it was found that a mutation was generated during cloning that changed the coding sequence of ERG9 as follows: (cccgacgttAtccagaagaac (SEQ ID NO:86); F317I in the encoded protein).
Two overlapping fragments from this cassette, a 2.4 kb AlwNI-SmaI fragment and a 1.9 kb AlwNI-AflII fragment, were cotransformed into MF760 and Ura+ colonies were selected. PCR analysis showed that one, designated MF921, contains the erg9::URA3 cassette replacing the wild type ERG9 gene. MF921 produced greater than 30 mg β-carotene per g DCW after 4 days of growth at 30° C. in YPD.
2I. Production of Y. Lipolytica Expressing Carotene Hydroxylase, Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase:
MF740 was transformed with pMB4837 cleaved with SalI, and a Ura+ colony was selected and designated MF1011. MF1011 produced 6 mg of zeaxanthin and 1.5 mg of β-carotene per g DCW after 4 days of growth at 30° C. in YPD.
2J. Production of Y. Lipolytica Expressing Carotene Hydroxylase, Carotene Ketolase, Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase:
MF889 was transformed with pMB4837 cleaved with SalI, and a prototrophic colony was selected and designated MF1016. MF1016 produced 1.5 mg of astaxanthin and 3 mg of canthaxanthin per g DCW after 4 days of growth at 30° C. in YPD.
Example 3
Extraction of Carotenoids
3a: Total Extraction of Carotenoids from Yarrowia lipolytica Cells
Yarrowia lipolytica cultures to be tested for carotenoid production were grown in 20 ml YPD medium (1% yeast extract, 2% peptone, 2% glucose) in 125 flasks at 30° C. Following incubation for 72-96 hr, the cultures were harvested by centrifugation and the solvent extractions were performed to determine carotenoid form and quantity. Dry cell weights were determined by transferring 1.8 ml of each culture to an Eppendorf tube, which was then centrifuged to pellet the cells, and then the pellet washed twice with 1 ml water. After the second wash, the cells were resuspended in water and transferred to a pre-weighed snap-cap tube with a hole poked in the top, frozen, and then lyophilized overnight. After drying to constant weight, the tube was weighed in order to calculate dry cell weight (mg dry cell weight/ml).
The carotenoid content of the culture was calculated by solvent extraction from 0.25 ml of culture from the same shake flask culture. This 0.25 ml culture sample was transferred to a 2 ml screw-cap tube, the cells pelleted, and the supernatant aspirated. Such pelleted cells may be extracted immediately or frozen at −80° C. and stored.
An equal volume of cubic zirconia beads was added to cell pellets, along with 1 ml ice-cold extraction solvent (a 50/50 v/v mix of hexane and ethyl acetate containing 0.01% butylhydroxytoluene (BHT)). The mixture was then agitated (Mini-BeadBeater-8, BioSpec Products, Inc.) at maximum speed for 5 minutes at 4° C. The mixture was then spun at maximum speed for 1 minute, and the supernatant was collected and deposited in a cold 16 ml glass vial.
The remaining cell debris was re-extracted at least three times, without the addition of zirconia beads; all supernatants were pooled in the 16 ml glass vial. Following extraction, the glass vial was spun for 5 minutes at 2000 rpm at 4° C. in a Sorvall tabletop centrifuge, and the supernatant was transferred to a new cold 16 ml glass vial. A Speed Vac was used to concentrate the supernatant (room temperature in dark), and the samples were stored at −20° C. or −80° C. until immediately before HPLC analysis. Prior to HPLC analysis, the samples were resuspended in 1 ml ice-cold solvent and then transferred to a cold amber vial. Throughout the protocol, care was taken to avoid contact with oxygen, light, heat, and acids.
The use of a hexane:ethyl acetate (50:50) mixture to extract carotenoids efficiently extracted all carotenoids analyzed from Yarrowia even though the carotenoids possessed different polarity levels. For instance, in a strain containing β-carotene, γ-carotene, echinenone, and canthaxanthin, a hexane:ethyl acetate (50:50) mixture efficiently extracted all carotenoids even though echinenone and canthaxanthin, respectively, are progressively more polar than either β-carotene or γ-carotene. Given the high efficiency of extraction observed for all carotenoids with 50:50 hexane:ethyl acetate, these conditions were chosen as a “100%” standard against which the extraction efficiency of other conditions could be compared.
3B. Extraction of β-Carotene from Y. lipolytica MF858.
Y. lipolytica strain MF858 was grown as described in Example 3a and found to contain β-carotene as the dominant carotenoid. Extraction and breakage with hexane yielded an equal amount of β-carotene as was observed with a 50:50 hexane:ethyl acetate mixture.
3C. Extraction of Mixed Carotenoids from Y. Lipolytica MF838.
Y. lipolytica strain MF838 (example 2g) had previously been found to contain the following types carotenoids when extracted as described in Example 3a: β-carotene, γ-carotene, echinenone, and canthaxanthin. Extraction with 750 μl of hexane resulted in the following extraction efficiencies for each of the carotenoids (extraction efficiency is reported independently for each of the carotenoid species based on the total amount found by hexane:ethyl acetate extraction): β-carotene (79.3%), γ-carotene (82.4%), echinenone (42.6%), and canthaxanthin (8.0%).
When an identical aliquot of MF838 was extracted with 1 ml of ethanol (95%), the extraction efficiency of the same four carotenoids was as follows: β-carotene (53.6%), γ-carotene (71.3%), echinenone (39.9%), and canthaxanthin (28.0%). Thus ethanol can be used to extract both polar and nonpolar carotenoids from fungi (e.g. Y. lipolytica).
Example 4
Quantification of Carotenoid Production by HPLC
For carotenoid analysis, samples were resuspended in ice-cold extraction solvent (a 50/50 v/v mix of hexane and ethyl acetate containing 0.01% butylhydroxytoluene (BHT)). An Alliance 2795 HPLC (Waters) equipped with a Waters XBridge C18 column (3.5 μm, 2.1×50 mm) and Thermo Basic 8 guard column (2.1×10 mm) was used to resolve carotenoid at 25° C.; authentic carotenoid samples were used as standards. The mobile phases and flow rates are shown below (Solvent A=Ethyl Acetate; Solvent B=Water; Solvent C=Methanol; Solvent D=Acetonitrile). The injection volume was 10 μL. The detector is a Waters 996 photodiode array detector. The retention times for lipophilic molecules include astaxanthin (1.159 min), zeaxanthin (1.335), β-apo-8′-carotenal (2.86 min), ergosterol (3.11 min), lycopene (3.69 min), β-carotene (4.02 min), Canthaxanthin (2.50 min), Echinenone (3.38 min), and phytoene (4.13 min) Astaxanthin, zeaxanthin, β-apo-8′-carotenal, lycopene, β-carotene, canthaxanthin, and echinenone are detected at 475 nm, whereas ergosterol and phytoene were detected at 286 nm.







TABLE 28







Retention Times for Lipophilic Molecules













Time
Flow 







(min)
(mL/min)
% A
% B
% C
% D
Curve

















0.50
0.0
20.0
0.0
80.0



3.00
1.00
20.0
0.0
0.0
80.0
6


4.50
1.00
80.0
0.0
20.0
0.0
6


5.00
1.00
0.0
0.0
100.0
0.0
6


6.00
1.00
0.0
0.0
100.0
0.0
6


6.50
1.00
0.0
20.0
0.0
80.0
6


7.00
0.50
0.0
20
0.0
80.0
6









Example 5A
2 Liter Fed-Batch Fermentation of β-Carotene Producing Strain MF760
FIG. 9A depicts the production and intracellular accumulation of phytoene and β-carotene by strain MF760 (Example 2F) when grown in fed-batch fermentation on various carbon sources. Fermentation medium and process parameters are described below. Carbon sources used were glucose, glycerol, or olive oil. Feeding was initiated during the early exponential growth phase at a rate of 15.2 ml/hr. This feed rate either continued until feed exhaustion or, when the dissolved oxygen (dO2) level of the culture reached 20% saturation, feed was added to maintain the dO2 at 20% (DO controlled feed). As seen in FIG. 9a, β-carotene accumulates in all fermentations from 1.5 to 2.2% of DCW weight. Substantial phytoene accumulation was observed in the constant feed fermentations but not in the DO controlled feed fermentations.
FIG. 9B depicts dry cell weight accumulation during the course of the fermentations. For each carbon source examined, constant feeding resulted in greater biomass production relative to the DO controlled feed fermentation. This was especially true for the olive oil fed-batch fermentations where the constant feed fermentation reached greater than 150 g/L DCW. This was expected as Y. lipolytica has been reported to accumulate greater than 40% its biomass as lipid when grown on oils under conditions of excess carbon and oxygen limitation (Pananikolaou et al., Appl. Microbiol. Biotechnol. 58:p 308, 2002) and was independent of nitrogen concentration.
Batch Medium—1 L


















Carbon Source (one of the following): 
Glucose
60 
g




Glycerol
75 
g




Olive Oil
50 
ml



Yeast Nitrogen Base

4.1 
g



w/o Amino Acids and (NH4)2SO4






(NH4)2SO4

6 
g



Uracil

72 
mg



Antifoam 204 (Sigma catalog A6426)

5 
ml










Feed Medium—1 L
















Carbon Source (one of the following):
Glucose
500 
g



Glycerol
500 
g



Olive Oil
500 
ml


(NH4)2SO4

72 
g


KH2PO4

13.5 
g


MgSO4

5 
g


Inositol

70 
mg


Thiamine

10 
mg


Uracil

900 
mg


Trace Metal Solution

40 
ml











FeCl3•6H2O
2.7 
g/L




ZnCl2•4H2O
2.0 
g/L




CaCl2•2H2O
2.0 
g/L




Na2MoO4•2H2O
2.0 
g/L




CuSO4•5H2O
1.9 
g/L




H3BO3
0.5 
g/L




MnSO4•H2O
2.23 
g/L




Concentrated HCl
10 
ml/L




Vitamins Solution


40 
ml


Pantothenic acid
5.4 
g/L




Pyridoxine
1.4 
g/L




Niacin
6.1 
g/L




Folic acid
0.04 
g/L




Biotin
0.06 
g/L












Fermentation Parameter:
pH 5.5, controlled





Temp - 30° C.





Air Flow - 1.4 lpm





Agitation - 1200 rpm









Inoculum - 200 ml overnight culture grown in YEP + 5% glucose









Example 5B
2 Liter Fed-Batch of β-Carotene Producing Strain MF760
FIG. 9c depicts the production and intracellular accumulation of β-carotene by strain MF760 when grown in fed-batch fermentation. In this fermentation, additions of olive oil were combined with a glucose feeding protocol. Medium and process parameters are described below. Both glucose and olive oil were present in the batch medium. Feeding of the glucose containing feed medium was initiated during the early exponential growth phase at a rate of 15.2 ml/hr, this feed rate continued until feed exhaustion. 25 ml of olive oil was added at 24, 48, and 72 hr.
As shown in FIG. 9c, this combined glucose and oil feeding protocol resulted in substantially higher DCW production when compared to glucose as the sole carbon source (example 5a). In addition, β-carotene accumulated to over 5% of the DCW at the end of the fermentation, higher then either the glucose or oil fermentations of example 5a.
Batch Medium—1 L

















Glucose
40
g



Olive Oil
50 
ml



Yeast Nitrogen Base
4.1 
g



w/o Amino Acids and (NH4)2SO4





(NH4)2SO4
6 
g



Uracil
72 
mg



Antifoam 204
5 
ml










Feed Medium—1 L
















Glucose

500 
g


(NH4)2SO4

72 
g


KH2PO4

13.5 
g


MgSO4

5 
g


Inositol

70 
mg


Thiamine

10 
mg


Uracil

900 
mg


Trace Metal Solution

40 
ml


Vitamins Solution

40 
ml


Olive Oil Additions - 25 ml at 





24, 48, and 72 hr





Fermentation Parameters:
pH 5.5, controlled





Temp - 30° C.





Air Flow - 1.4 lpm





Agitation - 1150 rpm









Inoculum - 200 ml overnight culture grown in YEP + 


5% glucose + 2.5% olive oil









Example 5C
2 Liter Fed-Batch of Canthaxanthin Producing Strain MF840
FIG. 9d depicts the production and intracellular accumulation of canthaxanthin, echinenone and β-carotene by strain 840 (Example 2g) when grown in fed-batch fermentation. Medium and process parameters are described below. Both glucose and olive oil were present in the batch medium. Feeding of the glucose containing feed medium was initiated during the early exponential growth phase at a rate of 15.2 ml/hr; this feed rate continued until the dissolved oxygen reached 20%, at which time feed was added to maintain the dO2 at 20% (DO controlled feed) for the remainder of the fermentation.
As seen in FIG. 9d, the combined total amount of canthaxanthin, echinenone and β-carotene represented over 8% of the DCW at the end of the fermentation and demonstrates the ability of genetically engineered Y. lipolytica to produce and accumulate significant amounts of carotenoids.
Batch Medium—1 L

















Glucose
40 
g



Olive Oil
50
ml



Yeast Nitrogen Base
4.1 
g



w/o Amino Acids and (NH4)2SO4





(NH4)2SO4
6 
g



Antifoam 204
5 
ml










Feed Medium—1 L



















Glucose

500 
g



(NH4)2SO4

72 
g



KH2PO4

13.5 
g



MgSO4

5 
g



Inositol

70 
mg



Thiamine

10 
mg



Trace Metal Solution

40 
ml



Vitamins Solution

40 
ml











Fermentation Parameters:
pH 5.5, controlled





Temp - 30° C.





Air Flow - 1.4 lpm





Agitation - 1150 rpm










Inoculum - 200 ml overnight culture grown in YEP + 



5% glucose + 2.5% olive oil










Example 5D
2 Liter Fed-Batch of Canthaxanthin Producing Strain MF838
FIG. 9e depicts the production and intracellular accumulation of canthaxanthin and echinenone by strain MF838 (Example 2g) in fed-batch fermentation together with DCW levels. This example demonstrates the advantage of a two phase feeding protocol in which the first phase of feeding is designed to maintain excess carbon and oxygen limited conditions, while the second phase of feeding results in oxygen excess conditions via carbon limitation.
Fermentations A and B are depicted on FIG. 9e. Medium and process parameters are described below. In both fermentations, feeding of the glucose containing feed medium was initiated during the early exponential growth phase at a rate of 22.8 ml/hr. In fermentation A, this feed rate continued until the dissolved oxygen reached 20%, at which time feed was added to maintain the dO2 at 20% (DO controlled feed) for the remainder of the fermentation. In fermentation B, the constant feed rate was maintained such that glucose was in excess, and dO2 level was essential zero, until approximately hour 40 of the fermentation. At that time feed was added to maintain the dO2 at 20% (DO controlled feed) for the remainder of the fermentation. As seen in FIG. 9e, the extended period of carbon excess and oxygen limitation resulted in higher peak DCW, altered kinetics of canthaxanthin production, and produced a higher final level canthaxanthin—over 3.5% of DCW.
Batch Medium—1 L

















Glucose
40 
g



Yeast Nitrogen Base
8.2 
g



w/o Amino Acids and (NH4)2SO4





(NH4)2SO4
6 
g



Antifoam 204
5 
ml










Feed Medium—1 L
















Glucose

500 
g


(NH4)2SO4

72 
g


KH2PO4

13.5 
g


MgSO4

5 
g


Inositol

70 
mg


Thiamine

10 
mg


Trace Metal Solution

40 
ml


Vitamins Solution

40 
ml


Fermentation Parameters:
pH 5.5, controlled





Temp - 30° C.





Air Flow - 1.4 lpm





Agitation - 1150 rpm









Inoculum - 200 ml overnight culture grown in YEP + 5% glucose









Example 6
Introduction of Heterologous Carotene Hydroxylase and Carotene Ketolase Genes into Y. lipolytica Strains Producing Carotenoid for Production of Astaxanthin
For introduction of carotene hydroxylase and carotene ketolase into carotenoid producing Y. lipolytica, pMB4692 and pMB4698, described as in Example 1E and 1F above, can be sequentially introduced into MF740 or MF746 (described in Example 2E). For the introduction of pMB4692, the plasmid may be cleaved with SalI or BsrGI to direct integration at the ura3 locus, or with XbaI to promote random integration, selecting for uracil prototrophy. Ura+ transformants from MF740 or MF746 harboring pMB4692 are screened for zeaxanthin production in YPD. Zeaxanthin-producing cells are transformed with pMB4698 (which can be cleaved with PpuMI, SspI or BbvCI to direct integration at the ade1 locus, or with EcoRV to promote random integration) and prototrophic colonies are screened for astaxanthin production.
Alternatively, the order of plasmid transformation may be reversed wherein pMB4698 is transformed first and transformants are selected for adenine prototrophy. Ade+ transformants from MF740 or MF746 harboring pMB4698 are screened for canthaxanthin production. Canthaxanthin-producing MF740[pMB4698] or MF746[pMB4698] cells are transformed with pMB4692 and prototrophic colonies are screened for astaxanthin production.
In another approach, the carotenoid ketolase and carotenoid hydroxylase genes from P. marcusii can be introduced into a Leu2− version of MF740 or MF746, in order to convert β-carotene into astaxanthin. P. marcusii genomic DNA is amplified with two primers.









CrtZfwd:







(SEQ ID NO: 87)









5′ CACACCGTCTCAAatgaccaatttcctgatcgtcgtc



 



CrtZrev:







(SEQ ID NO: 88)









5′ CACACAGATCtcacgtgcgctcctgcgcc,






and the resulting fragment is cleaved with BsmBI, modified with the Klenow fragment of DNA polymerase, and cleaved with BglII. This fragment is inserted into PmlI- and BamHI-cleaved pINA1269 (J. Mol. Microbiol. Biotechnol. 2 (2000): 207-216), containing the hp4d promoter, the XPR2 terminator, the selectable LEU2 gene, and sequences necessary for selection and propagation in E. coli. The resulting plasmid “pA” contains sequences encoding carotene hydroxylase from P. marcusii (crtZ gene) (Genbank accession: CAB56060.1) under the control of the hp4d promoter.

“pYEG1TEF” is modified by substituting the LIP2 terminator for the XPR2 terminator as follows. pINA1291 is digested with AvrII, modified with the Klenow fragment of DNA polymerase, and cleaved with EcoRI, and the small LIP2t containing fragment is ligated to “pYEG1TEF” that has been digested with SacII, modified with T4 DNA polymerase in the presence of dNTP, and cleaved with EcoRI. The resulting plasmid is named “pYEG1TEF-LIP2t”.
In order to amplify the carotenoid ketolase gene, P. marcusii genomic DNA is amplified with two primers.









CrtWfwd:







(SEQ ID NO: 89)









5′ CACACCCTAGGCCatgagcgcacatgccctgc



 



CrtWrev:







(SEQ ID NO: 90)









5′ CACACAAGCTTtcatgcggtgtcccccttg,






and the resulting fragment is cleaved with AvrII and HindIII, and inserted into AvrII- and HindIII-cleaved “pYEG1TEF-LIP2t”. The resulting plasmid, “pBt”, contains sequences encoding the carotene ketolase (crtW gene) (Genbank accession: CAB56059.1) under the control of the constitutive TEF1 promoter.

In order to combine the two expression cassettes into a single plasmid, “pBt” is cleaved with ClaI, modified with the Klenow fragment of DNA polymerase, and cleaved with EcoRI, and the crtW-containing fragment is isolated, mixed with the phosphorylated oligonucleotide adaptor pair:







(SEQ ID NO: 91)









5′ AATTCGCGGCCGCT



and



 







(SEQ ID NO: 92)









5′ AGCGGCCGCG,






cleaved with Nod, and ligated to NotI-digested “pA”. The resulting plasmid, “pABt”, contains both the TEF1p/crtW/LIP2t cassette and the hp4d/crtZ/XPR2t cassette as well as the selectable LEU2 gene.

“pABt” can be introduced into MF740 or MF746 and transformants selected for leucine prototrophy.
Example 7
Partial Inactivation of Y. Lipolytica ERG9 Gene Encoding Squalene Synthase Results in Increased Carotenoid Production
7A.
In order to partially inactivate the ERG9 gene encoding squalene synthase, the neighboring FOL3 gene is disrupted, resulting in a folinic acid requirement. This strain is then transformed with a mutagenized fragment of DNA partially spanning the two genes, and Fol+ transformants are screened for decreased squalene synthase activity.
The following oligonucleotides are synthesized:









PRIMER K







(SEQ ID NO: 93)









5′-CCTTCTAGTCGTACGTAGTCAGC;



 



PRIMER L







(SEQ ID NO: 94)









5′-CCACTGATCTAGAATCTCTTTCTGG






and used to amplify a 2.3 kb fragment from Y. lipolytica genomic DNA spanning most of the FOL3 gene, using Pfu polymerase. The resulting fragment is cleaved with XbaI and phosphorylated, then ligated into pBluescriptSK− that has been cleaved with KpnI, treated with T4 DNA polymerase (T4pol) in the presence of dNTPs, and subsequently cleaved with XbaI. The resultant plasmid, designated pBS-fol3, is then cleaved with Acc65I and EcoRI, treated with T4pol as above, and ligated to the 3.4 kb EcoRV-SpeI ADE1 fragment (treated with T4pol) from pMB4529.

The resulting plasmid, pBSfol3Δade, can be cleaved with BsiWI and XbaI to liberate a 5.5 kb fragment that is used to transform MF740 or MF746 to adenine prototrophy. Resulting Ade+ transformants are screened for a folinic acid requirement, and for homologous integration by PCR analysis.
Strains that harbor the resultant fol3ΔADE1 allele can be transformed with a 3.5 kb DNA fragment generated by mutagenic PCR amplification using the primers:









PRIMER M







(SEQ ID NO: 95)









5′-GGCTCATTGCGCATGCTAACATCG;



 



PRIMER N







(SEQ ID NO: 96)









5′-CGACGATGCTATGAGCTTCTAGACG,






and Y. lipolytica genomic DNA as template. The resulting fragment containing the N-terminal three-quarters of the FOL3 ORF and the C-terminal nine-tenths of the ERG9 ORF is used to transform strains. The resulting Fol+ Ade− transformants are screened for decreased squalene synthase activity by sensitivity to agents such as zaragozic acid, itraconazole, or fluconazole. Additionally, the resulting transformants are screened for increased carotenoid production.

7B.
Alternatively, the PCR fragment produced in 7A could be cloned and altered in such a way as to remove the 3′-untranslated region of ERG9 gene. Replacement of the fol3ΔADE1 disruption by this fragment results in decreased expression of squalene synthase [Schuldiner et al. (2005), Cell 123:507-519][Muhlrad and Parker (1999), RNA 5:1299-1307], which can be confirmed as in 7A. This approach may also be used in a Fol+ Ade− strain, using the ADE1 marker to disrupt the ERG9 3′-UTR.
7C.
In still another approach, partially defective ERG9 alleles can be identified in S. cerevisiae using plasmid shuffling techniques [Boeke et al. (1987), Methods Enzymol. 154:164-175], and using drug sensitivities as a phenotype. Defective genes can be transferred to Y. lipolytica using standard molecular genetic techniques.
Example 8
Treatment of Y. Lipolytica Strains Producing Carotenoid with Inhibitor of an Isoprenoid Biosynthesis Competitor Polypeptide Results in Increased Carotenoid Production
Cultures produced in Example 2 are treated with the squalene synthase inhibitor, zaragozic acid (zaragozic acid at 0.5 μM) and monitored for β-carotene production, as described above.
Example 9
Constructing an Oleaginous Strain of Saccharomyces cerevisiae 
The genes encoding the two subunits of ATP-citrate lyase from N. crassa, the AMP deaminase from Saccharomyces cerevisiae, and the cytosolic malic enzyme from M. circinelloides are overexpressed in S. cereviseae strains in order to increase the total lipid content. Similar approaches to enhance lipid production could be employed in other host organisms such as Xanthophyllomyces dendrorhous (Phaffia rhodozyma), using the same, homologous, or functionally similar oleaginic polypeptides.
Qiagen RNAEasy kits (Qiagen, Valencia, Calif.) are used to prepare messenger RNA from lyophilized biomass prepared from cultures of N. crassa. Subsequently, RT-PCR is performed in two reactions containing the mRNA template and either of the following primer pairs.









acl1:



1fwd:







(SEQ ID NO: 97)









5′ CACACGGATCCTATAatgccttccgcaacgaccg



 



1rev:







(SEQ ID NO: 98)









5′ CACACACTAGttaaatttggacctcaacacgaccc



 



acl2:



2fwd:







(SEQ ID NO: 99)









5′ CACACGGATCCAATATAAatgtctgcgaagagcatcctcg



 



2rev:







(SEQ ID NO: 100)









5′ CACACGCATGCttaagcttggaactccaccgcac






The resulting fragment from the acl1 reaction is cleaved with SpeI and BamHI, and that from the acl2 reaction is cleaved with BamHI and SphI, and both are ligated together into YEp24 that has been digested with NheI and SphI, creating the plasmid “p12”. The bi-directional GAL1-10 promoter is amplified from S. cerevisiae genomic DNA using the primers.







gal10:







(SEQ ID NO: 101)







5′ CACACGGATCCaattttcaaaaattcttactttttttttggatggac


 


gal1:







(SEQ ID NO: 102)







5′ CACACGGATCCttttttctccttgacgttaaagtatagagg,






and the resulting 0.67 kb fragment is cleaved with BamHI and ligated in either orientation to BamHI-digested “p12” to create “p1gal2” and “p2gal1”, containing GAL1-acl1/GAL10-acl2 and GAL10-acl1/GAL1-acl2, respectively (Genbank accession: acl1: CAB91740.2; acl2: CAB91741.2).

In order to amplify the S. cereviseae gene encoding AMP deaminase and a promoter suitable for expressing this gene, S. cerevisiae genomic DNA is amplified using two primer pairs in separate reactions:







AMD1 ORF:


AMD1FWD:







(SEQ ID NO: 103)







5′ CACACGAGCTCAAAAatggacaatcaggctacacagag


 


AMD1rev:







(SEQ ID NO: 104)







5′ CACACCCTAGGtcacttttcttcaatggttctcttgaaattg


 


GAL7p:


gal7prox:







(SEQ ID NO: 105)







5′ CACACGAGCTCggaatattcaactgtttttttttatcatgttgatg


 


gal7dist:







(SEQ ID NO: 106)







5′ CACACGGAtccttcttgaaaatatgcactctatatcttttag,






and the resulting fragment from the AMD1 reaction (2.4 kb) is cleaved with SacI and AvrII, and that from the GAL7 reaction (0.7 kb) is cleaved with BamHI and SphI, and both are ligated together into YEp13 that has been digested with NheI and BamHI, creating the plasmid “pAMPD”. This plasmid carries the S. cerevisiae gene, AMD1, encoding AMP deaminase, under the control of the galactose-inducible GAL7 promoter.

Messenger RNA is prepared from lyophilized biomass of M. circinelloides, as described above, and the mRNA template is used in a RT-PCR reaction with two primers:







MAEfwd:







(SEQ ID NO: 107)







5′ CACACGCTAGCTACAAAatgttgtcactcaaacgcatagcaac


 


MAErev:







(SEQ ID NO: 108)







5′ CACACGTCGACttaatgatctcggtatacgagaggaac,






and the resulting fragment is cleaved with NheI and SalI, and ligated to XbaI- and XhoI-digested pRS413TEF (Mumberg, D. et al. (1995) Gene, 156:119-122), creating the plasmid “pTEFMAE”, which contains sequences encoding the cytosolic NADP+-dependant malic enzyme from M. circinelloides (E.C. 1.1.1.40; mce gene; Genbank accession: AY209191) under the control of the constitutive TEF1 promoter.

The plasmids “p1gal2”, “pAMPD”, and “pTEFMAE” are sequentially transformed into a strain of S. cereviseae to restore prototrophy for uracil (“p1gal2”), leucine (“pAMPD”), and histidine (“pTEFMAE”) (Guthrie and Fink Methods in Enzymology 194:1-933, 1991). The resulting transformants are tested for total lipid content following shake flask testing in either synthetic complete (SC) medium lacking uracil, leucine and histidine, as described in Example 3, or in a 2-step fermentation process. In the 2-step process, 1.5 ml of cells from an overnight 2 ml roll tube culture containing SC medium lacking uracil, leucine and histidine are centrifuged, washed in distilled water, and resuspended in 20 ml of a nitrogen-limiting medium suitable for lipid accumulation (30 g/L glucose, 1.5 g/L yeast extract, 0.5 g/L NH4C1, 7 g/L KH2PO4, 5 g/L Na2HPO4-12H2O, 1.5 g/L MgSO4-7H2O, 0.08 g/L FeCl3-6H2O, 0.01 g/L ZnSO4-7H2O, 0.1 g/L CaCl2-2H2O, 0.1 mg/L MnSO4-5H2O, 0.1 mg/L CuSO4-5H2O, 0.1 mg/L Co(NO3)2-6H2O; pH 5.5 (J Am Oil Chem Soc 70:891-894 (1993)).
Intracellular lipid content of the modified and control S. cerevisiae strains is analyzed using the fluorescent probe, Nile Red (J Microbiol Meth (2004) 56:331-338). In brief, cells diluted in buffer are stained with Nile Red, excited at 488 nm, and the fluorescent emission spectra in the wavelength region of 400-700 nm are acquired and compared to the corresponding spectra from cells not stained with Nile Red. To confirm results from the rapid estimation method, the total lipid content is determined by gas chromatographic analysis of the total fatty acids directly transmethylesterified from dried cells, as described (Appl Microbiol Biotechnol. 2002 November; 60(3):275-80). Non-transformed S. cerevisiae strains produce 6% and 10% total lipid (dry cell weight basis) after growth in YPD and lipid accumulation medium, respectively. Yeast strains expressing the multiple oleaginic polypeptides produce 17% and 25% total lipid following growth in YPD and lipid accumulation medium, respectively.
Example 10
Introduction of Heterologous Carotene Hydroxylase into Y. Lipolytica Strains Producing Carotenoid or Production of Zeaxanthin
MF578 (tef-carRP tef-carB) was transformed with pMB4692 that had been cleaved with SalI. Several Ura+ colonies inferred to contain tef-crtZ by PCR analysis were able to produce zeaxanthin in YPD shake flasks, and in one case, all of the β-carotene was depleted.
Example 11
Regulatory Sequences
Sequences which consist of, consist essentially of, and comprise the following regulatory sequences (e.g. promoters and terminator sequences, including functional fragments thereof) may be useful to control expression of endogenous and heterologous genes in engineered host cells, and particularly in engineered fungal cells described herein.








Met2 promoter









(SEQ ID NO: 109)









5′cctctcactttgtgaatcgtgaaacatgaatcttcaagccaagaatgttaggcaggggaagctttctttcagactttttggaattggtcctcttttggac



attattgacgatattattattttttccccgtccaatgttgacccttgtaagccattccggttctggagcgcatctcgtctgaaggagtcttcgtgtggctata


actacaagcgttgtatggtggatcctatgaccgtctatatagggcaacttttgctcttgttcttccccctccttgagggacgtatggcaatggctatgaca


actatcgtagtgagcctctataacccattgaagtacaagtcctccaccttgctgccaaactcgcgagaaaaaaagtccaccaactccgccgggaaat


actggagaacacctctaagacgtgggcttctgcacctgtgtggcttgggtctgggttttgcgagctctgagccacaacctaaggacggtgtgattgg


gagataagtagtcgttggttttctaatcgcacgtgatatgcaagccacacttataacacaatgaagacaggccgatgaactgcatgtcattgtacaggt


gcggagagcaagaaactctggggcggaggtgaaagatgagacaaaaagcctcaggtgcaaggtagggagttgatcaacgtcaaacacaaataa


tctaggttgttaggcagctaaacatgtatataactgggctgccaccgagtgttacttgtcattaacgtcgcattttcgcctacacaaaatttgggttactcg


ccactacactgctcaaatctttcagctgtgcaacaagctttcaggtcacacatagactcgcataaggacccgggtcatctgttattctccactggtaaac


caatagtcctagctgatttgggtacagaagctcactttcacatcttttcatcttcttctacaaccatc


 


Met3 promoter








(SEQ ID NO: 110)









5′atctgtgaggagcccctggcgtcactgtcgactgtgccggcatttctgatggtatttccagccccgcagttctcgagacccccgaacaaatgtgcc



acacccttgccaaaatgacgaatacacggcgtcgcggccgggaatcgaactcttggcaccgccacaggagtgaaatttgaaatttgaaatttgaaa


aataattcacattttgagtttcaataatatatcgatgaccctcccaaaagacccaagtcgagacgcaaaaaaacacccagacgacatggatgcggtc


acgtgaccgcaaaaaccgccccggaaatccgtttgtgacgtgttcaattccatctctatgtttttctgcggtttctacgatgccgcaatggtggccaatg


tgcgtttcactgccgtagtggctggaacaagccacagggggtcgtcgggccaatcagacggtccctgacatggttctgcgccctaacccgggaac


tctaacccccgtggtggcgcaatcgctgtcttcatgtgctttatctcacgtgacggctggaatctggcagaagacggagtatgtacattttgtcgttggt


cacgttatccctaaaacgtggtgtttaaactggtcgaatgcttggcccagaacacaagaagaaaaaaacgagacaacttgatcagtttcaacgccac


agcaagcttgtcttcactgtggttggtcttctccacgccacaagcaacacgtacatgtcaattacgtcagggtcttttaagttctgtggcttttgaaccagt


tataaagaaccaaccacccttttttcaaagctaatcaagacggggaaattttttttttgatatttttcgaca


 


Met6 promoter








(SEQ ID NO: 111)









5′gatactgcagacggtgcattacttacccgtgtcgactgagagtctacttggtacttggccctgtggctaagcagtatttgagcaacaatgcaatgca



gttgctgactcggttccagatccccttgccccgatgtgtggaagcgttgtttttggggcaagggcatgtgggggctgcatcatactgtggctggggcc


gttggaagagccgtcggcagcgagcctgagtcgcttctcggggccttattccccccgcctctaggtcagcggcggccgaagtgtcgtactcagctc


gcctgtacagtatgacgtgaccgaatagcctctggaaggttggagaagtacagtgcaaaaaaaagttgcaaaatttcattttagcgttcgatccgacg


tggcagttggacaatgaatcgatggagacatgatcatgggcagaaatagaaggtctccatgttcaatggcagtaccaattgagcaacagacgggtc


gacaggcggcgggcacaccatccgccctccacatggcgcaatcgtcagtgcagcgattcgtactcggattgcatcatgttgcaccgaaagttggg


gcccgcacgttggagaggcgaggagccagggttagctttggtggggtcctttgttgtcacgtggcatcagcgaatggcgtcctccaatcagggcc


gtcagcgaagtcggcgtgtgatagtgcgtggggagcgaatagagtttctgggggggggcggcccaaaacgtgaaatccgagtacgcatgtaga


gtgtaaattgggtgtatagtgacattgtttgactctgaccctgagagtaatatataatgtgtacgtgtccccctccgttggtcttctttttttct


cctttctcctaaccaacacccaaactaatcaatc


 


Met25 promoter








(SEQ ID NO: 112)









5′aagtcgtattaacataactttccttacatttttttaaagcacgtcactatccacgtgacctagccacgcgataccaagtattcatccataatgacacact



catgacgtccggaggacgtcatcatcgtccagtcacgtgccaaggcacatgactaatcataacaccttatgactagcttctgaatcgctacacagttc


caattcgcaaataaactcgaaatgacgaaatgccataataaaaatgacgaaactcgagattgagagcagcacatgcactgaagtggtggacaacc


agcgtatccggagacacgacggatccagcaccatggaagctggccgaaaaagagatccccagcacattgagcaaccaagtcagctcaattgagt


aacatcacacactcagatcgagtctgatggtggtccccttttgttccttcacttgaaaaataattgaaaataacaataacaataaaaataaaaacaaaat


aaaaataaaaataaaaataaaaataaaaaaataaaaaaaccttgccgcatttagcgtcagccaccccccgcattgacctgagtacgttggattgacc


ccgatcctgcacgtcgagcgtggtcggccaaaaagcgcccgtggctggtgagtcagaaatagcagggttgcaagagagagctgcgcaacgagc


aataaacggtgtttttttcgcttctgtgctgcttagagtggagagccgaccctcgccatgctcacgtgaccattcacgtggttgcaaactccaccttagt


atagccgtgtccctctcgctacccattatcgcatcgtactccagccacatttttttgttccccgctaaatccggaaccttatctgggtcacgtgaaattgc


aatctcgacaggaggttatacttatagagtgagacactccacgcaaggtgttgcaagtcaattgacaccacctcacctcagactaacatccaca


 


Pox2 promoter








(SEQ ID NO: 113)









5′gaatctgcccccacattttatctccgcttttgactgtttttctcccccctttcacactctgcttttggctacataaaccccgcaccgtttggaactct



gttggtccggggaagccgccgttaggtgtgtcagatggagagcgccagacgagcagaaccgagggacagcggatcgggggagggctgtcacgtga


cgaagggcactgttgacgtggtgaatgtcgcccgttctcacgtgacccgtctcctctatatgtgtatccgcctctttgtttggttttttttctgcttcccccc


ccccccccccaccccaatcacatgctcagaaagtagacatctgcatcgtcctgcatgccatcccacaagacgaacaagtgataggccgagagccg


aggacgaggtggagtgcacaaggggtaggcgaatggtacgattccgccaagtgagactggcgatcgggagaagggttggtggtcatgggggat


agaatttgtacaagtggaaaaaccactacgagtagcggatttgataccacaagtagcagagatatacagcaatggtgggagtgcaagtatcggaat


gtactgtacctcctgtactcgtactcgtacggcactcgtagaaacggggcaatacgggggagaagcgatcgcccgtctgttcaatcgccacaagtc


cgagtaatgctcgagtatcgaagtcttgtacctccctgtcaatcatggcaccactggtcttgacttgtctattcatactggacaagcgccagagttaagc


ttgtagcgaatttcgccctcggacatcaccccatacgacggacacacatgcccgacaaacagcctctcttattgtagctgaaagtatattgaatgtgaa


cgtgtacaatatcaggtaccagcgggaggttacggccaaggtgataccggaataaccctggcttggagatggtcggtccattgtactgaagtgtccgtgtc


gtttccgtcactgccccaattggacatgtttgtttttccgatctttcgggcgccctctccttgtctccttgtctgtctcctggactgttgctaccccatt


tctttggcctccattggttcctccccgtctttcacgtcgtctatggttgcatggtttcccttatacttttccccacagtcacatgttatggaggggtctag


atggaggcctaattttgacgtgcaaggggcgaattggggcgagaaacacgtcgtggacatggtgcaaggcccgcagggttgattcgacgcttttccgc


gaaaaaaacaagtccaaatacccccgtttattctccctcggctctcggtatttcacatgaaaactataacctagactacacgggcaaccttaaccccag


agtatacttatataccaaagggatgggtcctcaaaaatcacacaagcaacg


 


Yef3 (YALI0E13277g) promoter








(SEQ ID NO: 114)









5′cgccattcggttccttccagaccattccagatcaatccacctcttcttatctcaggtgggtgtgctgacatcagaccccgtagcccttctcccagtgg



cgaacagcaggcataaaacagggccattgagcagagcaaacaaggtcggtgaaatcgtcgaaaaagtcggaaaacggttgcaagaaattggag


cgtcacctgccaccctccaggctctatataaagcattgccccaattgctaacgcttcatatttacacctttggcaccccagtccatccctccaataaaat


gtactacatgggacacaacaagagaggatgcgcgcccaaaccctaacctagcacatgcacgatgattctctttgtctgtgaaaaaatttttccaccaa


aatttccccattgggatgaaaccctaaccgcaaccaaaagtttttaactatcatcttgtacgtcacggtttccgattcttctcttctctttcatcatcat


cacttgtgacc


 


Cam1 (YALI0C24420g) promoter








(SEQ ID NO: 115)









5′aactaccataaagtaccgagaaatataggcaattgtacaaattgtccacctccttcacttacattaccgaaccatggccatatcaccaaaatacccc



gagtgctaaaacacctccctccaaatgttctcttaccttccaccgaaaaccgatcttattatcccaacgcttgttgtggcttgacgcgccgcacccgctg


ggcttgccatttcgataccaatccaagaggaaaagctcatgagaaacaatcggaatatcacgagaacggcctggcgaaccaacaggatatttttga


atataattacccctcgaatctagtcatatctatgtctactgtagacttgggcggcatcatgatgtacattattttagcgtctggaaccctaaagttcacgta


caatcatgtgacaaacgaggctaaaaaatgtcaatttcgtatattagtgttattacgtggctcacatttccgaatcatctaccaccccccacctaaaaa


 


YALI0D16467g promoter








(SEQ ID NO: 116)









5′tttttttaattttcatatttattttcatatttattttcatatttattttcatttatttattcatgtatttatttattactttttaagtattttaaa



ctcctcactaaaccgtcgattgcacaatattaaccttcattacacctgcagcgtggtttttgtggtcgttagccgaagtcttccaacgtg


ggtataagtaggaacaattgggccgattttttgagccgtctaaatctctcgactcaattgatctgctgtcgaaaatccggctctctagc


tccttttccccgtccgctggagctcctcttcattgtgccgtttttccaacatttaactttgccacccaccaccacccccactaccatcacc


cactcgatctctgttcgtgtcaccacgactttgtcttctcacacatactctgtttgtgcaccacacattgcgaa


 


Tef4 (YALI0B12562g) promoter








(SEQ ID NO: 117)









5′gctacaatagctttattggccctattgagcacgctacaattcggtccagtatgtacaacgtctatgcgcactaacggccatacagtgagttacagca



cacccaaaagtaaccctgcctgacctgtctgcctgagacaggaagattaactcttgtagtgaccgagctcgataagactcaagccacacaattttttta


tagccttgcttcaagagtcgccaaaatgacattacacaactccacggaccgtcggttccatgtccacacccttggatgggtaagcgctccacgcacg


taccacgtgcattgagtttaaccacaaacataggtctgtgtcccagagttaccctgctgcatcagccaagtcttgaaagcaaaatttcttgcacaattttt


cctcttcttttcttcactgatcgcagtccaaacacaaaca


 


YALI0D12903g promoter








(SEQ ID NO: 118)









5′gcgctctgatccacttgtatggctccaagttcagtgtaccaagtagttggtgatgcagggagggatgtctctatccaccaataatgaactcatgggcgaa



attgtttctgttaaacactccaactgtcgttttaaatctcattctctttgcatttggactccattcgcttccgttgggccaatataatccatcgtaacgtac


tttagatggaaatttagttacctgctacttgtctcaacaccccaacaggggctgttcgacagaggtaatagagcgtcaatgggttaataaaaacacactgtcg


attttcactcattgtctttatgatattacctgttttccgctgttatcaatgccgagcatcgtgttatatcttccaccccaactacttgcatttacttaactat


tacctcaactatttacaccccgaattgttacctcccaataagtaactttatttcaaccaatgggacgagagcatctctgagaacatcgatctatctctgtca


atattgcccagaatcgttcgaaaaaaaacaccaaaaggtttacagcgccattataaatataaattcgttgtcaattcccccgcaatgtctgttgaaatctc


attttgagaccttccaacattaccctctctcccgtctggtcacatgacgtgactgcttcttcccaaaacgaacactcccaactcttcccccccgtcagtg


aaaagtatacatccgacctccaaatcttttcttcactcaac


 


Tef1 (YALI0C09141g) promoter








(SEQ ID NO: 119)









5′agagacgggttggcggcgtatttgtgtcccaaaaaacagccccaattgccccaattgaccccaaattgacccagtagcgggcccaaccccggc



gagagcccccttcaccccacatatcaaacctcccccggttcccacacttgccgttaagggcgtagggtactgcagtctggaatctacgcttgttcaga


ctttgtactagtttctttgtctggccatccgggtaacccatgccggacgcaaaatagactactgaaaatttttttgctttgtggttgggactttagccaagg


gtataaaagaccaccgtccccgaattacctttcctcttcttttctctctctccttgtcaactcacacccgaaatcgttaagcatttccttctgagtataa


gaatcattc


 


Fba1 (YALI0E26004g) promoter








(SEQ ID NO: 120)









5′gctgcgctgatctggacaccacagaggttccgagcactttaggttgcaccaaatgtcccaccaggtgcaggcagaaaacgctggaacagcgtg



tacagtttgtcttagcaaaaagtgaaggcgctgaggtcgagcagggtggtgtgacttgttatagcctttagagctgcgaaagcgcgtatggatttggc


tcatcaggccagattgagggtctgtggacacatgtcatgttagtgtacttcaatcgccccctggatatagccccgacaataggccgtggcctcatttttt


tgccttccgcacatttccattgctcggtacccacaccttgcttctcctgcacttgccaaccttaatactggtttacattgaccaacatcttacaagcgggg


ggcttgtctagggtatatataaacagtggctctcccaatcggttgccagtctcttttttcctttctttccccacagattcgaaatctaaactacacatc


 


Pox2 terminator:








(SEQ ID NO: 121)









5′gatgaggaatagacaagcgggtatttattgtatgaataaagattatgtattgattgcaaaaaagtgcatttgtagatgtggtttattgtagagagtacg



gtatgtactgtacgaacattaggagctacttctacaagtagattttcttaacaagggtgaaatttactaggaagtacatgcatatttcgttagtagaatcac


aaaagaaatgtacaagcacgtactacttgtactccacaatgtggagtgggagcaaaaaaattggacgacaccggaatcgaaccggggacctcgc


gcatgctaagcgcatgtgataaccaactacaccagacgcccaagaactttcttggtgattatggaatacgtggtctgctatatctcaattttgctgtaatg


aatcattagaattaaaaaaaaaaccccatttttgtgtgattgtcggccaagagatggaacaggaagaatacgtgaacaagcgagcacgaatgccatatg


ctcttctgaacaaccgagtccgaatccgatttgtgggtatcacatgtctcaagtagctgaaatgtatttcgctagaataaaataaatgagattaagaattaa


aaatattggaatatattttcctagaatagaaactttggattttttttcggctattacagtctgaactggacaaacggctgactatatataaatattattggg


tctgttttcttgtttatgtcgaaattatctgggttttactactgtgtcgtcgagtatagagtggcctgactggagaaaatgcagtagtatggacagtaggt


actgccagccagagaagtttttggaattgatacttgagtcatttttccattccccattccccattccaacacaatcaactgtttctgaacattttccaaaacg


cggagatgtatgtcacttggcactgcaagtctcgattcaaaatgcatctctttcagaccaaagtgtcatcagctttgtttggccccaaattaccgcaaat


acttgtcgaaattgaagtgcaatacggcctcgtctgccatgaaacctgcctattctcttcaaattggcgtcaggtttcacgtccagcattcctcgcccag


acagagttgctatggttgaatcgtgtactgttaatatatgtatgtattatactcgtactacgatatactgttcaatagagtctcttataatcgtacga


cgattctgggca






Example 12
Y. lipolytica Oleaginic and Isoprenoid Biosynthesis Genes
FIG. 10 is a list of Y. lipolytica genes representing various polypeptides (e.g. oleaginic and isoprenoid biosynthesis peptides) useful in the fungal strains and methods described herein. The Genbank accession number and GI number is given for each polypeptide in addition to oligo pairs which can be used to amplify the coding region for each gene from Y. lipolytica genomic DNA or cDNA. Resulting PCR fragments can be cleaved with restriction enzyme pairs (e.g. depending on what site is present within the oligo sequence, XbaI/MluI or NheI/MluI or XbaI/AscI or NheI/AscI) and inserted into expression vectors (e.g. fungal expression vectors including Y. lipolytica expression vectors such as MB4629 and MB4691 described herein).
The DNA and proteins they encode of the Y. lipolytica genes represented in FIG. 10 are as follows (intron sequence is underlined):








YALI0F30481g



DNA:








(SEQ ID NO: 122)









atgtcgcaaccccagaacgttggaatcaaagccctcgagatctacgtgccttctcgaattgtcaaccaggctgagctcgagaagcacgacggtgtc



gctgctggcaagtacaccattggtcttggtcagaccaacatggcctttgtcgacgacagagaggacatctattcctttgccctgaccgccgtctctcg


actgctcaagaacaacaacatcgaccctgcatctattggtcgaatcgaggttggtactgaaacccttctggacaagtccaagtccgtcaagtctgtgc


tcatgcagctctttggcgagaacagcaacattgagggtgtggacaacgtcaacgcctgctacggaggaaccaacgccctgttcaacgctatcaact


gggttgagggtcgatcttgggacggccgaaacgccatcgtcgttgccggtgacattgccctctacgcaaagggcgctgcccgacccaccggagg


tgccggctgtgttgccatgctcattggccccgacgctcccctggttcttgacaacgtccacggatcttacttcgagcatgcctacgatttctacaagcct


gatctgacctccgagtacccctatgttgatggccactactccctgacctgttacacaaaggccctcgacaaggcctacgctgcctacaacgcccgag


ccgagaaggtcggtctgttcaaggactccgacaagaagggtgctgaccgatttgactactctgccttccacgtgcccacctgcaagcttgtcaccaa


gtcttacgctcgacttctctacaacgactacctcaacgacaagagcctgtacgagggccaggtccccgaggaggttgctgccgtctcctacgatgc


ctctctcaccgacaagaccgtcgagaagaccttccttggtattgccaaggctcagtccgccgagcgaatggctccttctctccagggacccaccaa


caccggtaacatgtacaccgcctctgtgtacgcttctctcatctctctgctgacttttgtccccgctgagcagctgcagggcaagcgaatctctctcttct


cttacggatctggtcttgcttccactcttttctctctgaccgtcaagggagacatttctcccatcgtcaaggcctgcgacttcaaggctaagctcgatgac


cgatccaccgagactcccgtcgactacgaggctgccaccgatctccgagagaaggcccacctcaagaagaactttgagccccagggagacatca


agcacatcaagtctggcgtctactacctcaccaacatcgatgacatgttccgacgaaagtacgagatcaagcagtag


 


Protein:








(SEQ ID NO: 123)









Msqpqnvgikaleiyvpsrivnqaelekhdgvaagkytiglgqtnmafvddrediysfaltavsrllknnnidpasigrievgtetlldksksvk



svlmqlfgensniegvdnvnacyggtnalfnainwvegrswdgrnaivvagdialyakgaarptggagcvamligpdaplvldnvhgsyfe


haydfykpdltseypyvdghysltcytkaldkayaaynaraekvglfkdsdkkgadrfdysafhvptcklvtksyarllyndylndkslyegq


vpeevaavsydasltdktvektflgiakaqsaermapslqgptntgnmytasvyaslislltfvpaeqlqgkrislfsygsglastlfsltvkgdisp


ivkacdfkaklddrstetpvdyeaatdlrekahlkknfepqgdikhiksgvyyltniddmfrrkyeikq


 


YALI0B16038g


DNA:








(SEQ ID NO: 124)









atggactacatcatttcggcgccaggcaaagtgattctatttggtgaacatgccgctgtgtttggtaagcctgcgattgcagcagccatcgacttgcga



acatacctgcttgtcgaaaccacaacatccgacaccccgacagtcacgttggagtttccagacatccacttgaacttcaaggtccaggtggacaagc


tggcatctctcacagcccagaccaaggccgaccatctcaattggtcgactcccaaaactctggataagcacattttcgacagcttgtctagcttggcg


cttctggaagaacctgggctcactaaggtccagcaggccgctgttgtgtcgttcttgtacctctacatccacctatgtcccccttctgtgtgcgaagatt


catcaaactgggtagttcgatcaacgctgcctatcggcgcgggcctgggctcttccgcatccatttgtgtctgtttggctgcaggtcttctggttctcaa


cggccagctgagcattgaccaggcaagagatttcaagtccctgaccgagaagcagctgtctctggtggacgactggtccttcgtcggtgaaatgtg


cattcacggcaacccgtcgggcatcgacaatgctgtggctactcagggaggtgctctgttgttccagcgacctaacaaccgagtccctcttgttgac


attcccgagatgaagctgctgcttaccaatacgaagcatcctcgatctaccgcagacctggttggtggagtcggagttctcactaaagagtttggctc


catcatggatcccatcatgacttcagtaggcgagatttccaaccaggccatggagatcatttctagaggcaagaagatggtggaccagtctaaccttg


agattgagcagggtatcttgcctcaacccacctctgaggatgcctgcaacgtgatggaagatggagctactcttcaaaagttgagagatatcggttcg


gaaatgcagcatctagtgagaatcaatcacggcctgcttatcgctatgggtgtttcccacccgaagctcgaaatcattcgaactgcctccattgtccac


aacctgggtgagaccaagctcactggtgctggaggaggaggttgcgccatcactctagtcacttctaaagacaagactgcgacccagctggagga


aaatgtcattgctttcacagaggagatggctacccatggcttcgaggtgcacgagactactattggtgccagaggagttggtatgtgcattgaccatc


cctctctcaagactgttgaagccttcaagaaggtggagcgggcggatctcaaaaacatcggtccctggacccattag


 


Protein:








(SEQ ID NO: 125)









mdyiisapgkvilfgehaavfgkpaiaaaidlrtyllvetttsdtptvtlefpdihlnfkvqvdklasltaqtkadhlnwstpktldkhifdslsslall



eepgltkvqqaavvsflylyihlcppsvcedssnwvvrstlpigaglgssasicyclaagllvlngqlsidqardfksltekqlslvddwsfvgem


cihgnpsgidnavatqggallfqrpnnrvplvdipemkllltntkhprstadlvggvgvltkefgsimdpimtsvgeisnqameiisrgkkmv


dqsnleieqgilpqptsedacnvmedgatlqklrdigsemqhlvrinhglliamgvshpkleiirtasivhnlgetkltgaggggcaitlvtskdk


tatqleenviafteemathgfevhettigargvgmcidhpslktveafkkveradlknigpwth


 


YALI0E06193g


DNA:








(SEQ ID NO: 126)









atgaccacctattcggctccgggaaaggccctcctttgcggcggttatttggttattgatccggcgtattcagcatacgtcgtgggcctctcggcgcgt



atttacgcgacagtttcggcttccgaggcctccaccacctctgtccatgtcgtctctccgcagtttgacaagggtgaatggacctacaactacacgaa


cggccagctgacggccatcggacacaacccatttgctcacgcggccgtcaacaccgttctgcattacgttcctcctcgaaacctccacatcaacatc


agcatcaaaagtgacaacgcgtaccactcgcaaattgacagcacgcagagaggccagtttgcataccacaaaaaggcgatccacgaggtgccta


aaacgggcctcggtagctccgctgctcttaccaccgttcttgtggcagctttgctcaagtcatacggcattgatcccttgcataacacccacctcgttca


caacctgtcccaggttgcacactgctcggcacagaagaagattgggtctggatttgacgtggcttcggccgtttgtggctctctagtctatagacgttt


cccggcggagtccgtgaacatggtcattgcagctgaagggacctccgaatacggggctctgttgagaactaccgttaatcaaaagtggaaggtga


ctctggaaccatccttcttgccgccgggaatcagcctgcttatgggagacgtccagggaggatctgagactccaggtatggtggccaaggtgatgg


catggcgaaaagcaaagccccgagaagccgagatggtgtggagagatctcaacgctgccaacatgctcatggtcaagttgttcaacgacctgcgc


aagctctctctcactaacaacgaggcctacgaacaacttttggccgaggctgctcctctcaacgctctaaagatgataatgttgcagaaccctctcgg


agaactagcacgatgcattatcactattcgaaagcatctcaagaagatgacacgggagactggtgctgctattgagccggatgagcagtctgcattg


ctcaacaagtgcaacacttatagtggagtcattggaggtgttgtgcctggagcaggaggctacgatgctatttctcttctggtgatcagctctacggtg


aacaatgtcaagcgagagagccagggagtccaatggatggagctcaaggaggagaacgagggtctgcggctcgagaaggggttcaagtag


 


Protein:








(SEQ ID NO: 127)









mttysapgkallcggylvidpaysayvvglsariyatvsaseasttsvhvvspqfdkgewtynytngqltaighnpfahaavntvlhyvpprnl



hinisiksdnayhsqidstqrgqfayhkkaihevpktglgssaalttvlvaallksygidplhnthlvhnlsqvahcsaqkkigsgfdvasavcgs


lvyrrfpaesvnmviaaegtseygallrttvnqkwkvtlepsflppgisllmgdvqggsetpgmvakvmawrkakpreaemvwrdlnaan


mlmvklfildlrklsltnneayeqllaeaaplnalkmimlqnplgelarciitirkhlkkmtretgaaiepdeqsallnkcntysgviggvvpgag


gydaisllvisstvnnvkresqgvqwmelkeeneglrlekgfk


 


YALI0F05632g


DNA:








(SEQ ID NO: 128)









atgatccaccaggcctccaccaccgctccggtgaacattgcgacactcaagtactggggcaagcgagaccctgctctcaatctgcccactaacaac



tccatctccgtgactttgtcgcaggatgatctgcggaccctcaccacagcctcgtgttcccctgatttcacccaggacgagctgtggctcaatggcaa


gcaggaggacgtgagcggcaaacgtctggttgcgtgtttccgagagctgcgggctctgcgacacaaaatggaggactccgactcttctctgcctaa


gctggccgatcagaagctcaagatcgtgtccgagaacaacttccccaccgccgctggtctcgcctcatcggctgctggctttgccgccctgatccg


agccgttgcaaatctctacgagctccaggagacccccgagcagctgtccattgtggctcgacagggctctggatccgcctgtcgatctctctacgga


ggctacgtggcatgggaaatgggcaccgagtctgacggaagcgactcgcgagcggtccagatcgccaccgccgaccactggcccgagatgcg


agccgccatcctcgttgtctctgccgacaagaaggacacgtcgtccactaccggtatgcaggtgactgtgcacacttctcccctcttcaaggagcga


gtcaccactgtggttcccgagcggtttgcccagatgaagaagtcgattctggaccgagacttccccacctttgccgagctcaccatgcgagactcaa


accagttccacgccacctgtctggactcgtatcctcccattttctacctcaacgacgtgtcgcgagcctccattcgggtagttgaggccatcaacaag


gctgccggagccaccattgccgcctacacctttgatgctggacccaactgtgtcatctactacgaggacaagaacgaggagctggttctgggtgct


ctcaaggccattctgggccgtgtggagggatgggagaagcaccagtctgtggacgccaagaagattgatgttgacgagcggtgggagtccgagc


tggccaacggaattcagcgggtgatccttaccaaggttggaggagatcccgtgaagaccgctgagtcgcttatcaacgaggatggttctctgaaga


acagcaagtag


 


Protein:








(SEQ ID NO: 129)









mihqasttapvniatlkywgkrdpalnlptnnsisvtlsqddlrtlttascspdftqdelwlngkqedvsgkrlvacfrelralrhkmedsdsslpk



ladqklkivsennfptaaglassaagfaaliravanlyelqetpeqlsivarqgsgsacrslyggyvawemgtesdgsdsravqiatadhwpem


raailvvsadkkdtssttgmqvtvhtsplfkervttvvperfaqmkksildrdfptfaeltmrdsnqfhatcldsyppifylndvsrasirvveain


kaagatiaaytfdagpncviyyedkneelvlgalkailgrvegwekhqsvdakkidvderweselangiqrviltkvggdpvktaeslinedg


slknsk


 


YALI0F04015g


DNA:








(SEQ ID NO: 130)









Atgacgacgtcttacagcgacaaaatcaagagtatcagcgtgagctctgtggctcagcagtttcctgaggtggcgccgattgcggacgtgtccaag



gctagccggcccagcacggagtcgtcggactcgtcggccaagctatttgatggccacgacgaggagcagatcaagctgatggacgagatctgtg


tggtgctggactgggacgacaagccgattggcggcgcgtccaaaaagtgctgtcatctgatggacaacatcaacgacggactggtgcatcgggc


cttttccgtgttcatgttcaacgaccgcggtgagctgcttctgcagcagcgggcggcggaaaaaatcacctttgccaacatgtggaccaacacgtgc


tgctcgcatcctctggcggtgcccagcgagatgggcgggctggatctggagtcccggatccagggcgccaaaaacgccgcggtccggaagctt


gagcacgagctgggaatcgaccccaaggccgttccggcagacaagttccatttcctcacccggatccactacgccgcgccctcctcgggcccctg


gggcgagcacgagattgactacattctgtttgtccggggcgaccccgagctcaaggtggtggccaacgaggtccgcgataccgtgtgggtgtcgc


agcagggactcaaggacatgatggccgatcccaagctggttttcaccccttggttccggctcatttgtgagcaggcgctgtttccctggtgggacca


gttggacaatctgcccgcgggcgatgacgagattcggcggtggatcaagtag


 


Protein:








(SEQ ID NO: 131)









mttsysdkiksisyssvaqqfpevapiadvskasrpstessdssaklfdghdeeqiklmdeicvvldwddkpiggaskkcchlmdnindglv



hrafsvfmfndrgelllqqraaekitfanmwtntccshplavpsemggldlesriqgaknaavrklehelgidpkavpadkfhfltrihyaapss


gpwgeheidyilfvrgdpelkvvanevrdtvwvsqqglkdmmadpklvftpwfrliceqalfpwwdqldnlpagddeirrwik


 


YALI0E05753


DNA:








(SEQ ID NO: 132)









atgtccaaggcgaaattcgaaagcgtgttcccccgaatctccgaggagctggtgcagctgctgcgagacgagggtctgccccaggatgccgtgc



agtggttttccgactcacttcagtacaactgtgtgggtggaaagctcaaccgaggcctgtctgtggtcgacacctaccagctactgaccggcaagaa


ggagctcgatgacgaggagtactaccgactcgcgctgctcggctggctgattgagctgctgcaggcgtttttcctcgtgtcggacgacattatggat


gagtccaagacccgacgaggccagccctgctggtacctcaagcccaaggtcggcatgattgccatcaacgatgctttcatgctagagagtggcat


ctacattctgcttaagaagcatttccgacaggagaagtactacattgaccttgtcgagctgttccacgacatttcgttcaagaccgagctgggccagct


ggtggatcttctgactgcccccgaggatgaggttgatctcaaccggttctctctggacaagcactcctttattgtgcgatacaagactgcttactactcc


ttctacctgcccgttgttctagccatgtacgtggccggcattaccaaccccaaggacctgcagcaggccatggatgtgctgatccctctcggagagt


acttccaggtccaggacgactaccttgacaactttggagaccccgagttcattggtaagatcggcaccgacatccaggacaacaagtgctcctggct


cgttaacaaagcccttcagaaggccacccccgagcagcgacagatcctcgaggacaactacggcgtcaaggacaagtccaaggagctcgtcatc


aagaaactgtatgatgacatgaagattgagcaggactaccttgactacgaggaggaggttgttggcgacatcaagaagaagatcgagcaggttga


cgagagccgaggcttcaagaaggaggtgctcaacgctttcctcgccaagatttacaagcgacagaagtag


 


Protein:








(SEQ ID NO: 133)









mskakfesvfpriseelvqllrdeglpqdavqwfsdslqyncvggklnrglsvvdtyqlltgkkelddeeyyrlallgwliellqafflvsddim



desktrrgqpcwylkpkvgmiaindafmlesgiyillkkhfrqekyyidlvelfhdisfktelgqlvdlltapedevdlnrfsldkhsfivrykta


yysfylpvvlamyvagitnpkdlqqamdvliplgeyfqvqddyldnfgdpefigkigtdiqdnkcswlvnkalqkatpeqrqilednygvk


dkskelvikklyddmkieqdyldyeeevvgdikkkieqvdesrgfkkevlnaflakiykrqk


 


YALI0E18634g


DNA:








(SEQ ID NO: 134)









atgttacgactacgaaccatgcgacccacacagaccagcgtcagggcggcgcttgggcccaccgccgcggcccgaaacatgtcctcctccagc



ccctccagcttcgaatactcgtcctacgtcaagggcacgcgggaaatcggccaccgaaaggcgcccacaacccgtctgtcggttgagggcccca


tctacgtgggcttcgacggcattcgtcttctcaacctgccgcatctcaacaagggctcgggattccccctcaacgagcgacgggaattcagactcag


tggtcttctgccctctgccgaagccaccctggaggaacaggtcgaccgagcataccaacaattcaaaaagtgtggcactcccttagccaaaaacgg


gttctgcacctcgctcaagttccaaaacgaggtgctctactacgccctgctgctcaagcacgttaaggaggtcttccccatcatctatacaccgactca


gggagaagccattgaacagtactcgcggctgttccggcggcccgaaggctgcttcctcgacatcaccagtccctacgacgtggaggagcgtctg


ggagcgtttggagaccatgacgacattgactacattgtcgtgactgactccgagggtattctcggaattggagaccaaggagtgggcggtattggta


tttccatcgccaagctggctctcatgactctatgtgctggagtcaacccctcacgagtcattcctgtggttctggatacgggaaccaacaaccaggag


ctgctgcacgaccccctgtatctcggccgacgaatgccccgagtgcgaggaaagcagtacgacgacttcatcgacaactttgtgcagtctgcccga


aggctgtatcccaaggcggtgatccatttcgaggactttgggctcgctaacgcacacaagatcctcgacaagtatcgaccggagatcccctgcttca


acgacgacatccagggcactggagccgtcactttggcctccatcacggccgctctcaaggtgctgggcaaaaatatcacagatactcgaattctcgt


gtacggagctggttcggccggcatgggtattgctgaacaggtctatgataacctggttgcccagggtctcgacgacaagactgcgcgacaaaacat


ctttctcatggaccgaccgggtctactgaccaccgcacttaccgacgagcagatgagcgacgtgcagaagccgtttgccaaggacaaggccaatt


acgagggagtggacaccaagactctggagcacgtggttgctgccgtcaagccccatattctcattggatgttccactcagcccggcgcctttaacga


gaaggtcgtcaaggagatgctcaaacacacccctcgacccatcattctccctctttccaaccccacacgtcttcatgaggctgtccctgcagatctgt


acaagtggaccgacggcaaggctctggttgccaccggctcgccctttgacccagtcaacggcaaggagacgtctgagaacaataactgctttgtttt


ccccggaatcgggctgggagccattctgtctcgatcaaagctcatcaccaacaccatgattgctgctgccatcgagtgcctcgccgaacaggcccc


cattctcaagaaccacgacgagggagtacttcccgacgtagctctcatccagatcatttcggcccgggtggccactgccgtggttcttcaggccaag


gctgagggcctagccactgtcgaggaagagctcaagcccggcaccaaggaacatgtgcagattcccgacaactttgacgagtgtctcgcctgggt


cgagactcagatgtggcggcccgtctaccggcctctcatccatgtgcgggattacgactag


 


Protein:








(SEQ ID NO: 135)








mlrlrtmrptqtsvraalgptaaarnmsssspssfeyssyvkgtreighrkapttrlsvegpiyvgfdgirllnlphlnkgsgfplnerrefrlsgllp


saeatleeqvdrayqqfkkcgtplakngfctslkfqnevlyyalllkhvkevfpiiytptqgeaieqysrlfrrpegcflditspydveerlgafgdh


ddidyivvtdsegilgigdqgvggigisiaklalmtlcagvnpsrvipvvldtgtnnqellhdplylgrrmprvrgkqyddfidnfvqsarrlyp


kavihfedfglanahkildkyrpeipcfnddiqgtgavtlasitaalkvlgknitdtrilvygagsagmgiaeqvydnlvaqglddktarqniflm


drpgllttaltdeqmsdvqkpfakdkanyegvdtktlehvvaavkphiligcstqpgafnekvvkemlkhtprpiilplsnptrlheavpadly


kwtdgkalvatgspfdpvngketsennncfvfpgiglgailsrsklitntmiaaaieclaeqapilknhdegvlpdvaliqiisarvatavvlqak


aeglatveeelkpgtkehvqipdnfdeclawvetqmwrpvyrplihvrdyd


 


YALI0E11495g


DNA:








(SEQ ID NO: 136)








atgccgcagcaagcaatggatatcaagggcaaggccaagtctgtgcccatgcccgaagaagacgacctggactcgcattttgtgggtcccatctct


ccccgacctcacggagcagacgagattgctggctacgtgggctgcgaagacgacgaagacgagcttgaagaactgggaatgctgggccgatct


gcgtccacccacttctcttacgcggaagaacgccacctcatcgaggttgatgccaagtacagagctcttcatggccatctgcctcatcagcactctca


gagtcccgtgtccagatcttcgtcatttgtgcgggccgaaatgaaccacccccctcccccaccctccagccacacccaccaacagccagaggacg


atgacgcatcttccactcgatctcgatcgtcgtctcgagcttctggacgcaagttcaacagaaacagaaccaagtctggatcttcgctgagcaagggt


ctccagcagctcaacatgaccggatcgctcgaagaagagccctacgagagcgatgacgatgcccgactatctgcggaagacgacattgtctatga


tgctacccagaaagacacctgcaagcccatatctcctactctcaaacgcacccgcaccaaggacgacatgaagaacatgtccatcaacgacgtca


aaatcaccaccaccacagaagatcctcttgtggcccaggagctgtccatgatgttcgaaaaggtgcagtactgccgagacctccgagacaagtacc


aaaccgtgtcgctacagaaggacggagacaaccccaaggatgacaagacacactggaaaatttaccccgagcctccaccaccctcctggcacga


gaccgaaaagcgattccgaggctcgtccaaaaaggagcaccaaaagaaagacccgacaatggatgaattcaaattcgaggactgcgaaatcccc


ggacccaacgacatggtcttcaagcgagatcctacctgtgtctatcaggtctatgaggatgaaagctctctcaacgaaaataagccgtttgttgccatc


ccctcaatccgagattactacatggatctggaggatctcattgtggcttcgtctgacggacctgccaagtcttttgctttccgacgactgcaatatctag


aagccaagtggaacctctactacctgctcaacgagtacacggagacaaccgagtccaagaccaacccccatcgagacttttacaacgtacgaaag


gtcgacacccacgttcaccactctgcctgcatgaaccagaagcatctgctgcgattcatcaaatacaagatgaagaactgccctgatgaagttgtcat


ccaccgagacggtcgggagctgacactctcccaggtgtttgagtcacttaacttgactgcctacgacctgtctatcgatacccttgatatgcatgctca


caaggactcgttccatcgatttgacaagttcaacctcaagtacaaccctgtcggtgagtctcgactgcgagaaatcttcctaaagaccgacaactaca


tccagggtcgatacctagctgagatcacaaaggaggtgttccaggatctcgagaactcgaagtaccagatggcggagtaccgtatttccatctacg


gtcggtccaaggacgagtgggacaagctggctgcctgggtgctggacaacaaactgttttcgcccaatgttcggtggttgatccaggtgcctcgact


gtacgacatttacaagaaggctggtctggttaacacctttgccgacattgtgcagaacgtctttgagcctcttttcgaggtcaccaaggatcccagtac


ccatcccaagctgcacgtgttcctgcagcgagttgtgggctttgactctgtcgatgacgagtcgaagctggaccgacgtttccaccgaaagttccca


actgcagcatactgggacagcgcacagaaccctccctactcgtactggcagtactatctatacgccaacatggcctccatcaacacctggagacag


cgtttgggctataatacttttgagttgcgaccccatgctggagaggctggtgacccagagcatcttctgtgcacttatctggttgctcagggtatcaacc


acggtattctgttgcgaaaggtgcccttcattcagtacctttactacctggaccagatccccattgccatgtctcctgtgtccaacaatgcgctgttcctc


acgttcgacaagaaccccttctactcatacttcaagcggggtctcaacgtgtccttgtcatcggatgatcctctgcagtttgcttacactaaggaggctc


tgattgaggagtactctgtggctgcgctcatttacaagctttccaacgtggatatgtgtgagcttgctcgaaactcggtactgcaatctggctttgagcg


aatcatcaaggagcattggatcggcgaaaactacgagatccatggccccgagggcaacaccatccagaagacaaacgtgcccaatgtgcgtctg


gccttccgagacgagactttgacccacgagcttgctctggtggacaagtacaccaatcttgaggagtttgagcggctgcatggttaa


 


Protein:








(SEQ ID NO: 137)









mpqqamdikgkaksvpmpeeddldshfvgpisprphgadeiagyvgceddedeleelgmlgrsasthfsyaeerhlievdakyralhghl



phqhsqspvsrsssfvraemnhpppppsshthqqpedddasstrsrsssrasgrkfnrnrtksgsslskglqqlnmtgsleeepyesdddarls


aeddivydatqkdtckpisptlkrtrtkddmknmsindvkittttedplvaqelsmmfekvqycrdlrdkyqtvslqkdgdnpkddkthwki


ypeppppswhetekrfrgsskkehqkkdptmdefkfedceipgpndmvfkrdptcvyqvyedesslnenkpfvaipsirdyymdledliv


assdgpaksfafrrlqyleakwnlyyllneytettesktnphrdfynvrkvdthvhhsacmnqkhllrfikykmkncpdevvihrdgreltlsq


vfeslnltaydlsidtldmhahkdsfhrfdkfnlkynpvgesrlreiflktdnyiqgrylaeitkevfqdlenskyqmaeyrisiygrskdewdkl


aawvldnklfspnvrwliqvprlydiykkaglvntfadivqnvfeplfevtkdpsthpklhvflqrvvgfdsvddeskldrrfhrkfptaaywd


saqnppysywqyylyanmasintwrqrlgyntfelrphageagdpehllctylvaqginhgillrkvpfiqylyyldqipiamspvsnnalflt


fdknpfysyfkrglnyslssddplqfaytkealieeysvaaliyklsnvdmcelarnsvlqsgferiikehwigenyeihgpegntiqktnvpnv


rlafrdetlthelalvdkytnleeferlhg


 


YALI0D16753g


DNA:








(SEQ ID NO: 138)









atgttccgaacccgagttaccggctccaccctgcgatccttctccacctccgctgcccgacagcacaaggttgtcgtccttggcgccaacggaggc



attggccagcccctgtctctgctgctcaagctcaacaagaacgtgaccgacctcggtctgtacgatctgcgaggcgcccccggcgttgctgccgat


gtctcccacatccccaccaactccaccgtggccggctactctcccgacaacaacggcattgccgaggccctcaagggcgccaagctggtgctgat


ccccgccggtgtcccccgaaagcccggcatgacccgagacgatctgttcaacaccaacgcctccattgtgcgagacctggccaaggccgtcggt


gagcacgcccccgacgcctttgtcggagtcattgctaaccccgtcaactccaccgtccccattgtcgccgaggtgctcaagtccaagggcaagtac


gaccccaagaagctcttcggtgtcaccaccctcgacgtcatccgagccgagcgattcgtctcccagctcgagcacaccaaccccaccaaggagta


cttccccgttgttggcggccactccggtgtcaccattgtccccctcgtgtcccagtccgaccaccccgacattgccggtgaggctcgagacaagctt


gtccaccgaatccagtttggcggtgacgaggttgtcaaggccaaggacggtgccggatccgccaccctttccatggcccaggctgccgcccgatt


cgccgactctctcctccgaggtgtcaacggcgagaaggacgttgttgagcccactttcgtcgactctcctctgttcaagggtgagggcatcgacttct


tctccaccaaggtcactcttggccctaacggtgttgaggagatccaccccatcggaaaggtcaacgagtacgaggagaagctcatcgaggctgcc


aaggccgatctcaagaagaacattgagaagggtgtcaactttgtcaagcagaacccttaa


 


Protein:








(SEQ ID NO: 139)









mfrtrvtgstlrsfstsaarqhkvvvlganggigqplslllklnknvtdlglydlrgapgvaadvshiptnstvagyspdnngiaealkgaklvlip



agvprkpgmtrddlfntnasivrdlakavgehapdafvgvianpvnstvpivaevlkskgkydpkklfgvttldviraerfvsqlehtnptkey


fpvvgghsgvtivplvsqsdhpdiageardklvhriqfggdevvkakdgagsatlsmaqaaarfadsllrgvngekdvveptfvdsplfkgeg


idffstkvtlgpngveeihpigkvneyeeklieaakadlkkniekgvnfvkqnp


 


YALI0D16247g


DNA:








(SEQ ID NO: 140)









atgacacaaacgcacaatctgttttcgccaatcaaagtgggctcttcggagctccagaaccggatcgttctcgcacccttgactcgaaccagagctct



gcccggaaacgtgccctcggatcttgccacagagtactacgcacaaagagcagcatctccaggcactctcctcatcaccgaggccacatacatctc


ccccggatctgctggagtgcccattccaggagacggaatcgttccgggcatctggagtgacgagcagctcgaagcatggaaaaaggtgttcaag


gccgtgcacgaccgaggatccaaaatctacgtccagctgtgggacattggacgtgtcgcatggtaccacaagctgcaggaactgggcaactactt


ccctacaggcccctcagctatccccatgaagggagaggagagcgagcatctcaaggctctgactcactgggagatcaagggcaaggtggccctc


tacgtcaacgctgccaagaacgccattgccgcaggcgctgatggcgtcgagatccactcggccaacggctaccttcccgacacatttctgagaag


cgcctccaaccaacgaacagacgaatatggaggaagcatcgagaaccgggcccgattctcgctggagattgtcgacgctatcaccgaggccatt


ggagcagacaaaaccgccatccgtctgtctccctggtccactttccaggacattgaggtgaatgacaccgagacccccgcacagttcacatacctg


tttgagcagctgcagaagcgagccgacgagggaaagcagctggcctacgtgcatgtagttgagccccgactgtttggtccccccgagccctggg


ccaccaatgagcctttcagaaaaatttggaagggtaacttcattagagcaggtggatacgatagagagactgctcttgaggatgcagacaagtcaga


caacaccctgattgcctttggtcgagacttcattgccaatcctgatctcgtccaacgcctcaagaataacgagcctttggccaagtacgacagaacaa


ccttctacgttccaggtgccaagggctacactgattaccctgcgtacaagatgtaa


 


Protein:








(SEQ ID NO: 141)









mtqthnlfspikvgsselqnrivlapltrtralpgnvpsdlateyyaqraaspgtlliteatyispgsagvpipgdgivpgiwsdeqleawkkvfk



avhdrgskiyvqlwdigrvawyhklqelgnyfptgpsaipmkgeesehlkalthweikgkvalyvnaaknaiaagadgveihsangylpdt


flrsasnqrtdeyggsienrarfsleivdaiteaigadktairlspwstfqdievndtetpaqftylfeqlqkradegkqlayvhvveprlfgppep


watnepfrkiwkgnfiraggydretaledadksdntliafgrdfianpdlvqrlknneplakydrttfyvpgakgytdypaykm


 


YALI0A15972g


DNA:








(SEQ ID NO: 142)









atggaagccaaccccgaagtccagaccgatatcatcacgctgacccggttcattctgcaggaacagaacaaggtgggcgcgtcgtccgcaatccc



caccggagacttcactctgctgctcaactcgctgcagtttgccttcaagttcattgcccacaacatccgacgatcgaccctggtcaacctgattggcct


gtcgggaaccgccaactccaccggcgacgaccagaagaagctggacgtgatcggagacgagatcttcatcaacgccatgaaggcctccggtaa


ggtcaagctggtggtgtccgaggagcaggaggacctcattgtgtttgagggcgacggccgatacgccgtggtctgcgaccccatcgacggatcct


ccaacctcgacgccggcgtctccgtcggcaccattttcggcgtctacaagctccccgagggctcctccggatccatcaaggacgtgctccgaccc


ggaaaggagatggttgccgccggctacaccatgtacggtgcctccgccaacctggtgctgtccaccggaaacggctgcaacggcttcactctcga


tgaccctctgggagagttcatcctgacccaccccgatctcaagctccccgatctgcgatccatctactccgtcaacgagggtaactcctccctgtggt


ccgacaacgtcaaggactacttcaaggccctcaagttccccgaggacggctccaagccctactcggcccgatacattggctccatggtcgccgac


gtgcaccgaaccattctctacggaggtatgtttgcctaccccgccgactccaagtccaagaagggcaagctccgacttttgtacgagggtttccccat


ggcctacatcattgagcaggccggcggtcttgccatcaacgacaacggcgagcgaatcctcgatctggtccccaccgagatccacgagcgatcc


ggcgtctggctgggctccaagggcgagattgagaaggccaagaagtaccttctgaaatga


 


Protein:








(SEQ ID NO: 143)









meanpevqtdiitltrfilqeqnkvgassaiptgdftlllnslqfafkfiahnirrstlvnliglsgtanstgddqkkldvigdetttnamkasgkvkl



vvseeqedlivfegdgryavvcdpidgssnldagvsvgtifgvyklpegssgsikdvlrpgkemvaagytmygasanlvlstgngcngftld


dplgefilthpdlklpdlrsiysvnegnsslwsdnvkdyfkalkfpedgskpysaryigsmvadvhrtilyggmfaypadskskkgklrllye


gfpmayiieqagglaindngerildlvpteihersgvwlgskgeiekakkyllk


 


YALI0E11099g


DNA:








(SEQ ID NO: 144)









atgcgactcactctgccccgacttaacgccgcctacattgtaggagccgcccgaactcctgtcggcaagttcaacggagccctcaagtccgtgtctg



ccattgacctcggtatcaccgctgccaaggccgctgtccagcgatccaaggtccccgccgaccagattgacgagtttctgtttggccaggtgctgac


cgccaactccggccaggcccccgcccgacaggtggttatcaagggtggtttccccgagtccgtcgaggccaccaccatcaacaaggtgtgctctt


ccggcctcaagaccgtggctctggctgcccaggccatcaaggccggcgaccgaaacgttatcgtggccggtggaatggagtccatgtccaacac


cccctactactccggtcgaggtcttgttttcggcaaccagaagctcgaggactccatcgtcaaggacggtctctgggacccctacaacaacatccac


atgggcaactgctgcgagaacaccaacaagcgagacggcatcacccgagagcagcaggacgagtacgccatcgagtcctaccgacgggccaa


cgagtccatcaagaacggcgccttcaaggatgagattgtccccgttgagatcaagacccgaaagggcaccgtgactgtctccgaggacgaggag


cccaagggagccaacgccgagaagctcaagggcctcaagcctgtctttgacaagcagggctccgtcactgccggtaacgcctcccccatcaacg


atggtgcttctgccgttgtcgttgcctctggcaccaaggccaaggagctcggtacccccgtgctcgccaagattgtctcttacgcagacgccgccac


cgcccccattgactttaccattgctccctctctggccattcccgccgccctcaagaaggctggccttaccaaggacgacattgccctctgggagatca


acgaggccttctccggtgtcgctctcgccaacctcatgcgactcggaattgacaagtccaaggtcaacgtcaagggtggagctgttgctctcggcc


accccattggtgcctccggtaaccgaatctttgtgactttggtcaacgccctcaaggagggcgagtacggagttgccgccatctgcaacggtggag


gagcttccaccgccatcgtcatcaagaaggtctcttctgtcgagtag


 


Protein:








(SEQ ID NO: 145)









mrltlprlnaayivgaartpvgkfngalksvsaidlgitaakaavqrskvpadqideflfgqvltansgqaparqvvikggfpesveattinkvcs



sglktvalaaqaikagdrnvivaggmesmsntpyysgrglvfgnqkledsivkdglwdpynnihmgnccentnkrdgitreqqdeyaiesy


rranesikngafkdeivpveiktrkgtvtvsedeepkganaeklkglkpvfdkqgsvtagnaspindgasavvvasgtkakelgtpvlakivsy


adaatapidftiapslaipaalkkagltkddialweineafsgvalanlmrlgidkskvnvkggavalghpigasgnrifvtlvnalkegeygva


aicngggastaivikkvssve


 


YALI0E34793g


DNA:








(SEQ ID NO: 146)









atgtctgccaacgagaacatctcccgattcgacgcccctgtgggcaaggagcaccccgcctacgagctcttccataaccacacacgatctttcgtct



atggtctccagcctcgagcctgccagggtatgctggacttcgacttcatctgtaagcgagagaacccctccgtggccggtgtcatctatcccttcggc


ggccagttcgtcaccaagatgtactggggcaccaaggagactcttctccctgtctaccagcaggtcgagaaggccgctgccaagcaccccgaggt


cgatgtcgtggtcaactttgcctcctctcgatccgtctactcctctaccatggagctgctcgagtacccccagttccgaaccatcgccattattgccgag


ggtgtccccgagcgacgagcccgagagatcctccacaaggcccagaagaagggtgtgaccatcattggtcccgctaccgtcggaggtatcaagc


ccggttgcttcaaggttggaaacaccggaggtatgatggacaacattgtcgcctccaagctctaccgacccggctccgttgcctacgtctccaagtc


cggaggaatgtccaacgagctgaacaacattatctctcacaccaccgacggtgtctacgagggtattgctattggtggtgaccgataccctggtact


accttcattgaccatatcctgcgatacgaggccgaccccaagtgtaagatcatcgtcctccttggtgaggttggtggtgttgaggagtaccgagtcat


cgaggctgttaagaacggccagatcaagaagcccatcgtcgcttgggccattggtacttgtgcctccatgttcaagactgaggttcagttcggccac


gccggctccatggccaactccgacctggagactgccaaggctaagaacgccgccatgaagtctgctggcttctacgtccccgataccttcgagga


catgcccgaggtccttgccgagctctacgagaagatggtcgccaagggcgagctgtctcgaatctctgagcctgaggtccccaagatccccattga


ctactcttgggcccaggagcttggtcttatccgaaagcccgctgctttcatctccactatttccgatgaccgaggccaggagcttctgtacgctggcat


gcccatttccgaggttttcaaggaggacattggtatcggcggtgtcatgtctctgctgtggttccgacgacgactccccgactacgcctccaagtttctt


gagatggttctcatgcttactgctgaccacggtcccgccgtatccggtgccatgaacaccattatcaccacccgagctggtaaggatctcatttcttcc


ctggttgctggtctcctgaccattggtacccgattcggaggtgctcttgacggtgctgccaccgagttcaccactgcctacgacaagggtctgtcccc


ccgacagttcgttgataccatgcgaaagcagaacaagctgattcctggtattggccatcgagtcaagtctcgaaacaaccccgatttccgagtcgag


cttgtcaaggactttgttaagaagaacttcccctccacccagctgctcgactacgcccttgctgtcgaggaggtcaccacctccaagaaggacaacc


tgattctgaacgttgacggtgctattgctgtttcttttgtcgatctcatgcgatcttgcggtgcctttactgtggaggagactgaggactacctcaagaac


ggtgttctcaacggtctgttcgttctcggtcgatccattggtctcattgcccaccatctcgatcagaagcgactcaagaccggtctgtaccgacatcctt


gggacgatatcacctacctggttggccaggaggctatccagaagaagcgagtcgagatcagcgccggcgacgtttccaaggccaagactcgatc


atag


 


Protein:








(SEQ ID NO: 147)









msanenisrfdapvgkehpayelfhnhtrsfvyglqpracqgmldfdfickrenpsvagviypfggqfvtkmywgtketllpvyqqvekaa



akhpevdvvvnfassrsvysstmelleypqfrtiaiiaegvperrareilhkaqkkgvtiigpatvggikpgcfkvgntggmmdnivasklyr


pgsvayvsksggmsnelnniishttdgvyegiaiggdrypgttfidhilryeadpkckiivllgevggveeyrvieavkingqikkpivawaigt


casmfktevqfghagsmansdletakaknaamksagfyvpdtfedmpevlaelyekmvakgelsrisepevpkipidyswaqelglirkp


aafistisddrgqellyagmpisevfkedigiggvmsllwfrrrlpdyaskflemvlmltadhgpavsgamntiittragkdlisslvaglltigtrf


ggaldgaatefttaydkglsprqfvdtmrkqnklipgighrvksrnnpdfrvelvkdfvkknfpstqlldyalaveevttskkdnlilnvdgaia


vsfvdlmrscgaftveetedylkngvlnglfvlgrsigliahhldqkrlktglyrhpwdditylvgqeaiqkkrveisagdvskaktrs


 


YALI0D24431g


DNA:








(SEQ ID NO: 148)









atgtcagcgaaatccattcacgaggccgacggcaaggccctgctcgcacactttctgtccaaggcgcccgtgtgggccgagcagcagcccatca



acacgtttgaaatgggcacacccaagctggcgtctctgacgttcgaggacggcgtggcccccgagcagatcttcgccgccgctgaaaagacctac


ccctggctgctggagtccggcgccaagtttgtggccaagcccgaccagctcatcaagcgacgaggcaaggccggcctgctggtactcaacaagt


cgtgggaggagtgcaagccctggatcgccgagcgggccgccaagcccatcaacgtggagggcattgacggagtgctgcgaacgttcctggtcg


agccctttgtgccccacgaccagaagcacgagtactacatcaacatccactccgtgcgagagggcgactggatcctcttctaccacgagggagga


gtcgacgtcggcgacgtggacgccaaggccgccaagatcctcatccccgttgacattgagaacgagtacccctccaacgccacgctcaccaagg


agctgctggcacacgtgcccgaggaccagcaccagaccctgctcgacttcatcaaccggctctacgccgtctacgtcgatctgcagtttacgtatct


ggagatcaaccccctggtcgtgatccccaccgcccagggcgtcgaggtccactacctggatcttgccggcaagctcgaccagaccgcagagtttg


agtgcggccccaagtgggctgctgcgcggtcccccgccgctctgggccaggtcgtcaccattgacgccggctccaccaaggtgtccatcgacgc


cggccccgccatggtcttccccgctcctttcggtcgagagctgtccaaggaggaggcgtacattgcggagctcgattccaagaccggagcttctct


gaagctgactgttctcaatgccaagggccgaatctggacccttgtggctggtggaggagcctccgtcgtctacgccgacgccattgcgtctgccgg


ctttgctgacgagctcgccaactacggcgagtactctggcgctcccaacgagacccagacctacgagtacgccaaaaccgtactggatctcatgac


ccggggcgacgctcaccccgagggcaaggtactgttcattggcggaggaatcgccaacttcacccaggttggatccaccttcaagggcatcatcc


gggccttccgggactaccagtcttctctgcacaaccacaaggtgaagatttacgtgcgacgaggcggtcccaactggcaggagggtctgcggttg


atcaagtcggctggcgacgagctgaatctgcccatggagatttacggccccgacatgcacgtgtcgggtattgttcctttggctctgcttggaaagcg


gcccaagaatgtcaagccttttggcaccggaccttctactgaggcttccactcctctcggagtttaa


 


Protein:








(SEQ ID NO: 149)









Msaksiheadgkallahflskapvwaeqqpintfemgtpklasltfedgvapeqifaaaektypwllesgakfvakpdqlikrrgkagllvlnk



sweeckpwiaeraakpinvegidgvlrtflvepfvphdqkheyyinihsvregdwilfyheggvdvgdvdakaakilipvdieneypsnatl


tkellahvpedqhqtlldfinrlyavyvdlqftyleinplvviptaqgvevhyldlagkldqtaefecgpkwaaarspaalgqvvtidagstkvsi


dagpamvfpapfgrelskeeayiaeldsktgaslkltvlnakgriwtlvagggasvvyadaiasagfadelanygeysgapnetqtyeyaktvl


dlmtrgdahpegkvlfigggianftqvgstfkgiirafrdyqsslhnhkvkiyvrrggpnwqeglrliksagdelnlpmeiygpdmhvsgivp


lallgkrpknvkpfgtgpsteastplgv


 


YALI0E14190g


DNA:








(SEQ ID NO: 150)









atggttattatgtgtgtgggacctcagcacacgcatcatcccaacacagggtgcagtatatatagacagacgtgttccttcgcaccgttcttcacatatc



aaaacactaacaaattcaaaagtgagtatcatggtgggagtcaattgattgctcggggagttgaacaggcaacaatggcatgcacagggccagtga


aggcagactgcagtcgctgcacatggatcgtggttctgaggcgttgctatcaaaagggtcaattacctcacgaaacacagctggatgttgtgcaatc


gtcaattgaaaaacccgacacaatgcaagatctctttgcgcgcattgccatcgctgttgccatcgctgtcgccatcgccaatgccgctgcggattatta


tccctaccttgttccccgcttccgcacaaccggcgatgtctttgtatcatgaactctcgaaactaactcagtggttaaagctgtcgttgccggagccgct


ggtggtattggccagcccctttctcttctcctcaaactctctccttacgtgaccgagcttgctctctacgatgtcgtcaactcccccggtgttgccgctga


cctctcccacatctccaccaaggctaaggtcactggctacctccccaaggatgacggtctcaagaacgctctgaccggcgccaacattgtcgttatc


cccgccggtatcccccgaaagcccggtatgacccgagacgatctgttcaagatcaacgctggtatcgtccgagatctcgtcaccggtgtcgcccag


tacgcccctgacgcctttgtgctcatcatctccaaccccgtcaactctaccgtccctattgctgccgaggtcctcaagaagcacaacgtcttcaaccct


aagaagctcttcggtgtcaccacccttgacgttgtccgagcccagaccttcaccgccgctgttgttggcgagtctgaccccaccaagctcaacatcc


ccgtcgttggtggccactccggagacaccattgtccctctcctgtctctgaccaagcctaaggtcgagatccccgccgacaagctcgacgacctcgt


caagcgaatccagtttggtggtgacgaggttgtccaggctaaggacggtcttggatccgctaccctctccatggcccaggctggtttccgatttgccg


aggctgtcctcaagggtgccgctggtgagaagggcatcatcgagcccgcctacatctaccttgacggtattgatggcacctccgacatcaagcgag


aggtcggtgtcgccttcttctctgtccctgtcgagttcggccctgagggtgccgctaaggcttacaacatccttcccgaggccaacgactacgagaa


gaagcttctcaaggtctccatcgacggtctttacggcaacattgccaagggcgaggagttcattgttaaccctcctcctgccaagtaa


 


Protein:








(SEQ ID NO: 152)









vvkavvagaaggigqplslllklspyvtelalydvvnspgvaadlshistkakvtgylpkddglknaltganivvipagiprkpgmtrddlfkin



agivrdlvtgvaqyapdafvliisnpvnstvpiaaevlkkhnvfnpkklfgvttldvvraqtftaavvgesdptklnipvvgghsgdtivpllsltk


pkveipadklddlvkriqfggdevvqakdglgsatlsmaqagfrfaeavlkgaagekgiiepayiyldgidgtsdikrevgvaffsvpvefgpe


gaakaynilpeandyekkllkvsidglygniakgeefivnpppak


 


YALI0E22649g


DNA:








(SEQ ID NO: 151)









atgactggcaccttacccaagttcggcgacggaaccaccattgtggttcttggagcctccggcgacctcgctaagaagaagaccgtgagtattgaa



ccagactgaggtcaattgaagagtaggagagtctgagaacattcgacggacctgattgtgctctggaccactcaattgactcgttgagagccccaat


gggtcttggctagccgagtcgttgacttgttgacttgttgagcccagaacccccaacttttgccaccatacaccgccatcaccatgacacccagatgt


gcgtgcgtatgtgagagtcaattgttccgtggcaaggcacagcttattccaccgtgttccttgcacaggtggtctttacgctctcccactctatccgagc


aataaaagcggaaaaacagcagcaagtcccaacagacttctgctccgaataaggcgtctagcaagtgtgcccaaaactcaattcaaaaatgtcaga


aacctgatatcaacccgtcttcaaaagctaaccccagttccccgccctcttcggcctttaccgaaacggcctgctgcccaaaaatgttgaaatcatcg


gctacgcacggtcgaaaatgactcaggaggagtaccacgagcgaatcagccactacttcaagacccccgacgaccagtccaaggagcaggcca


agaagttccttgagaacacctgctacgtccagggcccttacgacggtgccgagggctaccagcgactgaatgaaaagattgaggagtttgagaag


aagaagcccgagccccactaccgtcttttctacctggctctgccccccagcgtcttccttgaggctgccaacggtctgaagaagtatgtctaccccg


gcgagggcaaggcccgaatcatcatcgagaagccctttggccacgacctggcctcgtcacgagagctccaggacggccttgctcctctctggaa


ggagtctgagatcttccgaatcgaccactacctcggaaaggagatggtcaagaacctcaacattctgcgatttggcaaccagttcctgtccgccgtgt


gggacaagaacaccatttccaacgtccagatctccttcaaggagccctttggcactgagggccgaggtggatacttcaacgacattggaatcatcc


gagacgttattcagaaccatctgttgcaggttctgtccattctagccatggagcgacccgtcactttcggcgccgaggacattcgagatgagaaggtc


aaggtgctccgatgtgtcgacattctcaacattgacgacgtcattctcggccagtacggcccctctgaagacggaaagaagcccggatacaccgat


gacgatggcgttcccgatgactcccgagctgtgacctttgctgctctccatctccagatccacaacgacagatgggagggtgttcctttcatcctccg


agccggtaaggctctggacgagggcaaggtcgagatccgagtgcagttccgagacgtgaccaagggcgttgtggaccatctgcctcgaaatgag


ctcgtcatccgaatccagccctccgagtccatctacatgaagatgaactccaagctgcctggccttactgccaagaacattgtcaccgacctggatct


gacctacaaccgacgatactcggacgtgcgaatccctgaggcttacgagtctctcattctggactgcctcaagggtgaccacaccaactttgtgcga


aacgacgagctggacatttcctggaagattttcaccgatctgctgcacaagattgacgaggacaagagcattgtgcccgagaagtacgcctacggc


tctcgtggccccgagcgactcaagcagtggctccgagaccgaggctacgtgcgaaacggcaccgagctgtaccaatggcctgtcaccaagggct


cctcgtga


 


Protein:








(SEQ ID NO: 153)









mtgtlpkfgdgttivvlgasgdlakkktfpalfglyrngllpknveiigyarskmtqeeyherishyfktpddqskeqakkflentcyvqgpyd



gaegyqrlnekieefekkkpephyrlfylalppsvfleaanglkkyvypgegkariiiekpfghdlassrelqdglaplwkeseifridhylgke


mvknlnilrfgnqflsavwdkntisnvqisfkepfgtegrggyfndigiirdviqnhllqvlsilamerpvtfgaedirdekvkvlrcvdilnidd


vilgqygpsedgkkpgytdddgvpddsravtfaalhlqihndrwegvpfilragkaldegkveirvqfrdvtkgvvdhlprnelviriqpsesi


ymkmnsklpgltaknivtdldltynrrysdvripeayeslildclkgdhtnfvrndeldiswkiftdllhkidedksivpekyaygsrgperlkq


wlrdrgyvrngtelyqwpvtkgss


 


YALI0B15598g


DNA:








(SEQ ID NO: 154)









atgactgacacttcaaacatcaagtgagtattgccgcacacaattgcaatcaccgccgggctctacctcctcagctctcgacgtcaatgggccagca



gccgccatttgaccccaattacactggttgtgtaaaaccctcaaccacaatcgcttatgctcaccacagactacgacttaaccaagtcatgtcacaggt


caaagtaaagtcagcgcaacaccccctcaatctcaacacacttttgctaactcaggcctgtcgctgacattgccctcatcggtctcgccgtcatgggc


cagaacctgatcctcaacatggccgaccacggtaagtatcaattgactcaagacgcaccagcaagatacagagcatacccagcaatcgctcctctg


ataatcgccattgtaacactacgttggttagattgatctaaggtcgttgctggttccatgcacttccacttgctcatatgaagggagtcaaactctattttg


atagtgtcctctcccatccccgaaatgtcgcattgttgctaacaataggctacgaggttgttgcctacaaccgaaccacctccaaggtcgaccacttcc


tcgagaacgaggccaagggtgagtatccgtccagctatgctgtttacagccattgaccccaccttcccccacaattgctacgtcaccattaaaaaaca


aaattaccggtatcggcaagctagactttcatgcaacctacgcagggtaacaagttgagtttcagccgtgcaccttacaggaaaaccagtcatacgc


cgaggcagtgtgaaagcgaaagcacacagcctacggtgattgattgcatttttttgacataggagggaaacacgtgacatggcaagtgcccaacac


gaatactaacaaacaggaaagtccattattggtgctcactctatcaaggagctgtgtgctctgctgaagcgaccccgacgaatcattctgctcgttaag


gccggtgctgctgtcgattctttcatcgaacagctcctgccctatctcgataagggtgatatcatcattgacggtggtaactcccacttccccgactcca


accgacgatacgaggagcttaacgagaagggaatcctctttgttggttccggtgtttccggcggtgaggagggtgcccgatacggtccctccatcat


gcccggtggaaacaaggaggcctggccccacattaagaagattttccaggacatctctgctaaggctgatggtgagccctgctgtgactgggtcgg


tgacgctggtgccggccactttgtcaagatggttcacaacggtattgagtatggtgacatgcagcttatctgcgaggcttacgacctcatgaagcgag


gtgctggtttcaccaatgaggagattggagacgttttcgccaagtggaacaacggtatcctcgactccttcctcattgagatcacccgagacatcttca


agtacgacgacggctctggaactcctctcgttgagaagatctccgacactgctggccagaagggtactggaaagtggaccgctatcaacgctcttg


accttggtatgcccgtcaccctgatcggtgaggccgtcttcgctcgatgcattctgccctcaagcaggagcgtgtccgagcttccaaggttcttgatg


gccccgagcccgtcaagttcactggtgacaagaaggagtttgtcgaccagctcgagcaggccctttacgcctccaagatcatctcttacgcccagg


gtttcatgcttatccgagaggccgccaagacctacggctgggagctcaacaacgccggtattgccctcatgtggcgaggtggttgcatcatccgatc


cgtcttccttgctgacatcaccaaggcttaccgacaggaccccaacctcgagaacctgctgttcaacgacttcttcaagaacgccatctccaaggcc


aacccctcttggcgagctaccgtggccaaggctgtcacctggggtgttcccactcccgcctttgcctcggctctggctttctacgacggttaccgatct


gccaagctccccgctaacctgctccaggcccagcgagactacttcggcgcccacacctaccagctcctcgatggtgatggaaagtggatccacac


caactggaccggccgaggtggtgaggtttcttcttccacttacgatgcttaa


 


Protein:








(SEQ ID NO: 155)









mtdtsnikpvadialiglavmgqnlilnmadhgyevvaynrttskvdhfleneakgksiigahsikelcallkrprriillvkagaavdsfieqll



pyldkgdiiidggnshfpdsnrryeelnekgilfvgsgvsggeegarygpsimpggnkeawphikkifqdisakadgepccdwvgdagag


hfvkmvhngieygdmqliceaydlmkrgagftneeigdvfakwnngildsflieitrdifkyddgsgtplvekisdtagqkgtgkwtainald


lgmpvtligeavfarclsalkqervraskvldgpepvkftgdkkefvdqleqalyaskiisyaqgfmlireaaktygwelnnagialmwrggci


irsvfladitkayrqdpnlenllfndffknaiskanpswratvakavtwgvptpafasalafydgyrsaklpanllqaqrdyfgahtyqlldgdgk


wihtnwtgrggevssstyda


 


YALI0D06303g


DNA:








(SEQ ID NO: 156)









atgctcaaccttagaaccgcccttcgagctgtgcgacccgtcactctggtgagtatctcggagcccgggacggctaccaacacacaagcaagatg



caacagaaaccggactttttaaatgcggattgcggaaaatttgcatggcggcaacgactcggagaaggagcgggacaattgcaatggcaggatgc


cattgacgaactgagggtgatgagagaccgggcctccgatgacgtggtggtgacgacagcccggctggtgttgccgggactgtctctgaaaagcaatt


tctctatctccggtctcaacagactccccttctctagctcaattggcattgtcttcagaaggtgtcttagtggtatccccattgttatcttcttttcccca


atgtcaatgtcaatgtcaatggctccgacctctttcacattaacacggcgcaaacacagataccacggaaccgactcaaacaaatccaaagagacg


cagcggaataattggcatcaacgaacgatttgggatactctggcgagaatgccgaaatatttcgcttgtcttgttgtttctcttgagtgagttgtttgtgaa


gtcgtttggaagaaggttcccaatgtcacaaaccataccaactcgttacagccagcttgtaatcccccacctcttcaatacatactaacgcagacccg


atcctacgccacttccgtggcctctttcaccggccagaagaactccaacggcaagtacactgtgtctctgattgagggagacggtatcggaaccga


gatctccaaggctgtcaaggacatctaccatgccgccaaggtccccatcgactgggaggttgtcgacgtcacccccactctggtcaacggcaaga


ccaccatccccgacagcgccattgagtccatcaaccgaaacaaggttgccctcaagggtcccctcgccacccccatcggtaagggccacgtttcc


atgaacctgactctgcgacgaaccttcaacctgttcgccaacgtccgaccttgcaagtccgtcgtgggctacaagaccccttacgagaacgtcgac


accctgctcatccgagagaacactgagggtgagtactccggtatcgagcacaccgtcgtccccggtgtcgttcagtccatcaagctgatcacccga


gaggcttccgagcgagtcatccggtacgcttacgagtacgccctgtcccgaggcatgaagaaggtccttgttgtccacaaggcctctattatgaagg


tctccgatggtcttttccttgaggttgctcgagagctcgccaaggagtacccctccattgacctttccgtcgagctgatcgacaacacctgtctgcgaat


ggtccaggaccccgctctctaccgagatgtcgtcatggtcatgcccaacctttacggtgacattctgtccgatcttgcctccggtcttatcggtggtctt


ggtctgaccccctccggtaacatgggtgacgaggtctccatcttcgaggccgtccacggatccgctcccgacattgctggcaagggtcttgctaac


cccactgctctgctgctctcctccgtgatgatgctgcgacacatgggtctcaacgacaacgccaccaacatcgagcaggccgtctttggcaccattg


cttccggccccgagaaccgaaccaaggatcttaagggtaccgccaccacttctcactttgctgagcagattatcaagcgactcaagtag


 


Protein:








(SEQ ID NO: 157)









mlnlrtalravrpvtltrsyatsvasftgqknsngkytvsliegdgigteiskavkdiyhaakvpidwevvdvtptlvngkttipdsaiesinrnkv



alkgplatpigkghvsmnltlrrtfnlfanvrpcksvvgyktpyenvdtllirentegeysgiehtvvpgvvqsiklitreaserviryayeyalsrg


mkkvlvvhkasimkvsdglflevarelakeypsidlsvelidntclrmvqdpalyrdvvmvmpnlygdilsdlasgligglgltpsgnmgde


vsifeavhgsapdiagkglanptalllssvmmlrhmglndnatnieqavfgtiasgpenrtkdlkgtattshfaeqiikrlk









Example 13
Determination of Lipid Levels of Y. Lipolytica 
12A. Determination of Lipid Levels of Y. Lipolytica in Various Growth Conditions of Varying Carbon to Nitrogen Ratios.
Shake flask testing was conducted using carbon to nitrogen (C/N) ratios of 160, 80, 60, 40, 30, 20, and 10 with yeast nitrogen base being the base medium providing vitamins, trace elements and salts Ammonium sulfate (which contains 21% nitrogen) was used as the nitrogen source and glucose (which contains 40% carbon) was used as the carbon source at a concentration of 30 g/L. The concentrations of ammonium sulfate corresponding to these ratios are: 0.36, 0.71, 0.95, 1.43, 1.91, 2.86, and 4.6 g/L, respectively. Uracil was supplemented at 0.2 mM. As controls, strains were also grown in yeast extract-peptone with 50 g/L of glucose (media in which lipids do not accumulate at high levels) and yeast extract-peptone with 5% olive oil (v/v) (media in which lipids accumulate at high levels).
Strain MF760 (10-14 ml of culture) was harvested after 4 days of growth at 30° C., during which time the cultures were shaking at 250 rpm. Following harvesting, cells were washed three times with water, with the exception of the oil-grown cells which were washed three times in 0.5% BSA and one time with water before lipid extractions. Lipids were extracted as described in Folch J, Lees, M, and Stanley, G. H. S. J. Biol. Chem. 226: 497-509, 1957. In brief, cell pellets were resuspended in 6 ml of water. A 1 ml aliquot was transferred to a pre-weighed tube with a hole on the lid, spun down and the cell pellet lyophilized overnight to determine the dry cell weight. The remaining 5 ml were placed in a 15 ml Falcon tube and spun down. Cell pellets were frozen at −20° C. until extractions were performed.
Two to three volumes of a Zymolyase solution (2 mg/ml Zymolyase 100T in 1M Sorbitol, 50 mM EDTA and 0.01% β-mercaptoethanol) was added to each cell pellet and placed at 37° C. with constant agitation for 1 hr. Two volumes of cubic zirconia beads were added to each tube and vortexed for 15-20 min. Samples were viewed under a microscope to ensure cell breakage before continuing with extractions. After cell breakage was complete, 6 ml of extraction solvent was added (a 2:1 mix of chloroform and methanol) and mixed. The mixture was spun down for 5 min at 3000 rpm and the organic layer was transferred to a clean tube. NaCl was added to the remaining aqueous layer to make it a 0.29% NaCl solution. 6 ml of extraction solvent was added and mixed, and the mixture was spun down for 5 min. The organic layers were pooled and filtered through a 0.2 μm filter to get rid of any cell debris. The extract was washed with 0.2 volumes of 0.29% NaCl solution and another 6 ml of extraction solvent added and mixed. Mixtures were spun and the organic layer was placed in a pre-weighed glass vial, the solvent was evaporated under a flow on nitrogen and the vial was weighed again to determine the weight of the lipid extracted. The dry cell weight is used to determine the percentage of lipid per dry cell weight. The lipid accumulation results are in the Table 48 below:







TABLE 48







Lipid accumulation under various carbon:


nitrogen ratio growth conditions










C/N Ratio
% lipid












YNB
160
61


3% Glucose
80
49



60
34



40
17



30
16



20
14



10
15


YEP
5% Glucose
22



5% olive oil
38









Other nitrogen sources tested were proline (12% nitrogen), sodium glutamate (7% nitrogen), soy acid hydrolysate (12% nitrogen), and yeast extract-peptone (26.8% nitrogen). All nitrogen sources tested at C/N ratios of 80 (with glucose as a carbon source), had significantly larger lipid bodies than at C/N ratios of 10 (also with glucose as a carbon source).

Strains MF858 and MF921 (example 2F and 2H) were harvested after 4 days of growth at 30° C. (3% glucose was used as the carbon source). Cells were washed three times with water and lipids extracted as described above. Lipid accumulation data for soy hydrolysate, yeast extract-peptone and yeast nitrogen base, used as a control, are listed in Table 49 below.







TABLE 49







Lipid accumulation under different carbon and nitrogen 


conditions with various nitrogen sources













% lipid













C/N Ratio
MF858
MF921







Soy hydrolysate
80
36
36




60
36
35




10
14
15



Yeast Extract-
80
37
37



Peptone
10
15
14



Yeast Nitrogen 
80
37
38



Base
10
13
11










12b. Determination of Lipid Levels Under High Carbon and Phosphate or Magnesium Limiting Conditions.

To test whether other nutrient limitations, under high carbon conditions, will allow for higher lipid accumulation, phosphate or magnesium limiting conditions were tested. For phosphate limiting conditions, yeast nitrogen base medium without phosphate was prepared. Shake flask testing was performed using carbon to phosphate ratios ranging from 5376 down to 42. This range corresponds to 7.8 mg/L up to 1 g/L, respectively, and the latter concentration corresponds to that are commonly used in yeast nitrogen base medium. Glucose, at 30 g/L, was used at the carbon source. Potassium phosphate monobasic (containing 28.7% phosphate) was used as the phosphate source.
For magnesium limiting conditions, yeast nitrogen base medium without magnesium was prepared. Shake flask testing was conducted using carbon to magnesium ratios ranging from 31360 down to 245. This range corresponds to 0.375 mg/L up to 0.5 g/L, and the latter magnesium concentration corresponds to that commonly used in yeast nitrogen base. Glucose, at 30 g/L, was used as the carbon source. Magnesium sulfate (containing 9.8% magnesium) was used as the magnesium source.
Strains MF858 and MF921 were harvested after 4 days of growth at 30° C., during which time the cultures were shaking at 250 rpm. Cells were washed three times with water before lipid extraction. Lipids were extracted as described above. Lipid accumulation data is listed in the Table 50 below:







TABLE 50







Lipid accumulation in phosphate or magnesium 


limiting growth conditions













% Lipid













g/L
MF858
MF921
















phosphate
1
14
14




0.0625
18
20




0.0313
34
41




0.0156
62
63




0.0078
83
76



magnesium
0.5
12
11




0.0313
NA
16




0.0156
NA
25




0.0078
NA
42




0.0039
48
48










Example 14
Effect of Temperature on Carotenoid Production
MF740 was transformed with pMB4719 with SalI, and a Ura+ colony was designated ML878. MF740 was transformed with pMB4629 cleaved with SalI, an Ade+ colony was designated ML857, and subsequently transformed with pMB4719 cleaved with SalI, to create ML836. ML878 and ML836 were grown for 4 days in YPD at 20° C., 24° C., and 28° C., and carotenoids were extracted and analyzed by HPLC. β-carotene or zeaxanthin yield (% dry cell weight) at 20° C. was chosen as a standard against which yields at other temperatures were compared. In addition, the ratio of zeaxanthin/carotenoid (% dry cell weight) was calculated for each temperature. Whereas the β-carotene levels fell with decreasing temperatures, the ratio of zeaxanthin to β-carotene increased with lower temperatures (Table 51).







TABLE 51







Effect of Temperature on carotenoid production












Temperature
β-carotene
Zeaxanthin
Zeaxanthin/






(β-carotene ratio


Strain
(° C.)
yield*
yield**
(% dry cell weight)***





MF878
20
1.0
1.0
2.4


MF878
24
1.3
1.0
1.9


MF878
28
3.2
1.5
1.1


MF836
20
1.0
1.0
1.0


MF836
24
1.9
1.2
0.7


MF836
28
3.4
1.1
0.4





*β-carotene yield is calculated as % DCW β-carotene at 20° C. divided by % DCW β-carotene at each temperature


**Zeaxanthin yield is calculated as % DCW zeaxanthin at 20° C. divided by % DCW zeaxanthin at each temperature


***Zeaxanthin/β-carotene ratio is calculated as % DCW zeaxanthin divided by % DCW β-carotene






Example 15
Construction of a Recyclable URA3 Marker Plasmid pMB5082
To create a selectively excisable (“recyclable”) URA3 marker, an 860 bp SpeI-SacI (blunt ended with T4 DNA ligase) fragment (containing the URA3 promoter and the first 121 nucleotides of the URA3 gene) from plasmid pMB4691 was inserted into the SpeI-NotI sites of plasmid pMB4534 to create pMB5055.
The URA3 promoter was excised from pMB5055 as an 878 bp fragment by XbaI-SpeI digest, and was ligated into XbaI-cleaved pMB4691. Orientation of the promoter was verified by restriction digest. The resulting plasmid, designated pMB5082, contained the URA3 promoter both upstream of the URA3 gene and downstream of its terminator. This cassette, once integrated into the Yarrowia genome, permits excision of the URA3 marker by homologous recombination between the two copies of the URA3 promoter. Colonies containing the excision may be selected on 5-FOA.
Example 16
Effects of Mutations in the Transcriptional Regulator, SPT8 on Carotenoid Production
Y. Lipolytica strain ML1018 was isolated by plasmid insertion mutagenesis. ML1018 was darker in hue, shiny, exclusively yeast-form rather than partial mycelial morphology and exhibited increased carotenoid levels when compared to its sibling transformants. Sequence analysis identified the site of ML1018 plasmid insertion between base pairs 701 and 702 of the SPT8 coding sequence. Experiments were undertaken to examine carotenoid levels in a targeted SPT8 disruption strain.
A 2.5 kb fragment containing the SPT8 gene (YALI0E23804g) with its endogenous promoter and terminator was amplified from genomic DNA isolated from Y. lipolytica strain NRRL Y-1095 using primers: MO5651 (5′-CACAAACTAGTGTCAGGAATATGAAACCAGG-3′) (SEQ ID NO:158) and MO5652 (5′-CACAAACTAGTGCATGTGATAGGAAGGAGGA-3′) (SEQ ID NO:159). Plasmid pMB5083 was constructed by phosphorylating the 2.5 kb SPT8 fragment with T4 polynucleotide kinase and ligating the phosphorylated fragment with desphosphorylated, EcoRV-digested pBluescriptSK−.
A 3.4 kb fragment containing the TEF1 promoter, XPR terminator, and a recyclable URA3 marker was isolated from plasmid pMB5082 bp Acc65I and XbaI (subsequently made blunt with Klenow) digestion. This fragment was cloned into the BsiWI and SmaI sites of pMB5083 to create pMB5086. BamHI-XbaI digestion of pMB5086 yields a 5.6 kb Y. Lipolytica SPT8 disruption fragment containing the TEF1 promoter and XPR terminators followed by a recyclable URA3 marker between base pairs 752 and 753 of the SPT8 coding sequence (SPT8::URA3 disruption cassette).
A 3.6 kb fragment containing the XPR terminator and ADE1 gene was excised from plasmid pMB4629 by MluI and EcoRV digest and subsequently cloned into MluI-Pml1-digested pMB5086. The resulting plasmid, pMB5124, contains a 5.8 kb BamHI-XbaI SPT8 disruption cassette similar to that in pMB5086, with the distinction that the recyclable URA3 marker is replaced with a non-recyclable ADE1 marker (SPT8::ADE1 disruption cassette).
Y. lipolytica strains MF740 and MF746 (both ade1 ura3) are transformed with a 5.8 kb BamHI-XbaI fragment from pMB5124 (spt8::ADE1). spt8 disruptants are distinguished from ectopic integrants by colony morphology, as spt8 strains are shinier, darker in hue, and less mycelial than SPT8 strains. Correct integration may be assayed by PCR or by Southern blotting. Carotenoid yield is assayed in spt8 disrupted and SPT8+ strains by harvesting carotenoids after a four-day fermentation in YPD shake flasks at 30° C.
Example 17
Construction Plasmid pMB4844 Encoding a Chimeric β-Carotene Hydroxylase-Ketolase (crtZW)
A β-carotene hydroxylase:β-carotene ketolase chimera is constructed as follows. First, a 0.5 kb fragment containing crtZ from Erythrobacter litoralis is amplified from pMB4715, a plasmid containing a copy of the crtZ gene, using primers MO4814: 5′-CACAACGTCTCTCTAGACACAAAAATGAGCT-3′ (SEQ ID NO:160) and MO4816: 5′-CACAACGTCTCAGCCGGCACCTGCTCCCATAGAATCTCG-3′ (SEQ ID NO:161) and the resulting fragment is digested with XbaI and BsmBI. Similarly, a 0.8 kb fragment containing crtW from Parvularcula bermudensis is amplified from pMB4731, a plasmid containing a copy of the crtW gene, with primers MO5060: 5′-CACAAGAAGACAACGGCGCAGGAGCCATGGACCCTACCGGAGACG-3′ (SEQ ID NO:162) and MO5061: 5′-CACAAGAAGACAACGCGTTTAAGGGCCGGTTCTCTTTC-3′ (SEQ ID NO:163) and the resulting fragment is digested with BbsI and MluI. The digested fragments containing the crtZ and crtW genes are then ligated in a three-piece reaction into NheI-MluI cleaved vector pMB4691 to create pMB4844. Sequence analysis confirms the creation of an in-frame fusion of crtZ and crtW placed under control of the TEF1 promoter and the XPR terminator. The chimeric sequence is designated crtZW. The amino acid sequence of crtZW is:







(SEQ ID NO: 175)







mswwaialivfgavvgmeffawfahkyimhgwgwswhrdhhephdntle


 


kndlfavvfgsvaallfvigalwsdplwwaavgitlygviytlvhdglvh


 


qrywrwtpkrgyakrlvqahrlhhatvgkeggvsfgfvfardpaklka


 


elkqqreqglavvrdsmgagagagamdptgdvtasprpqttipvrq


 


alwglslagaiiaawvfmhigfvffapldpivlalapviillqswls


 


vglfiishdaihgslapgrpafnramgrlcmtlyagfdfdrmaaa


 


hhrhhrspgtaadpdfsvdspdrplpwfgaffrryfgwrpfl


 


tvnavvftywlvlganpvnivlfygvpallsagqlfyfgtflphrherq


 


gfadhhrarsvrspymlslvtcyhfggyhhehhlfphepwwrlpq


 


rggwerdrrkrtgp






Example 18
pH Effects on Total Carotenoid Yield and Hydroxylation of Beta-Carotene
The effect of altering pH on total carotenoid yield and relative amount of individual carotenoids was investigated. Strain ML1011 (MF740 transformed with multiple integrated copies of the X. autotrophicus crtZ gene) which accumulates a mixture of carotenoids comprising beta-carotene, beta-cryptoxanthin, and zeaxanthin was fermented under the following parameters.

    
    
        Batch medium: YPD
        Temperature setpoint: 30° C.
        Initial volume: 210 ml
        Vessel volume: 400 ml
        Agitation rate: 1000 rpm
        Feed: 40% glucose
        Feed rate: 2 ml/hour, starting at 24th hour after inoculation
    
    


Four separate fermentor units were setup and the pH was controlled as follows:

    
    
        Unit 1: pH 5.5
        Unit 2: pH 7.0
        Unit 3: pH 7.0 at inoculation, continuously rising to a setpoint of pH 8.0 at 48 hours (change of 0.021 pH units/hour)
        Unit 4: pH 7.0 at inoculation, continuously rising to a setpoint of pH 9.0 at 48 hours (change of 0.042 pH units/hour
    
    


Additionally, the glucose feed of unit 4 was halted at 64 hours (see below). FIG. 12a depicts accumulation of total carotenoid (absorbance units per unit dry cell weight) throughout the fermentation. Excluding the last timepoint, units 1 and 2 accumulated similar amounts of carotenoid throughout the run. This result, consistent with previous experiments, suggests that varying the pH in the range of 5.5-7.0 does not affect total carotenoid yield. During this same period, fermentor unit 3 accumulated more carotenoid than units 1 and 2, suggesting setting pH to be within the range of 7.0-8.0 improves the rate of carotenoid biosynthesis. In unit 4, carbon dioxide evolution (indicating metabolic activity) and carotenoid accumulation started to fall precipitously when the unit reached pH 8.3 at approximately 31 hours (FIG. 12d), suggesting toxicity due to high pH. The feed to this unit was therefore stopped at 64 hours. Together, these results suggest that carotenoid yield may be maximized by maintaining pH within the range 7.0-8.0, while pH levels below or above this range were ineffective or toxic, respectively.
FIG. 12b depicts accumulation of zeaxanthin (absorbance units per dry cell weight; AU) over the course of the fermentation. As seen in FIG. 12b, zeaxanthin accumulation improves with increasing pH. Unit 4, at highest pH, shows superior zeaxanthin accumulation compared to all other units until hour 64, when its feed was terminated. Likewise, unit 3, maintained at pH 8.0 after hour 48, shows significantly improved zeaxanthin accumulation over units 1 and 2, maintained at pH 5.5 and 7.0, respectively. These results indicate that hydroxylation of beta carotene to zeaxanthin is favored by higher pH.
FIG. 12c depicts the fraction of carotenoid as zeaxanthin (AU zeaxanthin/AU total carotenoid) throughout the course of the fermentation. Unit 3 hydroxylated a greater fraction of beta-carotene than units 1 and 2, in addition to producing more total carotenoid (FIG. 12a) and more total zeaxanthin (FIG. 12b). This result demonstrates that at pH 8.0, zeaxanthin accumulation outpaced the global increase in carotenoid biosynthesis also seen at this pH
As seen in FIG. 12e, biomass accumulated fastest in unit 3 and remained above all other units until the hundred-thirtieth or so hour of fermentation. This unit similarly was the most metabolically active, as shown by its increased rate of carbon dioxide evolution compared to the other units over the same time period (FIG. 12d). The subsequent decline in biomass in this unit may be attributed to accelerated metabolism of carbon stored as intracellular oil, relative to the other three units. Thus, it appears that the pH range of 7.0-8.0 enables Yarrowia lipolytica both to accumulate biomass and metabolize stored carbon at rates faster than it is able at lower pH.
Together, these results indicate that total biomass accumulation, percentage of biomass representing carotenoid accumulation, and the hydroxylation of beta-carotene to zeaxanthin may be manipulated by maintaining fermentation pH in the approximate range of 7.0-8.0. Moreover, these results suggest that within this same range, an optimum pH may be selected at which to maximize production of both non-oxygenated carotenoids and xanthophylls (e.g. hydroxylation of b-carotene to zeaxanthin and total carotenoid production.
Example 19
Lycopene Epsilon Cyclase Sequences
The DNA and proteins they encode of the certain lycopene epsilon cyclase sequences are provided below. Corresponding Genbank Accession and GI numbers are found in table 23.








Ostreococcus lucimarinus sequence XP_001422490



DNA








(SEQ ID NO: 164)









ATGAAGGATGATCGCGAATGGATTGCGTTTCAACAGCGCAAGGTGTTTAGTGAGCAAAA



GCAAATCAAAGAGTACCTCAGTGCTTTGAACGACCGCGACAAGGTCGACGTTCTCGTTGT


CGGTGCGGGCCCCGCAGGTCTGGCGATCGCAGCGGAGACGGCGAAGAAGGGTCTTTCTG


TTGGTCTCGTCGCACCAGACACCCCGTTCGTGAACAACTACGGAGTATGGCTCGACGAGT


TCAAAGATCTAGGGCTCGAACACTGCTTGCTTCATAAGTATGACGACGCATTGGTTTGGT


TCGATGATTCTGATCCTGCGAGTGGAACTGAACTCGGTCGACCTTACGGTCAAGTGTGCC


GCAGGCGTCTTCGCGACCATTTGTTGAAGGAGTGCGCGGCGGCTGGCGTCAAGTATTTAC


CAGGCCTGGTAGATTTTGTGCGTCACGGTGACGTCGAAAAGAACGAGTTAGCCGAAGCA


AACAGAGGCCAGCAATTCACGTTGAATTCGCGTCTCGTCGTTGCCGGCACCGGTCACAAC


CGCGACATGCTCAGCTACGAAGAGGGTGCGCCGCCGGGCTGGCAGACTGCGTATGGCGT


TGAGGTGCGCATTCCGAACCACGGTTTTCCCGTGAACAAGGCCGTGTTCATGGATTTTCG


TCAAAGCGATCCGGAGGCGATGAAAGAGGAACAAGACGAGGGCGTTTGGCGCGTGCCG


TCTTTCCTTTACGTGTTACCCGTGGACAAGGATGTGGTGTTCGTCGAGGAGACGTGCCTC


GTCGCGCGCGTACAAGTGCCGTTCGATGAACTCAAACGGCGATTGTATCGTCGTATGAAG


CGGATGGGTATGGAAATCGTCGAAGAAGACATCTTGGAAGTCGAGGCGAGTTGGATTCC


ACTGGGCGGTACCCCGCCGGTTGCCCCGCAACGCACCATCGCGTACGGTGCAGCAGCCG


GCATGGTCCACCCTGCGTCTGGCTACTCCGTCGTAAACAGTATTAGCAAAGCTCCGCGTG


TTGCGACGGCCATGGCCGAAGGCTTGAAGGAGGGTGGCGAGATTGAGGCGAGCCGAAG


AGCGTGGGAAATCCTTTGGGGTGCGGAGCCACGAAGACAAATCGGTTTCTACCAGTTCG


GTATGGAGCTTCTCATGTCGCTTCGCATCGAGCAGATGCGCAACTTCTTTAGTACCTTCTT


TGCGCTTCCAACAAATCTGAGCAGAGGATTTTTGGGTAACAGATTGTCGAGCTCAGAGTT


GATCATGTTTGCTCTCACTACGTTCGCAATTGGTAACAACGAACTTCGTGGGTTGTTGCTC


GCTCACCTGGTTTCA


 


Protein








(SEQ ID NO: 165)








MKDDREWIAFQQRKVFSEQKQIKEYLSALNDRDKVDVLVVGAGPAGLAIAAETAKKGLSVG


LVAPDTPFVNNYGVWLDEFKDLGLEHCLLHKYDDALVWFDDSDPASGTELGRPYGQVCRR


RLRDHLLKECAAAGVKYLPGLVDFVRHGDVEKNELAEANRGQQFTLNSRLVVAGTGHNRD


MLSYEEGAPPGWQTAYGVEVRIPNHGFPVNKAVFMDFRQSDPEAMKEEQDEGVWRVPSFL


YVLPVDKDVVFVEETCLVARVQVPFDELKRRLYRRMKRMGMEIVEEDILEVEASWIPLGGTP


PVAPQRTIAYGAAAGMVHPASGYSVVNSISKAPRVATAMAEGLKEGGEIEASRRAWEILWG


AEPRRQIGFYQFGMELLMSLRIEQMRNFFSTFFALPTNLSRGFLGNRLSSSELIMFALTTFAIGN


NELRGLLLAHLVS


 


lycopene epsilon cyclase (Diospyros kaki) sequence BAE94036


DNA








(SEQ ID NO: 166)









ACTACGGCGTATGGGAGGATGAATTTAGAGATCTTGGACTTGAAAGGTGTATTGAACAT



GTTTGGAGAGACACAATTGTATATCTTGATGACAATGATCCCATTCTGATTGGTCGTGCT


TATGGACGAGTTAGTCGTCACTTGCTCCACGAGGAGCTATTAAGAAGGTGTGTGGAGTCA


GGTGTTTCATATTTGAGCTCAAAAGTGGAAAGAATTATTGAAACTACGAATGGGCAGAG


TCTCATAGAGTGCGGAACTGATGTTGTTGTCCCATGCAGGCTTGCTACTGTTGCTTCGGG


AGCAGCTTCTGGGAAACTTTTGAAGTTTGAGGTGGGAGGACCCAGAGTTTCTGTTCAAAC


AGCTTATGGTGTGGAGGTTGAGGTGGAAAACAATCCATATGACCCCAACTTGATGGTTTT


CATGGATTACAGAGACTATGCCAAACAAAAAGTTCAGCCTTTGGAAGCACAATATCCAA


CATTTCTTTATGCCATGCCTATGTCCCCTACAAGAGTCTTCTTTGAGGAAACTTGTTTGGC


TTCAAAGGATGCCATGCCTTTTGATCTATTAAAGAGGAAACTCATGGACAGATTAGAGAC


AATGGGAGTCCATGTTCTAAAAACGTATGAGGAGGAATGGTCTT


 


Protein








(SEQ ID NO: 167)









YGVWEDEFRDLGLERCIEHVWRDTIVYLDDNDPILIGRAYGRVSRHLLHEELLRRCVESGVS



YLSSKVERIIETTNGQSLIECGTDVVVPCRLATVASGAASGKLLKFEVGGPRVSVQTAYGVEV


EVENNPYDPNLMVFMDYRDYAKQKVQPLEAQYPTFLYAMPMSPTRVFFEETCLASKDAMP


FDLLKRKLMDRLETMGVHVLKTYEEEWS






Example 20
Construction of a Lutein Producing Strain
The following sequence, optimized for Y. lipolytica codon bias and encoding a putative lycopene epsilon cyclase from Ostreococcus lucimarinus CCE9901, is synthesized de novo:







(SEQ ID NO: 168)







TTCTAGAACAAAATGAAGGACGACCGAGAGTGGATCGCCTTCCAGCAGC


 


GAAAGGTGTTCTCTGAGCAGAAGCAGATCAAGGAGTACCTGTCTGCCCT


 


GAACGACCGAGACAAGGTGGACGTGCTGGTGGTGGGCGCCGGCCCCGCC


 


GGCCTGGCCATCGCCGCCGAGACCGCCAAGAAGGGCCTGTCTGTGGGCC


 


TGGTGGCCCCCGACACCCCCTTCGTGAACAACTACGGCGTGTGGCTGGA


 


CGAGTTCAAGGACCTGGGCCTGGAGCACTGTCTGCTGCACAAGTACGAC


 


GACGCCCTGGTGTGGTTCGACGACTCTGACCCCGCCTCTGGCACCGAGC


 


TGGGCCGACCCTACGGCCAGGTGTGTCGACGACGACTGCGAGACCACCT


 


GCTGAAGGAGTGTGCCGCCGCCGGCGTGAAGTACCTGCCCGGCCTGGTG


 


GACTTCGTGCGACACGGCGACGTGGAGAAGAACGAGCTGGCCGAGGCCA


 


ACCGAGGCCAGCAGTTCACCCTGAACTCTCGACTGGTGGTGGCCGGCAC


 


CGGCCACAACCGAGACATGCTGTCTTACGAGGAGGGCGCCCCCCCCGGC


 


TGGCAGACCGCCTACGGCGTGGAGGTGCGAATCCCCAACCACGGCTTCC


 


CCGTGAACAAGGCCGTGTTCATGGACTTCCGACAGTCTGACCCCGAGGC


 


CATGAAGGAGGAGCAGGACGAGGGCGTGTGGCGAGTGCCCTCTTTCCTG


 


TACGTGCTGCCCGTGGACAAGGACGTGGTGTTCGTGGAGGAGACCTGTC


 


TGGTGGCCCGAGTGCAGGTGCCCTTCGACGAGCTGAAGCGACGACTGTA


 


CCGACGAATGAAGCGAATGGGCATGGAGATCGTGGAGGAGGACATCCTG


 


GAGGTGGAGGCCTCTTGGATCCCCCTGGGCGGCACCCCCCCCGTGGCCC


 


CCCAGCGAACCATCGCCTACGGCGCCGCCGCCGGCATGGTGCACCCCGC


 


CTCTGGCTACTCTGTGGTGAACTCTATCTCTAAGGCCCCCCGAGTGGCC


 


ACCGCCATGGCCGAGGGCCTGAAGGAGGGCGGCGAGATCGAGGCCTCTC


 


GACGAGCCTGGGAGATCCTGTGGGGCGCCGAGCCCCGACGACAGATCGG


 


CTTCTACCAGTTCGGCATGGAGCTGCTGATGTCTCTGCGAATCGAGCAG


 


ATGCGAAACTTCTTCTCTACCTTCTTCGCCCTGCCCACCAACCTGTCTC


 


GAGGCTTCCTGGGCAACCGACTGTCTTCTTCTGAGCTGATCATGTTCGC


 


CCTGACCACCTTCGCCATCGGCAACAACGAGCTGCGAGGCCTGCTGCTG


 


GCCCACCTGGTGTCTTAAACGCGT






This fragment, liberated with XbaI and MluI, is cloned into NheI- and MluI-cleaved pMB5082 to produce pEpCyOs1.
A second putative lycopene epsilon cyclase from Ostreococcus lucimarinus CCE9901 is similarly codon-optimized and synthesized de novo:







(SEQ ID NO: 169)







TTCTAGAACAAAATGCGAGCCCGACGAGCCCCCGCCGCCCGAGTGACCC


 


GAGCCATCCGAGCCCGAGGCGACGCCGGCACCCGAGCCCGAGACGTGGC


 


CCCCGGCGCCACCCGACGAGGCGCCTCTGCCACCCCCCGAGCCACCCGA


 


CGACCCTCTGCCCGAGAGACCCGACCCGAGCTGTACGGCCTGGACGCCT


 


CTTGGGACCCCCTGACCTCTGGCGACCGACGAGAGTCTGAGGAGTCTCG


 


AACCCCCCTGCCCGAGACCCTGCCCAACGTGCGATGGGGCACCTCTGCC


 


TCTGAGGCCTACGACCTGGTGATCGTGGGCTGTGGCCCCGCCGGCCTGA


 


CCGCCGCCGACGAGGCCTCTAAGCGAGGCCTGCGAGTGGCCCTGATGGA


 


CCCCTCTCCCCTGGCCCCCTGGATGAACAACTACGGCGTGTGGTGTGAC


 


GAGTTCAAGTCTCTGGGCTTCGACGACTGTTACCGAGCCGTGTGGAACA


 


AGGCCCGAGTGATCATCGACGACGGCGACGCCGACGGCAAGATGCTGGA


 


CCGAGCCTACGCCCAGGTGGACCGAAAGAAGCTGAAGCAGAAGCTGATC


 


GCCCGATCTGTGACCCAGGGCGTGGAGTTCGGCATCGCCGCCGTGGACT


 


CTTGTGACAACTCTGACCCCAACCACTCTGTGGTGACCCTGTCTGACGG


 


CCGAAAGGTGTACGCCAAGATGGTGCTGGACGCCACCGGCCACTCTCGA


 


AAGCTGGTGGACTTCGACCGAGACTTCACCCCCGGCTACCAGGCCGCCT


 


TCGGCATCGTGTGTACCGTGGAGAAGCACGACTTCCCCCTGGACACCAT


 


GCTGTTCATGGACTGGCGAGACGAGCACCTGTCTCCCGAGTTCAAGCGA


 


GCCAACGACCGACTGCCCACCTTCCTGTACGCCATGCCCTTCTCTGAGA


 


CCGAGGTGTTCCTGGAGGAGACCTCTCTGGTGGCCCGACCCGGCCTGGA


 


GTTCGACGACCTGAAGCTGAAGCTGAAGGAGCGACTGGACTACCTGGGC


 


GTGAAGGTGACCAAGGTGCACGAGGAGGAGTACTGTCTGATCCCCATGG


 


GCGGCGTGCTGCCCACCTTCCCCCAGCGAACCCTGGGCATCGGCGGCAC


 


CGCCGGCATGGTGCACCCCTCTACCGGCTTCATGGTGGCCAAGACCATG


 


CTGTGTGTGCGAACCCTGGTGGGCACCCTGGACGAGGCCCTGAAGGCCG


 


GCAAGCGAGGCGACATCACCGGCGCCCTGGAGGCCGCCGAGGCCGCCCA


 


GATGAACAACGGCAAGTTCGACGCCGACGCCACCGCCGCCCTGGTGTGG


 


AACTCTATCTGGCCCGAGAACGACCTGCGAATGCGAACCTTCATGTGTT


 


TCGGCATGGAGACCCTGATGCAGCTGGACATCGACGGCACCCGACAGTT


 


CTTCGACACCTTCTTCGACCTGCCCAAGGACGTGTGGGCCGGCTTCCTG


 


TCTTGGCGAATCCAGCCCGTGGGCCTGCTGTCTCTGGGCGTGAACCTGT


 


TCGCCCTGTTCTCTAACTACATGCGAGTGAACTTCGTGAAGTCTGCCCT


 


GCCCTTCATGGGCTCTTTCTTCGCCAACTAAACGCGT






This fragment, liberated with XbaI and MluI, is cloned into NheI- and MluI-cleaved pMB5082 to produce pEpCyOs2.
The following sequence, optimized for Y. lipolytica codon bias and encoding a putative carotene epsilon hydroxylase from Ostreococcus tauri, is synthesized de novo:







(SEQ ID NO: 170)







TTCTAGAACAAAATGAAGGACGGCCAGGACGAGGACTCTGACGAGATCT


 


GGGGCGGCCAGCGACACGCCTCTGAGATGAAGACCCCCACCCGACGAAA


 


GGCCCGAACCAAGGCCGAGCGAGAGGCCTCTGCCGCCTCTTACGAGTGG


 


TCTGCCTGGGCCTCTTCTTGTGGCGTGATCTCTGTGGCCATCACCGCCA


 


CCTACTTCCGAATCCTGCGAGAGGTGGACGTGAACGGCGGCGTGTTCCC


 


CGTGGCCGAGCTGGTGGCCCAGCTGGCCCTGATCGCCGGCGCCGCCGTG


 


GGCATGGAGTTCTACGCCCGATACGCCCACAAGCACCTGTGGCACGGCT


 


CTTGGTGGACCATGTCTAACAAGTACCGACAGGAGTGGAACCGACCCAT


 


CTGGCTGCTGCACGAGTCTCACCACCTGCCCCGAGAGGGCGCCTTCGAG


 


GCCAACGACGTGTTCGCCCTGATGAACGGCGTGCCCGCCTTCGCCCTGT


 


GTGCCTTCGGCTTCTTCACCCCCGGCGTGTTCGGCGGCCTGTGTTTCGG


 


CGCCGGCCTGGGCATCACCCTGTTCGGCATCGCCTACATGTACGTGCAC


 


GACGGCCTGGTGCACAAGCGATTCCCCACCGGCCCCCTGGGCAAGCTGC


 


CCGTGATGCGACGAATCGCCGCCGGCCACACCATCCACCACACCGAGGC


 


CTTCGAGGGCGTGCCCTGGGGCCTGTTCCTGGGCATCCAGGAGCTGGCC


 


GCCGTGCCCGGCGGCCTGGAGGAGCTGGAGAAGGTGGTGATCGCCGCCG


 


AGCGAAAGGAGAAGCGAGACGAGCTGGAGCTGGCCCGACGAGCCTCTGT


 


GGGCCTGGTGACCGAGGGCGCCCACATCCCCTCTATGAAGGAGGCCCCC


 


CAGTGTAAGCTGCCCGAGGACCCCTAAACGCGT






This fragment, liberated with XbaI and MluI, is cloned into NheI- and MluI-cleaved pMB5082 to produce pEpHyOs1.
The 1.9 kb KpnI-SacI TEF1p-crtZ fragment from pMB4837 (example 1O) is cloned into KpnI- and SacI-cleaved pMB5082 to create pCrtZ-Ub.
A strain expressing carRP, carB, GGS, and HMG1trunc and auxotrophic for ura3 (MF946; example 2F) is transformed successively, in any order, with the URA3 plasmids pEpCyOs1 (or pEpCyOs2), pEpHyOs1, and pCrtZ-Ub, with the recycling of the ura3 marker between each step, as described in Example 15. Such a strain is expected to produce >1 mg/gDCW lutein. This strain may be further modified by transformation with pMB4789 (erg9[F317I]-3′UTR::URA3), as described in example 2H.
The following tables are referenced throughout the description. Each reference and information designated by each of the Genbank Accession and GI numbers are hereby incorporated by reference in their entirety. The order of genes, polypeptides and sequences presented in the tables is not indicative of their relative importance and/or suitability to any of the embodiments disclosed herein.







TABLE 1







Examples of acetyl-CoA carboxylase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION












XP_410263
49097606
hypothetical protein AN6126.2 [Aspergillus nidulans FGSC A4]


XP_329580
32418204
hypothetical protein [Neurospora crassa]


XP_386756
46124405
hypothetical protein FG06580.1 [Gibberella zeae PH-1]


XP_367702
39972623
hypothetical protein MG07613.4 [Magnaporthe grisea 70-15]


XP_501721
50548503
hypothetical protein [Yarrowia lipolytica]


EAK99708
46440402
hypothetical protein CaO19.7466 [Candida albicans SC5314]


XP_457211
50413128
unnamed protein product [Debaryomyces hansenii]


NP_982612
45184894
AAR071Wp [Eremothecium gossypii]


XP_449236
50293649
unnamed protein product [Candida glabrata]


NP_593271
19114183
acetyl-coa carboxylase [Schizosaccharomyces pombe]


NP_014413
6324343
Acclp [Saccharomyces cerevisiae]


XP_455355
50310667
unnamed protein product [Kluyveromyces lactis]


T42531
11272737
acetyl-CoA carboxylase (EC 6.4.1.2)—fission yeast




(Schizosaccharomyces pombe)


AAA20073
171504
acetyl-CoA carboxylase


EAL20176
50257469
hypothetical protein CNBF2520 [Cryptococcus neoformans var.




neoformans B-3501A]


XP_571316
58268320
acetyl-CoA carboxylase, putative [Cryptococcus neoformans var.




neoformans JEC21]


XP_402244
49076566
hypothetical protein UM04629.1 [Ustilago maydis 521]


S60200
2133343
acetyl-CoA carboxylase (EC 6.4.1.2)—smut fungus (Ustilago maydis)


BAA24410
2804173
acetyl-coenzyme A carboxylase like carboxylase [Saccharomyces




cerevisiae]


P32874
1708192
HFA1 protein


S55089
7438088
probable acetyl-CoA carboxylase (EC 6.4.1.2) HFA1—yeast




(Saccharomyces cerevisiae)


NP_990836
45382859
acetyl-Coenzyme A carboxylase alpha [Gallus gallus]


CAE01471
32526576
Acetyl-CoA carboxylase 2 [Homo sapiens]


AAR37018
40019048
acetyl-CoA carboxylase 2 [Homo sapiens]


NP_001 . . .
57164283
acetyl-CoA carboxylase [Ovis aries]


NP_776649
27806341
acetyl-coenzyme A carboxylase alpha [acetyl-coA carboxylase]




[Bos taurus]


CAI25271
56205878
acetyl-Coenzyme A carboxylase [Mus musculus]


XP_109883
51828611
PREDICTED: acetyl-Coenzyme A carboxylase [Mus musculus]


NP_942134
38679971
acetyl-Coenzyme A carboxylase alpha isoform 3 [Homo sapiens]


NP_942131
38679960
acetyl-Coenzyme A carboxylase alpha isoform 1 [Homo sapiens]


NP_942135
38679974
acetyl-Coenzyme A carboxylase alpha isoform 4 [Homo sapiens]


NP_942136
38679977
acetyl-Coenzyme A carboxylase alpha isoform 2 [Homo sapiens]


AAP94122
33112885
acetyl-CoA carboxylase 1 [Homo sapiens]


NP_071529
11559962
acetyl-coenzyme A carboxylase alpha [Rattus norvegicus]


2006242A
740964
Ac-CoA carboxylase


AAS13685
42405896
acetyl-CoA carboxylase 1 [Mus musculus]


NP_598665
48976025
acetyl-Coenzyme A carboxylase beta [Mus musculus]


Q13085
2493311
Acetyl-CoA carboxylase 1 (ACC-alpha) [Includes: Biotin carboxylase]


XP_548250
57091783
PREDICTED: similar to acetyl-CoA carboxylase [Canis familiaris]


XP_314071
58385597
ENSANGP00000015662 [Anopheles gambiae str. PEST]


CAG08536
47226520
unnamed protein product [Tetraodon nigroviridis]


NP_724636
24586460
CG11198-PB, isoform B [Drosophila melanogaster]


NP_610342
24586458
CG11198-PA, isoform A [Drosophila melanogaster]


NP_001084
4501855
acetyl-Coenzyme A carboxylase beta [Homo sapiens]


NP_446374
16758804
acetyl-Coenzyme A carboxylase beta [Rattus norvegicus]


EAL63219
60465120
acetyl-CoA carboxylase [Dictyostelium discoideum]


NP_921034
37533464
putative acetyl-CoA carboxylase [Oryza sativa (japonica cultivar-




group)]


T07084
7438099
acetyl-CoA carboxylase (EC 6.4.1.2) A—soybean


AAP78896
32264940
acetyl-coenzyme A carboxylase ACC1A [Zea mays]


AAO62903
29123370
acetyl-coenzyme A carboxylase [Setaria italica]


BAA07012
1100253
acetyl-CoA carboxylase [Arabidopsis thaliana]


AAL02056
15558947
acetyl-coenzyme A carboxylase [Setaria italica]


AAG40563
11869927
acetyl-CoA carboxylase 1 [Arabidopsis thaliana]


D86483
25293894
protein F5J5.19 [imported]—Arabidopsis thaliana


T07920
7438090
probable acetyl-CoA carboxylase (EC 6.4.1.2)—rape


A57710
2130099
acetyl-CoA carboxylase (EC 6.4.1.2)—wheat


AAO62902
29123376
acetyl-coenzyme A carboxylase [Setaria italica]


2208491A
1588584
Ac-CoA carboxylase


T09538
7438102
acetyl-CoA carboxylase (EC 6.4.1.2)—alfalfa


CAC19875
12057067
acetyl-CoA carboxylase [Brassica napus]


AAP78897
32264942
acetyl-coenzyme A carboxylase ACC1B [Zea mays]


T02235
7438095
acetyl-CoA carboxylase (EC 6.4.1.2)—maize


AAG40564
11869928
acetyl-CoA carboxylase 2 [Arabidopsis thaliana]


E86483
25293893
probable acetyl-CoA carboxylase, 9984-22276 [imported]—




Arabidopsis thaliana


CAC84161
20975574
acetyl-coenzyme A carboxylase [Alopecurus myosuroides]


T07081
7438097
acetyl-CoA carboxylase (EC 6.4.1.2) B—soybean (fragment)


CAC19876
12057069
acetyl-CoA carboxylase [Brassica napus]
















TABLE 2







Examples of pyruvate decarboxylase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION












1QPBB
7245977
Chain B, Pyruvate Decarboyxlase From Yeast (Form B) Complexed




With Pyruvamide


CAA54522
871533
pyruvate decarboxylase [Saccharomyces cerevisiae]


1PYDB
515237
Chain B, Pyruvate Decarboxylase (Pdc) (E.C.4.1.1.1)


CAA28380
4109
pyruvate decarboxylase [Saccharomyces cerevisiae]


1PVDB
1127233
Chain B, Pyruvate Decarboxylase (Pdc) (E.C.4.1.1.1)


CAA33709
4114
unnamed protein product [Saccharomyces cerevisiae]


AAN77243
25992752
pyruvate decarboxylase [Candida glabrata]


NP_013235
6323163
Minor isoform of pyruvate decarboxylase, key enzyme in alcoholic




fermentation [Saccharomyces cerevisiae]


Q6FJA3
57012668
Pyruvate decarboxylase


S36363
486942
pyruvate decarboxylase (EC 4.1.1.1)—yeast 




(Kluyveromyces marxianus)


Q12629
52788279
Pyruvate decarboxylase


AAP75898
37359468
pyruvate decarboxylase [Saccharomyces kluyveri]


S70684
2131152
pyruvate decarboxylase (EC 4.1.1.1)—yeast 




(Kluyveromyces marxianus var. lactis)


NP_011601
6321524
Minor isoform of pyruvate decarboxylase, key enzyme in alcoholic




fermentation [Saccharomyces cerevisiae]


AAQ73618
34500072
pyruvate decarboxylase [Saccharomyces kluyveri]


NP_983270
45185554
ACL134Cp [Eremothecium gossypii]


AAF78895
8745337
putative pyruvate decarboxylase [Saccharomyces kluyveri]


CAB65554
6689662
putative pyruvate decarboxylase [Zygosaccharomyces bisporus]


AAP75899
37359470
pyruvate decarboxylase [Saccharomyces kluyveri]


NP_982469
45184751
AAL073Wp [Eremothecium gossypii]


CAA97091
1945321
PDC6 [Saccharomyces cerevisiae]


S50700
1086157
pyruvate decarboxylase (EC 4.1.1.1)—yeast (Hanseniaspora uvarum)


XP_446491
50288125
unnamed protein product [Candida glabrata]


XP_462338
50427451
unnamed protein product [Debaryomyces hansenii]


AAC03164
17066784
pyruvate decarboxylase 1 [Pichia stipitis]


EAK96569
46437219
hypothetical protein CaO19.10395 [Candida albicans SC5314]


XP_457131
50412425
unnamed protein product [Debaryomyces hansenii]


AAC03165
2734883
pyruvate decarboxylase 2 [Pichia stipitis]


XP_459224
50421349
unnamed protein product [Debaryomyces hansenii]


CAH56494
52673248
pyruvate decarboxylase [Pichia anomala]


XP_502647
50550349
hypothetical protein [Yarrowia lipolytica]


NP_010203
6320123
Probable decarboxylase, [Saccharomyces cerevisiae]


BAA04886
1786148
THI3 regulatory protein [Saccharomyces cerevisiae]


XP_449074
50293325
unnamed protein product [Candida glabrata]


EAL04098
46444826
hypothetical protein CaO19.12078 [Candida albicans SC5314]


CAD60727
27803024
unnamed protein product [Podospora anserina]


T38759
25777585
probable pyruvate decarboxylase (EC 4.1.1.1)—fission yeast




(Schizosaccharomyces pombe)


XP_331173
32421459
hypothetical protein [Neurospora crassa]


NP_594083
19114995
pyruvate decarboxylase [Schizosaccharomyces pombe]


XP_401609
49075036
hypothetical protein UM03994.1 [Ustilago maydis 521]


XP_390010
46136637
hypothetical protein FG09834.1 [Gibberella zeae PH-1]


XP_409025
49095128
DCPY_EMENI Pyruvate decarboxylase [Aspergillus nidulans




FGSC A4]


NP_984350
45188127
ADR254Wp [Eremothecium gossypii]


AAD16178
4323053
pyruvate decarboxylase [Aspergillus oryzae]


P87208
2501326
Pyruvate decarboxylase


EAL18331
50255598
hypothetical protein CNBJ2540 [Cryptococcus neoformans var.




neoformans B-3501A]


XP_567475 
58260130
pyruvate decarboxylase, putative [Cryptococcus neoformans var.




neoformans JEC21]


AAM73540
21666011
pyruvate decarboxylase PdcB [Rhizopus oryzae]


AAM73539
21666009
pyruvate decarboxylase PdcA [Rhizopus oryzae]


XP_502508 
50550071
hypothetical protein [Yarrowia lipolytica]


CAA93158
1177659
SPAC3H8.01 [Schizosaccharomyces pombe]


XP_412533 
49123327
hypothetical protein AN8396.2 [Aspergillus nidulans FGSC A4]


P51844
1706333
Pyruvate decarboxylase


XP_455842
50311631
unnamed protein product [Kluyveromyces lactis]


CAA61155
3688422
pyruvate decarboxylase [Kluyveromyces lactis]


XP_444902
50284947
unnamed protein product [Candida glabrata]


CAA47319
4118 
pyruvate decarboxylase [Saccharomyces cerevisiae]
















TABLE 3







Examples of isocitrate dehydrogenase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION












O13285
3023996
Isocitrate dehydrogenase [NADP], mitochondrial precursor (IDH)




(NADP+-specific ICDH) (IDP) (CtIDP1)


EAK91676
46432179
hypothetical protein CaO19.5211 [Candida albicans SC5314]


O13285
3023996
Isocitrate dehydrogenase [NADP], mitochondrial precursor (IDH)




(NADP+-specific ICDH) (IDP) (CtIDP1)


EAK94305
46434909
hypothetical protein CaO19.3733 [Candida albicans SC5314]


XP_451683
50303483
unnamed protein product [Kluyveromyces lactis]


XP_459772
50422415
unnamed protein product [Debaryomyces hansenii]


O13294
27805482
Isocitrate dehydrogenase [NADP] peroxisomal (Oxalosuccinate




decarboxylase) (IDH) (PS-NADP-IDH) (CtIDP2)


XP_460289
50423413
unnamed protein product [Debaryomyces hansenii]


XP_390523
46137663
hypothetical protein FG10347.1 [Gibberella zeae PH-1]


XP_367343
39971905
hypothetical protein MG07268.4 [Magnaporthe grisea 70-15]


XP_323176
32405126
hypothetical protein [Neurospora crassa]


XP_445447
50286037
unnamed protein product [Candida glabrata]


AAK76730
15027826
mitochondrial NADP-dependent isocitrate dehydrogenase




[Aspergillu snidulans]


NP_010217
6320137
Idp1p [Saccharomyces cerevisiae]


NP_984921
45190667
AER061Cp [Eremothecium gossypii]


AAK76731
15027827
peroxisomal NADP-dependent isocitrate dehydrogenase [Aspergillus




nidulans]


P79089
3023999
Isocitrate dehydrogenase [NADP], mitochondrial precursor (IDH)




(NADP+-specific ICDH) (IDP)


NP_013275
6323203
Cytosolic NADP-specific isocitrate dehydrogenase [Saccharomyces




cerevisiae]


XP_407136
49091350
IDHP_ASPNG ISOCITRATE DEHYDROGENASE [NADP],




MITOCHONDRIAL PRECURSOR (IDP) [Aspergillus nidulans




FGSC A4]


NP_982520
45184802
AAL022Wp [Eremothecium gossypii]


XP_446953
50289047
unnamed protein product [Candida glabrata]


XP_445184
50285511
unnamed protein product [Candida glabrata]


XP_455638
50311227
unnamed protein product [Kluyveromyces lactis]


AAA64516
736722
isocitrate dehydrogenase


NP_970434
42525054
isocitrate dehydrogenase (NADP) [Bdellovibrio bacteriovorus HD100]


AAT93173
51013759
YNL009W [Saccharomyces cerevisiae]


XP_569233
58264154
isocitrate dehydrogenase (NADP+), putative [Cryptococcus




neoformans var. neoformans JEC21]


XP_569234
58264156
isocitrate dehydrogenase (NADP+), putative [Cryptococcus




neoformans var. neoformans JEC21]


XP_403726
49080406
hypothetical protein UM06111.1 [Ustilago maydis 521]


XP_503571
50552322



XP_458151
50428131
unnamed protein product [Debaryomyces hansenii]


O13302
13124301
Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial precursor




(NAD+-specific ICDH)


XP_409927
49096934
IDH1_AJECA Isocitrate dehydrogenase [NAD] subunit 1,




mitochondrial precursor [Aspergillus nidulans FGSC A4]


XP_385909
46122711
IDH1_AJECA Isocitrate dehydrogenase [NAD] subunit 1,




mitochondrial precursor [Gibberella zeae PH-1]


XP_365293
39967489
hypothetical protein MG01995.4 [Magnaporthe grisea 70-15]


NP_983873
45187650
ADL223Wp [Eremothecium gossypii]


XP_455266
50310493
IDH1_KLULA [Kluyveromyces lactis]


NP_594397
19115309
putative isocitrate dehydrogenase (EC 1.1.1.41) [Schizosaccharomyces




pombe]


XP_324955 
32408949
hypothetical protein [Neurospora crassa]


CAE81942
38636405
probable isocitrate dehydrogenase [NAD] subunit 1, mitochondrial




precursor [Neurospora crassa]


NP_014361
6324291
Idh1p [Saccharomyces cerevisiae]


XP_446479
50288101
unnamed protein product [Candida glabrata]


XP_567378
58259936
isocitrate dehydrogenase (NAD+), putative [Cryptococcus neoformans




var. neoformans JEC21]


XP_398944 
49069310
hypothetical protein UM01329.1 [Ustilago maydis 521]


XP_502479 
50550013
hypothetical protein [Yarrowia lipolytica]


EAK96238
46436883
hypothetical protein CaO19.13213 [Candida albicans SC5314]


EAK96305
46436951
hypothetical protein CaO19.5791 [Candida albicans SC5314]


XP_461797
50426401
unnamed protein product [Debaryomyces hansenii]


XP_328403 
32415850
hypothetical protein [Neurospora crassa]


CAF31997
42820684
isocitrate dehydrogenase, putative [Aspergillus fumigatus]


XP_389756 
46136129
hypothetical protein FG09580.1 [Gibberella zeae PH-1]


XP_363786
39952139
hypothetical protein MG01712.4 [Magnaporthe grisea 70-15]


AAL73035
18463935
isocitrate dehydrogenase [Coccidioides immitis]


XP_405140 
49086142
hypothetical protein AN1003.2 [Aspergillus nidulans FGSC A4]


NP_595203
19111995
probable isocitrate dehydrogenase [nad] subunit 2, mitochondrial




precursor [Schizosaccharomyces pombe]


NP_014779
6324709
Idh2p [Saccharomyces cerevisiae]


XP_447564
50290265
unnamed protein product [Candida glabrata]


NP_985684 
45198655
AFR137Cp [Eremothecium gossypii]


XP_566837
58258849
isocitrate dehydrogenase, putative [Cryptococcus neoformans var.




neoformans JEC21]


XP_454086 
50308171
IDH2_KLULA [Kluyveromyces lactis]


XP_398943
49069308
hypothetical protein UM01328.1 [Ustilago maydis 521]
















TABLE 4







Examples of ATP-citrate lyase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION












XP_327071
32413182
hypothetical protein [Neurospora crassa]


O93988
30912679
ATP-citrate synthase subunit 1 (ATP-citrate (pro-S-)-lyase 1) (Citrate




cleavage enzyme subunit 1)


XP_370222
39977669
hypothetical protein MG06719.4 [Magnaporthe grisea 70-15]


XP_406573
49090008
ACL1_NEUCR Probable ATP-citrate synthase subunit 1 [Aspergillus




nidulans FGSC A4]


XP_504787
50554757
hypothetical protein [Yarrowia lipolytica]


Q9P7W3
30912748
Probable ATP-citrate synthase subunit 1 (ATP-citrate (pro-S-)-lyase 1)




(Citrate cleavage enzyme subunit 1)


XP_398620
49068662
hypothetical protein UM01005.1 [Ustilago maydis 521]


NP_596202
19112994
probable ATP citrate lyase [Schizosaccharomyces pombe]


XP_567460
58260100
conserved hypothetical protein [Cryptococcus neoformans var.




neoformans JEC21]


NP_001008
56118260
acly-prov protein [Xenopus tropicalis]


XP_418154
50760837
PREDICTED: similar to ATP citrate lyase [Gallus gallus]


AAH84253
54038148
LOC495086 protein [Xenopus laevis]


NP_942127
38569423
ATP citrate lyase isoform 2 [Homo sapiens]


NP_001087
38569421
ATP citrate lyase isoform 1 [Homo sapiens]


P53396
20141248
ATP-citrate synthase (ATP-citrate (pro-S-)-lyase) (Citrate cleavage




enzyme)


AAL34316
17028103
ATP-citrate lyase [Rattus norvegicus]


NP_001002
50540366
zgc:92008 [Danio rerio]


AAH84776
54311201
LOC495316 protein [Xenopus laevis]


S21173
105392
ATP citrate (pro-S)-lyase—human


AAT94429
51092031
RE70805p [Drosophila melanogaster]


AAD34754
28372804
LD21334p [Drosophila melanogaster]


AAH21502
18204829
Acly protein [Mus musculus]


XP_319323
58392375
ENSANGP00000012364 [Anopheles gambiae str. PEST]


NP_725514
24653990
CG8322-PB, isoform B [Drosophila melanogaster]


EAL26601
54637198
GA20986-PA [Drosohilia pseudoobscura]


CAE56725
39579419
Hypothetical protein CBG24512 [Caenorhabditis briggsae]


CAE64663
39593194
Hypothetical protein CBG09435 [Caenorhabditis briggsae]


XP_511495
55645405
PREDICTED: similar to ATP citrate lyase isoform 1 [Pan troglodytes]


CAF95829
47210997
unnamed protein product [Tetraodon nigroviridis]


AAO22565
27754223
putative ATP citrate lyase [Arabidopsis thaliana]


AAL33788
17065616
putative ATP citrate lyase [Arabidopsis thaliana]


CAB46077
5304837
ATP citrate lyase [Cyanophora paradoxa]


CAF96044
47204726
unnamed protein product [Tetraodon nigroviridis]


AAK13318
13160653
ATP: citrate lyase [Capsicum annuum]


AAQ75159
34558815
citrate lyase subunit 2 [Alvinella pompejana epibiont 7G3]


AAQ75128
34558783
citrate lyase subunit 2 [Alvinella pompejana epibiont 6C6]


XP_537640
57091075
PREDICTED: similar to ATP citrate lyase isoform 2 [Canis familiaris]


XP_327069
32413178
hypothetical protein ( (AJ243817) ATP citrate lyase, subunit 2 




[Sordaria macrospora]) [Neurospora crassa]


CAB76164
7160184
ATP citrate lyase, subunit 2 [Sordaria macrospora]


XP_370223
39977671
hypothetical protein MG06720.4 [Magnaporthe grisea 70-15]


XP_386215
46123323
hypothetical protein FG06039.1 [Gibberella zeae PH-1]


CAA10666
7159697
ATP-citrat-lyase [Gibberella pulicaris]


XP_406572
49090004
conserved hypothetical protein [Aspergillus nidulans FGSC A4]


XP_503231
50551515
hypothetical protein [Yarrowia lipolytica]


NP_593246
19114158
putative ATP-citrate (pro-S-) lyase (EC 4.1.3.8) [Schizosaccharomyces




pombe]


XP_398620 
49068662
hypothetical protein UM01005.1 [Ustilago maydis 521]


XP_567460 
58260100
conserved hypothetical protein [Cryptococcus neoformans var.




neoformans JEC21]


AAT94429
51092031
RE70805p [Drosophila melanogaster]


NP_725514 
24653990
CG8322-PB, isoform B [Drosophila melanogaster]


AAD34754
28372804
LD21334p [Drosophila melanogaster]


EAL26601
54637198
GA20986-PA [Drosophila pseudoobscura]


XP_319323 
58392375
ENSANGP00000012364 [Anopheles gambiae str. PEST]


AAH84776
54311201
LOC495316 protein [Xenopus laevis]


BAB00624
9229902
ATP citrate-lyase [Ciona intestinalis]


NP_001008 
56118260
acly-prov protein [Xenopus tropicalis]


AAH84253
54038148
LOC495086 protein [Xenopus laevis]


AAH56378
38614162
ATP citrate lyase [Mus musculus]


NP_001087
38569421
ATP citrate lyase isoform 1 [Homo sapiens]


NP_942127
38569423
ATP citrate lyase isoform 2 [Homo sapiens]


P53396
20141248
ATP-citrate synthase (ATP-citrate (pro-S-)-lyase) (Citrate cleavage




enzyme)


XP_511495
55645405
PREDICTED: similar to ATP citrate lyase isoform 1 [Pan troglodytes]


NP_058683
8392839
ATP citrate lyase [Rattus norvegicus]


NP_001002
50540366
zgc: 92008 [Danio rerio]


S21173
105392
ATP citrate (pro-S)-lyase—human


NP_508280 
17551266
atp citrate lyase (XC101) [Caenorhabditis elegans]


CAE64663
39593194
Hypothetical protein CBG09435 [Caenorhabditis briggsae]


CAE56725
39579419
Hypothetical protein CBG24512 [Caenorhabditis briggsae]


NP_506267 
17557344
ATP citrate lyase (120.6 kD) (5N599) [Caenorhabditis elegans]


XP_537640
57091075
PREDICTED: similar to ATP citrate lyase isoform 2 [Canis familiaris]


CAF96059
47204551
unnamed protein product [Tetraodon nigroviridis]


F96633
25404292
hypothetical protein F8A5.32 [imported]—Arabidopsis thaliana


AAM91141
22136126
similar to ATP-citrate-lyase [Arabidopsis thaliana]


NP_849634 
30681854
expressed protein [Arabidopsis thaliana]


AAO23582
27764922
At1g09430/F19J9_9 [Arabidopsis thaliana]


AAM65078
21593129
ATP citrate-lyase, putative [Arabidopsis thaliana]


CAC86996
15919089
ATP citrate lyase b-subunit [Lupinus albus]


AAQ75158
34558814
citrate lyase subunit 1 [Alvinella pompejana epibiont 7G3]


AAQ75127
34558782
citrate lyase subunit 1 [Alvinella pompejana epibiont 6C6]
















TABLE 5







Examples of malic enzyme polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





NP_012896
6322823
Mae1p [Saccharomyces cerevisiae]


XP_448858
50292851
unnamed protein product [Candida glabrata]


XP_454793
50309563
unnamed protein product [Kluyveromyces lactis]


NP_986598
45201028
AGL068Wp [Eremothecium gossypii]


XP_460887
50424595
unnamed protein product [Debaryomyces hansenii]


EAK97738
46438407
hypothetical protein CaO19.3419 [Candida albicans SC5314]


XP_504112
50553402
hypothetical protein [Yarrowia lipolytica]


XP_330094
32419237
hypothetical protein [Neurospora crassa]


XP_380981
46107844
hypothetical protein FG00805.1 [Gibberella zeae PH-1]


XP_411070
49102552
hypothetical protein AN6933.2 [Aspergillus nidulans FGSC A4]


XP_362875
39946676
hypothetical protein MG08562.4 [Magnaporthe grisea 70-15]


NP_587760
19075260
malate oxidoreductase [nad] [Schizosaccharomyces pombe]


NP_978189
42780942
malate oxidoreductase [Bacillus cereus ATCC 10987]


YP_035982
49481098
NAD-dependent malic enzyme [Bacillus thuringiensis serovar




konkukian str. 97-27]


YP_027934
49184682
malate oxidoreductase [Bacillus anthracis str. Sterne]


YP_018438
47527089
malate oxidoreductase [Bacillus anthracis str. ‘Ames Ancestor’]


ZP_002365
47565532
malate oxidoreductase VC1188 [Bacillus cereus G9241]


YP_083209
52143619
NAD-dependent malic enzyme [Bacillus cereus ZK]


XP_571672
58269032
malate dehydrogenase, putative [Cryptococcus neoformans var.




neoformans JEC21]


NP_391586
16080758
hypothetical protein BSU37050 [Bacillus subtilis subsp. subtilis str.




168]


YP_092693
52786864
MalS [Bacillus licheniformis ATCC 14580]


NP_831516
30019885
NAD-dependent malic enzyme [Bacillus cereus ATCC 14579]


YP_093460
52787631
YwkA [Bacillus licheniformis ATCC 14580]


YP_081030
52082239
Malic oxidoreductase [Bacillus licheniformis ATCC 14580]


NP_822689
29828055
putative malate dehydrogenase [Streptomyces avermitilis MA-4680]


O34389
33517449
Probable NAD-dependent malic enzyme 3 (NAD-ME 3)


EAL19111
50256386
hypothetical protein CNBH2110 [Cryptococcus neoformans var.




neoformans B-3501A]


NP_825047
29830413
putative malate dehydrogenase [Streptomyces avermitilis MA-4680]


ZP_002340
47096498
NADP-dependent malic enzyme [Listeria monocytogenes str. 1/2a




F6854]


NP_928837
37525493
malate dehydrogenase (oxaloacetate-decarboxylating) [Photorhabdus




luminescens subsp. laumondii TTO1]


NP_230833
15641201
malate oxidoreductase [Vibrio cholerae O1 biovar eltor str. N16961]


NP_934257
37679648
malic enzyme [Vibrio vulnificus YJ016]


NP_761613
27366085
Malic enzyme [Vibrio vulnificus CMCP6]


AC1314
25283688
malolactic enzyme (malate dehydrogenase) homolog lmo1915 - Listeria




monocytogenes (strain EGD-e)


YP_055602
50842375
NAD-dependent malic enzyme [Propionibacterium acnes KPA171202]


YP_095310
52841511
malate oxidoreductase [Legionella pneumophila subsp. pneumophila




str. Philadelphia 1]


ZP_002315
47093832
NADP-dependent malic enzyme [Listeria monocytogenes str. 4b




H7858]


AC1686
25283689
malolactic enzyme (malate dehydrogenase) homolog lin2029




[imported] - Listeria innocua (strain Clip11262)


YP_126594
54294179
malate oxidoreductase [Legionella pneumophila str. Lens]


YP_123567
54297198
malate oxidoreductase [Legionella pneumophila str. Paris]


EAJ76260
44510091
unknown [environmental sequence]


YP_114273
53803890
malate oxidoreductase [Methylococcus capsulatus str. Bath]


NP_797637
28898032
malate oxidoreductase [Vibrio parahaemolyticus RIMD 2210633]


YP_040250
49483026
putative malolactic enzyme [Staphylococcus aureus subsp. aureus




MRSA252]


ZP_001276
53693400
COG0281: Malic enzyme [Pseudomonas syringae pv. syringae B728a]


YP_044961
50083451
NAD-linked malate dehydrogenase, Rossman fold [Acinetobacter sp.




ADP1]


YP_128226
54295811
hypothetical protein lpl2901 [Legionella pneumophila str. Lens]


NP_719387
24375344
malate oxidoreductase [Shewanella oneidensis MR-1]


XP_572853
58271394
nad-dependent malic enzyme, putative [Cryptococcus neoformans var.




neoformans JEC21]


NP_252161
15598667
probable malic enzyme [Pseudomonas aeruginosa PAO1]


ZP_001368
46164263
COG0281: Malic enzyme [Pseudomonas aeruginosa UCBPP-PA14]


YP_125345
54298976
hypothetical protein lpp3043 [Legionella pneumophila str. Paris]


NP_793695
28871076
malate dehydrogenase [Pseudomonas syringae pv. tomato str. DC3000]


YP_096964
52843165
malate dehydrogenase (NAD-linked) [Legionella pneumophila subsp.




pneumophila str. Philadelphia 1]


EAH92280
44245125
unknown [environmental sequence]


YP_154988
56459707
Malic enzyme [Idiomarina loihiensis L2TR]


EAI68195
44354928
unknown [environmental sequence]


YP_070054
51595863
NAD-dependent malic enzyme [Yersinia pseudotuberculosis IP 32953]


YP_133025
54303032
putative malate oxidoreductase [Photobacterium profundum SS9]


NP_969623
42524243
NAD-dependent malic enzyme [Bdellovibrio bacteriovorus HD100]


NP_856009
31793516
PROBABLE [NAD] DEPENDENT MALATE OXIDOREDUCTASE




MEZ (MALIC ENZYME) (NAD-MALIC ENZYME) (MALATE




DEHYDROGENASE TATE


DECARBOXY
ATING))
PYRUVIC-MALIC CARBOXYLASE) (NAD-ME) [Mycobacterium




bovis AF2122/97]


NP_935035
37680426
malic enzyme [Vibrio vulnificus YJ016]


YP_050922
50121755
NAD-dependent malic enzyme [Erwinia carotovora subsp. atroseptica




SCRI1043]


E70705
7431223
probable malate oxidoreductase - Mycobacterium tuberculosis (strain




H37RV)


NP_216848
57116971
PROBABLE [NAD] DEPENDENT MALATE OXIDOREDUCTASE




MEZ (MALIC ENZYME) (NAD-MALIC ENZYME) (MALATE




DEHYDROGENASE TATE


DECARBOXY
ATING))
PYRUVIC-MALIC CARBOXYLASE) (NAD-ME) [Mycobacterium




tuberculosis H37Rv]


YP_143786
55980489
NAD-dependent malic enzyme (malate dehydrogenase) [Thermus




thermophilus HB8]


YP_130202
54309182
putative malate oxidoreductase [Photobacterium profundum SS9]


NP_415996
16129438
NAD-linked malate dehydrogenase [Escherichia coli K12]


NP_819843
29654151
malate oxidoreductase [Coxiella burnetii RSA 493]


NP_753809
26247769
NAD-dependent malic enzyme [Escherichia coli CFT073]


NP_707611
56479957
NAD-linked malate dehydrogenase (malic enzyme) [Shigella flexneri




2a str. 301]


F85728
25283682
NAD-linked malate dehydrogenase (malic enzyme) - Escherichia coli




(strain O157:H7, substrain EDL933)


YP_163690
56552851
malic enzyme [Zymomonas mobilis subsp. mobilis ZM4]


YP_150562
56413487
NAD-linked malic enzyme [Salmonella enterica subsp. enterica serovar




Paratypi A str. ATCC 9150]


NP_720610
24378655
malolactic enzyme [Streptococcus mutans UA159]


NP_460525
16764910
NAD-linked malate dehydrogenase [Salmonella typhimurium LT2]


ZP_003193
48865537
COG0281: Malic enzyme [Oenococcus oeni PSU-1]


NP_784797
28377905
malolactic enzyme [Lactobacillus plantarum WCFS1]


T13496
7431227
malolactic enzyme (EC 1.1.1.—) - Leuconostoc oenos


AAV65766
55793550
malolactic enzyme [Oenococcus oeni]


A97096
25283683
malic enzyme [imported] - Clostridium acetobutylicum


YP_193951
58337366
malolactic enzyme [Lactobacillus acidophilus NCFM]


H97096
25283684
malic enzyme [imported] - Clostridium acetobutylicum


ZP_003237
48870993
COG0281: Malic enzyme [Pediococcus pentosaceus ATCC 25745]


ZP_001460
41689468
COG0281: Malic enzyme [Psychrobacter sp. 273-4]


D86737
25283676
malolactic enzyme [imported] - Lactococcus lactis subsp. lactis (strain




IL1403)


ZP_002870
48825851
COG0281: Malic enzyme [Enterococcus faecium]


ZP_001439
34762975
Malolactic enzyme [Fusobacterium nucleatum subsp. vincentii ATCC




49256]


1922245A
737262
malolactic enzyme


YP_169914
56708018
NAD-dependent malic enzyme [Francisella tularensis subsp. tularensis




Schu 4]


YP_055027
50841800
putative malate oxidoreductase [Propionibacterium acnes KPA171202]


ZP_000625
23023297
COG0281: Malic enzyme [Leuconostoc mesenteroides subsp.




mesenteroides ATCC 8293]


NP_296302
15807565
malate oxidoreductase [Deinococcus radiodurans R1]


NP_285599
15807938
malate oxidoreductase [Deinococcus radiodurans R1]


YP_132069
54302076
hypothetical malate oxidoreductase [Photobacterium profundum SS9]


CAA50716
467569
malolactic enzyme [Lactococcus lactis]


ZP_002906
48833596
COG0281: Malic enzyme [Magnetococcus sp. MC-1]


ZP_003155
48861632
COG0281: Malic enzyme [Microbulbifer degradans 2-40]


NP_773109
27381580
malic enzyme [Bradyrhizobium japonicum USDA 110]


AAQ95658
37622953
malic enzyme [Dictyostelium discoideum]


CAC19505
56204311
malic enzyme 1, NADP(+)-dependent, cytosolic [Homo sapiens]


AAH80660
51873855
Mod1 protein [Mus musculus]


P40927
729986
NADP-dependent malic enzyme (NADP-ME)


AAT02533
46850200
NADP-dependent malic enzyme 1 [Hydrilla verticillata]


BAC37086
26346875
unnamed protein product [Mus musculus]


T02763
7431235
probable malate dehydrogenase (oxaloacetate-decarboxylating)




(NADP) (EC 1.1.1.40) - maize


XP_387367
46125627
hypothetical protein FG07191.1 [Gibberella zeae PH-1]


AAC50613
1465733
cytosolic NADP(+)-dependent malic enzyme


CAA39421
669118
sbcA8 recE fusion [Escherichia coli]


CAA39420
669117
sbcA8 recE fusion [Escherichia coli]


NP_032641
6678912
malic enzyme, supernatant [Mus musculus]


CAA39419
581228
sbcA8 recE fusion [Escherichia coli]


AAB01380
1335389
NADP-dependent malic enzyme


JC4160
1085347
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC




1.1.1.40) - human


E96828
25283677
probable malate oxidoreductase, 93001-96525 [imported] - Arabidopsis




thaliana


BAD87910
57899974
cytosolic NADP malic enzyme [Oryza sativa (japonica cultivar-group)]


EAJ77083
44511304
unknown [environmental sequence]


P13697
266504
NADP-dependent malic enzyme (NADP-ME) (Malic enzyme 1)


NP_036732
7106353
malic enzyme 1 [Rattus norvegicus]


YP_065939
51246055
related to NAD-dependent malic enzyme [Desulfotalea psychrophila




LSv54]


CAC18164
16944467
related to malate dehydrogenase (oxaloacetate-decarboxylating)




(NADP+) [Neurospora crassa]


XP_322953
32404680
hypothetical protein [Neurospora crassa]


AAK91502
18460985
NADP-dependent malic enzyme [Zea mays]


AAQ88396
37147841
non-photosynthetic NADP-malic enzyme [Zea mays]


NP_001003
57525624
zgc:100941 [Danio rerio]


1GQ2P
21465488
Chain P, Malic Enzyme From Pigeon Liver


AAO26053
28195290
malic enzyme [Mucor circinelloides]


AAH84250
54038006
Me2 protein [Xenopus laevis]


XP_362590
39946106
hypothetical protein MG08173.4 [Magnaporthe grisea 70-15]


AAH03287
13096987
Mod1 protein [Mus musculus]


Q29558
2497785
NADP-dependent malic enzyme (NADP-ME) (Malic enzyme 1)


XP_532217
57094622
PREDICTED: similar to malate dehydrogenase decarboxylase




(NADP+) [Canis familiaris]


P28227
126734
NADP-dependent malic enzyme (NADP-ME)


NP_496968
17537199
malic enzyme nadp-dependent (2O518) [Caenorhabditis elegans]


NP_914533
34906372
unnamed protein product [Oryza sativa (japonica cultivar-group)]


AAD10504
4096786
NADP-malic enzyme [Zea mays]


AAO67523
50897495
mitochondrial malic enzyme 2 [Xenopus laevis]


P43279
1170871
NADP-dependent malic enzyme, chloroplast precursor (NADP-ME)


AAK83074
15077109
putative cytosolic NADP-malic enzyme [Flaveria pringlei]


AAP33011
30575690
NADP-malic enzyme [Zea mays]


AAN86690
27357017
malic enzyme [Mastigamoeba balamuthi]


P78715
41017288
Malic enzyme, hydrogenosomal precursor (ME)


AAP32204
30526303
NADP-dependent malic enzyme [Sorghum bicolor]


AAV31249
54287505
NADP malic enzyme [Oryza sativa (japonica cultivar-group)]


T06402
7431232
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC




1.1.1.40) 2, cytosolic - tomato


Q99KE1
55583978
NAD-dependent malic enzyme, mitochondrial precursor (NAD-ME)




(Malic enzyme 2)


XP_399922
49071266
hypothetical protein UM02307.1 [Ustilago maydis 521]


P36444
547886
NADP-dependent malic enzyme, chloroplast precursor (NADP-ME)


AAO30034
28059162
malate oxidoreductase (malic enzyme) [Arabidopsis thaliana]


AAK83073
15077107
putative cytosolic NADP-malic enzyme [Flaveria pringlei]


NP_002387
4505145
malic enzyme 2, NAD(+)-dependent, mitochondrial [Homo sapiens]


AAA33487
168528
NADP-dependent malic enzyme (EC 1.1.1.40)


BAA74735
4239891
NADP-malic enzyme [Aloe arborescens]


NP_989634
45383538
malic enzyme 1, NADP(+)-dependent, cytosolic [Gallus gallus]


1GZ3D
31615316
Chain D, The Regulation Of Human Mitochondrial Nad(P)+-




Dependent Malic Enzyme By Atp And Fumarate


AAW56450
57791240
chloroplast NADP-dependent malic enzyme precursor [Flaveria




bidentis]


AAT02534
46850202
NADP-dependent malic enzyme 2 [Hydrilla verticillata]


S29742
422339
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC




1.1.1.40) - pig roundworm


1O0SB
34811253
Chain B, Crystal Structure Of Ascaris Suum Malic Enzyme Complexed




With Nadh


P27443
126732
NAD-dependent malic enzyme, mitochondrial precursor (NAD-ME)


T06401
7431231
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC




1.1.1.40) precursor - tomato


AAL16175
16226466
AT5g11670/T22P22_60 [Arabidopsis thaliana]


AAF73006
8118507
NADP-dependent malic protein [Ricinus communis]


AAK97530
15420975
malic enzyme [Meleagris gallopavo]


EAI90348
44385841
unknown [environmental sequence]


P51615
1708924
NADP-DEPENDENT MALIC ENZYME (NADP-ME)


AAA19575
169327
NADP-dependent malic enzyme


S43718
1084300
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC




1.1.1.40) - common ice plant


P34105
1346485
NADP-DEPENDENT MALIC ENZYME (NADP-ME)


AAS38597
42733630
similar to Mastigamoeba balamuthi Malic enzyme (EC 1.1.1.38)




[Dictyostelium discoideum]


BAC54101
27530932
cytosolic NADP-malic enzyme [Lithospermum erythrorhizon]


AAT02535
46850204
NADP-dependent malic enzyme 3 [Hydrilla verticillata]


CAB66003
6706333
NADP-dependent malate dehydrogenase (decarboxylating) [Apium




graveolens]


AAH84860
54311418
LOC495390 protein [Xenopus laevis]


CAA39422
669119
sbcA8 recE fusion [Escherichia coli]


NP_916713
34910732
P0022F10.12 [Oryza sativa (japonica cultivar-group)]


CAA56354
510876
NADP dependent malic enzyme [Phaseolus vulgaris]


DEFBC
7427668
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC




1.1.1.40) - kidney bean


JC5967
7431234
malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC




1.1.1.40) - aloe


NP_197960
15239517
malate oxidoreductase, putative [Arabidopsis thaliana]


NP_651959
21356279
CG5889-PA [Drosophila melanogaster]


CAB64263
6634090
malate dehydrogenase (NADP-dependent oxaloacetate




decarboxylating), malic enzyme [Drosophila melanogaster]


BAB20887
54606800
NADP dependent malic enzyme [Oryza sativa (japonica cultivar-




group)]


EAL27424
54638022
GA19206-PA [Drosophila pseudoobscura]


NP_006671
5729920
malic enzyme 3, NADP(+)-dependent, mitochondrial [Homo sapiens]


AAB08874
1561774
malate dehydrogenase [Vitis vinifera]


1PJLH
33358128
Chain H, Crystal Structure Of Human M-Nad-Me In Ternary Complex




With Nad And Lu3+


1GZ4D
22218682
Chain D, The Regulation Of Human Mitochondrial Nad(P)+-




Dependent Malic Enzyme By Atp And Fumarate


1QR6B
5822327
Chain B, Human Mitochondrial Nad(P)-Dependent Malic Enzyme


1PJ3D
39654475
Chain D, Crystal Structure Of Human Mitochondrial Nad(P)+-




Dependent Malic Enzyme


P22178
126736
NADP-dependent malic enzyme, chloroplast precursor (NADP-ME)


XP_410305
49097690
hypothetical protein AN6168.2 [Aspergillus nidulans FGSC A4]


AAH22472
18490280
Malic enzyme 3, NADP(+)-dependent, mitochondrial [Homo sapiens]
















TABLE 6







Examples of AMP deaminase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





AAA34420
171053
AMP deaminase (EC 3.5.4.6)


XP_446684
50288509
unnamed protein product [Candida glabrata]


NP_983153
45185436
ABR204Cp [Eremothecium gossypii]


XP_453337
50306727
unnamed protein product [Kluyveromyces lactis]


EAL02322
46443037
adenosine/AMP deaminase [Candida albicans SC5314]


XP_460211
50423261
unnamed protein product [Debaryomyces hansenii]


XP_503822
50552824
hypothetical protein [Yarrowia lipolytica]


XP_413009
49131023
hypothetical protein AN8872.2 [Aspergillus nidulans FGSC A4]


XP_360256
39941438
hypothetical protein MG05630.4 [Magnaporthe grisea 70-15]


XP_381547
46108978
hypothetical protein FG01371.1 [Gibberella zeae PH-1]


XP_330167
32419447
probable AMP deaminase [MIPS] [Neurospora crassa]


CAB97316
16945394
probable AMP deaminase [Neurospora crassa]


T50996
11359582
probable AMP deaminase [imported] - Neurospora crassa


NP_595153
19111945
amp deaminase [Schizosaccharomyces pombe]


EAL22226
50259553
hypothetical protein CNBC3640 [Cryptococcus neoformans var.




neoformans B-3501A]


XP_402237
49076548
hypothetical protein UM04622.1 [Ustilago maydis 521]


CAA62797
995562
AMP deaminase [Schizosaccharomyces pombe]


AAF65407
7638159
AMP deaminase [Dictyostelium discoideum]


XP_537039
57088163
PREDICTED: similar to AMP deaminase 2 (AMP deaminase isoform




L) [Canis familiaris]


AAH49119
29145073
Adenosine monophosphate deaminase 2 (isoform L) [Mus musculus]


XP_569691
58265070
AMP deaminase, putative [Cryptococcus neoformans var. neoformans




JEC21]


AAD56303
5922018
AMP deaminase isoform L [Homo sapiens]


NP_004028
21264318
adenosine monophosphate deaminase 2 (isoform L) isoform 1 [Homo




sapiens]


A44313
345738
AMP deaminase (EC 3.5.4.6) isoform L - human


CAI19307
56206061
adenosine monophosphate deaminase 2 (isoform L) [Homo sapiens]


AAA62126
644509
AMP deaminase isoform L splicing variant


CAI19305
56206059
adenosine monophosphate deaminase 2 (isoform L) [Homo sapiens]


XP_310497
58424203
ENSANGP00000017310 [Anopheles gambiae str. PEST]


CAI19306
56206060
adenosine monophosphate deaminase 2 (isoform L) [Homo sapiens]


AAC50308
608499
AMP deaminase


CAG06825
47229629
unnamed protein product [Tetraodon nigroviridis]


NP_727741
45551453
CG32626-PD, isoform D [Drosophila melanogaster]


NP_727739
45551452
CG32626-PA, isoform A [Drosophila melanogaster]


NP_727740
24641890
CG32626-PB, isoform B [Drosophila melanogaster]


AAN09337
22832227
CG32626-PC, isoform C [Drosophila melanogaster]


T01259
7484807
AMP deaminase homolog F16M14.21 - Arabidopsis thaliana


XP_506591
51963676
PREDICTED P0034A04.129 gene product [Oryza sativa (japonica




cultivar-group)]


NP_850294
30687456
AMP deaminase, putative/myoadenylate deaminase, putative




[Arabidopsis thaliana]


CAG07509
47228777
unnamed protein product [Tetraodon nigroviridis]


NP_494974
32564190
Adenosine/AMP deaminase (85.4 kD) (2F499) [Caenorhabditis elegans]


T15771
7497030
hypothetical protein C34F11.3 - Caenorhabditis elegans


CAE59064
39596837
Hypothetical protein CBG02349 [Caenorhabditis briggsae]


NP_494973
32564194
Adenosine/AMP deaminase family member (2F499) [Caenorhabditis




elegans]


BAA06505
1321635
erythrocyte-type AMP deaminase [Homo sapiens]


NP_000471
4502079
adenosine monophosphate deaminase (isoform E) [Homo sapiens]


S68147
2134756
AMP deaminase (EC 3.5.4.6), erythrocte, splice form 1c - human


AAH56380
38614134
Ampd3 protein [Mus musculus]


O08739
2494043
AMP DEAMINASE 3 (AMP DEAMINASE ISOFORM E) (AMP




DEAMINASE H-TYPE) (HEART-TYPE AMPD)


NP_113732
13928736
adenosine monophosphate deaminase 3 [Rattus norvegicus]


O09178
2494044
AMP deaminase 3 (AMP deaminase isoform E)


XP_420973
50747746
PREDICTED: similar to AMP deaminase 3 (Erythrocyte AMP




deaminase) [Gallus gallus]


NP_956142
41054127
AMP deaminase 3 [Danio rerio]


CAG01709
47222742
unnamed protein product [Tetraodon nigroviridis]


NP_957187
41053780
hypothetical protein MGC77905 [Danio rerio]


XP_392957
48104570
similar to ENSANGP00000017310 [Apis mellifera]


AAH07183
13938134
Ampd3 protein [Mus musculus]


CAG05605
47220579
unnamed protein product [Tetraodon nigroviridis]


NP_620231
20302047
adenosine monophosphate deaminase 1 (isoform M) [Rattus norvegicus]


XP_540247
57098851
PREDICTED: similar to AMP deaminase 1 (AMP deaminase isoform




M) [Canis familiaris]


CAF99638
47230445
unnamed protein product [Tetraodon nigroviridis]


XP_513671
55587796
PREDICTED: adenosine monophosphate deaminase 1 (isoform M) [Pan




troglodytes]


CAI18828
56203368
adenosine monophosphate deaminase 1 (isoform M) [Homo sapiens]


CAI18829
56203369
OTTHUMP00000059283 [Homo sapiens]


CAI18830
56203370
adenosine monophosphate deaminase 1 (isoform M) [Homo sapiens]


EAA19931
23484684
AMP deaminase homolog [Plasmodium yoelii yoelii]


CAH99706
56500932
AMP deaminase, putative [Plasmodium berghei]


XP_131103
38076931
similar to AMP deaminase 1 (Myoadenylate deaminase) (AMP




deaminase isoform M) [Mus musculus]


CAH77387
56523366
AMP deaminase, putative [Plasmodium chabaudi]
















TABLE 7







Examples of acetoacetyl-CoA thiolase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





P10551
135758
Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)


Q04677
418002
Acetyl-CoA acetyltransferase IB (Peroxisomal acetoacetyl-CoA




thiolase) (Thiolase IB)


Q12598
34925109
Acetyl-CoA acetyltransferase IA (Peroxisomal acetoacetyl-CoA




thiolase) (Thiolase IA)


T10247
7433657
acetyl-CoA C-acetyltransferase (EC 2.3.1.9), cytosolic - radish


T42741
11257345
probable acetyl-CoA C-acetyltransferase (EC 2.3.1.9) - fission yeast




(Schizosaccharomyces pombe)


AAL18924
16417944
acetyl Co-A acetyltransferase [Hevea brasiliensis]


AAM67058
21618008
acetoacyl-CoA-thiolase [Arabidopsis thaliana]


AAO51605
28829030
similar to acetyl-coa acetyltransferase (EC 2.3.1.9)




[Schizosaccharomyces pombe]


AAU95618
53854350
cytosolic acetoacetyl-coenzyme A thiolase [Nicotiana tabacum]


AAU95619
53854352
peroxisomal acetoacetyl-coenzyme A thiolase [Nicotiana tabacum]


BAA97003
8777413
acetyl-CoA C-acetyltransferase [Arabidopsis thaliana]


CAE76429
38567134
probable acetoacetyl-CoA thiolase [Neurospora crassa]


EAK90852
46431255
hypothetical protein CaO19.1591 [Candida albicans SC5314]


EAL32264
54643520
GA10651-PA [Drosophila pseudoobscura]


NP_015297
6325229
Acetyl-CoA C-acetyltransferase (acetoacetyl-CoA thiolase)




[Saccharomyces cerevisiae]


NP_568694
30695411
acetyl-CoA C-acyltransferase, putative/3-ketoacyl-CoA thiolase,




putative [Arabidopsis thaliana]


NP_572414
24640423
CG10932-PA [Drosophila melanogaster]


NP_596686
19113478
acetyl-coa acetyltransferase (EC 2.3.1.9) [Schizosaccharomyces pombe]


NP_851154
30695409
acetyl-CoA C-acyltransferase, putative/3-ketoacyl-CoA thiolase,




putative [Arabidopsis thaliana]


NP_908411
34894172
putative acetoacetyl-coenzyme A thiolase [Oryza sativa (japonica




cultivar-group)]


NP_974900
42573608
acetyl-CoA C-acyltransferase, putative/3-ketoacyl-CoA thiolase,




putative [Arabidopsis thaliana]


NP_974901
42573610
acetyl-CoA C-acyltransferase, putative/3-ketoacyl-CoA thiolase,




putative [Arabidopsis thaliana]


NP_984262
45188039
ADR165Cp [Eremothecium gossypii]


XP_389497
46134945
hypothetical protein FG09321.1 [Gibberella zeae PH-1]


XP_401186
49074048
hypothetical protein UM03571.1 [Ustilago maydis 521]


XP_405546
49087148
hypothetical protein AN1409.2 [Aspergillus nidulans FGSC A4]


XP_449306
50293789
unnamed protein product [Candida glabrata]


XP_449306
50293789
unnamed protein product [Candida glabrata]


XP_450298
50899020
putative acetyl-CoA C-acyltransferase [Oryza sativa (japonica cultivar-




group)]


XP_453599
50307241
unnamed protein product [Kluyveromyces lactis]


XP_460741
50424309
unnamed protein product [Debaryomyces hansenii]


XP_500646
50546253
hypothetical protein [Yarrowia lipolytica]
















TABLE 8







Examples of HMG-CoA synthase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





B55729
1083370
hydroxymethylglutaryl-CoA synthase (EC 4.1.3.5), mitochondrial -




mouse


P54869
1708235
Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor (HMG-




CoA synthase)


S13887
86312
hydroxymethylglutaryl-CoA synthase (EC 4.1.3.5) - chicken


S27197
284048
hydroxymethylglutaryl-CoA synthase (EC 4.1.3.5), cytosolic, fibroblast




isoform - human


AAA37076
387072
3-hydroxy-3-methylglutaryl coenzyme A synthase (HMG CoA)


AAF89580
9621905
3-hydroxy-3-methylglutaryl coenzyme A synthase [Dendroctonus




jeffreyi]


AAH00297
33991031
HMGCS1 protein [Homo sapiens]


AAH31363
21618633
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 [Mus musculus]


AAH42929
27552834
Hmgcs1-prov protein [Xenopus laevis]


AAH79694
50925193
MGC80816 protein [Xenopus laevis]


AAH83543
54035469
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 [Rattus




norvegicus]


AAO52569
28830079
similar to Homo sapiens (Human). Hypothetical protein FLJ40785




[Dictyostelium discoideum]


AAP35966
30583443
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (soluble) [Homo




sapiens]


BAB23657
12836439
unnamed protein product [Mus musculus]


BAC04559
21754758
unnamed protein product [Homo sapiens]


BAC05233
21758044
unnamed protein product [Mus musculus]


CAA52032
1772495
hydroxymethylglutaryl-CoA synthase [Blattella germanica]


CAC18553
11602786
putative 3-hydroxy-3-methylglutaryl coenzyme A synthase




[Phycomyces blakesleeanus]


CAG33131
48145817
HMGCS2 [Homo sapiens]


CAH92111
55730782
hypothetical protein [Pongo pygmaeus]


CAI22408
56205097
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 (mitochondrial)




[Homo sapiens]


EAK97451
46438115
hypothetical protein CaO19.7312 [Candida albicans SC5314]


EAL25034
54635631
GA18098-PA [Drosophila pseudoobscura]


NP_002121
54020720
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (soluble) [Homo




sapiens]


NP_013580
6323509
3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase




[Saccharomyces cerevisiae]


NP_032282
31560689
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 [Mus musculus]


NP_058964
8393538
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 [Rattus




norvegicus]


NP_593859
19114771
hydroxymethylglutaryl-coa synthase (EC 4.1.3.5) [Schizosaccharomyces




pombe]


NP_666054
31981842
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 [Mus musculus]


NP_725570
24654139
CG4311-PE, isoform E [Drosophila melanogaster]


NP_775117
27465521
3-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 [Rattus




norvegicus]


NP_957379
41055180
similar to 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 [Danio




rerio]


NP_983739
45187516
ADL356Cp [Eremothecium gossypii]


NP_990742
45382279
3-hydroxy-3-methylglutaryl-CoA synthase [Gallus gallus]


NP_999545
47523816
hydroxymethylglutaryl-CoA synthase [Sus scrofa]


XP_315872
58387870
ENSANGP00000017491 [Anopheles gambiae str. PEST]


XP_323241
32405256
probable hydroxymethylglutaryl-CoA synthase [MIPS] [Neurospora




crassa]


XP_368218
39973655
hypothetical protein MG01026.4 [Magnaporthe grisea 70-15]


XP_389442
46134253
conserved hypothetical protein [Gibberella zeae PH-1]


XP_397202
48141273
similar to CG4311-PA [Apis mellifera]


XP_402977
49078452
hypothetical protein UM05362.1 [Ustilago maydis 521]


XP_409060
49095198
hypothetical protein AN4923.2 [Aspergillus nidulans FGSC A4]


XP_446972
50289085
unnamed protein product [Candida glabrata]


XP_453529
50307101
unnamed protein product [Kluyveromyces lactis]


XP_456470
50405663
unnamed protein product [Debaryomyces hansenii]


XP_506052
50557288
hypothetical protein [Yarrowia lipolytica]


XP_513693
55587844
PREDICTED: 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 2




(mitochondrial) [Pan troglodytes]


XP_536483
57085299
PREDICTED: similar to HMGCS1 protein [Canis familiaris]


XP_569805
58265298
hydroxymethylglutaryl-CoA synthase, putative [Cryptococcus


XP_571930
58269548
conserved hypothetical protein [Cryptococcus neoformans var.




neoformans JEC21]
















TABLE 9







Examples of HMG-CoA reductase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





A23586
90238
hydroxymethylglutaryl-CoA reductase (EC 1.1.1.88) - golden hamster


O74164
11132850
3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA




reductase)


P51639
1708252
3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA




reductase)


P54960
1708251
3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA




reductase)


Q12649
18276268
3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA




reductase)


Q29512
2495262
3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA




reductase)


Q9Y7D2
11133211
3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA




reductase)


S30338
422383
hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) -




German cockroach


S72194
7450066
hydroxymethylglutaryl-CoA reductase (EC 1.1.1.88) - fission yeast




(Schizosaccharomyces pombe)


AAA36989
387052
3-hydroxy-3-methylglutaryl coenzyme A [Mesocricetus auratus]


AAA37077
305355
3-hydroxy-3-methylglutaral coenzyme A reductase (EC 1.1.1.34)


AAA49740
214237
3-hydroxy-3-methylglutaryl-coenzyme A reductase


AAD20975
9817458
3-hydroxy-3-methylglutaryl coenzyme A reductase [Ips paraconfusus]


AAH74197
49257596
Unknown (protein for MGC:82101) [Xenopus laevis]


AAL09351
15824453
3-hydroxy-3-methylglutaryl coenzyme A reductase [Ips pini]


AAO85434
29468180
HMG-CoA reductase [Aspergillus nidulans]


AAP72015
32165622
3-hydroxy-3-methylglutaryl-Coenzyme A reductase [Homo sapiens]


AAR02862
45272118
HMG-CoA reductase [Dicentrarchus labrax]


AAT92819
51013051
YLR450W [Saccharomyces cerevisiae]


BAC20567
23574646
HMG-CoA reductase [Penicillium citrinum]


CAA63970
4376229
HMG-CoA-reductase; hydroxymethylglutaryl-CoA reductase (NADPH)




[Gibberella fujikuroi]


CAE47850
41581201
3-hydroxy-3-methylglutaryl-coenzyme a reductase, putative [Aspergillus




fumigatus]


CAF92135
47213283
unnamed protein product [Tetraodon nigroviridis]


CAH92577
55731745
hypothetical protein [Pongo pygmaeus]


EAK94577
46435190
hypothetical protein CaO19.8633 [Candida albicans SC5314]


EAL20195
50257490
hypothetical protein CNBF0070 [Cryptococcus neoformans var.




neoformans B-3501A]


AAF80374
8886086
HMG-CoA reductase [Dendroctonus jeffreyi]


NP_013555
6323483
Hmg2p [Saccharomyces cerevisiae]


NP_013636
6323565
Hmg1p [Saccharomyces cerevisiae]


NP_032281
56119096
3-hydroxy-3-methylglutaryl-Coenzyme A reductase [Mus musculus]


NP_037266
40538852
3-hydroxy-3-methylglutaryl-Coenzyme A reductase [Rattus norvegicus]


NP_588235
19075735
3-hydroxy-3-methylglutaryl-coenzyme a reductase




[Schizosaccharomyces pombe]


NP_985010
45190756
AER152Wp [Eremothecium gossypii]


NP_989816
45383193
3-hydroxy-3-methylglutaryl-CoA reductase [Gallus gallus]


NP_999724
47551099
HMGCoA reductase [Strongylocentrotus purpuratus]


XP_324892
32408825
hypothetical protein [Neurospora crassa]


XP_364130
39955070
hypothetical protein MG08975.4 [Magnaporthe grisea 70-15]


XP_389373
46134115
hypothetical protein FG09197.1 [Gibberella zeae PH-1]


XP_400629
49072680
hypothetical protein UM03014.1 [Ustilago maydis 521]


XP_405730
49087632
hypothetical protein AN1593.2 [Aspergillus nidulans FGSC A4]


XP_407954
49092986
hypothetical protein AN3817.2 [Aspergillus nidulans FGSC A4]


XP_449268
50293713
unnamed protein product [Candida glabrata]


XP_451740
50303597
unnamed protein product [Kluyveromyces lactis]


XP_458872
50420671
unnamed protein product [Debaryomyces hansenii]


XP_503558
50552167
hypothetical protein [Yarrowia lipolytica ]


XP_536323
57084803
PREDICTED: similar to 3-hydroxy-3-methylglutaryl-coenzyme A




reductase (HMG-CoA reductase) [Caniss ]


XP_571450
58268588
hydroxymethylglutaryl-CoA reductase (NADPH), putative




[Cryptococcus neoformans var. neoformans JEC21]
















TABLE 10







Examples of mevalonate kinase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





XP_386088
46123069
hypothetical protein FG05912.1 [Gibberella zeae PH-1]


XP_408006
49093090
hypothetical protein AN3869.2 [Aspergillus nidulans FGSC A4]


XP_370449
39978123
hypothetical protein MG06946.4 [Magnaporthe grisea 70-15]


EAL04797
46445529
hypothetical protein CaO19.4809 [Candida albicans SC5314]


XP_322935
32404644
hypothetical protein ((AL513444) related to MEVALONATE




KINASE [Neurospora crassa])


NP_001007
55925207
zgc:103473 [Danio rerio]


XP_460851
50424525
unnamed protein product [Debaryomyces hansenii]


XP_567851
58260882
cystathionine beta-lyase, putative [Cryptococcus neoformans var.




neoformans JEC21]


XP_567850
58260880
cystathionine beta-lyase, putative [Cryptococcus neoformans var.




neoformans JEC21]


AAQ02416
33303805
mevalonate kinase [synthetic construct]


CAA53059
450346
unnamed protein product [Hepatitis B virus]


AAH16140
16359371
MVK protein [Homo sapiens]


AAH05606
13542811
Mevalonate kinase [Mus musculus]


XP_403111
49078786
hypothetical protein UM05496.1 [Ustilago maydis 521]


XP_452532
50305147
unnamed protein product [Kluyveromyces lactis]


CAG08527
47226511
unnamed protein product [Tetraodon nigroviridis]


XP_446138
50287417
unnamed protein product [Candida glabrata]


AAO51522
28828936
similar to Rattus norvegicus (Rat). Mevalonate kinase (EC 2.7.1.36)




(MK) [Dictyostelium discoideum]


NP_985191
45190937
AER335Wp [Eremothecium gossypii]


XP_500956
50546973
hypothetical protein [Yarrowia lipolytica]


NP_013935
6323864
Erg12p [Saccharomyces cerevisiae]


AAD45421
5578718
mevalonate kinase [Arabidopsis thaliana]


NP_920723
37532842
putative mevalonate kinase [Oryza sativa (japonica cultivar-group)]


NP_851084
30690651
mevalonate kinase (MK) [Arabidopsis thaliana]


AAL18925
16417946
mevalonate kinase [Hevea brasiliensis]


NP_788338
28573850
CG33009-PA, isoform A [Drosophila melanogaster]


AAU20834
51988124
Hypothetical protein Y42G9A.4b [Caenorhabditis elegans]


AAU87813
52839819
Hypothetical protein Y42G9A.4d [Caenorhabditis elegans]


AAU20835
51988125
Hypothetical protein Y42G9A.4c [Caenorhabditis elegans]


YP_183887
57641409
mevalonate kinase [Thermococcus kodakaraensis KOD1]


NP_143478
14591399
mevalonate kinase [Pyrococcus horikoshii OT3]


BAA24409
2804172
mevalonate kinase [Saccharomyces cerevisiae]


NP_126232
14520757
mevalonate kinase [Pyrococcus abyssi GE5]


XP_522574
55639331
PREDICTED: similar to Mevalonate kinase (MK) [Pan troglodytes]


NP_071114
11499870
mevalonate kinase (mvk) [Archaeoglobus fulgidus DSM 4304]


XP_423949
50797461
PREDICTED: similar to mevalonate kinase [Gallus gallus]


NP_633786
21227864
Mevalonate kinase [Methanosarcina mazei Go1]


ZP_002971
48840229
COG1577: Mevalonate kinase [Methanosarcina barkeri str. fusaro]


EAH50787
44170778
unknown [environmental sequence]


NP_615566
20089491
mevalonate kinase [Methanosarcina acetivorans C2A]


1VISA
40890012
Chain A, Crystal Structure Of Mevalonate Kinase


EAK03559
44549994
unknown [environmental sequence]


NP_248080
15669275
mevalonate kinase [Methanocaldococcus jannaschii DSM 2661]


1KKHA
20150886
Chain A, Crystal Structure Of The Methanococcus Jannaschii




Mevalonate Kinase


Q50559
2497518
Mevalonate kinase (MK)


CAF88123
47200914
unnamed protein product [Tetraodon nigroviridis]


NP_275189
15678075
mevalonate kinase [Methanothermobacter thermautotrophicus str. Delta




H]


EAI88745
44383877
unknown [environmental sequence]


ZP_002040
46141948
COG1577: Mevalonate kinase [Methanococcoides burtonii DSM 6242]


XP_543435
57105916
PREDICTED: similar to Mevalonate kinase (MK) [Canis familiaris]


EAI38920
44313360
unknown [environmental sequence]


NP_148611
14602065
mevalonate kinase [Aeropyrum pernix K1]


EAD08953
43286228
unknown [environmental sequence]


EAD45697
43361720
unknown [environmental sequence]


YP_134862
55377012
mevalonate kinase [Haloarcula marismortui ATCC 43049]


NP_720650
24378695
putative mevalonate kinase [Streptococcus mutans UA159]


NP_614276
20094429
Mevalonate kinase [Methanopyrus kandleri AV19]


E84270
25409931
mevalonate kinase [imported] - Halobacterium sp. NRC-1


NP_691146
23097680
mevalonate kinase [Oceanobacillus iheyensis HTE831]


ZP_003233
48870579
COG1577: Mevalonate kinase [Pediococcus pentosaceus ATCC 25745]


AAG02440
9937386
mevalonate kinase [Enterococcus faecalis]


EAD12278
43292898
unknown [environmental sequence]


NP_498328
17555862
mevalonate kinase (64.1 kD) (3H214) [Caenorhabditis elegans]


EAB31483
42928976
unknown [environmental sequence]


ZP_003319
50590618
COG1577: Mevalonate kinase [Streptococcus suis 89/1591]


NP_814642
29375488
mevalonate kinase [Enterococcus faecalis V583]


AC1434
25514495
mevalonate kinase homolog lin0010 [imported] - Listeria innocua




(strain Clip11262)


ZP_003577
53796847
COG1577: Mevalonate kinase [Chloroflexus aurantiacus]


EAD82048
43454743
unknown [environmental sequence]


CAE73618
39586491
Hypothetical protein CBG21109 [Caenorhabditis briggsae]


YP_012624
46906235
mevalonate kinase [Listeria monocytogenes str. 4b F2365]


NP_988455
45358898
Mevalonate kinase [Methanococcus maripaludis S2]


ZP_002348
47097293
mevalonate kinase [Listeria monocytogenes str. 1/2a F6854]


ZP_002862
48824993
COG1577: Mevalonate kinase [Enterococcus faecium]


ZP_002307
47093020
mevalonate kinase [Listeria monocytogenes str. 4b H7858]


NP_597102
19173299
MEVALONATE KINASE [Encephalitozoon cuniculi]


CAD24422
20429111
phosphomevalonate kinase [Paracoccus zeaxanthinifaciens]


NP_785308
28378416
mevalonate kinase [Lactobacillus plantarum WCFS1]


EAA39098
29247539
GLP_305_18405_19430 [Giardia lamblia ATCC 50803]


NP_819638
29653946
phosphomevalonate kinase, putative [Coxiella burnetii RSA 493]


EAH49746
44168765
unknown [environmental sequence]


EAH49745
44168764
unknown [environmental sequence]


NP_378182
15922513
hypothetical protein ST2185 [Sulfolobus tokodaii str. 7]


ZP_000459
23002259
COG1577: Mevalonate kinase [Lactobacillus gasseri]


H90181
25393827
mevalonate kinase [imported] - Sulfolobus solfataricus


YP_054120
50405028
Mevalonate kinase, putative [Paramecium tetraurelia]


BAB07790
9695270
mevalonate kinase [Streptomyces sp. CL190]


AAG02435
9937379
mevalonate kinase [Staphylococcus epidermidis]


NP_560495
18313828
mevalonate kinase [Pyrobaculum aerophilum str. IM2]


YP_187834
57866187
mevalonate kinase [Staphylococcus epidermidis RP62A]


EAK40782
44602942
unknown [environmental sequence]


CAC51370
15212070
mevalonate kinase [Lactobacillus helveticus]


AAG02424
9937364
mevalonate kinase [Staphylococcus aureus]


YP_185521
57651465
mevalonate kinase [Staphylococcus aureus subsp. aureus COL]


YP_040044
49482820
mevalonate kinase [Staphylococcus aureus subsp. aureus MRSA252]


YP_194037
58337452
mevalonate kinase [Lactobacillus acidophilus NCFM]


D86675
25400965
mevalonate kinase [imported] - Lactococcus lactis subsp. lactis (strain




IL1403)


NP_763916
27467279
mevalonate kinase [Staphylococcus epidermidis ATCC 12228]


CAF89434
47197810
unnamed protein product [Tetraodon nigroviridis]


EAF38333
43767792
unknown [environmental sequence]


EAK46841
44611394
unknown [environmental sequence]


H89827
25507776
mevalonate kinase [imported] - Staphylococcus aureus (strain N315)


ZP_003149
48861061
COG0153: Galactokinase [Microbulbifer degradans 2-40]


EAK17824
44570143
unknown [environmental sequence]


EAH86276
44235719
unknown [environmental sequence]


YP_118418
54024176
putative mevalonate kinase [Nocardia farcinica IFM 10152]


ZP_003196
48865749
COG1577: Mevalonate kinase [Oenococcus oeni PSU-1]


AAG02430
9937372
mevalonate kinase [Staphylococcus haemolyticus]


NP_269075
15674901
mevalonate kinase [Streptococcus pyogenes M1 GAS]


NP_802520
28896170
putative mevalonate kinase [Streptococcus pyogenes SSI-1]


AAL97579
19748102
mevalonate kinase [Streptococcus pyogenes MGAS8232]


ZP_003666
56808907
COG1577: Mevalonate kinase [Streptococcus pyogenes M49 591]


NP_965060
42519130
mevalonate kinase [Lactobacillus johnsonii NCC 533]


NP_819639
29653947
mevalonate kinase, putative [Coxiella burnetii RSA 493]


EAD97024
43484567
unknown [environmental sequence]


BAD86800
57753870
mevalonate kinase [Streptomyces sp. KO-3988]
















TABLE 11







Examples of phosphomevalonate kinase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





AAA34596
171479
phosphomevalonate kinase


XP_452514
50305111
unnamed protein product [Kluyveromyces lactis]


NP_985210
45190956
AER354Wp [Eremothecium gossypii]


XP_446144
50287429
unnamed protein product [Candida glabrata]


XP_462340
50427455
unnamed protein product [Debaryomyces hansenii]


EAL04096
46444824
hypothetical protein CaO19.12076 [Candida albicans SC5314]


EAL03941
46444668
hypothetical protein CaO19.4606 [Candida albicans SC5314]


XP_503619
50552418
hypothetical protein [Yarrowia lipolytica]


XP_389940
46136497
hypothetical protein FG09764.1 [Gibberella zeae PH-1]


XP_329795
32418634
hypothetical protein [Neurospora crassa]


XP_369652
39976529
hypothetical protein MG05812.4 [Magnaporthe grisea 70-15]


XP_406448
49089559
hypothetical protein AN2311.2 [Aspergillus nidulans FGSC A4]


NP_593421
19114333
putative phosphomevalonate kinase [Schizosaccharomyces pombe]


XP_568385
58261950
expressed protein [Cryptococcus neoformans var. neoformans JEC21]


EAL17628
50254887
hypothetical protein CNBM0120 [Cryptococcus neoformans var.




neoformans B-3501A]


AAL18926
16417948
phosphomevalonate kinase [Hevea brasiliensis]


BAD43274
51969164
hypothetical protein [Arabidopsis thaliana]


BAD44652
51971975
hypothetical protein [Arabidopsis thaliana]


XP_398375
49068172
hypothetical protein UM00760.1 [Ustilago maydis 521]


BAD44486
51971643
hypothetical protein [Arabidopsis thaliana]


F90479
25393214
(Phospho) mevalonate kinase, probable [imported] - Sulfolobus




solfataricus


YP_194039
58337454
phosphomevalonate kinase [Lactobacillus acidophilus NCFM]
















TABLE 12







Examples of mevalonate pyrophosphate decarboxylase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





AAT93171
51013755
YNR043W [Saccharomyces cerevisiae]


1FI4A
13786942
Chain A, The X-Ray Crystal Structure Of Mevalonate 5-Diphosphate




Decarboxylase At 2.3 Angstrom Resolution.


XP_455548
50311049
unnamed protein product [Kluyveromyces lactis]


XP_445335
50285813
unnamed protein product [Candida glabrata]


XP_456912
50409853
unnamed protein product [Debaryomyces hansenii]


NP_986435
45200865
AGL232Cp [Eremothecium gossypii]


AAF19399
6625790
diphosphomevalonate decarboxylase MVD1 [Candida albicans]


XP_328845
32416734
hypothetical protein [Neurospora crassa]


XP_505041
50555265
hypothetical protein [Yarrowia lipolytica]


NP_594027
19114939
diphosphomevalonate decarboxylase [Schizosaccharomyces pombe]


XP_364905
39963452
hypothetical protein MG09750.4 [Magnaporthe grisea 70-15]


XP_390600
46137817
hypothetical protein FG10424.1 [Gibberella zeae PH-1]


XP_408551
49094180
hypothetical protein AN4414.2 [Aspergillus nidulans FGSC A4]


AAA34506
7544604
ORF [Saccharomyces cerevisiae]


EAL18927
50256200
hypothetical protein CNBI1880 [Cryptococcus neoformans var.




neoformans B-3501A]


XP_568247
58261674
diphosphomevalonate decarboxylase, putative [Cryptococcus




neoformans var. neoformans JEC21]


XP_402794
49077992
hypothetical protein UM05179.1 [Ustilago maydis 521]


AAH81784
51980639
Mevalonate (diphospho) decarboxylase [Rattus norvegicus]


EAL00166
46440864
hypothetical protein CaO19.6105 [Candida albicans SC5314]


NP_619597
20149736
mevalonate (diphospho) decarboxylase [Mus musculus]


NP_112324
13592005
mevalonate (diphospho) decarboxylase [Rattus norvegicus]


BAC40852
26354448
unnamed protein product [Mus musculus]


XP_546783
57087071
Mevalonate pyrophosphate decarboxylase [Canis familiaris]


Q99JF5
23814095
Diphosphomevalonate decarboxylase (Mevalonate pyrophosphate




decarboxylase)


AAH63907
39645379
LOC394871 protein [Xenopus tropicalis]


CAF99534
47230341
unnamed protein product [Tetraodon nigroviridis]


AAP35576
30582699
mevalonate (diphospho) decarboxylase [Homo sapiens]


AAP36301
30584105
Homo sapiens mevalonate (diphospho) decarboxylase [synthetic




construct]


AAL18927
16417950
mevalonate disphosphate decarboxylase [Hevea brasiliensis]


AAV32433
54292590
mevalonate disphosphate decarboxylase [Ginkgo biloba]


AAP68208
31711704
At2g38700 [Arabidopsis thaliana]


AAM64988
21593039
mevalonate diphosphate decarboxylase [Arabidopsis thaliana]


NP_566995
18410026
mevalonate diphosphate decarboxylase, putative [Arabidopsis thaliana]


XP_423130
50771155
PREDICTED: similar to mevalonate pyrophosphate decarboxylase




[Gallus gallus]


AAM65192
21593243
diphosphomevalonate decarboxylase-like protein [Arabidopsis thaliana]


NP_001007
55925435
zgc:100824 [Danio rerio]


NP_573068
28571205
CG8239-PA [Drosophila melanogaster]


BAD27942
50252009
putative mevalonate disphosphate decarboxylase [Oryza sativa (japonica




cultivar-group)]


T47584
11281655
diphosphomevalonate decarboxylase (EC 4.1.1.33) F24B22.210




[similarity] - Arabidopsis thaliana


XP_307373
31196851
ENSANGP00000013738 [Anopheles gambiae str. PEST]


CAE73245
39591192
Hypothetical protein CBG20661 [Caenorhabditis briggsae]


NP_496966
17537201
mevalonate decarboxylase (41.5 kD) (2O512) [Caenorhabditis elegans]


XP_393230
48121058
similar to mevalonate pyrophosphate decarboxylase [Apis mellifera]


G90479
25393662
diphosphomevalonate decarboxylase, probable [imported] - Sulfolobus




solfataricus


NP_496967
17537203
mevalonate decarboxylase (2O512) [Caenorhabditis elegans]


NP_691147
23097681
mevalonate diphosphate decarboxylase [Oceanobacillus iheyensis




HTE831]


EAL29282
54640164
GA20922-PA [Drosophila pseudoobscura]


AD1434
25515042
mevalonate diphosphate decarboxylase homolog lin0011 [imported] -




Listeria innocua (strain Clip11262)


ZP_002308
47093021
diphosphomevalonate decarboxylase [Listeria monocytogenes str. 4b




H7858]


YP_012625
46906236
diphosphomevalonate decarboxylase [Listeria monocytogenes str. 4b




F2365]


ZP_002348
47097294
diphosphomevalonate decarboxylase [Listeria monocytogenes str. 1/2a




F6854]


NP_819637
29653945
diphosphomevalonate decarboxylase [Coxiella burnetii RSA 493]


NP_376888
15921219
hypothetical diphosphomevalonate decarboxylase [Sulfolobus tokodaii




str. 7]


ZP_003319
50590617
COG3407: Mevalonate pyrophosphate decarboxylase [Streptococcus




suis 89/1591]


NP_585805
19074299
MEVALONATE PYROPHOSPHATE DECARBOXYLASE




[Encephalitozoon cuniculi]


YP_187835
57866188
mevalonate diphosphate decarboxylase [Staphylococcus epidermidis




RP62A]


CAD24423
20429112
mevalonate diphosphate decarboxylase [Paracoccus zeaxanthinifaciens]


AAG02431
9937373
mevalonate diphosphate decarboxylase [Staphylococcus haemolyticus]


NP_763917
27467280
mevalonate diphosphate decarboxylase [Staphylococcus epidermidis




ATCC 12228]


AAG02446
9937394
mevalonate diphosphate decarboxylase [Enterococcus faecium]


ZP_002863
48824994
COG3407: Mevalonate pyrophosphate decarboxylase [Enterococcus




faecium]


AAG02441
9937387
mevalonate diphosphate decarboxylase [Enterococcus faecalis]


YP_185522
57651466
mevalonate diphosphate decarboxylase [Staphylococcus aureus subsp.




aureus COL]


A89828
25505863
mevalonate diphosphate decarboxylase [imported] - Staphylococcus




aureus (strain N315)


NP_814641
29375487
mevalonate diphosphate decarboxylase [Enterococcus faecalis V583]


YP_040045
49482821
mevalonate diphosphate decarboxylase [Staphylococcus aureus subsp.




aureus MRSA252]


NP_785307
28378415
diphosphomevalonate decarboxylase [Lactobacillus plantarum WCFS1]


ZP_003196
48865750
COG3407: Mevalonate pyrophosphate decarboxylase [Oenococcus oeni




PSU-1]


ZP_003233
48870580
COG3407: Mevalonate pyrophosphate decarboxylase [Pediococcus




pentosaceus ATCC 25745]


E86675
25400967
diphosphomevalonate decarboxylase [imported] - Lactococcus lactis




subsp. lactis (strain IL1403)


EAE31110
43552684
unknown [environmental sequence]


BAB07791
9695271
diphosphomevalonate decarboxylase [Streptomyces sp. CL190]


CAC51371
15212071
mevalonate diphosphate decarboxylase [Lactobacillus helveticus]


ZP_000459
23002258
COG3407: Mevalonate pyrophosphate decarboxylase [Lactobacillus




gasseri]


NP_965061
42519131
mevalonate pyrophosphate decarboxylase [Lactobacillus johnsonii NCC




533]


BAD86801
57753871
mevalonate diphosphate decarboxylase [Streptomyces sp. KO-3988]


YP_194038
58337453
mevalonate diphosphate decarboxylase [Lactobacillus acidophilus




NCFM]


YP_118419
54024177
putative diphosphomevalonate decarboxylase [Nocardia farcinica IFM




10152]


EAK18820
44571499
unknown [environmental sequence]


EAI85935
44379784
unknown [environmental sequence]


NP_721336
24379381
putative mevalonate diphosphate decarboxylase [Streptococcus mutans




UA159]


D95044
25388338
diphosphomevalonate decarboxylase [imported] - Streptococcus




pneumoniae (strain TIGR4)


AAG02456
9937408
mevalonate diphosphate decarboxylase [Streptococcus pneumoniae]


C97914
25511486
diphosphomevalonate decarboxylase (EC 4.1.1.33) [imported] -




Streptococcus pneumoniae (strain R6)


EAK47683
44612560
unknown [environmental sequence]


EAB86425
43039778
unknown [environmental sequence]


YP_140971
55822530
mevalonate pyrophosphate decarboxylase [Streptococcus thermophilus




CNRZ1066]


YP_139081
55820639
mevalonate pyrophosphate decarboxylase [Streptococcus thermophilus




LMG 18311]


BAD07376
40882372
mevalonate diphosphate decarboxylase [Actinoplanes sp. A40644]


NP_968512
42523132
Diphosphomevalonate decarboxylase [Bdellovibrio bacteriovorus




HD100]


EAI06705
44265427
unknown [environmental sequence]


YP_060018
50914046
Diphosphomevalonate decarboxylase [Streptococcus pyogenes




MGAS10394]


AAG02451
9937401
mevalonate diphosphate decarboxylase [Streptococcus pyogenes]


NP_269076
15674902
mevalonate pyrophosphate decarboxylase [Streptococcus pyogenes M1




GAS]


ZP_003666
56808906
COG3407: Mevalonate pyrophosphate decarboxylase [Streptococcus




pyogenes M49 591]


NP_688323
22537472
diphosphomevalonate decarboxylase [Streptococcus agalactiae




2603V/R]


NP_735832
25011437
hypothetical protein gbs1395 [Streptococcus agalactiae NEM316]


EAC40267
43149093
unknown [environmental sequence]


AAL97580
19748103
mevalonate pyrophosphate decarboxylase [Streptococcus pyogenes




MGAS8232]


EAI76915
44367119
unknown [environmental sequence]


EAD35042
43339207
unknown [environmental sequence]


YP_073129
51598941
mevalonate pyrophosphate decarboxylase [Borrelia garinii PBi]


EAI90092
44385501
unknown [environmental sequence]


BAB07818
9711347
mevalonate diphosphate decaroboxylase [Kitasatospora griseola]


EAD72850
43433025
unknown [environmental sequence]


NP_212820
15595031
mevalonate pyrophosphate decarboxylase [Borrelia burgdorferi B31]


YP_124337
54297968
hypothetical protein lpp2023 [Legionella pneumophila str. Paris]


YP_096056
52842257
mevalonate diphosphate decarboxylase [Legionella pneumophila subsp.




pneumophila str. Philadelphia 1]


EAA39903
29248368
GLP_479_14176_13169 [Giardia lamblia ATCC 50803]


EAH06252
44088237
unknown [environmental sequence]


YP_127354
54294939
hypothetical protein lpl2018 [Legionella pneumophila str. Lens]


EAD45753
43361830
unknown [environmental sequence]


NP_802519
28896169
putative mevalonate pyrophosphate decarboxylase [Streptococcus




pyogenes SSI-1]
















TABLE 13







Examples of IPP isomerase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





NP_015208
6325140
Idi1p [Saccharomyces cerevisiae]


XP_448008
50291151
unnamed protein product [Candida glabrata]


NP_983828
45187605
ADL268Cp [Eremothecium gossypii]


XP_455121
50310203
unnamed protein product [Kluyveromyces lactis]


XP_462358
50427491
unnamed protein product [Debaryomyces hansenii]


EAL01685
46442395
potential isopentenyl diphosphate isomerase [Candida albicans SC5314]


XP_504974
50555131
hypothetical protein [Yarrowia lipolytica]


XP_328425
32415894
hypothetical protein [Neurospora crassa]


XP_367200
39971619
hypothetical protein MG07125.4 [Magnaporthe grisea 70-15]


XP_389898
46136413
conserved hypothetical protein [Gibberella zeae PH-1]


XP_404716
49085144
hypothetical protein AN0579.2 [Aspergillus nidulans FGSC A4]


CAD37150
21627818
isopentenyl-diphosphate delta-isomerase [Aspergillus fumigatus]


NP_595164
19111956
isopentenyl-diphosphate delta-isomerase [Schizosaccharomyces pombe]


XP_566641
58258457
isopentenyl-diphosphate delta-isomerase, putative [Cryptococcus




neoformans var. neoformans JEC21]


XP_402453
49077100
hypothetical protein UM04838.1 [Ustilago maydis 521]


O35586
6225528
Isopentenyl-diphosphate delta-isomerase 1 (IPP isomerase 1)


AAP36609
30584713
Homo sapiens isopentenyl-diphosphate delta isomerase [synthetic




construct]


AAF37873
7188790
isopentenyl pyrophosphate isomerase [Dictyostelium discoideum]


NP_445991
16758306
isopentenyl-diphosphate delta isomerase [Rattus norvegicus]


O42641
6225529
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


BAA33979
3790386
IPP isomerase [Xanthophyllomyces dendrorhous]


Q13907
6225527
Isopentenyl-diphosphate delta-isomerase 1 (IPP isomerase 1)


AAH22418
48257241
IDI1 protein [Homo sapiens]


AAH19227
48257312
IDI1 protein [Homo sapiens]


AAH57827
35505325
IDI1 protein [Homo sapiens]


NP_004499
40018633
isopentenyl-diphosphate delta isomerase [Homo sapiens]


AAH89786
58477715
Unknown (protein for MGC:108635) [Rattus norvegicus]


CAH91844
55730243
hypothetical protein [Pongo pygmaeus]


XP_418561
50732281
PREDICTED: similar to isopentenyl-diphosphate delta isomerase; IPP




isomerase [Gallus gallus]


AAH06999
48257093
IDI1 protein [Homo sapiens]


CAF98782
47225155
unnamed protein product [Tetraodon nigroviridis]


NP_808875
29366820
isopentenyl-diphosphate delta isomerase [Mus musculus]


XP_507622
55633353
PREDICTED: similar to isopentenyl-diphosphate delta isomerase; IPP




isomerase [Pan troglodytes]


AAH82648
52139082
LOC494671 protein [Xenopus laevis]


NP_001011
58332496
hypothetical LOC496783 [Xenopus tropicalis]


AAF29976
6856556
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Lactuca sativa]


AAG10423
9971806
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Tagetes erecta]


O48964
6225525
Isopentenyl-diphosphate delta-isomerase I (IPP isomerase I)




(Isopentenyl pyrophosphate isomerase I)


AAF29973
6856550
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Adonis palaestina]


AAF29977
6856558
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Tagetes erecta]


AAQ84167
35186998
isopentenyl pyrophosphate isomerase [Pueraria montana var. lobata]


AAF29974
6856552
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Adonis palaestina]


Q39472
6225526
Isopentenyl-diphosphate delta-isomerase I (IPP isomerase I)




(Isopentenyl pyrophosphate isomerase I)


S49588
1085973
isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) 1 - Clarkia




breweri (fragment)


AAL91980
19568939
isopentenyl pyrophosphate isomerase IDI1 [Melaleuca alternifolia]


BAB40973
13603406
isopentenyl diphosphate isomerase 1 [Nicotiana tabacum]


AAF29975
6856554
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Lactuca sativa]


T52027
25493162
isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) 1 [validated] -




Haematococcus pluvialis


AAL91979
19568937
isopentenyl pyrophosphate isomerase IDI2 [Melaleuca alternifolia]


T46812
11362218
isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) [imported] -




Haematococcus pluvialis


T51248
11362217
isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) 2 [validated] -




Haematococcus pluvialis


BAB40974
13603408
isopentenyl diphosphate isomerase 2 [Nicotiana tabacum]


O48965
6225532
Isopentenyl-diphosphate delta-isomerase II (IPP isomerase II)




(Isopentenyl pyrophosphate isomerase II)


XP_225509
34877710
similar to isopentenyl diphosphate delta-isomerase type 2 [Rattus




norvegicus]


XP_506401
51963472
PREDICTED OJ1612_A04.101 gene product [Oryza sativa (japonica




cultivar-group)]


AAF29978
6856560
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Oryza sativa]


AAH76541
50369278
Unknown (protein for IMAGE:7037641) [Danio rerio]


AAT94033
51038230
putative isopentenyl-diphosphate delta-isomerase [Oryza sativa




(japonica cultivar-group)]


XP_225502
34876517
similar to isopentenyl diphosphate delta-isomerase type 2 [Rattus




norvegicus]


Q39471
6225533
Isopentenyl-diphosphate delta-isomerase II (IPP isomerase II)




(Isopentenyl pyrophosphate isomerase II)


AAB67743
1213450
isopentenyl pyrophosphate isomerase [Clarkia breweri]


NP_197148
22326844
isopentenyl-diphosphate delta-isomerase I [Arabidopsis thaliana]


BAB09611
9759126
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Arabidopsis thaliana]


AAD41766
5305669
isopentenyl pyrophosphate isomerase [Hevea brasiliensis]


AAB67741
1213442
isopentenyl pyrophosphate isomerase [Arabidopsis thaliana]


XP_395125
48101420
similar to CG8646-PA [Apis mellifera]


AAN28784
23505849
At3g02780/F13E7_28 [Arabidopsis thaliana]


AAF36996
7110585
isopentenyl pyrophosphate:dimethylallyl pyrophosphate isomerase




[Brassica oleracea var. botrytis]


BAB16690
15289752
putative IPP isomerase [Eucommia ulmoides]


AAQ14869
33340598
isopentenyl pyrophosphate isomerase [Zea mays]


BAC65421
28971819
isopentenyl-diphosphate delta-isomerase [Periploca sepium]


S71369
2129625
isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) 1 - Arabidopsis




thaliana


AAF29979
6856562
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Arabidopsis thaliana]


AAF29980
6856564
isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase




[Arabidopsis thaliana]


AAP21674
30267831
isopentenyl diphosphate delta-isomerase type 2 [Mus musculus]


Q39664
6225534
Isopentenyl-diphosphate delta-isomerase II (IPP isomerase II)




(Isopentenyl pyrophosphate isomerase II)


NP_650962
24648688
CG5919-PA [Drosophila melanogaster]


AAM50284
21429130
RE22306p [Drosophila melanogaster]


XP_321388
58395620
ENSANGP00000011643 [Anopheles gambiae str. PEST]


Q9BXS1
20978506
Isopentenyl-diphosphate delta-isomerase 2 (IPP isomerase 2))


T07979
7484383
isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) ipi1 -




Chlamydomonas reinhardtii


XP_225508
34876527
similar to diphosphate dimethylallyl diphosphate isomerase 2 [Rattus




norvegicus]


AAT92102
51011386
isopentenyl-diphosphate delta-isomerase [Ixodes pacificus]


XP_225507
34876555
similar to isopentenyl diphosphate delta-isomerase type 2 [Rattus




norvegicus]


XP_344623
34876537
similar to isopentenyl diphosphate delta-isomerase type 2 [Rattus




norvegicus]


S44843
630677
K06H7.3 protein - Caenorhabditis elegans


XP_225498
27687955
similar to diphosphate dimethylallyl diphosphate isomerase 2 [Rattus




norvegicus]


AAT08468
47013849
isopentenyl-diphosphate isomerase [Caenorhabditis elegans]


EAI79636
44370808
unknown [environmental sequence]


CAE75055
39587401
Hypothetical protein CBG22969 [Caenorhabditis briggsae]


EAL04047
46444775
potential isopentenyl diphosphate isomerase fragment [Candida albicans




SC5314]


XP_225528
34876543
similar to isopentenyl diphosphate delta-isomerase type 2 [Rattus




norvegicus]


XP_544282
57040602
PREDICTED: similar to isopentenyl-diphosphate delta isomerase [Canis




familiaris]


XP_225511
27688013
similar to diphosphate dimethylallyl diphosphate isomerase 2 [Rattus




norvegicus]


P26173
114853
Isopentenyl-diphosphate delta-isomerase (IPP isomerase)




(Bacteriochlorophyll synthase 20 kDa chain)


EAJ04069
44405322
unknown [environmental sequence]


EAH27496
44127513
unknown [environmental sequence]


AAF91499
9653280
isopentenyl pyrophosphate isomerase [Daucus carota]


AAM48661
21328655
isopentyl-diphosphate delta-isomerase [uncultured proteobacterium]


EAK17826
44570145
unknown [environmental sequence]


EAD59515
43391069
unknown [environmental sequence]


YP_128702
54307682
hypothetical isopentenyldiphosphate isomerase [Photobacterium




profundum SS9]


EAK66656
44639203
unknown [environmental sequence]


YP_118189
54023947
putative isopentenyldiphosphate isomerase [Nocardia farcinica IFM




10152]


T50740
11282665
isopentenyl diphosphate isomerase homolog [imported] - Rhodobacter




sphaeroides


ZP_002077
46193541
COG1443: Isopentenyldiphosphate isomerase [Rhodobacter sphaeroides




2.4.1]


EAK16470
44568229
unknown [environmental sequence]


YP_165403
56695056
isopentyl-diphosphate delta-isomerase [Silicibacter pomeroyi DSS-3]


EAD08775
43285885
unknown [environmental sequence]


YP_195623
58616494
putative isopentenyl-diphosphate delta-isomerase [Azoarcus sp. EbN1]


EAI38918
44313358
unknown [environmental sequence]


NP_930583
37527239
hypothetical protein plu3365 [Photorhabdus luminescens subsp.




laumondii TTO1]


YP_160254
56478665
isopentenyl-diphosphate delta-isomerase [Azoarcus sp. EbN1]


EAH69842
44206571
unknown [environmental sequence]


EAK26254
44582307
unknown [environmental sequence]


AAR24381
38569721
isopentyl-diphosphate delta isomerase [Sus scrofa]


AAM48607
21328600
isopentenyl-diphosphate delta-isomerase, putative [uncultured




proteobacterium]


EAD82049
43454744
unknown [environmental sequence]


ZP_001924
45914126
COG1443: Isopentenyldiphosphate isomerase [Mesorhizobium sp.




BNC1]


YP_056780
50843553
isopentenyl-diphosphate delta-isomerase [Propionibacterium acnes




KPA171202]


YP_050880
50121713
putative isopentenyl-diphosphate delta-isomerase [Erwinia carotovora




subsp. atroseptica SCRI1043]


EAF29235
43749645
unknown [environmental sequence]


NP_630823
21225044
putative IPP isomerase [Streptomyces coelicolor A3(2)]


Q82MJ7
34582349
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


ZP_003374
52010110
COG1443: Isopentenyldiphosphate isomerase [Silicibacter sp. TM1040]


AAS75819
45737905
isopentenyl/dimethylallyl diphosphate isomerase [Nicotiana




benthamiana]


Q8KP37
30913023
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


XP_507621
55633351
PREDICTED: similar to isopentenyl-diphosphate delta isomerase 2 [Pan




troglodytes]


XP_344621
34876521
similar to diphosphate dimethylallyl diphosphate isomerase 2 [Rattus




norvegicus]


XP_346322
34880719
similar to diphosphate dimethylallyl diphosphate isomerase 2 [Rattus




norvegicus]


YP_152060
56414985
probable isomerase [Salmonella enterica subsp. enterica serovar Paratypi




A str. ATCC 9150]


AAT42442
48429280
putative isopentenyl diphosphate isomerase [Edwardsiella ictaluri]


Q9KK75
13878536
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


NP_806649
29143307
probable isomerase [Salmonella enterica subsp. enterica serovar Typhi




Ty2]


YP_063124
50955836
isopentenyldiphosphate isomerase [Leifsonia xyli subsp. xyli str.




CTCB07]


Q8FND7
46395593
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


CAF20647
41326485
ISOPENTENYLDIPHOSPHATE ISOMERASE [Corynebacterium




glutamicum ATCC 13032]


Q8NN99
23821718
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


Q7X5H2
46395586
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


NP_336246
15841209
isopentenyl-diphosphate delta-isomerase [Mycobacterium tuberculosis




CDC1551]


Q83MJ9
46395588
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


P60923
46395576
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


Q8FE75
31563050
Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenyl




pyrophosphate isomerase)


1R67A
38493022
Chain A, Y104a Mutant Of E. Coli Ipp Isomerase


Q9KWD1
13878537
Isopentenyl-diphosphate delta-isomerase (IPP isomerase)


Q7VEU0
46395585
Isopentenyl-diphosphate delta-isomerase (IPP isomerase)


B84333
25410326
isopentenyl pyrophosphate isomerase [imported] - Halobacterium sp.




NRC-1


NP_417365
16130791
isopentenyl diphosphate isomerase [Escherichia coli K12]


E85944
25355426
probable enzyme Z4227 [imported] - Escherichia coli (strain O157:H7,




substrain EDL933)


1HZTA
15826050
Chain A, Crystal Structure Of Metal-Free Isopentenyl




Diphosphate:dimethylallyl Diphosphate Isomerase


1PVFB
50513321
Chain B, E. Coli Ipp Isomerase In Complex With Diphosphate


EAD63579
43403471
unknown [environmental sequence]


1I9AB
13786886
Chain B, Mevalonate 5-Diphosphate Decarboxylase And Isopentenyl




Diphosphate Isomerase


YP_012992
46906603
MutT/nudix family protein [Listeria monocytogenes str. 4b F2365]


ZP_002293
47091503
MutT/nudix family protein [Listeria monocytogenes str. 4b H7858]


EAI37194
44310821
unknown [environmental sequence]


YP_137864
55380014
probable isopentenyl-diphosphate delta-isomerase [Haloarcula




marismortui ATCC 43049]


CAD92056
42516867
putative isopentenyl diphosphate isomerase type 1 [Haloferax




mediterranei]


1OW2B
42543244
Chain B, Isopentenylpyrophosphate-Dimethylallylpyrophosphate




Isomerase: Complex Of C67a Mutant With Eipp
















TABLE 14







Examples of FPP synthase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





Q92250
2497455
Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyl




diphosphate synthetase)


XP_363065
39948036
hypothetical protein MG08649.4 [Magnaporthe grisea 70-15]


XP_386960
46124813
FPPS_GIBFU Farnesyl pyrophosphate synthetase (FPP synthetase)




(FPS) [Gibberella zeae PH-1]


Q92235
3122099
Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyl




diphosphate synthetase)


XP_412149
49116518
hypothetical protein AN8012.2 [Aspergillus nidulans FGSC A4]


XP_503599
50552378
hypothetical protein [Yarrowia lipolytica]


NP_593299
19114211
farnesyl pyrophosphate synthetase [Schizosaccharomyces pombe]


CAD42869
21955860
farnesyl pyrophosphate synthase [Mucor circinelloides f. lusitanicus]


XP_448787
50292709
unnamed protein product [Candida glabrata]


NP_012368
6322294
Erg20p [Saccharomyces cerevisiae]


T42081
7433997
farnesyl-pyrophosphate synthetase - fission yeast




(Schizosaccharomyces pombe) (fragment)


EAK93751
46434339
likely farnesyl diphosphate synthetase [Candida albicans SC5314]


XP_451300
50302727
FPPS_KLULA [Kluyveromyces lactis]


XP_571137
58267962
isoprenoid biosynthesis-related protein, putative [Cryptococcus




neoformans var. neoformans JEC21]


XP_460720
50424267
unnamed protein product [Debaryomyces hansenii]


NP_984739
45190485
AEL122Wp [Eremothecium gossypii]


BAD15361
46367743
farnesyl diphosphate synthase [Lactarius chrysorrheus]


S71433
7433991
farnesyl-pyrophosphate synthetase - ergot fungus (fragment)


CAA65643
1523990
farnesyl pyrophosphate synthetase [Claviceps purpurea]


XP_399061
49069544
hypothetical protein UM01446.1 [Ustilago maydis 521]


S71432
7433990
farnesyl-pyrophosphate synthetase - Sphaceloma manihoticola




(fragment)


AAH68912
46249832
MGC83119 protein [Xenopus laevis]


1FPS
1065289
Chain, Avian Farnesyl Diphosphate Synthase (Fps) (E.C.2.5.1.10)


P08836
3915686
Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyl




diphosphate synthetase)


AAH83515
53733369
Unknown (protein for IMAGE:7049076) [Danio rerio]


1UBX
1942050
Chain, Structure Of Farnesyl Pyrophosphate Synthetase


1UBY
1942051
Chain, Structure Of Farnesyl Pyrophosphate Synthetase


AAF37872
7188788
farnesyl diphosphate synthase [Dictyostelium discoideum]


NP_803463
29135293
farnesyl diphosphate synthase [Bos taurus]


AAK63847
14488053
farnesyl diphosphate synthase [Mentha × piperita]


AAV58896
55710092
farnesyl diphosphate synthase [Centella asiatica]


T06272
7433988
farnesyl-pyrophosphate synthetase FPS1 - tomato


JC4846
2117737
farnesyl-pyrophosphate synthetase - Artemisia annua


P05369
120478
Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyl




diphosphate synthetase)


O24241
25452945
Farnesyl pyrophosphate synthetase 1 (FPP synthetase 1)


O24242
25452946
Farnesyl pyrophosphate synthetase 2 (FPP synthetase 2)


AAH59125
37590777
Testis-specific farnesyl pyrophosphate synthetase [Rattus norvegicus]


AAH48497
28913418
Farnesyl diphosphate synthetase [Mus musculus]


AAP74720
32329199
farnesyl diphosphate synthase [Artemisia tridentata subsp. spiciformis]


CAG11850
47225367
unnamed protein product [Tetraodon nigroviridis]


AAM51429
21436457
putative farnesyl-pyrophosphate synthetase FPS2 [Arabidopsis thaliana]


AAP74719
32329197
farnesyl diphosphate synthase [Artemisia tridentata subsp. spiciformis]


AAM08927
20135548
farnesyl pyrophosphate synthase [Malus × domestica]


XP_537252
57089113
PREDICTED: similar to farnesyl diphosphate synthase [Canis




familiaris]


AAQ56011
34013692
farnesyl diphosphate synthase [Hevea brasiliensis]


AAQ14872
33340604
truncated geranylgeranyl-diphosphate synthase [Zea mays]


AAQ14871
33340602
geranylgeranyl-diphosphate synthase [Zea mays]


AAD17204
4324960
farnesyl diphosphate synthase [Artemisia annua]


AAH87886
56789674
Farnesyl diphosphate synthetase [Mus musculus]


AAK68152
14573639
farnesyldiphosphate synthase [×Citrofortunella microcarpa]


AAA52423
182399
farnesyl pyrophosphate synthetase (EC 2.5.1.1)


S66470
2129849
farnesyl-pyrophosphate synthetase fps1 - white lupine


CAA29064
4725
unnamed protein product [Saccharomyces cerevisiae]


CAI12715
55957735
farnesyl diphosphate synthase [Homo sapiens]


BAA03523
40788949
KIAA1293 [Homo sapiens]


P14324
1346031
Farnesyl pyrophosphate synthetase (FPP synthetase)


S66471
2129850
farnesyl-pyrophosphate synthetase fps2 - white lupine


AAA35820
182405
farnesyl pyrophosphate synthetase


CAA59170
1491641
dimethylallyltransferase [Capsicum annuum]


BAB16687
15289750
putative FPP synthase 1 [Eucommia ulmoides]


CAA72793
1922251
farnesyl pyrophosphate synthase [Gossypium arboreum]


CAH91070
55728661
hypothetical protein [Pongo pygmaeus]


AAK58594
14279425
farnesyl pyrophosphate synthase [Humulus lupulus]


AAB07264
1146159
farnesyl diphosphate synthase short form [Arabidopsis thaliana]


Q09152
21431776
Farnesyl pyrophosphate synthetase 1, mitochondrial precursor (FPP




synthetase 1)


O64905
6016044
Farnesyl pyrophosphate synthetase (FPP synthetase)


BAB60822
14422406
putative FPP synthase 2 [Eucommia ulmoides]


S52009
1076319
farnesyl-pyrophosphate synthetase FPS1 - Arabidopsis thaliana


NP_917118
34911542
putative farnesyl-pyrophosphate synthetase [Oryza sativa (japonica




cultivar-group)]


AAD32648
4894899
farnesyl diphosphate synthase [Artemisia annua]


AAA40960
203582
cholesterol-regulated protein CR39


AAR27053
38684029
farnesyl diphosphate synthetase [Ginkgo biloba]


AAU43998
52353430
putative farnesyl pyrophosphate synthase [Oryza sativa (japonica




cultivar-group)]


AAL82595
18958450
farnesyl pyrophosphare synthase [Musa acuminata]


NP_917069
34911444
putative farnesyl-pyrophosphate synthetase [Oryza sativa (japonica




cultivar-group)]


XP_228802
34879769
similar to testis-specific farnesyl pyrophosphate synthetase [Rattus




norvegicus]


BAD81810
56785155
putative farnesyl-pyrophosphate synthetase fps2 [Oryza sativa (japonica




cultivar-group)]


AAN62522
24796660
farnesyl pyrophosphate synthetase [Eucommia ulmoides]


NP_595334
19112126
farnesyl pyrophosphate synthetase [Schizosaccharomyces pombe]


T52066
25458583
probable farnesyl pyrophosphate synthase [imported] - rice


AAL49067
17946048
RE52884p [Drosophila melanogaster]


CAA08919
3395483
dimethylallyltransferase; farnesyl pyrophosphate synthase [Drosophila




melanogaster]


XP_547662
57089869
PREDICTED: similar to farnesyl diphosphate synthase [Canis




familiaris]


EAL26135
54636732
GA11601-PA [Drosophila pseudoobscura]


BAB60821
14422404
putative FPP synthase 1 [Eucommia ulmoides]


AAP74721
32329201
chrysanthemyl diphosphate synthase [Artemisia tridentata subsp.




spiciformis]


XP_496902
51466663
PREDICTED: similar to Farnesyl pyrophosphate synthetase (FPP




synthetase) [Homo sapiens]


XP_474182
50929309
OSJNBa0071I13.18 [Oryza sativa (japonica cultivar-group)]


CAA87327
1160178
partial sequence [Homo sapiens]


BAD20729
47776234
farnesyl pyrophosphate synthase [Candida glabrata]


BAC53873
30984142
farnesyl pyrophosphate synthase [Phaseolus lunatus]


BAB69490
15991313
farnesyl pyrophosphate syntase [Bombyx mori]


NP_974565
42572937
farnesyl pyrophosphate synthetase 2 (FPS2)/FPP synthetase 2




[Arabidopsis thaliana]


CAA08918
5678609
dimethylallyltransferase; farnesyl pyrophosphate synthase [Agrotis




ipsilon]


AAP86267
32527731
Ac2-125 [Rattus norvegicus]


AAO17735
30522953
farnesyl pyrophosphate synthase [Trypanosoma brucei]


AAK71861
14647139
farnesyl pyrophosphate synthase [Trypanosoma cruzi]


AAL73357
18478919
farnesyl diphosphate synthase precursor [Trypanosoma cruzi]


AAO63552
29124957
putative farnesyl pyrophosphate synthase [Plasmodium falciparum]


CAI00471
56498227
farnesyl pyrophosphate synthase, putative [Plasmodium berghei]


NP_701155
23508486
farnesyl pyrophosphate synthase, putative [Plasmodium falciparum




3D7]


XP_474180
50929305
OSJNBa0071I13.16 [Oryza sativa (japonica cultivar-group)]


AAL73358
18478922
farnesyl diphosphate synthase precursor [Trypanosoma cruzi]


EAH48995
44167328
unknown [environmental sequence]


NP_493027
17508563
farnesyl pyrophosphate synthetase (1M510) [Caenorhabditis elegans]


CAE71711
39580204
Hypothetical protein CBG18688 [Caenorhabditis briggsae]


XP_487220
51766977
similar to farnesyl pyrophosphate synthase [Mus musculus]
















TABLE 15







Examples of GGPP synthase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





AAT92871
51013155
YPL069C [Saccharomyces cerevisiae]


XP_447025
50289191
unnamed protein product [Candida glabrata]


NP_984623
45190369
AEL238Cp [Eremothecium gossypii]


XP_390273
46137163
GGPP_GIBFU Geranylgeranyl pyrophosphate synthetase (GGPP




synthetase) [Gibberella zeae PH-1]


XP_404791
49085320
hypothetical protein AN0654.2 [Aspergillus nidulans FGSC A4]


XP_368486
39974191
hypothetical protein MG00758.4 [Magnaporthe grisea 70-15]


Q92236
6831550
Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)


AAO85432
29468176
geranylgeranyl diphosphate synthase [Aspergillus nidulans]


XP_572774
58271236
farnesyltranstransferase, putative [Cryptococcus neoformans var.




neoformans JEC21]


XP_502923
50550901
hypothetical protein [Yarrowia lipolytica]


AAK11525
13021716
geranylgeranyl pyrophosphate synthase [Penicillium paxilli]


XP_326920
32412880
GERANYLGERANYL PYROPHOSPHATE SYNTHETASE (GGPP




SYNTHETASE) [Neurospora crassa]


CAF32032
42820719
geranylgeranyl pyrophosphate synthetase, putative [Aspergillus




fumigatus]


BAD29965
50355599
Phoma betae geranylgeranyl diphosphate synthase


XP_384767
46117498
hypothetical protein FG04591.1 [Gibberella zeae PH-1]


BAD29970
50355631
geranylgeranyldiphosphate synthase [Phoma betae]


CAB89115
7649674
geranylgeranyl pyrophosphate synthase [Mucor circinelloides f. lusitanicus]


CAG09545
47229030
unnamed protein product [Tetraodon nigroviridis]


CAI13753
55960163
geranylgeranyl diphosphate synthase 1 [Homo sapiens]


AAH69913
47124116
Geranylgeranyl diphosphate synthase 1 [Mus musculus]


AAH67768
45709211
GGPS1 protein [Homo sapiens]


XP_455003
50309979
unnamed protein product [Kluyveromyces lactis]


P56966
9296978
Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)


NP_001007
56090562
geranylgeranyl diphosphate synthase 1 [Rattus norvegicus]


AAT65717
49409613
geranylgeranyl diphosphate synthase [Aspergillus flavus]


NP_956329
41053321
geranylgeranyl diphosphate synthase 1 [Danio rerio]


BAA90525
6899844
geranylgeranyl diphosphate synthase [Nigrospora sphaerica]


XP_405729
49087630
hypothetical protein AN1592.2 [Aspergillus nidulans FGSC A4]


AAK11531
13021724
geranylgeranyl pyrophosphate synthase [Penicillium paxilli]


XP_412280
49119197
hypothetical protein AN8143.2 [Aspergillus nidulans FGSC A4]


AAC05273
2944400
geranylgeranyl pyrophosphate synthase [Drosophila melanogaster]


NP_523958
24660002
CG8593-PA [Drosophila melanogaster]


XP_402074
49076128
hypothetical protein UM04459.1 [Ustilago maydis 521]


EAL30191
54641441
GA21189-PA [Drosophila pseudoobscura]


XP_536340
57084951
PREDICTED: hypothetical protein XP_536340 [Canis familiaris]


XP_424685
50811194
PREDICTED: similar to geranylgeranyl diphosphate synthase 1, partial




[Gallus gallus]


AAH06798
13905030
Ggps1 protein [Mus musculus]


AAP06018
29841005
similar to NM_010282 geranylgeranyl diphosphate synthase 1; GGPP




synthase [Schistosoma japonicum]


XP_460338
50423511
unnamed protein product [Debaryomyces hansenii]


AAC05595
2957271
geranylgeranyl pyrophosphate synthase [Drosophila melanogaster]


EAK92197
46432727
hypothetical protein CaO19.6674 [Candida albicans SC5314]


XP_535573
57108760
PREDICTED: similar to geranylgeranyl diphosphate synthase 1 [Canis




familiaris]


AAH83212
53734594
Zgc:56514 protein [Danio rerio]


XP_486466
51827552
similar to geranylgeranyl diphosphate synthase 1; GGPP synthase [Mus




musculus]


CAH18006
51469024
geranylgeranyl diphosphate synthase [Fusarium proliferatum]


CAA75568
3549881
geranylgeranyl diphosphate synthase [Gibberella fujikuroi]


XP_397455
48143654
similar to CG8593-PA [Apis mellifera]


XP_410947
49101294
hypothetical protein AN6810.2 [Aspergillus nidulans FGSC A4]


XP_381914
46109712
hypothetical protein FG01738.1 [Gibberella zeae PH-1]


XP_364478
39959279
hypothetical protein MG09448.4 [Magnaporthe grisea 70-15]


XP_360889
39942704
hypothetical protein MG03432.4 [Magnaporthe grisea 70-15]


XP_369218
39975655
hypothetical protein MG00026.4 [Magnaporthe grisea 70-15]


XP_406544
49089926
hypothetical protein AN2407.2 [Aspergillus nidulans FGSC A4]


XP_367595
39972409
hypothetical protein MG07506.4 [Magnaporthe grisea 70-15]


XP_363775
39952117
hypothetical protein MG01701.4 [Magnaporthe grisea 70-15]


XP_368486
39974191
hypothetical protein MG00758.4 [Magnaporthe grisea 70-15]


XP_390273
46137163
GGPP_GIBFU Geranylgeranyl pyrophosphate synthetase (GGPP




synthetase) [Gibberella zeae PH-1]


Q92236
6831550
Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)


AAK11525
13021716
geranylgeranyl pyrophosphate synthase [Penicillium paxilli]


CAF32032
42820719
geranylgeranyl pyrophosphate synthetase, putative [Aspergillus




fumigatus]


XP_404791
49085320
hypothetical protein AN0654.2 [Aspergillus nidulans FGSC A4]


AAO85432
29468176
geranylgeranyl diphosphate synthase [Aspergillus nidulans]


BAD29965
50355599
Phoma betae geranylgeranyl diphosphate synthase


BAD29970
50355631
geranylgeranyldiphosphate synthase [Phoma betae]


BAA90525
6899844
geranylgeranyl diphosphate synthase [Nigrospora sphaerica]


AAT65717
49409613
geranylgeranyl diphosphate synthase [Aspergillus flavus]


XP_384767
46117498
hypothetical protein FG04591.1 [Gibberella zeae PH-1]


CAB89115
7649674
geranylgeranyl pyrophosphate synthase [Mucor circinelloides f. lusitanicus]


XP_572774
58271236
farnesyltranstransferase, putative [Cryptococcus neoformans var.




neoformans JEC21]


AAK11531
13021724
geranylgeranyl pyrophosphate synthase [Penicillium paxilli]


XP_502923
50550901
hypothetical protein [Yarrowia lipolytica]


CAI13753
55960163
geranylgeranyl diphosphate synthase 1 [Homo sapiens]


CAG09545
47229030
unnamed protein product [Tetraodon nigroviridis]


XP_412280
49119197
hypothetical protein AN8143.2 [Aspergillus nidulans FGSC A4]


P56966
9296978
Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)


NP_001007
56090562
geranylgeranyl diphosphate synthase 1 [Rattus norvegicus]


AAH69913
47124116
Geranylgeranyl diphosphate synthase 1 [Mus musculus]


AAH67768
45709211
GGPS1 protein [Homo sapiens]


NP_956329
41053321
geranylgeranyl diphosphate synthase 1 [Danio rerio]


EAL30191
54641441
GA21189-PA [Drosophila pseudoobscura]


XP_424685
50811194
PREDICTED: similar to geranylgeranyl diphosphate synthase 1, partial




[Gallus gallus]


XP_536340
57084951
PREDICTED: hypothetical protein XP_536340 [Canis familiaris]


NP_523958
24660002
CG8593-PA [Drosophila melanogaster]


AAC05273
2944400
geranylgeranyl pyrophosphate synthase [Drosophila melanogaster]


XP_405729
49087630
hypothetical protein AN1592.2 [Aspergillus nidulans FGSC A4]


AAC05595
2957271
geranylgeranyl pyrophosphate synthase [Drosophila melanogaster]


XP_402074
49076128
hypothetical protein UM04459.1 [Ustilago maydis 521]


AAP06018
29841005
similar to NM_010282 geranylgeranyl diphosphate synthase 1; GGPP




synthase [Schistosoma japonicum]


AAH06798
13905030
Ggps1 protein [Mus musculus]


XP_535573
57108760
PREDICTED: similar to geranylgeranyl diphosphate synthase 1 [Canis




familiaris]


AAH83212
53734594
Zgc: 56514 protein [Danio rerio]


AAP21085
30097620
albino-3 [Neurospora crassa]


NP_984623
45190369
AEL238Cp [Eremothecium gossypii]


XP_447025
50289191
unnamed protein product [Candida glabrata]


AAT92871
51013155
YPL069C [Saccharomyces cerevisiae]


XP_486466
51827552
similar to geranylgeranyl diphosphate synthase 1; GGPP synthase [Mus




musculus]


XP_410947
49101294
hypothetical protein AN6810.2 [Aspergillus nidulans FGSC A4]


XP_397455
48143654
similar to CG8593-PA [Apis mellifera]


XP_455003
50309979
unnamed protein product [Kluyveromyces lactis]


EAK92197
46432727
hypothetical protein CaO19.6674 [Candida albicans SC5314]


XP_381914
46109712
hypothetical protein FG01738.1 [Gibberella zeae PH-1]


XP_460338
50423511
unnamed protein product [Debaryomyces hansenii]


CAH18006
51469024
geranylgeranyl diphosphate synthase [Fusarium proliferatum]


XP_360889
39942704
hypothetical protein MG03432.4 [Magnaporthe grisea 70-15]


XP_406544
49089926
hypothetical protein AN2407.2 [Aspergillus nidulans FGSC A4]


XP_364478
39959279
hypothetical protein MG09448.4 [Magnaporthe grisea 70-15]


XP_363775
39952117
hypothetical protein MG01701.4 [Magnaporthe grisea 70-15]


XP_367595
39972409
hypothetical protein MG07506.4 [Magnaporthe grisea 70-15]


XP_369218
39975655
hypothetical protein MG00026.4 [Magnaporthe grisea 70-15]


C39273
483124
phytoene synthase - Erwinia herbicola


BAB79600
18143445
crtE [Pantoea agglomerans pv. milletiae]


BAA14124
216682
crtE [Pantoea ananatis]


AAN85596
27228290
Geranylgeranyl Pyrophosphate Synthase [Pantoea stewartii]


AAA32797
413730
geranylgeranyl pyrophosphate synthase


Q08291
585326
Geranyltranstransferase (Farnesyl-diphosphate synthase) (FPP synthase)


S52584
1073293
crtE protein - Erwinia herbicola


S53722
1076576
farnesyltranstransferase (EC 2.5.1.29) precursor - pepper


AAC44848
1842242
geranylgeranyl synthase


BAA19583
1944371
geranylgeranyl pyrophosphate synthase [Arabidopsis thaliana]


S71230
2129674
geranylgeranyl pyrophosphate synthase (EC 2.5.1.—) 2 precursor -




Arabidopsis thaliana


BAA23157
2578822
geranyl geranyl pyrophosphate synthase [Arabidopsis thaliana]


AAC77874
3885426
geranylgeranyl pyrophosphate synthase [Helianthus annuus]


CAB38744
4490594
geranylgeranyl pyrophosphate synthase [Rhodobacter sphaeroides]


BAA78047
4958920
GGPP synthase [Daucus carota]


BAA82613
5631295
geranylgeranyl diphosphate synthase (SelGGPS) [Synechococcus




elongatus]


CAB56064
5912297
geranylgeranyl pyrophosphate synthase [Paracoccus marcusii]


BAA86284
6277254
geranylgeranyl pyrophosphate synthase [Croton sublyratus]


T11021
7447356
farnesyltranstransferase (EC 2.5.1.29) - white lupine


AAF78199
8650415
geranylgeranyl synthase [Bradyrhizobium sp. ORS278]


AAG10424
9971808
GGDP synthase [Tagetes erecta]


CAC10561
10637876
gpp synthase large subunit [Mentha × piperita]


T50879
11279298
phytoene synthase [imported] - Rubrivivax gelatinosus


BAB01343
11994221
geranyl geranyl pyrophosphate synthase-like protein [Arabidopsis




thaliana]


Q42698
13431546
Geranylgeranyl pyrophosphate synthetase, chloroplast precursor (GGPP




synthetase)


Q43133
13431547
Geranylgeranyl pyrophosphate synthetase, chloroplast precursor (GGPP




synthetase)


P54976
13878921
Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)




(Farnesyltranstransferase)


BAB50600
14023995
geranyltranstransferase; farnesyl-diphosphate synthase [Mesorhizobium




loti MAFF303099]


BAB60678
14325238
geranylgeranyl diphosphate synthase [Hevea brasiliensis]


BAB60820
14422402
putative GGPP synthase [Eucommia ulmoides]


NP_189589
15228704
geranylgeranyl pyrophosphate synthase, putative/GGPP synthetase




[Arabidopsis thaliana]


NP_188651
15231055
geranylgeranyl pyrophosphate synthase, putative/GGPP synthetase




[Arabidopsis thaliana]


NP_188069
15231869
geranylgeranyl pyrophosphate synthase, putative/GGPP synthetase




[Arabidopsis thaliana]


NP_188073
15231881
geranylgeranyl pyrophosphate synthase, putative/GGPP synthetase




[Arabidopsis thaliana]


AAL01997
15553715
farnesyl diphosphate synthase [Xanthobacter sp. Py2]


AAL01998
15553717
geranylgeranyl diphosphate synthase [Xanthobacter sp. Py2]


NP_252732
15599238
geranyltranstransferase [Pseudomonas aeruginosa PAO1]


NP_245470
15602398
IspA [Pasteurella multocida subsp. multocida str. Pm70]


NP_390308
16079484
hypothetical protein BSU24280 [Bacillus subtilis subsp. subtilis str. 168]


NP_440010
16329282
geranylgeranyl pyrophosphate synthase [Synechocystis sp. PCC 6803]


NP_440010
16329282
geranylgeranyl pyrophosphate synthase [Synechocystis sp. PCC 6803]


AAL17614
17352451
geranylgeranyl diphosphate synthase [Abies grandis]


NP_520343
17546941
PROBABLE GERANYLTRANSTRANSFERASE (FARNESYL-




DIPHOSPHATE SYNTHASE) PROTEIN [Ralstonia solanacearum GM


AAL76349
18645048
geranyltranstransferase [uncultured proteobacterium]


AAM21638
20386366
geranylgeranyl pyrophosphate synthase [Cistus incanus subsp. creticus]


AAM21639
20386368
geranylgeranyl pyrophosphate synthase [Cistus incanus subsp. creticus]


NP_622916
20807745
Geranylgeranyl pyrophosphate synthase [Thermoanaerobacter




tengcongensis MB4]


AAM48650
21328644
geranylgeranyl pyrophosphate synthetase [uncultured proteobacterium]


NP_659794
21492720
probable polyprenyl synthetase. [Rhizobium etli]


AAM64496
21592547
putative geranylgeranyl pyrophosphate synthase GGPS3 [Arabidopsis




thaliana]


AAM65107
21593158
geranylgeranyl pyrophosphate synthase [Arabidopsis thaliana]


NP_680811
22297564
geranylgeranyl pyrophosphate synthase [Thermosynechococcus




elongatus BP-1]


ZP_000474
23003800
COG0142: Geranylgeranyl pyrophosphate synthase [Lactobacillus




gasseri]


ZP_001252
23469933
COG0142: Geranylgeranyl pyrophosphate synthase [Pseudomonas




syringae pv. syringae B728a]


NP_698760
23502633
geranyltranstransferase [Brucella suis 1330]


E84566
25313373
probable geranylgeranyl pyrophosphate synthase [imported] -




Arabidopsis thaliana


F85434
25313385
geranylgeranyl pyrophosphate synthase [imported] - Arabidopsis




thaliana


AC1245
25313389
geranyltranstransferase homolog lmo1363 [imported] - Listeria




monocytogenes (strain EGD-e)


E83997
25313393
geranyltranstransferase BH2781 [imported] - Bacillus halodurans (strain




C-125)


G84566
25313395
probable geranylgeranyl pyrophosphate synthase [imported] -




Arabidopsis thaliana


AH2910
25315863
geranyltranstransferase [imported] - Agrobacterium tumefaciens (strain




C58, Dupont)


D87505
25398795
geranyltranstransferase [imported] - Caulobacter crescentus


A89932
25505949
hypothetical protein ispA [imported] - Staphylococcus aureus (strain




N315)


F97685
25520741
geranyltransferase (AF203881) [imported] - Agrobacterium tumefaciens




(strain C58, Cereon)


AI3285
25527013
geranyltranstransferase (EC 2.5.1.10) [imported] - Brucella melitensis




(strain 16M)


BAC42571
26450928
putative geranylgeranyl pyrophosphate synthase GGPS3 [Arabidopsis




thaliana]


NP_785195
28378303
geranyltranstransferase [Lactobacillus plantarum WCFS1]


NP_790546
28867927
geranyltranstransferase [Pseudomonas syringae pv. tomato str. DC3000]


AAO63392
28950937
At2g23800 [Arabidopsis thaliana]


AAO93113
29893480
geranylgeranyl pyrophosphate synthetase; CrtE [Rubrivivax




gelatinosus]


NP_833891
30022260
Dimethylallyltransferase [Bacillus cereus ATCC 14579]


AAP59037
31621279
CrtE [Thiocapsa roseopersicina]


ZP_001374
32039216
COG0142: Geranylgeranyl pyrophosphate synthase [Pseudomonas




aeruginosa UCBPP-PA14]


NP_864766
32471772
geranylgeranyl pyrophosphate synthetase [precursor] [Rhodopirellula




baltica SH 1]


NP_875521
33240579
Geranylgeranyl pyrophosphate synthase [Prochlorococcus marinus




subsp. marinus str. CCMP1375]


NP_881399
33593755
probable geranyltranstransferase [Bordetella pertussis Tohama I]


NP_884694
33597051
probable geranyltranstransferase [Bordetella parapertussis 12822]


NP_888456
33600896
probable geranyltranstransferase [Bordetella bronchiseptica RB50]


NP_893187
33861626
Polyprenyl synthetase [Prochlorococcus marinus subsp. pastoris str.




CCMP1986]


NP_894940
33863380
Polyprenyl synthetase [Prochlorococcus marinus str. MIT 9313]


NP_896835
33865276
geranylgeranyl pyrophosphate synthase [Synechococcus sp. WH 8102]


NP_896835
33865276
geranylgeranyl pyrophosphate synthase [Synechococcus sp. WH 8102]


AAQ65086
34365549
At3g14530 [Arabidopsis thaliana]


NP_945877
39933601
putative geranyltranstransferase (farnesyl-diphosphate synthase)




[Rhodopseudomonas palustris CGA009]


NP_946867
39934591
geranylgeranyl pyrophosphate synthase [Rhodopseudomonas palustris




CGA009]


NP_952815
39996864
geranyltranstransferase [Geobacter sulfurreducens PCA]


AAR37805
40062934
polyprenyl synthetase [uncultured bacterium 442]


AAR37858
40062988
geranylgeranyl pyrophosphate synthetase [uncultured bacterium 443]


AAR98495
41018904
geranyl geranyl synthase [Bradyrhizobium sp. ORS278]


AAR99082
41059107
geranylgeranyl pyrophosphate synthase [Plectranthus barbatus]


NP_965349
42519419
geranyltranstransferase [Lactobacillus johnsonii NCC 533]


NP_980544
42783297
geranyltranstransferase [Bacillus cereus ATCC 10987]


EAA96348
42858148
unknown [environmental sequence]


EAB36506
42939031
unknown [environmental sequence]


EAB36642
42939300
unknown [environmental sequence]


EAC39208
43146996
unknown [environmental sequence]


EAD26007
43320598
unknown [environmental sequence]


EAE43084
43576643
unknown [environmental sequence]


EAE70061
43630884
unknown [environmental sequence]


EAF70308
43832107
unknown [environmental sequence]


EAG88494
44055952
unknown [environmental sequence]


EAH52060
44173220
unknown [environmental sequence]


EAH78354
44221788
unknown [environmental sequence]


EAH84117
44231960
unknown [environmental sequence]


EAI11762
44272832
unknown [environmental sequence]


EAI49391
44328289
unknown [environmental sequence]


EAI54846
44336042
unknown [environmental sequence]


EAI68356
44355138
unknown [environmental sequence]


EAI68713
44355672
unknown [environmental sequence]


EAI69401
44356609
unknown [environmental sequence]


EAI73873
44362658
unknown [environmental sequence]


EAJ73634
44506168
unknown [environmental sequence]


EAJ77351
44511694
unknown [environmental sequence]


EAK70639
44644254
unknown [environmental sequence]


ZP_001751
45523854
COG0142: Geranylgeranyl pyrophosphate synthase [Crocosphaera




watsonii WH 8501]


AAS76253
45752710
At1g49530 [Arabidopsis thaliana]


ZP_001957
45916757
COG0142: Geranylgeranyl pyrophosphate synthase [Mesorhizobium sp.




BNC1]


1RTRB
46015556
Chain B, Crystal Structure Of S. Aureus Farnesyl Pyrophosphate




Synthase


ZP_001863
46105954
COG0142: Geranylgeranyl pyrophosphate synthase [Rubrobacter




xylanophilus DSM 9941]


ZP_002002
46107045
COG0142: Geranylgeranyl pyrophosphate synthase [Rubrobacter




xylanophilus DSM 9941]


ZP_001711
46132567
COG0142: Geranylgeranyl pyrophosphate synthase [Ralstonia eutropha




JMP134]


ZP_002073
46192680
COG0142: Geranylgeranyl pyrophosphate synthase [Rhodobacter




sphaeroides 2.4.1]


ZP_002074
46192861
COG0142: Geranylgeranyl pyrophosphate synthase [Rhodobacter




sphaeroides 2.4.1]


AAS82860
46241274
geranyl diphosphate synthase large subunit [Antirrhinum majus]


ZP_002108
46308696
COG0142: Geranylgeranyl pyrophosphate synthase [Ehrlichia canis str.




Jake]


YP_010568
46579760
geranylgeranyl diphosphate synthase [Desulfovibrio vulgaris subsp.




vulgaris str. Hildenborough]


BAD18313
47076770
geranyltranstransferase [Geobacillus stearothermophilus]


ZP_002315
47093750
geranyltranstransferase [Listeria monocytogenes str. 4b H7858]


ZP_002335
47095946
geranyltranstransferase [Listeria monocytogenes str. 1/2a F6854]


AAT35222
47531118
fusion of carotene synthesis proteins [synthetic construct]


ZP_002401
47569437
geranyltranstransferase [Bacillus cereus G9241]


ZP_002435
47573473
COG0142: Geranylgeranyl pyrophosphate synthase [Rubrivivax




gelatinosus PM1]


ZP_002626
48728941
COG0142: Geranylgeranyl pyrophosphate synthase [Pseudomonas




fluorescens PfO-1]


ZP_002702
48765678
COG0142: Geranylgeranyl pyrophosphate synthase [Rhodospirillum




rubrum]


ZP_002705
48766028
COG0142: Geranylgeranyl pyrophosphate synthase [Rhodospirillum




rubrum]


ZP_002732
48768894
COG0142: Geranylgeranyl pyrophosphate synthase [Ralstonia




metallidurans CH34]


ZP_002914
48834438
COG0142: Geranylgeranyl pyrophosphate synthase [Magnetococcus sp.




MC-1]


ZP_003024
48848203
COG0142: Geranylgeranyl pyrophosphate synthase [Novosphingobium




aromaticivorans DSM 12444]


ZP_003129
48858958
COG0142: Geranylgeranyl pyrophosphate synthase [Clostridium




thermocellum ATCC 27405]


ZP_003177
48863841
COG0142: Geranylgeranyl pyrophosphate synthase [Microbulbifer




degradans 2-40]


ZP_003225
48869790
COG0142: Geranylgeranyl pyrophosphate synthase [Pediococcus




pentosaceus ATCC 25745]


AAT51323
49086036
PA4043 [synthetic construct]


ZP_003301
49236117
COG0142: Geranylgeranyl pyrophosphate synthase [Moorella




thermoacetica ATCC 39073]


YP_034222
49476181
Geranyltranstransferase (farnesyl-diphosphate synthase) [Bartonella




henselae str. Houston-1]


YP_040995
49483771
putative geranyltranstransferase [Staphylococcus aureus subsp. aureus




MRSA252]


YP_043579
49486358
putative geranyltranstransferase [Staphylococcus aureus subsp. aureus




MSSA476]


AAT71982
50253560
At3g32040 [Arabidopsis thaliana]


AAT90315
50952782
putative geranylgeranyl pyrophosphate synthetase [uncultured




proteobacterium eBACred25D05]


YP_066435
51246551
probable geranylgeranyl pyrophosphate synthase [Desulfotalea




psychrophila LSv54]


YP_075673
51892982
geranylgeranyl pyrophosphate synthase [Symbiobacterium




thermophilum IAM 14863]


YP_085511
52141318
geranyltranstransferase [Bacillus cereus ZK]


YP_092166
52786337
YqiD [Bacillus licheniformis ATCC 14580]


ZP_001298
53691368
COG0142: Geranylgeranyl pyrophosphate synthase [Desulfovibrio




desulfuricans G20]


YP_105136
53716444
geranyltranstransferase [Burkholderia mallei ATCC 23344]


YP_111769
53722784
geranyltranstransferase [Burkholderia pseudomallei K96243]


ZP_003630
54030933
COG0142: Geranylgeranyl pyrophosphate synthase [Polaromonas sp.




JS666]


YP_129021
54308001
putative geranyltranstransferase [Photobacterium profundum SS9]


AAV74395
56122554
geranylgeranyl diphosphate synthase [Adonis palaestina]


AAV74396
56122556
geranylgeranyl diphosphate synthase [Adonis palaestina]


YP_148246
56420928
geranyltranstransferase (farnesyl-diphosphate synthase) [Geobacillus




kaustophilus HTA426]


YP_156518
56461237
Geranylgeranyl pyrophosphate synthase [Idiomarina loihiensis L2TR]


YP_162590
56551751
geranyltranstransferase [Zymomonas mobilis subsp. mobilis ZM4]


YP_171470
56750769
geranylgeranyl pyrophosphate synthase [Synechococcus elongatus PCC




6301]


YP_175959
56964228
geranyltranstransferase [Bacillus clausii KSM-K16]


YP_186407
57650478
geranyltranstransferase [Staphylococcus aureus subsp. aureus COL]


YP_190690
58038726
Dimethylallyltransferase [Gluconobacter oxydans 621H]


AAW66658
58201026
geranyl diphosphate synthase [Picrorhiza kurrooa]


YP_194187
58337602
geranylgeranyl diphosphate (GGPP) synthase [Lactobacillus acidophilus




NCFM]


YP_197469
58579257
Possible geranyltranstransferase [Ehrlichia ruminantium str.




Welgevonden]


YP_201938
58582922
geranyltranstransferase; farnesyl-diphosphate synthase [Xanthomonas




oryzae pv. oryzae KACC10331]


YP_196510
58617311
Possible geranyltranstransferase [Ehrlichia ruminantium str. Gardel]
















TABLE 16







Examples of squalene synthetase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





AAA34597
171481
squalene synthetase


CAA42583
3686
farnesyl-diphosphate farnesyltransferase [Saccharomyces cerevisiae]


Q9HGZ6
51704336
Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)




(SS) (FPP:FPP farnesyltransferase)


BAB12207
9955387
squalene synthase [Candida glabrata]


XP_453457
50306959
unnamed protein product [Kluyveromyces lactis]


Q752X9
51701405
Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)




(SS) (FPP:FPP farnesyltransferase)


O74165
51701378
Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)




(SS) (FPP:FPP farnesyltransferase)


XP_458579
50420093
unnamed protein product [Debaryomyces hansenii]


EAK95451
46436082
hypothetical protein CaO19.11099 [Candida albicans SC5314]


P78589
2499979
Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)




(SS) (FPP:FPP farnesyltransferase)


Q9Y753
51701459
Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)




(SS) (FPP:FPP farnesyltransferase)


XP_407513
49092104
hypothetical protein AN3376.2 [Aspergillus nidulans FGSC A4]


XP_364394
39958237
hypothetical protein MG09239.4 [Magnaporthe grisea 70-15]


Q7S4Z6
51701416
Probable farnesyl-diphosphate farnesyltransferase (Squalene synthetase)


CAD60581
27764301
unnamed protein product [Podospora anserina]


XP_389557
46135731
hypothetical protein FG09381.1 [Gibberella zeae PH-1]


NP_595363
19112155
farnesyl-diphosphate farnesyltransferase [Schizosaccharomyces pombe]


B48057
477750
farnesyl-diphosphate farnesyltransferase (EC 2.5.1.21) - fission yeast




(Schizosaccharomyces pombe )


NP_034321
34328173
farnesyl diphosphate farnesyl transferase 1 [Mus musculus]


CAH92517
55731622
hypothetical protein [Pongo pygmaeus]


AAF00038
6002565
squalene synthase [Mus musculus]


P53798
1706773
Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)




(SS) (FPP:FPP farnesyltransferase)


NP_004453
31542632
farnesyl-diphosphate farnesyltransferase 1 [Homo sapiens]


AAP36671
30584837
Homo sapiens farnesyl-diphosphate farnesyltransferase 1 [synthetic




construct]


1EZFC
11514497
Chain C, Crystal Structure Of Human Squalene Synthase


AAH09251
14328083
Farnesyl-diphosphate farnesyltransferase 1 [Homo sapiens]


AAH84016
54035372
LOC494973 protein [Xenopus laevis]


I52090
2136196
squalene synthase - human


XP_420043
50745256
PREDICTED: similar to Farnesyl-diphosphate farnesyltransferase 1




[Gallus gallus]


AAH81810
51858605
Farnesyl diphosphate farnesyl transferase 1 [Rattus norvegicus]


CAE48363
50841455
TPA: FDFT1 protein [Bos taurus]


XP_569783
58265254
farnesyl-diphosphate farnesyltransferase, putative [Cryptococcus




neoformans var. neoformans JEC21]


XP_569782
58265252
farnesyl-diphosphate farnesyltransferase, putative [Cryptococcus




neoformans var. neoformans JEC21]


XP_534557
57105080
PREDICTED: similar to FDFT1 protein [Canis familiaris]


XP_401989
49075920
FDFT_USTMA Farnesyl-diphosphate farnesyltransferase (Squalene




synthetase) [Ustilago maydis 521]
















TABLE 17a







Examples of phytoene dehydrogenase polypeptides.








ACCESSION
PROTEIN DESCRIPTION





1613414B
crtI gene


1613414F
crtD gene


1904206A
methoxyneurosporene dehydrogenase


2121278A
zeta carotene desaturase


A86203
hypothetical protein [imported] - Arabidopsis thaliana


A96612
hypothetical protein F12K22.18 [imported] - Arabidopsis thaliana


A99470
phytoene dehydrogenase (desaturase) (crtI) [imported] - Sulfolobus solfataricus


AAA24820
phytoene dehydrogenase [Pantoea agglomerans]


AAA34001
phytoene desaturase


AAA50313
photoprotective pigment


AAA64981
phytoene dehydrogenase [Pantoea agglomerans]


AAA91161
zeta-carotene desaturase precursor


AAA99519
phytoene desaturase


AAC44798
hydroxyneurosporene and rhodopin dehydrogenase [Rubrivivax gelatinosus]


AAC44850
phytoene desaturase


AAC48983
phytoene dehydrogenase precursor


AAF78201
phytoene desaturase [Bradyrhizobium sp. ORS278]


AAG10426
phytoene desaturase [Tagetes erecta]


AAG14399
zeta-carotene desaturase precursor [Oryza sativa]


AAG28700
CrtI [Streptomyces griseus]


AAG50743
hypothetical protein [Arabidopsis thaliana]


AAH85048
Unknown (protein for MGC: 97898) [Xenopus laevis]


AAK51545
phytoene desaturase [Citrus × paradisi]


AAK51557
zeta-carotene desaturase precursor [Citrus × paradisi]


AAK64299
phytoene desaturase [Corynebacterium glutamicum]


AAL02000
phytoene dehydrogenase [Xanthobacter sp. Py2]


AAL15300
AT4g14210/dl3145c [Arabidopsis thaliana]


AAL38046
phytoene desaturase [Hordeum vulgare]


AAL73986
hypothetical protein MMT-7 [Mus musculus]


AAL80005
phytoene desaturase [Sandersonia aurantiaca]


AAL91366
carotenoid isomerase [Lycopersicon esculentum]


AAM45380
phytoene desaturase [Tagetes erecta]


AAM48646
phytoene dehydrogenase [uncultured proteobacterium]


AAM63349
putative zeta-carotene desaturase precursor [Arabidopsis thaliana]


AAM94364
phytoene desaturase [Agromyces mediolanus]


AAN75037
CrtD [Rhodospirillum rubrum]


AAN85599
Phytoene Desaturase [Pantoea stewartii]


AAO24235
phytoene desaturase [Crocus sativus]


AAO46892
phytoene dehydrogenase [Blakeslea trispora]


AAO46894
phytoene dehydrogenase [Blakeslea trispora]


AAO53257
phytoene desaturase [Xanthophyllomyces dendrorhous]


AAO53258
phytoene desaturase splice variant [Xanthophyllomyces dendrorhous]


AAO64750
At5g49550/K6M13_10 [Arabidopsis thaliana]


AAO93135
phytoene dehydrogenase; CrtI [Rubrivivax gelatinosus]


AAP59036
CrtD [Thiocapsa roseopersicina]


AAP79175
phytoene dehydrogenase [Bigelowiella natans]


AAQ04224
zeta-carotene desaturase ZDS1 [Malus × domestica]


AAQ04225
zeta-carotene desaturase ZDS2 [Malus × domestica]


AAQ65246
phytoene desaturase [Methylobacterium extorquens]


AAQ65246
phytoene desaturase [Methylobacterium extorquens]


AAQ88931
WLPL439 [Homo sapiens]


AAR37797
methoxyneurosporene dehydrogenase [uncultured bacterium 442]


AAR37802
phytoene dehydrogenase [uncultured bacterium 442]


AAR37850
methoxyneurosporene dehydrogenase [uncultured bacterium 443]


AAR37855
phytoene dehydrogenase [uncultured bacterium 443]


AAR86105
phytoene desaturase [Momordica charantia var. abbreviata]


AAR98491
phytoene desaturase [Bradyrhizobium sp. ORS278]


AAR98494
phytoene dehydrogenase [Bradyrhizobium sp. ORS278]


AAR98733
phytoene desaturase [Lilium longiflorum]


AAS17750
phytoene desaturase [Solanum tuberosum]


AAT01639
phytoene desaturase [Petunia × hybrida]


AAT35222
fusion of carotene synthesis proteins [synthetic construct]


AAT74579
PDS [Citrus sinensis]


AAT74580
ZDS [Citrus sinensis]


AAT76050
zeta-carotene desaturase [Citrus clementina]


AAT76434
phytoene desaturase [Hydrilla verticillata]


AAT90316
putative methoxyneurosporene dehydrogenase [uncultured proteobacterium



eBACred25D05]


AAU34019
retina and RPE/choroid [Macaca fascicularis]


AAW23161
phytoene dehydrogenase [Rhodococcus erythropolis]


AB2035
phytoene desaturase [imported] - Nostoc sp. (strain PCC 7120)


AB2064
hypothetical protein alr2064 [imported] - Nostoc sp. (strain PCC 7120)


AC2446
hypothetical protein all5123 [imported] - Nostoc sp. (strain PCC 7120)


AF1557
phytoene dehydrogenase homolog lin0999 [imported] - Listeria innocua (strain



Clip11262)


AF2029
hypothetical protein alr1788 [imported] - Nostoc sp. (strain PCC 7120)


AG2103
zeta-carotene desaturase [imported] - Nostoc sp. (strain PCC 7120)


AG2509
zeta-carotene desaturase [imported] - Nostoc sp. (strain PCC 7120) plasmid



pCC7120alpha


AH1199
phytoene dehydrogenase homolog lmo1000 [imported] - Listeria monocytogenes



(strain EGD-e)


AI2185
hypothetical protein all3040 [imported] - Nostoc sp. (strain PCC 7120)


AI2273
hypothetical protein all3744 [imported] - Nostoc sp. (strain PCC 7120)


B55548
crtN protein - Staphylococcus aureus


B84327
phytoene dehydrogenase [imported] - Halobacterium sp. NRC-1


B90061
squalene synthase [imported] - Staphylococcus aureus (strain N315)


BAA14127
crtI [Pantoea ananatis]


BAA20276
phytoene desaturase [Erythrobacter longus]


BAA76534
Phytoene disaturase [Acidiphilium rubrum]


BAB10768
phytoene dehydrogenase-like [Arabidopsis thaliana]


BAB50520
phytoene dehydrogenase [Mesorhizobium loti MAFF303099]


BAB51896
mlr5446 [Mesorhizobium loti MAFF303099]


BAB68552
zeta-carotene desaturase [Citrus unshiu]


BAB79603
crtI [Pantoea agglomerans pv. milletiae]


BAB82461
phytoene desaturase [Gentiana lutea]


BAB82462
phytoene desaturase [Gentiana lutea]


BAB98016
Phytoene dehydrogenase and related proteins [Corynebacterium glutamicum ATCC



13032]


BAC75676
putative phytoene desaturase [Gordonia sp. TM414]


BAC77668
phytoene desaturase [marine bacterium P99-3]


BAC77671
gamma-carotene desaturase [marine bacterium P99-3]


BAD07279
phytoene desaturase [Citrus sinensis]


BAD07280
zeta-carotene desaturase [Citrus sinensis]


BAD07287
phytoene desaturase [Citrus limon]


BAD07288
zeta-carotene desaturase [Citrus limon]


CAA52098
squalene synthase [Staphylococcus aureus]


CAA60479
Phytoene desaturase [Haematococcus pluvialis]


CAA66626
unnamed protein product [Staphylococcus aureus]


CAB38739
phytoene dehydrogenase [Rhodobacter sphaeroides]


CAB38743
methoxyneurosporene dehydrogenase [Rhodobacter sphaeroides]


CAB40843
phytoene dehydrogenase [Mucor circinelloides f. lusitanicus]


CAB56041
zeta-carotene desaturase [Nostoc sp. PCC 7120]


CAB56062
phytoene desaturase [Paracoccus marcusii]


CAB59726
phytoene desaturase [Lycopersicon esculentum]


CAB65434
zeta carotene desaturase [Synechococcus leopoliensis]


CAB94794
phytoene dehydrogenase [Mycobacterium aurum]


CAC85667
zeta-carotene desaturase [Citrus sinensis]


CAD19989
phytoene dehydrogenase [Gibberella fujikuroi]


CAD27442
putative zeta-carotene desaturase [Helianthus annuus]


CAD55814
putative zeta-carotene desaturase [Helianthus annuus]


CAE00192
phytoene desaturase [Nicotiana benthamiana]


CAE83576
phytoene desaturase [Nicotiana tabacum]


CAF19330
PHYTOENE DEHYDROGENASE (DESATURASE) [Corynebacterium



glutamicum ATCC 13032]


CAF21094
PHYTOENE DEHYDROGENASE (DESATURASE) (N-terminal fragment)



[Corynebacterium glutamicum ATCC 13032]


CAF21337
phytoene desaturase [Pisum sativum]


CAH91165
hypothetical protein [Pongo pygmaeus]


E90061
hypothetical protein SA2351 [imported] - Staphylococcus aureus (strain N315)


EAA90383
unknown [environmental sequence]


EAA98598
unknown [environmental sequence]


EAB09790
unknown [environmental sequence]


EAB14136
unknown [environmental sequence]


EAB18725
unknown [environmental sequence]


EAB29729
unknown [environmental sequence]


EAB30992
unknown [environmental sequence]


EAB41377
unknown [environmental sequence]


EAB54727
unknown [environmental sequence]


EAB76679
unknown [environmental sequence]


EAB87028
unknown [environmental sequence]


EAB92587
unknown [environmental sequence]


EAB94459
unknown [environmental sequence]


EAB96864
unknown [environmental sequence]


EAC01884
unknown [environmental sequence]


EAC38895
unknown [environmental sequence]


EAC60360
unknown [environmental sequence]


EAD05874
unknown [environmental sequence]


EAD05999
unknown [environmental sequence]


EAD20520
unknown [environmental sequence]


EAE06978
unknown [environmental sequence]


EAE70773
unknown [environmental sequence]


EAF04985
unknown [environmental sequence]


EAF51354
unknown [environmental sequence]


EAF62819
unknown [environmental sequence]


EAF75453
unknown [environmental sequence]


EAG09111
unknown [environmental sequence]


EAG19412
unknown [environmental sequence]


EAG23070
unknown [environmental sequence]


EAG25053
unknown [environmental sequence]


EAG25054
unknown [environmental sequence]


EAG29279
unknown [environmental sequence]


EAG39845
unknown [environmental sequence]


EAG56100
unknown [environmental sequence]


EAG63013
unknown [environmental sequence]


EAG68633
unknown [environmental sequence]


EAG71574
unknown [environmental sequence]


EAG89835
unknown [environmental sequence]


EAH04928
unknown [environmental sequence]


EAH04936
unknown [environmental sequence]


EAH08586
unknown [environmental sequence]


EAH22597
unknown [environmental sequence]


EAH22853
unknown [environmental sequence]


EAH31648
unknown [environmental sequence]


EAH55579
unknown [environmental sequence]


EAH68071
unknown [environmental sequence]


EAH73302
unknown [environmental sequence]


EAH79041
unknown [environmental sequence]


EAH86965
unknown [environmental sequence]


EAH97108
unknown [environmental sequence]


EAH99977
unknown [environmental sequence]


EAI01660
unknown [environmental sequence]


EAI03576
unknown [environmental sequence]


EAI06784
unknown [environmental sequence]


EAI11087
unknown [environmental sequence]


EAI15261
unknown [environmental sequence]


EAI15547
unknown [environmental sequence]


EAI17521
unknown [environmental sequence]


EAI21398
unknown [environmental sequence]


EAI29728
unknown [environmental sequence]


EAI38468
unknown [environmental sequence]


EAI43591
unknown [environmental sequence]


EAI51589
unknown [environmental sequence]


EAI58453
unknown [environmental sequence]


EAI72974
unknown [environmental sequence]


EAI77885
unknown [environmental sequence]


EAI78272
unknown [environmental sequence]


EAI80262
unknown [environmental sequence]


EAI83937
unknown [environmental sequence]


EAI86664
unknown [environmental sequence]


EAJ00517
unknown [environmental sequence]


EAJ05570
unknown [environmental sequence]


EAJ08238
unknown [environmental sequence]


EAJ15524
unknown [environmental sequence]


EAJ18144
unknown [environmental sequence]


EAJ20649
unknown [environmental sequence]


EAJ21683
unknown [environmental sequence]


EAJ24413
unknown [environmental sequence]


EAJ28774
unknown [environmental sequence]


EAJ30522
unknown [environmental sequence]


EAJ35157
unknown [environmental sequence]


EAJ37407
unknown [environmental sequence]


EAJ39929
unknown [environmental sequence]


EAJ54356
unknown [environmental sequence]


EAJ54959
unknown [environmental sequence]


EAJ56207
unknown [environmental sequence]


EAJ58447
unknown [environmental sequence]


EAJ59958
unknown [environmental sequence]


EAJ63347
unknown [environmental sequence]


EAJ66054
unknown [environmental sequence]


EAJ67637
unknown [environmental sequence]


EAJ69812
unknown [environmental sequence]


EAJ74441
unknown [environmental sequence]


EAJ76472
unknown [environmental sequence]


EAJ76473
unknown [environmental sequence]


EAJ80355
unknown [environmental sequence]


EAJ80839
unknown [environmental sequence]


EAJ81408
unknown [environmental sequence]


EAJ86174
unknown [environmental sequence]


EAJ87600
unknown [environmental sequence]


EAJ88203
unknown [environmental sequence]


EAJ88682
unknown [environmental sequence]


EAJ92341
unknown [environmental sequence]


EAJ94774
unknown [environmental sequence]


EAJ97555
unknown [environmental sequence]


EAJ97958
unknown [environmental sequence]


EAK07654
unknown [environmental sequence]


EAK08513
unknown [environmental sequence]


EAK08529
unknown [environmental sequence]


EAK10609
unknown [environmental sequence]


EAK10614
unknown [environmental sequence]


EAK12902
unknown [environmental sequence]


EAK13034
unknown [environmental sequence]


EAK15092
unknown [environmental sequence]


EAK22483
unknown [environmental sequence]


EAK23222
unknown [environmental sequence]


EAK24187
unknown [environmental sequence]


EAK24674
unknown [environmental sequence]


EAK28785
unknown [environmental sequence]


EAK34731
unknown [environmental sequence]


EAK34742
unknown [environmental sequence]


EAK36883
unknown [environmental sequence]


EAK37522
unknown [environmental sequence]


EAK42705
unknown [environmental sequence]


EAK43213
unknown [environmental sequence]


EAK52580
unknown [environmental sequence]


EAK53452
unknown [environmental sequence]


EAK58759
unknown [environmental sequence]


EAK62665
unknown [environmental sequence]


EAK63558
unknown [environmental sequence]


F84187
phytoene dehydrogenase [imported] - Halobacterium sp. NRC-1


F90272
phytoene dehydrogenase related protein [imported] - Sulfolobus solfataricus


G87635
phytoene dehydrogenase-related protein [imported] - Caulobacter crescentus


G90413
phytoene dehydrogenase related protein [imported] - Sulfolobus solfataricus


H83880
hypothetical protein BH1848 [imported] - Bacillus halodurans (strain C-125)


H84320
phytoene dehydrogenase [imported] - Halobacterium sp. NRC-1


JC7723
phytoene desaturase (EC 1.14.99.—) 1 - citrus


NP_060220
all-trans-13,14-dihydroretinol saturase [Homo sapiens]


NP_080435
all-trans-13,14-dihydroretinol saturase [Mus musculus]


NP_193157
phytoene dehydrogenase, chloroplast/phytoene desaturase (PDS) [Arabidopsis



thaliana]


NP_214383
protoporphyrinogen oxidase [Aquifex aeolicus VF5]


NP_276913
phytoene dehydrogenase [Methanothermobacter thermautotrophicus str. Delta H]


NP_293819
phytoene dehydrogenase, putative [Deinococcus radiodurans R1]


NP_294534
dehydrogenase, putative [Deinococcus radiodurans R1]


NP_294585
phytoene dehydrogenase [Deinococcus radiodurans R1]


NP_295972
methoxyneurosporene dehydrogenase [Deinococcus radiodurans R1]


NP_338490
oxidoreductase, putative [Mycobacterium tuberculosis CDC1551]


NP_376437
hypothetical protein ST0549 [Sulfolobus tokodaii str. 7]


NP_377056
hypothetical protein ST1130 [Sulfolobus tokodaii str. 7]


NP_388895
protoporphyrinogen IX and coproporphyrinogen III oxidase [Bacillus subtilis subsp.



subtilis str. 168]


NP_441167
phytoene desaturase [Synechocystis sp. PCC 6803]


NP_441254
hypothetical protein sll0254 [Synechocystis sp. PCC 6803]


NP_442491
b-carotene ketolase [Synechocystis sp. PCC 6803]


NP_442727
hypothetical protein sll0033 [Synechocystis sp. PCC 6803]


NP_562475
probable diapophytoene dehydrogenase [Clostridium perfringens str. 13]


NP_568712
amine oxidase-related [Arabidopsis thaliana]


NP_601630
hypothetical protein NCgl2346 [Corynebacterium glutamicum ATCC 13032]


NP_601630
hypothetical protein NCgl2346 [Corynebacterium glutamicum ATCC 13032]


NP_616426
phytoene dehydrogenase family protein [Methanosarcina acetivorans C2A]


NP_624522
putative phytoene dehydrogenase (phytoene desaturase) (putative secreted protein)



[Streptomyces coelicolor A3(2)]


NP_626360
putative carotenoid dehydrogenase (putative secreted protein) [Streptomyces



coelicolor A3(2)]


NP_630834
putative phytoene dehydrogenase [Streptomyces coelicolor A3(2)]


NP_643053
phytoene dehydrogenase [Xanthomonas axonopodis pv. citri str. 306]


NP_647302
hypothetical protein MW2485 [Staphylococcus aureus subsp. aureus MW2]


NP_659552
all-trans-13,14-dihydroretinol saturase [Rattus norvegicus]


NP_661086
lycopene cyclase, putative [Chlorobium tepidum TLS]


NP_661546
carotenoid isomerase, putative [Chlorobium tepidum TLS]


NP_661701
phytoene desaturase [Chlorobium tepidum TLS]


NP_662300
zeta-carotene desaturase [Chlorobium tepidum TLS]


NP_681023
putative phytoene dehydrogenase [Thermosynechococcus elongatus BP-1]


NP_681127
zeta-carotene desaturase [Thermosynechococcus elongatus BP-1]


NP_682351
phytoene dehydrogenase/phytoene desaturase [Thermosynechococcus elongatus



BP-1]


NP_693380
phytoene dehydrogenase [Oceanobacillus iheyensis HTE831]


NP_693382
phytoene dehydrogenase [Oceanobacillus iheyensis HTE831]


NP_737250
phytoene desaturase [Corynebacterium efficiens YS-314]


NP_763380
hypothetical protein VV21505 [Vibrio vulnificus CMCP6]


NP_786524
squalene synthase [Lactobacillus plantarum WCFS1]


NP_822198
phytoene desaturase [Streptomyces avermitilis MA-4680]


NP_822828
squalene/phytoene dehydrogenase [Streptomyces avermitilis MA-4680]


NP_827278
putative phytoene dehydrogenase [Streptomyces avermitilis MA-4680]


NP_851528
putative phytoene dehydrogenase [Streptomyces rochei]


NP_857496
PUTATIVE DEHYDROGENASE [Mycobacterium bovis AF2122/97]


NP_868798
probable phytoene dehydrogenase [Rhodopirellula baltica SH 1]


NP_869339
phytoene dehydrogenase [Rhodopirellula baltica SH 1]


NP_870237
phytoene dehydrogenase [Rhodopirellula baltica SH 1]


NP_874530
Zeta-carotene desaturase [Prochlorococcus marinus subsp. marinus str. CCMP1375]


NP_874561
Phytoene dehydrogenase, phytoene desaturase [Prochlorococcus marinus subsp.



marinus str. CCMP1375]


NP_874977
Phytoene dehydrogenase/carotenoid isomerase [Prochlorococcus marinus subsp.



marinus str. CCMP1375]


NP_892236
zeta-carotene desaturase [Prochlorococcus marinus subsp. pastoris str. CCMP1986]


NP_892265
phytoene desaturase [Prochlorococcus marinus subsp. pastoris str. CCMP1986]


NP_892458
Bacterial-type phytoene dehydrogenase [Prochlorococcus marinus subsp. pastoris



str. CCMP1986]


NP_893232
putative carotenoid isomerase [Prochlorococcus marinus subsp. pastoris str.



CCMP1986]


NP_894882
putative carotenoid isomerase [Prochlorococcus marinus str. MIT 9313]


NP_895385
NAD binding site [Prochlorococcus marinus str. MIT 9313]


NP_895793
zeta-carotene desaturase [Prochlorococcus marinus str. MIT 9313]


NP_895829
phytoene desaturase [Prochlorococcus marinus str. MIT 9313]


NP_896854
hypothetical protein SYNW0761 [Synechococcus sp. WH 8102]


NP_896994
Carotenoid isomerase [Synechococcus sp. WH 8102]


NP_898304
zeta-carotene desaturase [Synechococcus sp. WH 8102]


NP_898346
phytoene desaturase [Synechococcus sp. WH 8102]


NP_902647
hypothetical protein CV2977 [Chromobacterium violaceum ATCC 12472]


NP_923340
beta-carotene ketolase [Gloeobacter violaceus PCC 7421]


NP_923639
hypothetical protein gll0693 [Gloeobacter violaceus PCC 7421]


NP_923813
phytoene dehydrogenase [Gloeobacter violaceus PCC 7421]


NP_925079
hypothetical protein gvip293 [Gloeobacter violaceus PCC 7421]


NP_931515
phytoene dehydrogenase (phytoene desaturase) [Photorhabdus luminescens subsp.



laumondii TTO1]


NP_936379
hypothetical protein VVA0323 [Vibrio vulnificus YJ016]


NP_940208
phytoene dehydrogenase related enzyme [Corynebacterium diphtheriae NCTC



13129]


NP_945754
NAD binding site:Amine oxidase [Rhodopseudomonas palustris CGA009]


NP_946860
phytoene dehydrogenase CrtI [Rhodopseudomonas palustris CGA009]


NP_946866
methoxyneurosporene dehydrogenase [Rhodopseudomonas palustris CGA009]


NP_948851
phytoene dehydrogenase-related protein [Rhodopseudomonas palustris CGA009]


NP_962004
hypothetical protein MAP3070 [Mycobacterium avium subsp. paratuberculosis str.



k10]


NP_968600
Phytoene dehydrogenase [Bdellovibrio bacteriovorus HD100]


NP_974222
zeta-carotene desaturase (ZDS1)/carotene 7,8-desaturase [Arabidopsis thaliana]


NP_974545
phytoene dehydrogenase, chloroplast/phytoene desaturase (PDS) [Arabidopsis



thaliana]


O49901
Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)


P17059
Methoxyneurosporene dehydrogenase


P54971
Phytoene dehydrogenase (Phytoene desaturase)


P54978
Phytoene dehydrogenase (Phytoene desaturase)


P54979
Phytoene dehydrogenase (Phytoene desaturase)


P54981
Phytoene dehydrogenase (Phytoene desaturase)


P54982
Phytoene dehydrogenase (Phytoene desaturase)


P74306
Zeta-carotene desaturase (Carotene 7,8-desaturase)


Q01671
Methoxyneurosporene dehydrogenase


Q02861
Phytoene dehydrogenase (Phytoene desaturase)


Q38893
Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)


Q40406
Phytoene dehydrogenase, chloroplast precursor (Phytoene desaturase)


Q9FV46
Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)


Q9SE20
Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)


Q9SMJ3
Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)


Q9ZTN9
Phytoene dehydrogenase, chloroplast precursor (Phytoene desaturase)


Q9ZTP4
Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)


S29314
phytoene dehydrogenase (EC 1.3.—.—) - pepper


S32171
hydroxyneurosporene dehydrogenase (EC 1.3.—.—) - Myxococcus xanthus


S49624
methoxyneurosporene dehydrogenase (EC 1.3.—.—) CrtD - Rhodobacter sphaeroides


S52586
phytoene dehydrogenase (EC 1.3.—.—) - Erwinia herbicola


S65060
phytoene desaturase precursor - maize


T10701
probable phytoene dehydrogenase (EC 1.3.—.—) - green alga (Dunaliella bardawil)


T31463
probable diapophytoene dehydrogenase crtN - Heliobacillus mobilis


T46822
phytoene desaturase (EC 1.3.—.—) [validated] - Xanthophyllomyces dendrorhous


T48646
phytoene dehydrogenase (EC 1.—.—.—) [validated] - Cercospora nicotianae


T50745
phytoene dehydrogenase (EC 1.3.—.—) [imported] - Rhodobacter sphaeroides


T50749
methoxyneurosporene dehydrogenase (EC 1.3.—.—) crtD [imported] - Rhodobacter



sphaeroides


T50893
methoxyneurosporene dehydrogenase [imported] - Rubrivivax gelatinosus


T50910
phytoene dehydrogenase [imported] - Rubrivivax gelatinosus


T51119
phytoene desaturase crtI [imported] - Brevibacterium linens


T51123
betacarotene desaturase [imported] - Brevibacterium linens


XP_324732
PHYTOENE DEHYDROGENASE (PHYTOENE DESATURASE) (ALBINO-1



PROTEIN) [Neurospora crassa]


XP_383241
hypothetical protein FG03065.1 [Gibberella zeae PH-1]


XP_401825
hypothetical protein UM04210.1 [Ustilago maydis 521]


XP_470568
Putative phytoene dehydrogenase precursor [Oryza sativa]


XP_473486
OSJNBa0084K11.8 [Oryza sativa (japonica cultivar-group)]


XP_477063
putative zeta-carotene desaturase precursor [Oryza sativa (japonica cultivar-group)]


XP_525801
PREDICTED: hypothetical protein XP_525801 [Pan troglodytes]


XP_540198
PREDICTED: hypothetical protein XP_540198 [Canis familiaris]


YP_006049
phytoene dehydrogenase [Thermus thermophilus HB27]


YP_013621
phytoene dehydrogenase, putative [Listeria monocytogenes str. 4b F2365]


YP_024310
phytoene dehydrogenase [Picrophilus torridus DSM 9790]


YP_041986
squalene synthase [Staphylococcus aureus subsp. aureus MRSA252]


YP_041988
putative phytoene dehydrogenase related protein [Staphylococcus aureus subsp.



aureus MRSA252]


YP_044561
squalene synthase [Staphylococcus aureus subsp. aureus MSSA476]


YP_044564
putative phytoene dehydrogenase related protein [Staphylococcus aureus subsp.



aureus MSSA476]


YP_062471
phytoene dehydrogenase [Leifsonia xyli subsp. xyli str. CTCB07]


YP_117947
putative phytoene desaturase [Nocardia farcinica IFM 10152]


YP_120612
putative phytoene desaturase [Nocardia farcinica IFM 10152]


YP_135077
phytoene dehydrogenase [Haloarcula marismortui ATCC 43049]


YP_136483
phytoene dehydrogenase [Haloarcula marismortui ATCC 43049]


YP_145331
probable phytoene dehydrogenase [Thermus thermophilus HB8]


YP_145348
phytoene dehydrogenase [Thermus thermophilus HB8]


YP_171014
carotene isomerase [Synechococcus elongatus PCC 6301]


YP_172823
phytoene dehydrogenase [Synechococcus elongatus PCC 6301]


YP_173078
carotene isomerase [Synechococcus elongatus PCC 6301]


YP_173207
zeta-carotene desaturase [Synechococcus elongatus PCC 6301]


YP_184572
predicted oxidoreductase [Thermococcus kodakaraensis]


YP_187368
dehydrosqualene desaturase [Staphylococcus aureus subsp. aureus COL]


YP_187371
phytoene dehydrogenase [Staphylococcus aureus subsp. aureus COL]


YP_187371
phytoene dehydrogenase [Staphylococcus aureus subsp. aureus COL]


YP_187371
phytoene dehydrogenase [Staphylococcus aureus subsp. aureus COL]


ZP_000490
COG1233: Phytoene dehydrogenase and related proteins [Magnetospirillum



magnetotacticum MS-1]


ZP_000509
COG1233: Phytoene dehydrogenase and related proteins [Magnetospirillum



magnetotacticum MS-1]


ZP_000518
COG1233: Phytoene dehydrogenase and related proteins [Magnetospirillum



magnetotacticum MS-1]


ZP_000566
COG0562: UDP-galactopyranose mutase [Magnetospirillum magnetotacticum MS-



1]


ZP_000627
COG1233: Phytoene dehydrogenase and related proteins [Leuconostoc



mesenteroides subsp. mesenteroides ATCC 8293]


ZP_000627
COG1233: Phytoene dehydrogenase and related proteins [Leuconostoc



mesenteroides subsp. mesenteroides ATCC 8293]


ZP_001073
COG1233: Phytoene dehydrogenase and related proteins [Nostoc punctiforme PCC



73102]


ZP_001081
COG1233: Phytoene dehydrogenase and related proteins [Nostoc punctiforme PCC



73102]


ZP_001091
COG3349: Uncharacterized conserved protein [Nostoc punctiforme PCC 73102]


ZP_001116
COG1233: Phytoene dehydrogenase and related proteins [Nostoc punctiforme PCC



73102]


ZP_001117
COG3349: Uncharacterized conserved protein [Nostoc punctiforme PCC 73102]


ZP_001119
COG3349: Uncharacterized conserved protein [Nostoc punctiforme PCC 73102]


ZP_001124
COG1233: Phytoene dehydrogenase and related proteins [Nostoc punctiforme PCC



73102]


ZP_001510
COG1233: Phytoene dehydrogenase and related proteins [Dechloromonas aromatica



RCB]


ZP_001591
COG3349: Uncharacterized conserved protein [Anabaena variabilis ATCC 29413]


ZP_001593
COG1233: Phytoene dehydrogenase and related proteins [Anabaena variabilis



ATCC 29413]


ZP_001602
COG3349: Uncharacterized conserved protein [Anabaena variabilis ATCC 29413]


ZP_001614
COG3349: Uncharacterized conserved protein [Anabaena variabilis ATCC 29413]


ZP_001645
COG3349: Uncharacterized conserved protein [Synechococcus elongatus PCC 7942]


ZP_001650
COG3349: Uncharacterized conserved protein [Synechococcus elongatus PCC 7942]


ZP_001722
COG1233: Phytoene dehydrogenase and related proteins [Methylobacillus



flagellatus KT]


ZP_001746
COG3349: Uncharacterized conserved protein [Crocosphaera watsonii WH 8501]


ZP_001752
COG3349: Uncharacterized conserved protein [Crocosphaera watsonii WH 8501]


ZP_001770
COG1232: Protoporphyrinogen oxidase [Crocosphaera watsonii WH 8501]


ZP_001777
COG1233: Phytoene dehydrogenase and related proteins [Crocosphaera watsonii



WH 8501]


ZP_001787
COG3349: Uncharacterized conserved protein [Crocosphaera watsonii WH 8501]


ZP_001837
COG1233: Phytoene dehydrogenase and related proteins [Exiguobacterium sp. 255-



15]


ZP_001867
COG1233: Phytoene dehydrogenase and related proteins [Rubrobacter xylanophilus



DSM 9941]


ZP_002073
COG1233: Phytoene dehydrogenase and related proteins [Rhodobacter sphaeroides



2.4.1]


ZP_002077
COG1233: Phytoene dehydrogenase and related proteins [Rhodobacter sphaeroides



2.4.1]


ZP_002339
phytoene dehydrogenase, putative [Listeria monocytogenes str. 1/2a F6854]


ZP_002680
COG1233: Phytoene dehydrogenase and related proteins [Rhodospirillum rubrum]


ZP_002705
COG1233: Phytoene dehydrogenase and related proteins [Rhodospirillum rubrum]


ZP_002771
COG1232: Protoporphyrinogen oxidase [Burkholderia fungorum LB400]


ZP_002892
hypothetical protein Mmc102002317 [Magnetococcus sp. MC-1]


ZP_002916
COG3349: Uncharacterized conserved protein [Thermobifida fusca]


ZP_002963
COG1233: Phytoene dehydrogenase and related proteins [Methanosarcina barkeri



str. fusaro]


ZP_003022
COG1233: Phytoene dehydrogenase and related proteins [Novosphingobium



aromaticivorans DSM 12444]


ZP_003036
COG1233: Phytoene dehydrogenase and related proteins [Novosphingobium



aromaticivorans DSM 12444]


ZP_003107
COG1233: Phytoene dehydrogenase and related proteins [Cytophaga hutchinsonii]


ZP_003202
COG1233: Phytoene dehydrogenase and related proteins [Oenococcus oeni PSU-1]


ZP_003258
COG1233: Phytoene dehydrogenase and related proteins [Trichodesmium



erythraeum IMS101]


ZP_003268
COG3349: Uncharacterized conserved protein [Trichodesmium erythraeum IMS101]


ZP_003269
COG3349: Uncharacterized conserved protein [Trichodesmium erythraeum IMS101]


ZP_003276
COG1233: Phytoene dehydrogenase and related proteins [Trichodesmium



erythraeum IMS101]


ZP_003283
COG1233: Phytoene dehydrogenase and related proteins [Trichodesmium



erythraeum IMS101]


ZP_003557
COG1233: Phytoene dehydrogenase and related proteins [Exiguobacterium sp. 255-



15]


ZP_003559
COG3349: Uncharacterized conserved protein [Chloroflexus aurantiacus]


ZP_003565
COG1233: Phytoene dehydrogenase and related proteins [Chloroflexus aurantiacus]


ZP_003577
COG1233: Phytoene dehydrogenase and related proteins [Chloroflexus aurantiacus]


ZP_003593
COG1233: Phytoene dehydrogenase and related proteins [Chloroflexus aurantiacus]


ZP_003595
COG1233: Phytoene dehydrogenase and related proteins [Chloroflexus aurantiacus]


ZP_003685
carotenoid isomerase, putative [Campylobacter lari RM2100]
















TABLE 17b







Examples of phytoene dehydrogenase polypeptides.










Row
Accession
GI
Protein Description













1
1613414B
227039
crtI gene


2
CAA36533
45998
unnamed protein product [Rhodobacter capsulatus]


3
ABP69925
145555312
Phytoene dehydrogenase-related protein [Rhodobacter sphaeroides





ATCC 17025]


4
ABG29855
109453650
phytoene dehydrogenase [Roseobacter denitrificans OCh 114]


5
YP_001 . . .
126462676
Phytoene dehydrogenase-related protein [Rhodobacter sphaeroides





ATCC 17029]


6
CAB38739
4490589
phytoene dehydrogenase [Rhodobacter sphaeroides]


7
AAF24289
6690721
CrtI [Rhodobacter sphaeroides]


8
ZP_019 . . .
149914257
Phytoene dehydrogenase [Roseobacter sp. AzwK-3b]


9
ZP_018 . . .
149203764
Phytoene dehydrogenase [Roseovarius sp. TM1035]


10
ZP_017 . . .
126734359
Phytoene dehydrogenase [Roseobacter sp. CCS2]


11
ZP_015 . . .
118735466
Phytoene dehydrogenase-related protein [Dinoroseobacter shibae





DFL 12]


12
EBA75398
134340305
hypothetical protein GOS_348183 [marine metagenome]


13
ZP_010 . . .
85703533
Phytoene dehydrogenase [Roseovarius sp. 217]


14
ZP_010 . . .
84514966
Phytoene dehydrogenase [Loktanella vestfoldensis SKA53]


15
EDJ26541
144155062
hypothetical protein GOS_1726264 [marine metagenome]


16
AAM48646
21328640
phytoene dehydrogenase [uncultured proteobacterium]


17
EBF29285
135068871
hypothetical protein GOS_9621672 [marine metagenome]


18
EDH88525
143962357
hypothetical protein GOS_524801 [marine metagenome]


19
ABD53060
88862183
phytoene dehydrogenase [Jannaschia sp. CCS1]


20
ECX23858
142320992
hypothetical protein GOS_2574166 [marine metagenome]


21
EDD83467
143241615
hypothetical protein GOS_1236491 [marine metagenome]


22
ECW60413
142235101
hypothetical protein GOS_2690740 [marine metagenome]


23
EDB24382
142880994
hypothetical protein GOS_1857800 [marine metagenome]


24
EDC65629
143078396
hypothetical protein GOS_1437717 [marine metagenome]


25
EDC66763
143079940
hypothetical protein GOS_1435710 [marine metagenome]


26
EBF73535
135137918
hypothetical protein GOS_9549173 [marine metagenome]


27
EDB61897
142933299
hypothetical protein GOS_1624464 [marine metagenome]


28
EDH58399
143920581
hypothetical protein GOS_579274 [marine metagenome]


29
ECV46406
142084909
hypothetical protein GOS_2893885 [marine metagenome]


30
EBG03643
135184853
hypothetical protein GOS_9500102 [marine metagenome]


31
ECW11301
142170256
hypothetical protein GOS_2778421 [marine metagenome]


32
EDG30167
143690631
hypothetical protein GOS_805431 [marine metagenome]


33
EBF89344
135162533
hypothetical protein GOS_9523433 [marine metagenome]


34
EDG14791
143664156
hypothetical protein GOS_832322 [marine metagenome]


35
ECW44302
142213461
hypothetical protein GOS_2720548 [marine metagenome]


36
EDC28179
143027347
hypothetical protein GOS_1503868 [marine metagenome]


37
EBF91518
135165888
hypothetical protein GOS_9519783 [marine metagenome]


38
EBG06098
135188689
hypothetical protein GOS_9496261 [marine metagenome]


39
YP_001 . . .
121998398
Phytoene dehydrogenase-related protein [Halorhodospira





halophila SL1]


40
ABC21298
83574747
Phytoene desaturase [Rhodospirillum rubrum ATCC 11170]


41
EDD45555
143188703
hypothetical protein GOS_1301547 [marine metagenome]


42
EBF89879
135163364
hypothetical protein GOS_9522488 [marine metagenome]


43
EDA94958
142836512
hypothetical protein GOS_1907603 [marine metagenome]


44
EBE40240
134934911
hypothetical protein GOS_9769793 [marine metagenome]


45
ABQ38355
146409849
Phytoene dehydrogenase (Phytoene desaturase) [Bradyrhizobium





sp. BTAi1]


46
ECV53668
142093711
hypothetical protein GOS_2880588 [marine metagenome]


47
EDJ05722
144126667
hypothetical protein GOS_1762374 [marine metagenome]


48
EDJ52003
144189327
hypothetical protein GOS_1681048 [marine metagenome]


49
CAL75489
146191484
Phytoene dehydrogenase (Phytoene desaturase) [Bradyrhizobium





sp. ORS278]


50
ZP_011 . . .
88706670
phytoene dehydrogenase [gamma proteobacterium KT 71]


51
ABD86823
90104786
amine oxidase [Rhodopseudomonas palustris BisB18]


52
ZP_019 . . .
149922641
amine oxidase [Plesiocystis pacifica SIR-1]


53
ECW14126
142173943
hypothetical protein GOS_2773516 [marine metagenome]


54
ABJ05267
115517283
amine oxidase [Rhodopseudomonas palustris BisA53]


55
ZP_020 . . .
156449192
Zeta-phytoene desaturase [Methylobacterium chloromethanicum





CM4]


56
ZP_020 . . .
153900167
FAD-dependent pyridine nucleotide-disulphide oxidoreductase





[Methylobacterium extorquens PA1]


57
EDO75157
157409160
Zeta-phytoene desaturase [Methylobacterium populi BJ001]


58
EBF26787
135064945
hypothetical protein GOS_9625603 [marine metagenome]


59
EBM47492
136188235
hypothetical protein GOS_8404015 [marine metagenome]


60
BAA94063
7416814
phytoene dehydrogenase [Rubrivivax gelatinosus]


61
AAO93135
29893506
phytoene dehydrogenase; CrtI [Rubrivivax gelatinosus]


62
ABE40987
91684685
amine oxidase [Rhodopseudomonas palustris BisB5]


63
ABC44467
83756354
phytoene dehydrogenase [Salinibacter ruber DSM 13855]


64
NP_946860
39934584
phytoene dehydrogenase CrtI [Rhodopseudomonas palustris





CGA009]


65
EDK95498
148522573
Phytoene dehydrogenase-related protein [Methylobacterium sp. 4-





46]


66
AAX48189
61653236
phytoene dehydrogenase [uncultured proteobacterium





DelRiverFos06H03]


67
ABD08704
86574147
Amine oxidase [Rhodopseudomonas palustris HaA2]


68
ECV97125
142151708
hypothetical protein GOS_2803067 [marine metagenome]


69
EBF91320
135165576
hypothetical protein GOS_9520100 [marine metagenome]


70
EDG74671
143780072
hypothetical protein GOS_728533 [marine metagenome]


71
AAR37802
40062931
phytoene dehydrogenase [uncultured bacterium 442]


72
ZP_016 . . .
119504131
amine oxidase [marine gamma proteobacterium HTCC2080]


73
EBY63975
138260458
hypothetical protein GOS_5033312 [marine metagenome]


74
ECW52975
142225047
hypothetical protein GOS_2704529 [marine metagenome]


75
EDB07926
142858428
hypothetical protein GOS_1885673 [marine metagenome]


76
ECX08477
142300457
hypothetical protein GOS_2602107 [marine metagenome]


77
EBE08763
134887517
hypothetical protein GOS_9823078 [marine metagenome]


78
EDG53739
143740094
hypothetical protein GOS_764800 [marine metagenome]


79
AAR37855
40062985
phytoene dehydrogenase [uncultured bacterium 443]


80
EBE55393
134957668
hypothetical protein GOS_9744377 [marine metagenome]


81
EBK49247
135888345
hypothetical protein GOS_8723699 [marine metagenome]


82
YP_001 . . .
154247504
Zeta-phytoene desaturase [Xanthobacter autotrophicus Py2]


83
EBJ38620
135714057
hypothetical protein GOS_8907038 [marine metagenome]


84
EBO29607
136458570
hypothetical protein GOS_8104065 [marine metagenome]


85
EDI63495
144067673
hypothetical protein GOS_399405 [marine metagenome]


86
ECH51213
139794606
hypothetical protein GOS_4963038 [marine metagenome]


87
ZP_014 . . .
113941052
amine oxidase [Herpetosiphon aurantiacus ATCC 23779]


88
P54978
85700409
Phytoene dehydrogenase (Phytoene desaturase)


89
AAY28420
63034218
phytoene desaturase [Paracoccus haeundaensis]


90
YP_001 . . .
148655097
Phytoene dehydrogenase-related protein [Roseiflexus sp. RS-1]


91
AAT35222
47531118
fusion of carotene synthesis proteins [synthetic construct]


92
CAB56062
5912295
phytoene desaturase [Paracoccus marcusii]


93
ZP_016 . . .
119484684
phytoene dehydrogenase CrtI [Lyngbya sp. PCC 8106]


94
YP_001 . . .
156932562
hypothetical protein ESA_00343 [Enterobacter sakazakii ATCC





BAA-894]


95
CAL34121
112702901
phytoene dehydrogenase CRTI [Enterobacter sakazakii]


96
ZP_014 . . .
114705593
phytoene dehydrogenase (phytoene desaturase) [Fulvimarina





pelagi HTCC2506]


97
ABU57678
156232895
Zeta-phytoene desaturase [Roseiflexus castenholzii DSM 13941]


98
EDJ24172
144151864
hypothetical protein GOS_1730347 [marine metagenome]


99
EBP04886
136575764
hypothetical protein GOS_7976019 [marine metagenome]


100
EDJ19941
144146057
hypothetical protein GOS_1737754 [marine metagenome]


101
EDE02809
143268695
hypothetical protein GOS_1202430 [marine metagenome]


102
EDA02972
142711842
hypothetical protein GOS_2076612 [marine metagenome]


103
AAC44850
1842244
phytoene desaturase


104
ECI48880
139936452
hypothetical protein GOS_4592564 [marine metagenome]


105
ECW29436
142194003
hypothetical protein GOS_2746710 [marine metagenome]


106
CAE79593
39575425
Phytoene dehydrogenase [Bdellovibrio bacteriovorus HD100]


107
EDJ16294
144141089
hypothetical protein GOS_1744028 [marine metagenome]


108
ABC50114
84043362
phytoene desaturase [Brevundimonas vesicularis]


109
CAE16714
36787607
phytoene dehydrogenase (phytoene desaturase) [Photorhabdus





luminescens subsp. laumondii TTO1]


110
AAZ73142
72536076
phytoene desaturase [Enterobacteriaceae bacterium DC416]


111
ECC15254
138850366
hypothetical protein GOS_5005338 [marine metagenome]


112
EBF96527
135173721
hypothetical protein GOS_9511771 [marine metagenome]


113
AAZ73130
72536062
phytoene desaturase [Enterobacteriaceae bacterium DC260]


114
AAW72814
92430259
CrtI [Pantoea sp. C1B1Y]


115
EBF63722
135122709
hypothetical protein GOS_9565260 [marine metagenome]


116
EDJ33653
144164568
hypothetical protein GOS_1713484 [marine metagenome]


117
BAB79603
18143448
crtI [Pantoea agglomerans pv. milletiae]


118
AAZ73136
72536069
phytoene desaturase [Enterobacteriaceae bacterium DC404]


119
ABD73281
89475493
phytoene dehydrogenase [Pantoea agglomerans]


120
AAF78201
8650417
phytoene desaturase [Bradyrhizobium sp. ORS278]


121
ZP_010 . . .
84704558
phytoene dehydrogenase (phytoene desaturase) [Parvularcula





bermudensis HTCC2503]


122
EBF30985
135071529
hypothetical protein GOS_9618780 [marine metagenome]


123
EDJ11107
144133947
hypothetical protein GOS_1752989 [marine metagenome]


124
YP_001 . . .
146284185
phytoene desaturase [Pseudomonas stutzeri A1501]


125
EDB39933
142902995
hypothetical protein GOS_1830750 [marine metagenome]


126
ZP_013 . . .
94496006
amine oxidase [Sphingomonas sp. SKA58]


127
P22871
117514
Phytoene dehydrogenase (Phytoene desaturase)


128
ECD12151
139058277
hypothetical protein GOS_4688757 [marine metagenome]


129
AAA64981
551855
phytoene dehydrogenase [Pantoea agglomerans]


130
ECS36705
141558903
hypothetical protein GOS_4990354 [marine metagenome]


131
ECJ26724
140055135
hypothetical protein GOS_5004115 [marine metagenome]


132
ECY06051
142435846
hypothetical protein GOS_2424849 [marine metagenome]


133
ZP_007 . . .
76261240
Amine oxidase: FAD dependent oxidoreductase [Chloroflexus





aurantiacus J-10-fl]


134
BAD99408
67003497
phytoene desaturase [Brevundimonas sp. SD212]


135
ZP_015 . . .
118048084
amine oxidase [Chloroflexus aggregans DSM 9485]


136
EAS49801
90336053
phytoene dehydrogenase [Aurantimonas sp. SI85-9A1]


137
EDF88410
143616932
hypothetical protein GOS_877736 [marine metagenome]


138
AAN85599
27228293
Phytoene Desaturase [Pantoea stewartii]


139
EDI65706
144070706
hypothetical protein GOS_395761 [marine metagenome]


140
AAA21263
148397
phytoene dehydrogenase [Pantoea agglomerans]


141
P21685
117515
Phytoene dehydrogenase (Phytoene desaturase)


142
AAZ73149
72536084
phytoene desaturase [Enterobacteriaceae bacterium DC413]


143
ZP_016 . . .
119476622
phytoene dehydrogenase [marine gamma proteobacterium





HTCC2143]


144
ABL97778
119713729
crtI phytoene dehydrogenase [uncultured marine bacterium





HF10_29C11]


145
ABL97829
119713781
crtI/crtB [uncultured marine bacterium HF10_49E08]


146
EDB02259
142846369
hypothetical protein GOS_1894993 [marine metagenome]


147
ECQ63324
141245988
hypothetical protein GOS_4882732 [marine metagenome]


148
EAS48195
90333025
phytoene dehydrogenase [marine gamma proteobacterium





HTCC2207]


149
EAU13549
113732481
Amine oxidase: FAD dependent oxidoreductase [Caulobacter sp.





K31]


150
ECV72481
142118377
hypothetical protein GOS_2846587 [marine metagenome]


151
ECZ41342
142625145
hypothetical protein GOS_2188322 [marine metagenome]


152
EDF61582
143556399
hypothetical protein GOS_924048 [marine metagenome]


153
EBN79105
136382241
hypothetical protein GOS_8187951 [marine metagenome]


154
YP_001 . . .
156974447
hypothetical protein VIBHAR_02162 [Vibrio harveyi ATCC





BAA-1116]


155
BAA20276
2130971
phytoene desaturase [Erythrobacter longus]


156
EBC81369
134685202
hypothetical protein GOS_10270 [marine metagenome]


157
ECS97023
141726243
hypothetical protein GOS_8923124 [marine metagenome]


158
ECY38926
142480300
hypothetical protein GOS_2368541 [marine metagenome]


159
YP_632230
108758926
putative phytoene dehydrogenase [Myxococcus xanthus DK 1622]


160
EDB72930
142948834
hypothetical protein GOS_1603748 [marine metagenome]


161
EDJ54243
144192357
hypothetical protein GOS_1677113 [marine metagenome]


162
EAR55130
89049570
phytoene dehydrogenase [Photobacterium sp. SKA34]


163
EDF01226
143447606
hypothetical protein GOS_1030671 [marine metagenome]


164
EDD12651
143142675
hypothetical protein GOS_1354831 [marine metagenome]


165
EDI08258
143990952
hypothetical protein GOS_491661 [marine metagenome]


166
EDI22441
144010457
hypothetical protein GOS_467843 [marine metagenome]


167
ABF54837
98978686
amine oxidase [Sphingopyxis alaskensis RB2256]


168
EBL74107
136074962
hypothetical protein GOS_8521797 [marine metagenome]


169
EBX98247
138142760
hypothetical protein GOS_6427327 [marine metagenome]


170
ECV76618
142124100
hypothetical protein GOS_2839194 [marine metagenome]


171
EBP18308
136596794
hypothetical protein GOS_7953009 [marine metagenome]


172
YP_265547
71082828
phytoene dehydrogenase [Candidatus Pelagibacter ubique





HTCC1062]


173
EAS85201
91718551
phytoene dehydrogenase [Candidatus Pelagibacter ubique





HTCC1002]


174
EDG91241
143827295
hypothetical protein GOS_699208 [marine metagenome]


175
ECV24805
142059343
hypothetical protein GOS_2935833 [marine metagenome]


176
AAY87313
68164584
predicted phytoene desaturase [uncultured bacterium BAC17H8]


177
EBD43768
134788236
hypothetical protein GOS_9929916 [marine metagenome]


178
EDG35515
143701587
hypothetical protein GOS_796054 [marine metagenome]


179
ZP_018 . . .
149185744
Phytoene dehydrogenase [Erythrobacter sp. SD-21]


180
ABL60986
119094156
phytoene dehydrogenase CrtI [uncultured marine bacterium





HF10_19P19]


181
ECZ18273
142592252
hypothetical protein GOS_2227647 [marine metagenome]


182
ABD26256
87135514
amine oxidase [Novosphingobium aromaticivorans DSM 12444]


183
EDG45712
143723898
hypothetical protein GOS_778645 [marine metagenome]


184
EBE76519
134988930
hypothetical protein GOS_9708797 [marine metagenome]


185
EDC75856
143092398
hypothetical protein GOS_1419598 [marine metagenome]


186
EDF35075
143504771
hypothetical protein GOS_970643 [marine metagenome]


187
ZP_014 . . .
114771897
phytoene dehydrogenase [alpha proteobacterium HTCC2255]


188
EDG12368
143659594
hypothetical protein GOS_836451 [marine metagenome]


189
AAT90320
50952787
putative phytoene dehydrogenase [uncultured proteobacterium





eBACred25D05]


190
EBV02567
137608266
hypothetical protein GOS_6968229 [marine metagenome]


191
ECB29435
138684670
hypothetical protein GOS_4941392 [marine metagenome]


192
EDI67354
144073017
hypothetical protein GOS_393156 [marine metagenome]


193
AAY78594
67633343
predicted phytoene dehydrogenase [uncultured bacterium





MedeBAC82F10]


194
ECY07797
142438219
hypothetical protein GOS_2421570 [marine metagenome]


195
EDI16519
144002234
hypothetical protein GOS_477455 [marine metagenome]


196
EDH58504
143920724
hypothetical protein GOS_579102 [marine metagenome]


197
EAU52387
114549505
phytoene dehydrogenase CrtI [alpha proteobacterium HTCC2255]


198
ECX42733
142346738
hypothetical protein GOS_2540243 [marine metagenome]


199
EBE06505
134884139
hypothetical protein GOS_9826927 [marine metagenome]


200
EDB92338
142976670
hypothetical protein GOS_1568269 [marine metagenome]


201
EBN30363
136310418
hypothetical protein GOS_8268666 [marine metagenome]
















TABLE 18







Examples of phytoene synthase and lycopene cyclase polypeptides.









Accession
GI



Number
Number
Description





1613414C
227040
crtB gene


A49558
1076590
phytoene synthase 2 precursor - tomato (fragment)


AAA19428
506623
phytoene synthase [Neurospora crassa]


AAA32836
413732
phytoene synthase


AAA64982
148413
phytoene synthase [Pantoea agglomerans]


AAB87738
29893495
phytoene synthase [Rubrivivax gelatinosus]


AAC44849
1842243
phytoene synthase


AAD38051
13542332
phytoene synthase [Citrus × paradisi]


AAF78202
8650418
phytoene synthase [Bradyrhizobium sp. ORS278]


AAF82616
9081847
phytoene synthase [Tagetes erecta]


AAG10427
9971814
phytoene synthase [Tagetes erecta]


AAG28701
11066678
CrtB [Streptomyces griseus]


AAK07734
18476085
phytoene synthase [Oryza sativa (japonica cultivar-group)]


AAK07735
18476089
phytoene synthase [Oryza sativa (japonica cultivar-group)]


AAK15621
13195243
phytoene synthase [Haematococcus pluvialis]


AAL02001
15553721
phytoene synthase [Xanthobacter sp. Py2]


AAL76346
18645045
phytoene synthase [uncultured proteobacterium]


AAL82578
21326700
phytoene synthase radicle isoform [Oryza sativa (indica cultivar-




group)]


AAM45379
21360353
phytoene synthase [Tagetes erecta]


AAM48647
21328641
phytoene synthase [uncultured proteobacterium]


AAM62787
21553694
phytoene synthase [Arabidopsis thaliana]


AAM94363
22296799
phytoene synthase [Agromyces mediolanus]


AAN85600
27228294
Phytoene Synthase [Pantoea stewartii]


AAO24767
27903500
phytoene synthase [Citrus maxima]


AAO39835
28403302
phytoene synthase [Citrus sinensis]


AAO46895
37729028
lycopene cyclase/phytoene synthase [Blakeslea trispora]


AAO47570
33465823
phytoene-beta carotene synthase [Xanthophyllomyces dendrorhous]


AAO73816
33465821
crtYB [Xanthophyllomyces dendrorhous]


AAP22038
30349414
phytoene synthase 2 [Zea mays]


AAP55451
32350232
phytoene synthase 2 [Zea mays]


AAP55453
32350236
phytoene synthase 2 [Zea mays]


AAP55461
32350252
phytoene synthase 2 [Zea mays]


AAP55471
32350272
phytoene synthase 2 [Zea mays]


AAP55484
32350298
phytoene synthase 2 [Zea mays]


AAP55486
32350302
phytoene synthase 2 [Zea mays]


AAP56083
32349564
phytoene synthase [Zea mays]


AAP56124
32349646
phytoene synthase [Zea mays]


AAP56127
32349652
phytoene synthase [Zea mays]


AAP56136
32349670
phytoene synthase [Zea mays]


AAP56148
32349694
phytoene synthase [Zea mays]


AAP56155
32349708
phytoene synthase [Zea mays]


AAP56156
32349710
phytoene synthase [Zea mays]


AAP56157
32349712
phytoene synthase [Zea mays]


AAP56158
32349714
phytoene synthase [Zea mays]


AAP79176
32307542
phytoene synthase [Bigelowiella natans]


AAQ91837
37499616
phytoene synthase 2 [Zea mays]


AAR08445
38037628
chloroplast phytoene synthase 1 [Zea mays]


AAR31885
39842609
chloroplast phytoene synthase [Zea mays]


AAR37803
40062932
phytoene synthase [uncultured bacterium 442]


AAR37856
40062986
phytoene synthase [uncultured bacterium 443]


AAR86104
40456029
phytoene synthase [Momordica charantia var. abbreviata]


AAR87868
40557193
phytoene synthase [Oncidium cv. ‘Gower Ramsey’]


AAR98492
41018901
phytoene synthase [Bradyrhizobium sp. ORS278]


AAS02284
41394357
phytoene synthase 2 [Zea mays]


AAS17009
42491736
phytoene synthase 2 [Oryza sativa (japonica cultivar-group)]


AAS18307
42521626
phytoene synthase 1; PSY1 [Oryza sativa (indica cultivar-group)]


AAT28184
47498515
phytoene synthase [Dunaliella salina]


AAT35222
47531118
fusion of carotene synthesis proteins [synthetic construct]


AAT38473
47779181
chloroplast phytoene synthase precursor [Chlamydomonas




reinhardtii]


AAT46069
48686711
phytoene synthase [Dunaliella salina]


AAT74581
50313418
PSY [Citrus sinensis]


AAT90319
50952786
putative phytoene synthase [uncultured proteobacterium




eBACred25D05]


AAV74394
56122551
phytoene synthase [Adonis palaestina]


AAW23162
56698928
phytoene synthase [Rhodococcus erythropolis]


AC2035
25366683
phytoene synthase [imported] - Nostoc sp. (strain PCC 7120)


AC2035
25366683
phytoene synthase [imported] - Nostoc sp. (strain PCC 7120)


BAB18514
11344507
phytoene synthase [Citrus unshiu]


BAB79604
18143449
crtB [Pantoea agglomerans pv. milletiae]


BAD07278
40809739
phytoene synthase [Citrus sinensis]


BAD07286
40809755
phytoene synthase [Citrus limon]


BAD62106
54291340
phytoene synthase [Oryza sativa (japonica cultivar-group)]


BAD62107
54291341
phytoene synthase-like [Oryza sativa (japonica cultivar-group)]


C90061
25506636
squalene desaturase [imported] - Staphylococcus aureus (strain




N315)


CAA47625
19347
mutant phytoene synthase [Lycopersicon esculentum]


CAA68575
19341
unnamed protein product [Lycopersicon esculentum]


CAB07958
1934837
unknown [Bacillus subtilis]


CAB38740
4490590
phytoene synthase [Rhodobacter sphaeroides]


CAB51949
5690074
phytoene-beta carotene synthase [Xanthophyllomyces dendrorhous]


CAB56063
5912296
phytoene synthase [Paracoccus marcusii]


CAB86388
7453011
phytoene synthase/lycopene cyclase [Phycomyces blakesleeanus]


CAB93661
8250520
lycopene cyclase/phytoene synthase [Phycomyces blakesleeanus]


CAB94795
8574392
phytoene synthase [Mycobacterium aurum]


CAC19567
11990226
phytoene synthase [Helianthus annuus]


CAC27383
12584564
phytoene synthase [Helianthus annuus]


CAD19988
18307500
carotene cyclase [Gibberella fujikuroi]


CAD29284
57282088
putative phytoene synthase [Oryza sativa]


CAE76609
38567321
geranylgeranyl-diphosphate geranylgeranyltransferase (AL-2)




[Neurospora crassa]


E37802
95606
crtB protein - Erwinia uredovora


E84320
25410251
phytoene synthase [imported] - Halobacterium sp. NRC-1


EAA98758
42863045
unknown [environmental sequence]


EAB01965
42869439
unknown [environmental sequence]


EAB04170
42873822
unknown [environmental sequence]


EAB07138
42879858
unknown [environmental sequence]


EAB09791
42885235
unknown [environmental sequence]


EAB19826
42905452
unknown [environmental sequence]


EAB35029
42936011
unknown [environmental sequence]


EAB41375
42948740
unknown [environmental sequence]


EAB78706
43024004
unknown [environmental sequence]


EAB92586
43052355
unknown [environmental sequence]


EAC06949
43081493
unknown [environmental sequence]


EAC18360
43104624
unknown [environmental sequence]


EAC25793
43119723
unknown [environmental sequence]


EAC29883
43128092
unknown [environmental sequence]


EAC32813
43133973
unknown [environmental sequence]


EAC33105
43134560
unknown [environmental sequence]


EAC38486
43145552
unknown [environmental sequence]


EAC52233
43173313
unknown [environmental sequence]


EAC60029
43189028
unknown [environmental sequence]


EAC68026
43204953
unknown [environmental sequence]


EAC96197
43261031
unknown [environmental sequence]


EAD08701
43285745
unknown [environmental sequence]


EAD20866
43310220
unknown [environmental sequence]


EAD32755
43334458
unknown [environmental sequence]


EAD38008
43345761
unknown [environmental sequence]


EAD50152
43370658
unknown [environmental sequence]


EAD50402
43371147
unknown [environmental sequence]


EAD81123
43452903
unknown [environmental sequence]


EAD93882
43478303
unknown [environmental sequence]


EAE12860
43516265
unknown [environmental sequence]


EAE16121
43522884
unknown [environmental sequence]


EAE31084
43552634
unknown [environmental sequence]


EAE35665
43561764
unknown [environmental sequence]


EAE44717
43579862
unknown [environmental sequence]


EAE46627
43583580
unknown [environmental sequence]


EAE47846
43586023
unknown [environmental sequence]


EAE72264
43635190
unknown [environmental sequence]


EAE76009
43642573
unknown [environmental sequence]


EAE86335
43662748
unknown [environmental sequence]


EAE89581
43669163
unknown [environmental sequence]


EAF18881
43728007
unknown [environmental sequence]


EAF64277
43819669
unknown [environmental sequence]


EAF67931
43827263
unknown [environmental sequence]


EAF84745
43861327
unknown [environmental sequence]


EAF94004
43880040
unknown [environmental sequence]


EAG06083
43903395
unknown [environmental sequence]


EAG21950
43933540
unknown [environmental sequence]


EAG43625
43973477
unknown [environmental sequence]


EAG50171
43985555
unknown [environmental sequence]


EAG57517
43999205
unknown [environmental sequence]


EAG62787
44009110
unknown [environmental sequence]


EAG65580
44014171
unknown [environmental sequence]


EAG68110
44018715
unknown [environmental sequence]


EAG72283
44026322
unknown [environmental sequence]


EAG78750
44037938
unknown [environmental sequence]


EAG80445
44041116
unknown [environmental sequence]


EAG93220
44064453
unknown [environmental sequence]


EAH04927
44085694
unknown [environmental sequence]


EAH08972
44093217
unknown [environmental sequence]


EAH10377
44095788
unknown [environmental sequence]


EAH22151
44117864
unknown [environmental sequence]


EAH31461
44134654
unknown [environmental sequence]


EAH50033
44169323
unknown [environmental sequence]


EAH64480
44196848
unknown [environmental sequence]


EAH79040
44223009
unknown [environmental sequence]


EAH99976
44255671
unknown [environmental sequence]


EAI02786
44259828
unknown [environmental sequence]


EAI02787
44259829
unknown [environmental sequence]


EAI03575
44260943
unknown [environmental sequence]


EAI05900
44264266
unknown [environmental sequence]


EAI61004
44344824
unknown [environmental sequence]


EAI70669
44358327
unknown [environmental sequence]


EAI83938
44377067
unknown [environmental sequence]


EAJ05110
44406802
unknown [environmental sequence]


EAJ05569
44407471
unknown [environmental sequence]


EAJ08876
44412338
unknown [environmental sequence]


EAJ35156
44449986
unknown [environmental sequence]


EAJ38900
44455130
unknown [environmental sequence]


EAJ49645
44470504
unknown [environmental sequence]


EAJ54357
44477026
unknown [environmental sequence]


EAJ60475
44485647
unknown [environmental sequence]


EAJ64125
44492007
unknown [environmental sequence]


EAJ67499
44497025
unknown [environmental sequence]


EAJ76471
44510405
unknown [environmental sequence]


EAJ76950
44511114
unknown [environmental sequence]


EAJ78637
44513596
unknown [environmental sequence]


EAJ78787
44513824
unknown [environmental sequence]


EAJ79616
44515082
unknown [environmental sequence]


EAJ80356
44516200
unknown [environmental sequence]


EAJ81914
44518489
unknown [environmental sequence]


EAJ87417
44526623
unknown [environmental sequence]


EAK08514
44557109
unknown [environmental sequence]


EAK08523
44557119
unknown [environmental sequence]


EAK12901
44563097
unknown [environmental sequence]


EAK22180
44576315
unknown [environmental sequence]


EAK24859
44580262
unknown [environmental sequence]


EAK28345
44585276
unknown [environmental sequence]


EAK34732
44594324
unknown [environmental sequence]


EAK34736
44594329
unknown [environmental sequence]


EAK37296
44597942
unknown [environmental sequence]


EAK37521
44598256
unknown [environmental sequence]


EAK56335
44624430
unknown [environmental sequence]


G84363
25410528
hypothetical protein ggt [imported] - Halobacterium sp. NRC-1


NP_274195
15677043
phytoene synthase, putative [Neisseria meningitidis MC58]


NP_284085
15794263
poly-isoprenyl transferase [Neisseria meningitidis Z2491]


NP_294586
15805888
phytoene synthase [Deinococcus radiodurans R1]


NP_388961
16078144
hypothetical protein BSU10810 [Bacillus subtilis subsp. subtilis str.




168]


NP_441168
16330440
phytoene synthase [Synechocystis sp. PCC 6803]


NP_443763
16519643
Y4aC [Rhizobium sp. NGR234]


NP_624523
21218744
putative phytoene synthase [Streptomyces coelicolor A3(2)]


NP_630832
21225053
putative phytoene synthase [Streptomyces coelicolor A3(2)]


NP_662273
21674208
phytoene desaturase [Chlorobium tepidum TLS]


NP_682350
22299103
phytoene synthase [Thermosynechococcus elongatus BP-1]


NP_693381
23099915
phytoene synthase [Oceanobacillus iheyensis HTE831]


NP_786525
28379633
phytoene synthase [Lactobacillus plantarum WCFS1]


NP_822199
29827565
phytoene synthase [Streptomyces avermitilis MA-4680]


NP_822829
29828195
squalene/phytoene synthase [Streptomyces avermitilis MA-4680]


NP_851527
30795077
putative phytoene synthase [Streptomyces rochei]


NP_868799
32475805
probable phytoene synthase [Rhodopirellula baltica SH 1]


NP_874560
33239618
Phytoene synthase, CrtB [Prochlorococcus marinus subsp. marinus




str. CCMP1375]


NP_879992
33592348
putative phytoene synthase [Bordetella pertussis Tohama I]


NP_884101
33596458
putative phytoene synthase [Bordetella parapertussis 12822]


NP_889809
33602249
putative phytoene synthase [Bordetella bronchiseptica RB50]


NP_892264
33860703
Squalene and phytoene synthases [Prochlorococcus marinus subsp.




pastoris str. CCMP1986]


NP_895828
33864268
Squalene and phytoene synthases [Prochlorococcus marinus str. MIT




9313]


NP_898345
33866786
phytoene synthases [Synechococcus sp. WH 8102]


NP_902648
34498433
probable geranylgeranyl-diphosphate geranylgeranyltransferase




[Chromobacterium violaceum ATCC 12472


NP_902649
34498434
probable phytoene synthase-related protein [Chromobacterium




violaceum ATCC 12472]


NP_924690
37521313
phytoene synthase [Gloeobacter violaceus PCC 7421]


NP_931516
37528171
phytoene synthase [Photorhabdus luminescens subsp. laumondii




TTO1]


NP_946861
39934585
CrtB phytoene synthase [Rhodopseudomonas palustris CGA009]


NP_949079
39936803
putative poly-isoprenyl transferase [Rhodopseudomonas palustris




CGA009]


NP_962005
41409169
hypothetical protein MAP3071 [Mycobacterium avium subsp.




paratuberculosis str. k10]


NP_968601
42523221
phytoene synthase [Bdellovibrio bacteriovorus HD100]


O07333
3913360
Phytoene synthase


P08196
585746
Phytoene synthase 1, chloroplast precursor (Fruit ripening specific




protein pTOM5)


P21683
30923192
Phytoene synthase


P37269
585009
Phytoene synthase


P37271
27735222
Phytoene synthase, chloroplast precursor


P37272
585749
Phytoene synthase, chloroplast precursor


P53797
1709885
Phytoene synthase, chloroplast precursor


P54975
1706137
Phytoene synthase


P54977
1706139
Phytoene synthase


P65860
54041032
Probable phytoene synthase


Q9SSU8
8928282
Phytoene synthase, chloroplast precursor


Q9UUQ6
34922667
CarRP protein [Includes: Lycopene cyclase; Phytoene synthase]


S22474
7489041
phytoene synthase (EC 2.5.1.—) - tomato


S32170
321671
phytoene synthetase - Myxococcus xanthus


S52587
1073300
prephytoene pyrophosphate synthase - Erwinia herbicola


S56668
2129505
geranylgeranyl-diphosphate geranylgeranyltransferase (EC 2.5.1.32)




precursor - muskmelon


S68307
2130144
phytoene synthase - maize


T10702
7484346
phytoene synthase (EC 2.5.1.—) - green alga (Dunaliella bardawil)


T46594
11291807
phytoene synthase (EC 2.5.1.—) [validated] - Mycobacterium




marinum


T50746
11356347
phytoene synthase (EC 2.5.1.—) [imported] - Rhodobacter sphaeroides


T50895
11291816
prephytoene pyrophosphate synthase [imported] - Rubrivivax




gelatinosus


XP_324765
32408567
PHYTOENE SYNTHASE [Neurospora crassa]


XP_383242
46114448
hypothetical protein FG03066.1 [Gibberella zeae PH-1]


XP_403902
49080862
hypothetical protein UM06287.1 [Ustilago maydis 521]


YP_006040
46255128
phytoene synthase [Thermus thermophilus HB27]


YP_103126
53723680
phytoene synthase, putative [Burkholderia mallei ATCC 23344]


YP_112342
53723357
squalene/phytoene synthase [Burkholderia pseudomallei K96243]


YP_117945
54023703
putative phytoene synthase [Nocardia farcinica IFM 10152]


YP_120611
54026369
putative phytoene synthase [Nocardia farcinica IFM 10152]


YP_136628
55378778
lycopene cyclase [Haloarcula marismortui ATCC 43049]


YP_136629
55378779
phytoene synthase [Haloarcula marismortui ATCC 43049]


YP_145340
55978284
phytoene synthase [Thermus thermophilus HB8]


YP_145343
55978287
phytoene synthase-related protein [Thermus thermophilus HB8]


YP_160917
56479328
probable terpenoid synthase-related protein [Azoarcus sp. EbN1]


YP_160918
56479329
putative terpenoid synthase [Azoarcus sp. EbN1]


YP_162605
56551766
phytoene/squalene synthetase [Zymomonas mobilis subsp. mobilis




ZM4]


YP_172822
56752121
phytoene synthase [Synechococcus elongatus PCC 6301]


YP_187369
57652299
dehydrosqualene synthase [Staphylococcus aureus subsp. aureus




COL]


YP_192648
58040684
Putative phytoene synthase [Gluconobacter oxydans 621H]


ZP_000044
22956752
COG1562: Phytoene/squalene synthetase [Rhodobacter sphaeroides




2.4.1]


ZP_001091
53688068
COG1562: Phytoene/squalene synthetase [Nostoc punctiforme PCC




73102]


ZP_001591
53763709
COG1562: Phytoene/squalene synthetase [Anabaena variabilis ATCC




29413]


ZP_001657
45514234
COG1562: Phytoene/squalene synthetase [Ralstonia eutropha




JMP134]


ZP_001690
46132223
COG1562: Phytoene/squalene synthetase [Ralstonia eutropha




JMP134]


ZP_001746
45523280
COG1562: Phytoene/squalene synthetase [Crocosphaera watsonii




WH 8501]


ZP_001837
53771530
COG1562: Phytoene/squalene synthetase [Exiguobacterium sp. 255-




15]


ZP_001867
45546711
COG1562: Phytoene/squalene synthetase [Rubrobacter xylanophilus




DSM 9941]


ZP_002096
46204978
COG1562: Phytoene/squalene synthetase [Magnetospirillum




magnetotacticum MS-1]


ZP_002248
46324513
COG1562: Phytoene/squalene synthetase [Burkholderia cepacia




R1808]


ZP_002450
47575031
COG1562: Phytoene/squalene synthetase [Rubrivivax gelatinosus




PM1]


ZP_002680
48763469
COG1562: Phytoene/squalene synthetase [Rhodospirillum rubrum]


ZP_002710
48766450
COG1562: Phytoene/squalene synthetase [Rhodospirillum rubrum]


ZP_002791
48782680
COG1562: Phytoene/squalene synthetase [Burkholderia fungorum




LB400]


ZP_002892
48832182
COG1562: Phytoene/squalene synthetase [Magnetococcus sp. MC-1]


ZP_002916
48834623
COG1562: Phytoene/squalene synthetase [Thermobifida fusca]


ZP_003036
48849426
COG1562: Phytoene/squalene synthetase [Novosphingobium




aromaticivorans DSM 12444]


ZP_003269
48893702
COG1562: Phytoene/squalene synthetase [Trichodesmium




erythraeum IMS101]


ZP_003351
52007802
COG1562: Phytoene/squalene synthetase [Thiobacillus denitrificans




ATCC 25259]


ZP_003487
53730362
COG1562: Phytoene/squalene synthetase [Dechloromonas aromatica




RCB]


ZP_003501
53759405
COG1562: Phytoene/squalene synthetase [Methylobacillus




flagellatus KT]


ZP_003591
53798896
COG1562: Phytoene/squalene synthetase [Chloroflexus aurantiacus]


ZP_003628
54030691
COG1562: Phytoene/squalene synthetase [Polaromonas sp. JS666]
















TABLE 19







Examples of carotenoid ketolase polypeptides.









Accession
GI



Number
Number
Description





AAA99932
609575
fatty acid desaturase


AAB48668
1870215
ORF [Emericella nidulans]


AAC25611
2541936
unknown [Pseudomonas syringae]


AAF78203
8650419
beta-carotene ketolase [Bradyrhizobium sp. ORS278]


AAH16427
16741158
2210008A03Rik protein [Mus musculus]


AAN03484
22597194
BKT [Haematococcus pluvialis]


AAN85497
26541510
putative fatty acid desaturase [Streptomyces atroolivaceus]


AAN86030
33439708
beta-carotene C4 oxygenase [Brevundimonas aurantiaca]


AAO64399
28976134
putative beta-carotene ketolase [Nodularia spumigena]


AAQ23139
33621091
CrtW/CrtY fusion protein [synthetic construct]


AAT35222
47531118
fusion of carotene synthesis proteins [synthetic construct]


AAT35555
47558911
beta-carotene ketolase [Haematococcus pluvialis]


AAV41372
55139370
beta-carotene ketolase/oxygenase [‘Chlorella’ zofingiensis]


AB2307
25530134
hypothetical protein alr4009 [imported] - Nostoc sp. (strain PCC




7120)


AF2204
25533132
beta-carotene ketolase [imported] - Nostoc sp. (strain PCC 7120)


BAB54999
14028447
mlr9395 [Mesorhizobium loti MAFF303099]


BAB58879
14270087
membrane fatty acid desaturase [Toxoplasma gondii]


BAC98366
37360914
alkane hydroxylase [Alcanivorax borkumensis]


CAA60478
2654318
beta-carotene C-4 oxygenase (ketolase) [Haematococcus pluvialis]


CAB56059
5912292
beta-carotene C-4-oxygenase (ketolase) [Paracoccus marcusii]


D87673
25398945
conserved hypothetical protein CC3422 [imported] - Caulobacter




crescentus


EAA79304
42823978
unknown [environmental sequence]


EAA80363
42826055
unknown [environmental sequence]


EAA81403
42828115
unknown [environmental sequence]


EAA84711
42834481
unknown [environmental sequence]


EAB82380
43031476
unknown [environmental sequence]


EAB86624
43040184
unknown [environmental sequence]


EAC05755
43079085
unknown [environmental sequence]


EAD12219
43292778
unknown [environmental sequence]


EAD71182
43427899
unknown [environmental sequence]


EAD94927
43480380
unknown [environmental sequence]


EAF11582
43712986
unknown [environmental sequence]


EAF98072
43888329
unknown [environmental sequence]


EAG19345
43928738
unknown [environmental sequence]


EAG38273
43963688
unknown [environmental sequence]


EAG79800
44039853
unknown [environmental sequence]


EAG96474
44070318
unknown [environmental sequence]


EAH00349
44077315
unknown [environmental sequence]


EAH36448
44143633
unknown [environmental sequence]


EAH40683
44151265
unknown [environmental sequence]


EAH53180
44175316
unknown [environmental sequence]


EAH96648
44250729
unknown [environmental sequence]


EAI05260
44263397
unknown [environmental sequence]


EAI17468
44281329
unknown [environmental sequence]


EAI53009
44333409
unknown [environmental sequence]


EAI54054
44334878
unknown [environmental sequence]


EAI67818
44354362
unknown [environmental sequence]


EAI68153
44354875
unknown [environmental sequence]


EAI89684
44384943
unknown [environmental sequence]


EAJ27674
44439188
unknown [environmental sequence]


EAJ45589
44464684
unknown [environmental sequence]


EAJ45589
44464684
unknown [environmental sequence]


EAJ67118
44496466
unknown [environmental sequence]


EAJ74221
44507022
unknown [environmental sequence]


EAJ74653
44507662
unknown [environmental sequence]


EAJ88396
44528064
unknown [environmental sequence]


EAJ88887
44528792
unknown [environmental sequence]


EAK06069
44553531
unknown [environmental sequence]


EAK11467
44561166
unknown [environmental sequence]


EAK16824
44568733
unknown [environmental sequence]


EAK28828
44585942
unknown [environmental sequence]


EAK28828
44585942
unknown [environmental sequence]


EAK31112
44589271
unknown [environmental sequence]


EAK42591
44605441
unknown [environmental sequence]


NP_045063
11465545
fatty-acid desaturase [Cyanidium caldarium]


NP_081575
27754029
sphingolipid delta 4 desaturase/C-4 hydroxylase [Mus musculus]


NP_338204
15843167
fatty acid desaturase, putative/ferredoxin reductase, electron transfer




component [Mycobacterium tuberculosis CDC1551]


NP_440788
16330060
b-carotene hydroxylase [Synechocystis sp. PCC 6803]


NP_441220
16330492
hypothetical protein sl11611 [Synechocystis sp. PCC 6803]


NP_682690
22299443
beta-carotene hydroxylase [Thermosynechococcus elongatus BP-1]


NP_770721
27379192
hypothetical protein blr4081 [Bradyrhizobium japonicum USDA 110]


NP_848964
30468077
beta-carotene hydroxylase [Cyanidioschyzon merolae strain 10D]


NP_857223
31794730
POSSIBLE ELECTRON TRANSFER PROTEIN FDXB




[Mycobacterium bovis AF2122/97]


NP_881760
33594116
putative fatty acid desaturase [Bordetella pertussis Tohama I]


NP_882469
33594826
putative fatty acid desaturase [Bordetella parapertussis 12822]


NP_886657
33599097
putative fatty acid desaturase [Bordetella bronchiseptica RB50]


NP_895643
33864083
beta carotene hydroxylase [Prochlorococcus marinus str. MIT 9313]


NP_896386
33864827
beta-carotene hydroxylase [Synechococcus sp. WH 8102]


NP_897461
33865902
possible beta-carotene ketolase [Synechococcus sp. WH 8102]


NP_924674
37521297
beta-carotene ketolase [Gloeobacter violaceus PCC 7421]


NP_927525
37524181
hypothetical protein plu0159 [Photorhabdus luminescens subsp.




laumondii TTO1]


NP_947075
39934799
Fatty acid desaturase family [Rhodopseudomonas palustris CGA009]


P54972
1706150
Beta-carotene ketolase (Beta-carotene oxygenase)


Q39982
2498257
Beta-carotene ketolase (Beta-carotene oxygenase)


Q44261
2498256
Beta-carotene ketolase (Beta-carotene oxygenase)


T31123
11361063
hypothetical protein 15 - Sphingomonas aromaticivorans plasmid




pNL1


XP_330780
32420673
hypothetical protein [Neurospora crassa]


XP_368852
39974923
hypothetical protein MG00392.4 [Magnaporthe grisea 70-15]


XP_380194
46102628
hypothetical protein FG00018.1 [Gibberella zeae PH-1]


XP_383758
46115480
hypothetical protein FG03582.1 [Gibberella zeae PH-1]


XP_405100
49086048
hypothetical protein AN0963.2 [Aspergillus nidulans FGSC A4]


XP_409222
49095522
hypothetical protein AN5085.2 [Aspergillus nidulans FGSC A4]


YP_102417
53725671
alkane-1 monooxygenase [Burkholderia mallei ATCC 23344]


YP_108945
53719959
putative alkane monooxygenase [Burkholderia pseudomallei K96243]


YP_132414
54302421
hypothetical putative delta-9 fatty acid desaturase [Photobacterium




profundum SS9]


YP_154670
56459389
Fatty-acid desaturase [Idiomarina loihiensis L2TR]


YP_166682
56696325
fatty acid desaturase family protein [Silicibacter pomeroyi DSS-3]


YP_168846
56698471
fatty acid desaturase family protein [Silicibacter pomeroyi DSS-3]


YP_172377
56751676
beta-carotene hydroxylase [Synechococcus elongatus PCC 6301]


ZP_001068
23124870
COG3239: Fatty acid desaturase [Nostoc punctiforme PCC 73102]


ZP_001112
53688676
COG3239: Fatty acid desaturase [Nostoc punctiforme PCC 73102]


ZP_001607
53764743
COG3239: Fatty acid desaturase [Anabaena variabilis ATCC 29413]


ZP_001757
46118877
COG3239: Fatty acid desaturase [Crocosphaera watsonii WH 8501]


ZP_001787
53736018
COG3239: Fatty acid desaturase [Crocosphaera watsonii WH 8501]


ZP_002218
46321435
COG3239: Fatty acid desaturase [Burkholderia cepacia R1808]


ZP_002456
47575608
COG3239: Fatty acid desaturase [Rubrivivax gelatinosus PM1]


ZP_003028
48848557
COG3239: Fatty acid desaturase [Novosphingobium aromaticivorans




DSM 12444]


ZP_003107
48856640
COG3239: Fatty acid desaturase [Cytophaga hutchinsonii]


ZP_003264
48893204
COG3239: Fatty acid desaturase [Trichodesmium erythraeum




IMS101]


ZP_003458
53688805
hypothetical protein Npun02000865 [Nostoc punctiforme PCC




73102]


ZP_003513
53763576
COG3239: Fatty acid desaturase [Anabaena variabilis ATCC 29413]
















TABLE 20







Examples of carotenoid hydroxylase polypeptides.









Accession
GI



Number
Number
Description





AAC44852
1842246
b-carotene hydroxylase


AAC49443
1575296
beta-carotene hydroxylase [Arabidopsis thaliana]


AAD54243
5852870
carotenoid hydroxylase [Haematococcus pluvialis]


AAG10430
9971820
beta hydroxylase [Tagetes erecta]


AAG10793
9988836
beta-carotene hydroxylase [Citrus unshiu]


AAG33636
11245486
beta-carotene hydroxylase [Citrus unshiu]


AAL80006
19071768
beta carotene hydroxylase [Sandersonia aurantiaca]


AAM44971
21280903
putative beta-carotene hydroxylase [Arabidopsis thaliana]


AAM51300
21436107
putative beta-carotene hydroxylase [Arabidopsis thaliana]


AAM77007
21734857
beta-carotene hydroxylase [Vitis vinifera]


AAN85601
27228295
Beta-Carotene Hydroxylase [Pantoea stewartii]


AAO53295
28911949
carotenoid hydroxylase [Haematococcus pluvialis]


AAS48097
44887642
beta-carotene hydroxylase [Citrus sinensis]


AAS55552
45184599
putative beta-carotene hydroxylase [Brassica rapa]


AAS88426
46326968
beta-carotene hydroxylase [Glycine max]


AAT48741
49036137
beta-carotene hydroxylase [Citrus sinensis]


AAT84408
50844570
beta carotene hydroxylase [Crocus sativus]


AAV85452
56267980
beta-ring oxygenase AdKeto1 [Adonis palaestina]


AAV85453
56267982
beta-ring oxygenase AdKeto2 [Adonis palaestina]


BAA14129
216687
crtZ [Pantoea ananatis]


BAB79605
18143450
crtZ [Pantoea agglomerans pv. milletiae]


BAC77670
31790567
gamma-carotene hydroxylase [marine bacterium P99-3]


BAD07283
40809749
beta-ring hydroxylase [Citrus sinensis]


BAD07291
40809765
beta-ring hydroxylase [Citrus limon]


CAA70427
2956671
beta-carotene hydrolase [Capsicum annuum]


CAA70888
2956717
beta-carotene hydroxylase 2 [Capsicum annuum]


CAB55625
5870598
beta-carotene hydroxylase [Lycopersicon esculentum]


CAB55626
5870600
beta-carotene hydroxylase [Lycopersicon esculentum]


CAB56060
5912293
carotene hydroxylase [Paracoccus marcusii]


CAC06712
9968545
beta-carotene hydroxylase [Narcissus pseudonarcissus]


CAC95130
33145986
beta-carotene hydroxylase [Crocus sativus]


EAB30128
42926157
unknown [environmental sequence]


EAC49462
43167766
unknown [environmental sequence]


EAC86129
43241003
unknown [environmental sequence]


EAD61089
43395962
unknown [environmental sequence]


EAD76156
43443111
unknown [environmental sequence]


EAD88640
43467793
unknown [environmental sequence]


EAE27903
43546376
unknown [environmental sequence]


EAE28203
43546980
unknown [environmental sequence]


EAE78743
43647896
unknown [environmental sequence]


EAF12173
43714211
unknown [environmental sequence]


EAH29370
44130906
unknown [environmental sequence]


EAH44202
44158360
unknown [environmental sequence]


EAI00766
44256844
unknown [environmental sequence]


EAI29017
44298625
unknown [environmental sequence]


EAJ30844
44443849
unknown [environmental sequence]


EAJ72524
44504516
unknown [environmental sequence]


EAK10611
44559981
unknown [environmental sequence]


EAK53455
44620561
unknown [environmental sequence]


EAK63955
44635271
unknown [environmental sequence]


H90469
25394049
beta carotene hydroxylase (crtZ) [imported] - Sulfolobus




solfataricus


NP_745389
26989964
beta-carotene hydroxylase [Pseudomonas putida KT2440]


NP_922503
37536402
putative beta-carotene hydroxylase [Oryza sativa (japonica




cultivar-group)]


P54973
1706152
Beta-carotene hydroxylase


Q44262
2498258
Beta-carotene hydroxylase


S52982
1073291
beta-carotene hydroxylase - Erwinia herbicola


XP_473611
50928167
OSJNBa0011J08.7 [Oryza sativa (japonica cultivar-group)]


YP_024309
48478603
beta carotene hydroxylase [Picrophilus torridus DSM 9790]


ZP_003055
48851297
COG3000: Sterol desaturase [Novosphingobium aromaticivorans




DSM 12444]


ZP_003107
48856620
COG3000: Sterol desaturase [Cytophaga hutchinsonii]
















TABLE 21







Examples of astaxanthin synthase polypeptides


and putative astaxanthin synthase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





AAM56288
21501451
Astaxanthin synthase [Xanthophyllomyces dendrorhous]


XP_571276
58268240
Cytochrome P450, putative [Cryptococcus neoformans var. neoformans




JEC21]


EAL20013
50257304
hypothetical protein CNBF3400 [Cryptococcus neoformans var.




neoformans B-3501A]


XP_401804
49075484
hypothetical protein UM04189.1 [Ustilago maydis 521]


XP_397817
49067054
hypothetical protein UM00202.1 [Ustilago maydis 521]


XP_399595
49070612
hypothetical protein UM01980.1 [Ustilago maydis 521]


XP_403279
49079218
hypothetical protein UM05664.1 [Ustilago maydis 521]


XP_382294
46110473
hypothetical protein FG02118.1 [Gibberella zeae PH-1]


XP_406021
49088382
hypothetical protein AN1884.2 [Aspergillus nidulans FGSC A4]


XP_381224
46108332
hypothetical protein FG01048.1 [Gibberella zeae PH-1]


XP_391479
46139577
hypothetical protein FG11303.1 [Gibberella zeae PH-1]


XP_569261
58264210
conserved hypothetical protein [Cryptococcus neoformans var.




neoformans JEC21]


EAL22841
50260180
hypothetical protein CNBB0620 [Cryptococcus neoformans var.




neoformans B-3501A]


XP_359866
39940658
hypothetical protein MG04911.4 [Magnaporthe grisea 70-15]
















TABLE 22







Examples of carotenoid epsilon hydroxylase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





ABB52076
79155148
putative epsilon-ring carotene hydroxylase [Daucus carota




subsp. sativus]


BAD94136
62319017
Cytochrom P450-like protein [Arabidopsis thaliana]


ABD28565
87162770
E-class P450, group I [Medicago truncatula]


AAT28222
47498772
putative 97B2-like cytochrome P450 [Ginkgo biloba]


ABC68396
85001685
cytochrome P450 monooxygenase CYP97A [Glycine max]


ABC59110
84514203
cytochrome P450 monooxygenase CYP97B [Medicago




truncatula]


NP_190881
42565881
LUT1 (LUTEIN DEFICIENT 1); oxygen binding




[Arabidopsis thaliana]


ABB47954
78708979
cytochrome P450 monooxygenase, putative [Oryza sativa




(japonica cultivar-group)]


NP_922604
37536604
putative cytochrome P450 monooxygenase [Oryza sativa




(japonica cultivar-group)]
















TABLE 23







Examples of lycopene cyclase polypeptides, beta and epsilon subunits.









ACCESSION
GI
PROTEIN DESCRIPTION





XP_001422490
145356548
predicted protein [Ostreococcus lucimarinus CCE9901]


BAE94036
94481238
lycopene epsilon cyclase (Diospyros kaki )


AAK07431
12746307
lycopene epsilon-cyclase [Adonis palaestina]


ABB52073
79154988
putative lycopene epsilon cyclase [Daucus carota subsp.




sativus]


Q38932
27735211
Lycopene epsilon cyclase, chloroplast precursor


AAB53336
1399181
lycopene epsilon cyclase


AAG10428
9971816
epsilon cyclase [Tagetes erecta]


AAK07434
12746313
lycopene epsilon-cyclase [Lactuca sativa]


AAM45382
21360359
epsilon cyclase [Tagetes erecta]


O65837
11132841
Lycopene epsilon cyclase, chloroplast precursor


AAL69394
18419661
lycopene epsilon-cyclase [Spinacia oleracea]


BAE79549
87299433
lycopene epsilon-cyclase [Chrysanthemum × morifolium]


XP_463351
50901836
putative lycopene epsilon-cyclase [Oryza sativa (japonica




cultivar-group)]


AAS48096
44887640
epsilon lycopene cyclase [Citrus sinensis]


AAX92679
62638188
lycopene epsilon cyclase [Citrus maxima]


AAL92114
19569601
lycopene epsilon-cyclase [Citrus × paradisi]


AAK07433
12746311
lycopene epsilon-cyclase [Solanum tuberosum]


AAL47019
17864021
lycopene epsilon-cyclase [Citrus sinensis]


AAT46065
48686703
chloroplast lycopene epsilon-cyclase precursor




[Chlamydomonas reinhardtii]


BAD07293
40809769
lycopene epsilon-cyclase [Citrus limon]


BAD07285
40809753
lycopene epsilon-cyclase [Citrus sinensis]


BAD07277
40809737
lycopene epsilon-cyclase [Citrus unshiu]


EAJ62839
44489138
unknown [environmental sequence]


BAE43547
73993068
putative lycopene beta cyclase [Taxodium distichum var.




distichum]


BAE43550
73993074
putative lycopene beta cyclase [Taxodium distichum var.




distichum]


BAE43557
73993088
putative lycopene beta cyclase [Taxodium distichum var.




imbricarium]


BAE43558
73993090
putative lycopene beta cyclase [Taxodium distichum var.




imbricarium]


BAE43553
73993080
putative lycopene beta cyclase [Taxodium distichum var.




imbricarium]


BAE43545
73993064
putative lycopene beta cyclase [Taxodium distichum var.




distichum]


BAE43556
73993086
putative lycopene beta cyclase [Taxodium distichum var.




imbricarium]


BAE43552
73993078
putative lycopene beta cyclase [Taxodium distichum var.




distichum]


BAE43560
73993094
putative lycopene beta cyclase [Taxodium distichum var.




imbricarium]


BAE43554
73993082
putative lycopene beta cyclase [Taxodium distichum var.




imbricarium]


BAE43551
73993076
putative lycopene beta cyclase [Taxodium distichum var.




distichum]


BAE43519
73993012
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43535
73993044
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43541
73993056
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43542
73993058
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43517
73993008
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43534
73993042
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43537
73993048
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43533
73993040
putative lycopene beta cyclase [Cryptomeria japonica]


BAD02774
38603277
putative lycopene beta cyclase [Cryptomeria japonica]


BAD02766
38603261
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43540
73993054
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43514
73993002
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43544
73993062
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43538
73993050
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43528
73993030
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43546
73993066
putative lycopene beta cyclase [Taxodium distichum var.




distichum]


BAE43526
73993026
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43543
73993060
putative lycopene beta cyclase [Cryptomeria japonica]


BAD02742
38603213
putative lycopene beta cyclase [Cryptomeria japonica]


BAD02770
38603269
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43522
73993018
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43559
73993092
putative lycopene beta cyclase [Taxodium distichum var.




imbricarium]


BAE43527
73993028
putative lycopene beta cyclase [Cryptomeria japonica]


BAE43548
73993070
putative lycopene beta cyclase [Taxodium distichum var.




distichum]


AAF44700
14550425
lycopene beta-cyclase [Citrus sinensis]


BAE43555
73993084
putative lycopene beta cyclase [Taxodium distichum var.




imbricarium]


BAE43549
73993072
putative lycopene beta cyclase [Taxodium distichum var.




distichum]


AAU14144
51922063
lycopene beta-cyclase [Citrus sinensis]


AAN86060
27261727
lycopene cyclase [Citrus unshiu]


AAR89632
40756518
lycopene-beta-cyclase [Citrus maxima]


AAM21152
20530862
lycopene beta-cyclase [Citrus sinensis]


AAD38049
13959731
lycopene cyclase [Citrus × paradisi]


AAU05146
51511939
lycopene beta-cyclase [Citrus sinensis]


AAU05145
51511937
lycopene beta-cyclase [Citrus sinensis]


AAK07430
12746305
lycopene beta-cyclase [Adonis palaestina]


ABB72443
82394885
lycopene beta-cyclase [Citrus sinensis]


BAE79544
87299423
lycopene beta-cyclase [Chrysanthemum × morifolium]


BAE78471
85717882
lycopene beta cyclase [Taraxacum officinale]


Q43415
11133019
Lycopene beta cyclase, chloroplast precursor


AAF23013
6665782
lycopene epsilon-cyclase [Daucus carota]


ABB52071
79154899
putative lycopene beta cyclase [Daucus carota subsp.




sativus]


AAW88382
59665024
lycopene beta-cyclase [Lycium barbarum]


AAG10429
9971818
beta cyclase [Tagetes erecta]


AAM45381
21360357
beta cyclase [Tagetes erecta]


AAM14335
20259239
putative lycopene beta cyclase [Arabidopsis thaliana]


AAO18661
27728515
lycopene beta-cyclase [Zea mays]


AAA81880
735882
lycopene cyclase


Q43503
11133022
Lycopene beta cyclase, chloroplast precursor


S66350
2129931
lycopene beta-cyclase (EC 5.5.1.—) - tomato


XP_464409
50905841
putative lycopene beta-cyclase [Oryza sativa (japonica




cultivar-group)]


CAD70565
45237491
lycopene cyclase [Bixa orellana]


Q43578
11133025
Lycopene beta cyclase, chloroplast precursor


AAL92175
19569782
beta-lycopene cyclase [Sandersonia aurantiaca]


AAX54906
61742130
putative chloroplast lycopene beta cyclase precursor




[Chlamydomonas reinhardtii]


S66349
2129954
lycopene beta-cyclase (EC 5.5.1.—) - common tobacco


AAG21133
10644119
chromoplast-specific lycopene beta-cyclase [Lycopersicon




esculentum]


CAB92977
8247354
neoxanthin synthase [Solanum tuberosum]


CAB93342
8249885
neoxanthin synthase [Lycopersicon esculentum]


Q9SEA0
11131528
Capsanthin/capsorubin synthase, chloroplast precursor


Q42435
12643508
Capsanthin/capsorubin synthase, chloroplast precursor


AAO64977
37730608
lycopene beta cyclase [Haematococcus pluvialis]


Q40424
11133011
Lycopene beta cyclase, chloroplast precursor


ABB52072
79154940
putative capsanthin-capsorubin synthase [Daucus carota




subsp. sativus]


AAQ02668
33304511
lycopene cyclase [Setaria italica]


CAA54961
840729
putative chromoplastic oxydo-reductase [Capsicum




annuum]


EAJ62838
44489136
unknown [environmental sequence]


YP_401079
81300871
Lycopene cyclase, beta and epsilon [Synechococcus




elongatus PCC 7942]


YP_172741
56752040
lycopene cyclase [Synechococcus elongatus PCC 6301]


ZP_011 . . .
88808972
lycopene beta cyclase [Synechococcus sp. WH 7805]


EAK50052
44615956
unknown [environmental sequence]


NP_892751
33861190
putative lycopene epsilon cyclase [Prochlorococcus




marinus subsp. pastoris str. CCMP1986]


NP_875182
33240240
Lycopene epsilon cyclase [Prochlorococcus marinus subsp.




marinus str. CCMP1375]


YP_382237
78213458
Lycopene cyclase, beta and epsilon [Synechococcus sp.




CC9605]


YP_397130
78779018
Lycopene cyclase, beta and epsilon [Prochlorococcus




marinus str. MIT 9312]


NP_896821
33865262
lycopene beta cyclase [Synechococcus sp. WH 8102]


YP_397570
78779458
Lycopene cyclase, beta and epsilon [Prochlorococcus




marinus str. MIT 9312]


ZP_010 . . .
87302144
lycopene cyclase [Synechococcus sp. WH 5701]


EAK17149
44569190
unknown [environmental sequence]


YP_291882
72382527
lycopene cyclase, beta and epsilon [Prochlorococcus




marinus str. NATL2A]


NP_875528
33240586
Lycopene beta cyclase related dehydrogenase




[Prochlorococcus marinus subsp. marinus str. CCMP1375]


NP_893181
33861620
putative lycopene beta cyclase [Prochlorococcus marinus




subsp. pastoris str. CCMP1986]


NP_895600
33864040
putative lycopene epsilon cyclase [Prochlorococcus




marinus str. MIT 9313]


EAI47456
44325573
unknown [environmental sequence]


YP_291268
72381913
lycopene cyclase, beta and epsilon [Prochlorococcus




marinus str. NATL2A]


ZP_010 . . .
84517806
Lycopene beta cyclase related dehydrogenase




[Prochlorococcus marinus str. MIT 9211]


AAF34191
6970079
lycopene epsilon cyclase [Daucus carota]


ZP_010 . . .
84518202
Lycopene epsilon cyclase [Prochlorococcus marinus str.




MIT 9211]


YP_376736
78184301
Lycopene cyclase, beta and epsilon [Synechococcus sp.




CC9902]


ZP_003 . . .
66796756
Lycopene cyclase, beta and epsilon [Deinococcus




geothermalis DSM 11300]


NP_894954
33863394
putative lycopene beta cyclase [Prochlorococcus marinus




str. MIT 9313]


AAT76051
50365502
lycopene cyclase [Citrus clementina]


EAK22047
44576122
unknown [environmental sequence]


NP_294525
15805827
lycopene cyclase [Deinococcus radiodurans R1]
















TABLE 24







Examples of carotenoid glucosyltransferase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





AAA21261
148395
CrtX [Pantoea agglomerans]


AAN85597
27228291
Zeaxanthin Glucosyl Transferase [Pantoea stewartii]


BAB79601
18143446
crtX [Pantoea agglomerans pv. milletiae]


AAZ73147
72536082
zeaxanthin glucosyl transferase [Enterobacteriaceae bacterium




DC413]


AAZ73128
72536060
zeaxanthin glucosyl transferase [Enterobacteriaceae bacterium




DC260]


AAZ73140
72536074
zeaxanthin glucosyl transferase [Enterobacteriaceae bacterium




DC416]


Q01330
231911
Zeaxanthin glucosyl transferase


ZP_006 . . .
71674312
UDP-glycosyltransferase, MGT [Trichodesmium erythraeum




IMS101]


NP_439972
16329244
zeaxanthin glucosyl transferase [Synechocystis sp. PCC 6803]


EAH29368
44130903
unknown [environmental sequence]


ZP_005 . . .
67926135
zeaxanthin glucosyl transferase, hypothetical protein




[Crocosphaera watsonii WH 8501]


YP_378763
78188425
hypothetical protein Cag_0447 [Chlorobium chlorochromatii




CaD3]


ZP_005 . . .
68549418
Glycosyl transferase, group 1 [Pelodictyon phaeoclathratiforme




BU-1]


ZP_010 . . .
85713606
glycosyl transferase, group 1 [Nitrobacter sp. Nb-311A]


YP_317171
75674750
glycosyl transferase, group 1 [Nitrobacter winogradskyi Nb-




255]


ZP_006 . . .
69929171
Glycosyl transferase, group 1 [Nitrobacter hamburgensis X14]


ZP_009 . . .
84500589
hypothetical protein OB2597_11541 [Oceanicola batsensis




HTCC2597]


ZP_009 . . .
83953176
hypothetical protein NAS141_12746 [Sulfitobacter sp. NAS-




14.1]


ZP_009 . . .
83942121
hypothetical protein EE36_07793 [Sulfitobacter sp. EE-36]


YP_508020
89052569
glycosyl transferase, group 1 [Jannaschia sp. CCS1]


ZP_010 . . .
85704103
hypothetical protein ROS217_13931 [Roseovarius sp. 217]


ZP_009 . . .
83370850
probable glycosyltransferase [Rhodobacter sphaeroides ATCC




17025]


ZP_006 . . .
69934465
Glycosyl transferase, group 1 [Paracoccus denitrificans




PD1222]


ZP_009 . . .
83949880
probable glycosyltransferase [Roseovarius nubinhibens ISM]


YP_376237
78183803
putative glycosyltransferase [Synechococcus sp. CC9902]


YP_376129
78183695
probable glycosyltransferase [Synechococcus sp. CC9902]


YP_374296
78186253
hypothetical protein Plut_0365 [Pelodictyon luteolum DSM




273]


ZP_010 . . .
87301651
Putative glycosyltransferase [Synechococcus sp. WH 5701]


ZP_011 . . .
88809938
Putative glycosyltransferase [Synechococcus sp. WH 7805]


BAE47471
78483937
carotenoid glucosyltransferase [Paracoccus sp. N81106]


ZP_010 . . .
87303273
probable glycosyltransferase [Synechococcus sp. WH 5701]


YP_376127
78183693
probable glycosyltransferase [Synechococcus sp. CC9902]


YP_501334
88196509
hypothetical protein SAOUHSC_02880 [Staphylococcus




aureus subsp. aureus NCTC 8325]


YP_187370
57652300
glycosyl transferase, group 2 family protein [Staphylococcus




aureus subsp. aureus COL]


CAA66627
1340131u
nnamed protein product [Staphylococcus aureus]


YP_041987
49484763
putative glycosyl transferase [Staphylococcus aureus subsp.




aureus MRSA252]


YP_417885
82752144
hypothetical protein SAB2436c [Staphylococcus aureus




RF122]


YP_252404
70725490
hypothetical protein SH0489 [Staphylococcus haemolyticus




JCSC1435]


NP_693379
23099913
hypothetical protein OB2458 [Oceanobacillus iheyensis




HTE831]


ZP_008 . . .
82501285
conserved hypothetical protein [Caldicellulosiruptor




saccharolyticus DSM 8903]


ZP_010 . . .
87303565
hypothetical protein WH5701_09900 [Synechococcus sp. WH




5701]
















TABLE 25







Examples of acyl CoA:diacyglycerol acyltransferase (DGAT) polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION





XP_957022
85082953
hypothetical protein [Neurospora crassa N150]


XP_386864
46124621
hypothetical protein FG06688.1 [Gibberella zeae PH-1]


XP_755172
71000982
diacylglycerol O-acyltransferase DGAT [Aspergillus




fumigatus Af293]


XP_663763
67539978
hypothetical protein AN6159.2 [Aspergillus nidulans FGSC




A4]


BAE65302
83775179
unnamed protein product [Aspergillus oryzae]


XP_502557
50550169
hypothetical protein [Yarrowia lipolytica]


AAS78662
56199782
diacylglycerol acyltransferase [Glycine max]


ABB84383
82582915
diacylglycerol acyltransferase [Jatropha curcas]


AAV31083
54145459
1,2-diacyl-sn-glycerol:acyl-CoA acyltransferase [Euonymus




alatus]


AAG23696
10803053
diacylglycerol acyltransferase [Perilla frutescens]


AAF64065
7576941
putative diacylglycerol acyltransferase [Brassica napus]


AAS01606
41387497
acyl-CoA:diacylglycerol acyltransferase 1 [Olea europaea]


AAT73629
50299542
acyl CoA:diacylglycerol acyltransferase [Glycine max]


AAM03340
67043496
putative diacylglycerol acyltransferase [Tropaeolum majus]


XP_645633
66824557
hypothetical protein DDB0202877 [Dictyostelium




discoideum]


AAF19345
6625653
diacylglycerol acylCoA acyltransferase [Nicotiana tabacum]


AAY40785
63376239
diacylglycerol acyltransferase DGAT2 [Brassica juncea]


AAW47581
57231736
diacylglycerol acyltransferase [Oryza sativa (japonica




cultivar-group)]


AAR11479
38146080
diacylglycerol acyltransferase [Ricinus communis]


AAY40784
63376226
diacylglycerol acyltransferase DGAT1 [Brassica juncea]


AAP68322
31711932
At2g19450 [Arabidopsis thaliana]


AAW51456
57545061
diacylglycerol acyltransferase [Lotus corniculatus var.




japonicus]


AAD45536
5579408
putative diacylglycerol acyltransferase [Brassica napus]


BAD53762
53791817
putative acyl-CoA:diacylglycerol acyltransferase [Oryza




sativa (japonica cultivar-group)]


NP_956024
41054343
hypothetical protein LOC325875 [Danio rerio]


AAL49962
18642598
diacylglycerol acyltransferase 1 [Bos taurus]


XP_930884
89028385
similar to Diacylglycerol O-acyltransferase 1 (Diglyceride




acyltransferase) (ACAT-related gene) [Homo sapiens]


NP_777118
27819636
diacylglycerol O-acyltransferase 1 [Bos taurus]


Q9GMF1
18202926
Diacylglycerol O-acyltransferase 1 (Diglyceride




acyltransferase)


NP_036211
6912332
diacylglycerol O-acyltransferase 1 [Homo sapiens]


AAH06263
34782946
DGAT1 protein [Homo sapiens]


XP_780515
72006039
similar to Diacylglycerol O-acyltransferase 1




[Strongylocentrotus purpuratus]


AAD40881
5225382
putative diacylglycerol acyltransferase [Brassica napus]


XP_539214
73974769
similar to Diacylglycerol O-acyltransferase 1 (ACAT related




gene product 1) isoform 1 [Canis familiaris]


AAZ22403
71063860
diacylglycerol O-acyltransferase 1 [Bubalus bubalis]


NP_999216
47522918
diacylglycerol acyltransferase [Sus scrofa]


NP_001 . . .
50539976
hypothetical protein LOC436731 [Danio rerio]


XP_849176
73974767
similar to Diacylglycerol O-acyltransferase 1 (ACAT related




gene product 1) isoform 2 [Canis familiaris]


NP_505828
71997360
H19N07.4 [Caenorhabditis elegans]


AAF82410
9049538
diacylglycerol acyltransferase [Caenorhabditis elegans]


CAE75170
39591950
Hypothetical protein CBG23107 [Caenorhabditis briggsae]


XP_626337
66358318
diacylglycerol acyltransferase 1 [Cryptosporidium parvum




Iowa II]


XP_668402
67624239
acyl-CoA:diacylglycerol acyltransferase 1-related enzyme




[Cryptosporidium hominis TU502]


AAP94208
33113253
acyl-CoA:diacylglycerol acyltransferase 1-related enzyme




[Toxoplasma gondii]


AAP94209
33113255
acyl-CoA:diacylglycerol acyltransferase 1-related enzyme




[Toxoplasma gondii]


XP_579557
62652535
PREDICTED: diacylglycerol O-acyltransferase 1 [Rattus




norvegicus]


BAC66171
29170489
diacylglycerol acyltransferase [Mus musculus]


Q9ERM3
18202872
Diacylglycerol O-acyltransferase 1 (Diglyceride




acyltransferase)


AAL78366
18698659
acyl coenzyme A:diacylglycerol acyltransferase [Drosophila




melanogaster]


NP_995724
45552403
CG31991-PD, isoform D [Drosophila melanogaster]


NP_724017
24584734
CG31991-PC, isoform C [Drosophila melanogaster]


XP_858062
73974765
similar to Diacylglycerol O-acyltransferase 1 (ACAT related




gene product 1) isoform 3 [Canis familiaris]


XP_728984
82915156
hypothetical protein PY01256 [Plasmodium yoelii yoelii str.




17XNL]


CAG11944
47225461
unnamed protein product [Tetraodon nigroviridis]


BAD27526
50199438
acyl-CoA:diacylglycerol acyltransferase [eukaryotic synthetic




construct]


XP_317656
31226099
ENSANGP00000002281 [Anopheles gambiae str. PEST]


AAV59457
55733950
putative diacylglycerol acyltransferase [Oryza sativa




(japonica cultivar-group)]


EAL33593
54644853
GA16599-PA [Drosophila pseudoobscura]


XP_678753
68073677
diacylglycerol O-acyltransferase [Plasmodium berghei strain




ANKA]


XP_520014
55631434
PREDICTED: similar to Diacylglycerol O-acyltransferase 1




(Diglyceride acyltransferase) [Pan troglodytes]


CAG10815
47219451
unnamed protein product [Tetraodon nigroviridis]


XP_624754
66522700
PREDICTED: similar to ENSANGP00000002281 [Apis




mellifera]


CAC69884
15620769
diacylglycerol acyltransferase I [Rattus norvegicus]


XP_686181
68363630
PREDICTED: similar to Diacylglycerol O-acyltransferase 1




(Diglyceride acyltransferase) [Danio rerio]


XP_734008
70921323
diacylglycerol O-acyltransferase [Plasmodium chabaudi




chabaudi]


XP_673128
68062248
hypothetical protein PB300300.00.0 [Plasmodium berghei




strain ANKA]


AAS72376
45642963
acyl-CoA:cholesterol acyltransferase beta [Toxoplasma




gondii]


AAS72375
45642961
acyl-CoA:cholesterol acyltransferase alpha [Toxoplasma




gondii]


NP_586145
19074639
STEROL O-ACYLTRANSFERASE [Encephalitozoon




cuniculi GB-M1]


XP_640280
66812202
hypothetical protein DDB0205259 [Dictyostelium




discoideum]


AAY40783
63376221
diacylglycerol acyltransferase [Brassica juncea]


XP_765774
71032265
diacylglycerol O-acyltransferase [Theileria parva strain




Muguga]


Q876L2
34582301
Sterol O-acyltransferase 2 (Sterol-ester synthase 2)


XP_571260
58268208
sterol O-acyltransferase [Cryptococcus neoformans var.




neoformans JEC21]


EAL20032
50257323
hypothetical protein CNBF3580 [Cryptococcus neoformans




var. neoformans B-3501A]


XP_954478
84999514
acyl transferase [Theileria annulata strain Ankara]


XP_505086
50555355
hypothetical protein [Yarrowia lipolytica]


NP_588558
19076058
hypothetical protein SPCP1E11.05c [Schizosaccharomyces




pombe 972h-]


AAC49441
1389739
acyl-CoA:sterol acyltransferase


NP_014416
6324346
Acyl-CoA:sterol acyltransferase, isozyme of Are1p; Are2p




[Saccharomyces cerevisiae]


XP_750354
70991010
sterol o-acyltransferase APE2 [Aspergillus fumigatus Af293]


XP_382192
46110268
hypothetical protein FG02016.1 [Gibberella zeae PH-1]


BAE54934
83764790
unnamed protein product [Aspergillus oryzae]


XP_885914
76617939
similar to Sterol O-acyltransferase 2 (Cholesterol




acyltransferase 2) (ACAT-2) isoform 2 [Bos taurus]


XP_591251
76617937
similar to Sterol O-acyltransferase 2 (Cholesterol




acyltransferase 2) (ACAT-2) isoform 1 [Bos taurus]


BAC00846
21392392
AcylCoA:Cholesterol Acyltransferase 2 [Rattus norvegicus]


NP_649816
28571583
CG8112-PA [Drosophila melanogaster]


NP_666176
22122547
sterol O-acyltransferase 2 [Mus musculus]


O88908
18202245
Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2)




(ACAT-2)


XP_761502
71022545
hypothetical protein UM05355.1 [Ustilago maydis 521]


NP_714950
40254723
sterol O-acyltransferase 2 [Rattus norvegicus]


EAQ86094
88178626
hypothetical protein CHGG_07347 [Chaetomium globosum




CBS 148.51]


XP_461395
50425599
hypothetical protein DEHA0F25652g [Debaryomyces




hansenii CBS767]


XP_661812
67527926
hypothetical protein AN4208.2 [Aspergillus nidulans FGSC




A4]


AAH96091
64654094
Sterol O-acyltransferase 2 [Homo sapiens]


O75908
18202149
Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2)




(ACAT-2)


AAH96090
64652990
Sterol O-acyltransferase 2 [Homo sapiens]


AAK48829
13898623
acyl coenzyme A: cholesterol acyltransferase-2 [Homo




sapiens]


XP_543637
73996435
PREDICTED: similar to sterol O-acyltransferase 2 [Canis




familiaris]


O77759
18202176
Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2)




(ACAT-2)


AAO32474
28564191
ARE2 [Saccharomyces castellii]


XP_323485
32405744
hypothetical protein [Neurospora crassa]


NP_982606
45184888
AAR065Cp [Eremothecium gossypii]


NP_593708
19114620
hypothetical protein SPAC13G7.06 [Schizosaccharomyces




pombe 972h-]


AAO32554
28564940
ARE2 [Saccharomyces kluyveri]


EAL28962
54639560
GA20833-PA [Drosophila pseudoobscura]


XP_449806
50294790
hypothetical protein CAGL0M10571g [Candida glabrata




CBS138]


NP_033256
84619697
sterol O-acyltransferase 1 [Mus musculus]


Q61263
18202591
Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1)




(ACAT-1)


BAC34925
26342537
unnamed protein product [Mus musculus]


XP_452607
50305295
unnamed protein product [Kluyveromyces lactis]


NP_001 . . .
77735363
hypothetical protein LOC504287 [Bos taurus]


Q60457
18202585
Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1)




(ACAT-1)


XP_320321
58393811
ENSANGP00000016512 [Anopheles gambiae str. PEST]


XP_320320
58393809
ENSANGP00000016486 [Anopheles gambiae str. PEST]


O70536
18202126
Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1)




(ACAT-1)


XP_714776
68482533
acyl-CoA cholesterol acyltransferase [Candida albicans




SC5314]


P84285
56404462
Sterol O-acyltransferase 2 (Sterol-ester synthase) (ASAT)


AAH77916
50416229
Soat1-prov protein [Xenopus laevis]


XP_692855
68364838
PREDICTED: similar to Soat1-prov protein [Danio rerio]


CAI13574
55960156
sterol O-acyltransferase (acyl-Coenzyme A: cholesterol




acyltransferase) 1 [Homo sapiens]


AAL56227
18028942
cholesterol acyltransferase 1 [Gorilla gorilla]


AAL56228
18028944
cholesterol acyltransferase 1 [Pongo pygmaeus]


AAC37532
4878022
acyl-coenzyme A: cholesterol acyltransferase [Homo sapiens]


2201440A
1585676
acyl-CoA/cholesterol acyltransferase


Q876L3
34582302
Sterol O-acyltransferase 1 (Sterol-ester synthase 1)


BAE01048
67969393
unnamed protein product [Macaca fascicularis]


XP_514030
55588858
PREDICTED: hypothetical protein XP_514030 [Pan




troglodytes]


XP_547445
73961286
similar to Sterol O-acyltransferase 1 (Cholesterol




acyltransferase 1) (ACAT-1) [Canis familiaris]


EAQ84619
88177151
hypothetical protein CHGG_08633 [Chaetomium globosum




CBS 148.51]


O77761
18202178
Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1)




(ACAT-1)


XP_422267
50751122
PREDICTED: similar to Sterol O-acyltransferase 1




(Cholesterol acyltransferase 1) (ACAT-1) [Gallus gallus]


XP_693284
68392980
PREDICTED: similar to Sterol O-acyltransferase 1




(Cholesterol acyltransferase 1) (ACAT-1) [Danio rerio]


AAT92940
51013293
YCR048W [Saccharomyces cerevisiae]


XP_956576
85080625
hypothetical protein [Neurospora crassa N150]


XP_624691
66564061
PREDICTED: similar to ENSANGP00000016486 [Apis




mellifera]


CAF96514
47222847
unnamed protein product [Tetraodon nigroviridis]


XP_788209
72085563
PREDICTED: similar to sterol O-acyltransferase 1




[Strongylocentrotus purpuratus]


XP_445307
50285757
unnamed protein product [Candida glabrata]


CAE70002
39596364
Hypothetical protein CBG16409 [Caenorhabditis briggsae]


CAG07990
47225647
unnamed protein product [Tetraodon nigroviridis]


NP_510623
17549960
B0395.2 [Caenorhabditis elegans]


AAX28331
76157393
SJCHGC04421 protein [Schistosoma japonicum]


CAI96158
66347204
Diacylglycerol O-acyltransferase [Bubalus bubalis]


XP_390039
46136695
hypothetical protein FG09863.1 [Gibberella zeae PH-1]


XP_643169
66819019
hypothetical protein DDB0203882 [Dictyostelium




discoideum]


AAO53095
28850306
hypothetical protein [Dictyostelium discoideum]


AAB06959
1515472
acyl-CoA:cholesterol acyltransferase [Oryctolagus cuniculus]


NP_945619
39933343
putative alginate o-acetyltransferase AlgI




[Rhodopseudomonas palustris CGA009]


ZP_008 . . .
77691302
Membrane bound O-acyl transferase, MBOAT




[Rhodopseudomonas palustris BisB5]


XP_465546
50908115
putative wax synthase [Oryza sativa (japonica cultivar-




group)]
















TABLE 29







Examples of Prenyldiphosphate synthase polypeptides









Accession
GI
Description










29A: Bacteria Proteins that require a mitochondrial targeting sequence









ZP_009 . . .
83373595
Trans-hexaprenyltranstransferase [Rhodobacter sphaeroides ATCC




17029]


ZP_009 . . .
83371280
Trans-hexaprenyltranstransferase [Rhodobacter sphaeroides ATCC




17025]


CAD24417
20429105
decaprenyl diphosphate synthase [Paracoccus zeaxanthinifaciens]


ZP_010 . . .
85705714
Geranylgeranyl pyrophosphate synthase/Polyprenyl synthetase




[Roseovarius sp. 217]


ZP_010 . . .
84515724
decaprenyl diphosphate synthase [Loktanella vestfoldensis SKA53]


YP_165582
56695234
decaprenyl diphosphate synthase [Silicibacter pomeroyi DSS-3]


ZP_010 . . .
86139019
decaprenyl diphosphate synthase [Roseobacter sp. MED193]


ZP_009 . . .
83941379
decaprenyl diphosphate synthase [Sulfitobacter sp. EE-36]


ZP_009 . . .
83854856
decaprenyl diphosphate synthase [Sulfitobacter sp. NAS-14.1]


ZP_006 . . .
69299873
Farnesyltranstransferase [Silicibacter sp. TM1040]


ZP_010 . . .
84683979
Geranylgeranyl pyrophosphate synthase/Polyprenyl synthetase




[Rhodobacterales bacterium HTCC2654]


ZP_009 . . .
84500217
decaprenyl diphosphate synthase [Oceanicola batsensis HTCC2597]


ZP_009 . . .
83952381
decaprenyl diphosphate synthase [Roseovarius nubinhibens ISM]


ZP_006 . . .
69937106
Trans-hexaprenyltranstransferase [Paracoccus denitrificans PD1222]


ZP_005 . . .
68180845
Trans-hexaprenyltranstransferase [Jannaschia sp. CCS1]


ZP_008 . . .
78495595
Polyprenyl synthetase [Rhodopseudomonas palustris BisB18]


AAY82368
67866738
decaprenyl diphosphate synthase [Agrobacterium tumefaciens]


NP_353656
15887975
hypothetical protein AGR_C_1125 [Agrobacterium tumefaciens str.




C58]


ZP_008 . . .
77688465
Farnesyltranstransferase [Rhodopseudomonas palustris BisB5]


NP_531334
17934544
octaprenyl-diphosphate synthase [Agrobacterium tumefaciens str.




C58]


YP_484709
86748213
Farnesyltranstransferase [Rhodopseudomonas palustris HaA2]


AAP56240
37903500
decaprenyl diphosphate synthase [Agrobacterium tumefaciens]


YP_192388
58040424
Decaprenyl diphosphate synthase [Gluconobacter oxydans 621H]







29B: Subunit 1- Proteins that contain mitochondrial targeting sequence









T43193
11279237
trans-pentaprenyltranstransferase homolog - fission yeast




(Schizosaccharomyces pombe )


AAD28559
4732024
trans-prenyltransferase [Homo sapiens]


AAI07275
78070698
Trans-prenyltransferase [Mus musculus]


BAE48216
81157931
subunit 1 of decaprenyl diphosphate synthase [Homo sapiens]


AAH49211
29165656
PDSS1 protein [Homo sapiens]


Q33DR2
85700953
Decaprenyl-diphosphate synthase subunit 1 (Solanesyl-diphosphate




synthase subunit 1) (Trans-prenyltransferase)


XP_507706
55633583
PREDICTED: similar to TPRT protein [Pan troglodytes]


XP_586717
76632198
PREDICTED: similar to trans-prenyltransferase [Bos taurus]


XP_849908
73948851
PREDICTED: similar to trans-prenyltransferase [Canis familiaris]







29C: Subunit 2- Proteins that contain mitochondrial targeting sequence









O13851
60389474
Decaprenyl-diphosphate synthase subunit 2 (Decaprenyl




pyrophosphate synthetase subunit 2)


BAE48218
81157935
subunit 2 of solanesyl diphosphate synthase [Mus musculus]


BAE48217
81157933
subunit 2 of decaprenyl diphosphate synthase [Homo sapiens]
















TABLE 30







Examples of PHB-Polyprenyltransferase polypeptides








GI
PROTEIN DESCRIPTION





51013645
YNR041C [Saccharomyces cerevisiae]


50285815
unnamed protein product [Candida glabrata]


50311051
unnamed protein product [Kluyveromyces lactis]


45200866
AGL231Wp [Eremothecium gossypii]


50555263
hypothetical protein [Yarrowia lipolytica]


68473193
para-hydroxybenzoate: polyprenyl transferase [Candida albicans SC5314]


50410039
hypothetical protein DEHA0A14212g [Debaryomyces hansenii CBS767]


83769349
unnamed protein product [Aspergillus oryzae]


70994900
para-hydroxybenzoate-polyprenyltransferase precursor [Aspergillus fumigatus



Af293]


19114131
hypothetical protein SPAC56F8. 04c [Schizosaccharomyces pombe 972h-]


39973573
hypothetical protein MG01067. 4 [Magnaporthe grisea 70-15]


85078920
protein related to para-hydroxybenzoate polyprenyltransferase precursor



[Neurospora crassa N150]


76660839
PREDICTED: similar to para-hydroxybenzoate-polyprenyltransferase,



mitochondrial [Bos taurus]


52138578
para-hydroxybenzoate-polyprenyltransferase, mitochondrial [Homo sapiens]


18088424
COQ2 protein [Homo sapiens]


47221448
unnamed protein product [Tetraodon nigroviridis]


58385249
ENSANGP00000012220 [Anopheles gambiae str. PEST]


50746583
PREDICTED: similar to hypothetical protein CL640 [Gallus gallus]


54638587
GA21912-PA [Drosophila pseudoobscura]


21355567
CG9613-PA [Drosophila melanogaster]


71005862
hypothetical protein UM01450. 1 [Ustilago maydis 521]
















TABLE 31







Examples of soluble transydrogenase polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAD40691
5163507
soluble pyridine nucleotide transhydrogenase [Azotobacter





vinelandii


2
ZP_013 . . .
107102541
hypothetical protein PaerPA_01003605 [Pseudomonas





aeruginosa PACS2]


3
ZP_012 . . .
94416745
hypothetical protein PaerP_01001583 [Pseudomonas aeruginosa





PA7]


4
O05139
11135075
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


5
YP_259077
70729340
soluble pyridine nucleotide transhydrogenase [Pseudomonas





fluorescens Pf-5]


6
YP_349590
77460083
soluble pyridine nucleotide transhydrogenase [Pseudomonas





fluorescens PfO-1]


7
YP_274087
71735155
soluble pyridine nucleotide transhydrogenase [Pseudomonas





syringae pv. phaseolicola 1448A]


8
YP_234983
66045142
soluble pyridine nucleotide transhydrogenase [Pseudomonas





syringae pv. syringae B728a]


9
YP_609219
104782721
soluble pyridine nucleotide transhydrogenase (NAD(P)(+)





transhydrogenase [B-specific]) [Pseudomonas entomophila L48]


10
Q884I6
38258471
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


11
ZP_009 . . .
82739140
soluble pyridine nucleotide transhydrogenase [Pseudomonas





putida F1]


12
YP_573629
92113701
pyridine nucleotide-disulphide oxidoreductase dimerisation





region [Chromohalobacter salexigens DSM 3043]


13
ZP_008 . . .
77951906
NAD(P) transhydrogenase [Marinobacter aquaeolei VT8]


14
YP_433907
83645472
Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzyme [Hahella chejuensis KCTC 2396]


15
ZP_011 . . .
89094310
soluble pyridine nucleotide transhydrogenase [Oceanospirillum





sp. MED92]


16
ZP_013 . . .
94499566
Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzyme [Oceanobacter sp. RED65]


17
ZP_011 . . .
88800089
soluble pyridine nucleotide transhydrogenase [Reinekea sp.





MED297]


18
ZP_010 . . .
87121312
soluble pyridine nucleotide transhydrogenase [Marinomonas sp.





MED121]


19
ZP_012 . . .
90417525
soluble pyridine nucleotide transhydrogenase [marine gamma





proteobacterium HTCC2207]


20
Q7MQ83
47606104
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


21
YP_527277
90021450
regulatory protein, ArsR [Saccharophagus degradans 2-40]


22
ZP_009 . . .
83586194
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Escherichia coli 101-1]


23
YP_219002
62182585
soluble pyridine nucleotide transhydrogenase [Salmonella





enterica subsp. enterica serovar Choleraesuis str. SC-B67]


24
YP_543498
91213512
soluble pyridine nucleotide transhydrogenase [Escherichia coli





UTI89]


25
Q87KN5
33301640
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


26
YP_153038
56415963
soluble pyridine nucleotide transhydrogenase [Salmonella





enterica subsp. enterica serovar Paratyphi A str. ATCC 9150]


27
YP_672034
110644304
soluble pyridine nucleotide transhydrogenase [Escherichia coli





536]


28
ZP_013 . . .
106883834
FAD-dependent pyridine nucleotide-disulphide





oxidoreductase:Pyridine nucleotide-disulphide oxidoreductase





dimerisation region:FAD dependent oxidoreductase





[Psychromonas ingrahamii 37]


29
ZP_006 . . .
75176647
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Shigella boydii BS512]


30
Q8FB93
38258590
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


31
ZP_007 . . .
75197835
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Escherichia coli HS]


32
ZP_007 . . .
75513852
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Escherichia coli 53638]


33
Q8X727
21362954
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


34
YP_267100
71278420
soluble pyridine nucleotide transhydrogenase [Colwellia





psychrerythraea 34H]


35
Q83MI1
39932373
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


36
ZP_007 . . .
75238410
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Escherichia coli E110019]


37
ZP_007 . . .
75854141
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Vibrio sp. Ex25]


38
YP_052329
50123162
soluble pyridine nucleotide transhydrogenase [Erwinia





carotovora subsp. atroseptica SCRI1043]


39
ZP_008 . . .
77973002
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Yersinia frederiksenii ATCC 33641]


40
ZP_008 . . .
77957412
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Yersinia bercovieri ATCC 43970]


41
ZP_008 . . .
78702791
NAD(P) transhydrogenase (B-specific) [Alkalilimnicola





ehrlichei MLHE-1]


42
YP_645986
108810219
soluble pyridine nucleotide transhydrogenase [Yersinia pestis





Nepal516]


43
ZP_007 . . .
75828016
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Vibrio cholerae O395]


44
Q7MBG9
47606102
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


45
ZP_008 . . .
77976809
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Yersinia intermedia ATCC 29909]


46
ZP_008 . . .
77961066
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Yersinia mollaretii ATCC 43969]


47
ZP_010 . . .
86148649
soluble pyridine nucleotide transhydrogenase [Vibrio sp.





MED222]


48
YP_205822
59713046
soluble pyridine nucleotide transhydrogenase [Vibrio fischeri





ES114]


49
ZP_009 . . .
84394322
pyridine nucleotide-disulfide oxidoreductase, class I [Vibrio





splendidus 12B01]


50
ZP_011 . . .
89074500
soluble pyridine nucleotide transhydrogenase [Photobacterium





sp. SKA34]


51
YP_154714
56459433
soluble pyridine nucleotide transhydrogenase [Idiomarina





loihiensis L2TR]


52
YP_046885
50085375
soluble pyridine nucleotide transhydrogenase [Acinetobacter sp.





ADP1]


53
ZP_012 . . .
90581098
soluble pyridine nucleotide transhydrogenase [Vibrio angustum





S14]


54
YP_693290
110834431
NAD(P) transhydrogenase [Alcanivorax borkumensis SK2]


55
ZP_011 . . .
88795508
soluble pyridine nucleotide transhydrogenase [Alteromonas





macleodii ‘Deep ecotype’]


56
ZP_012 . . .
90407259
soluble pyridine nucleotide transhydrogenase [Psychromonas sp.





CNPT3]


57
E65203
7431869
probable dehydrogenase (EC 1.8.1.—) udhA - Escherichia coli





(strain K-12)


58
YP_410260
82546313
putative oxidoreductase [Shigella boydii Sb227]


59
YP_312883
74314464
putative oxidoreductase [Shigella sonnei Ss046]


60
YP_131541
54310521
soluble pyridine nucleotide transhydrogenase [Photobacterium





profundum SS9]


61
AAC43068
396309
ORF_f444 [Escherichia coli]


62
H86087
25284914
probable oxidoreductase udhA [imported] - Escherichia coli





(strain O157:H7, substrain EDL933)


63
ZP_012 . . .
90414698
soluble pyridine nucleotide transhydrogenase [Photobacterium





profundum 3TCK]


64
NP_709766
56480495
soluble pyridine nucleotide transhydrogenase [Shigella flexneri





2a str. 301]


65
YP_405233
82778884
putative oxidoreductase [Shigella dysenteriae Sd197]


66
YP_691341
110807821
putative oxidoreductase [Shigella flexneri 5 str. 8401]


67
NP_667661
22124238
soluble pyridine nucleotide transhydrogenase [Yersinia pestis





KIM]


68
YP_341375
77361800
soluble pyridine nucleotide transhydrogenase





[Pseudoalteromonas haloplanktis TAC125]


69
YP_455837
85060135
soluble pyridine nucleotide transhydrogenase [Sodalis





glossinidius str. ‘morsitans’]


70
ZP_012 . . .
91771448
FAD-dependent pyridine nucleotide-disulphide





oxidoreductase:Pyridine nucleotide-disulphide oxidoreductase





dimerisation region:FAD dependent oxidoreductase





[Psychrobacter sp. PRwf-1]


71
ZP_011 . . .
88861405
soluble pyridine nucleotide transhydrogenase





[Pseudoalteromonas tunicata D2]


72
YP_264617
71065890
soluble pyridine nucleotide transhydrogenase [Psychrobacter





arcticus 273-4]


73
YP_580301
93005864
pyridine nucleotide-disulphide oxidoreductase dimerisation





region [Psychrobacter cryohalolentis K5]


74
ZP_010 . . .
85710769
soluble pyridine nucleotide transhydrogenase [Idiomarina baltica





OS145]


75
ZP_012 . . .
91227486
soluble pyridine nucleotide transhydrogenase [Vibrio





alginolyticus 12G01]


76
ZP_007 . . .
75814072
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Vibrio cholerae V52]


77
YP_666832
110670275
soluble pyridine nucleotide transhydrogenase [Francisella





tularensis subsp. tularensis FSC 198]


78
YP_169700
56707804
soluble pyridine nucleotide transhydrogenase [Francisella





tularensis subsp. tularensis SCHU S4]


79
YP_513671
89256309
soluble pyridine nucleotide transhydrogenase [Francisella





tularensis subsp. holarctica]


80
CAA46822
43237
udhA [Escherichia coli]


81
ZP_005 . . .
67929855
FAD-dependent pyridine nucleotide-disulphide





oxidoreductase:Pyridine nucleotide-disulphide oxidoreductase





dimerisation region [Solibacter usitatus Ellin6076]


82
YP_592298
94970250
pyridine nucleotide-disulphide oxidoreductase [Acidobacteria





bacterium Ellin345]


83
NP_961763
41408927
soluble pyridine nucleotide transhydrogenase [Mycobacterium





avium subsp. paratuberculosis K-10]


84
P66006
54042093
Probable soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


85
ZP_007 . . .
76783189
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Mycobacterium tuberculosis F11]


86
YP_716291
111225497
soluble pyridine nucleotide transhydrogenase [Frankia alni





ACN14a]


87
ZP_005 . . .
68235154
FAD-dependent pyridine nucleotide-disulphide





oxidoreductase:Pyridine nucleotide-disulphide oxidoreductase





dimerisation domain [Frankia sp. EAN1pec]


88
ZP_012 . . .
90205475
FAD-dependent pyridine nucleotide-disulphide





oxidoreductase:Pyridine nucleotide-disulphide oxidoreductase





dimerisation region [Mycobacterium vanbaalenii PYR-1]


89
YP_482962
86742562
pyridine nucleotide-disulphide oxidoreductase dimerisation





region [Frankia sp. CcI3]


90
NP_532346
17935556
soluble pyridine nucleotide transhydrogenase [Agrobacterium





tumefaciens str. C58]


91
AAY87873
68165826
pyridine nucleotide-disulfide oxidoreductase class I [Vibrio





cholerae]


92
AAY87863
68165806
pyridine nucleotide-disulfide oxidoreductase class I [Vibrio





cholerae]


93
AAY87865
68165810
pyridine nucleotide-disulfide oxidoreductase class I [Vibrio





cholerae]


94
YP_469365
86357473
probable pyridine nucleotide transhydrogenase protein





[Rhizobium etli CFN 42]


95
ZP_010 . . .
85706062
soluble pyridine nucleotide transhydrogenase [Roseovarius sp.





217]


96
ZP_014 . . .
113873124
putative soluble pyridine nucleotide transhydrogenase





[Sinorhizobium medicae WSM419]


97
NP_385835
15965482
soluble pyridine nucleotide transhydrogenase [Sinorhizobium





meliloti 1021]


98
YP_169016
56698639
soluble pyridine nucleotide transhydrogenase [Silicibacter





pomeroyi DSS-3]


99
ZP_009 . . .
83951172
soluble pyridine nucleotide transhydrogenase [Roseovarius





nubinhibens ISM]


100
YP_611681
99078423
pyridine nucleotide-disulphide oxidoreductase dimerisation





region [Silicibacter sp. TM1040]


101
ZP_010 . . .
86140117
soluble pyridine nucleotide transhydrogenase [Roseobacter sp.





MED193]


102
BAB53939
14027670
soluble pyridine nucleotide transhydrogenase [Mesorhizobium





loti MAFF303099]


103
YP_630631
108762684
NAD(P) transhydrogenase (B-specific) [Myxococcus xanthus





DK 1622]


104
YP_467034
86160249
FAD-dependent pyridine nucleotide-disulphide oxidoreductase





[Anaeromyxobacter dehalogenans 2CP-C]


105
YP_007724
46446359
soluble pyridine nucleotide transhydrogenase [Candidatus





Protochlamydia amoebophila UWE25]


106
YP_433307
83644872
Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzyme [Hahella chejuensis KCTC 2396]


107
YP_527988
90022161
soluble pyridine nucleotide transhydrogenase [Saccharophagus





degradans 2-40]


108
ZP_005 . . .
67931474
FAD-dependent pyridine nucleotide-disulphide





oxidoreductase:Pyridine nucleotide-disulphide oxidoreductase





dimerisation region [Solibacter usitatus Ellin6076]


109
YP_575887
92116158
Dihydrolipoamide dehydrogenase [Nitrobacter hamburgensis





X14]


110
NP_539063
17986429
dihydrolipoamide dehydrogenase [Brucella melitensis 16M]


111
NP_698895
23502768
dihydrolipoamide dehydrogenase [Brucella suis 1330]


112
YP_415258
82700684
Pyridine nucleotide-disulphide oxidoreductase, class-II:NAD





binding site:Adrenodoxin reductase:Mercuric reductase:Pyridine





nu . . . [Brucella melitensis biovar Abortus 2308]


113
ZP_011 . . .
88945707
Dihydrolipoamide dehydrogenase [Desulfotomaculum reducens





MI-1]


114
YP_675936
110635728
dihydrolipoamide dehydrogenase [Mesorhizobium sp. BNC1]


115
YP_483896
86747400
Dihydrolipoamide dehydrogenase [Rhodopseudomonas palustris





HaA2]


116
ZP_006 . . .
71836831
Dihydrolipoamide dehydrogenase [Pelobacter propionicus DSM





2379]


117
BAB50985
14024381
ferric leghemoglobin reductase-2 precursor, dihydrolipoamide





dehydrogenase [Mesorhizobium loti MAFF303099]


118
ZP_011 . . .
88946629
Dihydrolipoamide dehydrogenase [Desulfotomaculum reducens





MI-1]


119
YP_032854
49474812
dihydrolipoamide dehydrogenase [Bartonella quintana str.





Toulouse]


120
YP_317044
75674623
dihydrolipoamide dehydrogenase [Nitrobacter winogradskyi Nb-





255]


121
ZP_012 . . .
90421039
2-oxoglutarate dehydrogenase, E3 component, lipoamide





dehydrogenase [Aurantimonas sp. SI85-9A1]


122
NP_533297
17936507
dihydrolipoamide dehydrogenase [Agrobacterium tumefaciens





str. C58]


123
AAR21288
38489206
2-oxoglutarate dehydrogenase E3 component [Bartonella





henselae]


124
YP_034342
49476301
dihydrolipoamide dehydrogenase [Bartonella henselae str.





Houston-1]


125
ZP_008 . . .
78694497
Dihydrolipoamide dehydrogenase [Bradyrhizobium sp. BTAi1]


126
ZP_010 . . .
85713709
dihydrolipoamide dehydrogenase [Nitrobacter sp. Nb-311A]


127
YP_471355
86359463
dihydrolipoamide dehydrogenase protein [Rhizobium etli CFN





42]


128
ZP_008 . . .
77739670
Dihydrolipoamide dehydrogenase [Rhodopseudomonas palustris





BisA53]


129
NP_387154
15966801
dihydrolipoamide dehydrogenase [Sinorhizobium meliloti 1021]


130
YP_567689
91975030
Dihydrolipoamide dehydrogenase [Rhodopseudomonas palustris





BisB5]


131
ZP_009 . . .
83750811
COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,





dihydrolipoamide dehydrogenase (E3) component, and related





enzymes [Bartonella bacilliformis KC583]


132
NP_767089
27375560
dihydrolipoamide dehydrogenase [Bradyrhizobium japonicum





USDA 110]


133
ZP_014 . . .
113873546
dihydrolipoamide dehydrogenase [Sinorhizobium medicae





WSM419]


134
ZP_011 . . .
88801370
Pyruvate/2-oxoglutarate dehydrogenase complex [Polaribacter





irgensii 23-P]


135
AAN03817
22652790
dihydrolipoamide dehydrogenase [Methylobacterium





extorquens]


136
NP_945538
39933262
dihydrolipoamide dehydrogenase [Rhodopseudomonas palustris





CGA009]


137
ZP_010 . . .
86142639
Dihydrolipoyl dehydrogenase [Flavobacterium sp. MED217]


138
YP_005669
46200002
dihydrolipoamide dehydrogenase [Thermus thermophilus HB27]


139
ZP_012 . . .
90589077
Dihydrolipoamide dehydrogenase [Flavobacterium johnsoniae





UW101]


140
YP_143553
55980256
2-oxoglutarate dehydrogenase E3 component (dihydrolipoamide





dehydrogenase) [Thermus thermophilus HB8]


141
YP_679939
110639729
dihydrolipoyl dehydrogenanse [Cytophaga hutchinsonii ATCC





33406]


142
YP_530077
90421707
Dihydrolipoamide dehydrogenase [Rhodopseudomonas palustris





BisB18]


143
YP_681916
110678909
dihydrolipoamide dehydrogenase [Roseobacter denitrificans





OCh 114]


144
ZP_010 . . .
86135035
dihydrolipoamide dehydrogenase [Tenacibaculum sp. MED152]


145
ZP_011 . . .
89068141
2-oxoglutarate dehydrogenase, E3 component, dihydrolipoamide





dehydrogenase [Oceanicola granulosus HTCC2516]


146
ZP_007 . . .
75761004
Dihydrolipoamide dehydrogenase [Bacillus thuringiensis serovar





israelensis ATCC 35646]


147
ZP_010 . . .
84684243
2-oxoglutarate dehydrogenase, E3 component,





dihydrolipoamidedehydrogenase [Rhodobacterales bacterium





HTCC2654]


148
ZP_009 . . .
84500199
2-oxoglutarate dehydrogenase, E3 component,





dihydrolipoamidedehydrogenase [Oceanicola batsensis





HTCC2597]


149
ZP_006 . . .
71900956
Dihydrolipoamide dehydrogenase [Xylella fastidiosa Ann-1]


150
XP_829730
74026328
dihydrolipoyl dehydrogenase [Trypanosoma brucei TREU927]


151
ZP_010 . . .
86132778
dihydrolipoamide dehydrogenase [Cellulophaga sp. MED134]


152
P71317
11135239
Soluble pyridine nucleotide transhydrogenase (STH)





(NAD(P)(+) transhydrogenase [B-specific])


153
ZP_012 . . .
89891405
dihydrolipoyl dehydrogenase (pyruvate 2-oxoglutarate





dehydrogenase) [Flavobacteria bacterium BBFL7]


154
ZP_009 . . .
83950445
2-oxoglutarate dehydrogenase, E3 component,





dihydrolipoamidedehydrogenase [Roseovarius nubinhibens ISM]


155
AAA21748
472330
dihydrolipoamide dehydrogenase


156
Q04933
416906
Dihydrolipoyl dehydrogenase (Dihydrolipoamide





dehydrogenase)


157
ZP_011 . . .
88805521
Pyruvate/2-oxoglutarate dehydrogenase complex [Robiginitalea





biformata HTCC2501]


158
YP_351398
77461891
dihydrolipoamide dehydrogenase [Pseudomonas fluorescens





PfO-1]


159
ZP_006 . . .
71900678
Dihydrolipoamide dehydrogenase [Xylella fastidiosa Ann-1]


160
ZP_011 . . .
88936095
Dihydrolipoamide dehydrogenase [Geobacter uraniumreducens





Rf4]


161
YP_430607
83590598
Dihydrolipoamide dehydrogenase [Moorella thermoacetica





ATCC 39073]


162
YP_165603
56695257
2-oxoglutarate dehydrogenase, E3 component, dihydrolipoamide





dehydrogenase [Silicibacter pomeroyi DSS-3]


163
ZP_011 . . .
89359154
Dihydrolipoamide dehydrogenase [Xanthobacter autotrophicus





Py2]


164
YP_007150
46445785
dihydrolipoamide dehydrogenase [Candidatus Protochlamydia





amoebophila UWE25]


165
YP_632394
108758911
alpha keto acid dehydrogenase complex, E3 component,





lipoamide dehydrogenase [Myxococcus xanthus DK 1622]


166
ZP_010 . . .
85704799
2-oxoglutarate dehydrogenase, E3 component,





dihydrolipoamidedehydrogenase [Roseovarius sp. 217]


167
NP_778978
28198664
dihydrolipoamide dehydrogenase [Xylella fastidiosa Temecula1]


168
ZP_011 . . .
88949385
Dihydrolipoamide dehydrogenase [Halorhodospira halophila





SL1]


169
XP_749345
70988990
dihydrolipoamide dehydrogenase [Aspergillus fumigatus Af293]


170
YP_359567
78044229
alpha keto acid dehydrogenase complex, E3 component,





lipoamide dehydrogenase [Carboxydothermus





hydrogenoformans Z-2901]


171
XP_959535
85092766
hypothetical protein [Neurospora crassa OR74A]


172
ZP_009 . . .
83856665
Dihydrolipoyl dehydrogenase [Croceibacter atlanticus





HTCC2559]


173
ZP_006 . . .
69259929
Dihydrolipoamide dehydrogenase [Magnetococcus sp. MC-1]


174
NP_298837
15838149
dihydrolipoamide dehydrogenase [Xylella fastidiosa 9a5c]


175
YP_508779
89053328
Dihydrolipoamide dehydrogenase [Jannaschia sp. CCS1]


176
CAA72131
1854569
dihydrolipoamide dehydrogenase [Trypanosoma cruzi]


177
ZP_011 . . .
88713490
Dihydrolipoyl dehydrogenase [Flavobacteriales bacterium





HTCC2170]


178
P90597
6166121
Dihydrolipoyl dehydrogenase (Dihydrolipoamide





dehydrogenase)


179
ZP_009 . . .
83944432
2-oxoglutarate dehydrogenase, E3 component,





dihydrolipoamidedehydrogenase [Sulfitobacter sp. EE-36]


180
ZP_009 . . .
83953473
2-oxoglutarate dehydrogenase, E3 component,





dihydrolipoamidedehydrogenase [Sulfitobacter sp. NAS-14.1]


181
ZP_010 . . .
86141935
dihydrolipoamide dehydrogenase, E3 component of 2-





oxoglutarate and pyruvate dehydrogenase complexes





[Flavobacterium sp. MED217]


182
XP_818792
71663602
dihydrolipoyl dehydrogenase [Trypanosoma cruzi strain CL





Brener]


183
XP_812294
71422952
dihydrolipoyl dehydrogenase [Trypanosoma cruzi strain CL





Brener]


184
CAA72132
1854571
dihydrolipoamide dehydrogenase [Trypanosoma cruzi]


185
NP_623271
20808100
Dihydrolipoamide dehydrogenase/glutathione oxidoreductase





and related enzyme [Thermoanaerobacter tengcongensis MB4]


186
YP_265659
71082940
Dihydrolipoyl dehydrogenase [Candidatus Pelagibacter ubique





HTCC1062]


187
ZP_012 . . .
91762636
Dihydrolipoyl dehydrogenase [Candidatus Pelagibacter ubique





HTCC1002]


188
CAA11554
4210334
2-oxoglutarate dehydrogenase, E3 subunit [Arabidopsis thaliana]


189
NP_566570
30684428
LPD2 (LIPOAMIDE DEHYDROGENASE 2); FAD binding/





dihydrolipoyl dehydrogenase/disulfide oxidoreductase/





oxidoreductase [Arabidopsis thaliana]


190
ZP_010 . . .
84515869
2-oxoglutarate dehydrogenase, E3 component,





dihydrolipoamidedehydrogenase [Loktanella vestfoldensis





SKA53]


191
YP_355777
77917962
2-oxoglutarate dehydrogenase complex, E3 component,





lipoamide dehydrogenase [Pelobacter carbinolicus DSM 2380]


192
AAS47708
44804791
dihydrolipoamide dehydrogenase [Leishmania major]


193
AAC26053
3309269
ferric leghemoglobin reductase-2 precursor [Glycine max]


194
XP_712334
68487571
putative mitochondrial matrix dihydrolipoamide dehydrogenase





Lpd1p [Candida albicans SC5314]


195
ZP_008 . . .
78702525
Dihydrolipoamide dehydrogenase [Alkalilimnicola ehrlichei





MLHE-1]


196
YP_002403
45658317
dihydrolipoamide dehydrogenase [Leptospira interrogans serovar





Copenhageni str. Fiocruz L1-130]


197
ZP_008 . . .
82736566
Dihydrolipoamide dehydrogenase [Pseudomonas putida F1]


198
CAD60736
27803033
unnamed protein product [Podospora anserina]


199
NP_747467
26992042
dihydrolipoamide dehydrogenase [Pseudomonas putida KT2440]


200
ZP_013 . . .
106891371
Dihydrolipoamide dehydrogenase [Roseiflexus sp. RS-1]


201
EAQ92192
88184724
conserved hypothetical protein [Chaetomium globosum CBS





148.51]
















TABLE 32







Examples of transhydrogenase subunit alpha polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
NP_416120
16129561
NAD(P) transhydrogenase subunit alpha [Escherichia coli K12].


2
ZP_007 . . .
75512964
COG3288: NAD/NADP transhydrogenase alpha subunit





[Escherichia coli 53638]


3
ZP_009 . . .
83587938
COG3288: NAD/NADP transhydrogenase alpha subunit





[Escherichia coli 101-1]


4
YP_669455
110641725
NAD(P) transhydrogenase subunit alpha [Escherichia coli 536]


5
YP_540800
91210814
NAD(P) transhydrogenase subunit alpha [Escherichia coli





UTI89]


6
ZP_007 . . .
75236686
COG3288: NAD/NADP transhydrogenase alpha subunit





[Escherichia coli F11]


7
NP_753890
26247850
NAD(P) transhydrogenase subunit alpha [Escherichia coli





CFT073]


8
YP_310491
74312072
pyridine nucleotide transhydrogenase, alpha subunit [Shigella





sonnei Ss046]


9
ZP_007 . . .
75234916
COG3288: NAD/NADP transhydrogenase alpha subunit





[Escherichia coli E110019]


10
YP_403177
82776828
pyridine nucleotide transhydrogenase, alpha subunit [Shigella





dysenteriae Sd197]


11
ZP_007 . . .
75190643
COG3288: NAD/NADP transhydrogenase alpha subunit





[Escherichia coli E24377A]


12
ZP_009 . . .
83570993
COG3288: NAD/NADP transhydrogenase alpha subunit





[Shigella dysenteriae 1012]


13
ZP_007 . . .
75257022
COG3288: NAD/NADP transhydrogenase alpha subunit





[Escherichia coli E22]


14
YP_407977
82544030
pyridine nucleotide transhydrogenase, alpha subunit [Shigella





boydii Sb227]


15
ZP_006 . . .
75178502
COG3288: NAD/NADP transhydrogenase alpha subunit





[Shigella boydii BS512]


16
YP_689096
110805576
pyridine nucleotide transhydrogenase, alpha subunit [Shigella





flexneri 5 str. 8401]


17
NP_310336
15831563
NAD(P) transhydrogenase subunit alpha [Escherichia coli





O157:H7 str. Sakai]


18
YP_216484
62180067
NAD(P) transhydrogenase subunit alpha [Salmonella enterica





subsp. enterica serovar Choleraesuis str. SC-B67]


19
NP_460439
16764824
NAD(P) transhydrogenase subunit alpha [Salmonella





typhimurium LT2]


20
NP_805194
29141852
NAD(P) transhydrogenase subunit alpha [Salmonella enterica





subsp. enterica serovar Typhi Ty2]


21
ABF71058
102621428
NADP transhydrogenase alpha subunit [Enterobacter cloacae]


22
ZP_008 . . .
77963333
COG3288: NAD/NADP transhydrogenase alpha subunit





[Yersinia mollaretii ATCC 43969]


23
ZP_008 . . .
77958020
COG3288: NAD/NADP transhydrogenase alpha subunit





[Yersinia bercovieri ATCC 43970]


24
ZP_008 . . .
77975377
COG3288: NAD/NADP transhydrogenase alpha subunit





[Yersinia frederiksenii ATCC 33641]


25
YP_647693
108811926
NAD(P) transhydrogenase alpha subunit [Yersinia pestis





Nepal516]


26
YP_070740
51596549
NAD(P) transhydrogenase subunit alpha [Yersinia





pseudotuberculosis IP 32953]


27
ZP_007 . . .
77629299
COG3288: NAD/NADP transhydrogenase alpha subunit





[Yersinia pseudotuberculosis IP 31758]


28
YP_050297
50121130
NAD(P) transhydrogenase subunit alpha [Erwinia carotovora





subsp. atroseptica SCRI1043]


29
ZP_008 . . .
77979498
COG3288: NAD/NADP transhydrogenase alpha subunit





[Yersinia intermedia ATCC 29909]


30
NP_929427
37526083
NAD(P) transhydrogenase subunit alpha [Photorhabdus





luminescens subsp. laumondii TTO1]


31
YP_455168
85059466
pyridine nucleotide transhydrogenase alpha subunit [Sodalis





glossinidius str. ‘morsitans’]


32
YP_206544
59713769
NAD(P) transhydrogenase subunit alpha [Vibrio fischeri ES114]


33
ZP_007 . . .
75831475
COG3288: NAD/NADP transhydrogenase alpha subunit [Vibrio





cholerae MO10]


34
ZP_010 . . .
86147993
NAD(P) transhydrogenase subunit alpha [Vibrio sp. MED222]


35
ZP_009 . . .
84393928
NAD(P) transhydrogenase subunit alpha [Vibrio splendidus





12B01]


36
ZP_007 . . .
75857576
COG3288: NAD/NADP transhydrogenase alpha subunit [Vibrio





sp. Ex25]


37
ZP_012 . . .
91226112
NAD(P) transhydrogenase subunit alpha [Vibrio alginolyticus





12G01]


38
NP_936868
37676472
NAD(P) transhydrogenase subunit alpha [Vibrio vulnificus





YJ016]


39
NP_800432
28900777
NAD(P) transhydrogenase subunit alpha [Vibrio





parahaemolyticus RIMD 2210633]


40
NP_762287
27366760
NAD(P) transhydrogenase subunit alpha [Vibrio vulnificus





CMCP6]


41
ZP_012 . . .
90577759
NAD(P) transhydrogenase subunit alpha [Vibrio angustum S14]


42
ZP_011 . . .
89073747
NAD(P) transhydrogenase subunit alpha [Photobacterium sp.





SKA34]


43
NP_245690
15602618
NAD(P) transhydrogenase subunit alpha [Pasteurella multocida





subsp. multocida str. Pm70]


44
YP_088416
52425279
NAD(P) transhydrogenase subunit alpha [Mannheimia





succiniciproducens MBEL55E]


45
YP_718440
113460378
NAD(P)(+) transhydrogenase, alpha subunit (pyridine





nucleotide transhydrogenase) [Haemophilus somnus 129PT]


46
ZP_001 . . .
32030098
COG3288: NAD/NADP transhydrogenase alpha subunit





[Haemophilus somnus 2336]


47
ZP_005 . . .
68545628
NAD(P) transhydrogenase, alpha subunit [Shewanella





amazonensis SB2B]


48
ZP_012 . . .
90412639
NAD(P) transhydrogenase subunit alpha [Photobacterium





profundum 3TCK]


49
ZP_007 . . .
75429914
NAD/NADP transhydrogenase alpha subunit [Actinobacillus





succinogenes 130Z]


50
YP_249235
68250123
NAD(P) transhydrogenase subunit alpha [Haemophilus





influenzae 86-028NP]


51
YP_132574
54302581
NAD(P) transhydrogenase subunit alpha [Photobacterium





profundum SS9]


52
NP_439513
16273272
NAD(P) transhydrogenase subunit alpha [Haemophilus





influenzae Rd KW20]


53
ZP_009 . . .
82741968
NAD(P) transhydrogenase, alpha subunit [Shewanella sp. W3-





18-1]


54
ZP_014 . . .
113949477
NAD(P) transhydrogenase, alpha subunit [Shewanella baltica





OS195]


55
YP_561942
91792291
NAD(P) transhydrogenase, alpha subunit [Shewanella





denitrificans OS217]


56
NP_719279
24375236
NAD(P) transhydrogenase subunit alpha [Shewanella oneidensis





MR-1]


57
NP_874046
33152693
NAD(P) transhydrogenase subunit alpha [Haemophilus ducreyi





35000HP]


58
YP_735209
113971416
NAD(P) transhydrogenase, alpha subunit [Shewanella sp. MR-





4]


59
ZP_008 . . .
78686308
NAD(P) transhydrogenase, alpha subunit [Shewanella sp. ANA-





3]


60
YP_736947
114046397
NAD(P) transhydrogenase, alpha subunit [Shewanella sp. MR-





7]


61
ZP_006 . . .
69950756
NAD(P) transhydrogenase, alpha subunit [Shewanella





frigidimarina NCIMB 400]


62
ZP_007 . . .
75818840
COG3288: NAD/NADP transhydrogenase alpha subunit [Vibrio





cholerae V51]


63
ZP_013 . . .
106883669
NAD(P) transhydrogenase, alpha subunit [Psychromonas





ingrahamii 37]


64
NP_283944
15794122
NAD(P) transhydrogenase subunit alpha [Neisseria meningitidis





Z2491]


65
YP_434236
83645801
NAD(P) transhydrogenase, alpha subunit [Hahella chejuensis





KCTC 2396]


66
NP_274017
15676872
NAD(P) transhydrogenase subunit alpha [Neisseria meningitidis





MC58]


67
YP_208522
59801810
NAD(P) transhydrogenase subunit alpha [Neisseria gonorrhoeae





FA 1090]


68
ZP_012 . . .
90408904
PntA [Psychromonas sp. CNPT3]


69
YP_268514
71281713
NAD(P) transhydrogenase subunit alpha [Colwellia





psychrerythraea 34H]


70
ZP_001 . . .
32035329
COG3288: NAD/NADP transhydrogenase alpha subunit





[Actinobacillus pleuropneumoniae serovar 1 str. 4074]


71
ZP_012 . . .
90202099
NAD(P) transhydrogenase, alpha subunit [Mycobacterium





vanbaalenii PYR-1]


72
YP_342322
77163797
NAD(P) transhydrogenase subunit alpha [Nitrosococcus oceani





ATCC 19707]


73
ZP_009 . . .
84495285
NAD(P) transhydrogenase subunit alpha [Janibacter sp.





HTCC2649]


74
AAY87755
68165590
NAD(P) transhydrogenase alpha subunit [Vibrio cholerae]


75
ZP_011 . . .
89340414
NAD(P) transhydrogenase, alpha subunit [Mycobacterium





flavescens PYR-GCK]


76
AAY87751
68165582
NAD(P) transhydrogenase alpha subunit [Vibrio cholerae]


77
AAY87754
68165588
NAD(P) transhydrogenase alpha subunit [Vibrio cholerae]


78
AAY87762
68165604
NAD(P) transhydrogenase alpha subunit [Vibrio cholerae]


79
YP_422187
83311923
NAD/NADP transhydrogenase alpha subunit [Magnetospirillum





magneticum AMB-1]


80
YP_637279
108797082
NAD(P) transhydrogenase, alpha subunit [Mycobacterium sp.





MCS]


81
YP_115165
53803088
NAD(P) transhydrogenase subunit alpha [Methylococcus





capsulatus str. Bath]


82
NP_821578
29826944
NAD(P) transhydrogenase subunit alpha [Streptomyces





avermitilis MA-4680]


83
ZP_006 . . .
69261416
NAD(P) transhydrogenase, alpha subunit [Magnetococcus sp.





MC-1]


84
NP_440856
16330128
NAD(P) transhydrogenase subunit alpha [Synechocystis sp.





PCC 6803]


85
ZP_002 . . .
46202292
COG3288: NAD/NADP transhydrogenase alpha subunit





[Magnetospirillum magnetotacticum MS-1]


86
YP_298860
73538493
NAD(P) transhydrogenase subunit alpha [Ralstonia eutropha





JMP134]


87
ZP_004 . . .
66966825
NAD(P) transhydrogenase, alpha subunit [Arthrobacter sp.





FB24]


88
ZP_006 . . .
71366730
NAD(P) transhydrogenase, alpha subunit [Nocardioides sp.





JS614]


89
YP_524985
89902514
NAD(P) transhydrogenase, alpha subunit [Rhodoferax





ferrireducens T118]


90
YP_055339
50842112
NAD(P) transhydrogenase subunit alpha [Propionibacterium





acnes KPA171202]


91
NP_631664
21225885
NAD(P) transhydrogenase subunit alpha [Streptomyces





coelicolor A3(2)]


92
ZP_006 . . .
74018096
NAD(P) transhydrogenase, alpha subunit [Burkholderia





ambifaria AMMD]


93
CAJ96500
113530153
NAD(P) transhydrogenase subunit alpha [Ralstonia eutropha





H16]


94
YP_366916
78060341
NAD(P) transhydrogenase subunit alpha [Burkholderia sp. 383]


95
YP_574538
92114610
NAD(P) transhydrogenase, alpha subunit [Chromohalobacter





salexigens DSM 3043]


96
ZP_004 . . .
67542770
NAD(P) transhydrogenase, alpha subunit [Burkholderia





vietnamiensis G4]


97
YP_702683
111019711
NAD(P) transhydrogenase alpha subunit [Rhodococcus sp.





RHA1]


98
ZP_007 . . .
75821435
COG3288: NAD/NADP transhydrogenase alpha subunit [Vibrio





cholerae RC385]


99
ZP_011 . . .
88798022
NAD(P) transhydrogenase subunit alpha [Reinekea sp.





MED297]


100
ZP_009 . . .
83371049
NAD(P) transhydrogenase, alpha subunit [Rhodobacter





sphaeroides ATCC 17025]


101
ZP_006 . . .
69933435
NAD(P) transhydrogenase, alpha subunit [Paracoccus





denitrificans PD1222]


102
YP_353313
77463809
NAD(P) transhydrogenase subunit alpha [Rhodobacter





sphaeroides 2.4.1]


103
ZP_009 . . .
83373326
NAD(P) transhydrogenase, alpha subunit [Rhodobacter





sphaeroides ATCC 17029]


104
ZP_010 . . .
85704984
NAD(P) transhydrogenase subunit alpha [Roseovarius sp. 217]


105
YP_612703
99080549
NAD(P) transhydrogenase, alpha subunit [Silicibacter sp.





TM1040]


106
YP_683504
110680497
NAD(P) transhydrogenase, alpha subunit [Roseobacter





denitrificans OCh 114]


107
AAQ87369
36958944
NAD(P) transhydrogenase subunit alpha [Rhizobium sp.





NGR234]


108
ZP_010 . . .
86137634
NAD(P) transhydrogenase subunit alpha [Roseobacter sp.





MED193]


109
XP_799127
72030333
PREDICTED: similar to nicotinamide nucleotide





transhydrogenase [Strongylocentrotus purpuratus]


110
ZP_010 . . .
84503572
NAD(P) transhydrogenase subunit alpha [Oceanicola batsensis





HTCC2597]


111
ZP_010 . . .
84516763
NAD(P) transhydrogenase subunit alpha [Loktanella





vestfoldensis SKA53]


112
NP_533164
17936374
NAD(P) transhydrogenase subunit alpha [Agrobacterium





tumefaciens str. C58]


113
XP_562937
57968100
ENSANGP00000025507 [Anopheles gambiae str. PEST]


114
YP_511224
89055773
NAD(P) transhydrogenase, alpha subunit [Jannaschia sp. CCS1]


115
ZP_009 . . .
83942708
NAD(P) transhydrogenase subunit alpha [Sulfitobacter sp. EE-





36]


116
YP_168028
56697658
NAD(P) transhydrogenase subunit alpha [Silicibacter pomeroyi





DSS-3]


117
EAT35199
108870974
nadp transhydrogenase [Aedes aegypti]


118
ZP_009 . . .
83953947
NAD(P) transhydrogenase subunit alpha [Sulfitobacter sp. NAS-





14.1]


119
ZP_009 . . .
83949483
NAD(P) transhydrogenase subunit alpha [Roseovarius





nubinhibens ISM]


120
XP_367628
39972475
hypothetical protein MG07539.4 [Magnaporthe grisea 70-15]


121
NP_999921
47550793
nicotinamide nucleotide transhydrogenase [Danio rerio]


122
XP_961047
85100871
hypothetical protein (mitochondrial nicotinamide nucleotide





transhydrogenase-related protein [imported] - Neurospora crassa





OR74A)


123
AAH81117
51703526
MGC83563 protein [Xenopus laevis]


124
CAF99322
47223713
unnamed protein product [Tetraodon nigroviridis]


125
CAB88572
16416047
related to mitochondrial nicotinamide nucleotide





transhydrogenase [Neurospora crassa]


126
AAI10544
83405154
Nicotinamide nucleotide transhydrogenase [Homo sapiens]


127
AAI10545
83405537
Nicotinamide nucleotide transhydrogenase [Homo sapiens]


128
NP_509028
17550456
Nicotinamide Nucleotide Transhydrogenase family member





(nnt-1) [Caenorhabditis elegans]


129
2211247B
1589396
nicotinamide nucleotide transhydrogenase


130
ZP_010 . . .
84686399
NAD(P) transhydrogenase subunit alpha [Rhodobacterales





bacterium HTCC2654]


131
NP_776368
27806831
nicotinamide nucleotide transhydrogenase [Bos taurus]


132
AAA21440
163397
nicotinamide nucleotide transhydrogenase


133
P11024
128400
NAD(P) transhydrogenase, mitochondrial precursor (Pyridine





nucleotide transhydrogenase) (Nicotinamide nucleotide





transhydrogenase)


134
XP_536481
73953769
PREDICTED: similar to NAD(P) transhydrogenase,





mitochondrial precursor (Pyridine nucleotide transhydrogenase)





(Nicotinamide nucleotide transhydrogenase) isoform 1 [Canis





familiaris]


135
XP_970382
91083631
PREDICTED: similar to nicotinamide nucleotide





transhydrogenase [Tribolium castaneum]


136
NP_001 . . .
61557127
nicotinamide nucleotide transhydrogenase [Rattus norvegicus]


137
NP_892022
33695086
nicotinamide nucleotide transhydrogenase [Homo sapiens]


138
XP_867928
73953777
PREDICTED: similar to NAD(P) transhydrogenase,





mitochondrial precursor (Pyridine nucleotide transhydrogenase)





(Nicotinamide nucleotide transhydrogenase) isoform 5 [Canis





familiaris]


139
NP_036475
33695084
nicotinamide nucleotide transhydrogenase [Homo sapiens]


140
XP_424784
50761621
PREDICTED: similar to nicotinamide nucleotide





transhydrogenase [Gallus gallus]


141
XP_646840
66826971
NAD(P)+ transhydrogenase (AB-specific) [Dictyostelium





discoideum AX4]


142
BAC40113
26352966
unnamed protein product [Mus musculus]


143
EAS31570
90301939
conserved hypothetical protein [Coccidioides immitis RS]


144
XP_867922
73953775
PREDICTED: similar to NAD(P) transhydrogenase,





mitochondrial precursor (Pyridine nucleotide transhydrogenase)





(Nicotinamide nucleotide transhydrogenase) isoform 4 [Canis





familiaris]


145
CAF99856
47230663
unnamed protein product [Tetraodon nigroviridis]


146
Q61941
51338804
NAD(P) transhydrogenase, mitochondrial precursor (Pyridine





nucleotide transhydrogenase) (Nicotinamide nucleotide





transhydrogenase)


147
2211247A
1589395
nicotinamide nucleotide transhydrogenase


148
NP_032736
31543330
nicotinamide nucleotide transhydrogenase [Mus musculus]


149
BAE35294
74198248
unnamed protein product [Mus musculus]


150
XP_748064
70985116
nicotinamide nucleotide transhydrogenase [Aspergillus





fumigatus Af293]


151
XP_389182
46130902
hypothetical protein FG09006.1 [Gibberella zeae PH-1]


152
CAE68875
39598183
Hypothetical protein CBG14838 [Caenorhabditis briggsae]


153
AAK18179
13310152
nicotinamide nucleotide transhydrogenase [Acetabularia





acetabulum]


154
AAG02246
11597233
NAD(P)H transhydrogenase [Acetabularia acetabulum]


155
AAC41577
6478876
pyridine nucleotidetranshydrogenase [Entamoeba histolytica]


156
XP_627136
66359916
pyridine nucleotide/NAD(P) transhydrogenase alpha plus beta





subunits, duplicated gene, [Cryptosporidium parvum Iowa II]


157
XP_666495
67602649
transhydrogenase 7B2 [Cryptosporidium hominis TU502]


158
BAE40577
74219995
unnamed protein product [Mus musculus]


159
CAH90079
55726630
hypothetical protein [Pongo pygmaeus]


160
AAA80188
571367
nicotinamide nucleotide transhydrogenase


161
EAQ86424
88178956
conserved hypothetical protein [Chaetomium globosum CBS





148.51]


162
AAA29077
305062
transhydrogenase


163
AAA29081
158904
transhydrogenase


164
YP_724141
113478080
NAD(P)(+) transhydrogenase (AB-specific) [Trichodesmium





erythraeum IMS101]


165
NP_487450
17230902
nicotinamide nucleotide transhydrogenase, subunit alpha





[Nostoc sp. PCC 7120]


166
YP_323932
75909636
Alanine dehydrogenase/PNT-like [Anabaena variabilis ATCC





29413]


167
ZP_005 . . .
67924536
NAD(P)(+) transhydrogenase (AB-specific) [Crocosphaera





watsonii WH 8501]


168
ZP_013 . . .
110607624
Alanine dehydrogenase/PNT-like [Maricaulis maris MCS10]


169
ZP_012 . . .
91222948
NAD(P) transhydrogenase subunit alpha [Psychroflexus torquis





ATCC 700755]


170
ZP_009 . . .
82737423
NAD/NADP transhydrogenase, NAD(H)-binding DI subunit





[Pseudomonas putida F1]


171
YP_000046
45655960
proton-translocating transhydrogenase, subunit alpha part 1





[Leptospira interrogans serovar Copenhageni str. Fiocruz L1-





130]


172
YP_257267
70733627
NAD(P) transhydrogenase, alpha subunit part 1 [Pseudomonas





fluorescens Pf-5]


173
ZP_001 . . .
23130320
COG3288: NAD/NADP transhydrogenase alpha subunit





[Nostoc punctiforme PCC 73102]


174
ZP_013 . . .
110593183
NAD(P)(+) transhydrogenase (AB-specific) [Acidovorax sp.





JS42]


175
ZP_009 . . .
83859916
nicotinamide nucleotide transhydrogenase, subunit





[Oceanicaulis alexandrii HTCC2633]


176
YP_526430
90020603
Glycogen/starch/alpha-glucan phosphorylase [Saccharophagus





degradans 2-40]


177
ZP_012 . . .
89362826
nicotinamide nucleotide transhydrogenase, subunit alpha1





[Xanthobacter autotrophicus Py2]


178
YP_277175
71737873
NAD(P) transhydrogenase, subunit alpha part 1 [Pseudomonas





syringae pv. phaseolicola 1448A]


179
YP_238081
66048240
Alanine dehydrogenase/PNT, C-terminal:Alanine





dehydrogenase/PNT, N-terminal [Pseudomonas syringae pv.





syringae B728a]


180
YP_675347
110635139
alanine dehydrogenase/PNT-like [Mesorhizobium sp. BNC1]


181
YP_345847
77456342
NAD(P)(+) transhydrogenase (AB-specific) [Pseudomonas





fluorescens PfO-1]


182
AAQ87237
36958769
NAD(P) transhydrogenase subunit alpha [Rhizobium sp.





NGR234]


183
ZP_013 . . .
94499798
pyridine nucleotide transhydrogenase alpha subunit





[Oceanobacter sp. RED65]


184
NP_881481
33593837
NAD(P) transhydrogenase, subunit alpha part 1 [Bordetella





pertussis Tohama I]


185
P0C186
91207608
NAD(P) transhydrogenase subunit alpha part 1 (Pyridine





nucleotide transhydrogenase subunit alpha 1) (Nicotinamide





nucleotide transhydrogenase subunit alpha 1) (Proton-





translocating transhydrogenase component 1) (dI)


186
1PTJB
37927621
Chain B, Crystal Structure Analysis Of The Di And Diii





Complex Of Transhydrogenase With A Thio-Nicotinamide





Nucleotide Analogue


187
YP_485056
86748560
NAD(P)(+) transhydrogenase (AB-specific)





[Rhodopseudomonas palustris HaA2]


188
YP_620103
107021776
alanine dehydrogenase/PNT-like [Burkholderia cenocepacia AU





1054]


189
ZP_008 . . .
77952426
pyridine nucleotide transhydrogenase alpha subunit





[Marinobacter aquaeolei VT8]


190
NP_840933
30248863
Alanine dehydrogenase and pyridine nucleotide





transhydrogenase [Nitrosomonas europaea ATCC 19718]


191
2FRDB
90109601
Chain B, Structure Of Transhydrogenase





(Di.S138a.Nadh)2(Diii.Nadph)1 Asymmetric Complex


192
NP_888491
33600931
NAD(P) transhydrogenase, subunit alpha part 1 [Bordetella





bronchiseptica RB50]


193
XP_726447
82596885
NAD(P) transhydrogenase subunit beta [Plasmodium yoelii





yoelii str. 17XNL]


194
YP_551329
91790377
NAD(P)(+) transhydrogenase (AB-specific) [Polaromonas sp.





JS666]


195
ZP_006 . . .
71548985
NAD(P)(+) transhydrogenase (AB-specific) [Nitrosomonas





eutropha C71]


196
YP_568553
91975894
NAD(P)(+) transhydrogenase (AB-specific)





[Rhodopseudomonas palustris BisB5]


197
2FSVB
90109621
Chain B, Structure Of Transhydrogenase (Di.D135n.Nad+)





2(Diii.E155w.Nadp+)1 Asymmetric Complex


198
1NM5B
42543078
Chain B, R. Rubrum Transhydrogenase (Di.Q132n)2(Diii)1





Asymmetric Complex


199
1L7DB
27065343
Chain B, Crystal Structure Of R. Rubrum Transhydrogenase





Domain I Without Bound Nad(H)


200
ZP_012 . . .
90418769
NAD(P) transhydrogenase, subunit alpha part 1 [Aurantimonas





sp. SI85-9A1]


201
2FR8B
90109598
Chain B, Structure Of Transhydrogenase





(Di.R127a.Nad+)2(Diii.Nadp+)1 Asymmetric Complex
















TABLE 33







Examples of transhydrogenase subunit beta polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
NP_416119
16129560
pyridine nucleotide transhydrogenase [Escherichia coli K12].


2
YP_669454
110641724
NAD(P) transhydrogenase subunit beta [Escherichia coli 536]


3
ZP_007 . . .
75234915
COG1282: NAD/NADP transhydrogenase beta subunit





[Escherichia coli E110019]


4
ZP_007 . . .
75230949
COG1282: NAD/NADP transhydrogenase beta subunit





[Escherichia coli B7A]


5
YP_407978
82544031
pyridine nucleotide transhydrogenase, beta subunit [Shigella





boydii Sb227]


6
YP_150630
56413555
pyridine nucleotide transhydrogenase [Salmonella enterica





subsp. enterica serovar Paratyphi A str. ATCC 9150]


7
YP_216485
62180068
pyridine nucleotide transhydrogenase [Salmonella enterica





subsp. enterica serovar Choleraesuis str. SC-B67]


8
ABF71059
102621429
NADP transhydrogenase beta subunit [Enterobacter cloacae]


9
NP_929428
37526084
pyridine nucleotide transhydrogenase [Photorhabdus





luminescens subsp. laumondii TTO1]


10
YP_050298
50121131
pyridine nucleotide transhydrogenase [Erwinia carotovora





subsp. atroseptica SCRI1043]


11
ZP_008 . . .
77979497
COG1282: NAD/NADP transhydrogenase beta subunit





[Yersinia intermedia ATCC 29909]


12
ZP_008 . . .
77975378
COG1282: NAD/NADP transhydrogenase beta subunit





[Yersinia frederiksenii ATCC 33641]


13
ZP_008 . . .
77958019
COG1282: NAD/NADP transhydrogenase beta subunit





[Yersinia bercovieri ATCC 43970]


14
ZP_008 . . .
77963332
COG1282: NAD/NADP transhydrogenase beta subunit





[Yersinia mollaretii ATCC 43969]


15
YP_647692
108811925
NAD(P) transhydrogenase subunit beta [Yersinia pestis





Nepal516]


16
YP_455167
85059465
pyridine nucleotide transhydrogenase beta subunit [Sodalis





glossinidius str. ‘morsitans’]


17
NP_719280
24375237
pyridine nucleotide transhydrogenase [Shewanella oneidensis





MR-1]


18
YP_736946
114046396
NAD(P) transhydrogenase, beta subunit [Shewanella sp. MR-7]


19
ZP_009 . . .
82741967
NAD(P) transhydrogenase, beta subunit [Shewanella sp. W3-18-





1]


20
NP_245689
15602617
pyridine nucleotide transhydrogenase [Pasteurella multocida





subsp. multocida str. Pm70]


21
ZP_005 . . .
68541685
NAD(P) transhydrogenase, beta subunit [Shewanella baltica





OS155]


22
ZP_012 . . .
90412640
putative NAD(P) transhydrogenase, beta subunit





[Photobacterium profundum 3TCK]


23
ZP_001 . . .
53732668
COG1282: NAD/NADP transhydrogenase beta subunit





[Haemophilus influenzae R2846]


24
YP_249234
68250122
pyridine nucleotide transhydrogenase [Haemophilus influenzae





86-028NP]


25
NP_439514
16273273
pyridine nucleotide transhydrogenase [Haemophilus influenzae





Rd KW20]


26
ZP_005 . . .
68545629
NAD(P) transhydrogenase, beta subunit [Shewanella





amazonensis SB2B]


27
YP_132575
54302582
pyridine nucleotide transhydrogenase [Photobacterium





profundum SS9]


28
ZP_011 . . .
89073748
pyridine nucleotide transhydrogenase [Photobacterium sp.





SKA34]


29
NP_800431
28900776
pyridine nucleotide transhydrogenase [Vibrio parahaemolyticus





RIMD 2210633]


30
ZP_012 . . .
90577760
pyridine nucleotide transhydrogenase [Vibrio angustum S14]


31
ZP_007 . . .
75857577
COG1282: NAD/NADP transhydrogenase beta subunit [Vibrio





sp. Ex25]


32
NP_936867
37676471
pyridine nucleotide transhydrogenase [Vibrio vulnificus YJ016]


33
ZP_007 . . .
75818461
COG1282: NAD/NADP transhydrogenase beta subunit [Vibrio





cholerae V51]


34
ZP_007 . . .
75831476
COG1282: NAD/NADP transhydrogenase beta subunit [Vibrio





cholerae MO10]


35
ZP_012 . . .
91226113
pyridine nucleotide transhydrogenase [Vibrio alginolyticus





12G01]


36
YP_206543
59713768
pyridine nucleotide transhydrogenase [Vibrio fischeri ES114]


37
YP_088415
52425278
pyridine nucleotide transhydrogenase [Mannheimia





succiniciproducens MBEL55E]


38
ZP_001 . . .
32035330
COG1282: NAD/NADP transhydrogenase beta subunit





[Actinobacillus pleuropneumoniae serovar 1 str. 4074]


39
ZP_006 . . .
69950757
NAD(P) transhydrogenase, beta subunit [Shewanella





frigidimarina NCIMB 400]


40
ZP_010 . . .
86147992
pyridine nucleotide transhydrogenase [Vibrio sp. MED222]


41
ZP_009 . . .
84393927
NAD(P) transhydrogenase, beta subunit [Vibrio splendidus





12B01]


42
ZP_007 . . .
75429915
NAD/NADP transhydrogenase beta subunit [Actinobacillus





succinogenes 130Z]


43
NP_274015
15676870
pyridine nucleotide transhydrogenase [Neisseria meningitidis





MC58]


44
NP_283942
15794120
pyridine nucleotide transhydrogenase [Neisseria meningitidis





Z2491]


45
YP_208524
59801812
pyridine nucleotide transhydrogenase [Neisseria gonorrhoeae





FA 1090]


46
YP_718441
113460379
NAD(P)(+) transhydrogenase, beta subunit (pyridine nucleotide





transhydrogenase) [Haemophilus somnus 129PT]


47
NP_874045
33152692
pyridine nucleotide transhydrogenase [Haemophilus ducreyi





35000HP]


48
YP_561941
91792290
NAD(P) transhydrogenase, beta subunit [Shewanella





denitrificans OS217]


49
YP_434235
83645800
NAD/NADP transhydrogenase beta subunit [Hahella chejuensis





KCTC 2396]


50
YP_268515
71280969
pyridine nucleotide transhydrogenase [Colwellia





psychrerythraea 34H]


51
ZP_013 . . .
106883670
NAD(P) transhydrogenase, beta subunit [Psychromonas





ingrahamii 37]


52
ZP_009 . . .
84495284
pyridine nucleotide transhydrogenase [Janibacter sp.





HTCC2649]


53
YP_637278
108797081
NAD(P) transhydrogenase, beta subunit [Mycobacterium sp.





MCS]


54
ZP_012 . . .
90408905
NAD(P) transhydrogenase subunit beta [Psychromonas sp.





CNPT3]


55
ZP_011 . . .
89340413
NAD(P) transhydrogenase, beta subunit [Mycobacterium





flavescens PYR-GCK]


56
ZP_012 . . .
90202100
NAD(P) transhydrogenase, beta subunit [Mycobacterium





vanbaalenii PYR-1]


57
NP_631663
21225884
NAD(P) transhydrogenase beta subunit [Streptomyces





coelicolor A3(2)]


58
NP_821577
29826943
pyridine nucleotide transhydrogenase, beta subunit





[Streptomyces avermitilis MA-4680]


59
YP_702682
111019710
NAD(P) transhydrogenase beta subunit [Rhodococcus sp.





RHA1]


60
YP_422186
83311922
NAD/NADP transhydrogenase beta subunit [Magnetospirillum





magneticum AMB-1]


61
ZP_006 . . .
71366731
NAD(P) transhydrogenase, beta subunit [Nocardioides sp.





JS614]


62
YP_115164
53803089
NAD(P) transhydrogenase, beta subunit [Methylococcus





capsulatus str. Bath]


63
YP_524984
89902513
NAD(P) transhydrogenase, beta subunit [Rhodoferax





ferrireducens T118]


64
NP_440860
16330132
pyridine nucleotide transhydrogenase beta subunit





[Synechocystis sp. PCC 6803]


65
ZP_004 . . .
66966824
NAD(P) transhydrogenase, beta subunit [Arthrobacter sp. FB24]


66
ZP_011 . . .
88798021
pyridine nucleotide transhydrogenase [Reinekea sp. MED297]


67
YP_342321
77163796
NAD(P) transhydrogenase, beta subunit [Nitrosococcus oceani





ATCC 19707]


68
ZP_006 . . .
69261415
NAD(P) transhydrogenase, beta subunit [Magnetococcus sp.





MC-1]


69
ZP_004 . . .
67542769
NAD(P) transhydrogenase, beta subunit [Burkholderia





vietnamiensis G4]


70
YP_366915
78060340
NAD(P) transhydrogenase, beta subunit [Burkholderia sp. 383]


71
ZP_006 . . .
74018097
NAD(P) transhydrogenase, beta subunit [Burkholderia ambifaria





AMMD]


72
YP_298859
73538492
NAD(P) transhydrogenase, beta subunit [Ralstonia eutropha





JMP134]


73
YP_055340
50842113
NAD(P) transhydrogenase subunit beta [Propionibacterium





acnes KPA171202]


74
ZP_009 . . .
83949482
NAD(P)+ transhydrogenase, beta subunit [Roseovarius





nubinhibens ISM]


75
CAJ96499
113530152
NAD(P) transhydrogenase subunit beta [Ralstonia eutropha





H16]


76
ZP_006 . . .
69933434
NAD(P) transhydrogenase, beta subunit [Paracoccus





denitrificans PD1222]


77
YP_168027
56697657
NAD(P)+ transhydrogenase, beta subunit [Silicibacter pomeroyi





DSS-3]


78
NP_533165
17936375
NAD(P)+ transhydrogenase beta chain [Agrobacterium





tumefaciens str. C58]


79
AAQ87370
36958945
NAD(P) transhydrogenase subunit beta [Rhizobium sp.





NGR234]


80
ZP_009 . . .
83942707
NAD(P)+ transhydrogenase, beta subunit [Sulfitobacter sp. EE-





36]


81
ZP_009 . . .
83953946
NAD(P)+ transhydrogenase, beta subunit [Sulfitobacter sp.





NAS-14.1]


82
ZP_007 . . .
75813705
COG1282: NAD/NADP transhydrogenase beta subunit [Vibrio





cholerae V52]


83
ZP_010 . . .
84503573
NAD(P)+ transhydrogenase, beta subunit [Oceanicola batsensis





HTCC2597]


84
ZP_010 . . .
84686400
NAD(P)+ transhydrogenase, beta subunit [Rhodobacterales





bacterium HTCC2654]


85
YP_612702
99080548
NAD(P) transhydrogenase, beta subunit [Silicibacter sp.





TM1040]


86
ZP_010 . . .
84516762
NAD(P)+ transhydrogenase, beta subunit [Loktanella





vestfoldensis SKA53]


87
ZP_010 . . .
86137633
NAD(P)+ transhydrogenase, beta subunit [Roseobacter sp.





MED193]


88
YP_511223
89055772
NAD(P) transhydrogenase, beta subunit [Jannaschia sp. CCS1]


89
ZP_010 . . .
85704983
NAD(P)+ transhydrogenase, beta subunit [Roseovarius sp. 217]


90
ZP_007 . . .
75822802
COG1282: NAD/NADP transhydrogenase beta subunit [Vibrio





cholerae RC385]


91
YP_683503
110680496
NAD(P) transhydrogenase, beta subunit [Roseobacter





denitrificans OCh 114]


92
NP_949516
39937240
nicotinamide nucleotide transhydrogenase, subunit beta





[Rhodopseudomonas palustris CGA009]


93
YP_418478
83269187
NAD(P) transhydrogenase, beta subunit [Brucella melitensis





biovar Abortus 2308]


94
YP_485058
86748562
NAD(P) transhydrogenase, beta subunit [Rhodopseudomonas





palustris HaA2]


95
ZP_009 . . .
83859918
nicotinamide nucleotide transhydrogenase, subunit beta





[Oceanicaulis alexandrii HTCC2633]


96
ZP_008 . . .
77740973
NAD(P) transhydrogenase, beta subunit [Rhodopseudomonas





palustris BisA53]


97
ZP_012 . . .
89362731
NAD(P) transhydrogenase, beta subunit [Xanthobacter





autotrophicus Py2]


98
ZP_008 . . .
77814001
NAD(P) transhydrogenase, beta subunit [Shewanella





putrefaciens CN-32]


99
ZP_010 . . .
84704197
PntB, NAD(P) transhydrogenase, beta subunit [Parvularcula





bermudensis HTCC2503]


100
YP_533811
90425441
NAD(P) transhydrogenase, beta subunit [Rhodopseudomonas





palustris BisB18]


101
P0C188
91207612
NAD(P) transhydrogenase subunit beta (Pyridine nucleotide





transhydrogenase subunit beta) (Nicotinamide nucleotide





transhydrogenase subunit beta) (Proton-translocating





transhydrogenase NADP(H)-binding component) (dIII)


102
YP_568555
91975896
NAD(P) transhydrogenase, beta subunit [Rhodopseudomonas





palustris BisB5]


103
ZP_012 . . .
90418771
NAD(P) transhydrogenase, subunit beta [Aurantimonas sp.





SI85-9A1]


104
YP_526432
90020605
NAD(P) transhydrogenase, beta subunit [Saccharophagus





degradans 2-40]


105
ZP_008 . . .
78699497
NAD(P)+ transhydrogenase beta chain [Bradyrhizobium sp.





BTAi1]


106
XP_424784
50761621
PREDICTED: similar to nicotinamide nucleotide





transhydrogenase [Gallus gallus]


107
XP_799127
72030333
PREDICTED: similar to nicotinamide nucleotide





transhydrogenase [Strongylocentrotus purpuratus]


108
ZP_010 . . .
85716091
NAD/NADP transhydrogenase beta subunit [Nitrobacter sp. Nb-





311A]


109
YP_605919
104779421
pyridine nucleotide transhydrogenase, beta subunit





[Pseudomonas entomophila L48]


110
YP_457359
85373297
PntB, NAD(P) transhydrogenase, beta subunit [Erythrobacter





litoralis HTCC2594]


111
XP_970382
91083631
PREDICTED: similar to nicotinamide nucleotide





transhydrogenase [Tribolium castaneum]


112
BAB51677
14025075
nicotinamide nucleotide transhydrogenase, subunit beta





[Mesorhizobium loti MAFF303099]


113
ZP_012 . . .
94413536
hypothetical protein PaerP_01004711 [Pseudomonas aeruginosa





PA7]


114
ZP_011 . . .
88938736
NAD/NADP transhydrogenase beta subunit-like [Acidiphilium





cryptum JF-5]


115
NP_795188
28872569
NAD(P) transhydrogenase, beta subunit [Pseudomonas syringae





pv. tomato str. DC3000]


116
YP_257265
70733625
NAD(P) transhydrogenase, beta subunit [Pseudomonas





fluorescens Pf-5]


117
NP_773764
27382235
NAD(P)+ transhydrogenase beta chain [Bradyrhizobium





japonicum USDA 110]


118
YP_576517
92116788
NAD(P) transhydrogenase, beta subunit [Nitrobacter





hamburgensis X14]


119
ZP_013 . . .
107099186
hypothetical protein PaerPA_01000196 [Pseudomonas





aeruginosa PACS2]


120
YP_557045
91781839
Putative NAD(P) transhydrogenase, beta subunit [Burkholderia





xenovorans LB400]


121
ZP_009 . . .
82737421
pyridine nucleotide transhydrogenase, beta subunit





[Pseudomonas putida F1]


122
YP_345845
77456340
NAD(P) transhydrogenase, beta subunit [Pseudomonas





fluorescens PfO-1]


123
NP_999921
47550793
nicotinamide nucleotide transhydrogenase [Danio rerio]


124
YP_411848
82702282
NAD(P) transhydrogenase, beta subunit [Nitrosospira





multiformis ATCC 25196]


125
CAF99856
47230663
unnamed protein product [Tetraodon nigroviridis]


126
YP_675345
110635137
NAD(P) transhydrogenase, beta subunit [Mesorhizobium sp.





BNC1]


127
EAT35199
108870974
nadp transhydrogenase [Aedes aegypti]


128
YP_277177
71736851
NAD(P) transhydrogenase, beta subunit [Pseudomonas syringae





pv. phaseolicola 1448A]


129
YP_263852
71065125
NAD(P) transhydrogenase, beta subunit [Psychrobacter arcticus





273-4]


130
NP_840935
30248865
NAD(P) transhydrogenase beta subunit [Nitrosomonas europaea





ATCC 19718]


131
XP_867922
73953775
PREDICTED: similar to NAD(P) transhydrogenase,





mitochondrial precursor (Pyridine nucleotide transhydrogenase)





(Nicotinamide nucleotide transhydrogenase) isoform 4 [Canis





familiaris]


132
XP_867916
73953773
PREDICTED: similar to NAD(P) transhydrogenase,





mitochondrial precursor (Pyridine nucleotide transhydrogenase)





(Nicotinamide nucleotide transhydrogenase) isoform 3 [Canis





familiaris]


133
XP_536481
73953769
PREDICTED: similar to NAD(P) transhydrogenase,





mitochondrial precursor (Pyridine nucleotide transhydrogenase)





(Nicotinamide nucleotide transhydrogenase) isoform 1 [Canis





familiaris]


134
XP_867928
73953777
PREDICTED: similar to NAD(P) transhydrogenase,





mitochondrial precursor (Pyridine nucleotide transhydrogenase)





(Nicotinamide nucleotide transhydrogenase) isoform 5 [Canis





familiaris]


135
NP_001 . . .
61557127
nicotinamide nucleotide transhydrogenase [Rattus norvegicus]


136
YP_238083
66048242
NAD(P) transhydrogenase, beta subunit [Pseudomonas syringae





pv. syringae B728a]


137
BAE40577
74219995
unnamed protein product [Mus musculus]


138
BAC39226
26351179
unnamed protein product [Mus musculus]


139
ZP_013 . . .
94494989
NAD(P) transhydrogenase, beta subunit [Sphingomonas sp.





SKA58]


140
NP_032736
31543330
nicotinamide nucleotide transhydrogenase [Mus musculus]


141
BAC40113
26352966
unnamed protein product [Mus musculus]


142
ZP_004 . . .
67155631
NAD(P) transhydrogenase, beta subunit [Azotobacter vinelandii





AvOP]


143
YP_579812
93005375
NAD(P) transhydrogenase, beta subunit [Psychrobacter





cryohalolentis K5]


144
YP_297031
73542511
NAD(P) transhydrogenase, beta subunit [Ralstonia eutropha





JMP134]


145
YP_585107
94311897
NAD(P) transhydrogenase, beta subunit [Ralstonia





metallidurans CH34]


146
YP_497119
87199862
NAD(P) transhydrogenase, beta subunit [Novosphingobium





aromaticivorans DSM 12444]


147
AAQ87239
36958771
NAD(P) transhydrogenase subunit beta [Rhizobium sp.





NGR234]


148
NP_888489
33600929
NAD(P) transhydrogenase subunit beta [Bordetella





bronchiseptica RB50]


149
Q61941
51338804
NAD(P) transhydrogenase, mitochondrial precursor (Pyridine





nucleotide transhydrogenase) (Nicotinamide nucleotide





transhydrogenase)


150
NP_776368
27806831
nicotinamide nucleotide transhydrogenase [Bos taurus]


151
NP_884728
33597085
NAD(P) transhydrogenase subunit beta [Bordetella parapertussis





12822]


152
AAA21440
163397
nicotinamide nucleotide transhydrogenase


153
YP_441808
83721084
NAD(P) transhydrogenase, beta subunit [Burkholderia





thailandensis E264]


154
AAI10544
83405154
Nicotinamide nucleotide transhydrogenase [Homo sapiens]


155
NP_899769
34495554
NAD(P) transhydrogenase, beta subunit [Chromobacterium





violaceum ATCC 12472]


156
NP_422097
16127533
NAD(P) transhydrogenase, beta subunit [Caulobacter crescentus





CB15]


157
XP_312859
58383882
ENSANGP00000016622 [Anopheles gambiae str. PEST]


158
ZP_009 . . .
84360819
COG1282: NAD/NADP transhydrogenase beta subunit





[Burkholderia dolosa AUO158]


159
ZP_014 . . .
113935785
NAD(P) transhydrogenase, beta subunit [Caulobacter sp. K31]


160
ZP_006 . . .
71548983
NAD(P) transhydrogenase, beta subunit [Nitrosomonas eutropha





C71]


161
AAH81117
51703526
MGC83563 protein [Xenopus laevis]


162
CAH90079
55726630
hypothetical protein [Pongo pygmaeus]


163
BAE35294
74198248
unnamed protein product [Mus musculus]


164
ZP_014 . . .
113872300
probable NAD(P) transhydrogenase subunit beta transmembrane





protein [Sinorhizobium medicae WSM419]


165
AAI10545
83405537
Nicotinamide nucleotide transhydrogenase [Homo sapiens]


166
NP_036475
33695084
nicotinamide nucleotide transhydrogenase [Homo sapiens]


167
YP_727574
113869085
NAD(P) transhydrogenase subunit beta [Ralstonia eutropha





H16]


168
2211247B
1589396
nicotinamide nucleotide transhydrogenase


169
2211247A
1589395
nicotinamide nucleotide transhydrogenase


170
AAN62246
24461677
putative pyridine nucleotide transhydrogenase, beta subunit





[Pseudomonas aeruginosa]


171
P11024
128400
NAD(P) transhydrogenase, mitochondrial precursor (Pyridine





nucleotide transhydrogenase) (Nicotinamide nucleotide





transhydrogenase)


172
NP_892022
33695086
nicotinamide nucleotide transhydrogenase [Homo sapiens]


173
NP_386966
15966613
PROBABLE NAD(P) TRANSHYDROGENASE SUBUNIT





BETA TRANSMEMBRANE PROTEIN [Sinorhizobium





meliloti 1021]


174
YP_299910
73539543
NAD(P) transhydrogenase, beta subunit [Ralstonia eutropha





JMP134]


175
ZP_012 . . .
91769178
NAD(P) transhydrogenase, beta subunit [Psychrobacter sp.





PRwf-1]


176
YP_293241
72383887
NAD(P) transhydrogenase, beta subunit [Ralstonia eutropha





JMP134]


177
YP_299480
73539113
NAD(P) transhydrogenase, beta subunit [Ralstonia eutropha





JMP134]


178
YP_293567
72384213
NAD(P) transhydrogenase, beta subunit [Ralstonia eutropha





JMP134]


179
YP_725774
113867285
NAD(P) transhydrogenase subunit beta [Ralstonia eutropha





H16]


180
YP_620105
107021778
NAD(P) transhydrogenase, beta subunit [Burkholderia





cenocepacia AU 1054]


181
YP_725367
113866878
NAD(P) transhydrogenase subunit beta [Ralstonia eutropha





H16]


182
NP_520854
17547452
PROBABLE TRANSMEMBRANE NADP





TRANSHYDROGENASE (BETA SUBUNIT)





OXIDOREDUCTASE PROTEIN [Ralstonia solanacearum





GMI1000]


183
ZP_009 . . .
83746755
PntB [Ralstonia solanacearum UW551]


184
ZP_013 . . .
100235717
hypothetical protein Bpse4_03000891 [Burkholderia





pseudomallei 406e]


185
YP_334763
76809085
NAD(P) transhydrogenase subunit beta [Burkholderia





pseudomallei 1710b]


186
ZP_013 . . .
100917505
hypothetical protein Bmal10_03001254 [Burkholderia mallei





10399]


187
ZP_004 . . .
67667725
NAD(P) transhydrogenase, beta subunit [Burkholderia





cenocepacia HI2424]


188
ZP_012 . . .
91762289
NAD(p) transhydrogenase subunit beta [Candidatus Pelagibacter





ubique HTCC1002]


189
YP_471093
86359201
NAD(P)(+) transhydrogenase (AB-specific), beta subunit





protein [Rhizobium etli CFN 42]


190
ZP_010 . . .
85707884
PntB, NAD(P) transhydrogenase, beta subunit [Erythrobacter sp.





NAP1]


191
YP_293266
72383912
NAD(P) transhydrogenase, beta subunit [Ralstonia eutropha





JMP134]


192
ZP_009 . . .
84356795
COG1282: NAD/NADP transhydrogenase beta subunit





[Burkholderia cenocepacia PC184]


193
YP_266000
71083281
NAD(p) transhydrogenase subunit beta [Candidatus





Pelagibacter ubique HTCC1062]


194
CAE68875
39598183
Hypothetical protein CBG14838 [Caenorhabditis briggsae]


195
YP_368033
78065264
NAD(P) transhydrogenase, beta subunit [Burkholderia sp. 383]


196
YP_616428
103486867
NAD(P) transhydrogenase, beta subunit [Sphingopyxis





alaskensis RB2256]


197
YP_246075
67458451
NAD(p) transhydrogenase subunit beta [Rickettsia felis





URRWXCal2]


198
YP_537194
91204839
NAD(p) transhydrogenase subunit beta [Rickettsia bellii





RML369-C]


199
XP_646840
66826971
NAD(P)+ transhydrogenase (AB-specific) [Dictyostelium





discoideum AX4]


200
ZP_009 . . .
83747817
NAD(P) transhydrogenase subunit beta [Ralstonia solanacearum





UW551]


201
YP_047599
50086089
pyridine nucleotide transhydrogenase, beta subunit





[Acinetobacter sp. ADP1]
















TABLE 34







Examples of pox2 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_505264.1
50555712
YlPOX2 [Yarrowia lipolytica].


2
O74936
59799074
Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)


3
XP_504475
50554133
YlPOX4 [Yarrowia lipolytica]


4
XP_502199
50549457
YlPOX5 [Yarrowia lipolytica]


5
O74934
59799072
Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)


6
XP_504703
50554589
YlPOX1 [Yarrowia lipolytica]


7
XP_503632
50552444
hypothetical protein [Yarrowia lipolytica]


8
XP_760471
71020481
hypothetical protein UM04324.1 [Ustilago maydis 521]


9
XP_571768
58269224
Acyl-coenzyme A oxidase I [Cryptococcus neoformans var.





neoformans JEC21]


10
XP_717995
68475844
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


11
P08790
17373073
Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)


12
Q6BRD5
59799027
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


13
OXCKX5
66061
acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal - yeast





(Candida tropicalis )


14
BAA83482
5763520
acyl-CoA oxidase [Candida tropicalis]


15
XP_457726
50417804
hypothetical protein DEHA0C01155g [Debaryomyces hansenii





CBS767]


16
BAA83483
5763522
acyl-CoA oxidase [Candida tropicalis]


17
OXCKPM
66060
acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast





(Candida maltosa )


18
AAA34362
170912
acyl-coenzyme A oxidase II precursor


19
Q9Y7B1
60391213
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


20
XP_721610
68468582
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


21
AAA34361
170910
PXP-2 protein


22
1306283A
225549
oxidase, fatty acyl


23
P06598
17373023
Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)





(Peroxisomal fatty acyl-CoA oxidase)


24
XP_721613
68468588
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


25
XP_459232
50421365
hypothetical protein DEHA0D18667g [Debaryomyces hansenii





CBS767]


26
Q00468
2498206
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)


27
Q6CKK7
59799028
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


28
NP_011310
6321233
Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-





oxidation pathway; localized to the peroxisomal matrix; Pox1p





[Saccharomyces cerevisiae]


29
AAA34891
172217
acyl-coenzyme A oxidase


30
Q6FY63
59799032
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


31
Q756A9
60391210
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


32
O65202
62286589
Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chain





acyl-CoA oxidase) (AtCX1)


33
1W07B
58177067
Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 1


34
NP_567513
18414744
ACX1 (ACYL-COA OXIDASE 1) [Arabidopsis thaliana]


35
H71434
7488059
probable apetala2 domain TINY - Arabidopsis thaliana


36
XP_001 . . .
109118312
PREDICTED: similar to acyl-Coenzyme A oxidase isoform b





[Macaca mulatta]


37
Q5RC19
62286600
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


38
Q15067
17380467
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)


39
NP_009223
30089974
acyl-Coenzyme A oxidase isoform b [Homo sapiens]


40
AAB30019
7689914
peroxisomal acyl-coenzyme A oxidase [Homo sapiens]


41
CAH90691
55727877
hypothetical protein [Pongo pygmaeus]


42
AAL01888
15553480
acyl-CoA oxidase [Glycine max]


43
AAA19113
458119
acyl-CoA oxidase


44
AAA18595
495475
peroxisomal fatty acyl-coA oxidase


45
XP_540441
73965013
PREDICTED: similar to acyl-Coenzyme A oxidase isoform a





[Canis familiaris]


46
NP_001 . . .
54400372
hypothetical protein LOC449662 [Danio rerio]


47
NP_001 . . .
78369480
acyl-Coenzyme A oxidase 1, palmitoyl [Bos taurus]


48
NP_004026
30089972
acyl-Coenzyme A oxidase isoform a [Homo sapiens]


49
AAH08767
14250616
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


50
CAD97622
31873262
hypothetical protein [Homo sapiens]


51
I38095
2117541
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal - human


52
NP_001 . . .
55741614
acyl-Coenzyme A oxidase 1, palmitoyl [Gallus gallus]


53
CAA68660
2673
acyl-coenzyme A oxidase [Candida tropicalis]


54
Q8HYL8
34098564
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


55
B54942
1082171
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II -





human


56
AAH10425
14714578
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


57
CAJ83302
89271321
acyl-Coenzyme A oxidase 2, branched chain [Xenopus





tropicalis]


58
AAO15577
27462768
acyl-CoA oxidase type 2 [Phascolarctos cinereus]


59
XP_414406
50754485
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Gallus gallus]


60
AAH97101
67678187
Zgc: 92584 protein [Danio rerio]


61
AAH85743
55249685
Acyl-Coenzyme A oxidase 1, palmitoyl [Rattus norvegicus]


62
2DDHA
93279231
Chain A, Crystal Structure Of Acyl-Coa Oxidase Complexed





With 3-Oh-Dodecanoate


63
Q9ZQP2
62286640
Putative acyl-coenzyme A oxidase 1.2, peroxisomal


64
AAH63727
39795632
MGC68531 protein [Xenopus laevis]


65
NP_001 . . .
62751552
MGC108278 protein [Xenopus tropicalis]


66
AAH68891
46250227
MGC83074 protein [Xenopus laevis]


67
AAW78689
58531948
peroxisomal acyl-CoA oxidase 1A [Lycopersicon esculentum]


68
2FONC
109157678
Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa





Oxidase From Lycopersicon Esculentum (Tomato)


69
ABE83706
92875906
acyl-CoA oxidase [Medicago truncatula]


70
XP_511690
55645995
PREDICTED: similar to hypothetical protein [Pan troglodytes]


71
AAW78691
58531952
peroxisomal acyl-CoA oxidase 1A [Lycopersicon cheesmaniae]


72
AAL01887
15553478
acyl-CoA oxidase [Glycine max]


73
Q9Z1N0
17367267
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


74
BAA86870
6429156
peroxisomal acyl-CoA oxidase [Mus musculus]


75
Q9R0H0
51338830
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


76
BAF18456
113594582
Os06g0103500 [Oryza sativa (japonica cultivar-group)]


77
AAI08648
83318302
Unknown (protein for MGC: 131363) [Xenopus laevis]


78
AAB62926
2253380
peroxisomal acyl-CoA oxidase [Mus musculus]


79
NP_056544
66793429
acyl-Coenzyme A oxidase 1, palmitoyl [Mus musculus]


80
XP_320717
58394415
ENSANGP00000020118 [Anopheles gambiae str. PEST]


81
AAH21339
18204156
Acox2 protein [Mus musculus]


82
BAE25794
74188249
unnamed protein product [Mus musculus]


83
Q9QXD1
17367045
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


84
XP_320718
58394417
ENSANGP00000020032 [Anopheles gambiae str. PEST]


85
EAT39640
108875415
acyl-CoA oxidase [Aedes aegypti]


86
NP_665713
21955130
acyl-Coenzyme A oxidase 2, branched chain [Rattus norvegicus]


87
XP_625136
66556360
PREDICTED: similar to CG5009-PA, partial [Apis mellifera]


88
CAE63479
39592402
Hypothetical protein CBG07946 [Caenorhabditis briggsae]


89
XP_879996
76648809
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 6 [Bos taurus]


90
BAC26167
26324826
unnamed protein product [Mus musculus]


91
XP_592892
76648807
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 1 [Bos taurus]


92
AAH47700
28839704
Acyl-Coenzyme A oxidase 2, branched chain [Homo sapiens]


93
XP_541826
73985284
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Canis familiaris]


94
XP_782824
72015136
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


95
EAR95568
89297580
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


96
CAE63477
39592400
Hypothetical protein CBG07944 [Caenorhabditis briggsae]


97
NP_510603
17568313
F59F4.1 [Caenorhabditis elegans]


98
EAT48205
108883980
acyl-CoA oxidase [Aedes aegypti]


99
XP_785210
72015040
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


100
O02767
17366131
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


101
AAW78690
58531950
peroxisomal acyl-CoA oxidase 1B [Lycopersicon esculentum]


102
CAE63480
39592403
Hypothetical protein CBG07947 [Caenorhabditis briggsae]


103
EAS31618
90301987
hypothetical protein CIMG_07097 [Coccidioides immitis RS]


104
CAE63476
39592399
Hypothetical protein CBG07943 [Caenorhabditis briggsae]


105
XP_973660
91082769
PREDICTED: similar to CG5009-PA [Tribolium castaneum]


106
CAE69737
39596101
Hypothetical protein CBG16008 [Caenorhabditis briggsae]


107
NP_611264
24654595
CG5009-PA [Drosophila melanogaster]


108
AAF73843
8163758
acyl-CoA oxidase ACX3 [Arabidopsis thaliana]


109
Q9LLH9
62286634
Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)





(Medium-chain acyl-CoA oxidase) (AtCX3)


110
EAL26359
54636956
GA18591-PA [Drosophila pseudoobscura]


111
AAH54727
68262425
Acox1 protein [Mus musculus]


112
XP_783450
72111190
PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl





[Strongylocentrotus purpuratus]


113
XP_758355
71010163
hypothetical protein UM02208.1 [Ustilago maydis 521]


114
AAL28144
16767852
GH01266p [Drosophila melanogaster]


115
NP_001 . . .
71983346
F08A8.1a [Caenorhabditis elegans]


116
EAS04704
89306716
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


117
NP_493263
17506533
F08A8.3 [Caenorhabditis elegans]


118
BAC35782
74197284
unnamed protein product [Mus musculus]


119
XP_635946
66804335
hypothetical protein DDBDRAFT_0188674 [Dictyostelium





discoideum AX4]


120
NP_493264
17506535
F08A8.4 [Caenorhabditis elegans]


121
CAJ58493
85539740
Hypothetical protein F08A8.1c [Caenorhabditis elegans]


122
NP_001 . . .
71983355
F08A8.1b [Caenorhabditis elegans]


123
EAS02716
89304728
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


124
XP_879827
76648805
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 5 [Bos taurus]


125
CAH91864
55730283
hypothetical protein [Pongo pygmaeus]


126
NP_499119
17552648
C48B4.1 [Caenorhabditis elegans]


127
ZP_012 . . .
90587482
Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-





CoA dehydrogenase, central region [Flavobacterium johnsoniae





UW101]


128
BAE55537
83765394
unnamed protein product [Aspergillus oryzae]


129
XP_637610
66807775
hypothetical protein DDBDRAFT_0187085 [Dictyostelium





discoideum AX4]


130
BAF19505
113595631
Os06g0354500 [Oryza sativa (japonica cultivar-group)]


131
EAT87650
111066530
hypothetical protein SNOG_05259 [Phaeosphaeria nodorum





SN15]


132
CAE65171
39590798
Hypothetical protein CBG10043 [Caenorhabditis briggsae]





hypothetical protein DDBDRAFT_0188084 [Dictyostelium


133
XP_636605
66805767
discoideum AX4]


134
XP_664356
67541164
hypothetical protein AN6752.2 [Aspergillus nidulans FGSC A4]


135
EAR99631
89301643
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


136
NP_493262
17506531
F08A8.2 [Caenorhabditis elegans]


137
XP_382463
46110811
hypothetical protein FG02287.1 [Gibberella zeae PH-1]


138
AAL39944
17862934
SD03592p [Drosophila melanogaster]


139
NP_523802
17647123
acyl-Coenzyme A oxidase at 57D proximal CG9707-PA





[Drosophila melanogaster]


140
XP_587157
76620513
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Bos taurus]


141
EAR98581
89300593
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


142
Q9LMI7
62286635
Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor


143
O65201
62286588
Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)





(Long-chain acyl-CoA oxidase) (AtCX2)


144
AAC13497
3044212
acyl-CoA oxidase [Arabidopsis thaliana]


145
CAH91120
55728762
hypothetical protein [Pongo pygmaeus]


146
EAR89261
89291273
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


147
XP_646395
66826081
hypothetical protein DDBDRAFT_0216722 [Dictyostelium





discoideum AX4]


148
O64894
62286587
Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)





(Long-chain acyl-CoA oxidase)


149
NP_998312
47085909
pristanoyl acyl-Coenzyme A oxidase 3 [Danio rerio]


150
O15254
17366151
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


151
AAL48010
17944231
LD22081p [Drosophila melanogaster]


152
ZP_012 . . .
89890388
acyl-CoA oxidase [Flavobacteria bacterium BBFL7]


153
XP_758113
71007469
hypothetical protein UM01966.1 [Ustilago maydis 521]


154
EAL26647
54637244
GA21980-PA [Drosophila pseudoobscura]


155
NP_109646
34328334
acyl-Coenzyme A oxidase 3, pristanoyl [Mus musculus]


156
YP_290295
72162638
hypothetical protein Tfu_2239 [Thermobifida fusca YX]


157
AAH44725
28703869
Acox3 protein [Mus musculus]


158
NP_445791
16758056
acyl-Coenzyme A oxidase 3, pristanoyl [Rattus norvegicus]


159
YP_445820
83816544
acyl-coenzyme A oxidase I, putative [Salinibacter ruber DSM





13855]


160
AAB67883
1575556
acyl-CoA oxidase homolog [Phalaenopsis sp. ‘True Lady’]


161
AAR00586
37699750
acyl-CoA oxidase [Phalaenopsis cv. ‘True Lady’]


162
XP_969513
91093755
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Tribolium castaneum]


163
XP_786025
72005645
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


164
YP_634556
108758121
putative acyl-CoA dehydrogenase [Myxococcus xanthus DK





1622]


165
EAT87454
111066334
hypothetical protein SNOG_05063 [Phaeosphaeria nodorum





SN15]


166
Q9EPL9
17366740
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


167
XP_545908
73951751
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Canis familiaris]


168
EAL26648
54637245
GA21981-PA [Drosophila pseudoobscura]


169
BAC26136
26324764
unnamed protein product [Mus musculus]


170
CAA04688
2370232
putative acyl-CoA oxidase [Hordeum vulgare subsp. vulgare]


171
BAE42553
74143079
unnamed protein product [Mus musculus]


172
YP_702012
111019040
acyl-CoA oxidase [Rhodococcus sp. RHA1]


173
XP_786081
72005647
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


174
NP_001 . . .
79332306
ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase





[Arabidopsis thaliana]


175
NP_572371
24640268
CG4586-PA [Drosophila melanogaster]


176
NP_961035
41408199
hypothetical protein MAP2101 [Mycobacterium avium subsp.





paratuberculosis K-10]


177
EAL32329
54643586
GA18278-PA [Drosophila pseudoobscura]


178
ZP_012 . . .
90205075
Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-





CoA dehydrogenase, central region [Mycobacterium vanbaalenii





PYR-1]


179
ABA94670
108864573
Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,





expressed [Oryza sativa (japonica cultivar-group)]


180
BAE60166
83770031
unnamed protein product [Aspergillus oryzae]


181
ZP_011 . . .
89339305
Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-





CoA dehydrogenase, central region [Mycobacterium flavescens





PYR-GCK]


182
NP_609027
45550141
CG9527-PA [Drosophila melanogaster]


183
EAT48670
108884445
acyl-CoA oxidase [Aedes aegypti]


184
ZP_012 . . .
92908524
Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-





CoA dehydrogenase, central region [Mycobacterium sp. JLS]


185
AAH17053
16877606
ACOX3 protein [Homo sapiens]


186
ZP_004 . . .
66967405
Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal





[Arthrobacter sp. FB24]


187
NP_508036
17560134
F25C8.1 [Caenorhabditis elegans]


188
ZP_011 . . .
88854811
acyl-CoA oxidase [marine actinobacterium PHSC20C1]


189
AAL48950
17945806
RE34879p [Drosophila melanogaster]


190
YP_640598
108800401
acyl-CoA dehydrogenase-like protein [Mycobacterium sp.





MCS]


191
NP_724181
24585195
CG17544-PC, isoform C [Drosophila melanogaster]


192
AAL14003
16186117
SD05719p [Drosophila melanogaster]


193
XP_642669
66817952
hypothetical protein DDBDRAFT_0169270 [Dictyostelium





discoideum AX4]


194
CAA96917
1945301
POX1 [Saccharomyces cerevisiae]


195
NP_500943
17540842
F58F9.7 [Caenorhabditis elegans]


196
XP_664369
67541190
hypothetical protein AN6765.2 [Aspergillus nidulans FGSC A4]
















TABLE 35







Examples of pox1a polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_504703
50554589
YlPOX1 [Yarrowia lipolytica].


2
O74934
59799072
Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)


3
O74936
59799074
Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)


4
XP_502199
50549457
YlPOX5 [Yarrowia lipolytica]


5
O74935
59799073
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)


6
XP_503632
50552444
hypothetical protein [Yarrowia lipolytica]


7
XP_504475
50554133
YlPOX4 [Yarrowia lipolytica]


8
XP_760471
71020481
hypothetical protein UM04324.1 [Ustilago maydis 521]


9
XP_571768
58269224
Acyl-coenzyme A oxidase I [Cryptococcus neoformans var.





neoformans JEC21]


10
XP_717995
68475844
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


11
P08790
17373073
Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)


12
OXCKX5
66061
acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal - yeast





(Candida tropicalis )


13
Q9Y7B1
60391213
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


14
Q6BRD5
59799027
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


15
XP_457726
50417804
hypothetical protein DEHA0C01155g [Debaryomyces hansenii





CBS767]


16
AAA34362
170912
acyl-coenzyme A oxidase II precursor


17
XP_459232
50421365
hypothetical protein DEHA0D18667g [Debaryomyces hansenii





CBS767]


18
BAA83482
5763520
acyl-CoA oxidase [Candida tropicalis]


19
BAA83483
5763522
acyl-CoA oxidase [Candida tropicalis]


20
OXCKPM
66060
acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast





(Candida maltosa )


21
AAA34361
170910
PXP-2 protein


22
XP_721610
68468582
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


23
1306283A
225549
oxidase, fatty acyl


24
P06598
17373023
Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)





(Peroxisomal fatty acyl-CoA oxidase)


25
XP_721613
68468588
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


26
Q00468
2498206
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)


27
Q6CKK7
59799028
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


28
Q6FY63
59799032
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


29
Q756A9
60391210
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


30
NP_011310
6321233
Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-





oxidation pathway; localized to the peroxisomal matrix; Pox1p





[Saccharomyces cerevisiae]


31
AAA34891
172217
acyl-coenzyme A oxidase


32
O65202
62286589
Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chain





acyl-CoA oxidase) (AtCX1)


33
1W07B
58177067
Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 1


34
H71434
7488059
probable apetala2 domain TINY - Arabidopsis thaliana


35
NP_567513
18414744
ACX1 (ACYL-COA OXIDASE 1) [Arabidopsis thaliana]


36
Q9ZQP2
62286640
Putative acyl-coenzyme A oxidase 1.2, peroxisomal


37
AAL01888
15553480
acyl-CoA oxidase [Glycine max]


38
CAA68660
2673
acyl-coenzyme A oxidase [Candida tropicalis]


39
AAL01887
15553478
acyl-CoA oxidase [Glycine max]


40
BAF18456
113594582
Os06g0103500 [Oryza sativa (japonica cultivar-group)]


41
NP_001 . . .
55741614
acyl-Coenzyme A oxidase 1, palmitoyl [Gallus gallus]


42
AAH68891
46250227
MGC83074 protein [Xenopus laevis]


43
2FONC
109157678
Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa





Oxidase From Lycopersicon Esculentum (Tomato)


44
NP_001 . . .
54400372
hypothetical protein LOC449662 [Danio rerio]


45
AAW78689
58531948
peroxisomal acyl-CoA oxidase 1A [Lycopersicon esculentum]


46
XP_001 . . .
109118312
PREDICTED: similar to acyl-Coenzyme A oxidase isoform b





[Macaca mulatta]


47
AAW78691
58531952
peroxisomal acyl-CoA oxidase 1A [Lycopersicon cheesmaniae]


48
Q5RC19
62286600
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


49
ABE83706
92875906
acyl-CoA oxidase [Medicago truncatula]


50
NP_009223
30089974
acyl-Coenzyme A oxidase isoform b [Homo sapiens]


51
Q15067
17380467
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)


52
AAA18595
495475
peroxisomal fatty acyl-coA oxidase


53
AAA19113
458119
acyl-CoA oxidase


54
NP_001 . . .
78369480
acyl-Coenzyme A oxidase 1, palmitoyl [Bos taurus]


55
AAH63727
39795632
MGC68531 protein [Xenopus laevis]


56
AAB30019
7689914
peroxisomal acyl-coenzyme A oxidase [Homo sapiens]


57
NP_001 . . .
62751552
MGC108278 protein [Xenopus tropicalis]


58
BAA86870
6429156
peroxisomal acyl-CoA oxidase [Mus musculus]


59
Q9R0H0
51338830
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


60
AAH85743
55249685
Acyl-Coenzyme A oxidase 1, palmitoyl [Rattus norvegicus]


61
AAB62926
2253380
peroxisomal acyl-CoA oxidase [Mus musculus]


62
CAH90691
55727877
hypothetical protein [Pongo pygmaeus]


63
CAJ83302
89271321
acyl-Coenzyme A oxidase 2, branched chain [Xenopus





tropicalis]


64
AAH97101
67678187
Zgc:92584 protein [Danio rerio]


65
NP_004026
30089972
acyl-Coenzyme A oxidase isoform a [Homo sapiens]


66
AAH08767
14250616
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


67
CAD97622
31873262
hypothetical protein [Homo sapiens]


68
B54942
1082171
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II -





human


69
2DDHA
93279231
Chain A, Crystal Structure Of Acyl-Coa Oxidase Complexed





With 3-Oh-Dodecanoate


70
XP_540441
73965013
PREDICTED: similar to acyl-Coenzyme A oxidase isoform a





[Canis familiaris]


71
I38095
2117541
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal - human


72
AAH10425
14714578
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


73
NP_056544
66793429
acyl-Coenzyme A oxidase 1, palmitoyl [Mus musculus]


74
AAI08648
83318302
Unknown (protein for MGC:131363) [Xenopus laevis]


75
Q9Z1N0
17367267
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


76
XP_414406
50754485
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Gallus gallus]


77
Q8HYL8
34098564
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


78
XP_511690
55645995
PREDICTED: similar to hypothetical protein [Pan troglodytes]


79
AAO15577
27462768
acyl-CoA oxidase type 2 [Phascolarctos cinereus]


80
XP_625136
66556360
PREDICTED: similar to CG5009-PA, partial [Apis mellifera]


81
XP_320717
58394415
ENSANGP00000020118 [Anopheles gambiae str. PEST]


82
EAT39640
108875415
acyl-CoA oxidase [Aedes aegypti]


83
BAC26167
26324826
unnamed protein product [Mus musculus]


84
EAS31618
90301987
hypothetical protein CIMG_07097 [Coccidioides immitis RS]


85
XP_382463
46110811
hypothetical protein FG02287.1 [Gibberella zeae PH-1]


86
XP_320718
58394417
ENSANGP00000020032 [Anopheles gambiae str. PEST]


87
CAE63479
39592402
Hypothetical protein CBG07946 [Caenorhabditis briggsae]


88
AAW78690
58531950
peroxisomal acyl-CoA oxidase 1B [Lycopersicon esculentum]


89
CAE69737
39596101
Hypothetical protein CBG16008 [Caenorhabditis briggsae]


90
AAH21339
18204156
Acox2 protein [Mus musculus]


91
BAE25794
74188249
unnamed protein product [Mus musculus]


92
EAR95568
89297580
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


93
BAE55537
83765394
unnamed protein product [Aspergillus oryzae]


94
Q9QXD1
17367045
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


95
NP_510603
17568313
F59F4.1 [Caenorhabditis elegans]


96
XP_785210
72015040
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


97
XP_973660
91082769
PREDICTED: similar to CG5009-PA [Tribolium castaneum]


98
XP_782824
72015136
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


99
AAH47700
28839704
Acyl-Coenzyme A oxidase 2, branched chain [Homo sapiens]


100
CAE63480
39592403
Hypothetical protein CBG07947 [Caenorhabditis briggsae]


101
O02767
17366131
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


102
NP_665713
21955130
acyl-Coenzyme A oxidase 2, branched chain [Rattus norvegicus]


103
XP_664356
67541164
hypothetical protein AN6752.2 [Aspergillus nidulans FGSC A4]


104
EAT48205
108883980
acyl-CoA oxidase [Aedes aegypti]


105
CAE63477
39592400
Hypothetical protein CBG07944 [Caenorhabditis briggsae]


106
XP_758355
71010163
hypothetical protein UM02208.1 [Ustilago maydis 521]


107
CAE65171
39590798
Hypothetical protein CBG10043 [Caenorhabditis briggsae]


108
XP_637610
66807775
hypothetical protein DDBDRAFT_0187085 [Dictyostelium





discoideum AX4]


109
NP_499119
17552648
C48B4.1 [Caenorhabditis elegans]


110
XP_635946
66804335
hypothetical protein DDBDRAFT_0188674 [Dictyostelium





discoideum AX4]


111
XP_592892
76648807
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 1 [Bos taurus]


112
XP_879996
76648809
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 6 [Bos taurus]


113
XP_783450
72111190
PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl





[Strongylocentrotus purpuratus]


114
XP_541826
73985284
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Canis familiaris]


115
EAR89261
89291273
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


116
AAH54727
68262425
Acox1 protein [Mus musculus]


117
BAC35782
74197284
unnamed protein product [Mus musculus]


118
NP_493263
17506533
F08A8.3 [Caenorhabditis elegans]


119
AAF14635
6503198
acyl-CoA oxidase [Petroselinum crispum]


120
CAE63476
39592399
Hypothetical protein CBG07943 [Caenorhabditis briggsae]


121
AAL39944
17862934
SD03592p [Drosophila melanogaster]


122
NP_523802
17647123
acyl-Coenzyme A oxidase at 57D proximal CG9707-PA





[Drosophila melanogaster]


123
ZP_012 . . .
90587482
Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-





CoA dehydrogenase, central region [Flavobacterium johnsoniae





UW101]


124
AAR00586
37699750
acyl-CoA oxidase [Phalaenopsis cv. ‘True Lady’]


125
XP_758113
71007469
hypothetical protein UM01966.1 [Ustilago maydis 521]


126
AAB67883
1575556
acyl-CoA oxidase homolog [Phalaenopsis sp. ‘True Lady’]


127
NP_001 . . .
71983346
F08A8.1a [Caenorhabditis elegans]


128
NP_001 . . .
71983355
F08A8.1b [Caenorhabditis elegans]


129
CAJ58493
85539740
Hypothetical protein F08A8.1c [Caenorhabditis elegans]


130
AAC13497
3044212
acyl-CoA oxidase [Arabidopsis thaliana]


131
O65201
62286588
Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)





(Long-chain acyl-CoA oxidase) (AtCX2)


132
EAS04704
89306716
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


133
EAL26359
54636956
GA18591-PA [Drosophila pseudoobscura]


134
XP_636605
66805767
hypothetical protein DDBDRAFT_0188084 [Dictyostelium





discoideum AX4]


135
O64894
62286587
Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)





(Long-chain acyl-CoA oxidase)


136
NP_611264
24654595
CG5009-PA [Drosophila melanogaster]


137
NP_493264
17506535
F08A8.4 [Caenorhabditis elegans]


138
AAH44725
28703869
Acox3 protein [Mus musculus]


139
NP_109646
34328334
acyl-Coenzyme A oxidase 3, pristanoyl [Mus musculus]


140
XP_786025
72005645
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


141
XP_646395
66826081
hypothetical protein DDBDRAFT_0216722 [Dictyostelium





discoideum AX4]


142
EAT87650
111066530
hypothetical protein SNOG_05259 [Phaeosphaeria nodorum





SN15]


143
NP_998312
47085909
pristanoyl acyl-Coenzyme A oxidase 3 [Danio rerio]


144
YP_634556
108758121
putative acyl-CoA dehydrogenase [Myxococcus xanthus DK





1622]


145
AAL28144
16767852
GH01266p [Drosophila melanogaster]


146
YP_445820
83816544
acyl-coenzyme A oxidase I, putative [Salinibacter ruber DSM





13855]


147
EAL26647
54637244
GA21980-PA [Drosophila pseudoobscura]


148
XP_786081
72005647
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


149
EAR99631
89301643
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


150
NP_493262
17506531
F08A8.2 [Caenorhabditis elegans]


151
CAH91864
55730283
hypothetical protein [Pongo pygmaeus]


152
Q9LLH9
62286634
Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)





(Medium-chain acyl-CoA oxidase) (AtCX3)


153
AAF73843
8163758
acyl-CoA oxidase ACX3 [Arabidopsis thaliana]


154
XP_969513
91093755
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Tribolium castaneum]


155
O15254
17366151
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


156
Q9EPL9
17366740
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


157
NP_445791
16758056
acyl-Coenzyme A oxidase 3, pristanoyl [Rattus norvegicus]


158
ABA94670
108864573
Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,





expressed [Oryza sativa (japonica cultivar-group)]


159
EAT87454
111066334
hypothetical protein SNOG_05063 [Phaeosphaeria nodorum





SN15]


160
EAL26648
54637245
GA21981-PA [Drosophila pseudoobscura]


161
EAR98581
89300593
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


162
BAE42553
74143079
unnamed protein product [Mus musculus]


163
BAC26136
26324764
unnamed protein product [Mus musculus]


164
XP_879827
76648805
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 5 [Bos taurus]


165
XP_587157
76620513
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Bos taurus]


166
YP_290295
72162638
hypothetical protein Tfu_2239 [Thermobifida fusca YX]


167
CAH91120
55728762
hypothetical protein [Pongo pygmaeus]


168
EAS02716
89304728
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


169
AAL48010
17944231
LD22081p [Drosophila melanogaster]


170
XP_545908
73951751
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Canis familiaris]


171
ZP_011 . . .
88854811
acyl-CoA oxidase [marine actinobacterium PHSC20C1]


172
NP_001 . . .
79332306
ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase





[Arabidopsis thaliana]


173
BAF19505
113595631
Os06g0354500 [Oryza sativa (japonica cultivar-group)]


174
EAL32329
54643586
GA18278-PA [Drosophila pseudoobscura]


175
CAA04688
2370232
putative acyl-CoA oxidase [Hordeum vulgare subsp. vulgare]


176
ZP_012 . . .
89890388
acyl-CoA oxidase [Flavobacteria bacterium BBFL7]


177
Q9LMI7
62286635
Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor


178
XP_395486
66564429
PREDICTED: similar to CG9527-PA [Apis mellifera]


179
YP_702012
111019040
acyl-CoA oxidase [Rhodococcus sp. RHA1]


180
ZP_012 . . .
90205075
Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-





CoA dehydrogenase, central region [Mycobacterium vanbaalenii





PYR-1]


181
AAL48950
17945806
RE34879p [Drosophila melanogaster]


182
NP_609027
45550141
CG9527-PA [Drosophila melanogaster]


183
ZP_006 . . .
71369913
Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal:Acyl-





CoA dehydrogenase, central region:Acyl-CoA dehydrogenase,





N-terminal [Nocardioides sp. JS614]


184
ZP_012 . . .
92908524
Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-





CoA dehydrogenase, central region [Mycobacterium sp. JLS]


185
EAT48670
108884445
acyl-CoA oxidase [Aedes aegypti]


186
XP_317446
58390030
ENSANGP00000011863 [Anopheles gambiae str. PEST]


187
EAS36523
90306892
hypothetical protein CIMG_01877 [Coccidioides immitis RS]


188
NP_572371
24640268
CG4586-PA [Drosophila melanogaster]


189
XP_642669
66817952
hypothetical protein DDBDRAFT_0169270 [Dictyostelium





discoideum AX4]


190
CAA96917
1945301
POX1 [Saccharomyces cerevisiae]


191
ZP_011 . . .
89339305
Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-





CoA dehydrogenase, central region [Mycobacterium flavescens





PYR-GCK]


192
ZP_003 . . .
62426247
COG1960: Acyl-CoA dehydrogenases [Brevibacterium linens





BL2]


193
YP_640598
108800401
acyl-CoA dehydrogenase-like protein [Mycobacterium sp.





MCS]


194
NP_724181
24585195
CG17544-PC, isoform C [Drosophila melanogaster]


195
AAL14003
16186117
SD05719p [Drosophila melanogaster]


196
AAH17053
16877606
ACOX3 protein [Homo sapiens]


197
EAL32912
54644170
GA21857-PA [Drosophila pseudoobscura]
















TABLE 36







Examples of pox4 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1 
XP_504475.1
50554133
YlPOX4 [Yarrowia lipolytica]


2
O74935
59799073
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)


3
O74936
59799074
Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)


4 
XP_502199
50549457
YlPOX5 [Yarrowia lipolytica]


5 
O74934
59799072
Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)


6 
XP_504703
50554589
YlPOX1 [Yarrowia lipolytica]


7
XP_503632
50552444
hypothetical protein [Yarrowia lipolytica]


8 
XP_760471
71020481
hypothetical protein UM04324.1 [Ustilago maydis 521]


9 
XP_571768
58269224
Acyl-coenzyme A oxidase I [Cryptococcus neoformans var.





neoformans JEC21]


10
XP_717995
68475844
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


11
BAA83482
5763520
acyl-CoA oxidase [Candida tropicalis]


12 
BAA83483
5763522
acyl-CoA oxidase [Candida tropicalis]


13 
OXCKPM
66060
acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal-yeast





(Candida maltosa)


14
XP_721610
68468582
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


15
AAA34362
170912
acyl-coenzyme A oxidase II precursor


16
P08790
17373073
Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)


17
OXCKX5
66061
acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal-yeast





(Candida tropicalis)


18 
Q6BRD5
59799027
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


19
XP_457726
50417804
hypothetical protein DEHA0C01155g [Debaryomyces hansenii





CBS767]


20
P06598
17373023
Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)





(Peroxisomal fatty acyl-CoA oxidase)


21 
1306283A
225549
oxidase, fatty acyl


22
AAA34361
170910
PXP-2 protein


23 
XP_459232
50421365
hypothetical protein DEHA0D18667g [Debaryomyces hansenii





CBS767]


24 
Q9Y7B1
60391213
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


25
XP_721613
68468588
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


26
Q00468
2498206
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)


27 
Q6FY63
59799032
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


28
NP_011310
6321233
Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-





oxidation pathway; localized to the peroxisomal matrix; Pox1p





[Saccharomyces cerevisiae]


29 
AAA34891
172217
acyl-coenzyme A oxidase


30 
Q6CKK7
59799028
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


31
Q756A9
60391210
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


32
O65202
62286589
Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chain





acyl-CoA oxidase) (AtCX1)


33
CAA68660
2673 
acyl-coenzyme A oxidase [Candida tropicalis]


34
1W07B
58177067
Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 1


35
AAL01888
15553480
acyl-CoA oxidase [Glycine max]


36 
H71434
7488059
probable apetala2 domain TINY-Arabidopsis thaliana


37 
NP_567513
18414744
ACX1 (ACYL-COA OXIDASE 1) [Arabidopsis thaliana]


38 
AAH63727
39795632
MGC68531 protein [Xenopus laevis]


39 
AAL01887
15553478
acyl-CoA oxidase [Glycine max]


40 
AAI08648
83318302
Unknown (protein for MGC: 131363) [Xenopus laevis]


41 
BAF18456
113594582
Os06g0103500 [Oryza sativa (japonica cultivar-group)]


42 
Q9ZQP2
62286640
Putative acyl-coenzyme A oxidase 1.2, peroxisomal


43 
NP_001 . . . 
78369480
acyl-Coenzyme A oxidase 1, palmitoyl [Bos taurus]


44
ABE83706
92875906
acyl-CoA oxidase [Medicago truncatula]


45 
NP_001 . . . 
62751552
MGC108278 protein [Xenopus tropicalis]


46 
NP_001 . . . 
55741614
acyl-Coenzyme A oxidase 1, palmitoyl [Gallus gallus]


47 
AAW78689
58531948
peroxisomal acyl-CoA oxidase 1A [Lycopersicon esculentum]


48 
2FONC
109157678
Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa





Oxidase From Lycopersicon Esculentum (Tomato)


49
NP_001 . . . 
54400372
hypothetical protein LOC449662 [Danio rerio]


50
AAW78691
58531952
peroxisomal acyl-CoA oxidase 1A [Lycopersicon cheesmaniae]


51
Q5RC19
62286600
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


52 
XP_001 . . . 
109118312
PREDICTED: similar to acyl-Coenzyme A oxidase isoform b





[Macaca mulatta]


53
Q15067
17380467
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)


54 
NP_009223
30089974
acyl-Coenzyme A oxidase isoform b [Homo sapiens]


55 
AAO15577
27462768
acyl-CoA oxidase type 2 [Phascolarctos cinereus]


56 
AAB30019
7689914
peroxisomal acyl-coenzyme A oxidase [Homo sapiens]


57
AAH97101
67678187
Zgc: 92584 protein [Danio rerio]


58 
XP_414406
50754485
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Gallus gallus]


59 
AAA19113
458119 
acyl-CoA oxidase


60 
AAA18595
495475 
peroxisomal fatty acyl-coA oxidase


61
Q9Z1N0
17367267
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


62
Q8HYL8
34098564
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


63 
AAH85743
55249685
Acyl-Coenzyme A oxidase 1, palmitoyl [Rattus norvegicus]


64 
AAH10425
14714578
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


65
CAH90691
55727877
hypothetical protein [Pongo pygmaeus]


66 
CAD97622
31873262
hypothetical protein [Homo sapiens]


67 
AAH08767
14250616
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


68 
NP_004026
30089972
acyl-Coenzyme A oxidase isoform a [Homo sapiens]


69
I38095
2117541
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal-human


70 
BAA86870
6429156
peroxisomal acyl-CoA oxidase [Mus musculus]


71 
CAJ83302
89271321
acyl-Coenzyme A oxidase 2, branched chain [Xenopus





tropicalis]


72
Q9R0H0
51338830
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


73 
AAB62926
2253380
peroxisomal acyl-CoA oxidase [Mus musculus]


74 
B54942
1082171
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II-





human


75 
XP_320717
58394415
ENSANGP00000020118 [Anopheles gambiae str. PEST]


76
BAE25794
74188249
unnamed protein product [Mus musculus]


77
AAH21339
18204156
Acox2 protein [Mus musculus]


78 
2DDHA
93279231
Chain A, Crystal Structure Of Acyl-Coa Oxidase Complexed





With 3-Oh- Dodecanoate


79
Q9QXD1
17367045
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


80 
AAH68891
46250227
MGC83074 protein [Xenopus laevis]


81 
XP_540441
73965013
PREDICTED: similar to acyl-Coenzyme A oxidase isoform a





[Canis familiaris]


82
XP_320718
58394417
ENSANGP00000020032 [Anopheles gambiae str. PEST]


83 
XP_511690
55645995
PREDICTED: similar to hypothetical protein [Pan troglodytes]


84
NP_056544
66793429
acyl-Coenzyme A oxidase 1, palmitoyl [Mus musculus]


85
EAT39640
108875415
acyl-CoA oxidase [Aedes aegypti]


86 
XP_783450
72111190
PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl





[Strongylocentrotus purpuratus]


87 
NP_665713
21955130
acyl-Coenzyme A oxidase 2, branched chain [Rattus norvegicus]


88
XP_973660
91082769
PREDICTED: similar to CG5009-PA [Tribolium castaneum]


89
CAE63476
39592399
Hypothetical protein CBG07943 [Caenorhabditis briggsae]


90 
XP_625136
66556360
PREDICTED: similar to CG5009-PA, partial [Apis mellifera]


91
XP_592892
76648807
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 1 [Bos taurus]


92
XP_879996
76648809
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 6 [Bos taurus]


93
AAW78690
58531950
peroxisomal acyl-CoA oxidase 1B [Lycopersicon esculentum]


94
AAH47700
28839704
Acyl-Coenzyme A oxidase 2, branched chain [Homo sapiens]


95
CAE69737
39596101
Hypothetical protein CBG16008 [Caenorhabditis briggsae]


96 
NP_499119
17552648
C48B4.1 [Caenorhabditis elegans]


97 
CAE65171
39590798
Hypothetical protein CBG10043 [Caenorhabditis briggsae]


98 
XP_541826
73985284
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Canis familiaris]


99
NP_510603
17568313
F59F4.1 [Caenorhabditis elegans]


100
NP_001 . . . 
71983346
F08A8.1a [Caenorhabditis elegans]


101 
EAR95568
89297580
Acyl-CoA oxidase family protein [Tetrahymena thermophila]





SB210]


102 
NP_001 . . . 
71983355
F08A8.1b [Caenorhabditis elegans]


103 
CAJ58493
85539740
Hypothetical protein F08A8.1c [Caenorhabditis elegans]


104
EAL26359
54636956
GA18591-PA [Drosophila pseudoobscura]


105
BAC26167
26324826
unnamed protein product [Mus musculus]


106
CAE63479
39592402
Hypothetical protein CBG07946 [Caenorhabditis briggsae]


107
O02767
17366131
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


108
NP_611264
24654595
CG5009-PA [Drosophila melanogaster]


109
CAE63480
39592403
Hypothetical protein CBG07947 [Caenorhabditis briggsae]


110
XP_758355
71010163
hypothetical protein UM02208.1 [Ustilago maydis 521]


111
EAT48205
108883980
acyl-CoA oxidase [Aedes aegypti]


112 
XP_782824
72015136
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


113 
AAL28144
16767852
GH01266p [Drosophila melanogaster]


114
XP_785210
72015040
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


115
EAS31618
90301987
hypothetical protein CIMG_07097 [Coccidioides immitis RS]


116 
XP_879827
76648805
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 5 [Bos taurus]


117
CAH91864
55730283
hypothetical protein [Pongo pygmaeus]


118 
NP_493263
17506533
F08A8.3 [Caenorhabditis elegans]


119
Q9LLH9
62286634
Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)





(Medium-chain acyl-CoA oxidase) (AtCX3)


120
AAF73843
8163758
acyl-CoA oxidase ACX3 [Arabidopsis thaliana]


121
AAL39944
17862934
SD03592p [Drosophila melanogaster]


122 
NP_523802
17647123
acyl-Coenzyme A oxidase at 57D proximal CG9707-PA





[Drosophila melanogaster]


123
AAH54727
68262425
Acox1 protein [Mus musculus]


124
BAC35782
74197284
unnamed protein product [Mus musculus]


125
BAE55537
83765394
unnamed protein product [Aspergillus oryzae]


126 
CAE63477
39592400
Hypothetical protein CBG07944 [Caenorhabditis briggsae]


127
XP_636605
66805767
hypothetical protein DDBDRAFT_0188084 [Dictyostelium





discoideum AX4]


128 
NP_493264
17506535
F08A8.4 [Caenorhabditis elegans]


129 
NP_493262
17506531
F08A8.2 [Caenorhabditis elegans]


130 
EAL26648
54637245
GA21981-PA [Drosophila pseudoobscura]


131
AAF14635
6503198
acyl-CoA oxidase [Petroselinum crispum]


132 
XP_664356
67541164
hypothetical protein AN6752.2 [Aspergillus nidulans FGSC A4]


133
EAL26647
54637244
GA21980-PA [Drosophila pseudoobscura]


134 
AAL48010
17944231
LD22081p [Drosophila melanogaster]


135 
ZP_012 . . . 
90587482
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Flavobacterium johnsoniae





UW101]


136 
CAA04688
2370232
putative acyl-CoA oxidase [Hordeum vulgare subsp. vulgare]


137
Q9LMI7
62286635
Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor


138 
EAR89261
89291273
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


139
YP_290295
72162638
hypothetical protein Tfu_2239 [Thermobifida fusca YX]


140
XP_758113
71007469
hypothetical protein UM01966.1 [Ustilago maydis 521]


141
BAF19505
113595631
Os06g0354500 [Oryza sativa (japonica cultivar-group)]


142
XP_317446
58390030
ENSANGP00000011863 [Anopheles gambiae str. PEST]


143 
XP_635946
66804335
hypothetical protein DDBDRAFT_0188674 [Dictyostelium





discoideum AX4]


144 
XP_382463
46110811
hypothetical protein FG02287.1 [Gibberella zeae PH-2]


145 
YP_445820
83816544
acyl-coenzyme A oxidase I, putative [Salinibacter ruber DSM





13855]


146 
EAR99631
89301643
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


147 
EAT87650
111066530
hypothetical protein SNOG_05259 [Phaeosphaeria nodorum





SN15]


148 
O15254
17366151
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


149
NP_508036
17560134
F25C8.1 [Caenorhabditis elegans]


150 
NP_998312
47085909
pristanoyl acyl-Coenzyme A oxidase 3 [Danio rerio]


151 
EAL32329
54643586
GA18278-PA [Drosophila pseudoobscura]


152 
EAS02716
89304728
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


153
EAT48670
108884445
acyl-CoA oxidase [Aedes aegypti]


154 
CAH91120
55728762
hypothetical protein [Pongo pygmaeus]


155 
EAS04704
89306716
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


156 
ZP_012 . . . 
89890388
acyl-CoA oxidase [Flavobacteria bacterium BBFL7]


157
O64894
62286587
Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)





(Long-chain acyl-CoA oxidase)


158
XP_969513
91093755
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Tribolium castaneum]


159
AAC13497
3044212
acyl-CoA oxidase [Arabidopsis thaliana]


160 
O65201
62286588
Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)





(Long-chain acyl-CoA oxidase) (AtCX2)


161 
XP_646395
66826081
hypothetical protein DDBDRAFT_0216722 [Dictyostelium





discoideum AX4]


162 
YP_634556
108758121
putative acyl-CoA dehydrogenase [Myxococcus xanthus DK





1622]


163 
XP_587157
76620513
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Bos taurus]


164 
EAR98581
89300593
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


165
XP_637610
66807775
hypothetical protein DDBDRAFT_0187085 [Dictyostelium





discoideum AX4]


166 
NP_572371
24640268
CG4586-PA [Drosophila melanogaster]


167
EAT87454
111066334
hypothetical protein SNOG_05063 [Phaeosphaeria nodorum





SN15]


168 
AAB67883
1575556
acyl-CoA oxidase homolog [Phalaenopsis sp. ‘True Lady’]


169
NP_961035
41408199
hypothetical protein MAP2101 [Mycobacterium avium subsp.





paratuberculosis K-10]


170 
ABA94670
108864573
Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,





expressed [Oryza sativa (japonica cultivar-group)]


171 
AAR00586
37699750
acyl-CoA oxidase [Phalaenopsis cv. ‘True Lady’]


172 
XP_545908
73951751
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Canis familiaris]


173 
YP_702012
111019040
acyl-CoA oxidase [Rhodococcus sp. RHA1]


174 
ZP_012 . . . 
90205075
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium vanbaalenii





PYR-1]


175 
EAS36523
90306892
hypothetical protein CIMG_01877 [Coccidioides immitis RS]


176
NP_001 . . . 
79332306
ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase





[Arabidopsis thaliana]


177 
CAA68661 
2674 
44 kD translation product [Candida tropicalis]


178
ZP_012 . . . 
92908524
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium sp. JLS]


179 
XP_786025
72005645
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


180
CAA96917
1945301
POX1 [Saccharomyces cerevisiae]


181
BAE60166
83770031
unnamed protein product [Aspergillus oryzae]


182
ZP_011 . . . 
89339305
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium flavescens





PYR-GCK]


183
YP_640598
108800401
acyl-CoA dehydrogenase-like protein [Mycobacterium sp.





MCS]


184 
ZP_006 . . . 
71369913
Acyl-CoA oxidase: Acyl-CoA dehydrogenase, C-terminal: Acyl-





CoA dehydrogenase, central region: Acyl-CoA dehydrogenase,





N-terminal [Nocardioides sp. JS614]


185
AAL14003
16186117
SD05719p [Drosophila melanogaster]


186 
NP_724181
24585195
CG17544-PC, isoform C [Drosophila melanogaster]


187
AAH44725
28703869
Acox3 protein [Mus musculus]


188
NP_109646
34328334
acyl-Coenzyme A oxidase 3, pristanoyl [Mus musculus]


189
EAL33335
54644594
GA14550-PA [Drosophila pseudoobscura]


190
ZP_004 . . . 
66967405
Acyl-CoA oxidase: Acyl-CoA dehydrogenase, C-terminal





[Arthrobacter sp. FB24]


191
NP_445791
16758056
acyl-Coenzyme A oxidase 3, pristanoyl [Rattus norvegicus]


192 
XP_786081
72005647
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


193 
Q9EPL9
17366740
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


194 
NP_609027
45550141
CG9527-PA [Drosophila melanogaster]


195 
ZP_006 . . . 
69287897
Acyl-CoA dehydrogenase, C-terminal: Acyl-CoA





dehydrogenase, central region [Kineococcus radiotolerans





SRS30216]


196
BAE47462
78483008
acyl-CoA oxidase [Arthrobacter ureafaciens]
















TABLE 37







Examples of pox1 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1 
XP_503632
50552444
hypothetical protein [Yarrowia lipolytica].


2 
O74935
59799073
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)


3 
O74936
59799074
Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)


4
XP_502199
50549457
YlPOX5 [Yarrowia lipolytica]


5
O74934
59799072
Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)


6 
XP_504703
50554589
YlPOX1 [Yarrowia lipolytica]


7
XP_504475
50554133
YlPOX4 [Yarrowia lipolytica]


8 
XP_760471
71020481
hypothetical protein UM04324.1 [Ustilago maydis 521]


9 
XP_571768
58269224
Acyl-coenzyme A oxidase I [Cryptococcus neoformans var.





neoformans JEC21]


10
AAA34362
170912
acyl-coenzyme A oxidase II precursor


11
BAA83482
5763520
acyl-CoA oxidase [Candida tropicalis]


12 
XP_717995
68475844
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


13
BAA83483
5763522
acyl-CoA oxidase [Candida tropicalis]


14 
XP_721610
68468582
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


15
OXCKPM
66060
acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal-yeast





(Candida maltosa)


16 
P08790
17373073
Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)


17
OXCKX5
66061
acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal-yeast





(Candida tropicalis)


18 
XP_721613
68468588
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


19 
AAA34361
170910
PXP-2 protein


20
Q6BRD5
59799027
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


21 
1306283A
225549
oxidase, fatty acyl


22 
P06598
17373023
Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)





(Peroxisomal fatty acyl-CoA oxidase)


23 
XP_459232
50421365
hypothetical protein DEHA0D18667g [Debaryomyces hansenii





CBS767]


24
Q00468
2498206
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)


25 
XP_457726
50417804
hypothetical protein DEHA0C01155g [Debaryomyces hansenii





CBS767]


26
Q9Y7B1
60391213
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


27 
Q6CKK7
59799028
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


28
NP_011310
6321233
Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-





oxidation pathway; localized to the peroxisomal matrix; Pox1p





[Saccharomyces cerevisiae]


29 
AAA34891
172217
acyl-coenzyme A oxidase


30 
Q6FY63
59799032
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


31
Q756A9
60391210
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


32 
CAA68660
2673 
acyl-coenzyme A oxidase [Candida tropicalis]


33
1W07B
58177067
Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 1


34
O65202
62286589
Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chain





acyl-CoA oxidase) (AtCX1)


35 
NP_001 . . . 
55741614
acyl-Coenzyme A oxidase 1, palmitoyl [Gallus gallus]


36
AAH85743
55249685
Acyl-Coenzyme A oxidase 1, palmitoyl [Rattus norvegicus]


37 
XP_414406
50754485
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Gallus gallus]


38 
H71434
7488059 
probable apetala2 domain TINY-Arabidopsis thaliana


39
2DDHA
93279231
Chain A, Crystal Structure Of Acyl-Coa Oxidase Complexed





With 3-Oh- Dodecanoate


40 
NP_567513
18414744
ACX1 (ACYL-COA OXIDASE 1) [Arabidopsis thaliana]


41
NP_001 . . . 
62751552
MGC108278 protein [Xenopus tropicalis]


42
AAI08648
83318302
Unknown (protein for MGC: 131363) [Xenopus laevis]


43 
AAH97101
67678187
Zgc: 92584 protein [Danio rerio]


44 
AAH63727
39795632
MGC68531 protein [Xenopus laevis]


45 
NP_001 . . . 
54400372
hypothetical protein LOC449662 [Danio rerio]


46
AAL01888
15553480
acyl-CoA oxidase [Glycine max]


47
ABE83706
92875906
acyl-CoA oxidase [Medicago truncatula]


48
AAL01887
15553478
acyl-CoA oxidase [Glycine max]


49
BAE25794
74188249
unnamed protein product [Mus musculus]


50 
NP_056544
66793429
acyl-Coenzyme A oxidase 1, palmitoyl [Mus musculus]


51 
XP_001 . . . 
109118312
PREDICTED: similar to acyl-Coenzyme A oxidase isoform b





[Macaca mulatta]


52
BAA86870
6429156
peroxisomal acyl-CoA oxidase [Mus musculus]


53
Q9R0H0
51338830
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


54 
AAB62926
2253380
peroxisomal acyl-CoA oxidase [Mus musculus]


55
AAA18595
495475
peroxisomal fatty acyl-coA oxidase


56 
Q5RC19
62286600
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


57 
2FONC
109157678
Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa





Oxidase From Lycopersicon Esculentum (Tomato)


58
AAW78689
58531948
peroxisomal acyl-CoA oxidase 1A [Lycopersicon esculentum]


59 
AAW78691
58531952
peroxisomal acyl-CoA oxidase 1A [Lycopersicon cheesmaniae]


60 
CAH90691
55727877
hypothetical protein [Pongo pygmaeus]


61
NP_009223
30089974
acyl-Coenzyme A oxidase isoform b [Homo sapiens]


62 
Q15067
17380467
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)


63
AAH21339
18204156
Acox2 protein [Mus musculus]


64
NP_004026
30089972
acyl-Coenzyme A oxidase isoform a [Homo sapiens]


65
NP_001 . . . 
78369480
acyl-Coenzyme A oxidase 1, palmitoyl [Bos taurus]


66
Q9ZQP2
62286640
Putative acyl-coenzyme A oxidase 1.2, peroxisomal


67 
AAH08767
14250616
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


68
AAH68891
46250227
MGC83074 protein [Xenopus laevis]


69 
Q8HYL8
34098564
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


70 
XP_540441
73965013
PREDICTED: similar to acyl-Coenzyme A oxidase isoform a





[Canis familiaris]


71
AAB30019
7689914
peroxisomal acyl-coenzyme A oxidase [Homo sapiens]


72 
CAD97622
31873262
hypothetical protein [Homo sapiens]


73
I38095
2117541
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal-human


74 
BAF18456
113594582
Os06g0103500 [Oryza sativa (japonica cultivar-group)]


75
AAH10425
14714578
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


76 
AAA19113
458119 
acyl-CoA oxidase


77
B54942
1082171
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II-





human


78 
Q9QXD1
17367045
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


79
Q9Z1N0
17367267
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


80
CAJ83302
89271321
acyl-Coenzyme A oxidase 2, branched chain [Xenopus





tropicalis]


81 
XP_511690
55645995
PREDICTED: similar to hypothetical protein [Pan troglodytes]


82
XP_592892
76648807
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 1 [Bos taurus]


83 
XP_879996
76648809
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 6 [Bos taurus]


84
AAO15577
27462768
acyl-CoA oxidase type 2 [Phascolarctos cinereus]


85
NP_665713
21955130
acyl-Coenzyme A oxidase 2, branched chain [Rattus norvegicus]


86
XP_320718
58394417
ENSANGP00000020032 [Anopheles gambiae str. PEST]


87 
NP_510603
17568313
F59F4.1 [Caenorhabditis elegans]


88
XP_541826
73985284
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Canis familiaris]


89 
CAE69737
39596101
Hypothetical protein CBG16008 [Caenorhabditis briggsae]


90 
CAE63479
39592402
Hypothetical protein CBG07946 [Caenorhabditis briggsae]


91
XP_782824
72015136
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


92 
AAH47700
28839704
Acyl-Coenzyme A oxidase 2, branched chain [Homo sapiens]


93 
XP_785210
72015040
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


94
EAT39640
108875415
acyl-CoA oxidase [Aedes aegypti]


95
EAS31618
90301987
hypothetical protein CIMG_07097 [Coccidioides immitis RS]


96
O02767
17366131
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


97 
NP_998312
47085909
pristanoyl acyl-Coenzyme A oxidase 3 [Danio rerio]


98 
XP_783450
72111190
PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl





[Strongylocentrotus purpuratus]


99
EAR95568
89297580
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


100 
XP_320717
58394415
ENSANGP00000020118 [Anopheles gambiae str. PEST]


101 
NP_493263
17506533
F08A8.3 [Caenorhabditis elegans]


102 
AAF73843
8163758 
acyl-CoA oxidase ACX3 [Arabidopsis thaliana]


103
BAC26167
26324826
unnamed protein product [Mus musculus]


104
Q9LLH9
62286634
Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)





(Medium-chain acyl-CoA oxidase) (AtCX3)


105
NP_493264
17506535
F08A8.4 [Caenorhabditis elegans]


106 
XP_758355
71010163
hypothetical protein UM02208.1 [Ustilago maydis 521]


107
XP_664356
67541164
hypothetical protein AN6752.2 [Aspergillus nidulans FGSC A4]


108
EAT48205
108883980
acyl-CoA oxidase [Aedes aegypti]


109
XP_879827
76648805
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 5 [Bos taurus]


110
NP_499119
17552648
C48B4.1 [Caenorhabditis elegans]


111
O15254
17366151
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


112
BAE55537
83765394
unnamed protein product [Aspergillus oryzae]


113
XP_625136
66556360
PREDICTED: similar to CG5009-PA, partial [Apis mellifera]


114 
CAE63476
39592399
Hypothetical protein CBG07943 [Caenorhabditis briggsae]


115 
NP_523802
17647123
acyl-Coenzyme A oxidase at 57D proximal CG9707-PA





[Drosophila melanogaster]


116
AAH54727
68262425
Acox1 protein [Mus musculus]


117
BAC35782
74197284
unnamed protein product [Mus musculus]


118 
AAW78690
58531950
peroxisomal acyl-CoA oxidase 1B [Lycopersicon esculentum]


119 
AAL39944
17862934
SD03592p [Drosophila melanogaster]


120 
XP_786081
72005647
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


121
ZP_012 . . . 
90587482
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Flavobacterium johnsoniae





UW102]


122
CAE63477
39592400
Hypothetical protein CBG07944 [Caenorhabditis briggsae]


123
EAR89261
89291273
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


124
CAE65171
39590798
Hypothetical protein CBG10043 [Caenorhabditis briggsae]


125
CAH91120
55728762
hypothetical protein [Pongo pygmaeus]


126
XP_587157
76620513
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Bos taurus]


127
XP_382463
46110811
hypothetical protein FG02287.1 [Gibberella zeae PH-2]


128
XP_973660
91082769
PREDICTED: similar to CG5009-PA [Tribolium castaneum]


129
CAH91864
55730283
hypothetical protein [Pongo pygmaeus]


130
NP_493262
17506531
F08A8.2 [Caenorhabditis elegans]


131
NP_001 . . . 
71983346
F08A8.1a [Caenorhabditis elegans]


132 
NP_109646
34328334
acyl-Coenzyme A oxidase 3, pristanoyl [Mus musculus]


133
AAH44725
28703869
Acox3 protein [Mus musculus]


134
XP_969513
91093755
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Tribolium castaneum]


135 
CAE63480
39592403
Hypothetical protein CBG07947 [Caenorhabditis briggsae]


136 
CAJ58493
85539740
Hypothetical protein F08A8.1c [Caenorhabditis elegans]


137
NP_001 . . . 
71983355
F08A8.1b [Caenorhabditis elegans]


138 
XP_635946
66804335
hypothetical protein DDBDRAFT_0188674 [Dictyostelium





discoideum AX4]


139
BAF19505
113595631
Os06g0354500 [Oryza sativa (japonica cultivar-group)]


140
XP_786025
72005645
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


141 
NP_611264
24654595
CG5009-PA [Drosophila melanogaster]


142
NP_445791
16758056
acyl-Coenzyme A oxidase 3, pristanoyl [Rattus norvegicus]


143
Q9EPL9
17366740
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


144 
Q9LMI7
62286635
Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor


145 
BAE42553
74143079
unnamed protein product [Mus musculus]


146 
AAL28144
16767852
GH01266p [Drosophila melanogaster]


147
EAT87650
111066530
hypothetical protein SNOG_05259 [Phaeosphaeria nodorum





SN15]


148 
BAC26136
26324764
unnamed protein product [Mus musculus]


149 
XP_545908
73951751
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Canis familiaris]


150
EAR99631
89301643
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


151 
AAC13497
3044212 
acyl-CoA oxidase [Arabidopsis thaliana]


152 
O65201
62286588
Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)





(Long-chain acyl-CoA oxidase) (AtCX2)


153 
AAF14635
6503198 
acyl-CoA oxidase [Petroselinum crispum]


154 
EAS02716
89304728
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


155 
AAR00586
37699750
acyl-CoA oxidase [Phalaenopsis cv. ‘True Lady’]


156 
EAS04704
89306716
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


157
YP_634556
108758121
putative acyl-CoA dehydrogenase [Myxococcus xanthus DK





1622]


158
O64894
62286587
Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)





(Long-chain acyl-CoA oxidase)


159 
AAB67883
1575556
acyl-CoA oxidase homolog [Phalaenopsis sp. ‘True Lady’]


160 
ZP_012 . . . 
89890388
acyl-CoA oxidase [Flavobacteria bacterium BBFL7]


161
EAL26359
54636956
GA18591-PA [Drosophila pseudoobscura]


162
EAL26647
54637244
GA21980-PA [Drosophila pseudoobscura]


163
EAR98581
89300593
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


164 
AAH17053
16877606
ACOX3 protein [Homo sapiens]


165
XP_636605
66805767
hypothetical protein DDBDRAFT_0188084 [Dictyostelium





discoideum AX4]


166 
YP_445820
83816544
acyl-coenzyme A oxidase I, putative [Salinibacter ruber DSM





13855]


167 
EAT87454
111066334
hypothetical protein SNOG_05063 [Phaeosphaeria nodorum





SN15]


168 
NP_001 . . . 
79332306
ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase





[Arabidopsis thaliana]


169
YP_290295
72162638
hypothetical protein Tfu_2239 [Thermobifida fusca YX]


170
XP_646395
66826081
hypothetical protein DDBDRAFT_0216722 [Dictyostelium





discoideum AX4]


171
XP_317513
58390136
ENSANGP00000010039 [Anopheles gambiae str. PEST]


172 
ZP_012 . . . 
90205075
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium vanbaalenii





PYR-1]


173
EAS36523
90306892
hypothetical protein CIMG_01877 [Coccidioides immitis RS]


174 
XP_758113
71007469
hypothetical protein UM01966.1 [Ustilago maydis 521]


175 
XP_395486
66564429
PREDICTED: similar to CG9527-PA [Apis mellifera]


176 
ABA94670
108864573
Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,





expressed [Oryza sativa (japonica cultivar-group)]


177 
XP_637610
66807775
hypothetical protein DDBDRAFT_0187085 [Dictyostelium





discoideum AX4]


178
ZP_003 . . . 
62426247
COG1960: Acyl-CoA dehydrogenases [Brevibacterium linens





BL2]


179
YP_702012
111019040
acyl-CoA oxidase [Rhodococcus sp. RHA1]


180
NP_500943
17540842
F58F9.7 [Caenorhabditis elegans]


181
EAT39346
108875121
acyl-CoA oxidase [Aedes aegypti]


182
CAA96917
1945301
POX1 [Saccharomyces cerevisiae]


183
NP_609027
45550141
CG9527-PA [Drosophila melanogaster]


184
CAA04688
2370232
putative acyl-CoA oxidase [Hordeum vulgare subsp. vulgare]


185
AAL48010
17944231
LD22081p [Drosophila melanogaster]


186
EAL32329
54643586
GA18278-PA [Drosophila pseudoobscura]


187
CAE61577
39584202
Hypothetical protein CBG05491 [Caenorhabditis briggsae]


188
AAL48950
17945806
RE34879p [Drosophila melanogaster]


189
NP_724181
24585195
CG17544-PC, isoform C [Drosophila melanogaster]


190
AAL14003
16186117
SD05719p [Drosophila melanogaster]


191
XP_317446
58390030
ENSANGP00000011863 [Anopheles gambiae str. PEST]


192
ZP_011 . . . 
89339305
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium flavescens





PYR-GCK]


193
ZP_004 . . . 
66967405
Acyl-CoA oxidase: Acyl-CoA dehydrogenase, C-terminal





[Arthrobacter sp. FB24]


194
ZP_011 . . . 
88803915
acyl-coenzyme A oxidase I, putative [Robiginitalea biformata





HTCC2501]


195
EAL32912
54644170
GA21857-PA [Drosophila pseudoobscura]


196
EAL26648
54637245
GA21981-PA [Drosophila pseudoobscura]


197
ZP_012 . . . 
92908524
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium sp. JLS]
















TABLE 38







Examples of pox3 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_503244
50551539
YlPOX3 [Yarrowia lipolytica]


2 
XP_502199
50549457
YlPOX5 [Yarrowia lipolytica]


3 
O74935
59799073
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)


4
O74934
59799072
Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)


5
XP_504703
50554589
YlPOX1 [Yarrowia lipolytica]


6
XP_504475
50554133
YlPOX4 [Yarrowia lipolytica]


7
XP_503632
50552444
hypothetical protein [Yarrowia lipolytica]


8
XP_571768
58269224
Acyl-coenzyme A oxidase I [Cryptococcus neoformans var.





neoformans JEC21]


9
XP_760471
71020481
hypothetical protein UM04324.1 [Ustilago maydis 521]


10
XP_717995
68475844
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


11 
Q6BRD5
59799027
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


12 
BAA83482
5763520
acyl-CoA oxidase [Candida tropicalis]


13
OXCKPM
66060
acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal-yeast





(Candida maltosa)


14
BAA83483
5763522
acyl-CoA oxidase [Candida tropicalis]


15
AAA34362
170912
acyl-coenzyme A oxidase II precursor


16
P08790
17373073
Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)


17
OXCKX5
66061
acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal-yeast





(Candida tropicalis)


18
XP_721610
68468582
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


19 
Q9Y7B1
60391213
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


20
XP_457726
50417804
hypothetical protein DEHA0C01155g [Debaryomyces hansenii





CBS767]


21
P06598
17373023
Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)





(Peroxisomal fatty acyl-CoA oxidase)


22
AAA34361
170910
PXP-2 protein


23 
1306283A
225549
oxidase, fatty acyl


24 
XP_721613
68468588
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


25
XP_459232
50421365
hypothetical protein DEHA0D18667g [Debaryomyces hansenii





CBS767]


26 
Q00468
2498206
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)


27
Q6FY63
59799032
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


28 
Q6CKK7
59799028
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


29 
Q756A9
60391210
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


30 
NP_011310
6321233
Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-





oxidation pathway; localized to the peroxisomal matrix; Pox1p





[Saccharomyces cerevisiae]


31 
AAA34891
172217
acyl-coenzyme A oxidase


32
CAA68660
2673
acyl-coenzyme A oxidase [Candida tropicalis]


33
BAF18456
113594582
Os06g0103500 [Oryza sativa (japonica cultivar-group)]


34 
O65202
62286589
Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chain





acyl-CoA oxidase) (AtCX1)


35
H71434
7488059
probable apetala2 domain TINY-Arabidopsis thaliana


36 
1W07B
58177067
Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 1


37
NP_567513
18414744
ACX1 (ACYL-COA OXIDASE 1) [Arabidopsis thaliana]


38 
AAH68891
46250227
MGC83074 protein [Xenopus laevis]


39 
AAL01888
15553480
acyl-CoA oxidase [Glycine max]


40 
ABE83706
92875906
acyl-CoA oxidase [Medicago truncatula]


41
Q9ZQP2
62286640
Putative acyl-coenzyme A oxidase 1.2, peroxisomal


42 
CAJ83302
89271321
acyl-Coenzyme A oxidase 2, branched chain [Xenopus





tropicalis]


43
BAE25794
74188249
unnamed protein product [Mus musculus]


44 
AAL01887
15553478
acyl-CoA oxidase [Glycine max]


45 
AAW78689
58531948
peroxisomal acyl-CoA oxidase 1A [Lycopersicon esculentum]


46
2FONC
109157678
Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa





Oxidase From Lycopersicon Esculentum (Tomato)


47 
AAW78691
58531952
peroxisomal acyl-CoA oxidase 1A [Lycopersicon cheesmaniae]


48 
AAH21339
18204156
Acox2 protein [Mus musculus]


49
XP_320717
58394415
ENSANGP00000020118 [Anopheles gambiae str. PEST]


50 
Q9QXD1
17367045
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


51
XP_414406
50754485
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Gallus gallus]


52 
NP_001 . . . 
54400372
hypothetical protein LOC449662 [Danio rerio]


53
AAH63727
39795632
MGC68531 protein [Xenopus laevis]


54 
EAT39640
108875415
acyl-CoA oxidase [Aedes aegypti]


55 
AAH97101
67678187
Zgc: 92584 protein [Danio rerio]


56 
NP_001 . . . 
55741614
acyl-Coenzyme A oxidase 1, palmitoyl [Gallus gallus]


57 
NP_001 . . . 
62751552
MGC108278 protein [Xenopus tropicalis]


58 
NP_665713
21955130
acyl-Coenzyme A oxidase 2, branched chain [Rattus norvegicus]


59 
XP_320718
58394417
ENSANGP00000020032 [Anopheles gambiae str. PEST]


60 
AAI08648
83318302
Unknown (protein for MGC: 131363) [Xenopus laevis]


61 
CAE63479
39592402
Hypothetical protein CBG07946 [Caenorhabditis briggsae]


62 
Q8HYL8
34098564
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


63
EAS31618
90301987
hypothetical protein CIMG_07097 [Coccidioides immitis RS]


64
CAH90691
55727877
hypothetical protein [Pongo pygmaeus]


65 
Q5RC19
62286600
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


66 
XP_001 . . . 
109118312
PREDICTED: similar to acyl-Coenzyme A oxidase isoform b





[Macaca mulatta]


67
XP_540441
73965013
PREDICTED: similar to acyl-Coenzyme A oxidase isoform a





[Canis familiaris]


68
I38095
2117541
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal-human


69 
AAH08767
14250616
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


70 
NP_004026
30089972
acyl-Coenzyme A oxidase isoform a [Homo sapiens]


71
CAD97622
31873262
hypothetical protein [Homo sapiens]


72
NP_510603
17568313
F59F4.1 [Caenorhabditis elegans]


73 
Q15067
17380467
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)


74
NP_009223
30089974
acyl-Coenzyme A oxidase isoform b [Homo sapiens]


75 
NP_001 . . . 
78369480
acyl-Coenzyme A oxidase 1, palmitoyl [Bos taurus]


76 
B54942
1082171
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II-





human


77 
AAA18595
495475
peroxisomal fatty acyl-coA oxidase


78 
AAA19113
458119
acyl-CoA oxidase


79 
AAB30019
7689914
peroxisomal acyl-coenzyme A oxidase [Homo sapiens]


80
XP_758355
71010163
hypothetical protein UM02208.1 [Ustilago maydis 521]


81 
AAH10425
14714578
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


82 
CAE65171
39590798
Hypothetical protein CBG10043 [Caenorhabditis briggsae]


83 
O02767
17366131
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


84 
AAH47700
28839704
Acyl-Coenzyme A oxidase 2, branched chain [Homo sapiens]


85 
AAO15577
27462768
acyl-CoA oxidase type 2 [Phascolarctos cinereus]


86
CAE69737
39596101
Hypothetical protein CBG16008 [Caenorhabditis briggsae]


87
2DDHA
93279231
Chain A, Crystal Structure Of Acyl-Coa Oxidase Complexed





With 3-Oh- Dodecanoate


88
NP_499119
17552648
C48B4.1 [Caenorhabditis elegans]


89
XP_625136
66556360
PREDICTED: similar to CG5009-PA, partial [Apis mellifera]


90 
XP_879996
76648809
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 6 [Bos taurus]


91
XP_592892
76648807
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 1 [Bos taurus]


92
XP_782824
72015136
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


93
Q9LLH9
62286634
Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)





(Medium-chain acyl-CoA oxidase) (AtCX3)


94
AAF73843
8163758
acyl-CoA oxidase ACX3 [Arabidopsis thaliana]


95 
AAH85743
55249685
Acyl-Coenzyme A oxidase 1, palmitoyl [Rattus norvegicus]


96 
XP_785210
72015040
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


97 
XP_511690
55645995
PREDICTED: similar to hypothetical protein [Pan troglodytes]


98 
NP_493263
17506533
F08A8.3 [Caenorhabditis elegans]


99
XP_973660
91082769
PREDICTED: similar to CG5009-PA [Tribolium castaneum]


100 
CAE63477
39592400
Hypothetical protein CBG07944 [Caenorhabditis briggsae]


101
NP_056544
66793429
acyl-Coenzyme A oxidase 1, palmitoyl [Mus musculus]


102 
Q9Z1N0
17367267
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


103 
EAT48205
108883980
acyl-CoA oxidase [Aedes aegypti]


104
BAA86870
6429156
peroxisomal acyl-CoA oxidase [Mus musculus]


105 
Q9R0H0
51338830
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


106 
EAR95568
89297580
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


107 
AAB62926
2253380
peroxisomal acyl-CoA oxidase [Mus musculus]


108 
AAW78690
58531950
peroxisomal acyl-CoA oxidase 1B [Lycopersicon esculentum]


109 
XP_635946
66804335
hypothetical protein DDBDRAFT_0188674 [Dictyostelium





discoideum AX4]


110 
NP_493264
17506535
F08A8.4 [Caenorhabditis elegans]


111
CAE63480
39592403
Hypothetical protein CBG07947 [Caenorhabditis briggsae]


112 
NP_001 . . . 
71983346
F08A8.1a [Caenorhabditis elegans]


113 
CAE63476
39592399
Hypothetical protein CBG07943 [Caenorhabditis briggsae]


114
BAC26167
26324826
unnamed protein product [Mus musculus]


115
XP_541826
73985284
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Canis familiaris]


116 
BAE55537
83765394
unnamed protein product [Aspergillus oryzae]


117 
NP_001 . . . 
71983355
F08A8.1b [Caenorhabditis elegans]


118
CAJ58493
85539740
Hypothetical protein F08A8.1c [Caenorhabditis elegans]


119 
EAS04704
89306716
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


120 
NP_493262
17506531
F08A8.2 [Caenorhabditis elegans]


121 
EAT87650
111066530
hypothetical protein SNOG_05259 [Phaeosphaeria nodorum





SN15]


122 
O64894
62286587
Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)





(Long-chain acyl-CoA oxidase)


123 
XP_664356
67541164
hypothetical protein AN6752.2 [Aspergillus nidulans FGSC A4]


124 
XP_783450
72111190
PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl





[Strongylocentrotus purpuratus]


125
BAF19505
113595631
Os06g0354500 [Oryza sativa (japonica cultivar-group)]


126
XP_382463
46110811
hypothetical protein FG02287.1 [Gibberella zeae PH-1]


127
XP_879827
76648805
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 5 [Bos taurus]


128
Q9LMI7
62286635
Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor


129 
AAR00586
37699750
acyl-CoA oxidase [Phalaenopsis cv. ‘True Lady’]


130 
CAH91864
55730283
hypothetical protein [Pongo pygmaeus]


131
NP_998312
47085909
pristanoyl acyl-Coenzyme A oxidase 3 [Danio rerio]


132
AAL39944
17862934
SD03592p [Drosophila melanogaster]


133 
NP_523802
17647123
acyl-Coenzyme A oxidase at 57D proximal CG9707-PA





[Drosophila melanogaster]


134
EAR99631
89301643
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


135
AAB67883
1575556
acyl-CoA oxidase homolog [Phalaenopsis sp. ‘True Lady’]


136
AAL48010
17944231
LD22081p [Drosophila melanogaster]


137 
EAR98581
89300593
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


138 
YP_445820
83816544
acyl-coenzyme A oxidase I, putative [Salinibacter ruber DSM





13855]


139
EAL26648
54637245
GA21981-PA [Drosophila pseudoobscura]


140
O65201
62286588
Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)





(Long-chain acyl-CoA oxidase) (AtCX2)


141 
AAC13497
3044212
acyl-CoA oxidase [Arabidopsis thaliana]


142
AAF14635
6503198
acyl-CoA oxidase [Petroselinum crispum]


143
XP_636605
66805767
hypothetical protein DDBDRAFT_0188084 [Dictyostelium





discoideum AX4]


144 
O15254
17366151
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


145
XP_758113
71007469
hypothetical protein UM01966.1 [Ustilago maydis 521]


146 
NP_611264
24654595
CG5009-PA [Drosophila melanogaster]


147 
XP_969513
91093755
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Tribolium castaneum]


148
NP_109646
34328334
acyl-Coenzyme A oxidase 3, pristanoyl [Mus musculus]


149
XP_637610
66807775
hypothetical protein DDBDRAFT_0187085 [Dictyostelium





discoideum AX4]


150
BAC35782
74197284
unnamed protein product [Mus musculus]


151 
EAL26647
54637244
GA21980-PA [Drosophila pseudoobscura]


152 
AAH44725
28703869
Acox3 protein [Mus musculus]


153
AAH54727
68262425
Acox1 protein [Mus musculus]


154 
XP_587157
76620513
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Bos taurus]


155
ZP_012 . . . 
90587482
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Flavobacterium johnsoniae





UW101]


156
CAA04688
2370232 
putative acyl-CoA oxidase [Hordeum vulgare subsp. vulgare]


157 
EAL26359
54636956
GA18591-PA [Drosophila pseudoobscura]


158 
AAL28144
16767852
GH01266p [Drosophila melanogaster]


159 
CAH91120
55728762
hypothetical protein [Pongo pygmaeus]


160 
NP_445791
16758056
acyl-Coenzyme A oxidase 3, pristanoyl [Rattus norvegicus]


161 
Q9EPL9
17366740
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


162
XP_786081
72005647
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


163 
EAR89261
89291273
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


164
ZP_012 . . . 
89890388
acyl-CoA oxidase [Flavobacteria bacterium BBFL7]


165
XP_646395
66826081
hypothetical protein DDBDRAFT_0216722 [Dictyostelium





discoideum AX4]


166 
NP_001 . . . 
79332306
ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase





[Arabidopsis thaliana]


167
BAC26136
26324764
unnamed protein product [Mus musculus]


168
BAE42553
74143079
unnamed protein product [Mus musculus]


169
EAS02716
89304728
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


170
ABA94670
108864573
Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,





expressed [Oryza sativa (japonica cultivar-group)]


171
YP_290295
72162638
hypothetical protein Tfu_2239 [Thermobifida fusca YX]


172
EAL32329
54643586
GA18278-PA [Drosophila pseudoobscura]


173
EAT87454
111066334
hypothetical protein SNOG_05063 [Phaeosphaeria nodorum





SN15]


174
YP_634556
1087581
putative acyl-CoA dehydrogenase [Myxococcus xanthus DK





211622]


175
NP_508036
17560134
F25C8.1 [Caenorhabditis elegans]


176 
NP_572371
24640268
CG4586-PA [Drosophila melanogaster]


177
ZP_012 . . . 
90205075
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium vanbaalenii





PYR-2]


178 
XP_545908
73951751
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Canis familiaris]


179 
YP_702012
111019040
acyl-CoA oxidase [Rhodococcus sp. RHA1]


180 
ZP_011 . . . 
89339305
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium flavescens





PYR-GCK]


181 
XP_786025
72005645
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


182 
BAE60166
83770031
unnamed protein product [Aspergillus oryzae]


183 
ZP_012 . . . 
92908524
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium sp. JLS]


184 
NP_961035
41408199
hypothetical protein MAP2101 [Mycobacterium avium subsp.





paratuberculosis K-10]


185 
YP_640598
108800401
acyl-CoA dehydrogenase-like protein [Mycobacterium sp.





MCS]


186 
XP_317446
58390030
ENSANGP00000011863 [Anopheles gambiae str. PEST]


187 
EAT48670
108884445
acyl-CoA oxidase [Aedes aegypti]


188 
BAE47462
78483008
acyl-CoA oxidase [Arthrobacter ureafaciens]


189 
ZP_003 . . . 
62426247
COG1960: Acyl-CoA dehydrogenases [Brevibacterium linens





BL2]


190
AAH17053
16877606
ACOX3 protein [Homo sapiens]


191 
ZP_011 . . . 
88854811
acyl-CoA oxidase [marine actinobacterium PHSC20C2]


192
ZP_006 . . . 
71369913
Acyl-CoA oxidase: Acyl-CoA dehydrogenase, C-terminal: Acyl-





CoA dehydrogenase, central region: Acyl-CoA dehydrogenase,





N-terminal [Nocardioides sp. J5614]


193
ZP_009 . . . 
84496319
hypothetical protein JNB_02330 [Janibacter sp. HTCC2649]


194
ZP_004 . . . 
66967405
Acyl-CoA oxidase: Acyl-CoA dehydrogenase, C-terminal





[Arthrobacter sp. FB24]


195 
ZP_011 . . . 
88803915
acyl-coenzyme A oxidase I, putative [Robiginitalea biformata





HTCC2501]


196
CAA68661
2674 
44 kD translation product [Candida tropicalis]
















TABLE 39







Examples of pox5 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_502199
50549457
YlPOX5 [Yarrowia lipolytica].


2
O74936
59799074
Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)


3
O74934
59799072
Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)


4 
XP_504703
50554589
YlPOX1 [Yarrowia lipolytica]


5
O74935
59799073
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)


6 
XP_504475
50554133
YlP0X4 [Yarrowia lipolytica]


7
XP_503632
50552444
hypothetical protein [Yarrowia lipolytica]


8 
XP_760471
71020481
hypothetical protein UM04324.1 [Ustilago maydis 521]


9
XP_571768
58269224
Acyl-coenzyme A oxidase I [Cryptococcus neoformans var.





neoformans JEC21]


10 
BAA83482
5763520
acyl-CoA oxidase [Candida tropicalis]


11 
BAA83483
5763522
acyl-CoA oxidase [Candida tropicalis]


12
OXCKPM
66060
acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal-yeast





(Candida maltosa)


13
P08790
17373073
Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)


14
AAA34362
170912
acyl-coenzyme A oxidase II precursor


15 
OXCKX5
66061
acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal-yeast





(Candida tropicalis)


16 
XP_717995
68475844
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


17 
Q9Y7B1
60391213
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


18 
XP_721610
68468582
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


19 
AAA34361
170910
PXP-2 protein


20
XP_721613
68468588
putative fatty-acyl coenzyme A oxidase [Candida albicans





SC5314]


21 
P06598
17373023
Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)





(Peroxisomal fatty acyl-CoA oxidase)


22
Q6BRD5
59799027
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


23
1306283A
225549
oxidase, fatty acyl


24 
XP_457726
50417804
hypothetical protein DEHA0C01155g [Debaryomyces hansenii





CBS767]


25 
XP_459232
50421365
hypothetical protein DEHA0D18667g [Debaryomyces hansenii





CBS767]


26 
Q00468
2498206
Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)


27 
Q756A9
60391210
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


28
Q6FY63
59799032
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


29 
NP_011310
6321233
Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-





oxidation pathway; localized to the peroxisomal matrix; Pox1p





[Saccharomyces cerevisiae]


30
AAA34891
172217
acyl-coenzyme A oxidase


31 
Q6CKK7
59799028
Acyl-coenzyme A oxidase (Acyl-CoA oxidase)


32 
1W07B
58177067
Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 1


33 
O65202
62286589
Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chain





acyl-CoA oxidase) (AtCX1)


34
CAA68660
2673
acyl-coenzyme A oxidase [Candida tropicalis]


35 
NP_567513
18414744
ACX1 (ACYL-COA OXIDASE 1) [Arabidopsis thaliana]


36
H71434
7488059
probable apetala2 domain TINY-Arabidopsis thaliana


37 
AAL01888
15553480
acyl-CoA oxidase [Glycine max]


38 
AAL01887
15553478
acyl-CoA oxidase [Glycine max]


39 
ABE83706
92875906
acyl-CoA oxidase [Medicago truncatula]


40 
BAF18456
113594582
Os06g0103500 [Oryza sativa (japonica cultivar-group)]


41 
2FONC
109157678
Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-Coa





Oxidase From Lycopersicon Esculentum (Tomato)


42 
AAW78689
58531948
peroxisomal acyl-CoA oxidase 1A [Lycopersicon esculentum]


43 
AAW78691
58531952
peroxisomal acyl-CoA oxidase 1A [Lycopersicon cheesmaniae]


44
Q9ZQP2
62286640
Putative acyl-coenzyme A oxidase 1.2, peroxisomal


45
NP_001 . . . 
54400372
hypothetical protein LOC449662 [Danio rerio]


46
XP_592892
76648807
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 1 [Bos taurus]


47
XP_879996
76648809
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 6 [Bos taurus]


48 
AAH68891
46250227
MGC83074 protein [Xenopus laevis]


49 
AAH97101
67678187
Zgc: 92584 protein [Danio rerio]


50 
XP_414406
50754485
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Gallus gallus]


51
NP_001 . . . 
55741614
acyl-Coenzyme A oxidase 1, palmitoyl [Gallus gallus]


52
XP_320717
58394415
ENSANGP00000020118 [Anopheles gambiae str. PEST]


53 
NP_510603
17568313
F59F4.1 [Caenorhabditis elegans]


54 
BAE25794
74188249
unnamed protein product [Mus musculus]


55 
CAE69737
39596101
Hypothetical protein CBG16008 [Caenorhabditis briggsae]


56 
AAH21339
18204156
Acox2 protein [Mus musculus]


57 
CAJ83302
89271321
acyl-Coenzyme A oxidase 2, branched chain [Xenopus





tropicalis]


58 
XP_320718
58394417
ENSANGP00000020032 [Anopheles gambiae str. PEST]


59 
Q9QXD1
17367045
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


60
AAH63727
39795632
MGC68531 protein [Xenopus laevis]


61 
Q5RC19
62286600
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


62
AAW78690
58531950
peroxisomal acyl-CoA oxidase 1B [Lycopersicon esculentum]


63 
XP_782824
72015136
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


64 
AAH47700
28839704
Acyl-Coenzyme A oxidase 2, branched chain [Homo sapiens]


65
EAT39640
108875415
acyl-CoA oxidase [Aedes aegypti]


66
NP_001 . . . 
62751552
MGC108278 protein [Xenopus tropicalis]


67
CAH90691
55727877
hypothetical protein [Pongo pygmaeus]


68
XP_001 . . . 
109118312
PREDICTED: similar to acyl-Coenzyme A oxidase isoform b





[Macaca mulatta]


69
Q15067
17380467
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)


70 
NP_009223
30089974
acyl-Coenzyme A oxidase isoform b [Homo sapiens]


71
AAA19113
458119
acyl-CoA oxidase


72 
AAB30019
7689914
peroxisomal acyl-coenzyme A oxidase [Homo sapiens]


73
XP_785210
72015040
PREDICTED: similar to Acyl-coenzyme A oxidase 1,





peroxisomal (Palmitoyl-CoA oxidase) (AOX)





[Strongylocentrotus purpuratus]


74
O02767
17366131
Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-





alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-





alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA





oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)





(THCA-CoA oxidase)


75 
NP_004026
30089972
acyl-Coenzyme A oxidase isoform a [Homo sapiens]


76 
AAA18595
495475
peroxisomal fatty acyl-coA oxidase


77 
I38095
2117541
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal-human


78 
AAH08767
14250616
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


79 
B54942
1082171
acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II-





human


80
NP_001 . . . 
78369480
acyl-Coenzyme A oxidase 1, palmitoyl [Bos taurus]


81
NP_499119
17552648
C48B4.1 [Caenorhabditis elegans]


82 
NP_665713
21955130
acyl-Coenzyme A oxidase 2, branched chain [Rattus norvegicus]


83 
CAD97622
31873262
hypothetical protein [Homo sapiens]


84
BAA86870
6429156
peroxisomal acyl-CoA oxidase [Mus musculus]


85 
NP_056544
66793429
acyl-Coenzyme A oxidase 1, palmitoyl [Mus musculus]


86
AAH85743
55249685
Acyl-Coenzyme A oxidase 1, palmitoyl [Rattus norvegicus]


87 
2DDHA
93279231
Chain A, Crystal Structure Of Acyl-Coa Oxidase Complexed





With 3-Oh- Dodecanoate


88
Q9R0H0
51338830
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


89
XP_758355
71010163
hypothetical protein UM02208.1 [Ustilago maydis 521]


90
AAH10425
14714578
Acyl-Coenzyme A oxidase 1, palmitoyl [Homo sapiens]


91
AAB62926
2253380
peroxisomal acyl-CoA oxidase [Mus musculus]


92
CAE65171
39590798
Hypothetical protein CBG10043 [Caenorhabditis briggsae]


93
XP_625136
66556360
PREDICTED: similar to CG5009-PA, partial [Apis mellifera]


94
XP_540441
73965013
PREDICTED: similar to acyl-Coenzyme A oxidase isoform a





[Canis familiaris]


95
Q8HYL8
34098564
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


96
CAE63476
39592399
Hypothetical protein CBG07943 [Caenorhabditis briggsae]


97
AAI08648
83318302
Unknown (protein for MGC: 131363) [Xenopus laevis]


98 
XP_879827
76648805
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) isoform 5 [Bos taurus]


99 
AAF73843
8163758
acyl-CoA oxidase ACX3 [Arabidopsis thaliana]


100
Q9LLH9
62286634
Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)





(Medium-chain acyl-CoA oxidase) (AtCX3)


101
XP_973660
91082769
PREDICTED: similar to CG5009-PA [Tribolium castaneum]


102
EAS31618
90301987
hypothetical protein C1MG_07097 [Coccidioides immitis RS]


103
EAR95568
89297580
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


104
Q9Z1N0
17367267
Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoA





oxidase) (AOX)


105
AAO15577
27462768
acyl-CoA oxidase type 2 [Phascolarctos cinereus]


106
XP_541826
73985284
PREDICTED: similar to Acyl-coenzyme A oxidase 2,





peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)





(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-





CoA oxidase) [Canis familiaris]


107
CAE63479
39592402
Hypothetical protein CBG07946 [Caenorhabditis briggsae]


108
XP_511690
55645995
PREDICTED: similar to hypothetical protein [Pan troglodytes]


109
BAC26167
26324826
unnamed protein product [Mus musculus]


110
CAE63477
39592400
Hypothetical protein CBG07944 [Caenorhabditis briggsae]


111
NP_493264
17506535
F08A8.4 [Caenorhabditis elegans]


112
Q9LMI7
62286635
Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor


113
CAJ58493
85539740
Hypothetical protein F08A8.1c [Caenorhabditis elegans]


114
NP_001 . . . 
71983355
F08A8.1b [Caenorhabditis elegans]


115
NP_001 . . . 
71983346
F08A8.1a [Caenorhabditis elegans]


116
BAF19505
113595631
Os06g0354500 [Oryza sativa (japonica cultivar-group)]


117
NP_493263
17506533
F08A8.3 [Caenorhabditis elegans]


118
O64894
62286587
Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)





(Long-chain acyl-CoA oxidase)


119
NP_493262
17506531
F08A8.2 [Caenorhabditis elegans]


120
CAE63480
39592403
Hypothetical protein CBG07947 [Caenorhabditis briggsae]


121
AAF14635
6503198
acyl-CoA oxidase [Petroselinum crispum]


122
BAE55537
83765394
unnamed protein product [Aspergillus oryzae]


123
NP_998312
47085909
pristanoyl acyl-Coenzyme A oxidase 3 [Danio rerio]


124
O65201
62286588
Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)





(Long-chain acyl-CoA oxidase) (AtCX2)


125
AAC13497
3044212
acyl-CoA oxidase [Arabidopsis thaliana]


126
EAT87650
111066530
hypothetical protein SNOG_05259 [Phaeosphaeria nodorum





SN15]


127
XP_587157
76620513
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Bos taurus]


128
EAT48205
108883980
acyl-CoA oxidase [Aedes aegypti]


129
EAT87454
111066334
hypothetical protein SNOG_05063 [Phaeosphaeria nodorum





SN15]


130
XP_664356
67541164
hypothetical protein AN6752.2 [Aspergillus nidulans FGSC A4]


131
AAB67883
1575556
acyl-CoA oxidase homolog [Phalaenopsis sp. ‘True Lady’]


132
AAR00586
37699750
acyl-CoA oxidase [Phalaenopsis cv. ‘True Lady’]


133
CAH91864
55730283
hypothetical protein [Pongo pygmaeus]


134
XP_636605
66805767
hypothetical protein DDBDRAFT_0188084 [Dictyostelium





discoideum AX4]


135
NP_611264
24654595
CG5009-PA [Drosophila melanogaster]


136
EAS04704
89306716
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


137
XP_635946
66804335
hypothetical protein DDBDRAFT_0188674 [Dictyostelium





discoideum AX4]


138
O15254
17366151
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


139
AAL39944
17862934
SD03592p [Drosophila melanogaster]


140
NP_523802
17647123
acyl-Coenzyme A oxidase at 57D proximal CG9707-PA





[Drosophila melanogaster]


141
AAL28144
16767852
GH01266p [Drosophila melanogaster]


142
XP_382463
46110811
hypothetical protein FG02287.1 [Gibberella zeae PH-2]


143
EAL26359
54636956
GA18591-PA [Drosophila pseudoobscura]


144
CAA04688
2370232
putative acyl-CoA oxidase [Hordeum vulgare subsp. vulgare]


145
XP_783450
72111190
PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl





[Strongylocentrotus purpuratus]


146 
AAL48010
17944231
LD22081p [Drosophila melanogaster]


147 
CAH91120
55728762
hypothetical protein [Pongo pygmaeus]


148
XP_646395
66826081
hypothetical protein DDBDRAFT_0216722 [Dictyostelium





discoideum AX4]


149 
XP_758113
71007469
hypothetical protein UM01966.1 [Ustilago maydis 521]


150
EAR99631
89301643
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


151 
EAR89261
89291273
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


152
XP_637610
66807775
hypothetical protein DDBDRAFT_0187085 [Dictyostelium





discoideum AX4]


153
ABA94670
108864573
Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,





expressed [Oryza sativa (japonica cultivar-group)]


154
EAL26647
54637244
GA21980-PA [Drosophila pseudoobscura]


155 
ZP_012 . . . 
90587482
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Flavobacterium johnsoniae





UW102]


156 
BAC35782
74197284
unnamed protein product [Mus musculus]


157
EAS02716
89304728
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


158
YP_634556
1087581
putative acyl-CoA dehydrogenase [Myxococcus xanthus DK





211622]


159 
AAH54727
68262425
Acox1 protein [Mus musculus]


160 
YP_445820
83816544
acyl-coenzyme A oxidase I, putative [Salinibacter ruber DSM





13855]


161 
AAH44725
28703869
Acox3 protein [Mus musculus]


162
NP_109646
34328334
acyl-Coenzyme A oxidase 3, pristanoyl [Mus musculus]


163 
XP_545908
73951751
PREDICTED: similar to Acyl-coenzyme A oxidase 3,





peroxisomal (Pristanoyl-CoA oxidase) [Canis familiaris]


164
NP_001 . . . 
79332306
ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase





[Arabidopsis thaliana]


165
EAR98581
89300593
Acyl-CoA oxidase family protein [Tetrahymena thermophila





SB210]


166
XP_969513
91093755
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Tribolium castaneum]


167 
ZP_012 . . . 
89890388
acyl-CoA oxidase [Flavobacteria bacterium BBFL7]


168
YP_290295
72162638
hypothetical protein Tfu_2239 [Thermobifida fusca YX]


169 
BAC26136
26324764
unnamed protein product [Mus musculus]


170
BAE42553
74143079
unnamed protein product [Mus musculus]


171 
EAL26648
54637245
GA21981-PA [Drosophila pseudoobscura]


172 
NP_445791
16758056
acyl-Coenzyme A oxidase 3, pristanoyl [Rattus norvegicus]


173
Q9EPL9
17366740
Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoA





oxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)


174
XP_786025
72005645
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


175
XP_786081
72005647
PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3





[Strongylocentrotus purpuratus]


176
EAL32329
54643586
GA18278-PA [Drosophila pseudoobscura]


177
NP_724181
24585195
CG17544-PC, isoform C [Drosophila melanogaster]


178 
AAL14003
16186117
SD05719p [Drosophila melanogaster]


179
CAA68661
2674
44 kD translation product [Candida tropicalis]


180
NP_572371
24640268
CG4586-PA [Drosophila melanogaster]


181
ZP_011 . . . 
88854811
acyl-CoA oxidase [marine actinobacterium PHSC20C1]


182
EAL33335
54644594
GA14550-PA [Drosophila pseudoobscura]


183
EAS36523
90306892
hypothetical protein CIMG_01877 [Coccidioides immitis RS]


184
EAT48670
108884445
acyl-CoA oxidase [Aedes aegypti]


185
YP_702012
111019040
acyl-CoA oxidase [Rhodococcus sp. RHA1]


186
ZP_003 . . . 
62426247
COG1960: Acyl-CoA dehydrogenases [Brevibacterium linens





BL2]


187
XP_317446
58390030
ENSANGP00000011863 [Anopheles gambiae str. PEST]


188
XP_317513
58390136
ENSANGP00000010039 [Anopheles gambiae str. PEST]


189
AAH17053
16877606
ACOX3 protein [Homo sapiens]


190
ZP_012 . . . 
90205075
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium vanbaalenii





PYR-1]


191
ZP_011 . . . 
88803915
acyl-coenzyme A oxidase I, putative [Robiginitalea biformata





HTCC2502]


192
XP_642669
66817952
hypothetical protein DDBDRAFT_0169270 [Dictyostelium





discoideum AX4]


193
NP_508036
17560134
F25C8.1 [Caenorhabditis elegans]


194
ZP_006 . . . 
71369913
Acyl-CoA oxidase: Acyl-CoA dehydrogenase, C-terminal: Acyl-





CoA dehydrogenase, central region: Acyl-CoA dehydrogenase,





N-terminal [Nocardioides sp. JS614]


195
BAE65934
83775815
unnamed protein product [Aspergillus oryzae]


196
ZP_012 . . . 
92908524
Acyl-CoA oxidase-like: Acyl-CoA dehydrogenase-like: Acyl-





CoA dehydrogenase, central region [Mycobacterium sp. JLS]
















TABLE 40







Examples of triglyceride lipase (tgl4) polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_505230
50555644
hypothetical protein [Yarrowia lipolytica].


2
XP_459553
50421985
hypothetical protein DEHA0E06127g [Debaryomyces hansenii





CBS767]


3
XP_387731
46126355
hypothetical protein FG07555.1 [Gibberella zeae PH-1]


4
XP_717704
68476486
putative patatin-like phospholipase [Candida albicans SC5314]


5
XP_958750
85091127
hypothetical protein [Neurospora crassa OR74A]


6
NP_013015
6322942
Triacylglycerol lipase involved in triacylglycerol mobilization





and degradation; found in lipid particles; potential Cdc28p





substrate; Tgl4p [Saccharomyces cerevisiae]


7
XP_659317
67522513
hypothetical protein AN1713.2 [Aspergillus nidulans FGSC A4]


8
NP_984327
45188104
ADR231Cp [Eremothecium gossypii]


9
CAD60564
27764284
unnamed protein product [Podospora anserina]


10
EAT92134
111071014
hypothetical protein SNOG_00639 [Phaeosphaeria nodorum





SN15]


11
BAE59228
83769091
unnamed protein product [Aspergillus oryzae]


12
XP_446465
50288073
unnamed protein product [Candida glabrata]


13
XP_751982
70994310
patatin-like serine hydrolase [Aspergillus fumigatus Af293]


14
XP_451336
50302799
unnamed protein product [Kluyveromyces lactis]


15
EAS30095
90300464
hypothetical protein CIMG_08841 [Coccidioides immitis RS]


16
EAQ83092
88175624
hypothetical protein CHGG_10910 [Chaetomium globosum





CBS 148.51]


17
NP_014724
6324655
Triacylglycerol lipase involved in TAG mobilization; localizes





to lipid particles; potential Cdc28p substrate; Tgl5p





[Saccharomyces cerevisiae]


18
XP_448470
50292075
unnamed protein product [Candida glabrata]


19
ABG79933
110628937
triacylglycerol lipase [Magnaporthe grisea]


20
NP_593197
19114109
hypothetical protein SPAC1A6.05c [Schizosaccharomyces





pombe 972h-]


21
EAR86065
89288077
Patatin-like phospholipase family protein [Tetrahymena





thermophila SB210]


22
XP_463448
50902030
P0512C01.22 [Oryza sativa (japonica cultivar-group)]


23
BAF06239
113533856
Os01g0762000 [Oryza sativa (japonica cultivar-group)]


24
YP_433865
83645430
predicted esterase of the alpha-beta hydrolase superfamily





[Hahella chejuensis KCTC 2396]


25
ZP_008 . . .
77951643
conserved hypothetical protein [Marinobacter aquaeolei VT8]


26
AAM97135
22531263
putative protein [Arabidopsis thaliana]


27
BAF13581
113550138
Os03g0810900 [Oryza sativa (japonica cultivar-group)]


28
ABE78088
92867978
phospholipase, patatin family, putative [Medicago truncatula]


29
YP_693301
110834442
hypothetical protein ABO_1581 [Alcanivorax borkumensis





SK2]


30
NP_974449
42572707
unknown protein [Arabidopsis thaliana]


31
BAE56507
83766364
unnamed protein product [Aspergillus oryzae]


32
EAR83738
89285729
Patatin-like phospholipase family protein [Tetrahymena





thermophila SB210]


33
ABE94194
92898449
Patatin [Medicago truncatula]


34
XP_752278
70995024
patatin-like serine hydrolase [Aspergillus fumigatus Af293]


35
YP_046026
50084516
hypothetical protein ACIAD1335 [Acinetobacter sp. ADP1]


36
ZP_011 . . .
88794068
predicted esterase of the alpha-beta hydrolase superfamily





protein [Alteromonas macleodii ‘Deep ecotype’]


37
XP_380696
46107274
hypothetical protein FG00520.1 [Gibberella zeae PH-1]


38
ZP_011 . . .
88703608
Patatin-like phospholipase [gamma proteobacterium KT 71]


39
EAT85718
111064598
hypothetical protein SNOG_07067 [Phaeosphaeria nodorum





SN15]


40
ZP_011 . . .
88707125
Patatin-like phospholipase [gamma proteobacterium KT 71]


41
XP_757164
71004996
hypothetical protein UM01017.1 [Ustilago maydis 521]


42
YP_615253
103485692
Patatin [Sphingopyxis alaskensis RB2256]


43
XP_964502
85113293
hypothetical protein [Neurospora crassa OR74A]


44
NP_594022
63054585
hypothetical protein SPAC31G5.20c [Schizosaccharomyces





pombe 972h-]


45
XP_502898
50550851
hypothetical protein [Yarrowia lipolytica]


46
XP_722550
68466709
putative patatin-like phospholipase [Candida albicans SC5314]


47
EAS31687
90302056
hypothetical protein CIMG_07166 [Coccidioides immitis RS]


48
BAE57969
83767830
unnamed protein product [Aspergillus oryzae]


49
XP_722412
68466994
putative patatin-like phospholipase [Candida albicans SC5314]


50
EAQ93362
88185894
hypothetical protein CHGG_01597 [Chaetomium globosum





CBS 148.51]


51
ZP_010 . . .
85708568
hypothetical protein NAP1_04995 [Erythrobacter sp. NAP1]


52
XP_457141
50412575
hypothetical protein DEHA0B04048g [Debaryomyces hansenii





CBS767]


53
XP_658012
67516253
hypothetical protein AN0408.2 [Aspergillus nidulans FGSC A4]


54
EAS33873
90304242
hypothetical protein CIMG_04897 [Coccidioides immitis RS]


55
XP_805126
71404931
hypothetical protein [Trypanosoma cruzi strain CL Brener]


56
CAB88226
7630152
conserved hypothetical protein L5213T.05 [Leishmania major]


57
CAJ06433
68127889
hypothetical protein, conserved [Leishmania major]


58
XP_750246
70990794
patatin-like serine hydrolase [Aspergillus fumigatus Af293]


59
ABG79934
110628939
triacylglycerol lipase [Magnaporthe grisea]


60
XP_386821
46124535
hypothetical protein FG06645.1 [Gibberella zeae PH-1]


61
EAT92413
111071293
hypothetical protein SNOG_00918 [Phaeosphaeria nodorum





SN15]


62
NP_588315
19075815
hypothetical protein SPCC1450.16c [Schizosaccharomyces





pombe 972h-]


63
EAQ90965
88183497
hypothetical protein CHGG_02900 [Chaetomium globosum





CBS 148.51]


64
XP_957267
85084210
hypothetical protein [Neurospora crassa OR74A]


65
XP_451445
50303015
unnamed protein product [Kluyveromyces lactis]


66
CAB11704
2388971
SPAC31G5.20c [Schizosaccharomyces pombe]


67
XP_626587
66358818
hypothetical protein cgd2_4050 [Cryptosporidium parvum Iowa





II]


68
XP_665308
67588018
hypothetical protein Chro.20432 [Cryptosporidium hominis





TU502]


69
XP_449952
50295082
hypothetical protein CAGL0M13981g [Candida glabrata





CBS138]


70
XP_722764
68466564
putative lipid particle triacylglycerol lipase fragment [Candida





albicans SC5314]


71
NP_986330
45200760
AGL337Cp [Eremothecium gossypii]


72
CAE84405
39722369
Tgl3 protein [Kluyveromyces delphensis]


73
XP_807283
71409928
hypothetical protein [Trypanosoma cruzi strain CL Brener]


74
XP_807016
71409330
hypothetical protein [Trypanosoma cruzi strain CL Brener]


75
XP_502944
50550941
hypothetical protein [Yarrowia lipolytica]


76
NP_014044
6323973
Triacylglycerol lipase of the lipid particle, responsible for all the





TAG lipase activity of the lipid particle; contains the consensus





sequence motif GXSXG, which is found in lipolytic enzymes;





Tgl3p [Saccharomyces cerevisiae]
















TABLE 41







Examples of triglyceride lipase (tgl3) polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_502944
50550941
hypothetical protein [Yarrowia lipolytica].


2
XP_752278
70995024
patatin-like serine hydrolase [Aspergillus fumigatus Af293]


3
BAE56507
83766364
unnamed protein product [Aspergillus oryzae]


4
EAT85718
111064598
hypothetical protein SNOG_07067 [Phaeosphaeria nodorum





SN15]


5
XP_380696
46107274
hypothetical protein FG00520.1 [Gibberella zeae PH-1]


6
XP_964502
85113293
hypothetical protein [Neurospora crassa OR74A]


7
EAQ93362
88185894
hypothetical protein CHGG_01597 [Chaetomium globosum





CBS 148.51]


8
XP_722764
68466564
putative lipid particle triacylglycerol lipase fragment [Candida





albicans SC5314]


9
NP_986330
45200760
AGL337Cp [Eremothecium gossypii]


10
CAE84405
39722369
Tgl3 protein [Kluyveromyces delphensis]


11
XP_449952
50295082
hypothetical protein CAGL0M13981g [Candida glabrata





CBS138]


12
XP_451445
50303015
unnamed protein product [Kluyveromyces lactis]


13
NP_014044
6323973
Triacylglycerol lipase of the lipid particle, responsible for all the





TAG lipase activity of the lipid particle; contains the consensus





sequence motif GXSXG, which is found in lipolytic enzymes;





Tgl3p [Saccharomyces cerevisiae]


14
EAS31687
90302056
hypothetical protein CIMG_07166 [Coccidioides immitis RS]


15
EAT92134
111071014
hypothetical protein SNOG_00639 [Phaeosphaeria nodorum





SN15]


16
XP_387731
46126355
hypothetical protein FG07555.1 [Gibberella zeae PH-1]


17
NP_588315
19075815
hypothetical protein SPCC1450.16c [Schizosaccharomyces





pombe 972h-]


18
XP_751982
70994310
patatin-like serine hydrolase [Aspergillus fumigatus Af293]


19
XP_958750
85091127
hypothetical protein [Neurospora crassa OR74A]


20
EAQ83092
88175624
hypothetical protein CHGG_10910 [Chaetomium globosum





CBS 148.51]


21
BAE59228
83769091
unnamed protein product [Aspergillus oryzae]


22
YP_693301
110834442
hypothetical protein ABO_1581 [Alcanivorax borkumensis





SK2]


23
XP_659317
67522513
hypothetical protein AN1713.2 [Aspergillus nidulans FGSC A4]


24
ZP_011 . . .
88703608
Patatin-like phospholipase [gamma proteobacterium KT 71]


25
BAF06239
113533856
Os01g0762000 [Oryza sativa (japonica cultivar-group)]


26
XP_463448
50902030
P0512C01.22 [Oryza sativa (japonica cultivar-group)]


27
EAS30095
90300464
hypothetical protein CIMG_08841 [Coccidioides immitis RS]


28
YP_433865
83645430
predicted esterase of the alpha-beta hydrolase superfamily





[Hahella chejuensis KCTC 2396]


29
XP_459553
50421985
hypothetical protein DEHA0E06127g [Debaryomyces hansenii





CBS767]


30
CAD60564
27764284
unnamed protein product [Podospora anserina]


31
ZP_008 . . .
77951643
conserved hypothetical protein [Marinobacter aquaeolei VT8]


32
XP_505230
50555644
hypothetical protein [Yarrowia lipolytica]


33
XP_446465
50288073
unnamed protein product [Candida glabrata]


34
AAM97135
22531263
putative protein [Arabidopsis thaliana]


35
BAF13581
113550138
Os03g0810900 [Oryza sativa (japonica cultivar-group)]


36
ABG79933
110628937
triacylglycerol lipase [Magnaporthe grisea]


37
XP_717704
68476486
putative patatin-like phospholipase [Candida albicans SC5314]


38
NP_013015
6322942
Triacylglycerol lipase involved in triacylglycerol mobilization





and degradation; found in lipid particles; potential Cdc28p





substrate; Tgl4p [Saccharomyces cerevisiae]


39
NP_594022
63054585
hypothetical protein SPAC31G5.20c [Schizosaccharomyces





pombe 972h-]


40
EAR83738
89285729
Patatin-like phospholipase family protein [Tetrahymena





thermophila SB210]


41
NP_984327
45188104
ADR231Cp [Eremothecium gossypii]


42
EAR86065
89288077
Patatin-like phospholipase family protein [Tetrahymena





thermophila SB210]


43
NP_014724
6324655
Triacylglycerol lipase involved in TAG mobilization; localizes





to lipid particles; potential Cdc28p substrate; Tgl5p





[Saccharomyces cerevisiae]


44
YP_046026
50084516
hypothetical protein ACIAD1335 [Acinetobacter sp. ADP1]


45
XP_451336
50302799
unnamed protein product [Kluyveromyces lactis]


46
ZP_011 . . .
88794068
predicted esterase of the alpha-beta hydrolase superfamily





protein [Alteromonas macleodii ‘Deep ecotype’]


47
XP_722550
68466709
putative patatin-like phospholipase [Candida albicans SC5314]


48
XP_722412
68466994
putative patatin-like phospholipase [Candida albicans SC5314]


49
EAS33873
90304242
hypothetical protein CIMG_04897 [Coccidioides immitis RS]


50
ABG79934
110628939
triacylglycerol lipase [Magnaporthe grisea]


51
ZP_011 . . .
88707125
Patatin-like phospholipase [gamma proteobacterium KT 71]


52
NP_593197
19114109
hypothetical protein SPAC1A6.05c [Schizosaccharomyces





pombe 972h-]


53
YP_615253
103485692
Patatin [Sphingopyxis alaskensis RB2256]


54
ZP_010 . . .
85708568
hypothetical protein NAP1_04995 [Erythrobacter sp. NAP1]


55
XP_658012
67516253
hypothetical protein AN0408.2 [Aspergillus nidulans FGSC A4]


56
XP_448470
50292075
unnamed protein product [Candida glabrata]


57
XP_807283
71409928
hypothetical protein [Trypanosoma cruzi strain CL Brener]


58
XP_386821
46124535
hypothetical protein FG06645.1 [Gibberella zeae PH-1]
















TABLE 42







Examples of acyl-coA-cholesterol polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_505086.1
50555355
hypothetical protein [Yarrowia lipolytica].


2
XP_449806
50294790
hypothetical protein CAGL0M10571g [Candida glabrata





CBS138]


3
AAO32554
28564940
ARE2 [Saccharomyces kluyveri]


4
XP_461395
50425599
hypothetical protein DEHA0F25652g [Debaryomyces hansenii





CBS767]


5
P84285
56404462
Sterol O-acyltransferase 2 (Sterol-ester synthase) (ASAT)


6
XP_714776
68482533
acyl-CoA cholesterol acyltransferase [Candida albicans





SC5314]


7
AAO32474
28564191
ARE2 [Saccharomyces castellii]


8
NP_982606
45184888
AAR065Cp [Eremothecium gossypii]


9
NP_014416
6324346
Acyl-CoA:sterol acyltransferase, isozyme of Are1p;





endoplasmic reticulum enzyme that contributes the major sterol





esterification activity in the presence of oxygen; Are2p





[Saccharomyces cerevisiae]


10
AAC49441
1389739
acyl-CoA:sterol acyltransferase


11
XP_452607
50305295
unnamed protein product [Kluyveromyces lactis]


12
Q876L2
34582301
Sterol O-acyltransferase 2 (Sterol-ester synthase 2)


13
Q876L3
34582302
Sterol O-acyltransferase 1 (Sterol-ester synthase 1)


14
AAT92940
51013293
YCR048W [Saccharomyces cerevisiae]


15
XP_445307
50285757
unnamed protein product [Candida glabrata]


16
NP_593707
19114619
hypothetical protein SPAC13G7.05 [Schizosaccharomyces





pombe 972h-]


17
XP_370268
39977761
hypothetical protein MG06765.4 [Magnaporthe grisea 70-15]


18
EAQ84619
88177151
hypothetical protein CHGG_08633 [Chaetomium globosum





CBS 148.51]


19
XP_961300
85102248
related to acyl-CoA sterol acyltransferase [MIPS] [Neurospora





crassa OR74A]


20
XP_750354
70991010
sterol o-acyltransferase APE2 [Aspergillus fumigatus Af293]


21
EAT80792
111059672
hypothetical protein SNOG_11748 [Phaeosphaeria nodorum





SN15]


22
XP_661812
67527926
hypothetical protein AN4208.2 [Aspergillus nidulans FGSC A4]


23
BAE54934
83764790
unnamed protein product [Aspergillus oryzae]


24
EAT89521
111068401
predicted protein [Phaeosphaeria nodorum SN15]


25
EAQ86094
88178626
hypothetical protein CHGG_07347 [Chaetomium globosum





CBS 148.51]


26
NP_588558
19076058
hypothetical protein SPCP1E11.05c [Schizosaccharomyces





pombe 972h-]


27
XP_956576
85080625
hypothetical protein [Neurospora crassa OR74A]


28
EAS32815
90303184
hypothetical protein CIMG_03839 [Coccidioides immitis RS]


29
XP_382192
46110268
hypothetical protein FG02016.1 [Gibberella zeae PH-1]


30
XP_761502
71022545
hypothetical protein UM05355.1 [Ustilago maydis 521]


31
EAL20032
50257323
hypothetical protein CNBF3580 [Cryptococcus neoformans var.





neoformans B-3501A]


32
XP_571260
58268208
sterol O-acyltransferase [Cryptococcus neoformans var.





neoformans JEC21]


33
EAR83561
89285549
MBOAT family protein [Tetrahymena thermophila SB210]


34
EAS03424
89305436
MBOAT family protein [Tetrahymena thermophila SB210]


35
AAS72375
45642961
acyl-CoA:cholesterol acyltransferase alpha [Toxoplasma gondii]


36
AAS72376
45642963
acyl-CoA:cholesterol acyltransferase beta [Toxoplasma gondii]


37
XP_640280
111226542
hypothetical protein DDBDRAFT_0205259 [Dictyostelium





discoideum AX4]


38
XP_645633
66824557
hypothetical protein DDBDRAFT_0202877 [Dictyostelium





discoideum AX4]


39
EAS35506
90305875
hypothetical protein CIMG_00860 [Coccidioides immitis RS]


40
XP_386864
46124621
hypothetical protein FG06688.1 [Gibberella zeae PH-1]


41
NP_649816
28571583
CG8112-PA [Drosophila melanogaster]


42
CAE75170
39591950
Hypothetical protein CBG23107 [Caenorhabditis briggsae]


43
NP_033256
84619697
sterol O-acyltransferase 1 [Mus musculus]


44
BAC34925
26342537
unnamed protein product [Mus musculus]


45
XP_359451
39939828
hypothetical protein MG05326.4 [Magnaporthe grisea 70-15]


46
Q61263
18202591
Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1) (Acyl





coenzyme A:cholesterol acyltransferase 1) (ACAT-1)


47
XP_975142
91083363
PREDICTED: similar to CG31991-PA, isoform A [Tribolium





castaneum]


48
EAL28962
54639560
GA20833-PA [Drosophila pseudoobscura]


49
XP_957022
85082953
hypothetical protein [Neurospora crassa OR74A]


50
XP_547445
73961286
PREDICTED: similar to Sterol O-acyltransferase 1 (Cholesterol





acyltransferase 1) (Acyl coenzyme A:cholesterol acyltransferase





1) (ACAT-1) [Canis familiaris]


51
EAQ89124
88181656
hypothetical protein CHGG_05743 [Chaetomium globosum





CBS 148.51]


52
EAT78735
111057615
hypothetical protein SNOG_13711 [Phaeosphaeria nodorum





SN15]


53
Q60457
18202585
Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1) (Acyl





coenzyme A:cholesterol acyltransferase 1) (ACAT-1)


54
XP_624754
110762262
PREDICTED: similar to midway CG31991-PA, isoform A





[Apis mellifera]


55
O70536
18202126
Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1) (Acyl





coenzyme A:cholesterol acyltransferase 1) (ACAT-1)


56
XP_728984
82915156
hypothetical protein PY01256 [Plasmodium yoelii yoelii str.





17XNL]


57
NP_505828
71997360
H19N07.4 [Caenorhabditis elegans]


58
NP_001 . . .
77735363
hypothetical protein LOC504287 [Bos taurus]


59
2201440A
1585676
acyl-CoA/cholesterol acyltransferase


60
XP_663763
67539978
hypothetical protein AN6159.2 [Aspergillus nidulans FGSC A4]


61
CAI13574
55960156
sterol O-acyltransferase (acyl-Coenzyme A: cholesterol





acyltransferase) 1 [Homo sapiens]


62
XP_514030
55588858
PREDICTED: hypothetical protein XP_514030 [Pan





troglodytes]


63
AAL56227
18028942
cholesterol acyltransferase 1 [Gorilla gorilla]


64
AAL56228
18028944
cholesterol acyltransferase 1 [Pongo pygmaeus]


65
AAC37532
4878022
acyl-coenzyme A: cholesterol acyltransferase [Homo sapiens]


66
EAT47694
108883469
sterol o-acyltransferase [Aedes aegypti]


67
XP_390039
46136695
hypothetical protein FG09863.1 [Gibberella zeae PH-1]


68
BAE01048
67969393
unnamed protein product [Macaca fascicularis]


69
O77761
18202178
Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1) (Acyl





coenzyme A:cholesterol acyltransferase 1) (ACAT-1)


70
AAH06263
34782946
DGAT1 protein [Homo sapiens]


71
XP_317656
31226099
ENSANGP00000002281 [Anopheles gambiae str. PEST]


72
XP_320320
58393809
ENSANGP00000016486 [Anopheles gambiae str. PEST]


73
XP_320321
58393811
ENSANGP00000016512 [Anopheles gambiae str. PEST]


74
BAE65302
83775179
unnamed protein product [Aspergillus oryzae]


75
NP_724017
24584734
midway CG31991-PC, isoform C [Drosophila melanogaster]


76
NP_995724
45552403
midway CG31991-PD, isoform D [Drosophila melanogaster]


77
EAL33593
54644853
GA16599-PA [Drosophila pseudoobscura]


78
NP_586145
19074639
STEROL O-ACYLTRANSFERASE [Encephalitozoon cuniculi





GB-M1]


79
XP_502557
50550169
hypothetical protein [Yarrowia lipolytica]


80
XP_885914
76617939
PREDICTED: similar to Sterol O-acyltransferase 2 (Cholesterol





acyltransferase 2) (Acyl coenzyme A:cholesterol acyltransferase





2) (ACAT-2) isoform 2 [Bos taurus]


81
XP_591251
76617937
PREDICTED: similar to Sterol O-acyltransferase 2 (Cholesterol





acyltransferase 2) (Acyl coenzyme A:cholesterol acyltransferase





2) (ACAT-2) isoform 1 [Bos taurus]


82
XP_624691
66564061
PREDICTED: similar to CG8112-PA [Apis mellifera]


83
O75908
18202149
Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2) (Acyl





coenzyme A:cholesterol acyltransferase 2) (ACAT-2)


84
XP_001 . . .
109096888
PREDICTED: sterol O-acyltransferase 2 [Macaca mulatta]


85
AAK48829
13898623
acyl coenzyme A: cholesterol acyltransferase-2 [Homo sapiens]


86
AAH77916
50416229
Soat1-prov protein [Xenopus laevis]


87
AAH96091
64654094
Sterol O-acyltransferase 2 [Homo sapiens]


88
EAT38531
108874306
sterol o-acyltransferase [Aedes aegypti]


89
AAH96090
64652990
Sterol O-acyltransferase 2 [Homo sapiens]


90
NP_001 . . .
50539976
hypothetical protein LOC436731 [Danio rerio]


91
NP_714950
40254723
sterol O-acyltransferase 2 [Rattus norvegicus]


92
XP_422267
50751122
PREDICTED: similar to Sterol O-acyltransferase 1 (Cholesterol





acyltransferase 1) (Acyl coenzyme A:cholesterol acyltransferase





1) (ACAT-1) [Gallus gallus]


93
O88908
18202245
Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2) (Acyl





coenzyme A:cholesterol acyltransferase 2) (ACAT-2)


94
O77759
18202176
Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2) (Acyl





coenzyme A:cholesterol acyltransferase 2) (ACAT-2)


95
NP_666176
22122547
sterol O-acyltransferase 2 [Mus musculus]


96
BAC00846
21392392
AcylCoA:Cholesterol Acyltransferase 2 [Rattus norvegicus]


97
XP_692855
68364838
PREDICTED: similar to Soat1-prov protein [Danio rerio]


98
XP_543637
73996435
PREDICTED: similar to sterol O-acyltransferase 2 [Canis





familiaris]


99
CAG11944
47225461
unnamed protein product [Tetraodon nigroviridis]


100
CAF96514
47222847
unnamed protein product [Tetraodon nigroviridis]


101
CAG10815
47219451
unnamed protein product [Tetraodon nigroviridis]


102
EAR94647
89296659
MBOAT family protein [Tetrahymena thermophila SB210]


103
AAP68322
31711932
At2g19450 [Arabidopsis thaliana]


104
EAR94441
89296453
MBOAT family protein [Tetrahymena thermophila SB210]


105
CAG07990
47225647
unnamed protein product [Tetraodon nigroviridis]


106
XP_788209
72085563
PREDICTED: similar to sterol O-acyltransferase 1





[Strongylocentrotus purpuratus]


107
AAO32475
28564193
ARE2 [Saccharomyces castellii]


108
XP_673128
68062248
hypothetical protein PB300300.00.0 [Plasmodium berghei strain





ANKA]
















TABLE 43







Examples of phospholipid-diacylglycerol polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_504038
50553256
hypothetical protein [Yarrowia lipolytica].


2
XP_458897
50420721
hypothetical protein DEHA0D10868g [Debaryomyces hansenii





CBS767]


3
XP_718878
68473963
hypothetical protein CaO19_13439 [Candida albicans SC5314]


4
XP_447501
50290139
hypothetical protein CAGL0I05786g [Candida glabrata





CBS138]


5
XP_455369
50310695
unnamed protein product [Kluyveromyces lactis]


6
NP_014405
6324335
Acyltransferase that catalyzes diacylglycerol esterification; one





of several acyltransferases that contribute to triglyceride





synthesis; putative homolog of human lecithin cholesterol





acyltransferase; Lro1p [Saccharomyces cerevisiae]


7
NP_985371
45198342
AFL179Cp [Eremothecium gossypii]


8
BAE57684
83767545
unnamed protein product [Aspergillus oryzae]


9
EAS32928
90303297
hypothetical protein CIMG_03952 [Coccidioides immitis RS]


10
EAT89812
111068692
hypothetical protein SNOG_03081 [Phaeosphaeria nodorum





SN15]


11
XP_662596
67537644
hypothetical protein AN4992.2 [Aspergillus nidulans FGSC A4]


12
XP_361017
39942960
hypothetical protein MG03560.4 [Magnaporthe grisea 70-15]


13
CAD60714
27803011
unnamed protein product [Podospora anserina]


14
XP_718980
68473754
hypothetical protein CaO19_6018 [Candida albicans SC5314]


15
XP_386551
46123995
hypothetical protein FG06375.1 [Gibberella zeae PH-1]


16
XP_959598
85092964
hypothetical protein [Neurospora crassa OR74A]


17
XP_754624
70999814
phospholipid:diacylglycerol acyltransferase [Aspergillus





fumigatus Af293]


18
O94680
21362753
Phospholipid:diacylglycerol acyltransferase (PDAT) (Pombe





LRO1 homolog 1)


19
EAQ92213
88184745
hypothetical protein CHGG_00448 [Chaetomium globosum





CBS 148.51]


20
XP_756469
71003606
hypothetical protein UM00322.1 [Ustilago maydis 521]


21
EAL18953
50256226
hypothetical protein CNBI2140 [Cryptococcus neoformans var.





neoformans B-3501A]


22
XP_568014
58261208
phospholipid:diacylglycerol acyltransferase [Cryptococcus





neoformans var. neoformans JEC21]


23
AAP47635
37785695
lecithine cholesterol acyltransferase-like protein [Medicago





truncatula]


24
AAS79590
45935132
putative phosphatidylcholine-sterol acyltransferase [Ipomoea





trifida]


25
BAF25212
113631531
Os09g0444200 [Oryza sativa (japonica cultivar-group)]


26
AAK96619
15450695
AT5g13640/MSH12_10 [Arabidopsis thaliana]


27
XP_829379
74025626
phospholipid:diacylglycerol acyltransferase-like protein





[Trypanosoma brucei TREU927]


28
XP_816552
71655997
phospholipid:diacylglycerol acyltransferase [Trypanosoma cruzi





strain CL Brener]


29
AAO17787
37724553
lecithine cholesterol acyltransferase-like protein [Arabidopsis





thaliana]


30
XP_821756
71660075
phospholipid:diacylglycerol acyltransferase [Trypanosoma cruzi





strain CL Brener]


31
CAD38153
27552462
putative phosphatidylcholine-sterol acetyltransferase





[Physcomitrella patens]


32
NP_190069
15230521
phosphatidylcholine-sterol O-acyltransferase [Arabidopsis





thaliana]


33
CAD38155
27552466
putative acetyltransferase [Physcomitrella patens]


34
CAJ02843
68124573
phospholipid:diacylglycerol acyltransferase, putative





[Leishmania major]
















TABLE 44







Examples of malate dehydrogenase polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_503933.1
50553046
hypothetical protein [Yarrowia lipolytica].


2
EAT83219
111062099
predicted protein [Phaeosphaeria nodorum SN15]


3
XP_747556
70984070
malate dehydrogenase, NAD-dependent [Aspergillus





fumigatus Af293]


4
BAE61776
83771646
unnamed protein product [Aspergillus oryzae]


5
EAQ89010
88181542
malate dehydrogenase, mitochondrial precursor [Chaetomium





globosum CBS 148.51]


6
EAS37226
90307595
hypothetical protein CIMG_02580 [Coccidioides immitis RS]


7
XP_572013
58269714
L-malate dehydrogenase [Cryptococcus neoformans var.





neoformans JEC21]


8
XP_748936
70986899
malate dehydrogenase, NAD-dependent [Aspergillus





fumigatus Af293]


9
BAE55502
83765359
unnamed protein product [Aspergillus oryzae]


10
EAQ88553
88181085
malate dehydrogenase, mitochondrial precursor [Chaetomium





globosum CBS 148.51]


11
ABH10641
111606553
malate dehydrogenase [Coccidioides posadasii]


12
XP_321163
58395331
ENSANGP00000020184 [Anopheles gambiae str. PEST]


13
XP_717047
68477790
putative peroxisomal malate dehydrogenase [Candida albicans





SC5314]


14
AAY63978
67043759
mitochondrial malate dehydrogenase [Lysiphlebus testaceipes]


15
AAX19496
60393102
mitochondrial malate dehydrogenase 2b [Xenopus laevis]


16
EAT40089
108875864
malate dehydrogenase [Aedes aegypti]


17
AAI06696
76780392
Mdh2a protein [Xenopus laevis]


18
XP_572038
58269764
malate dehydrogenase [Cryptococcus neoformans var.





neoformans JEC21]


19
XP_392478
66513092
PREDICTED: similar to mitochondrial malate dehydrogenase





precursor isoform 1 [Apis mellifera]


20
XP_973533
91085015
PREDICTED: similar to mitochondrial malate dehydrogenase





precursor [Tribolium castaneum]


21
CAG12894
47224065
unnamed protein product [Tetraodon nigroviridis]


22
NP_001 . . .
58332672
mitochondrial malate dehydrogenase 2 [Xenopus tropicalis]


23
XP_819104
71664243
malate dehydrogenase [Trypanosoma cruzi strain CL Brener]


24
CAJ07715
68129178
malate dehydrogenase [Leishmania major]


25
EAL29124
54639722
GA20754-PA [Drosophila pseudoobscura]


26
XP_708782
68367713
PREDICTED: similar to malate dehydrogenase, mitochondrial





isoform 6 [Danio rerio]


27
XP_708779
68367700
PREDICTED: similar to malate dehydrogenase, mitochondrial





isoform 3 [Danio rerio]


28
AAW79319
58613465
malate dehydrogenase [Isochrysis galbana]


29
CAI29601
56403598
hypothetical protein [Pongo pygmaeus]


30
XP_460754
50424335
hypothetical protein DEHA0F09911g [Debaryomyces





hansenii CBS767]


31
XP_001 . . .
109066259
PREDICTED: similar to mitochondrial malate dehydrogenase





precursor [Macaca mulatta]


32
AAK69767
14583133
malate dehydrogenase [Sphyraena idiastes]


33
XP_708778
68367696
PREDICTED: similar to malate dehydrogenase, mitochondrial





isoform 2 [Danio rerio]


34
NP_001 . . .
79327392
PMDH2 [Arabidopsis thaliana]


35
ABE84799
92877831
Malate dehydrogenase, NAD-dependent, eukaryotes and





gamma proteobacteria [Medicago truncatula]


36
AAU29200
52139820
glyoxisomal malate dehydrogenase [Lycopersicon





esculentum]


37
AAW27425
56758570
SJCHGC06124 protein [Schistosoma japonicum]


38
XP_708781
68367709
PREDICTED: similar to malate dehydrogenase, mitochondrial





isoform 5 [Danio rerio]


39
1SMKH
60593494
Chain H, Mature And Translocatable Forms Of Glyoxysomal





Malate Dehydrogenase Have Different Activities And





Stabilities But Similar Crystal Structures


40
XP_822509
71746908
mitochondrial malate dehydrogenase [Trypanosoma brucei





TREU927]


41
1SEVB
60593476
Chain B, Mature And Translocatable Forms Of Glyoxysomal





Malate Dehydrogenase Have Different Activities And





Stabilities But Similar Crystal Structures


42
XP_708780
68367705
PREDICTED: similar to malate dehydrogenase, mitochondrial





isoform 4 [Danio rerio]


43
ABD77290
89574129
mitochondrial malate dehydrogenase 2, NAD [Homo sapiens]


44
ABD77284
89574117
mitochondrial malate dehydrogenase 2, NAD [Rattus





norvegicus]


45
ABD77283
89574115
mitochondrial malate dehydrogenase 2, NAD [Mus musculus]


46
ABD77287
89574123
mitochondrial malate dehydrogenase 2, NAD [Oryctolagus





cuniculus]


47
ABD77280
89574109
mitochondrial malate dehydrogenase 2, NAD [Loxodonta





africana]


48
ABD77288
89574125
mitochondrial malate dehydrogenase 2, NAD [Lepus





europaeus]


49
XP_792004
72025672
PREDICTED: similar to mitochondrial malate dehydrogenase





precursor [Strongylocentrotus purpuratus]


50
ABD77293
89574135
mitochondrial malate dehydrogenase 2, NAD [Canis





familiaris]


51
ABD77294
89574137
mitochondrial malate dehydrogenase 2, NAD [Felis catus]


52
ABD77278
89574105
mitochondrial malate dehydrogenase 2, NAD [Didelphis





virginiana]


53
XP_809210
71414199
mitochondrial malate dehydrogenase [Trypanosoma cruzi





strain CL Brener]


54
ABD77301
89574151
mitochondrial malate dehydrogenase 2, NAD [Sus scrofa]


55
ABD77286
89574121
mitochondrial malate dehydrogenase 2, NAD [Mesocricetus





auratus]


56
ABD77298
89574145
mitochondrial malate dehydrogenase 2, NAD [Bos taurus]


57
AAT35230
47531133
mitochondrial malate dehydrogenase [Clonorchis sinensis]


58
ABD77281
89574111
mitochondrial malate dehydrogenase 2, NAD [Dasypus





novemcinctus]


59
ABD77296
89574141
mitochondrial malate dehydrogenase 2, NAD [Ceratotherium





simum]


60
ABA99939
108863014
Malate dehydrogenase, glyoxysomal precursor, putative,





expressed [Oryza sativa (japonica cultivar-group)]


61
AAU29198
52139816
mitochondrial malate dehydrogenase [Lycopersicon





esculentum]


62
ABD77279
89574107
mitochondrial malate dehydrogenase 2, NAD [Sminthopsis





douglasi]


63
CAJ07717
68129180
malate dehydrogenase, putative [Leishmania major]


64
XP_519160
55628772
PREDICTED: similar to mitochondrial malate dehydrogenase





precursor [Pan troglodytes]


65
ABD72702
89473780
putative mitochondrial malate dehydrogenase [Acyrthosiphon





pisum]


66
ABD77299
89574147
mitochondrial malate dehydrogenase 2, NAD [Balaenoptera





physalus]


67
BAF23792
113623847
Os08g0434300 [Oryza sativa (japonica cultivar-group)]


68
CAI11361
57337458
putative malate dehydrogenase [Orpinomyces sp. OUS1]


69
ABD77289
89574127
mitochondrial malate dehydrogenase 2, NAD [Tadarida





brasiliensis]


70
BAF06605
113534222
Os01g0829800 [Oryza sativa (japonica cultivar-group)]


71
ABD77292
89574133
mitochondrial malate dehydrogenase 2, NAD [Tupaia glis]


72
ABD77285
89574119
mitochondrial malate dehydrogenase 2, NAD [Cavia





porcellus]


73
BAF18303
113579940
Os05g0574400 [Oryza sativa (japonica cultivar-group)]


74
ZP_010 . . .
85712491
malate dehydrogenase [Idiomarina baltica OS145]


75
XP_539718
57097207
PREDICTED: similar to malate dehydrogenase 2, NAD





(mitochondrial) [Canis familiaris]


76
ABD77277
89574103
mitochondrial malate dehydrogenase 2, NAD [Monodelphis





domestica]


77
Q5R030
62286970
Malate dehydrogenase


78
YP_660122
109896867
malate dehydrogenase, NAD-dependent [Pseudoalteromonas





atlantica T6c]


79
Q87SU7
48428249
Malate dehydrogenase


80
ABD77291
89574131
mitochondrial malate dehydrogenase 2, NAD [Aotus





trivirgatus]


81
ZP_007 . . .
75854582
COG0039: Malate/lactate dehydrogenases [Vibrio sp. Ex25]


82
ZP_011 . . .
88795318
malate dehydrogenase [Alteromonas macleodii ‘Deep





ecotype’]


83
ZP_012 . . .
91228842
malate dehydrogenase [Vibrio alginolyticus 12G01]


84
ZP_011 . . .
89075547
malate dehydrogenase [Photobacterium sp. SKA34]


85
ZP_012 . . .
90580811
malate dehydrogenase [Vibrio angustum S14]


86
YP_671200
110643470
malate dehydrogenase [Escherichia coli 536]


87
ABD77295
89574139
mitochondrial malate dehydrogenase 2, NAD [Equus caballus]


88
Q5E875
66774139
Malate dehydrogenase


89
ZP_007 . . .
75209673
COG0039: Malate/lactate dehydrogenases [Escherichia coli





B171]


90
ZP_009 . . .
84394039
malate dehydrogenase [Vibrio splendidus 12B01]


91
ZP_007 . . .
75228638
COG0039: Malate/lactate dehydrogenases [Escherichia coli





B7A]


92
ZP_010 . . .
86147822
malate dehydrogenase [Vibrio sp. MED222]


93
BAD30064
50508045
malate dehydrogenase [Moritella sp. 36B1]


94
Q4QL89
73621201
Malate dehydrogenase


95
YP_404893
82778544
malate dehydrogenase [Shigella dysenteriae Sd197]


96
BAD30059
50508035
malate dehydrogenase [Moritella sp. 47A1]


97
BAD30066
50508049
malate dehydrogenase [Moritella sp. 36G1]


98
ZP_008 . . .
77958772
COG0039: Malate/lactate dehydrogenases [Yersinia





bercovieri ATCC 43970]


99
BAD30071
50508059
malate dehydrogenase [Moritella sp. 38F1]


100
ZP_008 . . .
77973999
COG0039: Malate/lactate dehydrogenases [Yersinia





frederiksenii ATCC 33641]


101
ZP_008 . . .
77977600
COG0039: Malate/lactate dehydrogenases [Yersinia





intermedia ATCC 29909]


102
P48364
1346511
Malate dehydrogenase


103
BAD30062
50508041
malate dehydrogenase [Moritella sp. 16H2]


104
BAD30069
50508055
malate dehydrogenase [Moritella sp. 56A1]


105
ZP_008 . . .
77961850
COG0039: Malate/lactate dehydrogenases [Yersinia mollaretii





ATCC 43969]


106
ZP_012 . . .
90411956
putative malate dehydrogenase [Photobacterium profundum





3TCK]


107
Q6AW21
57012891
Malate dehydrogenase


108
Q57JA9
68052390
Malate dehydrogenase


109
ZP_012 . . .
90407531
malate dehydrogenase [Psychromonas sp. CNPT3]


110
BAD36746
51172588
malate dehydrogenase [Moritella yayanosii]


111
Q6AW23
57012892
Malate dehydrogenase


112
ABG22106
108863015
Malate dehydrogenase, glyoxysomal precursor, putative,





expressed [Oryza sativa (japonica cultivar-group)]


113
ZP_005 . . .
68546610
Malate dehydrogenase, NAD-dependent, eukaryotes and





gamma proteobacteria [Shewanella amazonensis SB2B]


114
BAD30060
50508037
malate dehydrogenase [Moritella sp. 47B1]


115
EAL31008
54642259
GA10540-PA [Drosophila pseudoobscura]


116
YP_736674
114046124
malate dehydrogenase, NAD-dependent [Shewanella sp. MR-





7]


117
CAJ07716
68129179
malate dehydrogenase, putative [Leishmania major]


118
ZP_009 . . .
82743617
Malate dehydrogenase, NAD-dependent, eukaryotes and





gamma proteobacteria [Shewanella sp. W3-18-1]


119
Q47VL0
83288301
Malate dehydrogenase


120
ZP_011 . . .
88859032
malate dehydrogenase [Pseudoalteromonas tunicata D2]


121
YP_561838
91792187
malate dehydrogenase, NAD-dependent [Shewanella





denitrificans OS217]


122
ZP_005 . . .
68544347
Malate dehydrogenase, NAD-dependent, eukaryotes and





gamma proteobacteria [Shewanella baltica OS155]


123
ZP_007 . . .
75429373
malate dehydrogenase [Actinobacillus succinogenes 130Z]


124
AAW29940
56788316
malate dehydrogenase [Pasteurella trehalosi]


125
BAD30063
50508043
malate dehydrogenase [Shewanella sp. T4609]


126
EAL31009
54642260
GA10541-PA [Drosophila pseudoobscura]


127
ZP_006 . . .
69950735
Malate dehydrogenase, NAD-dependent, eukaryotes and





gamma proteobacteria [Shewanella frigidimarina NCIMB





400]


128
YP_341148
77361573
malate dehydrogenase [Pseudoalteromonas haloplanktis





TAC125]


129
ZP_013 . . .
106882260
malate dehydrogenase, NAD-dependent [Psychromonas





ingrahamii 37]


130
BAD30068
50508053
malate dehydrogenase [Shewanella sp. 33H2]


131
ZP_008 . . .
78368581
Malate dehydrogenase, NAD-dependent, eukaryotes and





gamma proteobacteria [Shewanella sp. PV-4]


132
XP_851105
74004024
PREDICTED: similar to malate dehydrogenase, mitochondrial





[Canis familiaris]


133
ABD77300
89574149
mitochondrial malate dehydrogenase 2, NAD [Hippopotamus





amphibius]


134
XP_816948
71656813
glycosomal malate dehydrogenase [Trypanosoma cruzi strain





CL Brener]


135
CAJ19596
82655060
malate dehydrogenase [Klebsiella pneumoniae]


136
AAW29939
56788314
malate dehydrogenase [Mannheimia glucosida]


137
CAJ19583
82655034
malate dehydrogenase [Klebsiella pneumoniae]


138
CAJ19589
82655046
malate dehydrogenase [Klebsiella pneumoniae]


139
CAJ19580
82655028
malate dehydrogenase [Klebsiella pneumoniae]


140
CAJ19591
82655050
malate dehydrogenase [Klebsiella pneumoniae]


141
CAJ19595
82655058
malate dehydrogenase [Klebsiella pneumoniae]


142
CAJ19593
82655054
malate dehydrogenase [Klebsiella pneumoniae]


143
AAW29937
56788310
malate dehydrogenase [Mannheimia haemolytica]


144
XP_812467
71423452
glycosomal malate dehydrogenase [Trypanosoma cruzi strain





CL Brener]


145
AAW29938
56788312
malate dehydrogenase [Mannheimia haemolytica]


146
AAW29936
56788308
malate dehydrogenase [Mannheimia haemolytica]


147
XP_849858
73993436
PREDICTED: similar to malate dehydrogenase, mitochondrial





[Canis familiaris]


148
AAW28048
56718658
malate dehydrogenase [Vibrio cholerae]


149
AAU88998
52856248
malate dehydrogenase [Shigella flexneri]


150
AAW28041
56718644
malate dehydrogenase [Vibrio cholerae]


151
AAW28047
56718656
malate dehydrogenase [Vibrio mimicus]


152
AAW28045
56718652
malate dehydrogenase [Vibrio mimicus]


153
ABD77282
89574113
mitochondrial malate dehydrogenase 2, NAD [Tamandua





tetradactyla]


154
AAU89018
52856288
malate dehydrogenase [Shigella boydii]


155
AAU89003
52856258
malate dehydrogenase [Escherichia coli]


156
AAU88960
52856172
malate dehydrogenase [Escherichia coli]


157
AAU88962
52856176
malate dehydrogenase [Shigella flexneri]


158
AAU88996
52856244
malate dehydrogenase [Escherichia coli]


159
AAU88972
52856196
malate dehydrogenase [Shigella boydii]


160
AAU88969
52856190
malate dehydrogenase [Shigella boydii]


161
ZP_007 . . .
75822170
COG0039: Malate/lactate dehydrogenases [Vibrio cholerae





RC385]


162
AAU89062
52856376
malate dehydrogenase [Shigella boydii]


163
AAU88982
52856216
malate dehydrogenase [Shigella dysenteriae]


164
AAU88995
52856242
malate dehydrogenase [Escherichia coli]


165
AAU88993
52856238
malate dehydrogenase [Escherichia coli]


166
AAU89044
52856340
malate dehydrogenase [Shigella flexneri]


167
AAU89015
52856282
malate dehydrogenase [Shigella boydii]


168
AAU88971
52856194
malate dehydrogenase [Shigella sonnei]


169
AAW28034
56718629
malate dehydrogenase [Vibrio cholerae]


170
AAU89011
52856274
malate dehydrogenase [Shigella flexneri]


171
AAU88958
52856168
malate dehydrogenase [Escherichia coli]


172
AAU88976
52856204
malate dehydrogenase [Shigella dysenteriae]


173
AAU88991
52856234
malate dehydrogenase [Escherichia coli]


174
XP_850818
73988067
PREDICTED: similar to mitochondrial malate dehydrogenase





precursor [Canis familiaris]


175
AAU86550
52697626
malate dehydrogenase [Shigella boydii]


176
AAU88979
52856210
malate dehydrogenase [Shigella dysenteriae]


177
AAU89005
52856262
malate dehydrogenase [Escherichia coli]


178
AAU89019
52856290
malate dehydrogenase [Shigella dysenteriae]


179
AAU88983
52856218
malate dehydrogenase [Shigella dysenteriae]


180
AAU86549
52697624
malate dehydrogenase [Escherichia albertii]


181
AAX85842
62532910
Mdh [Escherichia coli]


182
AAU89007
52856266
malate dehydrogenase [Shigella flexneri]


183
AAU88980
52856212
malate dehydrogenase [Shigella flexneri]


184
AAU89000
52856252
malate dehydrogenase [Shigella flexneri]


185
AAU88968
52856188
malate dehydrogenase [Shigella boydii]


186
AAU88988
52856228
malate dehydrogenase [Escherichia coli]


187
AAX85856
62532938
Mdh [Escherichia coli]


188
AAU86566
52697658
malate dehydrogenase [Shigella boydii]


189
AAU86571
52697668
malate dehydrogenase [Escherichia albertii]


190
ABF20150
94468239
Mdh [Escherichia coli]


191
AAU89051
52856354
malate dehydrogenase [Shigella boydii]


192
AAU89059
52856370
malate dehydrogenase [Shigella boydii]


193
AAU89057
52856366
malate dehydrogenase [Shigella boydii]


194
AAU89036
52856324
malate dehydrogenase [Shigella flexneri]


195
AAU86559
52697644
malate dehydrogenase [Shigella boydii]


196
ABF20151
94468241
Mdh [Escherichia coli]


197
ABF20142
94468223
Mdh [Escherichia coli]


198
AAU88990
52856232
malate dehydrogenase [Escherichia coli]


199
AAU86567
52697660
malate dehydrogenase [Shigella boydii]


200
AAU89032
52856316
malate dehydrogenase [Shigella dysenteriae]


201
AAU89012
52856276
malate dehydrogenase [Shigella flexneri]
















TABLE 45







Examples of glucose-6-phosphate dehydrogenase polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_504275
50553728
hypothetical protein [Yarrowia lipolytica]


2
XP_365081
39965237
hypothetical protein MG09926.4 [Magnaporthe grisea 70-15]


3
XP_381455
46108794
G6PD_ASPNG Glucose-6-phosphate 1-dehydrogenase





(G6PD) [Gibberella zeae PH-1]


4
XP_660585
67525047
glucose-6-phosphate 1-dehydrogenase [Aspergillus nidulans





FGSC A4]


5
P48826
1346070
Glucose-6-phosphate 1-dehydrogenase (G6PD)


6
CAA54840
1523782
glucose-6-phosphate 1-dehydrogenase [Aspergillus niger]


7
EAU38380
114196680
glucose-6-phosphate 1-dehydrogenase [Aspergillus terreus





NIH2624]


8
EAT83608
111062488
predicted protein [Phaeosphaeria nodorum SN15]


9
EAS28915
90299284
glucose-6-phosphate 1-dehydrogenase [Coccidioides immitis





RS]


10
XP_754767
71000100
glucose-6-phosphate 1-dehydrogenase [Aspergillus fumigatus





Af293]


11
XP_958320
85090234
GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE (G6PD)





[Neurospora crassa OR74A]


12
EAQ93370
88185902
glucose-6-phosphate 1-dehydrogenase [Chaetomium





globosum CBS 148.51]


13
CAA58825
642160
unnamed protein product [Emericella nidulans]


14
XP_458129
50419213
hypothetical protein DEHA0C11286g [Debaryomyces





hansenii CBS767]


15
AAB25541
299248
glucose-6-phosphate dehydrogenase [Pichia jadinii = yeast,





Peptide, 495 aa]


16
XP_723251
68465104
putative glucose-6-phosphate dehydrogenase [Candida





albicans SC5314]


17
XP_723440
68464725
putative glucose-6-phosphate dehydrogenase [Candida





albicans SC5314]


18
XP_453944
50307901
G6PD_KLULA [Kluyveromyces lactis]


19
NP_982741
45185024
ABL206Cp [Eremothecium gossypii]


20
XP_448038
50291211
unnamed protein product [Candida glabrata]


21
XP_572045
58269778
glucose-6-phosphate 1-dehydrogenase [Cryptococcus





neoformans var. neoformans JEC21]


22
NP_014158
6324088
Glucose-6-phosphate dehydrogenase (G6PD), catalyzes the





first step of the pentose phosphate pathway; involved in





adapting to oxidatve stress; homolog of the human G6PD





which is deficient in patients with hemolytic anemia; Zwf1p





[Saccharomyces cerevisiae]


23
AAT93017
51013447
YNL241C [Saccharomyces cerevisiae]


24
AAA34619
171545
glucose-6-phosphate dehydrogenase (ZWF1) (EC 1.1.1.49)


25
XP_761077
71021693
hypothetical protein UM04930.1 [Ustilago maydis 521]


26
NP_593344
63054535
glucose-6-phosphate 1-dehydrogenase [Schizosaccharomyces





pombe 972h-]


27
XP_644814
66822919
glucose 6-phosphate-1-dehydrogenase [Dictyostelium





discoideum AX4]


28
ABD72519
89357348
glucose 6-phosphate dehydrogenase [Trypanosoma cruzi]


29
BAE99888
110735823
glucose-6-phosphate dehydrogenase [Arabidopsis thaliana]


30
CAB52675
5732197
glucose-6-phosphate 1-dehydrogenase [Arabidopsis thaliana]


31
CAB08746
2104434
SPAC3A12.18 [Schizosaccharomyces pombe]


32
ABD72517
89357344
glucose 6-phosphate dehydrogenase [Trypanosoma cruzi]


33
ABD72518
89357346
glucose 6-phosphate dehydrogenase [Trypanosoma cruzi]


34
BAB96757
21262179
glucose-6-phosphate dehydrogenase 1 [Chlorella vulgaris]


35
XP_822502
71746894
glucose-6-phosphate 1-dehydrogenase [Trypanosoma brucei





TREU927]


36
CAJ07708
68129171
glucose-6-phosphate dehydrogenase [Leishmania major]


37
CAC07816
10045209
glucose-6-phosphate 1-dehydrogenase [Trypanosoma brucei]


38
BAF15046
113564703
Os04g0485300 [Oryza sativa (japonica cultivar-group)]


39
AAO37825
28261397
glucose-6-phosphate dehydrogenase [Leishmania mexicana]


40
AAM64228
27434608
glucose-6-phosphate dehydrogenase [Leishmania mexicana





amazonensis]


41
XP_001 . . .
110750934
PREDICTED: similar to Zwischenferment CG12529-PA,





isoform A [Apis mellifera]


42
XP_974096
91082561
PREDICTED: similar to CG12529-PA, isoform A [Tribolium





castaneum]


43
ABE83959
92876243
Glucose-6-phosphate dehydrogenase [Medicago truncatula]


44
BAE38077
74138546
unnamed protein product [Mus musculus]


45
NP_001 . . .
79313844
G6PD5; glucose-6-phosphate 1-dehydrogenase [Arabidopsis





thaliana]


46
CAB52674
5732195
glucose-6-phosphate 1-dehydrogenase [Arabidopsis thaliana]


47
AAD11426
4206114
cytoplasmic glucose-6-phosphate 1-dehydrogenase





[Mesembryanthemum crystallinum]


48
Q42919
3023815
Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform





(G6PD)


49
AAL79959
19071787
glucose-6-phosphate dehydrogenase [Oryza sativa (japonica





cultivar-group)]


50
CAE62054
39593761
Hypothetical protein CBG06072 [Caenorhabditis briggsae]


51
EAL31619
54642875
GA11679-PA [Drosophila pseudoobscura]


52
Q00612
54037161
Glucose-6-phosphate 1-dehydrogenase X (G6PD)


53
AAH75663
49523350
Glucose-6-phosphate dehydrogenase X-linked [Mus





musculus]


54
AAB69319
2352923
cytosolic glucose-6-phosphate dehydrogenase 2 [Petroselinum





crispum]


55
AAM64230
27434612
glucose-6-phosphate dehydrogenase [Leishmania guyanensis]


56
ABB29564
78183137
putative Zwischenferment [Drosophila yakuba]


57
AAL57688
18086470
AT3g27300/K17E12_12 [Arabidopsis thaliana]


58
NP_728287
24643352
Zwischenferment CG12529-PB, isoform B [Drosophila





melanogaster]


59
EAT38627
108874402
glucose-6-phosphate 1-dehydrogenase [Aedes aegypti]


60
AAR26303
89214190
glucose-6-phosphate dehydrogenase [Populus suaveolens]


61
AAA99073
1304700
glucose-6-phosphate 1-dehydrogenase [Drosophila





melanogaster]


62
AAK93503
15292469
SD03244p [Drosophila melanogaster]


63
AAB02809
1304686
glucose-6-phosphate 1-dehydrogenase [Drosophila





melanogaster]


64
NP_523411
24643350
Zwischenferment CG12529-PA, isoform A [Drosophila





melanogaster]


65
AAA99107
1305086
glucose-6-phosphate 1-dehydrogenase [Drosophila





melanogaster]


66
ABB29562
78183133
putative Zwischenferment [Drosophila simulans]


67
NP_502129
17538218
B0035.5 [Caenorhabditis elegans]


68
AAZ23850
71089991
glucose-6-phosphate dehydrogenase [Boophilus microplus]


69
P37830
585165
Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform





(G6PD)


70
AAB02812
1304692
glucose-6-phosphate 1-dehydrogenase [Drosophila





melanogaster]


71
ABB55386
81075965
glucose-6-phosphate 1-dehydrogenase cytoplasmic isoform-





like [Solanum tuberosum]


72
CAJ83683
89273424
glucose-6-phosphate dehydrogenase [Xenopus tropicalis]


73
NP_001 . . .
62859893
glucose-6-phosphate dehydrogenase 2 [Xenopus tropicalis]


74
ABB29563
78183135
putative Zwischenferment [Drosophila teissieri]


75
AAX45785
61394184
glucose-6-phosphate dehydrogenase isoform B [Ips





typographus]


76
AAX45784
61394183
glucose-6-phosphate dehydrogenase isoform A [Ips





typographus]


77
AAH81820
51980296
Glucose-6-phosphate dehydrogenase X-linked [Rattus





norvegicus]


78
XP_311452
58381765
ENSANGP00000018551 [Anopheles gambiae str. PEST]


79
XP_538209
74009187
PREDICTED: similar to Glucose-6-phosphate 1-





dehydrogenase (G6PD) [Canis familiaris]


80
AAH59324
111185531
Unknown (protein for MGC: 69058) [Xenopus laevis]


81
ABB29560
78183129
putative Zwischenferment [Drosophila erecta]


82
Q27638
3023810
Glucose-6-phosphate 1-dehydrogenase (G6PD)


83
Q29492
2494652
Glucose-6-phosphate 1-dehydrogenase (G6PD)


84
BAF09259
113536876
Os02g0600400 [Oryza sativa (japonica cultivar-group)]


85
O55044
62510568
Glucose-6-phosphate 1-dehydrogenase (G6PD)


86
CAA04993
3021510
glucose-6-phosphate dehydrogenase [Nicotiana tabacum]


87
ABB29561
78183131
putative Zwischenferment [Drosophila orena]


88
BAA97662
8918502
glucose-6-phosphate dehydrogenase [Triticum aestivum]


89
BAD17920
46849421
glucose-6-phosphate 1-dehydrogenase [Acipenser baerii]


90
XP_699168
68440567
PREDICTED: similar to glucose-6-phosphate dehydrogenase





[Danio rerio]


91
AAB96363
2734869
glucose-6-phosphate dehydrogenase [Takifugu rubripes]


92
NP_000393
109389365
glucose-6-phosphate dehydrogenase isoform a [Homo sapiens]


93
NP_001 . . .
108773793
glucose-6-phosphate dehydrogenase isoform b [Homo





sapiens]


94
AAA52500
182871
glucose-6-phosphate dehydrogenase variant A-(EC 1.1.1.49)


95
P11413
120731
Glucose-6-phosphate 1-dehydrogenase (G6PD)


96
AAA92653
1203978
G6PD [Homo sapiens]


97
AAX43335
61369430
glucose-6-phosphate dehydrogenase [synthetic construct]


98
P41571
1169799
Glucose-6-phosphate 1-dehydrogenase (G6PD)





(Zwischenferment)


99
2BHLB
66361518
Chain B, X-Ray Structure Of Human Glucose-6-Phosphate





Dehydrogenase (Deletion Variant) Complexed With Glucose-





6-Phosphate


100
ABC74527
85700174
glucose-6-phosphate dehydrogenase [Populus trichocarpa]


101
ABC74528
85700176
glucose-6-phosphate dehydrogenase [Populus trichocarpa]


102
AAA51463
157470
glucose-6-phosphate dehydrogenase


103
XP_001 . . .
109132852
PREDICTED: glucose-6-phosphate dehydrogenase isoform 1





[Macaca mulatta]


104
1QKIH
7546530
Chain H, X-Ray Structure Of Human Glucose 6-Phosphate





Dehydrogenase (Variant Canton R4591) Complexed With





Structural Nadp+


105
XP_001 . . .
109132850
PREDICTED: glucose-6-phosphate dehydrogenase isoform 2





[Macaca mulatta]


106
BAA97663
8918504
glucose-6-phosphate dehydrogenase [Triticum aestivum]


107
CAA04992
3021508
glucose-6-phosphate dehydrogenase [Nicotiana tabacum]


108
AAB69318
2352921
cytosolic glucose-6-phosphate dehydrogenase 1 [Petroselinum





crispum]


109
XP_307095
58375370
ENSANGP00000012074 [Anopheles gambiae str. PEST]


110
AAA41179
204197
glucose-6-phosphate dehydrogenase


111
AAA63175
182890
glucose-6-phosphate dehydrogenase [Homo sapiens]


112
BAA97664
8918506
glucose-6-phosphate dehydrogenase [Triticum aestivum]


113
AAW24823
56753227
SJCHGC02527 protein [Schistosoma japonicum]


114
CAA58590
5459313
glucose-6-phosphate 1-dehydrogenase [Takifugu rubripes]


115
CAG07451
47228719
unnamed protein product [Tetraodon nigroviridis]


116
CAJ28912
113207852
glucose-6-phosphate 1-dehydrogenase [Crassostrea gigas]


117
ABC25881
83628088
glucose-6-phosphate 1-dehydrogenase [Homo sapiens]


118
ABC25981
83628208
glucose-6-phosphate 1-dehydrogenase [Homo sapiens]


119
ABC25826
83628022
glucose-6-phosphate 1-dehydrogenase [Homo sapiens]


120
BAD17912
46849405
glucose-6-phosphate 1-dehydrogenase [Amia calva]


121
BAD17877
46849335
glucose-6-phosphate 1-dehydrogenase [Protopterus annectens]


122
BAD17947
46849475
glucose-6-phosphate 1-dehydrogenase [Callorhinchus





callorynchus]


123
AAI20828
111306848
Glucose-6-phosphate dehydrogenase 2 [Mus musculus]


124
BAD17927
46849435
glucose-6-phosphate 1-dehydrogenase [Polypterus





ornatipinnis]


125
BAD17898
46849377
glucose-6-phosphate 1-dehydrogenase [Oryzias latipes]


126
BAD17891
46849363
glucose-6-phosphate 1-dehydrogenase [Ambystoma





mexicanum]


127
BAD17951
46849483
glucose-6-phosphate 1-dehydrogenase [Lethenteron reissneri]


128
AAF19030
7629275
glucose-6-phosphate-1-dehydrogenase; G6PD [Pimephales





promelas]


129
BAD17941
46849463
glucose-6-phosphate 1-dehydrogenase [Potamotrygon motoro]


130
BAD17954
46849489
glucose-6-phosphate 1-dehydrogenase [Branchiostoma





belcheri]


131
BAD17905
46849391
glucose-6-phosphate 1-dehydrogenase [Lepisosteus osseus]


132
BAD17884
46849349
glucose-6-phosphate 1-dehydrogenase [Lepidosiren paradoxa]


133
BAD17934
46849449
glucose-6-phosphate 1-dehydrogenase [Cephaloscyllium





umbratile]


134
ABC74529
85700178
glucose-6-phosphate dehydrogenase [Populus trichocarpa]


135
CAB52685
5734379
plastidic glucose-6-phosphate dehydrogenase [Dunaliella





bioculata]


136
Q43793
3023817
Glucose-6-phosphate 1-dehydrogenase, chloroplast precursor





(G6PD)


137
AAF87216
9392607
plastidic glucose 6-phosphate dehydrogenase [Nicotiana





tabacum]


138
BAC23041
24745908
glucose 6-phosphate dehydrogenase [Solanum tuberosum]


139
CAB52708
5734502
glucose-6-phosphate 1-dehydrogenase [Solanum tuberosum]


140
BAF21344
113610966
Os07g0406300 [Oryza sativa (japonica cultivar-group)]


141
AAQ02671
33304517
putative plastidic glucose-6-phosphate dehydrogenase [Oryza





sativa (japonica cultivar-group)]


142
AAW82643
58803037
hepatic glucose-6-phosphate dehydrogenase [Rhabdosargus





sarba]


143
BAF12270
113548827
Os03g0412800 [Oryza sativa (japonica cultivar-group)]


144
AAN72144
25083966
glucose-6-phosphate dehydrogenase [Arabidopsis thaliana]


145
AAB69317
2352919
plastidic glucose-6-phosphate dehydrogenase [Petroselinum





crispum]


146
O24357
3334193
Glucose-6-phosphate 1-dehydrogenase, chloroplast precursor





(G6PD)


147
AAO23597
27764952
At1g24280/F3I6_22 [Arabidopsis thaliana]


148
Q8L743
25452975
Glucose-6-phosphate 1-dehydrogenase 3, chloroplast





precursor (G6PD3) (G6PDH3)


149
CAA59011
1166405
glucose-6-phosphate 1-dehydrogenase [Arabidopsis thaliana]


150
CAA59012
1174336
glucose-6-phosphate 1-dehydrogenase [Arabidopsis thaliana]


151
CAC05439
9955555
glucose-6-phosphate 1-dehydrogenase [Arabidopsis thaliana]


152
Q9FY99
25452980
Glucose-6-phosphate 1-dehydrogenase 2, chloroplast





precursor (G6PD2) (G6PDH2)


153
AAL57678
18086448
AT5g13110/T19L5_70 [Arabidopsis thaliana]


154
Q43839
3023818
Glucose-6-phosphate 1-dehydrogenase, chloroplast precursor





(G6PD)


155
CAA04696
3021305
plastidic glucose-6-phosphate dehydrogenase [Arabidopsis





thaliana]


156
CAB52681
5734372
glucose-6-phosphate 1-dehydrogenase [Cyanidium caldarium]


157
CAA04994
3021532
glucose-6-phosphate dehydrogenase [Nicotiana tabacum]


158
Q7YS37
62510624
Glucose-6-phosphate 1-dehydrogenase (G6PD)


159
CAG04059
47229307
unnamed protein product [Tetraodon nigroviridis]


160
CAD28862
29149997
glucose 6 phosphate dehydrogenase [Acraea encedana]


161
CAD28863
29149999
glucose 6 phosphate dehydrogenase [Acraea encedana]


162
AAM64231
27434614
glucose-6-phosphate dehydrogenase [Leishmania braziliensis]


163
AAG28728
11066848
glucose-6-phosphate-dehydrogenase [Drosophila mauritiana]


164
AAG28730
11066852
glucose-6-phosphate-dehydrogenase [Drosophila sechellia]


165
ABF96583
108708788
Glucose-6-phosphate 1-dehydrogenase, chloroplast precursor,





putative, expressed [Oryza sativa (japonica cultivar-group)]


166
CAA03941
2276348
Glucose-6-phosphate dehydrogenase [Spinacia oleracea]


167
XP_583628
76658972
PREDICTED: similar to Glucose-6-phosphate 1-





dehydrogenase (G6PD) [Bos taurus]


168
AAA52499
182869
glucose-6-phosphate dehydrogenase


169
AAM64229
27434610
glucose-6-phosphate dehydrogenase [Leishmania mexicana]


170
NP_587749
19075249
hypothetical protein SPCC794.01c [Schizosaccharomyces





pombe 972h-]


171
AAR12945
38156652
glucose-6-phosphate dehydrogenase [Drosophila mojavensis]


172
AAR12953
38156668
glucose-6-phosphate dehydrogenase [Drosophila mojavensis]


173
AAR12946
38156654
glucose-6-phosphate dehydrogenase [Drosophila mojavensis]


174
AAR12943
38156648
glucose-6-phosphate dehydrogenase [Drosophila mojavensis]


175
AAR12952
38156666
glucose-6-phosphate dehydrogenase [Drosophila mojavensis]


176
BAF11858
113548415
Os03g0318500 [Oryza sativa (japonica cultivar-group)]


177
XP_559252
57942974
ENSANGP00000028421 [Anopheles gambiae str. PEST]


178
NP_593614
19114526
hypothetical protein SPAC3C7.13c [Schizosaccharomyces





pombe 972h-]


179
BAD94743
62321397
glucose-6-phosphate dehydrogenase [Arabidopsis thaliana]


180
CAJ20381
95007160
glucose-6-phosphate-1-dehydrogenase [Toxoplasma gondii]


181
YP_605437
94986073
glucose-6-phosphate 1-dehydrogenase [Deinococcus





geothermalis DSM 11300]


182
CAE51228
37651949
glucose 6 phosphate dehydrogenase [Adalia bipunctata]


183
YP_007820
46446455
putative glucose-6-phosphate [Candidatus Protochlamydia





amoebophila UWE25]


184
NP_295319
15806604
glucose-6-phosphate 1-dehydrogenase [Deinococcus





radiodurans R1]


185
CAE51222
37651937
glucose 6 phosphate dehydrogenase [Adalia bipunctata]


186
CAE51229
37651951
glucose 6 phosphate dehydrogenase [Adalia decempunctata]


187
ZP_007 . . .
76260057
Glucose-6-phosphate dehydrogenase [Chloroflexus





aurantiacus J-10-fl]


188
ZP_002 . . .
47096622
glucose-6-phosphate 1-dehydrogenase [Listeria





monocytogenes str. 1/2a F6854]


189
ZP_004 . . .
66965919
Glucose-6-phosphate dehydrogenase [Arthrobacter sp.FB24]


190
ZP_002 . . .
47093301
glucose-6-phosphate 1-dehydrogenase [Listeria





monocytogenes str. 4b H7858]


191
NP_471419
16801151
hypothetical protein lin2085 [Listeria innocua Clip11262]


192
NP_693860
23100393
glucose-6-phosphate 1-dehydrogenase [Oceanobacillus





iheyensis HTE831]


193
NP_829405
29840299
glucose-6-phosphate 1-dehydrogenase [Chlamydophila caviae





GPIC]


194
CAJ71041
91203388
strongly similar to glucose-6-phosphate dehydrogenase





[Candidatus Kuenenia stuttgartiensis]


195
YP_629214
108761123
glucose-6-phosphate 1-dehydrogenase [Myxococcus xanthus





DK 1622]


196
ZP_009 . . .
84387050
glucose-6-phosphate 1-dehydrogenase [Vibrio splendidus





12B01]


197
ZP_011 . . .
88856188
glucose-6-phosphate 1-dehydrogenase [marine





actinobacterium PHSC20C1]


198
NP_827489
29832855
glucose-6-phosphate 1-dehydrogenase [Streptomyces





avermitilis MA-4680]


199
CAH10104
88319768
putative glucose-6-phosphate-1-dehydrogenase [Streptomyces





sp. SCC 2136]


200
YP_148187
56420869
glucose-6-phosphate 1-dehydrogenase [Geobacillus





kaustophilus HTA426]


201
ZP_006 . . .
71368421
Glucose-6-phosphate dehydrogenase [Nocardioides sp. JS614]
















TABLE 46







Examples of 6-phosphogluconate dehydrogenase polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_500938
50546937
hypothetical protein [Yarrowia lipolytica].


2
XP_458726
50420381
hypothetical protein DEHA0D06820g [Debaryomyces





hansenii CBS767]


3
XP_451408
50302941
unnamed protein product [Kluyveromyces lactis]


4
O13287
3334110
6-phosphogluconate dehydrogenase, decarboxylating


5
XP_722227
68467588
hypothetical protein CaO19_5024 [Candida albicans SC5314]


6
NP_012053
6321977
6-phosphogluconate dehydrogenase (decarboxylating),





catalyzes an NADPH regenerating reaction in the pentose





phosphate pathway; required for growth on D-glucono-delta-





lactone and adaptation to oxidative stress; Gnd1p





[Saccharomyces cerevisiae]


7
AAO32396
28564035
GND1 [Saccharomyces bayanus]


8
XP_750696
70991695
6-phosphogluconate dehydrogenase, decarboxylating





[Aspergillus fumigatus Af293]


9
CAD80254
29409963
6-phosphogluconate dehydrogenase [Aspergillus niger]


10
XP_661558
67526993
hypothetical protein AN3954.2 [Aspergillus nidulans FGSC





A4]


11
AAO32456
28564155
GND1 [Saccharomyces servazzii]


12
AAO32497
28564385
GND1 [Saccharomyces castellii]


13
BAE57349
83767210
unnamed protein product [Aspergillus oryzae]


14
AAT92830
51013073
YGR256W [Saccharomyces cerevisiae]


15
XP_449923
50295024
hypothetical protein CAGL0M13343g [Candida glabrata





CBS138]


16
NP_985676
45198647
AFR129Wp [Eremothecium gossypii]


17
EAS35799
90306168
6-phosphogluconate dehydrogenase, decarboxylating





[Coccidioides immitis RS]


18
XP_758724
71014537
hypothetical protein UM02577.1 [Ustilago maydis 521]


19
O60037
12229635
6-phosphogluconate dehydrogenase, decarboxylating


20
XP_964959
85115938
hypothetical protein [Neurospora crassa OR74A]


21
XP_381287
46108458
hypothetical protein FG01111.1 [Gibberella zeae PH-1]


22
EAT76717
111055597
predicted protein [Phaeosphaeria nodorum SN15]


23
XP_369069
39975357
hypothetical protein MG00175.4 [Magnaporthe grisea 70-15]


24
XP_567793
58260766
phosphogluconate dehydrogenase (decarboxylating)





[Cryptococcus neoformans var. neoformans JEC21]


25
NP_595095
19111887
6-phosphogluconate dehydrogenase [Schizosaccharomyces





pombe 972h-]


26
EAQ92608
88185140
hypothetical protein CHGG_00843 [Chaetomium globosum





CBS 148.51]


27
T42523
11251352
probable phosphogluconate dehydrogenase (decarboxylating)





(EC 1.1.1.44) - fission yeast (Schizosaccharomyces pombe )





(fragment)


28
XP_781394
72005545
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating [Strongylocentrotus purpuratus]


29
BAD98151
63003720
6-phosphogluconate dehydrogenase [Ascidia sydneiensis





samea]


30
XP_625090
66547531
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating, partial [Apis mellifera]


31
CAG32303
53134115
hypothetical protein [Gallus gallus]


32
2PGD
999886
Chain, 6-Phosphogluconate Dehydrogenase (6-Pgdh)





(E.C.1.1.1.44)


33
NP_001 . . .
57164179
6-phosphogluconate dehydrogenase (decarboxylating) [Ovis





aries]


34
XP_911640
82896232
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating isoform 6 [Mus musculus]


35
BAE31577
74225286
unnamed protein product [Mus musculus]


36
AAX43359
61369608
phosphogluconate dehydrogenase [synthetic construct]


37
CAI95751
66347393
phosphogluconate dehydrogenase [Homo sapiens]


38
XP_993478
94374014
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating isoform 4 [Mus musculus]


39
AAH11329
15030150
Phosphogluconate dehydrogenase [Mus musculus]


40
AAI02179
73586529
LOC514939 protein [Bos taurus]


41
AAA75302
984325
phosphogluconate dehydrogenase [Homo sapiens]


42
AAH59958
37747616
MGC68486 protein [Xenopus laevis]


43
ZP_005 . . .
67931108
6-phosphogluconate dehydrogenase, decarboxylating





[Solibacter usitatus Ellin6076]


44
EAT42557
108878332
6-phosphogluconate dehydrogenase [Aedes aegypti]


45
XP_535411
73950940
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating isoform 1 [Canis familiaris]


46
XP_313091
58384192
ENSANGP00000012857 [Anopheles gambiae str. PEST]


47
CAG07546
47228814
unnamed protein product [Tetraodon nigroviridis]


48
YP_007316
46445951
6-phosphogluconate dehydrogenase [Candidatus





Protochlamydia amoebophila UWE25]


49
NP_998717
47087205
phosphogluconate hydrogenase isoform 2 [Danio rerio]


50
XP_972051
91094851
PREDICTED: similar to phosphogluconate hydrogenase





isoform 2 [Tribolium castaneum]


51
CAE70848
39594980
Hypothetical protein CBG17632 [Caenorhabditis briggsae]


52
XP_001 . . .
94372948
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating isoform 9 [Mus musculus]


53
NP_998618
47087439
phosphogluconate hydrogenase isoform 1 [Danio rerio]


54
AAH95571
63102189
Pgd protein [Danio rerio]


55
XP_993446
94374016
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating isoform 3 [Mus musculus]


56
EAL31500
54642755
GA17642-PA [Drosophila pseudoobscura]


57
Q17761
74962414
6-phosphogluconate dehydrogenase, decarboxylating


58
P41573
1168233
6-phosphogluconate dehydrogenase, decarboxylating


59
AAL90185
19528141
AT26455p [Drosophila melanogaster]


60
NP_476860
24639279
Phosphogluconate dehydrogenase CG3724-PA [Drosophila





melanogaster]


61
NP_001 . . .
114053253
6-phosphogluconate dehydrogenase [Bombyx mori]


62
P41570
1168228
6-phosphogluconate dehydrogenase, decarboxylating


63
CAJ43391
95140247
6-phosphogluconate dehydrogenase [Bactrocera oleae]


64
CAJ43390
95140245
6-phosphogluconate dehydrogenase [Ceratitis capitata]


65
AAP92648
33086672
Cc2-27 [Rattus norvegicus]


66
YP_661682
109898427
6-phosphogluconate dehydrogenase, decarboxylating





[Pseudoalteromonas atlantica T6c]


67
XP_592859
76637462
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating [Bos taurus]


68
YP_526109
90020282
6-phosphogluconate dehydrogenase, decarboxylating





[Saccharophagus degradans 2-40]


69
ZP_001 . . .
53733078
COG0362: 6-phosphogluconate dehydrogenase [Haemophilus





influenzae R2846]


70
NP_761502
27365974
6-phosphogluconate dehydrogenase [Vibrio vulnificus





CMCP6]


71
YP_391484
78485559
6-phosphogluconate dehydrogenase, decarboxylating





[Thiomicrospira crunogena XCL-2]


72
YP_248262
68249150
6-phosphogluconate dehydrogenase [Haemophilus influenzae





86-028NP]


73
NP_934400
37679791
6-phosphogluconate dehydrogenase [Vibrio vulnificus YJ016]


74
ZP_007 . . .
75857693
COG0362: 6-phosphogluconate dehydrogenase [Vibrio sp.





Ex25]


75
NP_798087
28898482
6-phosphogluconate dehydrogenase [Vibrio parahaemolyticus





RIMD 2210633]


76
YP_206428
59713653
6-phosphogluconate dehydrogenase [Vibrio fischeri ES114]


77
ZP_001 . . .
53733322
COG0362: 6-phosphogluconate dehydrogenase [Haemophilus





influenzae R2866]


78
ZP_012 . . .
91224436
6-phosphogluconate dehydrogenase [Vibrio alginolyticus





12G01]


79
AAB20377
239383
6-phosphogluconate dehydrogenase [sheep, Peptide, 466 aa]


80
ZP_010 . . .
86145883
6-phosphogluconate dehydrogenase [Vibrio sp. MED222]


81
ZP_007 . . .
75432781
Phosphogluconate dehydrogenase (decarboxylating)





[Actinobacillus succinogenes 130Z]


82
ZP_001 . . .
46143450
COG0362: 6-phosphogluconate dehydrogenase





[Actinobacillus pleuropneumoniae serovar 1 str. 4074]


83
ZP_012 . . .
90578957
6-phosphogluconate dehydrogenase [Vibrio angustum S14]


84
YP_087205
52424068
6-phosphogluconate dehydrogenase [Mannheimia





succiniciproducens MBEL55E]


85
ZP_011 . . .
89073009
6-phosphogluconate dehydrogenase [Photobacterium sp.





SKA34]


86
NP_273081
15675963
6-phosphogluconate dehydrogenase [Neisseria meningitidis





MC58]


87
ZP_007 . . .
75825242
COG0362: 6-phosphogluconate dehydrogenase [Vibrio





cholerae O395]


88
ZP_007 . . .
75822319
COG0362: 6-phosphogluconate dehydrogenase [Vibrio





cholerae RC385]


89
ZP_007 . . .
75831146
COG0362: 6-phosphogluconate dehydrogenase [Vibrio





cholerae MO10]


90
YP_719859
113461790
6-phosphogluconate dehydrogenase [Haemophilus somnus





129PT]


91
ZP_012 . . .
90411828
6-phosphogluconate dehydrogenase [Photobacterium





profundum 3TCK]


92
YP_129657
54308637
6-phosphogluconate dehydrogenase [Photobacterium





profundum SS9]


93
ZP_001 . . .
53728695
COG0362: 6-phosphogluconate dehydrogenase [Haemophilus





somnus 2336]


94
BAD36766
51241757
6-phosphogluconate dehydrogenase [Cyanidioschyzon





merolae]


95
P70718
2492494
6-phosphogluconate dehydrogenase, decarboxylating


96
XP_642122
66816225
6-phosphogluconate dehydrogenase (decarboxylating)





[Dictyostelium discoideum AX4]


97
Q7VMX4
71152205
6-phosphogluconate dehydrogenase, decarboxylating


98
NP_283102
15793280
6-phosphogluconate dehydrogenase [Neisseria meningitidis





Z2491]


99
NP_246493
15603419
6-phosphogluconate dehydrogenase [Pasteurella multocida





subsp. multocida str. Pm70]


100
AAO19943
27573087
6-phosphogluconate dehydrogenase, decarboxylating





[Neisseria gonorrhoeae]


101
AAO19944
27573089
6-phosphogluconate dehydrogenase, decarboxylating





[Neisseria gonorrhoeae]


102
YP_208939
59802227
6-phosphogluconate dehydrogenase [Neisseria gonorrhoeae





FA 1090]


103
AAO19934
27573069
6-phosphogluconate dehydrogenase, decarboxylating





[Neisseria gonorrhoeae]


104
AAO19942
27573085
6-phosphogluconate dehydrogenase, decarboxylating





[Neisseria gonorrhoeae]


105
ZP_013 . . .
106881674
6-phosphogluconate dehydrogenase, decarboxylating





[Psychromonas ingrahamii 37]


106
XP_515670
55599346
PREDICTED: similar to 6-phosphogluconate dehydrogenase,





decarboxylating [Pan troglodytes]


107
ZP_010 . . .
87309497
6-phosphogluconate dehydrogenase [Blastopirellula marina





DSM 3645]


108
NP_865160
32472166
6-phosphogluconate dehydrogenase [Rhodopirellula baltica





SH 1]


109
AAW29923
56788282
6-phosphogluconate dehydrogenase [Mannheimia





haemolytica]


110
AAW29924
56788284
6-phosphogluconate dehydrogenase [Mannheimia glucosida]


111
AAW29925
56788286
6-phosphogluconate dehydrogenase [Pasteurella trehalosi]


112
NP_218771
15639322
6-phosphogluconate dehydrogenase [Treponema pallidum





subsp. pallidum str. Nichols]


113
YP_148197
56420879
6-phosphogluconate dehydrogenase [Geobacillus kaustophilus





HTA426]


114
YP_356348
77918533
probable phosphogluconate dehydrogenase (decarboxylating)





[Pelobacter carbinolicus DSM 2380]


115
NP_390267
50812264
6-phosphogluconate dehydrogenase [Bacillus subtilis subsp.





subtilis str. 168]


116
YP_092134
52786305
6-phosphogluconate dehydrogenase [Bacillus licheniformis





ATCC 14580]


117
ZP_011 . . .
89099010
6-phosphogluconate dehydrogenase [Bacillus sp. NRRL B-





14911]


118
NP_691106
23097640
6-phosphogluconate dehydrogenase [Oceanobacillus iheyensis





HTE831]


119
YP_219832
62185047
6-phosphogluconate dehydrogenase [Chlamydophila abortus





S26/3]


120
ZP_002 . . .
47565365
6-phosphogluconate dehydrogenase, decarboxylating [Bacillus





cereus G9241]


121
YP_026451
49183199
6-phosphogluconate dehydrogenase [Bacillus anthracis str.





Sterne]


122
YP_034514
49476731
6-phosphogluconate dehydrogenase [Bacillus thuringiensis





serovar konkukian str. 97-27]


123
YP_081773
52145056
6-phosphogluconate dehydrogenase [Bacillus cereus E33L]


124
YP_515493
89898383
6-phosphogluconate dehydrogenase [Chlamydophila felis





Fe/C-56]


125
NP_814782
29375628
6-phosphogluconate dehydrogenase [Enterococcus faecalis





V583]


126
ZP_003 . . .
65317607
COG0362: 6-phosphogluconate dehydrogenase [Bacillus





anthracis str. A2012]


127
YP_175422
56963691
6-phosphogluconate dehydrogenase [Bacillus clausii KSM-





K16]


128
ZP_006 . . .
69247351
6-phosphogluconate dehydrogenase, decarboxylating





[Enterococcus faecium DO]


129
NP_810135
29346632
6-phosphogluconate dehydrogenase [Bacteroides





thetaiotaomicron VPI-5482]


130
NP_829300
29840194
6-phosphogluconate dehydrogenase [Chlamydophila caviae





GPIC]


131
AAL76325
18644678
6-phosphogluconate dehydrogenase [Porphyra yezoensis]


132
YP_546705
91776949
6-phosphogluconate dehydrogenase, decarboxylating





[Methylobacillus flagellatus KT]


133
ZP_004 . . .
67546118
6-phosphogluconate dehydrogenase, decarboxylating





[Burkholderia vietnamiensis G4]


134
Q9CHU6
18202802
6-phosphogluconate dehydrogenase, decarboxylating


135
ZP_006 . . .
74014955
6-phosphogluconate dehydrogenase, decarboxylating





[Burkholderia ambifaria AMMD]


136
YP_372936
78063028
6-phosphogluconate dehydrogenase [Burkholderia sp. 383]


137
YP_624314
107026803
6-phosphogluconate dehydrogenase, decarboxylating





[Burkholderia cenocepacia AU 1054]


138
NP_928851
37525507
6-phosphogluconate dehydrogenase [Photorhabdus





luminescens subsp. laumondii TTO1]


139
ZP_002 . . .
47095960
6-phosphogluconate dehydrogenase, decarboxylating [Listeria





monocytogenes str. 1/2a F6854]


140
YP_438830
83717630
6-phosphogluconate dehydrogenase, decarboxylating





[Burkholderia thailandensis E264]


141
P96789
8134294
6-phosphogluconate dehydrogenase, decarboxylating


142
NP_924063
37520686
6-phosphogluconate dehydrogenase [Gloeobacter violaceus





PCC 7421]


143
AAA24207
146938
6-phosphogluconate dehydrogenase


144
ZP_009 . . .
84360352
COG0362: 6-phosphogluconate dehydrogenase [Burkholderia





dolosa AUO158]


145
YP_335987
76817886
6-phosphogluconate dehydrogenase [Burkholderia





pseudomallei 1710b]


146
AAA24495
147501
6-phosphogluconate dehydrogenase


147
NP_310857
15832084
6-phosphogluconate dehydrogenase [Escherichia coli





O157:H7 str. Sakai]


148
ZP_009 . . .
83571257
COG0362: 6-phosphogluconate dehydrogenase [Shigella





dysenteriae 1012]


149
ZP_007 . . .
75229110
COG0362: 6-phosphogluconate dehydrogenase [Escherichia





coli B7A]


150
ZP_013 . . .
100915196
hypothetical protein Bmal10_03003493 [Burkholderia mallei





10399]


151
AAG35219
11464518
6-phosphogluconate dehydrogenase [Escherichia coli]


152
ZP_013 . . .
100236192
hypothetical protein Bpse4_03000697 [Burkholderia





pseudomallei 406e]


153
YP_669972
110642242
6-phosphogluconate dehydrogenase, decarboxylating





[Escherichia coli 536]


154
ZP_013 . . .
100062231
hypothetical protein BpseP_03002198 [Burkholderia





pseudomallei Pasteur]


155
YP_114383
53803994
6-phosphogluconate dehydrogenase [Methylococcus





capsulatus str. Bath]


156
AAA24208
146940
6-phosphogluconate dehydrogenase


157
YP_310991
74312572
gluconate-6-phosphate dehydrogenase, decarboxylating





[Shigella sonnei Ss046]


158
ZP_003 . . .
48870455
COG0362: 6-phosphogluconate dehydrogenase [Pediococcus





pentosaceus ATCC 25745]


159
ZP_007 . . .
75514070
COG0362: 6-phosphogluconate dehydrogenase [Escherichia





coli 53638]


160
YP_049550
50120383
6-phosphogluconate dehydrogenase [Erwinia carotovora





subsp. atroseptica SCRI1043]


161
AP_002630
89108850
gluconate-6-phosphate dehydrogenase, decarboxylating





[Escherichia coli W3110]


162
ZP_007 . . .
75259178
COG0362: 6-phosphogluconate dehydrogenase [Escherichia





coli E22]


163
YP_541301
91211315
6-phosphogluconate dehydrogenase, decarboxylating





[Escherichia coli UTI89]


164
YP_013993
46907604
6-phosphogluconate dehydrogenase [Listeria monocytogenes





str. 4b F2365]


165
YP_403788
82777439
gluconate-6-phosphate dehydrogenase [Shigella dysenteriae





Sd197]


166
ZP_009 . . .
83588030
COG0362: 6-phosphogluconate dehydrogenase [Escherichia





coli 101-1]


167
AAD50492
5739470
6-phosphogluconate dehydrogenase Gnd [Escherichia coli]


168
ZP_006 . . .
75177157
COG0362: 6-phosphogluconate dehydrogenase [Shigella





boydii BS512]


169
AAA24209
146942
6-phosphogluconate dehydrogenase


170
AAG35221
11464522
6-phosphogluconate dehydrogenase [Escherichia coli]


171
ZP_007 . . .
75186836
COG0362: 6-phosphogluconate dehydrogenase [Escherichia





coli E24377A]


172
YP_689521
110806001
gluconate-6-phosphate dehydrogenase [Shigella flexneri 5 str.





8401]


173
ZP_008 . . .
77959279
COG0362: 6-phosphogluconate dehydrogenase [Yersinia





bercovieri ATCC 43970]


174
AAG35224
11464528
6-phosphogluconate dehydrogenase [Escherichia coli]


175
ZP_007 . . .
77636293
COG0362: 6-phosphogluconate dehydrogenase [Yersinia





pestis Angola]


176
ZP_008 . . .
77962467
COG0362: 6-phosphogluconate dehydrogenase [Yersinia





mollaretii ATCC 43969]


177
ZP_008 . . .
77978861
COG0362: 6-phosphogluconate dehydrogenase [Yersinia





intermedia ATCC 29909]


178
AAG35218
11464516
6-phosphogluconate dehydrogenase [Escherichia coli]


179
BAA77736
4867927
6-phosphogluconate dehydrogenase [Escherichia coli]


180
AAA24490
147491
6-phosphogluconate dehydrogenase


181
YP_648367
108812600
6-phosphogluconate dehydrogenase, decarboxylating





[Yersinia pestis Nepal516]


182
NP_669932
22126509
6-phosphogluconate dehydrogenase [Yersinia pestis KIM]


183
AAA23918
146232
6-phosphogluconate dehydrogenase (EC 1.1.1.44)


184
CAJ71042
91203389
strongly similar to 6-phosphogluconate dehydrogenase





(decarboxylating) [Candidatus Kuenenia stuttgartiensis]


185
AAA24206
146936
6-phosphogluconate dehydrogenase


186
AAA24494
147499
6-phosphogluconate dehydrogenase


187
AAA24492
147495
6-phosphogluconate dehydrogenase


188
YP_099135
53713143
6-phosphogluconate dehydrogenase [Bacteroides fragilis





YCH46]


189
AAA23925
146246
6-phosphogluconate dehydrogenase


190
YP_211552
60681408
6-phosphogluconate dehydrogenase [Bacteroides fragilis





NCTC 9343]


191
AAV74381
56122509
Gnd [Escherichia coli]


192
NP_992794
45441255
6-phosphogluconate dehydrogenase [Yersinia pestis biovar





Microtus str. 91001]


193
YP_650749
108806833
6-phosphogluconate dehydrogenase, decarboxylating





[Yersinia pestis Antiqua]


194
NP_876643
33241702
6-phosphogluconate dehydrogenase [Chlamydophila





pneumoniae TW-183]


195
NP_357929
15902379
6-phosphogluconate dehydrogenase [Streptococcus





pneumoniae R6]


196
ZP_014 . . .
111658214
hypothetical protein SpneT_02000606 [Streptococcus





pneumoniae TIGR4]


197
NP_782446
28211502
6-phosphogluconate dehydrogenase [Clostridium tetani E88]


198
AAG35223
11464526
6-phosphogluconate dehydrogenase [Escherichia coli]


199
AAA24493
147497
6-phosphogluconate dehydrogenase


200
ZP_007 . . .
75214880
COG0362: 6-phosphogluconate dehydrogenase [Escherichia





coli E110019]
















TABLE 47







Examples of Fructose 1,6 bisphosphatase polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_500111
50545147
hypothetical protein [Yarrowia lipolytica].


2
AAP85294
32492043
fructose-1,6-bisphosphatase [Yarrowia lipolytica]


3
XP_460410
50423651
hypothetical protein DEHA0F01309g [Debaryomyces





hansenii CBS767]


4
CAC69139
15528447
putative fructose-1,6-bisphosphatase [Pichia anomala]


5
XP_447425
50289987
hypothetical protein CAGL0I04048g [Candida glabrata





CBS138]


6
NP_986140
45199111
AFR593Cp [Eremothecium gossypii]


7
XP_454003
50308005
F16P_KLULA [Kluyveromyces lactis]


8
EAT78213
111057093
predicted protein [Phaeosphaeria nodorum SN15]


9
XP_710934
68490480
fructose-1,6-bisphosphatase [Candida albicans SC5314]


10
AAT92835
51013083
YLR377C [Saccharomyces cerevisiae]


11
XP_364050
39954137
hypothetical protein MG08895.4 [Magnaporthe grisea 70-15]


12
NP_001 . . .
68006542
fructose-1,6-bisphosphatase [Schizosaccharomyces pombe





972h-]


13
NP_595083
19111875
hypothetical protein SPBC1198.14c [Schizosaccharomyces





pombe 972h-]


14
XP_751698
70993702
fructose-1,6-bisphosphatase [Aspergillus fumigatus Af293]


15
XP_447010
50289161
unnamed protein product [Candida glabrata]


16
BAE58185
83768046
unnamed protein product [Aspergillus oryzae]


17
EAQ84924
88177456
conserved hypothetical protein [Chaetomium globosum CBS





148.51]


18
AAF34693
6980006
fructose 1,6-bisphosphatase [Candida albicans]


19
BAB12208
9955389
fructose-1,6-bisphosphatase [Aspergillus oryzae]


20
XP_663208
67538868
hypothetical protein AN5604.2 [Aspergillus nidulans FGSC





A4]


21
XP_389456
46134281
conserved hypothetical protein [Gibberella zeae PH-1]


22
XP_960423
85097320
hypothetical protein [Neurospora crassa OR74A]


23
EAS36192
90306561
fructose-1,6-bisphosphatase [Coccidioides immitis RS]


24
XP_566475
58258125
fructose-bisphosphatase [Cryptococcus neoformans var.





neoformans JEC21]


25
XP_758850
71015920
hypothetical protein UM02703.1 [Ustilago maydis 521]


26
P14766
119748
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase)


27
AAZ86538
73811203
fructose 1,6-bisphosphatase [Brassica rapa subsp. pekinensis]


28
Q9MA79
75312318
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase)


29
Q9SDL8
75313310
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase)


30
BAD81916
56785198
fructose-1,6-bisphosphatase [Oryza sativa (japonica cultivar-





group)]


31
P46267
1169585
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase)


32
P46276
1169586
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase) (CY-F1)


33
Q8RW99
75303233
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase)


34
Q43139
76363515
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase)


35
CAB46084
5305145
fructose-1,6-bisphosphatase [Pisum sativum]


36
BAF06820
113534437
Os01g0866400 [Oryza sativa (japonica cultivar-group)]


37
Q42649
76789650
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase)


38
Q9XF47
75315047
Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-





bisphosphate 1-phosphohydrolase) (FBPase)


39
CAA61409
895909
fructose-1,6-bisphosphatase [Saccharum hybrid cultivar H65-





7052]


40
1906373A
444324
cytosolic fructose bisphosphatase


41
EAR87347
89289359
fructose-1,6-bisphosphatase family protein [Tetrahymena





thermophila SB210]


42
NP_915641
34908588
fructose-1,6-bisphosphatase [Oryza sativa (japonica cultivar-





group)]


43
XP_475314
50931573
putative fructose-1,6-bisphosphatase [Oryza sativa (japonica





cultivar-group)]


44
NP_491004
17508131
K07A3.1 [Caenorhabditis elegans]


45
XP_782411
72013871
PREDICTED: similar to fructose-1,6-bisphosphatase 1, like





[Strongylocentrotus purpuratus]


46
CAE60538
39595500
Hypothetical protein CBG04165 [Caenorhabditis briggsae]


47
NP_610001
19921562
fructose-1,6-bisphosphatase CG31692-PA, isoform A





[Drosophila melanogaster]


48
NP_724223
45550998
fructose-1,6-bisphosphatase CG31692-PB, isoform B





[Drosophila melanogaster]


49
XP_319937
58393257
ENSANGP00000016841 [Anopheles gambiae str. PEST]


50
AAN31471
23394363
fructose-1 6-biphosphatase [Phytophthora infestans]


51
XP_425040
50762393
PREDICTED: similar to fructose 1,6-bisphosphatase [Gallus





gallus]


52
EAT47721
108883496
fructose-1,6-bisphosphatase [Aedes aegypti]


53
EAT47722
108883497
fructose-1,6-bisphosphatase [Aedes aegypti]


54
AAH53784
32450356
Fbp-prov protein [Xenopus laevis]


55
YP_001659
45657573
fructose-1,6-bisphosphatase [Leptospira interrogans serovar





Copenhageni str. Fiocruz L1-130]


56
NP_989145
45361017
Fructose-1,6-bisphosphatase [Xenopus tropicalis]


57
1YZ0B
62738852
Chain B, R-State Amp Complex Reveals Initial Steps Of The





Quaternary Transition Of Fructose-1,6-Bisphosphatase


58
1Q9DB
39654661
Chain B, Fructose-1,6-Bisphosphatase Complexed With A





New Allosteric Site Inhibitor (I-State)


59
NP_999144
47522784
fructose 1,6-bisphosphatase [Sus scrofa]


60
EAL32807
54644065
GA16400-PA [Drosophila pseudoobscura]


61
XP_848306
73946392
PREDICTED: similar to fructose-1,6-bisphosphatase 1





isoform 3 [Canis familiaris]


62
1FJ9B
11514534
Chain B, Fructose-1,6-Bisphosphatase (Mutant Y57w)





ProductsZNAMP Complex (T-State)


63
1LEVF
24987566
Chain F, Porcine Kidney Fructose-1,6-Bisphosphatase





Complexed With An Amp-Site Inhibitor


64
1BK4A
6729708
Chain A, Crystal Structure Of Rabbit Liver Fructose-1,6-





Bisphosphatase At 2.3 Angstrom Resolution


65
Q3SZB7
110808224
Fructose-1,6-bisphosphatase 1 (D-fructose-1,6-bisphosphate





1-phosphohydrolase 1) (FBPase 1)


66
AAA41131
310111
fructose-biphosphatase


67
P46275
2506391
Fructose-1,6-bisphosphatase, chloroplast precursor (D-





fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)


68
2F3HB
99032142
Chain B, Mechanism Of Displacement Of A Catalytically





Essential Loop From The Active Site Of Fructose-1,6-





Bisphosphatase


69
NP_036690
51036635
fructose-1,6-biphosphatase 1 [Rattus norvegicus]


70
AAC25597
3288991
fructose-1,6-bisphosphatase [Sus scrofa]


71
XP_967802
91077758
PREDICTED: similar to CG31692-PA, isoform A [Tribolium





castaneum]


72
AAK59929
14318171
fructose-1,6-bisphosphatase [Pisum sativum]


73
1DCUD
6730314
Chain D, Redox Signaling In The Chloroplast: Structure Of





Oxidized Pea Fructose-1,6-Bisphosphate Phosphatase


74
1DBZD
6730306
Chain D, C153s Mutant Of Pea Fructose-1,6-Bisphosphatase


75
CAB39759
4539148
fructose-1,6-bisphosphatase [Pisum sativum]


76
P09199
20141075
Fructose-1,6-bisphosphatase 1 (D-fructose-1,6-bisphosphate





1-phosphohydrolase 1) (FBPase 1)


77
CAA48719
20717
fructose-bisphosphatase [Pisum sativum]


78
1FPIB
1633402
Chain B, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-





Bisphosphate 1-Phosphohydrolase) Complexed With Amp,





2,5-Anhydro-D-Glucitol-1,6-Bisphosphate And Potassium





Ions (100 Mm)


79
AAB30523
546354
fructose-1,6-biphosphatase, FBPase {EC 3.1.3.11} [Pisum





sativum = peas, Lincoln, Peptide Chloroplast, 357 aa]


80
1KZ8F
24987484
Chain F, Crystal Structure Of Porcine Fructose-1,6-





Bisphosphatase Complexed With A Novel Allosteric-Site





Inhibitor


81
AAW25416
56754457
SJCHGC06706 protein [Schistosoma japonicum]


82
1FRPB
809402
Chain B, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-





Bisphosphate 1-Phosphohydrolase) (E.C.3.1.3.11) Complexed





With Fructose-2,6-Bisphosphate, Adenosine Monophosphate





(Amp), And Zinc


83
XP_425039
50762391
PREDICTED: similar to fructose-1,6-bisphosphatase [Gallus





gallus]


84
NP_998297
47085885
fructose-1,6-bisphosphatase 1 [Danio rerio]


85
1RDZB
1942591
Chain B, T-State Structure Of The Arg 243 To Ala Mutant Of





Pig Kidney Fructose 1,6-Bisphosphatase Expressed In E. Coli


86
1FSAB
2554913
Chain B, The T-State Structure Of Lys 42 To Ala Mutant Of





The Pig Kidney Fructose 1,6-Bisphosphatase Expressed In E. Coli


87
BAE28940
74146344
unnamed protein product [Mus musculus]


88
CAG05216
47228396
unnamed protein product [Tetraodon nigroviridis]


89
NP_956236
41053949
fructose-1,6-bisphosphatase 1, like [Danio rerio]


90
Q07204
585118
Fructose-1,6-bisphosphatase, chloroplast precursor (D-





fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)


91
BAF11578
113548135
Os03g0267300 [Oryza sativa (japonica cultivar-group)]


92
2FIXL
90109451
Chain L, Structure Of Human Liver Fbpase Complexed With





Potent Benzoxazole Allosteric Inhibitiors


93
2FHYL
90109424
Chain L, Structure Of Human Liver Fpbase Complexed With





A Novel Benzoxazole As Allosteric Inhibitor


94
XP_001 . . .
109112377
PREDICTED: fructose-1,6-bisphosphatase 1 isoform 2





[Macaca mulatta]


95
1FTAD
1311149
Chain D, Fructose-1,6-Bisphosphatase(D-Fructose-1,6-





Bisphosphate, 1-Phosphohydrolase) (E.C.3.1.3.11) Complexed





With The Allosteric Inhibitor Amp


96
CAH72692
55662224
fructose-1,6-bisphosphatase 1 [Homo sapiens]


97
CAG08190
47221528
unnamed protein product [Tetraodon nigroviridis]


98
XP_533504
73946534
PREDICTED: similar to Fructose-1,6-bisphosphatase isozyme





2 (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)





[Canis familiaris]


99
AAC25774
3293553
fructose-1,6-bisphosphatase [Homo sapiens]


100
AAA35817
182311
fructose-1,6-bisphosphatase


101
AAD12243
4218951
fructose-1,6-bisphosphatase precursor [Brassica napus]


102
NP_001 . . .
114051459
hypothetical protein LOC514066 [Bos taurus]


103
P09195
119745
Fructose-1,6-bisphosphatase, chloroplast precursor (D-





fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)


104
NP_001 . . .
57524507
hypothetical protein LOC445505 [Danio rerio]


105
NP_001 . . .
114051287
fructose-1,6-bisphosphatase [Bombyx mori]


106
NP_001 . . .
73853862
hypothetical protein LOC613108 [Xenopus tropicalis]


107
AAD25541
4585576
fructose-1,6-bisphosphatase precursor [Solanum tuberosum]


108
Q9N0J6
75067927
Fructose-1,6-bisphosphatase isozyme 2 (D-fructose-1,6-





bisphosphate 1-phosphohydrolase 2) (FBPase 2)


109
AAN31884
23397203
putative fructose-bisphosphatase precursor [Arabidopsis





thaliana]


110
AAH81229
51703601
Unknown (protein for MGC: 85456) [Xenopus laevis]


111
P22418
3915687
Fructose-1,6-bisphosphatase, chloroplast precursor (D-





fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)


112
CAA41154
11242
fructose-bisphosphatase [Arabidopsis thaliana]


113
XP_001 . . .
109112375
PREDICTED: fructose-1,6-bisphosphatase 1 isoform 1





[Macaca mulatta]


114
P70695
76363514
Fructose-1,6-bisphosphatase isozyme 2 (D-fructose-1,6-





bisphosphate 1-phosphohydrolase 2) (FBPase 2) (RAE-30)


115
CAG08189
47221527
unnamed protein product [Tetraodon nigroviridis]


116
AAI13633
109731177
Fructose-1,6-bisphosphatase 2 [Homo sapiens]


117
1SPID
999624
Chain D, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-





Bisphosphate 1-Phosphohydrolase) (E.C.3.1.3.11)


118
AAF72973
8118281
fructose-1,6-bisphosphatase [Zaocys dhumnades]


119
AAH12720
15215255
Fbp2 protein [Mus musculus]


120
O00757
76789651
Fructose-1,6-bisphosphatase isozyme 2 (D-fructose-1,6-





bisphosphate 1-phosphohydrolase 2) (FBPase 2)


121
XP_827196
71745132
fructose-1,6-bisphosphate cytosolic [Trypanosoma brucei





TREU927]


122
Q9Z1N1
76364186
Fructose-1,6-bisphosphatase isozyme 2 (D-fructose-1,6-





bisphosphate 1-phosphohydrolase 2) (FBPase 2)


123
BAE40306
74212301
unnamed protein product [Mus musculus]


124
CAC70747
15718373
fructose-1,6-bisphosphatase [Trypanosoma brucei]


125
NP_032020
6679761
fructose bisphosphatase 2 [Mus musculus]


126
AAP79192
32307574
fructose-1,6 bisphosphatase [Bigelowiella natans]


127
ZP_010 . . .
86130901
fructose-1,6-bisphosphatase [Cellulophaga sp. MED134]


128
YP_422024
83311760
Fructose-1,6-bisphosphatase [Magnetospirillum magneticum





AMB-1]


129
YP_679484
110639275
fructose-1,6-bisphosphatase [Cytophaga hutchinsonii ATCC





33406]


130
ZP_000 . . .
23014308
COG0158: Fructose-1,6-bisphosphatase [Magnetospirillum





magnetotacticum MS-1]


131
XP_888627
76363832
Leishmania major strain Friedlin cytosolic fructose-1,6-





bisphosphatase [Leishmania major strain Friedlin]


132
ZP_009 . . .
83855881
fructose-1,6-bisphosphatase [Croceibacter atlanticus





HTCC2559]


133
YP_437516
83649081
Fructose-1,6-bisphosphatase [Hahella chejuensis KCTC 2396]


134
ZP_011 . . .
88711300
fructose-1,6-bisphosphatase [Flavobacteriales bacterium





HTCC2170]


135
CAC82800
16519317
fructose 1,6-bisphosphatase [Galdieria sulphuraria]


136
ZP_012 . . .
91215105
fructose-1,6-bisphosphatase [Psychroflexus torquis ATCC





700755]


137
ZP_012 . . .
90591576
Inositol phosphatase/fructose-1,6-bisphosphatase





[Flavobacterium johnsoniae UW101]


138
XP_793452
72046390
PREDICTED: similar to fructose-1,6-bisphosphatase 1, like





[Strongylocentrotus purpuratus]


139
CAJ72223
91202584
strongly similar to fructose-1,6-bisphosphatase [Candidatus





Kuenenia stuttgartiensis]


140
ZP_011 . . .
88804197
fructose-1,6-bisphosphatase [Robiginitalea biformata





HTCC2501]


141
YP_445598
83815956
fructose-1,6-bisphosphatase [Salinibacter ruber DSM 13855]


142
ZP_007 . . .
75815977
COG0158: Fructose-1,6-bisphosphatase [Vibrio cholerae V52]


143
ZP_011 . . .
88802508
fructose-1,6-bisphosphatase [Polaribacter irgensii 23-P]


144
ZP_007 . . .
75827798
COG0158: Fructose-1,6-bisphosphatase [Vibrio cholerae





O395]


145
ZP_011 . . .
88797163
Fructose-1,6-bisphosphatase [Reinekea sp. MED297]


146
ZP_005 . . .
68553442
Inositol phosphatase/fructose-1,6-bisphosphatase





[Prosthecochloris aestuarii DSM 271]


147
ZP_007 . . .
75830525
COG0158: Fructose-1,6-bisphosphatase [Vibrio cholerae





MO10]


148
Q42796
2494415
Fructose-1,6-bisphosphatase, chloroplast precursor (D-





fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)


149
ZP_007 . . .
75822783
COG0158: Fructose-1,6-bisphosphatase [Vibrio cholerae





RC385]


150
NP_933227
37678618
fructose-1,6-bisphosphatase [Vibrio vulnificus YJ016]


151
XP_812636
71423971
fructose-1,6-bisphosphatase, cytosolic [Trypanosoma cruzi





strain CL Brener]


152
ZP_006 . . .
71480926
Inositol phosphatase/fructose-1,6-bisphosphatase





[Prosthecochloris vibrioformis DSM 265]


153
ZP_007 . . .
75854570
COG0158: Fructose-1,6-bisphosphatase [Vibrio sp. Ex25]


154
NP_931714
37528369
fructose-1,6-bisphosphatase [Photorhabdus luminescens





subsp. laumondii TTO1]


155
XP_805839
71406635
fructose-1,6-bisphosphatase, cytosolic [Trypanosoma cruzi





strain CL Brener]


156
YP_374392
78186349
fructose-1,6-bisphosphatase [Pelodictyon luteolum DSM 273]


157
NP_902097
34497882
fructose-1,6-bisphosphatase [Chromobacterium violaceum





ATCC 12472]


158
XP_646323
66825937
D-fructose-1,6-bisphosphate 1-phosphohydrolase





[Dictyostelium discoideum AX4]


159
ZP_010 . . .
86147594
fructose-1,6-bisphosphatase [Vibrio sp. MED222]


160
NP_796691
28897086
fructose-1,6-bisphosphatase [Vibrio parahaemolyticus RIMD





2210633]


161
YP_052014
50122847
fructose-1,6-bisphosphatase [Erwinia carotovora subsp.





atroseptica SCRI1043]


162
ZP_007 . . .
77634762
COG0158: Fructose-1,6-bisphosphatase [Yersinia pestis





Angola]


163
ZP_012 . . .
90406722
fructose-1,6-bisphosphatase [Psychromonas sp. CNPT3]


164
ZP_006 . . .
71549000
Inositol phosphatase/fructose-1,6-bisphosphatase





[Nitrosomonas eutropha C71]


165
ZP_013 . . .
106882698
Inositol phosphatase/fructose-1,6-bisphosphatase





[Psychromonas ingrahamii 37]


166
ZP_008 . . .
77973994
COG0158: Fructose-1,6-bisphosphatase [Yersinia





frederiksenii ATCC 33641]


167
ZP_012 . . .
90411963
fructose-1,6-bisphosphatase [Photobacterium profundum





3TCK]


168
ZP_005 . . .
67938188
Inositol phosphatase/fructose-1,6-bisphosphatase [Chlorobium





phaeobacteroides BS1]


169
NP_991956
45440417
fructose-1,6-bisphosphatase [Yersinia pestis biovar Microtus





str. 91001]


170
NP_840606
30248536
fructose-1,6-bisphosphatase [Nitrosomonas europaea ATCC





19718]


171
YP_649191
108813424
fructose-1,6-bisphosphatase [Yersinia pestis Nepal516]


172
ZP_010 . . .
86134593
fructose-1,6-bisphosphatase [Tenacibaculum sp. MED152]


173
ZP_012 . . .
94268582
Inositol phosphatase/fructose-1,6-bisphosphatase [delta





proteobacterium MLMS-1]


174
ZP_012 . . .
94264279
Inositol phosphatase/fructose-1,6-bisphosphatase [delta





proteobacterium MLMS-1]


175
ZP_005 . . .
67919158
Inositol phosphatase/fructose-1,6-bisphosphatase [Chlorobium





limicola DSM 245]


176
NP_661262
21673197
fructose-1,6-bisphosphatase [Chlorobium tepidum TLS]


177
YP_128618
54307598
fructose-1,6-bisphosphatase [Photobacterium profundum SS9]


178
YP_378918
78188580
fructose-1,6-bisphosphatase [Chlorobium chlorochromatii





CaD3]


179
ZP_005 . . .
68551142
Inositol phosphatase/fructose-1,6-bisphosphatase [Pelodictyon





phaeoclathratiforme BU-1]


180
YP_445968
83814754
fructose-1,6-bisphosphatase [Salinibacter ruber DSM 13855]


181
ZP_012 . . .
90580816
fructose-1,6-bisphosphatase [Vibrio angustum S14]


182
ZP_011 . . .
89075542
fructose-1,6-bisphosphatase [Photobacterium sp. SKA34]


183
YP_342093
77163568
fructose-1,6-bisphosphatase [Nitrosococcus oceani ATCC





19707]


184
ZP_009 . . .
84387793
fructose-1,6-bisphosphatase [Vibrio splendidus 12B01]


185
ZP_010 . . .
86141292
fructose-1,6-bisphosphatase [Flavobacterium sp. MED217]


186
ZP_005 . . .
67937321
Inositol phosphatase/fructose-1,6-bisphosphatase [Chlorobium





phaeobacteroides DSM 266]


187
ZP_012 . . .
91228829
fructose-1,6-bisphosphatase [Vibrio alginolyticus 12G01]


188
ZP_008 . . .
77961846
COG0158: Fructose-1,6-bisphosphatase [Yersinia mollaretii





ATCC 43969]


189
ZP_008 . . .
77977605
COG0158: Fructose-1,6-bisphosphatase [Yersinia intermedia





ATCC 29909]


190
YP_203647
59710871
fructose-1,6-bisphosphatase [Vibrio fischeri ES114]


191
ZP_013 . . .
110596824
Inositol phosphatase/fructose-1,6-bisphosphatase [Chlorobium





ferrooxidans DSM 13031]


192
YP_454036
85058334
fructose-1,6-bisphosphatase [Sodalis glossinidius str.





‘morsitans’]


193
ZP_001 . . .
32035025
COG0158: Fructose-1,6-bisphosphatase [Actinobacillus





pleuropneumoniae serovar 1 str. 4074]


194
YP_011058
46580250
fructose-1,6-bisphosphatase [Desulfovibrio vulgaris subsp.





vulgaris str. Hildenborough]


195
YP_219276
62182859
fructose-1,6-bisphosphatase [Salmonella enterica subsp.





enterica serovar Choleraesuis str. SC-B67]


196
YP_560077
91784871
Inositolphosphatase/fructose-1,6-bisphosphatase





[Burkholderia xenovorans LB400]


197
YP_316335
74318595
fructose-1,6-bisphosphatase [Thiobacillus denitrificans ATCC





25259]


198
YP_388561
78357112
fructose-1,6-bisphosphatase [Desulfovibrio desulfuricans





G20]


199
NP_313236
15834463
fructose-1,6-bisphosphatase [Escherichia coli O157:H7 str.





Sakai]


200
YP_313128
74314709
fructose-bisphosphatase [Shigella sonnei Ss046]


201
ZP_011 . . .
88801533
fructose-1,6-bisphosphatase [Polaribacter irgensii 23-P]
















TABLE 53







Examples of squalene epoxidase polypeptides










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
XP_503994
50553168
hypothetical protein [Yarrowia lipolytica].


2
EAS30670
90301039
hypothetical protein CIMG_06149 [Coccidioides immitis RS]


3
XP_753858
70998268
squalene monooxygenase Erg1 [Aspergillus fumigatus Af293]


4
XP_711894
68488538
squalene epoxidase [Candida albicans SC5314]


5
ABD48706
88697124
squalene epoxidase [Emericella nidulans]


6
XP_681020
67901528
hypothetical protein AN7751.2 [Aspergillus nidulans FGSC A4]


7
AAQ18215
33415411
squalene epoxidase [Trichophyton rubrum]


8
BAE62359
83772229
unnamed protein product [Aspergillus oryzae]


9
AAQ18216
61807216
squalene epoxidase [Trichophyton rubrum]


10
AAZ08563
70797544
squalene epoxidase [Trichophyton rubrum]


11
CAJ18281
90185988
squalene epoxidase [Hypocrea lixii]


12
XP_462160
50427105
hypothetical protein DEHA0G15202g [Debaryomyces hansenii





CBS767]


13
NP_011691
6321614
Squalene epoxidase, catalyzes the epoxidation of squalene to 2,3-





oxidosqualene; plays an essential role in the ergosterol-biosynthesis





pathway and is the specific target of the antifungal drug terbinafine;





Erg1p [Saccharomyces cerevisiae]


14
AAA34592
171471
squalene epoxidase


15
O13306
51704232
Squalene monooxygenase (Squalene epoxidase) (SE)


16
XP_455763
50311477
unnamed protein product [Kluyveromyces lactis]


17
XP_386391
46123675
hypothetical protein FG06215.1 [Gibberella zeae PH-1]


18
EAQ88139
88180671
hypothetical protein CHGG_04758 [Chaetomium globosum CBS





148.51]


19
XP_961806
85104779
hypothetical protein [Neurospora crassa OR74A]


20
XP_758545
71012984
hypothetical protein UM02398.1 [Ustilago maydis 521]


21
XP_369325
39975869
hypothetical protein MG06139.4 [Magnaporthe grisea 70-15]


22
XP_570092
58265872
squalene monooxygenase [Cryptococcus neoformans var.





neoformans JEC21]


23
Q9C1W3
51701448
Probable squalene monooxygenase (Squalene epoxidase) (SE)


24
EAT79729
111058609
hypothetical protein SNOG_12929 [Phaeosphaeria nodorum SN15]


25
CAG38355
108743007
squalene epoxidase [Aspergillus niger]


26
BAE73094
84579321
hypothetical protein [Macaca fascicularis]


27
EAU31524
114189824
hypothetical protein ATEG_08351 [Aspergillus terreus NIH2624]


28
NP_003120
62865635
squalene monooxygenase [Homo sapiens]


29
CAI46076
57997512
hypothetical protein [Homo sapiens]


30
BAE37374
74200967
unnamed protein product [Mus musculus]


31
XP_850640
73974448
PREDICTED: similar to squalene monooxygenase isoform 1 [Canis





familiaris]


32
Q75F69
51701415
Squalene monooxygenase (Squalene epoxidase) (SE)


33
AAS60234
45388098
squalene epoxidase 1 [Aspergillus fumigatus]


34
Q14534
12644414
Squalene monooxygenase (Squalene epoxidase) (SE)


35
XP_001 . . .
109087424
PREDICTED: similar to squalene monooxygenase [Macaca mulatta]


36
AAH97330
66911977
Sqle protein [Rattus norvegicus]


37
EAU30782
114189082
hypothetical protein ATEG_08650 [Aspergillus terreus NIH2624]


38
CAF98057
47218525
unnamed protein product [Tetraodon nigroviridis]


39
XP_861944
73974450
PREDICTED: similar to squalene monooxygenase isoform 2 [Canis





familiaris]


40
ABF94794
108706999
Squalene monooxygenase, putative, expressed [Oryza sativa





(japonica cultivar-group)]


41
BAF11377
113547934
Os03g0231800 [Oryza sativa (japonica cultivar-group)]


42
XP_470614
50920507
Putative Squalene monooxygenase [Oryza sativa (japonica cultivar-





group)]


43
ABF94791
108706996
Squalene monooxygenase, putative, expressed [Oryza sativa





(japonica cultivar-group)]


44
AAM61384
21537043
squalene epoxidase-like protein [Arabidopsis thaliana]


45
BAE98940
110742002
hypothetical protein [Arabidopsis thaliana]


46
ABE84801
92877833
Helix-turn-helix, AraC type; NAD-binding site; Fumarate lyase





[Medicago truncatula]


47
BAE36598
74183459
unnamed protein product [Mus musculus]


48
XP_693698
68403773
PREDICTED: similar to squalene monooxygenase [Danio rerio]


49
CAB80441
7270759
squalene epoxidase-like protein [Arabidopsis thaliana]


50
O48651
6685403
Squalene monooxygenase (Squalene epoxidase) (SE)


51
AAY22200
62945915
squalene monooxygenase [Datura innoxia]


52
BAD15330
46359651
squalene epoxidase [Panax ginseng]


53
CAD23248
27475610
squalene monooxygenase 2 [Medicago truncatula]


54
ABC94943
86371770
squalene epoxidase [Medicago sativa]


55
CAD23249
27475612
squalene monooxygenase 1 [Medicago truncatula]


56
AAN15558
23198062
squalene monooxygenase, putative [Arabidopsis thaliana]


57
NP_179868
15227757
oxidoreductase [Arabidopsis thaliana]


58
AAG50645
12321049
squalene monooxygenase, putative [Arabidopsis thaliana]


59
XP_629022
66800193
hypothetical protein DDBDRAFT_0192021 [Dictyostelium





discoideum AX4]


60
CAK11466
94733753
novel protein similar to vertebrate squalene epoxidase (SQLE)





[Danio rerio]


61
AAQ13595
33337947
putative squalene epoxidase [Lycopersicon esculentum]


62
ABF94792
108706997
Squalene monooxygenase, putative, expressed [Oryza sativa





(japonica cultivar-group)]


63
XP_604908
76660360
PREDICTED: similar to squalene monooxygenase [Bos taurus]


64
BAA11209
1483186
squalene epoxidase [Homo sapiens]


65
NP_197803
15237902
SQP1 [Arabidopsis thaliana]


66
NP_001 . . .
79328611
SQP1 [Arabidopsis thaliana]


67
CAA06772
3123331
squalene epoxidase homologue [Arabidopsis thaliana]


68
O65726
6685410
Squalene monooxygenase 1,2 (Squalene epoxidase 1,2) (SE 1,2)


69
O65727
6685411
Squalene monooxygenase 1,1 (Squalene epoxidase 1,1) (SE 1,1)


70
NP_197804
15237903
oxidoreductase [Arabidopsis thaliana]


71
CAJ03182
68125205
squalene monooxygenase-like protein [Leishmania major]


72
NP_197802
15237900
SQP2; oxidoreductase [Arabidopsis thaliana]


73
XP_828409
71754989
squalene monooxygenase [Trypanosoma brucei TREU927]


74
XP_808343
71412304
squalene monooxygenase [Trypanosoma cruzi strain CL Brener]


75
XP_789059
72038634
PREDICTED: similar to squalene monooxygenase





[Strongylocentrotus purpuratus]


76
XP_796297
72133073
PREDICTED: similar to squalene monooxygenase





[Strongylocentrotus purpuratus]


77
AAB69189
2352528
squalene epoxidase [Candida glabrata]


78
XP_813434
71649420
squalene monooxygenase [Trypanosoma cruzi strain CL Brener]


79
XP_796261
72133071
PREDICTED: similar to squalene monooxygenase





[Strongylocentrotus purpuratus]


80
XP_793783
72114550
PREDICTED: similar to squalene monooxygenase, partial





[Strongylocentrotus purpuratus]


81
XP_789028
72038632
PREDICTED: similar to squalene xygenase [Strongylocentrotus





purpuratus]


82
AAT97087
51105054
squalene epoxidase-like protein [Lymnaea stagnalis]


83
XP_804343
71402993
squalene monooxygenase [Trypanosoma cruzi strain CL Brener]


84
YP_115265
53803024
monooxygenase family protein [Methylococcus capsulatus str. Bath]


85
AAM91177
22136198
unknown protein [Arabidopsis thaliana]


86
XP_799134
72026766
PREDICTED: similar to Squalene monooxygenase (Squalene





epoxidase) (SE), partial [Strongylocentrotus purpuratus]
















TABLE 54







Examples of ERG1 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAA34592
171471
squalene epoxidase


2
O13306
51704232
Squalene monooxygenase (Squalene epoxidase) (SE)


3
XP_455763
50311477
unnamed protein product [Kluyveromyces lactis]


4
Q75F69
51701415
Squalene monooxygenase (Squalene epoxidase) (SE)


5
XP_462160
50427105
hypothetical protein DEHA0G15202g [Debaryomyces hansenii CBS767]


6
XP_711894
68488538
squalene epoxidase [Candida albicans SC5314]


7
XP_503994
50553168
hypothetical protein [Yarrowia lipolytica]


8
AAB69189
2352528
squalene epoxidase [Candida glabrata]


9
AAQ18215
33415411
squalene epoxidase [Trichophyton rubrum]


10
AAQ18216
61807216
squalene epoxidase [Trichophyton rubrum]


11
AAZ08563
70797544
squalene epoxidase [Trichophyton rubrum]


12
EAS30670
90301039
hypothetical protein CIMG_06149 [Coccidioides immitis RS]


13
Q9C1W3
51701448
Probable squalene monooxygenase (Squalene epoxidase) (SE)


14
XP_758545
71012984
hypothetical protein UM02398.1 [Ustilago maydis 521]


15
XP_681020
67901528
hypothetical protein AN7751.2 [Aspergillus nidulans FGSC A4]


16
ABD48706
88697124
squalene epoxidase [Emericella nidulans]


17
BAE62359
83772229
unnamed protein product [Aspergillus oryzae]


18
XP_753858
70998268
squalene monooxygenase Erg1 [Aspergillus fumigatus Af293]


19
XP_961806
85104779
hypothetical protein [Neurospora crassa OR74A]


20
XP_386391
46123675
hypothetical protein FG06215.1 [Gibberella zeae PH-1]


21
CAJ18281
90185988
squalene epoxidase [Hypocrea lixii]


22
BAE73094
84579321
hypothetical protein [Macaca fascicularis]


23
BAE37374
74200967
unnamed protein product [Mus musculus]


24
XP_570092
58265872
squalene monooxygenase [Cryptococcus neoformans var.neoformans





JEC21]


25
NP_003120
62865635
squalene monooxygenase [Homo sapiens]


26
EAT79729
111058609
hypothetical protein SNOG_12929 [Phaeosphaeria nodorum SN15]


27
AAH97330
66911977
Sqle protein [Rattus norvegicus]


28
CAI46076
57997512
hypothetical protein [Homo sapiens]


29
CAF98057
47218525
unnamed protein product [Tetraodon nigroviridis]


30
XP_850640
73974448
PREDICTED: similar to squalene monooxygenase isoform 1 [Canis





familiaris]


31
XP_369325
39975869
hypothetical protein MG06139.4 [Magnaporthe grisea 70-15]


32
Q14534
12644414
Squalene monooxygenase (Squalene epoxidase) (SE)


33
XP_001 . . .
109087424
PREDICTED: similar to squalene monooxygenase [Macaca mulatta]


34
EAQ88139
88180671
hypothetical protein CHGG_04758 [Chaetomium globosum CBS 148.51]


35
XP_693698
68403773
PREDICTED: similar to squalene monooxygenase [Danio rerio]


36
CAG38355
108743007
squalene epoxidase [Aspergillus niger]


37
XP_861944
73974450
PREDICTED: similar to squalene monooxygenase isoform 2 [Canis





familiaris]


38
XP_519950
55631226
PREDICTED: similar to squalene epoxidase [Pan troglodytes]


39
AAS60234
45388098
squalene epoxidase 1 [Aspergillus fumigatus]


40
XP_629022
66800193
hypothetical protein DDBDRAFT_0192021 [Dictyostelium discoideum





AX4]


41
CAK11466
94733753
novel protein similar to vertebrate squalene epoxidase (SQLE) [Danio





rerio]


42
BAE98940
110742002
hypothetical protein [Arabidopsis thaliana]


43
AAM61384
21537043
squalene epoxidase-like protein [Arabidopsis thaliana]


44
ABC94943
86371770
squalene epoxidase [Medicago sativa]


45
CAB80441
7270759
squalene epoxidase-like protein [Arabidopsis thaliana]


46
CAD23248
27475610
squalene monooxygenase 2 [Medicago truncatula]


47
BAE36598
74183459
unnamed protein product [Mus musculus]


48
AAQ13595
33337947
putative squalene epoxidase [Lycopersicon esculentum]


49
AAY22200
62945915
squalene monooxygenase [Datura innoxia]


50
ABF94791
108706996
Squalene monooxygenase, putative, expressed [Oryza sativa (japonica





cultivar-group)]


51
AAN15558
23198062
squalene monooxygenase, putative [Arabidopsis thaliana]


52
ABF94794
108706999
Squalene monooxygenase, putative, expressed [Oryza sativa (japonica





cultivar-group)]


53
XP_470614
50920507
Putative Squalene monooxygenase [Oryza sativa (japonica cultivar-group)]


54
BAF11377
113547934
Os03g0231800 [Oryza sativa (japonica cultivar-group)]


55
CAD23249
27475612
squalene monooxygenase 1 [Medicago truncatula]


56
AAG50645
12321049
squalene monooxygenase, putative [Arabidopsis thaliana]


57
NP_179868
15227757
oxidoreductase [Arabidopsis thaliana]


58
ABE84801
92877833
Helix-turn-helix, AraC type; NAD-binding site; Fumarate lyase [Medicago





truncatula]


59
ABF94792
108706997
Squalene monooxygenase, putative, expressed [Oryza sativa (japonica





cultivar-group)]


60
BAA11209
1483186
squalene epoxidase [Homo sapiens]


61
XP_604908
76660360
PREDICTED: similar to squalene monooxygenase [Bos taurus]


62
XP_828409
71754989
squalene monooxygenase [Trypanosoma brucei TREU927]


63
XP_808343
71412304
squalene monooxygenase [Trypanosoma cruzi strain CL Brener]


64
CAJ03182
68125205
squalene monooxygenase-like protein [Leishmania major]


65
O65726
6685410
Squalene monooxygenase 1,2 (Squalene epoxidase 1,2) (SE 1,2)


66
NP_197804
15237903
oxidoreductase [Arabidopsis thaliana]


67
O65727
6685411
Squalene monooxygenase 1,1 (Squalene epoxidase 1,1) (SE 1,1)


68
CAA06772
3123331
squalene epoxidase homologue [Arabidopsis thaliana]


69
NP_001 . . .
79328611
SQP1 [Arabidopsis thaliana]


70
NP_197803
15237902
SQP1 [Arabidopsis thaliana]


71
NP_197802
15237900
SQP2; oxidoreductase [Arabidopsis thaliana]
















TABLE 55







Examples of ERG7 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAT93062
51013537
YHR072W [Saccharomyces cerevisiae]


2
AAA16975
465105
lanosterol synthase


3
XP_448182
50291499
unnamed protein product [Candida glabrata]


4
XP_451982
50304065
unnamed protein product [Kluyveromyces lactis]


5
NP_987017
45201447
AGR351Wp [Eremothecium gossypii]


6
XP_457937
50418833
hypothetical protein DEHA0C06501g [Debaryomyces hansenii CBS767]


7
XP_722471
68467112
2,3-oxidosqualene-lanosterol cyclase [Candida albicans SC5314]


8
XP_722612
68466833
2,3-oxidosqualene-lanosterol cyclase [Candida albicans SC5314]


9
1903190A
383419
oxidosqualene cyclase


10
XP_504990
50555163
hypothetical protein [Yarrowia lipolytica]


11
AAB08472
1549343
inactive oxidosqualene-lansoterol cyclase [Saccharomyces cerevisiae]


12
Q96WJ0
30913110
Lanosterol synthase (Oxidosqualene--lanosterol cyclase) (2,3-





epoxysqualene--lanosterol cyclase) (OSC)


13
XP_747936
70984860
oxidosqualene:lanosterol cyclase [Aspergillus fumigatus Af293]


14
BAE61626
83771494
unnamed protein product [Aspergillus oryzae]


15
NP_593702
63054562
lanosterol synthase activity [Schizosaccharomyces pombe 972h-]


16
XP_758387
71010409
hypothetical protein UM02240.1 [Ustilago maydis 521]


17
XP_681529
67902546
hypothetical protein AN8260.2 [Aspergillus nidulans FGSC A4]


18
EAS37438
90307807
hypothetical protein CIMG_02792 [Coccidioides immitis RS]


19
XP_961026
85100788
lanosterol synthase related protein [MIPS] [Neurospora crassa OR74A]


20
XP_751627
70993560
oxidosqualene:lanosterol cyclase [Aspergillus fumigatus Af293]


21
EAQ86439
88178971
hypothetical protein CHGG_07692 [Chaetomium globosum CBS 148.51]


22
XP_386126
46123145
hypothetical protein FG05950.1 [Gibberella zeae PH-1]


23
BAE63415
83773288
unnamed protein product [Aspergillus oryzae]


24
EAS31167
90301536
hypothetical protein CIMG_06646 [Coccidioides immitis RS]


25
EAT81661
111060541
hypothetical protein SNOG_11162 [Phaeosphaeria nodorum SN15]


26
XP_570450
58266588
lanosterol synthase [Cryptococcus neoformans var.neoformans JEC21]


27
AAL56020
18028346
oxidosqualene:lanosterol cyclase [Cephalosporium caerulens]


28
BAC37102
26346907
unnamed protein product [Mus musculus]


29
Q8BLN5
62286881
Lanosterol synthase (Oxidosqualene--lanosterol cyclase) (2,3-





epoxysqualene--lanosterol cyclase) (OSC)


30
XP_001 . . .
109065021
PREDICTED: lanosterol synthase isoform 2 [Macaca mulatta]


31
1W6KA
56966682
Chain A, Structure Of Human Osc In Complex With Lanosterol


32
BAC31739
26336108
unnamed protein product [Mus musculus]


33
XP_646246
66825783
hypothetical protein DDB_0191311 [Dictyostelium discoideum AX4]


34
AAF80384
8886139
cycloartenol synthase [Dictyostelium discoideum]


35
CAB42828
4808278
lanosterol synthase [Homo sapiens]


36
1W6JA
56966681
Chain A, Structure Of Human Osc In Complex With Ro 48-8071


37
BAA08208
639865
2,3-oxidosqualene:lanosterol cyclase [Rattus norvegicus]


38
NP_112311
13591981
lanosterol synthase [Rattus norvegicus]


39
NP_001 . . .
114053041
lanosterol synthase (2,3-oxidosqualene-lanosterol cyclase) [Bos taurus]


40
P48450
62296496
Lanosterol synthase (Oxidosqualene--lanosterol cyclase) (2,3-





epoxysqualene--lanosterol cyclase) (OSC)


41
NP_001 . . .
57529773
lanosterol synthase (2,3-oxidosqualene-lanosterol cyclase) [Gallus gallus]


42
XP_751356
70993016
oxidosqualene cyclase [Aspergillus fumigatus Af293]


43
CAG08284
47222029
unnamed protein product [Tetraodon nigroviridis]


44
BAB83085
18147590
cycloartenol synthase [Betula platyphylla]


45
BAA76902
4589852
cycloartenol synthase [Glycyrrhiza glabra]


46
BAE61719
83771588
unnamed protein product [Aspergillus oryzae]


47
BAA33460
3688598
Cycloartenol Synthase [Panax ginseng]


48
XP_001 . . .
109065023
PREDICTED: lanosterol synthase isoform 1 [Macaca mulatta]


49
BAD34644
50896401
cycloartenol synthase [Cucurbita pepo]


50
BAA85266
6045133
cycloartenol synthase [Luffa aegyptiaca]


51
BAB83253
18147771
cycloartenol synthase [Costus speciosus]


52
ABB76767
82468805
cycloartenol synthase [Ricinus communis]


53
BAA23533
2627181
cycloartenol synthase [Pisum sativum]


54
BAD34645
50896403
cucurbitadienol synthase [Cucurbita pepo]


55
BAE53431
83016479
cycloartenol synthase [Lotus japonicus]


56
AAS83469
46242746
cycloartenol synthase [Bupleurum kaoi]


57
A49398
541855
cycloartenol synthase (EC 5.4.99.8) - Arabidopsis thaliana


58
AAN64509
24796994
At2g07050/T4E14.16 [Arabidopsis thaliana]


59
BAD34646
50896405
putative oxidosqualene cyclase [Cucurbita pepo]


60
AAC04931
452446
cycloartenol synthase; (S)-2,3-epoxysqualene mutase [Arabidopsis





thaliana]


61
BAE95408
108743265
lanosterol synthase [Arabidopsis thaliana]


62
AAG44096
12004573
cycloartenol synthase [Abies magnifica]


63
AAS01524
41387168
cycloartenol synthase [Centella asiatica]


64
BAB83086
18147592
cycloartenol synthase [Betula platyphylla]


65
AAF03375
6090879
putative cycloartenol synthase [Oryza sativa]


66
BAF07762
113535379
Os02g0139700 [Oryza sativa (japonica cultivar-group)]


67
BAE95410
108743269
lanosterol synthase [Lotus japonicus]


68
AAK82995
15076959
lanosterol synthase [Trypanosoma cruzi]


69
XP_820967
71668047
lanosterol synthase [Trypanosoma cruzi strain CL Brener]


70
BAA85267
6045135
oxidosqualene cyclase [Luffa aegyptiaca]


71
NP_190099
42565553
catalytic/lyase [Arabidopsis thaliana]


72
AAT38889
47834383
cycloartenol synthase [Avena longiglumis]


73
BAA86933
6456469
oxidosqualene cyclase [Taraxacum officinale]


74
AAT38891
47834387
cycloartenol synthase [Avena strigosa]


75
CAC84559
15866702
cycloartenol synthase [Avena strigosa]


76
AAT38890
47834385
cycloartenol synthase [Avena prostrata]


77
AAT38888
47834381
cycloartenol synthase [Avena longiglumis]


78
AAT38887
47834379
cycloartenol synthase [Avena clauda]


79
AAT38892
47834389
cycloartenol synthase [Avena ventricosa]


80
XP_819758
71665580
lanosterol synthase [Trypanosoma cruzi strain CL Brener]


81
BAA86930
6456434
lupeol synthase [Olea europaea]


82
CAA61078
984145
lanosterol synthase [Homo sapiens]


83
BAA33462
3688602
Oxidosqualene Cyclase [Panax ginseng]


84
AAG26328
11023151
lanosterol synthase [Trypanosoma brucei brucei]


85
XP_825673
71752517
lanosterol synthase [Trypanosoma brucei TREU927]


86
BAA86932
6456467
lupeol synthase [Taraxacum officinale]


87
CAD23247
27475608
beta-amyrin synthase [Medicago truncatula]


88
BAA97558
8918271
beta-amyrin synthase [Pisum sativum]


89
BAA86931
6456465
cycloartenol synthase [Olea europaea]


90
BAD08587
41687978
lupeol synthase [Glycyrrhiza glabra]


91
BAA84603
5922599
oxidosqualene cyclase [Allium macrostemon]


92
AAO33578
28194504
beta-amyrin synthase [Medicago truncatula]


93
BAB83087
18147594
lupeol synthase [Betula platyphylla]


94
BAB83254
18147773
multifunctional triterpene synthase [Costus speciosus]


95
BAA89815
6730969
beta-amyrin synthase [Glycyrrhiza glabra]


96
BAE53429
83016474
beta-amyrin synthase [Lotus japonicus]


97
AAO33579
28194506
putative beta-amyrin synthase [Lotus japonicus]


98
BAA33461
3688600
beta-Amyrin Synthase [Panax ginseng]


99
CAB72151
6911851
oxidosqualene cyclase-like protein [Arabidopsis thaliana]


100
CAJ02110
68124127
lanosterol synthase, putative [Leishmania major]


101
BAA33722
3721856
beta-Amyrin Synthase [Panax ginseng]


102
AAX14716
60203059
beta-amyrin synthase [Aster sedifolius]


103
BAE53430
83016477
lupeol synthase [Lotus japonicus]


104
ABE91090
92892072
Prenyltransferase/squalene oxidase [Medicago truncatula]


105
XP_681518
67902524
hypothetical protein AN8249.2 [Aspergillus nidulans FGSC A4]


106
AAC17080
3152599
Strong similarity to lupeol synthase gb|U49919 and cycloartenol synthase





gb|U02555 from A. thaliana (the third gene with similar homology).





[Arabidopsis thaliana]


107
BAF28067
113644926
Os11g0286800 [Oryza sativa (japonica cultivar-group)]


108
NP_683508
22330736
beta-amyrin synthase [Arabidopsis thaliana]


109
AAS83468
46242744
beta-armyrin synthase [Bupleurum kaoi]


110
AAO33580
28194508
multifunctional beta-amyrin synthase [Lotus japonicus]


111
BAE43642
73991374
beta-amyrin synthase [Euphorbia tirucalli]


112
BAB83088
18147596
beta-amyrin synthase [Betula platyphylla]


113
ABB76766
82468803
lupeol synthase [Ricinus communis]


114
ABG22399
108864084
Cycloartenol synthase, putative, expressed [Oryza sativa (japonica cultivar-





group)]


115
BAF28063
113644922
Os11g0285000 [Oryza sativa (japonica cultivar-group)]


116
ABG22398
108864083
Cycloartenol synthase, putative, expressed [Oryza sativa (japonica cultivar-





group)]


117
NP_849903
30699380
LUP1 (LUPEOL SYNTHASE 1); lupeol synthase [Arabidopsis thaliana]


118
AAB94341
2738027
2,3-oxidosqualene-triterpenoid cyclase [Arabidopsis thaliana]


119
AAN77001
25991999
2,3-oxidosqualene-triterpene cyclase [Arabidopsis thaliana]


120
AAT38893
47834391
beta-amyrin synthase [Avena clauda]


121
AAD05032
1762150
lupeol synthase [Arabidopsis thaliana]


122
NP_178017
30699377
ATLUP2; lupeol synthase [Arabidopsis thaliana]


123
ABE88599
92887080
squalene/oxidosqualene cyclases [Medicago truncatula]


124
ABG22449
108864253
Cycloartenol synthase, putative, expressed [Oryza sativa (japonica cultivar-





group)]


125
BAB68529
15787841
isomultiflorenol synthase [Luffa aegyptiaca]


126
AAT38898
47834401
beta-amyrin synthase [Avena ventricosa]


127
AAT38894
47834393
beta-amyrin synthase [Avena longiglumis]


128
AAT38897
47834399
beta-amyrin synthase [Avena strigosa]


129
NP_178016
22330734
catalytic/lyase [Arabidopsis thaliana]


130
AAT38895
47834395
beta-amyrin synthase [Avena longiglumis]


131
AAT38896
47834397
beta-amyrin synthase [Avena prostrata]


132
BAA97559
8918273
mixed-amyrin synthase [Pisum sativum]


133
AAC98864
4090722
pentacyclic triterpene synthase [Arabidopsis thaliana]


134
BAF28466
113645325
Os11g0562100 [Oryza sativa (japonica cultivar-group)]


135
AAG41762
11934652
pentacyclic triterpene synthase [synthetic construct]


136
XP_480759
50942463
putative Cycloartenol Synthase [Oryza sativa (japonica cultivar-group)]


137
BAE43643
73991380
putative oxidosqulene cyclase [Euphorbia tirucalli]


138
AAC17070
3152589
Strong similarity to lupeol synthase gb|U49919 from A. thaliana (second





gene in a series of three with similar homologies). [Arabidopsis thaliana]


139
BAD15332
46359655
beta-amyrin synthase [Panax ginseng]


140
AAM23264
23428800
beta-amyrin synthase [Glycine max]


141
ABC33922
83638481
beta-amyrin synthase [Gypsophila paniculata]


142
AAS01523
41387158
putative beta-amyrin synthase [Centella asiatica]


143
BAE99758
110743847
cycloartenol synthase [Arabidopsis thaliana]


144
BAB11065
10177752
cycloartenol synthase [Arabidopsis thaliana]


145
NP_177971
15218390
catalytic [Arabidopsis thaliana]


146
CAD39196
32526539
cycloartenol synthase [Stigmatella aurantiaca]


147
ABG22450
108864254
Cycloartenol synthase, putative, expressed [Oryza sativa (japonica cultivar-





group)]


148
CAA93571
1204221
erg7 [Schizosaccharomyces pombe]


149
NP_567462
18414430
ATPEN1; catalytic/lyase [Arabidopsis thaliana]


150
NP_199612
42568386
catalytic [Arabidopsis thaliana]


151
NP_193272
15233798
catalytic/lyase [Arabidopsis thaliana]


152
ABE88610
92887091
squalene/oxidosqualene cyclases [Medicago truncatula]


153
AAW30034
56790234
At5g42600 [Arabidopsis thaliana]


154
BAF01935
110740066
putative lupeol synthase [Arabidopsis thaliana]


155
NP_198464
15239312
ATPEN3; catalytic [Arabidopsis thaliana]


156
BAB83089
18147598
putative oxidosqualene cyclase [Betula platyphylla]


157
YP_115266
53803023
squalene cyclase family protein [Methylococcus capsulatus str. Bath]


158
CAB78579
7268284
lupeol synthase like protein [Arabidopsis thaliana]


159
CAB78576
7268281
lupeol synthase like protein [Arabidopsis thaliana]
















TABLE 56







Examples of ERG6 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
CAA89944
854482
Erg6p [Saccharomyces cerevisiae]


2
P25087
462024
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


3
CAA52308
396515
S-adenosyl-methionine:delta-24-sterol-C-methyltransferase





[Saccharomyces cerevisiae]


4
AAB31378
619251
putative S-adenosylmethionine-dependent methyltransferase





[Saccharomyces cerevisiae]


5
Q6FRZ7
62900214
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


6
AAX73200
62178560
C24 sterol methyltransferase [Candida glabrata]


7
P_446997
50289135
unnamed protein product [Candida glabrata]


8
CAG59930
49526306
unnamed protein product [Candida glabrata CBS138]


9
AAX73199
62178558
C24 sterol methyltransferase [Candida glabrata]


10
Q6CYB3
62900210
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


11
P_451076
50302283
unnamed protein product [Kluyveromyces lactis]


12
CAH02664
49640207
unnamed protein product [Kluyveromyces lactis NRRL Y-1140]


13
Q759S7
62900245
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


14
P_984292
45188069
ADR196Wp [Eremothecium gossypii]


15
AAS52116
44982886
ADR196Wp [Ashbya gossypii ATCC 10895]


16
CAA37826
4122
unnamed protein product [Saccharomyces cerevisiae]


17
Q875K1
62900279
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


18
AAO21936
27803704
S-adenosylmethionine:D24-methyltransferase [Clavispora





lusitaniae]


19
Q6BRB7
62900203
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


20
P_459253
50421405
hypothetical protein DEHA0D19151g [Debaryomyces hansenii





CBS767]


21
CAG87427
49654920
unnamed protein product [Debaryomyces hansenii CBS767]


22
P_721588
68468538
SAM:delta 24-methyltransferase [Candida albicans SC5314]


23
P_721708
68468297
SAM:delta 24-methyltransferase [Candida albicans SC5314]


24
EAL02920
46443640
hypothetical protein CaO19.1631 [Candida albicans SC5314]


25
EAL02792
46443511
hypothetical protein CaO19.9199 [Candida albicans SC5314]


26
O74198
6015114
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


27
AAC26626
3323500
sterol transmethylase [Candida albicans]


28
Q6C2D9
62900205
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


29
P_505173
50555530
hypothetical protein [Yarrowia lipolytica]


30
CAG77980
49651043
unnamed protein product [Yarrowia lipolytica CLIB122]


31
P_595787
19112579
hypothetical protein SPBC16E9.05 [Schizosaccharomyces pombe





972h-]


32
O14321
6166151
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


33
CAB16897
2467267
SPBC16E9.05 [Schizosaccharomyces pombe]


34
EAT84719
111063599
hypothetical protein SNOG_08443 [Phaeosphaeria nodorum SN15]


35
EAS29698
90300067
hypothetical protein CIMG_08444 [Coccidioides immitis RS]


36
EAQ70709
86196071
hypothetical protein MGG_ch7g116 [Magnaporthe grisea 70-15]


37
P_366350
39969919
hypothetical protein MG10568.4 [Magnaporthe grisea 70-15]


38
P_746550
70982043
sterol 24-c-methyltransferase [Aspergillus fumigatus Af293]


39
EAL84512
66844173
sterol 24-c-methyltransferase, putative [Aspergillus fumigatus





Af293]


40
BAE64809
83774686
unnamed protein product [Aspergillus oryzae]


41
P_965392
85118140
probable DELTA(24)-STEROL C-METHYLTRANSFERASE





[MIPS] [Neurospora crassa OR74A]


42
Q9P3R1
62900336
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


43
EAA36156
28927200
probable DELTA(24)-STEROL C-METHYLTRANSFERASE





[MIPS] [Neurospora crassa]


44
CAB97289
9367272
probable DELTA(24)-STEROL C-METHYLTRANSFERASE





(ERG6) [Neurospora crassa]


45
P_664750
67541965
hypothetical protein AN7146.2 [Aspergillus nidulans FGSC A4]


46
EAA61398
40742208
hypothetical protein AN7146.2 [Aspergillus nidulans FGSC A4]


47
P_382959
46111803
hypothetical protein FG02783.1 [Gibberella zeae PH-1]


48
EAA70778
42547935
hypothetical protein FG02783.1 [Gibberella zeae PH-1]


49
Q96WX4
62900323
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


50
AAK54439
14192727
S-adenosyl methionine:sterol methyl transferase [Pneumocystis





carinii]


51
EAQ89522
88182054
conserved hypothetical protein [Chaetomium globosum CBS





148.51]


52
BAA13793
41688402
unnamed protein product [Schizosaccharomyces pombe]


53
P_385916
46122725
hypothetical protein FG05740.1 [Gibberella zeae PH-1]


54
EAA75815
42552972
hypothetical protein FG05740.1 [Gibberella zeae PH-1]


55
P_361872
39944670
hypothetical protein MG04346.4 [Magnaporthe grisea 70-15]


56
Q5EN22
62900141
Sterol 24-C-methyltransferase (Delta(24)-sterol C-





methyltransferase)


57
AAX07631
59802827
sterol 24-C-methyltransferase-like protein [Magnaporthe grisea]


58
BAE61033
83770900
unnamed protein product [Aspergillus oryzae]


59
P_759329
71018197
hypothetical protein UM03182.1 [Ustilago maydis 521]


60
EAK84412
46099179
hypothetical protein UM03182.1 [Ustilago maydis 521]


61
AAK00294
12642580
sterol methyl transferase [Pneumocystis carinii f. sp. carinii]


62
P_360548
39942022
hypothetical protein MG10860.4 [Magnaporthe grisea 70-15]


63
P_568887
58262954
sterol 24-C-methyltransferase [Cryptococcus neoformans var.





neoformans JEC21]


64
AAW41580
57223537
sterol 24-C-methyltransferase, putative [Cryptococcus neoformans





var. neoformans JEC21]


65
EAL22628
50259962
hypothetical protein CNBB2600 [Cryptococcus neoformans var.





neoformans B-3501A]


66
AAC34951
3560474
S-adenosyl-methionine-sterol-C-methyltransferase [Nicotiana





tabacum]


67
AAC04265
2909846
(S)-adenosyl-L-methionine:delta 24-sterol methyltransferase [Zea





mays]


68
AAB49338
1872473
delta-24-sterol methyltransferase [Triticum aestivum]


69
Q9LM02
62901053
Cycloartenol-C-24-methyltransferase (24-sterol C-methyltransferase





1) (Sterol C-methyltransferase 1) (Protein STEROL





METHYLTRANSFERASE 1) (Protein CEPHALOPOD)


70
AAN15377
23197700
24-sterol C-methyltransferase [Arabidopsis thaliana]


71
AAM53274
21539443
24-sterol C-methyltransferase [Arabidopsis thaliana]


72
P_196875
15240691
SMT1 (STEROL METHYLTRANSFERASE 1) [Arabidopsis





thaliana]


73
AAG28462
11066105
sterol methyltransferase SMT1 [Arabidopsis thaliana]


74
BAB08698
9758037
24-sterol C-methyltransferase [Arabidopsis thaliana]


75
AAF78847
8745241
SAM:cycloartenol-C24-methyltransferase [Arabidopsis thaliana]


76
AAM53553
21434843
cephalopod [Arabidopsis thaliana]


77
AAB70886
1899060
endosperm C-24 sterol methyltransferase [Zea mays]


78
AAB37769
1706965
delta-24-sterol methyltransferase [Triticum aestivum]


79
BAF21068
113610690
Os07g0206700 [Oryza sativa (japonica cultivar-group)]


80
Q6ZIX2
68566037
Cycloartenol-C-24-methyltransferase 1 (24-sterol C-





methyltransferase 1) (Sterol C-methyltransferase 1)


81
P_477078
50935101
cycloartenol-C24-methyltransferase [Oryza sativa (japonica





cultivar-group)]


82
BAC83238
34393309
cycloartenol-C24-methyltransferase [Oryza sativa (japonica





cultivar-group)]


83
AAB04057
1399380
S-adenosyl-L-methionine:delta24-sterol-C-methyltransferase


84
AAB62812
2246458
S-adenosyl-methionine-sterol-C-methyltransferase [Ricinus





communis]


85
AAC35787
3603295
S-adenosyl-methionine cycloartenol-C24-methyltransferase





[Nicotiana tabacum]


86
AAC34988
3560531
cycloartenol-C24-methyltransferase [Oryza sativa subsp. japonica]


87
AAZ83345
73761691
24-sterol C-methyltransferase [Gossypium hirsutum]


88
EAS30660
90301029
hypothetical protein CIMG_06139 [Coccidioides immitis RS]


89
P_470035
50919277
putative endosperm C-24 sterol methyltransferase [Oryza sativa





(japonica cultivar-group)]


90
AAP21419
30103006
putative endosperm C-24 sterol methyltransferase [Oryza sativa





(japonica cultivar-group)]


91
AAR92099
40806291
S-adenosyl-L-methionine-C-24-delta-sterol-methyltransferase B





[Leishmania donovani]


92
AAR92098
40806289
S-adenosyl-L-methionine-C-24-delta-sterol-methyltransferase A





[Leishmania donovani]


93
CAJ09197
68129891
sterol 24-c-methyltransferase, putative [Leishmania major]


94
CAJ09196
68129890
sterol 24-c-methyltransferase, putative [Leishmania major]


95
P_802864
71399753
sterol 24-c-methyltransferase [Trypanosoma cruzi strain CL Brener]


96
EAN81418
70865128
sterol 24-c-methyltransferase, putative [Trypanosoma cruzi]


97
P_802716
71399140
sterol 24-c-methyltransferase [Trypanosoma cruzi strain CL Brener]


98
EAN81270
70864663
sterol 24-c-methyltransferase, putative [Trypanosoma cruzi]


99
P_822930
71747750
sterol 24-c-methyltransferase [Trypanosoma brucei TREU927]


100
AAZ40214
71738257
sterol methyltransferase [Trypanosoma brucei brucei]


101
CAJ16958
70908212
s-adenosyl-L-methionine-c-24-delta-sterol-methyltransferase a,





putative [Trypanosoma brucei]


102
EAN78102
70832598
sterol 24-c-methyltransferase, putative [Trypanosoma brucei]


103
P_636481
66805519
hypothetical protein DDBDRAFT_0188166 [Dictyostelium





discoideum AX4]


104
EAL62977
60464861
hypothetical protein DDBDRAFT_0188166 [Dictyostelium





discoideum AX4]


105
ABF99454
108711659
Cyclopropane-fatty-acyl-phospholipid synthase family protein,





expressed [Oryza sativa (japonica cultivar-group)]


106
P_802811
71399535
sterol 24-c-methyltransferase [Trypanosoma cruzi strain CL Brener]


107
EAN81365
70864963
sterol 24-c-methyltransferase, putative [Trypanosoma cruzi]


108
ABB90541
82780739
c24-sterol methyltransferase [Paracoccidioides brasiliensis]


109
AAB62807
2246452
S-adenosyl-methionine-sterol-C-methyltransferase homolog





[Nicotiana tabacum]


110
Q39227
62900893
24-methylenesterol C-methyltransferase 2 (24-sterol C-





methyltransferase 2) (Sterol-C-methyltransferase 2)


111
AAM45009
21281107
putative sterol-C-methyltransferase [Arabidopsis thaliana]


112
P_173458
15217917
SMT2 (STEROL METHYLTRANSFERASE 2) [Arabidopsis





thaliana]


113
AAK76716
15028255
putative sterol-C-methyltransferase [Arabidopsis thaliana]


114
AAG48780
12083242
putative sterol-C-methyltransferase [Arabidopsis thaliana]


115
AAF88156
9558593
Identical to 24-sterol C-methyltransferase from Arabidopsis thaliana





gi|2129517 and is a member of the ubiE/COQ5 methyltransferase





family PF|01209. ESTs gb|T42228, gb|T46520, gb|T41746,





gb|N38458, gb|AI993515, gb|AA389843, gb|AI099890,





gb|AI099653 come f


116
2207220A
1587694
sterol C-methyltransferase


117
CAA61966
1061040
sterol-C-methyltransferase [Arabidopsis thaliana]


118
AAN72104
25083682
24-sterol C-methyltransferase [Arabidopsis thaliana]


119
AAM91592
22136020
24-sterol C-methyltransferase [Arabidopsis thaliana]


120
Q94JS4
67472706
24-methylenesterol C-methyltransferase 3 (24-sterol C-





methyltransferase 3) (Sterol-C-methyltransferase 3)


121
AAM47339
21360447
At1g76090/T23E18_40 [Arabidopsis thaliana]


122
P_177736
15222955
SMT3; S-adenosylmethionine-dependent methyltransferase





[Arabidopsis thaliana]


123
AAK52981
14030613
At1g76090/T23E18_40 [Arabidopsis thaliana]


124
AAN31890
23397216
putative sterol-C-methyltransferase [Arabidopsis thaliana]


125
AAB62809
2246456
S-adenosyl-methionine-sterol-C-methyltransferase [Arabidopsis





thaliana]


126
AAB62808
2246454
S-adenosyl-methionine-sterol-C-methyltransferase [Nicotiana





tabacum]


127
AAM63753
21555010
sterol-C-methyltransferase [Arabidopsis thaliana]


128
BAF10805
113547362
Os03g0136200 [Oryza sativa (japonica cultivar-group)]


129
ABF93854
108706059
24-methylenesterol C-methyltransferase 2, putative, expressed





[Oryza sativa (japonica cultivar-group)]


130
O82427
68566013
24-methylenesterol C-methyltransferase 2 (24-sterol C-





methyltransferase 2) (Sterol-C-methyltransferase 2)
















TABLE 57







Examples of ERG5 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
P54781
1706693
Cytochrome P450 61 (C-22 sterol desaturase)


2
AAB06217
1235991
cytochrome P450


3
CAA89116
798924
unknown [Saccharomyces cerevisiae]


4
AAU09769
51830482
YMR015C [Saccharomyces cerevisiae]


5
AAX73198
62178556
C22 sterol desaturase [Candida glabrata]


6
AAX73197
62178554
C22 sterol desaturase [Candida glabrata]


7
P_449681
50294540
hypothetical protein CAGL0M07656g [Candida glabrata CBS138]


8
CAG62657
49528995
unnamed protein product [Candida glabrata CBS138]


9
P_453562
50307167
unnamed protein product [Kluyveromyces lactis]


10
CAH00658
49642696
unnamed protein product [Kluyveromyces lactis NRRL Y-1140]


11
P_982999
45185282
ABR053Cp [Eremothecium gossypii]


12
AAS50823
44980940
ABR053Cp [Ashbya gossypii ATCC 10895]


13
P_458727
50420383
hypothetical protein DEHA0D06842g [Debaryomyces hansenii





CBS767]


14
CAG86871
49654394
unnamed protein product [Debaryomyces hansenii CBS767]


15
P_888893
77022898
hypothetical protein CaJ7.0323 [Candida albicans SC5314]


16
BAE44790
76573706
hypothetical protein [Candida albicans]


17
P_716933
68478128
cytochrome P450 [Candida albicans SC5314]


18
P_717000
68477993
hypothetical protein CaO19.5178 [Candida albicans SC5314]


19
EAK98020
46438693
hypothetical protein CaO19.5178 [Candida albicans SC5314]


20
EAK97950
46438622
hypothetical protein CaO19.12645 [Candida albicans SC5314]


21
CAA21953
3850153
cytochrome P450 [Candida albicans]


22
P_500188
50545301
hypothetical protein [Yarrowia lipolytica]


23
CAG84120
49646053
unnamed protein product [Yarrowia lipolytica CLIB122]


24
BAC01142
21624361
sterol C-22 desaturase [Symbiotaphrina buchneri]


25
BAC01140
21624354
sterol C-22 desaturase [Symbiotaphrina buchneri]


26
BAC01141
21624359
sterol C-22 desaturase [Symbiotaphrina kochii]


27
BAC01139
21624352
sterol C22 desaturase [Symbiotaphrina kochii]


28
EAQ88206
88180738
conserved hypothetical protein [Chaetomium globosum CBS148.51]


29
P_961915
85105220
hypothetical protein [Neurospora crassa OR74A]


30
EAA32679
28923500
hypothetical protein [Neurospora crassa]


31
EAS33985
90304354
hypothetical protein CIMG_05009 [Coccidioides immitis RS]


32
P_750145
70990592
cytochrome P450 sterol C-22 desaturase [Aspergillus fumigatus





Af293]


33
EAL88107
66847777
cytochrome P450 sterol C-22 desaturase, putative [Aspergillus





fumigatus Af293]


34
EAT87119
111065999
hypothetical protein SNOG_06055 [Phaeosphaeria nodorum SN15]


35
BAE58068
83767929
unnamed protein product [Aspergillus oryzae]


36
P_382135
46110154
hypothetical protein FG01959.1 [Gibberella zeae PH-1]


37
EAA68855
42546012
hypothetical protein FG01959.1 [Gibberella zeae PH-1]


38
P_661646
67527317
hypothetical protein AN4042.2 [Aspergillus nidulans FGSC A4]


39
EAA59513
40740323
hypothetical protein AN4042.2 [Aspergillus nidulans FGSC A4]


40
P_383862
46115688
hypothetical protein FG03686.1 [Gibberella zeae PH-1]


41
EAA71499
42548656
hypothetical protein FG03686.1 [Gibberella zeae PH-1]


42
P_369417
39976053
hypothetical protein MG06047.4 [Magnaporthe grisea 70-15]


43
BAE57461
83767322
unnamed protein product [Aspergillus oryzae]


44
P_593788
19114700
hypothetical protein SPAC19A8.04 [Schizosaccharomyces pombe





972h-]


45
CAB11640
7007345
SPAC19A8.04 [Schizosaccharomyces pombe]


46
P_756497
71003662
hypothetical protein UM00350.1 [Ustilago maydis 521]


47
EAK81168
46095935
hypothetical protein UM00350.1 [Ustilago maydis 521]


48
P_571445
58268578
C-22 sterol desaturase [Cryptococcus neoformans var. neoformans





JEC21]


49
AAW44138
57227680
C-22 sterol desaturase, putative [Cryptococcus neoformans var.





neoformans JEC21]


50
EAL20298
50257593
hypothetical protein CNBF1100 [Cryptococcus neoformans var.





neoformans B-3501A]


51
EAQ86140
88178672
hypothetical protein CHGG_07393 [Chaetomium globosum CBS





148.51]


52
AAO48601
28864257
ERG5 [Clavispora lusitaniae]


53
P_647018
66827327
cytochrome P450 family protein [Dictyostelium discoideum AX4]


54
EAL73097
60475161
cytochrome P450 family protein [Dictyostelium discoideum AX4]


55
BAF04287
113531904
Os01g0211200 [Oryza sativa (japonica cultivar-group)]


56
P_913287
34903880
unnamed protein product [Oryza sativa (japonica cultivar-group)]


57
BAA96196
8096624
putative sterol C-22 desaturase [Oryza sativa (japonica cultivar-





group)]


58
BAA96154
8096581
putative sterol C-22 desaturase [Oryza sativa (japonica cultivar-





group)]


59
ABC59097
84514177
cytochrome P450 monooxygenase CYP710A15 [Medicago





truncatula]


60
P_180452
15226976
CYP710A4; heme binding/iron ion binding/monooxygenase/





oxygen binding [Arabidopsis thaliana]


61
AAC79590
3927833
putative cytochrome P450 [Arabidopsis thaliana]


62
P_913285
34903876
unnamed protein product [Oryza sativa (japonica cultivar-group)]


63
BAA96194
8096622
sterol C-22 desaturase-like [Oryza sativa (japonica cultivar-group)]


64
BAA96152
8096579
sterol C-22 desaturase-like [Oryza sativa (japonica cultivar-group)]


65
P_913291
34903888
unnamed protein product [Oryza sativa (japonica cultivar-group)]


66
BAA96200
8096628
sterol C-22 desaturase-like [Oryza sativa (japonica cultivar-group)]


67
BAA96158
8096585
sterol C-22 desaturase-like [Oryza sativa (japonica cultivar-group)]


68
BAF04286
113531903
Os01g0210900 [Oryza sativa (japonica cultivar-group)]


69
P_913284
34903874
unnamed protein product [Oryza sativa (japonica cultivar-group)]


70
BAA96193
8096621
sterol C-22 desaturase-like [Oryza sativa (japonica cultivar-group)]


71
BAA96151
8096578
sterol C-22 desaturase-like [Oryza sativa (japonica cultivar-group)]


72
BAE71351
84468537
CYP710 [Arabidopsis thaliana]


73
AAQ65177
34365731
At2g34500 [Arabidopsis thaliana]


74
AAN72080
25083451
putative cytochrome P450 [Arabidopsis thaliana]


75
AAM14944
20197156
putative cytochrome P450 [Arabidopsis thaliana]


76
P_180997
15226758
CYP710A1; heme binding/iron ion binding/monooxygenase/





oxygen binding [Arabidopsis thaliana]


77
AAC26690
3128210
putative cytochrome P450 [Arabidopsis thaliana]


78
P_180451
15226974
CYP710A3; heme binding/iron ion binding/monooxygenase/





oxygen binding [Arabidopsis thaliana]


79
AAC79589
3927832
putative cytochrome P450 [Arabidopsis thaliana]


80
BAE80316
89111285
CYP710 protein [Arabidopsis thaliana]


81
AAM26664
20856398
At2g34490/T31E10.17 [Arabidopsis thaliana]


82
AAM14945
20197157
putative cytochrome P450 [Arabidopsis thaliana]


83
AAL75888
18650637
At2g34490/T31E10.17 [Arabidopsis thaliana]


84
P_180996
15226756
CYP710A2; heme binding/iron ion binding/monooxygenase/





oxygen binding [Arabidopsis thaliana]


85
AAC26691
3128211
putative cytochrome P450 [Arabidopsis thaliana]


86
AAM62799
21553706
putative cytochrome P450 [Arabidopsis thaliana]


87
BAE93156
91204699
sterol 22-desaturase [Lycopersicon esculentum]
















TABLE 58







Examples of ERG3 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAT93015
51013443
YLR056W [Saccharomyces cerevisiae]


2
NP_013157
6323085
C-5 sterol desaturase, catalyzes the introduction of a C-5(6)


3
BAA20292
2143190
C-5 sterol desaturase [Saccharomyces cerevisiae]


4
CAA64303
1181277
C-5 sterol desaturase [Saccharomyces cerevisiae]


5
P32353
416963
C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta


6
AAB39844
233331
C-5 sterol desaturase [Saccharomyces cerevisiae]


7
AAA34595
171477
C-5 sterol desaturase


8
AAA34594
171475
C-5 sterol desaturase


9
XP_446050
50287241
unnamed protein product [Candida glabrata]


10
CAG58974
49525357
unnamed protein product [Candida glabrata CBS138]


11
P50860
1706691
C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta


12
AAB02330
755695
ERG3


13
Q754B9
51701406
C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta


14
NP_985698
45198669
AFR151Cp [Eremothecium gossypii]


15
AAS53522
44984679
AFR151Cp [Ashbya gossypii ATCC 10895A]


16
XP_455482
50310919
unnamed protein product [Kluyveromyces lactis]


17
CAG98190
49644618
unnamed protein product [Kluyveromyces lactis NRRL Y-1140]


18
Q8NJ57
51701432
C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta


19
CAD13131
22022945
ergosterol delta 5,6 desaturase [Candida dubliniensis]


20
XP_713577
68485022
hypothetical protein CaO19.767 [Candida albicans SC5314]


21
XP_713612
68484947
hypothetical protein CaO19.8387 [Candida albicans SC5314]


22
EAK94507
46435118
hypothetical protein CaO19.8387 [Candida albicans SC5314]


23
EAK94472
46435082
hypothetical protein CaO19.767 [Candida albicans SC5314]


24
O93875
51701379
C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta


25
AAC99343
4091929
C5,6 desaturase [Candida albicans]


26
XP_460747
50424321
hypothetical protein DEHA0F09757g [Debaryomyces hansenii





CBS76


27
CAG89088
49656416
unnamed protein product [Debaryomyces hansenii CBS767]


28
XP_503090
50551233
hypothetical protein [Yarrowia lipolytica]


29
CAG81282
49648958
unnamed protein product [Yarrowia lipolytica CLIB122]


30
XP_664110
67540672
hypothetical protein AN6506.2 [Aspergillus nidulans FGSC A4]


31
EAA57846
40738656
hypothetical protein AN6506.2 [Aspergillus nidulans FGSC A4]


32
BAE61784
83771654
unnamed protein product [Aspergillus oryzae]


33
XP_747563
70984086
sterol delta 5,6-desaturase ERG3 [Aspergillus fumigatus Af293]


34
EAL85525
66845190
sterol delta 5,6-desaturase ERG3 [Aspergillus fumigatus Af293]


35
AAU82098
52548218
C-5 sterol desaturase B-like [Aspergillus fumigatus]


36
BAE56076
83765933
unnamed protein product [Aspergillus oryzae]


37
XP_962923
85109451
hypothetical protein [Neurospora crassa OR74A]


38
Q7SBB6
51701418
Probable C-5 sterol desaturase (Sterol-C5-desaturase) (Ergoste


39
EAA33687
28924567
hypothetical protein [Neurospora crassa]


40
EAS37256
90307625
C-5 sterol desaturase [Coccidioides immitis RS]


41
Q8J207
51701428
C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta


42
AAN27998
23476431
sterol delta 5,6-desaturase ERG3 [Leptosphaeria maculans]


43
XP_363987
39953467
hypothetical protein MG08832.4 [Magnaporthe grisea 70-15]


44
EAT83541
111062421
hypothetical protein SNOG_09349 [Phaeosphaeria nodorum SN15]


45
O94457
51701380
Probable C-5 sterol desaturase 1 (Sterol-C5-desaturase 1) (Erg


46
NP_593135
19114047
hypothetical protein SPAC1687.16c [Schizosaccharomyces pombe 9


47
CAA22610
4106670
SPAC1687.16c [Schizosaccharomyces pombe]


48
XP_382678
46111241
hypothetical protein FG02502.1 [Gibberella zeae PH-1]


49
EAA67236
42544393
hypothetical protein FG02502.1 [Gibberella zeae PH-1]


50
BAE65607
83775487
unnamed protein product [Aspergillus oryzae]


51
O13666
6015113
Probable C-5 sterol desaturase 2 (Sterol-C5-desaturase 2) (Erg


52
CAA16898
2853109
SPBC27B12.03c [Schizosaccharomyces pombe]


53
BAA21457
2257565
C-5 STEROL DESATURASE [Schizosaccharomyces pombe]
















TABLE 59







Examples of ERG2 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAS56448
45270134
YMR202W [Saccharomyces cerevisiae]


2
CAA88643
736299
Erg2p [Saccharomyces cerevisiae]


3
P32352
416962
C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)


4
AAA34593
171473
C-8 sterol isomerase


5
P_985369
45198340
AFL181Cp [Eremothecium gossypii]


6
AAS53193
44984227
AFL181Cp [Ashbya gossypii ATCC 10895]


7
P_449233
50293643
unnamed protein product [Candida glabrata]


8
CAG62207
49528546
unnamed protein product [Candida glabrata CBS138]


9
P_455367
50310691
unnamed protein product [Kluyveromyces lactis]


10
CAG98075
49644503
unnamed protein product [Kluyveromyces lactis NRRL Y-1140]


11
P_458891
50420709
hypothetical protein DEHA0D10714g [Debaryomyces hansenii





CBS767]


12
CAG87043
49654558
unnamed protein product [Debaryomyces hansenii CBS767]


13
P_718886
68473979
sterol C8-C7 isomerase [Candida albicans SC5314]


14
P_718988
68473770
sterol C8-C7 isomerase [Candida albicans SC5314]


15
EAL00087
46440785
hypothetical protein CaO19.6026 [Candida albicans SC5314]


16
EAK99982
46440679
hypothetical protein CaO19.13447 [Candida albicans SC5314]


17
P_504668
50554519
hypothetical protein [Yarrowia lipolytica]


18
CAG80272
49650537
unnamed protein product [Yarrowia lipolytica CLIB122]


19
P_501006
50547073
hypothetical protein [Yarrowia lipolytica]


20
CAG83259
49646872
unnamed protein product [Yarrowia lipolytica CLIB122]


21
Q92254
67476925
C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)


22
CAC28749
12718205
C-8 sterol isomerase erg-1 [Neurospora crassa]


23
AAB09470
1575320
C-8 sterol isomerase


24
P_658055
67516339
hypothetical protein AN0451.2 [Aspergillus nidulans FGSC A4]


25
EAA66550
40747394
hypothetical protein AN0451.2 [Aspergillus nidulans FGSC A4]


26
P_593324
19114236
hypothetical protein SPAC20G8.07c [Schizosaccharomyces pombe





972h-]


27
P87113
3219796
Probable C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)


28
CAB08601
2094862
SPAC20G8.07c [Schizosaccharomyces pombe]


29
P_363040
39947737
hypothetical protein MG08624.4 [Magnaporthe grisea 70-15]


30
P33281
462023
C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)


31
CAA80454
311322
C-8 sterol isomerase [Magnaporthe grisea]


32
EAQ85888
88178420
hypothetical protein CHGG_07141 [Chaetomium globosum CBS148.51]


33
P_961312
85102300
C-8 STEROL ISOMERASE (DELTA-8--DELTA-7 STEROL





ISOMERASE) [Neurospora crassa OR74A]


34
EAA32076
28922855
C-8 STEROL ISOMERASE (DELTA-8--DELTA-7 STEROL





ISOMERASE) [Neurospora crassa]


35
P_844057
72387265
C-8 sterol isomerase, putative [Trypanosoma brucei]


36
P_826540
71905267
C-8 sterol isomerase, putative [Trypanosoma brucei]


37
AAZ10498
70800589
C-8 sterol isomerase, putative [Trypanosoma brucei]


38
AAX80634
62360216
C-8 sterol isomerase, putative [Trypanosoma brucei]


39
P_758081
71006989
C-8 sterol isomerase [Ustilago maydis 521]


40
EAK82388
46097155
ERG2_USTMA C-8 sterol isomerase (Delta-8--delta-7 sterol





isomerase) [Ustilago maydis 521]


41
P32360
416961
C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)


42
CAA78959
2967
C-8 sterol isomerase [Ustilago maydis]


43
P_567070
58259315
C-8 sterol isomerase [Cryptococcus neoformans var. neoformans





JEC21]


44
AAW41251
57223207
C-8 sterol isomerase, putative [Cryptococcus neoformans var.





neoformans JEC21]


45
EAL23045
50260386
hypothetical protein CNBA8120 [Cryptococcus neoformans var.





neoformans B-3501A]


46
P_821186
71658920
C-8 sterol isomerase [Trypanosoma cruzi strain CL Brener]


47
EAN99335
70886558
C-8 sterol isomerase, putative [Trypanosoma cruzi]


48
AAQ18796
33439494
C-8 sterol isomerase [Trypanosoma cruzi]


49
P_847879
73536920
C-8 sterol isomerase-like protein [Leishmania major strain Friedlin]


50
AAZ09671
70799755
C-8 sterol isomerase-like protein [Leishmania major strain Friedlin]
















TABLE 60







Examples of ERG3-like polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
BAA33730
3721884
sterol-C5-desaturase [Mus musculus]


2
BAE32506
74178504
unnamed protein product [Mus musculus]


3 
AAH24132
18848246
Sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog 





(S. cerevisae) [Mus musculus]


4 
NP_766357
27777693
sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog





[Mus musculus]


5
BAC36944
26346591
unnamed protein product [Mus musculus]


6
BAC31666
26335931
unnamed protein product [Mus musculus]


7 
AAH81704
51859106
Sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog





(S. cerevisae) [Rattus norvegicus


8 
NP_446094
25742651
sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog





[Rattus norvegicus]


9 
BAB19798
11990472
sterol C5-desaturase [Rattus norvegicus]


10
XP_853004
73955000
PREDICTED: similar to sterol-C5-desaturase-like [Canis familiaris]


11 
XP_508825
55637121
PREDICTED: similar to delta7-sterol-C5-desaturase 





[Pan troglodytes]


12 
NP_001 . . . 
68160945
sterol-C5-desaturase-like [Homo sapiens]


13 
NP_008849
68160941
sterol-C5-desaturase-like [Homo sapiens]


14
BAD96861
62897843
sterol-C5-desaturase (ERG3 delta-5-desaturase homolog, fungal)-





like variant [Homo sapiens]


15
BAD96406
62896931
sterol-C5-desaturase (ERG3 delta-5-desaturase homolog, fungal)-





like variant [Homo sapiens]


16
AAH50427
30046554
Sterol-C5-desaturase (ERG3 delta-5-desaturase homolog, fungal)-





like [Homo sapiens]


17
AAH12333
15147389
Sterol-C5-desaturase (ERG3 delta-5-desaturase homolog, fungal)-





like [Homo sapiens]


18
AAF00544
6003685
delta7-sterol-C5-desaturase [Homo sapiens]


19
BAB68218
15637108
sterol C5 desaturase [Homo sapiens]


20
O75845
6174975
Lathosterol oxidase (Lathosterol 5-desaturase) (Delta-7-sterol 5-





desaturase) (C-5 sterol desatur


21
BAA33729
3721882
sterol-C5-desaturase [Homo sapiens]


22 
XP_001 . . . 
1.09E+08
PREDICTED: sterol-C5-desaturase (ERG3 delta-5-desaturase





homolog, fungal)-like isoform 2 [Macaca


23 
AAH78055
50416254
Sc5d-prov protein [Xenopus laevis]


24
NP_001 . . . 
52219112
sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog





[Danio rerio]


25
AAH81395
51859008
Sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog 





(S. cerevisae) [Danio rerio]


26 
BAA18970
1906796
fungal sterol-C5-desaturase homolog [Homo sapiens]


27
XP_001 . . . 
1.09E+08
PREDICTED: sterol-C5-desaturase (ERG3 delta-5-desaturase





homolog, fungal)-like isoform 1 [Macaca


28
XP_793331
72159211
PREDICTED: similar to sterol-C5-desaturase (fungal ERG3, delta-





5-desaturase) homolog [Strongyloc


29
NP_001 . . . 
78369462
hypothetical protein LOC525154 [Bos taurus]


30 
AAI03339
74353920
Similar to sterol-C5-desaturase-like [Bos taurus]


31 
CAF90498
47207599
unnamed protein product [Tetraodon nigroviridis]
















TABLE 61







Examples of ERG27 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1 
Q12452
60392263
3-keto-steroid reductase


2
CAA97664
1360483
unnamed protein product [Saccharomyces cerevisiae]


3
AAB67544
1256850
Ylr100wp [Saccharomyces cerevisiae]


4 
Q6FIV3
62286920
3-keto-steroid reductase


5
P_449841
50294860
hypothetical protein CAGL0M11506g [Candida glabrata CBS138]


6
CAG62821
49529155 
unnamed protein product [Candida glabrata CBS138]


7
Q6CJC2
62286919 
3-keto-steroid reductase


8 
P_455967
50311871 
unnamed protein product [Kluyveromyces lactis]


9
CAG98675
49645103
unnamed protein product [Kluyveromyces lactis NRRL Y-1140]


10
Q74ZZ0
62286926
3-keto-steroid reductase


11
P_986733
45201163
AGR068Wp [Eremothecium gossypii]


12 
AAS54557
44985946
AGR068Wp [Ashbya gossypii ATCC 10895]


13 
Q6BNP0
62286917
3-keto-steroid reductase


14 
P_460180
50423199
hypothetical protein DEHA0E21263g [Debaryomyces hansenii CBS


15 
CAG88453
49655848 
unnamed protein product [Debaryomyces hansenii CBS767]


16
Q874K0
62286935 
3-keto-steroid reductase


17
AAN28009
29465858 
3-keto reductase [Candida albicans]


18 
P_717865
68476112
3-keto sterol reductase [Candida albicans SC5314]


19 
P_717931
68475981
3-keto sterol reductase [Candida albicans SC5314]


20
EAK98982
46439667
hypothetical protein CaO19.3240 [Candida albicans SC5314]


21 
EAK98915
46439599 
hypothetical protein CaO19.10750 [Candida albicans SC5314]


22 
Q6CE88
62286918 
3-keto-steroid reductase


23
P_501024
50547109
hypothetical protein [Yarrowia lipolytica]


24 
CAG83277
49646890 
unnamed protein product [Yarrowia lipolytica CLIB122]


25 
P_595440
19112232 
3-keto sterol reductase [Schizosaccharomyces pombe 972h-]


26 
CAA21246
3738145
SPBC1709.07 [Schizosaccharomyces pombe]


27
BAA13878
1749642 
unnamed protein product [Schizosaccharomyces pombe]


28
P_751680
70993666 
3-ketosteroid reductase [Aspergillus fumigatus Af293]


29 
EAL89642
66849314
3-ketosteroid reductase [Aspergillus fumigatus Af293]


30 
P_958799
85091228
hypothetical protein [Neurospora crassa OR74A]


31
EAA29563
28920185 
hypothetical protein [Neurospora crassa]


32
BAE58171
83768032
unnamed protein product [Aspergillus oryzae]


33 
EAQ85086
88177618
hypothetical protein CHGG_09100 [Chaetomium globosum CBS 148


34
EAT86025
111064905 
hypothetical protein SNOG_06194 [Phaeosphaeria nodorum SN15]


35 
P_663189
67538830
hypothetical protein AN5585.2 [Aspergillus nidulans FGSC A4]


36
EAA62228
40743038
hypothetical protein AN5585.2 [Aspergillus nidulans FGSC A4]


37
EAS36221
90306590
hypothetical protein CIMG_01575 [Coccidioides immitis RS]


38 
AAO64345
29150686
3-ketosteroid reductase [Botryotinia fuckeliana]


39 
P_796770
72131681
PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase


40 
P_793145
72086766 
PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase


41
P_570518
58266724 
3-keto sterol reductase [Cryptococcus neoformans var. neofor


42
AAW43211
57226751
3-keto sterol reductase, putative [Cryptococcus neoformans v


43
EAL21279
50258592
hypothetical protein CNBD3330 [Cryptococcus neoformans var.


44 
AAI00220
71681260 
Unknown (protein for MGC: 114978) [Xenopus laevis]


45
BAE06843
70720928
hypothetical protein [Epichloe festucae]


46 
P_001 . . . 
62859081
hydroxysteroid (17-beta) dehydrogenase 7 [Xenopus tropicalis


47
P_851698
74006237 
PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase


48 
CAC88119
18077845
17 beta-hydroxysteroid dehydrogenase type 7 [Mus musculus]


49
AAH11464
15079256
Hsd17b7 protein [Mus musculus]


50
P_034606
87162470
hydroxysteroid (17-beta) dehydrogenase 7 [Mus musculus]


51
BAC25918
26390565
unnamed protein product [Mus musculus]


52 
BAC34124
26340924
unnamed protein product [Mus musculus]


53 
O88736
8134403
3-keto-steroid reductase (Estradiol 17-beta-dehydrogenase 7)


54 
CAA75742
33199711
7-beta-hydroxysteroid dehydrogenase type 7 [Mus musculus]


55
P_695820
68440091
PREDICTED: similar to Hydroxysteroid (17-beta) dehydrogenase


56 
P_058931
8393576
hydroxysteroid (17-beta) dehydrogenase 7 [Rattus norvegicus]


57 
Q62904
8134405
3-keto-steroid reductase (Estradiol 17-beta-dehydrogenase 7)


58
AAC52623
1397235
ovarian-specific protein


59
BAC37061
26346825
unnamed protein product [Mus musculus]


60 
AAM21211
203851961
7-beta-hydroxysteroid dehydrogenase type 7 [Mus musculus]


61
P_363377
39951321
hypothetical protein MG01303.4 [Magnaporthe grisea 70-15]


62 
P_581467
76611932
PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase


63 
CAC88111
18077843
17 beta hydroxysteroid dehydrogenase [Homo sapiens]


64 
AAX42032
61361334
hydroxysteroid (17-beta) dehydrogenase 7 [synthetic construc


65
AAX42031
61361326
hydroxysteroid (17-beta) dehydrogenase 7 [synthetic construc


66 
CAI13457
55959848
hydroxysteroid (17-beta) dehydrogenase 7 [Homo sapiens]


67 
CAI15947
55959770
hydroxysteroid (17-beta) dehydrogenase 7 [Homo sapiens]


68 
AAH65246
40807207
Hydroxysteroid (17-beta) dehydrogenase 7 [Homo sapiens]


69 
AAQ89321
37183042
HSD17B7 [Homo sapiens]


70 
AAP35738
30582989
hydroxysteroid (17-beta) dehydrogenase 7 [Homo sapiens]


71 
AAH07068
13937918
Hydroxysteroid (17-beta) dehydrogenase 7 [Homo sapiens]


72 
CAC20418
12053691
17 beta-hydroxysteroid dehydrogenase type 7 [Homo sapiens]


73 
P56937
8134404
3-keto-steroid reductase (Estradiol 17-beta-dehydrogenase 7)


74
P_057455
7705421
hydroxysteroid (17-beta) dehydrogenase 7 [Homo sapiens]


75
AAF09266
6721095
17 beta-hydroxysteroid dehydrogenase type VII [Homo sapiens]


76 
ABB72853
82400271
17-beta hydroxysteroid dehydrogenase 7 [Macaca fascicularis]


77 
AAX29487
60653587
hydroxysteroid (17-beta) dehydrogenase 7 [synthetic construc


78
AAP36180
30583863
Homo sapiens hydroxysteroid (17-beta) dehydrogenase 7 [synth


79
AAF14537
6502988
17 beta-hydroxysteroid dehydrogenase type 7 [Homo sapiens]


80
AAK20950
13383374
17-beta-hydroxysteroid dehydrogenase type 7 [Oryctolagus cun


81
AAP97275
33150794
ovarian-specific protein; OSP [Homo sapiens]


82 
P_422210
50750970
PREDICTED: similar to Estradiol 17 beta-dehydrogenase 7 (17-
















TABLE 62







Examples of ERG26 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAT93045
51013503 
YGL001C [Saccharomyces cerevisiae]


2 
P53199
1723793 
Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating


3
CAA96701
1322447
unnamed protein product [Saccharomyces cerevisiae]


4 
P_446390
50287923
unnamed protein product [Candida glabrata]


5 
CAG59317
49525698 
unnamed protein product [Candida glabrata CBS138]


6 
P_453025
50306127 
unnamed protein product [Kluyveromyces lactis]


7
CAH01876
49642158 
unnamed protein product [Kluyveromyces lactis NRRL Y-1140]


8
CAC38016
13940379
putative C-3 sterol dehydrogenase [Zygosaccharomyces rouxii]


9 
P_985548
45198519 
AFR001 Wp [Eremothecium gossypii]


10 
AAS53372
44984470
AFR001Wp [Ashbya gossypii ATCC 10895]


11
P_458178
50419307
hypothetical protein DEHA0C12463g [Debaryomyces hansenii CBS767]


12 
CAG86252
49653844 
unnamed protein product [Debaryomyces hansenii CBS767]


13
P_715564
68481045 
C-3 sterol dehydrogenase/C-4 decarboxylase [Candida albicans SC53


14
P_715620
68480934 
C-3 sterol dehydrogenase/C-4 decarboxylase [Candida albicans SC53


15 
EAK96601
46437251
hypothetical protein CaO19.10427 [Candida albicans SC5314]


16
EAK96542
46437191
hypothetical protein CaO19.2909 [Candida albicans SC5314]


17
AAK69617
14582743
C-3 sterol dehydrogenase/C-4 decarboxylase [Candida albicans]


18 
P_502124
50549307 
hypothetical protein [Yarrowia lipolytica]


19 
CAG82444
49647991
unnamed protein product [Yarrowia lipolytica CLIB122]


20 
P_596741
19113533 
hypothetical protein SPBC3F6.02c [Schizosaccharomyces pombe 972h-


21
CAA17691
2924499
SPBC3F6.02c [Schizosaccharomyces pombe]


22
AAQ88129
37039511
C-3 sterol dehydrogenase [Cryptococcus neoformans var. grubii H99


23 
P_381379
46108642 
hypothetical protein FG01203.1 [Gibberella zeae PH-1]


24 
EAA67667
42544824 
hypothetical protein FG01203.1 [Gibberella zeae PH-1]


25 
EAQ90884
88183416 
conserved hypothetical protein [Chaetomium globosum CBS 148.51]


26
P_640712
66813066
3 beta-hydroxysteroid dehydrogenase [Dictypstelium discoideum AX4]


27
EAL66725
60468723 
3 beta-hydroxysteroid dehydrogenase [Dictypstelium discoideum AX4]


28 
EAT77489
111056369
hypothetical protein SNOG_15264 [Phaeosphaeria nodorum SN15]


29
P_965466
85118539
hypothetical protein [Neurospora crassa OR74A]


30 
CAE76518
38567226
related to C-3 sterol dehydrogenase (C-4 decarboxylase) [Neurospo


31
EAA36230
28927275
hypothetical protein [Neurospora crassa]


32 
P_420279
50745878
PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like


33 
P_001 . . . 
78369400 
hypothetical protein LOC616694 [Bos taurus]


34 
AAI03390
73586574 
Similar to NAD(P) dependent steroid dehydrogenase-like [Bos tauru


35 
P_001 . . . 
62859757
hypothetical protein LOC550044 [Xenopus tropicalis]


36 
AAH88699
56788986 
LOC496236 protein [Xenopus laevis]


37 
P_538199
74008671 
PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like


38 
P_853073
74008673
PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like


39 
AAH52834
31127258 
NAD(P) dependent steroid dehydrogenase-like [Mus musculus]


40
P_001 . . . 
109132673
PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like


41 
P_001 . . .
109132671
PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like


42
P_001 . . . 
57164113
NAD(P) dependent steroid dehydrogenase-like [Rattus norvegicus]


43 
AAH87626
56388600
NAD(P) dependent steroid dehydrogenase-like [Rattus norvegicus]


44 
BAE24522
74187675
unnamed protein product [Mus musculus]


45
P_035071
31982437
NAD(P) dependent steroid dehydrogenase-like [Mus musculus]


46 
Q9R1J0
8473695
Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating


47
CAA15948
7619723
NAD(P)H steroid dehydrogenase [Mus musculus]


48
AAD38448
5052206
putative NAD(P)H steroid dehydrogenase [Mus musculus]


49 
AAH19945
18043286
NAD(P) dependent steroid dehydrogenase-like [Mus musculus]


50
AAH07816
14043700
NAD(P) dependent steroid dehydrogenase-like [Homo sapiens]


51
AAH00245
12652969
NAD(P) dependent steroid dehydrogenase-like [Homo sapiens]


52
Q15738
8488997
Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (H105


53
P_057006
8393516
NAD(P) dependent steroid dehydrogenase-like [Homo sapiens]


54 
AAC50558
4457237
H105e3 [Homo sapiens]


55 
CAF99107
47222951
unnamed protein product [Tetraodon nigroviridis]


56 
P_756075
71002788
C-3 sterol dehydrogenase/C-4 decarboxylase [Aspergillus fumigatus


57 
EAL94037
66853713
C-3 sterol dehydrogenase/C-4 decarboxylase [Aspergillus fumigatus


58 
P_567299
58259773
C-3 sterol dehydrogenase (C-4 sterol decarboxylase) [Cryptococcus


59 
AAW45782
57229349
C-3 sterol dehydrogenase (C-4 sterol decarboxylase), putative [Cr


60
EAL18383
50255650
hypothetical protein CNBJ3060 [Cryptococcus neoformans var. neofo


61
P_001 . . . 
62955325
hypothetical protein LOC550369 [Danio rerio]


62
AAH93332
62204675
Zgc:112474 [Danio rerio]


63 
EAS37011
90307380
hypothetical protein CIMG_02365 [Coccidioides immitis RS]


64
P_755836
71002310
C-3 sterol dehydrogenase/C-4 decarboxylase [Aspergillus fumigatus


65
EAL93798
66853474
C-3 sterol dehydrogenase/C-4 decarboxylase [Aspergillus fumigatus


66
CAH90815
55728130
hypothetical protein [Pongo pygmaeus]


67 
P_760274
71020087
hypothetical protein UM04127.1 [Ustilago maydis 521]


68
EAK85155
46099922
hypothetical protein UM04127.1 [Ustilago maydis 521]


69
P_680844
67901176
hypothetical protein AN7575.2 [Aspergillus nidulans FGSC A4]


70
EAA62155
40742965
hypothetical protein AN7575.2 [Aspergillus nidulans FGSC A4]


71
AAZ14936
70906332
putative sterol dehydrogenase [Coprinellus disseminatus]
















TABLE 63







Examples of ERG25 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1 
AAS56153
45269545
YGR060W [Saccharomyces cerevisiae]


2
XP_448420
50291975
unnamed protein product [Candida glabrata]


3 
XP_451890
50303885 
unnamed protein product [Kluyveromyces lactis]


4 
NP_986119
45199090
AFR572Wp [Eremothecium gossypii]


5 
XP_456861
50409318 
hypothetical protein DEHA0A12661g [Debaryomyces hansenii





CBS767]


6 
XP_713420
68485318 
C-4 sterol methyl oxidase [Candida albicans SC5314]


7 
XP_461658
50426123 
hypothetical protein DEHA0G03124g [Debaryomyces hansenii





CBS767]


8 
XP_505281
50555746
hypothetical protein [Yarrowia lipolytica]


9 
XP_722703
68466442
putative C-4 sterol methyl oxidase [Candida albicans SC5314]


10
XP_722849
68466149 
putative C-4 sterol methyl oxidase [Candida albicans SC5314]


11 
ABF84061
107785180
C-4 sterol methyl oxidase [Chaetomium globosum]


12 
Q9UUH4
28558117
C-4 methylsterol oxidase (Methylsterol monooxygenase)


13
XP_962240
85106720
hypothetical protein [Neurospora crassa OR74A]


14
EAT84680
111063560
hypothetical protein SNOG_08404 [Phaeosphaeria nodorum SN15]


15 
XP_746668
70982279 
hypothetical protein Afu4g04820 [Aspergillus fumigatus Af293]


16
XP_390006
46136629
hypothetical protein FG09830.1 [Gibberella zeae PH-1]


17 
BAE65381
83775259 
unnamed protein product [Aspergillus oryzae]


18 
XP_360827
39942580
hypothetical protein MG03370.4 [Magnaporthe grisea 70-15]


19 
ABA70590
77377695 
hypothetical protein [Penicillium chrysogenum]


20 
XP_369331
39975881 
hypothetical protein MG06133.4 [Magnaporthe grisea 70-15]


21 
EAS29762
90300131
hypothetical protein CIMG_08508 [Coccidioides immitis RS]


22 
XP_762027
71023595 
hypothetical protein UM05880.1 [Ustilago maydis 521]


23 
XP_569526
58264740
C-4 methyl sterol oxidase [Cryptococcus neoformans var.





neoformans JEC21]


24
EAQ88125
88180657
hypothetical protein CHGG_04744 [Chaetomium globosum CBS





148.51]


25 
BAE66491
83776372
unnamed protein product [Aspergillus oryzae]


26 
XP_746962
70982869 
c-4 methyl sterol oxidase [Aspergillus fumigatus Af293]


27 
XP_682176
67903840 
hypothetical protein AN8907.2 [Aspergillus nidulans FGSC A4]


28 
XP_664577
67541619 
hypothetical protein AN6973.2 [Aspergillus nidulans FGSC A4]


29 
XP_646277
66825845 
hypothetical protein DDBDRAFT_0190553 [Dictyostelium





discoideum AX4]


30 
NP_998917
47523336
sterol-C4-methyl oxidase-like protein [Sus scrofa]


31 
AAI07880
79160074 
Sterol-C4-methyl oxidase-like [Homo sapiens]


32 
BAE01921
67971158 
unnamed protein product [Macaca fascicularis]


33 
XP_001 . . . 
109076099
PREDICTED: sterol-C4-methyl oxidase-like isoform 3 [Macaca





mulatta]


34 
XP_580615
61871492 
PREDICTED: similar to C-4 methylsterol oxidase (Methylsterol





monooxygenase) isoform 1 [Bos taurus]


35 
CAC24471
12311696
hypothetical protein [Candida albicans]


36
BAE30143
74185334
unnamed protein product [Mus musculus]


37 
XP_532714
57096891
PREDICTED: similar to C-4 methylsterol oxidase (Methylsterol





monooxygenase) isoform 1 [Canis familiaris]


38 
CAF92153
47211304 
unnamed protein product [Tetraodon nigroviridis]


39 
AAH63155
38649308
Sterol-C4-methyl oxidase-like [Rattus norvegicus]


40 
NP_001 . . . 
57530155 
sterol-C4-methyl oxidase-like [Gallus gallus]


41
NP_998518
47087009
sterol-C4-methyl oxidase-like [Danio rerio]


42 
NP_563789
18390767 
SMO2-2; C-4 methylsterol oxidase [Arabidopsis thaliana]


43 
AAI21457
111309060
Unknown (protein for MGC: 146461) [Xenopus tropicalis]


44 
AAM64821
21592871
putative C-4 sterol methyl oxidase [Arabidopsis thaliana]


45 
AAF79571
8778563
F22G5.23 [Arabidopsis thaliana]


46 
AAO13795
27448145
putative sterol 4-alpha-methyl-oxidase [Gossypium arboreum]


47 
AAO48604
28864263
ERG25 [Clavispora lusitaniae]


48 
AAQ83692
34978966
C-4 sterol methyl oxidase 2 [Nicotiana benthamiana]


49 
ABD97153
90658509
C-4 methyl sterol oxidase [Cryptococcus neoformans var.





neoformans]


50 
ABD97146
90658495
C-4 methyl sterol oxidase [Cryptococcus neoformans var. grubii]


51
ABD97147
90658497
C-4 methyl sterol oxidase [Cryptococcus neoformans var. grubii]


52 
ABD97134
90658471
C-4 methyl sterol oxidase [Cryptococcus neoformans var.





neoformans]


53 
AAL82576
27447203
putative sterol 4-alpha-methyl-oxidase [Zea mays]


54 
NP_850133
30684225
SMO2-1; C-4 methylsterol oxidase [Arabidopsis thaliana]


55 
NP_973559
42570971
SMO2-1; C-4 methylsterol oxidase [Arabidopsis thaliana]


56 
AAL32287
16973432
sterol 4-alpha-methyl-oxidase [Arabidopsis thaliana]


57 
ABE83226
92875070
Sterol desaturase [Medicago truncatula]


58 
BAF28920
113645779
Os11g0707600 [Oryza sativa (japonica cultivar-group)]


59
BAF20592
113610214
Os07g0101500 [Oryza sativa (japonica cultivar-group)]


60 
XP_787442
72077919
PREDICTED: similar to C-4 methylsterol oxidase (Methylsterol





monooxygenase) [Strongylocentrotus purpuratus]


61
AAM64359
21592408
putative C-4 sterol methyl oxidase [Arabidopsis thaliana]


62 
NP_973777
42571373
SMO2-2; C-4 methylsterol oxidase [Arabidopsis thaliana]


63 
NP_001 . . . 
62865628
sterol-C4-methyl oxidase-like isoform 2 [Homo sapiens]


64
AAX95419
62733302
4-alpha-methyl-sterol C4-methyl-oxidase [Oryza sativa (japonica





cultivar-group)]


65
XP_883875
76638226
PREDICTED: similar to C-4 methylsterol oxidase (Methylsterol





monooxygenase) isoform 3 [Bos taurus]


66 
ABE87434
92884635
Sterol desaturase [Medicago truncatula]


67 
XP_641553
66814748
hypothetical protein DDBDRAFT_0205936 [Dictyostelium





discoideum AX4]


68
AAM65428
21593461
putative C-4 sterol methyl oxidase [Arabidopsis thaliana]


69
NP_567669
18416002
SMO1-3 (STEROL 4-alpha METHYL OXIDASE); catalytic





[Arabidopsis thaliana]


70 
AAM64961
21593012
putative C-4 sterol methyl oxidase [Arabidopsis thaliana]


71
AAN18115
23308291
At4g12110/F16J13_180 [Arabidopsis thaliana]


72 
AAK61361
27446631
putative sterol 4-alpha-methyl-oxidase [Arabidopsis thaliana]


73
BAF01201
110738551
hypothetical protein [Arabidopsis thaliana]


74 
AAQ13424
33337546
sterol-4-methyl-oxidase [Arabidopsis thaliana]


75 
BAF27120
113639815
Os10g0545200 [Oryza sativa (japonica cultivar-group)]


76 
CAB78254
7267912
putative C-4 sterol methyl oxidase [Arabidopsis thaliana]


77 
AAQ94118
37591406
sterol-4-alpha methyl oxidase [Arabidopsis thaliana]


78
AAQ83691
34978964
C-4 sterol methyl oxidase 1 [Nicotiana benthamiana]


79 
ABD65536
89266491
sterol-C4-methyl oxidase-like [Ictalurus punctatus]


80 
BAC57961
28804511
putative C-4 sterol methyl oxidase [Aster tripolium]
















TABLE 64







Examples of ERG24 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAB30203
545906
sterol delta 14 reductase; Erg24p [Saccharomyces cerevisiae]


2
XP_447380
50289897
hypothetical protein CAGL0I02970g [Candida glabrata CBS138]


3 
XP_452744
50305569
unnamed protein product [Kluyveromyces lactis]


4
NP_985893
45198864
AFR346Wp [Eremothecium gossypii]


5 
XP_710670
68491033
sterol C-14 reductase [Candida albicans SC5314]


6 
XP_458371
50419687
hypothetical protein DEHA0C16984g [Debaryomyces hansenii





CBS767]


7 
XP_501260
50547581
hypothetical protein [Yarrowia lipolytica]


8
XP_566548
58258271
C-14 sterol reductase [Cryptococcus neoformans var. neoformans





JEC21]


9 
NP_596767
19113559
hypothetical protein SPBC16G5.18 [Schizosaccharomyces pombe





972h-]


10
EAL23454
50260804
hypothetical protein CNBA1040 [Cryptococcus neoformans var.





neoformans B-3501A]


11
XP_759786
71019111
hypothetical protein UM03639.1 [Ustilago maydis 521]


12
XP_386782
46124457
ER24_FUSSO Delta(14)-sterol reductase (C-14 sterol reductase)





(Sterol C14-reductase) [Gibberella zeae PH-1]


13
P_78575
6015106
Delta(14)-sterol reductase (C-14 sterol reductase) (Sterol C14-





reductase)


14
Q01447
3929349
Delta(14)-sterol reductase (C-14 sterol reductase) (Sterol C14-





reductase)
















TABLE 65







Examples of ERG11 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAA34546
171354
lanosterol 14 -demethylase cyto chrome P450


2
AAA34547
171356
lanosterol 14 -demethylase cyto chrome P450


3
AAY59417
66967944
14 alpha-demethylase [Candida glabrata]


4
XP_454109
50308217
unnamed protein product [Kluyveromyces lactis]


5
Q759W0
51701328
Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alpha





demethylase) (Lanosterol 14-alpha demethylase) (P450-14DM)


6
AAB32679
912807
cytochrome P-450 lanosterol-alpha-demethylase; P450-L1A1





[Candida glabrata]


7
AAX39316
61189834
lanosterol 14 alpha demethylase [Candida tropicalis]


8
AAF00598
6006769
cytochrome P450 lanosterol 14-alpha demethylase [Candida





albicans]


9
XP_716761
68478280
lanosterol 14-alpha-demethylase [Candida albicans SC5314]


10
XP_460143
50423125
hypothetical protein DEHA0E20383g [Debaryomyces hansenii





CBS767]


11
ABC41921
83728463
cytochrome P450 lanosterol 14 alpha demethylase [Candida





albicans]


12
AAX39315
61189832
lanosterol 14 alpha demethylase [Candida tropicalis]


13
O4CK51
65689
lanosterol 14 alpha-demethylase (EC 1.14.14.-) cytochrome P450 





51- yeast (Candida albicans)


14
XP_716822
68478161
lanosterol 14-alpha-demethylase [Candida albicans SC5314]


15
AAF00603
6006774
cytochrome P450 lanosterol 14-alpha demethylase [Candida





albicans]


16
AAF00600
6006771
cytochrome P450 lanosterol 14-alpha demethylase [Candida





albicans]


17
BAB03401
9558446
CYP51 variant 3 [Candida albicans]


18
AAK57519
14280372
lanosterol 14-alpha demethylase Erg11p [Candida dubliniensis]


19
AAF00602
6006773
cytochrome P450 lanosterol 14-alpha demethylase [Candida





albicans]


20
AAF00601
6006772
cytochrome P450 lanosterol 14-alpha demethylase [Candida





albicans]


21
BAB03400
9558444
CYP51 variant 2 [Candida albicans]


22
AAO83898
29378393
cytochrome P-450 lanosterol-alpha-demethylase [Issatchenkia





orientalis]


23
AAW50593
57341382
Erg11p [Candida albicans]


24
AAW50592
57341380
Erg11p [Candida albicans]


25
XP_500518
50545962
hypothetical protein [Yarrowia lipolytica]


26
BAC16517
23263326
cytochrome P-450 lanosterol 14 alpha-demethylase [Candida





albicans]


27
BAC16520
23263332
cytochrome P-450 lanosterol 14 alpha-demethylase [Candida





albicans]


28
BAC16518
23263328
cytochrome P-450 lanosterol 14 alpha-demethylase [Candida





albicans]


29
BAC16519
23263330
cytochrome P-450 lanosterol 14 alpha-demethylase [Candida





albicans]


30
Q02315
2493385
Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alpha





demethylase) (Lanosterol 14-alpha demethylase) (P450-14DM)


31
AAO38776
28395121
lanosterol 14 alpha demethylase; ERG11 [Pneumocystis carinii]


32
ABG91757
110816094
sterol 14 alpha-demethylase [Pneumocystis carinii]


33
BAE60239
83770104
unnamed protein product [Aspergillus oryzae]


34
XP_749134
70987441
14-alpha sterol demethylase Cyp51B [Aspergillus fumigatus Af293]


35
XP_659505
67522889
hypothetical protein AN1901.2 [Aspergillus nidulans FGSC A4]


36
XP_681552
67902592
hypothetical protein AN8283.2 [Aspergillus nidulans FGSC A4]


37
AAK73659
14861413
14-alpha sterol demethylase [Aspergillus fumigatus]


38 
XP_752137
70994720
14-alpha sterol demethylase Cyp51A [Aspergillus fumigatus Af293]


39
BAE57417
83767278
unnamed protein product [Aspergillus oryzae]


40
AAF79204
8778097
cytochrome P450 sterol 14 alpha-demethylase [Emericella nidulans]


41 
CAE18091
33300264
eburicol 14 alpha demethylase [Blumeria graminis]


42 
EAS28723
90299092
cytochrome P450 51 [Coccidioides immitis RS]


43 
CAE18094
33300270
eburicol 14 alpha demethylase [Blumeria graminis]


44 
CAC85624
33300256
eburicol 14 alpha demethylase [Blumeria graminis f. sp. tritici]


45 
CAE18095
33300272
eburicol 14 alpha demethylase [Blumeria graminis]


46 
CAE17515
33284834
eburicol 14 alpha demethylase [Blumeria graminis f. sp. tritici]


47 
AAU43734
52352491
eburicol 14 alpha-demethylase [Mycosphaerella graminicola]


48 
EAS35219
90305588
cytochrome P450 51 [Coccidioides immitis RS]


49 
CAE18102
33300286
eburicol 14 alpha demethylase [Blumeria graminis]


50
CAE18103
33300288
eburicol 14 alpha demethylase [Blumeria graminis]


51
CAE18105
33300292
eburicol 14 alpha demethylase [Blumeria graminis]


52 
NP_592990
19113902
hypothetical protein SPAC13A11.02c [Schizosaccharomyces pombe





972h-]


53 
CAE18100
33300282
eburicol 14 alpha demethylase [Blumeria graminis]


54 
AAP79601
32330152
eburicol 14 alpha-demethylase [Mycosphaerella graminicola]


55
AAC97606
4049645
eburicol 14 alpha demethylase; CYP51; cytochrome P450 sterol 14-





demethylase [Blumeria graminis f. sp. hordei]


56 
CAE18099
33300280
eburicol 14 alpha demethylase [Blumeria graminis]


57 
BAE63554
83773427
unnamed protein product [Aspergillus oryzae]


58
XP_381176
46108236
hypothetical protein FG01000.1 [Gibberella zeae PH-1]


59
AAF85983
9230788
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


60
AAP81934
32441730
eburicol 14 alpha-demethylase [Mycosphaerella graminicola]


61
XP_362183
39945292
hypothetical protein MG04628.4 [Magnaporthe grisea 70-15]


62 
AAP12370
30314338
lanosterol 14 alpha-demethylase; 14 alpha lanosterol demethylase





[Cryptococcus neoformans var. grubii]


63
AAF74756
8347731
eburicol 14-alpha demethylase [Mycosphaerella graminicola]


64
AAF76464
8570176
14 alpha-demethylase [Venturia inaequalis]


65
XP_566464
58258103
sterol 14-demethylase [Cryptococcus neoformans var. neoformans





JEC21]


66
EAQ93417
88185949
conserved hypothetical protein [Chaetomium globosum CBS 148.51]


67
AAL79180
18766932
eburicol 14 alpha-demethylase [Monilinia fructicola]


68 
AAU01157
51341094
lanosterol 14-alpha-demethylase [Coccidioides posadasii]


69
CAD27793
19572745
cytochrome P-450 14DM [Penicillium digitatum]


70 
XP_384268
46116500
hypothetical protein FG04092.1 [Gibberella zeae PH-1]


71 
AAG18433
10505323
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


72 
AAK26391
13445823
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


73 
AAG18431
10505318
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


74
AAK26386
13445813
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


75 
AAD55135
5881952
eburicol 14-alpha demethylase; cytochrome P450 sterol 14-alpha





demethylase; Erg11 [Uncinula necator]


76 
AAK26389
13445819
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


77
CAC85409
15864613
euburicol 14 alpha-demethylase [Venturia nashicola]


78
BAB03659
9664027
cytochrome P-450 14DM [Penicillium digitatum]


79
AAG18435
10505329
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


80
AAG18434
10505326
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


81
AAU01158
51341096
lanosterol 14-alpha-demethylase [Ajellomyces capsulatus]


82 
AAK26387
13445815
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


83
AAG18432
10505321
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


84 
AAK26388
13445817
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


85
XP_391200
46139019
hypothetical protein FG11024.1 [Gibberella zeae PH-1]


86
AAK26390
13445821
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


87 
O14442
14916976
Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alpha





demethylase) (Eburicol 14-alpha-demethylase) (P450-14DM)


88 
AAG18438
10505336
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


89 
XP_759809
71019157
sterol 14-alpha demethylase [Ustilago maydis 521]


90 
AAF18468
6581118 
eburicol 14 alpha-demethylase [Tapesia acuformis]


91
AAG18436
10505331
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


92 
AAC49801
5733843
eburicol 14-alpha demethylase [Uncinula necator]


93 
ABE01107
908232111
4 alpha demethylase [Blumeriella jaapii]


94 
AAG18437
10505334
eburicol 14 alpha-demethylase [Botryotinia fuckeliana]


95
CAD27792
19572743
cytochrome P-450 14DM [Penicillium digitatum]


96 
XP_964049
85111674
hypothetical protein [Neurospora crassa OR74A]


97 
AAF18469
11178694
eburicol 14 alpha-demethylase [Tapesia yallundae]


98
Q12664
2493386 
Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alpha





demethylase) (Eburicol 14-alpha-demethylase) (P450-14DM)


99 
AAG44832
12006321
eburicol 14-alpha demethylase [Tapesia yallundae]


100
AAG44831
12006319
eburicol 14-alpha demethylase [Tapesia yallundae]


101
AAN28927
23505745
sterol 14 alpha-demethylase ERG11 [Leptosphaeria maculans]


102 
XP_361987
39944900
hypothetical protein MG04432.4 [Magnaporthe grisea 70-15]


103
EAT88907
111067787
hypothetical protein SNOG_03702 [Phaeosphaeria nodorum SN15]


104 
AAU01160
51341100
lanosterol 14-alpha-demethylase [Phanerochaete chrysosporium]


105 
AAC23550
3220152 
cytochrome P450 L1A1 demethylase [Pichia anomala]


106
AAU01159
51341098
lanosterol 14-alpha-demethylase [Coprinopsis cinerea]


107
Q9UVC3
12229768
Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alpha





demethylase) (Lanosterol 14-alpha demethylase) (P450-14DM)


108 
AAQ88128
37039509
cytochrome P450 lanosterol 14a-demethylase [Cryptococcus





neoformans var. grubii H99]


109 
NP_064394
71061451
cytochrome P450, family 51 [Mus musculus]


110 
EAL24154
51094909
cytochrome P450, family 51, subfamily A, polypeptide 1 





[Homo sapiens]


111 
Q16850
3915660
Cytochrome P450 51A1 (CYPLI) (P45011) (Sterol 14-alpha





demethylase) (Lanosterol 14-alpha demethylase) (LDM) (P450-





14DM) (P45014DM)


112
NP_999597
47523914
cytochrome P450 51 [Sus scrofa]


113
BAC27231
26326975
unnamed protein product [Mus musculus]


114 
Q5RE72
83287777
Cytochrome P450 51A1 (CYPLI) (P45011) (Sterol 14-alpha





demethylase) (Lanosterol 14-alpha demethylase) (LDM) (P450-





14DM) (P45014DM)


115 
Q4PJW3
7507506614
Cytochrome P450 51A1 (CYPLI) (P45011) (Sterol 14-alpha





demethylase) (Lanosterol 14-alpha demethylase) (LDM) (P450-





DM) (P45014DM)


116 
AAF74562
8347236
lanosterol 14-alpha-demethylase [Mus musculus]


117 
AAC50951
1698484 
lanosterol 14-alpha demethylase [Homo sapiens]


118 
XP_532457
57095976
PREDICTED: similar to Cytochrome P450 51A1 (CYPLI) (P450LI)





(Sterol 14-alpha demethylase) (Lanosterol 14-alpha demethylase)





(LDM) (P450-14DM) (P45014DM) isoform 1 [Canis familiaris]


119 
AAF73986
8215679 
lanosterol 14-alpha-demethylase [Mus musculus]


120
AAH81210
51703589
MGC84806 protein [Xenopus laevis]


121
AAA87074
699396
lanosterol 14-alpha-demethylase


122
XP_418650
50732469
PREDICTED: similar to lanosterol 14-demethylase [Gallus gallus]


123
BAE01508
67970330
unnamed protein product [Macaca fascicularis]


124
AAR89624
40748287
14-alpha demethylase [Fundulus heteroclitus]


125 
NP_001 . . . 
50053648
cytochrome P450, family 51 [Strongylocentrotus purpuratus]


126
AAR89625
40748289
14-alpha demethylase [Danio rerio]


127
NP_001 . . . 
99028936
cytochrome P450, family 51 [Danio rerio]


128 
CAJ81841
89268132
cytochrome P450, family 51, subfamily A, polypeptide 1 [Xenopus





tropicalis]


129 
AAR89626
40748291
14-alpha demethylase [Abudefduf saxatilis]
















TABLE 66







Examples of ERG4 polypeptides.










Row
ACCESSION
GI
PROTEIN DESCRIPTION













1
AAD13895
4261595
Unknown [Saccharomyces cerevisiae]


2
AAT93224
51013861
YGL012W [Saccharomyces cerevisiae]


3
AAY42962
66270055
C24 sterol reductase [Candida glabrata]


4
XP_451223
50302575
unnamed protein product [Kluyveromyces lactis]


5
NP_986579
45201009
AGL087Cp [Eremothecium gossypii]


6
XP_456709
50407411
hypothetical protein DEHA0A08888g [Debaryomyces hansenii CBS767]


7
XP_717662
68476402
sterol C-24 (28) reductase [Candida albicans SC5314]


8
XP_503021
50551095
hypothetical protein [Yarrowia lipolytica]


9
EAU37607
114195907 
Delta(24(24(1)))-sterol reductase [Aspergillus terreus NIH2624]


10
BAE61064
83770931
unnamed protein product [Aspergillus oryzae]


11
NP_594742
19115654
hypothetical protein SPAC20G4.07c [Schizosaccharomyces pombe 972h-]


12
CAA45113
5109
sts1+ [Schizosaccharomyces pombe]


13
XP_662788
67538028
hypothetical protein AN5 184.2 [Aspergillus nidulans FGSC A4]


14
XP_750461
70991224
c-24(28) sterol reductase [Aspergillus fumigatus Af293]


15
EAS37114
90307483
hypothetical protein CIMG_02468 [Coccidioides immitis RS]


16
XP_365763
39968745
hypothetical protein MG02465.4 [Magnaporthe grisea 70-15]


17
CAC18223
16944336
probable sterol C-24 reductase [Neurospora crassa]


18
XP_961419
85102913
probable sterol C-24 reductase [MIPS] [Neurospora crassa OR74A]


19
XP_660288
67524453
hypothetical protein AN2684.2 [Aspergillus nidulans FGSC A4]


20
EAU33849
114192149 
Delta(24(24(1)))-sterol reductase [Aspergillus terreus NIH2624]


21
XP_753221
70996933
c-24(28) sterolreductase [Aspergillus fumigatus Af293]


22
BAE59624
83769489
unnamed protein product [Aspergillus oryzae]


23
EAT92432
111071312 
predicted protein [Phaeosphaeria nodorum SN15]


24
XP_390179
46136975
hypothetical protein FG10003.1 [Gibberella zeae PH-1]


25
XP_757645
71005958
hypothetical protein UM01498.1 [Ustilago maydis 521]


26
EAS37449
90307818
hypothetical protein CIMG_02803 [Coccidioides immitis RS]


27
NP_820201
29654509
c-24(28) sterol reductase, putative [Coxiella burnetii RSA 493]


28
ZP_012 . . . 
94491050
hypothetical protein CburD_01001859 [Coxiella burnetii Dugway 7E9-12]


29
AAQ88130
37039513
sterol C-24 reductase [Cryptococcus neoformans var. grubii H99]


30
XP_569697
58265082
delta24(24-1) sterol reductase [Cryptococcus neoformans var.





neoformans JEC21]


31
EAQ90721
88183253
hypothetical protein CHGG_02656 [Chaetomium globosum CBS 148.51]


32
BAE55606
83765463
unnamed protein product [Aspergillus oryzae]


33
CAJ06078
68128884
sterol C-24 reductase, putative [Leishmania major]


34
ABD46555
88601114
sterol C-24 reductase-like protein [Acanthamoeba castellanii]


35
XP_638613
66809779
ERG4/ERG24 ergosterol biosynthesis protein family protein





[Dictyostelium discoideum AX4]
















TABLE 67







Examples of beta-carotene 15,15′-monooxygenase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION












AAG15381
10242318
beta,beta-carotene 15,15′-dioxygenase [Mus musculus]


EDL92648
149038288
beta-carotene 15,15′-monooxygenase [Rattus norvegicus]


Q91XT5
46397349
Beta,beta-carotene 15,15′-monooxygenase (beta-carotene dioxygenase 1)


XP_546815
57087275
PREDICTED: similar to beta,beta-carotene 15,15-monooxygenase




(beta-carotene dioxygenase 1) [Canis familiaris]


XP_001 . . . 
149699876
PREDICTED: similar to beta,beta-carotene 15,15-dioxygenase




[Equus caballus]


EAW95537
119615943
beta-carotene 15,15′-monooxygenase 1, isoform CRA_a [Homo sapiens]


Q9HAY6
41688803
beta,beta-carotene 15,15′-monooxygenase (beta-carotene dioxygenase 1)


BAA91776
7022941
unnamed protein product [Homo sapiens]


BAC35679
26344045
unnamed protein product [Mus musculus]


NP_001 . . . 
66792910
beta-carotene 15,15′-monooxygenase 1 [Bos taurus]


XP_001 . . . 
126303742
PREDICTED: similar to beta,beta-carotene 15,15-dioxygenase




[Monodelphis domestica]


XP_523435
114663815
PREDICTED: beta-carotene 15,15′-monooxygenase 1 [Pan troglodytes]


XP_414163
50753878
PREDICTED: beta-carotene 15,15′-monooxygenase 1 [Gallus gallus]


EAW95538
119615944
beta-carotene 15,15′-monooxygenase 1, isoform CRA_b [Homo sapiens]


AAH56789
34784018
Zgc:63614 [Danio rerio]


NP_571873
42476258
beta-carotene 15,15′-monooxygenase 1 [Danio rerio]


CAC37566
13872740
putative b,b-carotene-15,15′-dioxygenase [Danio rerio]


CAF95764
47214429
unnamed protein product [Tetraodon nigroviridis]


CAF92469
47212035
unnamed protein product [Tetraodon nigroviridis]


ABQ09267
146186430
beta-carotene 15,15′-monooxygenase 1 [Oryzias latipes]


CAM14044
122890964
beta-carotene 15,15-dioxygenase 2 [Danio rerio]


AAI33726
126631776
Bcdo2 protein [Rattus norvegicus]


CAC37567
13872742
putative b,b-carotene-9′,10′-dioxygenase [Danio rerio]


AAI07007
76825286
beta-carotene 9′,10′-dioxygenase 2 [Mus musculus]


AAI35025
141795614
Bcdo2l protein [Danio rerio]


NP_001 . . . 
55741954
beta-carotene dioxygenase 2 [Xenopus tropicalis]


XP_417929
118102019
PREDICTED: similar to carotene-9,10-monooxygenase [Gallus gallus]


Q5RF16
75042584
beta,beta-carotene 9′,10′-dioxygenase (beta-carotene dioxygenase 2)




(B-diox-II)


XP_001 . . . 
109108669
PREDICTED: beta-carotene dioxygenase 2 [Macaca mulatta]


BAC41782
26449309
hypothetical protein [Macaca fascicularis]


Q8HXG8
47117670
beta,beta-carotene 9′,10′-dioxygenase (beta-carotene dioxygenase 2)




(B-diox-II)


AAI15260
92098295
beta-carotene 15,15-dioxygenase 2 [Danio rerio]


AAS20392
42560440
carotene-9′,10′-monooxygenase [Mustela putorius furo]


CAG03680
47217728
unnamed protein product [Tetraodon nigroviridis]


XP_536572
73955144
PREDICTED: similar to beta,beta-carotene 9,10-dioxygenase (beta-




carotene dioxygenase 2) (B-diox-II) [Canis familiaris]


XP_001 . . . 
126327024
PREDICTED: similar to carotene-9,10-monooxygenase [Monodelphis




domestica]


XP_001 . . . 
114640348
PREDICTED: beta-carotene dioxygenase 2 isoform 3 [Pan troglodytes]


XP_001 . . . 
114640346
PREDICTED: beta-carotene dioxygenase 2 isoform 4 [Pan troglodytes]


AAK69433
14582265
putative carotene dioxygenase [Homo sapiens]


Q9BYV7
41688802
beta,beta-carotene 9′,10′-dioxygenase (beta-carotene dioxygenase 2)




(B-diox-II)


EAW67194
119587598
beta-carotene dioxygenase 2, isoform CRA_f [Homo sapiens]


EAW67189
119587593
beta-carotene dioxygenase 2, isoform CRA_a [Homo sapiens]


XP_001 . . . 
149716895
PREDICTED: similar to carotene-9,10-monooxygenase [Equus caballus]


NP_001 . . . 
82617628
beta-carotene dioxygenase 2 isoform b [Homo sapiens]


NP_114144
82617624
beta-carotene dioxygenase 2 isoform a [Homo sapiens]


CAC27994
12666531
putative b,b-carotene-9′,10′-dioxygenase [Homo sapiens]


XP_508757
114640350
PREDICTED: hypothetical protein isoform 5 [Pan troglodytes]


BAB55379
14042749
unnamed protein product [Homo sapiens]


EAW67193
119587597
beta-carotene dioxygenase 2, isoform CRA_e [Homo sapiens]


NP_001 . . . 
147906096
hypothetical protein LOC791719 [Danio rerio]


XP_001 . . . 
125824393
PREDICTED: similar to retinal pigment epithelium 65b [Danio rerio]


AAH59559
37748750
Zgc:73213 [Danio rerio]


AAC14586
675485
retinal pigment epithelium-specific 61 kDa protein [Homo sapiens]


XP_001 . . . 
109008381
PREDICTED: retinal pigment epithelium-specific protein 65 kDa




[Macaca mulatta]


NP_001 . . . 
71480121
retinal pigment epithelium 65b [Danio rerio]


NP_084263
147902089
retinal pigment epithelium 65 [Mus musculus]


AAD42042
5326773
retinal pigment epithelium-specific protein RPE65 [Cercopithecus




aethiops]


AAL01119
15488446
RPE65 [Mus musculus]


CAA46988
564
membrane receptor p63 [Bos taurus]


AAC37306
163657
retinal pigment epithelium-specific 65 kD protein


EDL82582
149026339
retinal pigment epithelium 65 [Rattus norvegicus]


NP_446014
16758332
retinal pigment epithelium 65 [Rattus norvegicus]


NP_001 . . . 
148228575
retinal pigment epithelium-specific protein 65 kDa [Xenopus laevis]


AAC72356
3851555
retinal pigment epithelium-specific protein RPE65 [Canis familiaris]


CAF98473
47220374
unnamed protein product [Tetraodon nigroviridis]


NP_001 . . . 
50978910
retinal pigment epithelium-specific protein 65 kDa [Canis lupus




familiaris]


AAD12758
4001821
RPE65 protein; retinal pigment epithelium 65-protein [Ambystoma




tigrinum]


XP_001 . . . 
126305965
PREDICTED: similar to membrane receptor p63 [Monodelphis




domestica]


NP_001 . . . 
156120623
hypothetical protein LOC514135 [Bos taurus]


Q9YGX2
48475042
Retinal pigment epithelium-specific 65 kDa protein


NP_001 . . . 
147906384
MGC85437 protein [Xenopus laevis]


NP_001 . . . 
118344140
beta-carotene-15,15′-monooxygenase [Ciona intestinalis]


BAC41351
26005798
retinal pigment epithelium abundant protein [Cynops pyrrhogaster]


XP_001 . . . 
114557125
PREDICTED: retinal pigment epithelium-specific protein 65 kDa 




[Pan troglodytes]


NP_001 . . . 
148230104
beta-carotene dioxygenase 2 [Xenopus laevis]


XP_001 . . . 
114640352
PREDICTED: beta-carotene dioxygenase 2 isoform 2 [Pan troglodytes]


XP_001 . . . 
115928922
PREDICTED: similar to beta-carotene 15,15-dioxygenase




[Strongylocentrotus purpuratus]


AAL39096
17432605
RPE65 [Mus musculus]


XP_001 . . . 
125816256
PREDICTED: similar to beta-carotene 15,15-dioxygenase 2 




[Danio rerio]


XP_001 . . . 
156342819
hypothetical protein NEMVEDRAFT_v1g222532 [Nematostella




vectensis]


XP_001 . . . 
125824367
PREDICTED: similar to retinal pigment epithelium 65b [Danio rerio]


XP_001 . . . 
156393603
predicted protein [Nematostella vectensis]


XP_001 . . . 
156371447
predicted protein [Nematostella vectensis]


AAH67696
45767835
Bcdo2l protein [Danio rerio]


CAD45010
22657452
retinal pigment epithelium-specific protein [Canis familiaris]


NP_001 . . . 
118344130
RPE65 homolog [Ciona intestinalis]


XP_317319 
118789286
ENSANGP00000006854 [Anopheles gambiae str. PEST]


EAA12399
157014990
AGAP008143-PA [Anopheles gambiae str. PEST]


AAY85350
68132170
carotenoid 9′,10′ monoxygenase II [Rattus norvegicus]


XP_001 . . . 
115969938
PREDICTED: similar to beta-carotene 15,15-dioxygenase, partial




[Strongylocentrotus purpuratus]


XP_001 . . . 
157135394
beta-carotene dioxygenase [Aedes aegypti]


XP_967460
91093114
PREDICTED: similar to CG9347-PA [Tribolium castaneum]


NP_496729
71998242
Y46G5A.24 [Caenorhabditis elegans]


XP_001 . . . 
156398339
predicted protein [Nematostella vectensis]


XP_394000
66523635
PREDICTED: similar to neither inactivation nor afterpotential B




CG9347-PA isoform 1 [Apis mellifera]


F88115
25395537
protein F53C3.12 [imported] - Caenorhabditis elegans


AAC67462
26251528
Hypothetical protein F53C3.12 [Caenorhabditis elegans]


XP_001 . . . 
149709742
PREDICTED: similar to retinal pigment epithelium abundant protein




RPE65 [Equus caballus]


CAE71494
39582162
Hypothetical protein CBG18419 [Caenorhabditis briggsae]


CAE71509
39582177
Hypothetical protein CBG18441 [Caenorhabditis briggsae]


XP_001 . . . 
156555525
PREDICTED: similar to beta-carotene dioxygenase [Nasonia




vitripennis]


XP_001 . . . 
125824371
PREDICTED: similar to retinal pigment epithelium 65b [Danio rerio]


CAF91639
47209442
unnamed protein product [Tetraodon nigroviridis]


CAG02881
47222516
unnamed protein product [Tetraodon nigroviridis]


CAG06487
47224917
unnamed protein product [Tetraodon nigroviridis]


EDL95460
149041619
beta-carotene 9′,10′-dioxygenase 2 [Rattus norvegicus]


YP_001 . . . 
154707125
putative dioxygenase [Coxiella burnetii Dugway 7E9-12]


NP_650307
24646669
neither inactivation nor afterpotential B CG9347-PA [Drosophila




melanogaster]


BAA94508
7593040
DRPE65 [Drosophila melanogaster]


ZP_019 . . . 
153206838
dioxygenase, putative [Coxiella burnetii ′MSU Goat Q177′]


AAH92162
62132948
Zgc:110538 [Danio rerio]


YP_444280
83814867
15,15′ beta carotene dioxygenase [Salinibacter ruber DSM 13855]


BAB32248
12861637
unnamed protein product [Mus musculus]


EAW67192
119587596
beta-carotene dioxygenase 2, isoform CRA_d [Homo sapiens]


XP_001 . . . 
114640354
PREDICTED: hypothetical protein isoform 1 [Pan troglodytes]


BAC03747
21750237
unnamed protein product [Homo sapiens]


EAW67190
119587594
beta-carotene dioxygenase 2, isoform CRA_b [Homo sapiens]


XP_001 . . . 
125774315
GA21719-PA [Drosophila pseudoobscura]


YP_001 . . . 
134096631
lignostilbene-alpha/ beta-dioxygenase [Saccharopolyspora erythraea




NRRL 2338]


EAW67191
119587595
beta-carotene dioxygenase 2, isoform CRA_c [Homo sapiens]


XP_001 . . . 
149486496
PREDICTED: similar to b,b-carotene-9,10-dioxygenase, partial




[Ornithorhynchus anatinus]


AAO90531
29541592
dioxygenase, putative [Coxiella burnetii RSA 493]


XP_001 . . . 
109129384
PREDICTED: similar to beta,beta-carotene 15,15-monooxygenase




(beta-carotene dioxygenase 1) [Macaca mulatta]


CAJ53109
109626642
beta,beta-carotene 9′,10′-dioxygenase 2 [Haloquadratum walsbyi DSM




16790]


XP_001 . . . 
109129778
PREDICTED: similar to beta,beta-carotene 15,15-monooxygenase




(beta-carotene dioxygenase 1), partial [Macaca mulatta]


XP_001 . . . 
118109416
PREDICTED: similar to beta-carotene 15,15-dioxygenase, partial




[Gallus gallus]


ABF70124
102139989
dioxygenase-related protein [Musa balbisiana]


AAW59435
57918684
decreased apical dominance protein [Petunia x hybrida]


EAY74583
125526469
hypothetical protein OsI_002430 [Oryza sativa (indica cultivar-group)]


AAL66961
18377622
unknown protein [Arabidopsis thaliana]


EAY74584
125526470
hypothetical protein OsI_002431 [Oryza sativa (indica cultivar-group)]


BAC05598
21902049
putative dioxygenase [Oryza sativa (japonica cultivar-group)]


AAW33596
57116144
Dad1/CCD8 [Petunia x hybrida]


NP_001 . . . 
115439899
Os01g0746400 [Oryza sativa (japonica cultivar-group)]


EAY75798
125527684
hypothetical protein OsI_003645 [Oryza sativa (indica cultivar-group)]


EAZ13518
125572003
hypothetical protein OsJ_003343 [Oryza sativa (japonica cultivar-group)]


ABQ08577
146160696
beta-carotene 15,15′-monooxygenase 2 [Oryzias latipes]


BAB63485
15289786
retinal pigment epithelium 65-like [Oryza sativa (japonica cultivar-group)]


AAS66906
45504725
dioxygenase RAMOSUS1 [Pisum sativum]


ZP_013 . . . 
95927318
hypothetical protein CburR_01000925 [Coxiella burnetii RSA 331]


YP_658115
110668304
beta,beta-carotene 15,15′-monooxygenase; beta-carotene dioxygenase 1




[Haloquatratum walsbyi DSM 16790]


CAL90971
121495644
torulene oxygenase [Gibberella fujikuroi]


YP_134677
55376826
retinal pigment epithelial membrane protein [Haloarcula marismortui




ATCC 43049]


CAL90970
121495642
torulene oxygenase [Gibberella fujikuroi]


XP_382801
46111487
hypothetical protein FG02625.1 [Gibberella zeae PH-1]


XP_001 . . . 
149480289
PREDICTED: similar to carotene-9,10-monooxygenase, partial




[Ornithorhynchus anatinus]


ABQ76053
148508268
beta,beta-carotene 9′,10′-dioxygenase 2 [uncultured haloarchaeon]


YP_657779
110667968
beta,beta-carotene 9′,10′-dioxygenase 2 [Haloquatratum walsbyi




DSM 16790]


XP_001 . . . 
109149184
PREDICTED: similar to beta,beta-carotene 15,15-monooxygenase




(beta-carotene dioxygenase 1), partial [Macaca mulatta]


AAP92577
33086530
Ab2-079 [Rattus norvegicus]


ABN50352
125662819
carotenoid cleavage dioxygenase 1 [Hypcrea jecorina]


EAL93736
66853412
dioxygenase, putative [Aspergillus fumigatus Af293]


XP_001 . . . 
125876361
PREDICTED: hypothetical protein, partial [Danio rerio]


XP_001 . . . 
119481741
dioxygenase, putative [Neosartorya fischeri NRRL 181]


XP_001 . . . 
119494253
retinal pigment epithelial membrane family protein [Neosartorya




fischeri NRRL 181]


XP_958452
85090512
hypothetical protein [Neurospora crassa OR74A]


ED064867
157069539
predicted protein [Neurospora crassa OR74A]


XP_001 . . . 
121716178
dioxygenase, putative [Aspergillus clavatus NRRL 1]


CAL64769
148353839
putative carotene oxygenase [Blakeslea trispora]


BAD79505
56686283
lignostilbene-alpha beta-dioxygenase [Synechococcus elongatus




PCC 6301]


ZP_016 . . . 
119509407
Retinal pigment epithelial membrane protein [Nodularia spumigena




CCY9414]


BAE56886
83766746
unnamed protein product [Aspergillus oryzae]


BAE59247
83769110
unnamed protein product [Aspergillus oryzae]


ECC98172
139038333
hypothetical protein GOS_5249294 [marine metagenome]


ZP_017 . . . 
126656631
beta-carotene 15,15′-dioxygenase [Cyanothece sp. CCY0110]


BAC91630
35214261
gll3689 [Gloeobacter violaceus PCC 7421]


EAT90277
111069157
hypothetical protein SNOG_02065 [Phaeosphaeria nodorum SN15]


CAB79998
7270228
putative protein [Arabidopsis thaliana]


CAL49287
117557505
putative carotene-dioxygenase [Rhizopus oryzae]


XP_659308
67522495
hypothetical protein AN1704.2 [Aspergillus nidulans FGSC A4]


XP_001 . . . 
125824373
PREDICTED: similar to retinal pigment epithelium 65b [Danio rerio]


XP_001 . . . 
119185939
hypothetical protein CIMG_03017 [Coccidioides immitis RS]


2BIWB
66361521
Chain B, Crystal Structure Of Apocarotenoid Cleavage Oxygenase




From Synechocystis, Native Enzyme


ABA20860
75701184
Retinal pigment epithelial membrane protein [Anabaena variabilis




ATCC 29413]


XP_001 . . . 
116207620
hypothetical protein CHGG_03103 [Chaetomium globosum CBS 148.51]


XP_001 . . . 
145257182
hypothetical protein An04g02710 [Aspergillus niger]


BAB75983
17133419
lignostilbene-alpha, beta-dioxygenase [Nostoc sp. PCC 7120]


XP_501958
50548975
hypothetical protein [Yarrowia lipolytica]


XP_001 . . . 
109129782
PREDICTED: similar to beta,beta-carotene 15,15-monooxygenase




(beta-carotene dioxygenase 1), partial [Macaca mulatta]


ZP_016 . . . 
119484919
Retinal pigment epithelial membrane protein [Lyngbya sp. PCC 8106]


ZP_017 . . . 
126656882
Retinal pigment epithelial membrane protein [Cyanothece sp. CCY0110]


XP_001 . . . 
109149035
PREDICTED: similar to beta,beta-carotene 15,15-monooxygenase




(beta-carotene dioxygenase 1), partial [Macaca mulatta]


CAL49288
117557507
putative carotene-dioxygenase [Rhizopus oryzae]


ZP_001 . . . 
23130610
COG3670: Lignostilbene-alpha, beta-dioxygenase and related enzymes




[Nostoc punctiforme PCC 73102]


XP_362433
39945792
hypothetical protein MGG_08016 [Magnaporthe grisea 70-15]


XP_001 . . . 
115951205
PREDICTED: hypothetical protein [Strongylocentrotus purpuratus]


AAC12875
3033545
lignostilbene-alpha, beta-dioxygenase [Synechococcus sp. PCC 7942]


XP_001 . . . 
154282379
conserved hypothetical protein [Ajellomyces capsulatus NAm1]


ABG52331
110167791
Carotenoid oxygenase[Trichodesmium erythraeum IM S101]


ABC99263
86554305
putative lignostilbene-alpha, beta-dioxygenase [Synechococcus sp. 




JA-3-3Ab]


NP_931511
37528166
hypothetical protein plu 4336 [Photorhabdus luminescens subsp.




laumondii TTO1]


EDD33453
143171893
hypothetical protein GOS_1320815 [marine metagenome]


XP_001 . . . 
115387251
predicted protein [Aspergillus terreus NIH2624]


YP_885943
118467371
lignostilbene-alpha, beta-dioxygenase [Mycobacterium smegmatis str.




MC2 155]
















TABLE 68







Examples of beta-carotene retinol dehydrogenase polypeptides.









ACCESSION
GI
PROTEIN DESCRIPTION












AAX33670
60678607
epithelial retinol dehydrogenase [Mus musculus]


BAC34110
26340896 
unnamed protein product [Mus musculus]


XP_001 . . . 
149730699
PREDICTED: similar to short-chain dehydrogenase/reductase




RETSDR8 [Equus caballus]


XP_545513 
74004823
PREDICTED: similar to NADP-dependent retinol




dehydrogenase/reductase [Canis familiaris]


Q8HYR6
75064969
Dehydrogenase/reductase SDR family member 9 precursor 




(3-alpha hydroxysteroid dehydrogenase) (3 alpha-HSD)




(Short-chain dehydrogenase/reductase retSDR8)


XP_001 . . . 
114581559
PREDICTED: NADP-dependent retinol dehydrogenase/reductase




isoform 3 [Pan troglodytes]


XP_001 . . . 
109099963
PREDICTED: similar to NADP-dependent retinol




dehydrogenase/reductase isoform 3 [Macaca mulatta]


AAL37037
17224600 
short-chain dehydrogenase/reductase RETSDR8 [Homo sapiens]


AAD32458
4894382
retinol dehydrogenase homolog [Homo sapiens]


XP_001 . . . 
126326289
PREDICTED: similar to short-chain dehydrogenase/reductase




RETSDR8 [Monodelphis domestica]


XP_001 . . . 
149639643
PREDICTED: similar to short-chain dehydrogenase/reductase




RETSDR8 [Ornithorhynchus anatinus]


XP_001 . . . 
114581568
PREDICTED: NADP-dependent retinol dehydrogenase/reductase




isoform 1 [Pan troglodytes]


AAF82748
9082139
retinol dehydrogenase homolog isoform-1 [Homo sapiens]


XP_001 . . . 
109099969
PREDICTED: similar to NADP-dependent retinol




dehydrogenase/reductase isoform 1 [Macaca mulatta]


AAY24306
62988919
unknown [Homo sapiens]


XP_422015 
118093666
PREDICTED: similar to short-chain dehydrogenase/reductase




RETSDR8 [Gallus gallus]


XP_001 . . . 
114581566
PREDICTED: NADP-dependent retinol dehydrogenase/reductase




isoform 2 [Pan troglodytes]


NP_001 . . . 
147905288
NADP-dependent retinol dehydrogenase/reductase 




[Xenopus laevis]


AAH67304
45501367
Dehydrogenase/reductase (SDR family) member 9 




[Xenopus tropicalis]


EDM16447
149066574
rCG60176, isoform CRA_a [Rattus norvegicus]


AAH62000
38303814
Rdh2 protein [Rattus norvegicus]


AAC52316
1072046
retinol dehydrogenase type II


NP_001 . . . 
148227174
hypothetical protein LOC398882 [Xenopus laevis]


NP_033066 
6677697
retinol dehydrogenase 16 [Mus musculus]


NP_001 . . . 
147900576
hypothetical protein LOC432178 [Xenopus laevis]


NP_694773
23680945 
retinol dehydrogenase 9 [Mus musculus]


NP_003716
19743808 
hydroxysteroid (17-beta) dehydrogenase 6 [Homo sapiens]


BAE21017
74205129
unnamed protein product [Mus musculus]


EDL24523
148692576
mCG140848 [Mus musculus]


AAL14860
22651436
cis-retinol/3 alpha hydroxysterol short-chain dehydrogenase-like 




protein [Mus musculus]


P55006
1710631
Retinol dehydrogenase 7 (Retinol dehydrogenase type III) 




(RODH III)


AAH82896
52354822 
LOC494781 protein [Xenopus laevis]


XP_001 . . . 
109097334
PREDICTED: similar to 3-hydroxysteroid epimerase 




[Macaca mulatta]


AAI35515
134023801
LOC100124842 protein [Xenopus tropicalis]


P50169
1710629
Retinol dehydrogenase 3 (Retinol dehydrogenase type I) (RODH I)


BAC98304
37360649
cis-retinol/androgen dehydrogenase type 3 [Mus musculus]


NP_663399 
21703846 
cis-retinol/3 alpha hydroxysterol short-chain dehydrogenase-like 




[Mus musculus]


AAB07997
841197
retinol dehydrogenase type I


XP_001 . . . 
126343946
PREDICTED: similar to microsomal NAD+-dependent retinol




dehydrogenase 4 [Monodelphis domestica]


NP_775427 
27545384
hydroxysteroid (17-beta) dehydrogenase 6 [Rattus norvegicus]


EDL24527
148692580
mCG134493 [Mus musculus]


XP_531641 
73968454 
PREDICTED: similar to microsomal NAD+-dependent retinol




dehydrogenase 4 isoform 1 [Canis familiaris]


AAH24603
19354049 
Retinol dehydrogenase 7 [Mus musculus]


AAL02134
22074192
retinol dehydrogenase similar protein 2 [Mus musculus]


NP_536684 
20147789 
retinol dehydrogenase 1 (all trans) [Mus musculus]


AAH88104
56789874 
Hydroxysteroid (17-beta) dehydrogenase 6 [Rattus norvegicus]


EDL24532
148692585
hydroxysteroid (17-beta) dehydrogenase 9, isoform CRA_a 




[Mus musculus]


ABG81445
110665598
microsomal NAD+-dependent retinol dehydrogenase 4 




[Bos taurus]


EDL24533
148692586
hydroxysteroid (17-beta) dehydrogenase 9, isoform CRA_b 




[Mus musculus]


XP_538239 
73968448
PREDICTED: similar to 3-hydroxysteroid epimerase isoform 3 




[Canis familiaris]


CAJ81333
89272084
novel retinol dehydrogenase protein [Xenopus tropicalis]


AAH46694
28302191 
Rodh-A-prov protein [Xenopus laevis]


XP_001 . . . 
149715148
PREDICTED: similar to microsomal NAD+-dependent retinol




dehydrogenase 4 [Equus caballus]


XP_001 . . . 
109097338
PREDICTED: similar to microsomal NAD+-dependent retinol




dehydrogenase 4 isoform 2 [Macaca mulatta]


XP_001 . . . 
109097336
PREDICTED: similar to microsomal NAD+-dependent retinol




dehydrogenase 4 isoform 3 [Macaca mulatta]


XP_858182 
73968456 
PREDICTED: similar to microsomal NAD+-dependent retinol




dehydrogenase 4 isoform 2 [Canis familiaris]


AAI02627
74354657 
Similar to 3-hydroxysteroid epimerase [Bos taurus]


XP_858059
73968446 
PREDICTED: similar to 3-hydroxysteroid epimerase isoform 4 




[Canis familiaris]


AAC39922
3372592
sterol/retinol dehydrogenase [Homo sapiens]


AAY44823
66354281
retinol dehydrogenase 5 [Danio rerio]


XP_522604
55639443 
PREDICTED: retinol dehydrogenase 16 [Pan troglodytes]


AAH97151
66911361 
Retinol dehydrogenase 5 (11-cis/9-cis) [Danio rerio]


CAK05049
94732559 
novel protein similar to vertebrate retinol dehydrogenase family 




[Danio rerio]


NP_990044
45382649 
11-cis retinol dehydrogenase [Gallus gallus]


EAW96968
119617374
retinol dehydrogenase 16 (all-trans and 13-cis) [Homo sapiens]


NP_001 . . . 
148233310
hypothetical protein LOC398939 [Xenopus laevis]


CAG04959
47218630
unnamed protein product [Tetraodon nigroviridis]


AAH88014
56789076 
Hypothetical LOC496749 [Xenopus tropicalis]


AAI23192
114107846
Rdh9 protein [Xenopus laevis]


AAC72923
3859946
retinol dehydrogenase [Homo sapiens]


AAF82747
9082137
retinol dehydrogenase homolog isoform-2 [Homo sapiens]


AAH75455
49522586
MGC89248 protein [Xenopus tropicalis]


AAH59614
37590384
Retinol dehydrogenase 1, like [Danio rerio]


AAB88252
2661211
oxidative 3 alpha hydroxysteroid dehydrogenase [Homo sapiens]


EDL24633
148692686
retinol dehydrogenase 5, isoform CRA_b [Mus musculus]


BAE22435
74149341 
unnamed protein product [Mus musculus]


XP_538220 
73968269
PREDICTED: similar to 11-cis retinol dehydrogenase 




(11-cis RDH) [Canis familiaris]


NP_001 . . . 
147899633
MGC84134 protein [Xenopus laevis]


XP_001 . . . 
109097121
PREDICTED: retinol dehydrogenase 5 (11-cis and 9-cis) [Macaca




mulatta]


NP_001 . . . 
147905378
MGC84099 protein [Xenopus laevis]


CAF92451
47210426
unnamed protein product [Tetraodon nigroviridis]


XP_522429
55638373
PREDICTED: similar to 11-cis retinol dehydrogenase isoform 2 




[Pan troglodytes]


AAH88529
56788840 
Hypothetical LOC496830 [Xenopus tropicalis]


NP_002896
50726952
retinol dehydrogenase 5 (11-cis and 9-cis) [Homo sapiens]


CAA57715
663171
11-cis retinol dehydrogenase [Bos taurus]


AAH28298
20271410
Retinol dehydrogenase 5 (11-cis/9-cis) [Homo sapiens]


NP_001 . . . 
148230094
hypothetical protein LOC399015 [Xenopus laevis]


AAA80694
1054531
11-cis-retinol dehydrogenase


NP_932335
37620196 
retinol dehydrogenase 1 [Danio rerio]


XP_538240
73968424
PREDICTED: similar to orphan short-chain dehydrogenase/




reductase [Canis familiaris]


AAI34659
134024746
MGC151815 protein [Bos taurus]


AAH64820
40673988 
Orphan short chain dehydrogenase/reductase [Mus musculus]


EDL24531
148692584
orphan short chain dehydrogenase/reductase [Mus musculus]


AAB93668
1916935
9-cis-retinol specific dehydrogenase [Homo sapiens]


XP_001 . . . 
149715290
PREDICTED: hypothetical protein [Equus caballus]


XP_001 . . . 
109482100
PREDICTED: similar to retinol dehydrogenase similar protein 




[Rattus norvegicus]


EAW96967
119617373
orphan short-chain dehydrogenase/reductase [Homo sapiens]


XP_522439
114644207
PREDICTED: orphan short-chain dehydrogenase/reductase 




[Pan troglodytes]


EDL24528
148692581
mCG134494, isoform CRA_a [Mus musculus]


ABQ09278
146186452
retinol dehydrogenase 1 [Oryzias latipes]


ABQ09279
146186454
retinol dehydrogenase 5 [Oryzias latipes]


XP_001 . . . 
109097340
PREDICTED: similar to microsomal NAD+-dependent retinol




dehydrogenase 4 isoform 1 [Macaca mulatta]


EDM16444
149066571
orphan short chain dehydrogenase/reductase [Rattus norvegicus]


AAG44849
12006418 
microsomal retinol dehydrogenase [Branchiostoma lanceolatum]


BAE88760
90078160 
unnamed protein product [Macaca fascicularis]


AAG44847
12006414 
microsomal retinol dehydrogenase 1 [Branchiostoma floridae]


XP_782726
115665382
PREDICTED: similar to retinol dehydrogenase type 1, partial




[Strongylocentrotus purpuratus]


XP_001 . . . 
115939186
PREDICTED: similar to retinol dehydrogenase type 1




[Strongylocentrotus purpuratus]


XP_001 . . . 
118093664
PREDICTED: similar to MGC83505 protein [Gallus gallus]


XP_781379
115654644
PREDICTED: similar to retinol dehydrogenase type 1, partial




[Strongylocentrotus purpuratus]


XP_001 . . . 
115958895
PREDICTED: similar to retinol dehydrogenase type 1




[Strongylocentrotus purpuratus]


AAG44848
12006416 
microsomal retinol dehydrogenase 2 [Branchiostoma floridae]


XP_001 . . . 
115960451
PREDICTED: similar to retinol dehydrogenase type III




[Strongylocentrotus purpuratus]


EDL84786
149029615
rCG42422, isoform CRA_a [Rattus norvegicus]


AAL14861
22651438
cis-retinol/3 alpha hydroxysterol short-chain dehydrogenase-like 




protein isoform [Mus musculus]


XP_001 . . . 
156386264
predicted protein [Nematostella vectensis]


XP_001 . . . 
156389613
predicted protein [Nematostella vectensis]


XP_001 . . . 
156368581
predicted protein [Nematostella vectensis]


XP_001 . . . 
156362183
predicted protein [Nematostella vectensis]


BAC28142
26328807 
unnamed protein product [Mus musculus]


XP_001 . . . 
156367012
predicted protein [Nematostella vectensis]


XP_001 . . . 
156367010
predicted protein [Nematostella vectensis]


CAG14527
47203967 
unnamed protein product [Tetraodon nigroviridis]


XP_001 . . . 
156367016
predicted protein [Nematostella vectensis]


XP_001 . . . 
156401057
predicted protein [Nematostella vectensis]


AAB69884
2384782
Dehydrogenases, short chain protein 16 [Caenorhabditis elegans]


XP_001 . . . 
156367014
predicted protein [Nematostella vectensis]


XP_001 . . . 
156367008
predicted protein [Nematostella vectensis]


NP_871815 
32563809
DeHydrogenases, Short chain family member (dhs-2) 




[Caenorhabditis elegans]


NP_491575 
17507613
DeHydrogenases, Short chain family member (dhs-2) 




[Caenorhabditis elegans]


NP_505941 
115534660
DeHydrogenases, Short chain family member (dhs-20) 




[Caenorhabditis elegans]


CAE74886
39583813 
Hypothetical protein CBG22749 [Caenorhabditis briggsae]


XP_001 . . . 
156408325
predicted protein [Nematostella vectensis]


XP_001 . . . 
126343453
PREDICTED: similar to 3-hydroxybutyrate dehydrogenase, type 1




[Monodelphis domestica]


CAE64533
39593064 
Hypothetical protein CBG09275 [Caenorhabditis briggsae]


XP_001 . . . 
149571441
PREDICTED: similar to retinol dehydrogenase similar protein, 




partial [Ornithorhynchus anatinus]


NP_955017
49227085
truncated cis-retinol/3 alpha-hydroxysterol short-chain 




dehydrogenase [Mus musculus]


XP_001 . . . 
156363786
predicted protein [Nematostella vectensis]


XP_001 . . . 
109097342
PREDICTED: similar to microsomal NAD+-dependent retinol




dehydrogenase 4 [Macaca mulatta]


NP_001 . . . 
147899736
hypothetical protein LOC100037356 [Danio rerio]


XP_001 . . . 
156366980
predicted protein [Nematostella vectensis]


XP_001 . . . 
125853068
PREDICTED: hypothetical protein [Danio rerio]


AAH11964
15080429 
3-hydroxybutyrate dehydrogenase, type 1 [Homo sapiens]


XP_345771
109480152
PREDICTED: similar to retinol dehydrogenase 5 




[Rattus norvegicus]


XP_001 . . . 
149731507
PREDICTED: similar to 3-hydroxybutyrate dehydrogenase, type 1




[Equus caballus]


NP_976059
44680136 
3-hydroxybutyrate dehydrogenase precursor [Homo sapiens]


XP_001 . . . 
149633623
PREDICTED: similar to 3-hydroxybutyrate dehydrogenase, type 1




[Ornithorhynchus anatinus]


AAH89597
58476255 
BC089597 protein [Mus musculus]


XP_001 . . . 
114591350
PREDICTED: 3-hydroxybutyrate dehydrogenase isoform 1 




[Pan troglodytes]


XP_516981 
114591348
PREDICTED: 3-hydroxybutyrate dehydrogenase isoform 2




[Pan troglodytes]


XP_001 . . . 
156405501
predicted protein [Nematostella vectensis]


CAG04267
47223406 
unnamed protein product [Tetraodon nigroviridis]


XP_545160 
74002972
PREDICTED: similar to 3-hydroxybutyrate dehydrogenase 




precursor [Canis familiaris]


AAI03052
73587365 
3-hydroxybutyrate dehydrogenase, type 1 [Bos taurus]


BAF35260
116267595
11 beta-hydroxysteroid dehydrogenase short form 




[Anguilla japonica]


AAH65613
41350974 
Hydroxysteroid 11-beta dehydrogenase 2 [Danio rerio]


AAB59684
203921
D-beta-hydroxybutyrate dehydrogenase


BAE27076
74226863
unnamed protein product [Mus musculus]


NP_446447 
55742813
3-hydroxybutyrate dehydrogenase, type 1 [Rattus norvegicus]


P29147
68837285
D-beta-hydroxybutyrate dehydrogenase, mitochondrial precursor




(BDH) (3-hydroxybutyrate dehydrogenase)


EDK97750
148665334
3-hydroxybutyrate dehydrogenase, type 1 [Mus musculus]


CAE75331
39592111 
Hypothetical protein CBG23309 [Caenorhabditis briggsae]


BAE23523
74206030
unnamed protein product [Mus musculus]


BAC36453
26345604 
unnamed protein product [Mus musculus]


ABH02937
110931880
17-beta hydroxysteroid dehydrogenase 2 [Bos taurus]


NP_509415 
17568189 
F55E10.6 [Caenorhabditis elegans]


XP_546810 
73957269
PREDICTED: similar to hydroxysteroid (17-beta) 




dehydrogenase 2 [Canis familiaris]


XP_001 . . . 
115925077
PREDICTED: similar to retinol dehydrogenase type 1




[Strongylocentrotus purpuratus]


AAA58352
177198
(R)-3-hydroxybutyrate dehydrogenase


XP_422703 
50752249
PREDICTED: hypothetical protein [Gallus gallus]


XP_001 . . . 
149640222
PREDICTED: similar to 17-beta hydroxysteroid dehydrogenase 2




[Ornithorhynchus anatinus]


XP_511130
114663836
PREDICTED: hydroxysteroid (17-beta) dehydrogenase 2 [Pan




troglodytes]


P37059
544152
Estradiol 17-beta-dehydrogenase 2 (17-beta-HSD 2) (Microsomal 




17-beta-hydroxysteroid dehydrogenase) (20 alpha-hydroxysteroid




dehydrogenase) (20-alpha-HSD) (E2DH)


AAV38556
54696368 
hydroxysteroid (17-beta) dehydrogenase 2 [synthetic construct]


AAH90448
60649586 
Hsd17b2 protein [Danio rerio]


XP_001 . . . 
118087716
PREDICTED: hypothetical protein [Gallus gallus]


NP_001 . . . 
93277072
hydroxysteroid (17-beta) dehydrogenase 2[Danio rerio]


P51658
2507561
Estradiol 17-beta-dehydrogenase 2 (17-beta-HSD 2) (17-beta-




hydroxysteroid dehydrogenase 2)


BAC76709
30844232
11-beta-hydroxysteroid dehydrogenase [Oncorhynchus mykiss]


AAY84567
67975199 
17-beta hydroxysteroid dehydrogenase 2 [Macaca fascicularis]


BAD96721
62897563 
hydroxysteroid (17-beta) dehydrogenase 2 variant [Homo sapiens]


XP_414168
118096516
PREDICTED: similar to 17 beta hydroxysteroid dehydrogenase




type 2 [Gallus gallus]


CAE66933
39589698 
Hypothetical protein CBG12325 [Caenorhabditis briggsae]


AAK95857
22074155
retinol dehydrogenase similar protein [Rattus norvegicus]


AAH74144
49257832 
MGC81883 protein [Xenopus laevis]


XP_001 . . . 
125850087
PREDICTED: hypothetical protein [Danio rerio]


AAH90181
58701977 
Zgc:113142 [Danio rerio]


AAA87007
755574
11-beta-hydroxylsteroid dehydrogenase type 2


Q62730
3334165
Estradiol 17-beta-dehydrogenase 2 (17-beta-HSD 2) (17-beta-




hydroxysteroid dehydrogenase 2)


XP_001 . . . 
115956172
PREDICTED: similar to Retinol dehydrogenase 3 (Retinol




dehydrogenase type I) (RODH I) [Strongylocentrotus purpuratus]


CAA64982
1200097
17-beta-hydroxysteroid dehydrogenase type II [Mus musculus]


EDL11587
148679640
hydroxysteroid (17-beta) dehydrogenase 2 [Mus musculus]


EDL92656
149038296
hydroxysteroid (17-beta) dehydrogenase 2 [Rattus norvegicus]


XP_001 . . . 
149626583
PREDICTED: similar to 11 beta-hydroxysteroid dehydrogenase 




type 2 [Ornithorhynchus anatinus]


XP_001 . . . 
109482098
PREDICTED: similar to Retinol dehydrogenase 2 (Retinol




dehydrogenase type II) (RODH II) (29 k-protein) 




[Rattus norvegicus]


XP_001 . . . 
109128927
PREDICTED: similar to Corticosteroid 11-beta-dehydrogenase




isozyme 2 (11-DH2) (11-beta-hydroxysteroid dehydrogenase 




type 2) (11-beta-HSD2) (NAD-dependent 11-beta-hydroxysteroid




dehydrogenase) [Macaca mulatta]
















TABLE 69







Genes Comprising the SAGA Complex.










S. cerevisiae gene
Y lipolytica gene







SPT3
YALI0E21417g



SPT7
none identified



SPT8
YALI0E23804g



SPT20
YALI0C04070g



ADA2
YALI0F14443g



ADA3
none identified



GCN5
YALI0E02772g



ADA1
none identified



TRA1
YALI0C02057g










EQUIVALENTS
Those skilled in the art will recognize, or be able to ascertain using no more than routine experimentation, many equivalents to the specific embodiments of the invention described herein. The scope of the present invention is not intended to be limited to the above Description, but rather is as set forth in the following claims:

## Claims

1. An engineered Saccharomyces cerevisiae strain that produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, retinyl palmitate and combinations thereof, the strain comprising at least one retinologenic modification selected from the group consisting of increased expression or activity of a beta-carotene 15,15′-monooxygenase polypeptide, increased expression or activity of a retinol dehydrogenase polypeptide, and combinations thereof;
wherein the engineered strain can accumulate lipid to at least about 20% of its dry cell weight; and
wherein as a result of genetic engineering, the engineered strain produces the at least one retinolic compound to a level at least about 1% of its dry cell weight.

2. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the strain does not naturally produce the at least one retinolic compound.

3. The engineered Saccharomyces cerevisiae strain of claim 1, further comprising at least one oleaginic modification.

4. The engineered Saccharomyces cerevisiae strain of claim 3, wherein the at least one oleaginic modification increases or decreases expression or activity of at least one oleaginic polypeptide, selected from the group consisting of acetyl-CoA carboxylase polypeptide, pyruvate decarboxylase polypeptide, isocitrate dehydrogenase polypeptide, ATP-citrate lyase polypeptide, malic enzyme polypeptide, AMP deaminase polypeptide, malate dehydrogenase polypeptide, glucose-6-phosphate dehydrogenase polypeptide, 6-phosphogluconate dehydrogenase polypeptide, fructose 1,6 bisphosphatase polypeptide, NADH kinase polypeptide, transhydrogenase polypeptide, acyl-CoA:diacylglycerol acyltransferase polypeptide, phospholipid:diacylglycerol acyltransferase polypeptide, acyl-CoA:cholesterol acyltransferase polypeptide, triglyceride lipase polypeptide, acyl-coenzyme A oxidase polypeptide and combinations thereof.

5. The engineered Saccharomyces cerevisiae strain of claim 3, wherein the at least one oleaginic modification increases or decreases expression or activity of at least one oleaginic polypeptide selected from the group consisting of a polypeptide in any one of Tables 1 through 6 or 31-47.

6. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the at least one retinologenic modification confers to the engineered strain the ability to produce the at least one retinolic compound to a level at least about 1% of its dry cell weight.

7. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the at least one retinologenic modification confers to the engineered strain the ability to produce at least one retinolic compound which a non-engineered strain does not naturally produce.

8. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the at least one retinologenic modification increases expression or activity of beta-carotene 15,15′-monoxygenase.

9. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the beta-carotene 15,15′-monooxygenase polypeptide is selected from the group consisting of a polypeptide in Table 67.

10. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the at least one retinologenic modification further comprises decreasing the expression or activity of one or more components of the SAGA histone acetyltransferase complex.

11. The engineered Saccharomyces cerevisiae strain of claim 10, wherein the at least one retinologenic modification comprises disruption of the endogenous SPT8 gene.

12. The engineered Saccharomyces cerevisiae strain of claim 10, wherein the one or more components of the SAGA histone acetyltransferase complex are selected from the polypeptides listed in Table 69.

13. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the retinologenic modification further comprises altering the expression or activity of one or more carotenoid biosynthesis polypeptides.

14. The engineered Saccharomyces cerevisiae strain of claim 13, wherein the one or more carotenoid biosynthesis polypeptides are selected from the group consisting of phytoene synthase, phytoene dehydrogenase, lycopene cyclase, carotene ketolase, carotene hydroxylase, astaxanthin synthase, carotenoid epsilon hydroxylase, lycopene cyclase, carotenoid glucosyltransferase, acyl CoA:diacyglycerol acyltransferase, geranylgeranylpyrophosphate synthase, and truncated HMG-CoA reductase.

15. The engineered Saccharomyces cerevisiae strain of claim 13, wherein the one or more carotenoid biosynthesis polypeptides are selected from the sequences provided in Tables 17a-25.

16. A method of producing a retinolic compound, the method comprising steps of:
a. cultivating the fungus of claim 1 under conditions that allow production of the retinolic compound;
b. and isolating the produced retinolic compound.

17. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the at least one retinologenic modification comprises introduction of a gene encoding a heterologous beta-carotene 15,15′-monooxygenase polypeptide, a heterologous retinol dehydrogenase polypeptide, or combinations thereof.

18. The engineered Saccharomyces cerevisiae strain of claim 1, wherein the retinol dehydrogenase polypeptide is selected from the group consisting of a polypeptide in Table 68.

19. An engineered Saccharomyces cerevisiae strain that produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, retinyl palmitate and combinations thereof, the strain comprising at least one genetic modification selected from the group consisting of:
increased expression or activity of a beta-carotene 15,15′-monooxygenase polypeptide;
increased expression or activity of a retinol dehydrogenase polypeptide;
increased expression or activity of phytoene synthase;
increased expression or activity of lycopene cyclase;
increased expression or activity of phytoene dehydrogenase;
increased expression or activity of geranylgeranylpyrophosphate synthase;
increased expression or activity of truncated HMG-CoA reductase; and
combinations thereof;
wherein the engineered strain can accumulate lipid to at least about 20% of its dry cell weight; and
wherein as a result of genetic engineering, the engineered strain produces the at least one retinolic compound to a level at least about 1% of its dry cell weight.

20. The engineered Saccharomyces cerevisiae strain of claim 19, wherein the genetic modification comprises introduction of one or more heterologous genes encoding metabolic enzymes selected from the group consisting of: beta-carotene 15,15′-monooxygenase, phytoene synthase, lycopene cyclase, phytoene dehydrogenase, geranylgeranylpyrophosphate synthase, truncated HMG-CoA reductase, and combinations thereof.