protein_name
stringlengths 6
11
| species
stringclasses 299
values | sequence
stringlengths 5
4.97k
| annotation
stringlengths 5
2.1k
⌀ |
|---|---|---|---|
CYF_PHAVU | Phaseolus vulgaris | MQTRNAFSCIKEGITRSISISVMIYIIIRAPFSNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDMQVKQVLANGKKGTLNVGAVLILPEGFELAPPDRISPEIKEKIGNLSFQNYRPTKKNILVVGPVPGQKYKEITFPILSPDPASKRDIHFLKYPIYVGGNRGRGQIYLDGSKSNNNVYNATAAGIVKKIIRKEKGGYEITIVDTLDEHEVIDIIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFLASIILAQIFLVLKKKQFEKVQLFEMNF | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular locations: Plastid, Chloroplast thylakoid membrane |
CYSK_WHEAT | Triticum aestivum | MGEASSPAIAKDVTELIGNTPLVYLNKVTDGCVGRVAAKLESMEPCSSVKDRIGYSMITDAEEKGFIVPGKSVLIEPTSGNTGIGLAFMAAAKGYRLVLTMPASMSMERRIILKAFGAELILTDPLLGMKGAVQKAEELAAKTPNSYILQQFENAANPKIHYETTGPEIWKGTGGKIDGLVSGIGTGGTITGTGKYLQEQNPNIKLYGVEPTESAILNGGKPGPHKIQGIGAGFIPGVLDVDIIDETIQVSSDESIEMAKSLALKEGLLVGISSGAAAAAAIKVAQRPENAGKLFVVVFPSFGERYLSSVLFHSIKKEAESMVVE | Subcellular locations: Cytoplasm |
CYSZ_CUCMA | Cucurbita maxima | MPTDMELSPSNVARHRLAVLAAHLSAASLEPPVMASSLEAHCVSAQTMVAPPELVKGTLTIVDERTGKRYQVQVSEEGTIKATDLKKITTGPNDKGLKLYDPGYLNTAPVRSSISYIDGDLGILRYRGYPIEELAESSTYVEVAYLLMYGNLPSQSQLADWEFAISQHSAVPQGLVDIIQAMPHDAHPMGVLVSAMSALSVFHPDANPALRGQDLYKSKQVRDKQIARIIGKAPTIAAAAYLRLAGRPPVLPSSNLSYSENFLYMLDSLGNRSYKPNPRLARVLDILFILHAEHEMNCSTSAARHLASSGVDVFTALSGAVGALYGPLHGGANEAVLKMLSEIGTVNNIPEFIEGVKNRKRKMSGFGHRVYKNYDPRAKVIRKLAEEVFSIVGRDPLIEVAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPPEFFTVLFAIPRMAGYLAHWRESLDDPDTKIIRPQQVYTGEWLRHYIPPNERLVPAKADRLGQVSVSNASKRRLSGSGI | Subcellular locations: Glyoxysome |
DAD1_ORYSI | Oryza sativa subsp. indica | MPRATSDAKLLIQSLGKAYAATPTNLKIIDLYVVFAVATALIQVVYMGIVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKDNKEFKDLPPERAFADFVLCNLVLHLVIMNFLG | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular locations: Endoplasmic reticulum membrane |
DAD1_ORYSJ | Oryza sativa subsp. japonica | MPRATSDAKLLIQSLGKAYAATPTNLKIIDLYVVFAVATALIQVVYMGIVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKDNKEFKDLPPERAFADFVLCNLVLHLVIMNFLG | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular locations: Endoplasmic reticulum membrane |
DAD1_PEA | Pisum sativum | MAKTSSTTKDAQDLFHAIWSAYSATPTNLKIIDLYVVFAVFTALLQDVYMALVGPFPFNSFLSGVLSCVGTAVLAVCLRIQVNKENKEFKDLGPERAFADFVLCNLVLHLVIMNFLG | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular locations: Endoplasmic reticulum membrane |
DAD1_SOLLC | Solanum lycopersicum | MAKSSATKDAQALFHSLRSAYAATPTNLKIIDLYVIFAISTALIQVVYMAIVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKENKEFKDLPPERAFADFVLCNLVLHLVIMNFLG | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular locations: Endoplasmic reticulum membrane |
DAD2_HORVU | Hordeum vulgare | MPKAAGDAKLLIQSLNKAYAATPTNLKIIDLYVVFAVATALVQVVYMGIVGSFPFNSFLSGVLSSIGTAVLGVCLRIQVNKDNKEFKDLPPERAFADFVLCNLVLHLVIMNFLG | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular locations: Endoplasmic reticulum membrane |
DCVR_MAIZE | Zea mays | MATILLSSRLPTTGTATPSPTRPAPRFLSFPGTAIRRRGRGPLLASSAVSPPAPASAAQPYRALPASETTVLVTGATGYIGRYVVWELLRRGHRVLAVARSRSGIRGRNSPDDVVADLAPAQVVFSDVTDPAALLADLAPHGPVHAAVCCLASRGGGVQDSWRVDYRATLHTLQAARGLGAAHFVLLSAICVQKPLLEFQRAKLKFEEELAAEAARDPSFTYSVVRPTAFFKSLGGQVDIVKNGQPYVMFGDGKLCACKPISEEDLAAFIADCIYDQDKANKVLPIGGPGKALTPLEQGEMLFRLLGREPKFIKVPIQIMDAVIWVLDGLAKLFPGLEDAAEFGKIGRYYASESMLLLDPETGEYSDEKTPSYGKDTLEQFFQRVIREGMAGQELGEQTIF | Catalyzes the conversion of divinyl chlorophyllide to monovinyl chlorophyllide. Reduces the 8-vinyl group of the tetrapyrrole to an ethyl group using NADPH as the reductant. Can use (3,8-divinyl)-chlorophyllide a (DV-Chlidea) > (3,8-divinyl)-chlorophyll a (DV-Chla) > (3,8-divinyl)-protochlorophyllide a (DV-Pchlidea) > (3,8-divinyl)-magnesium-protoporphyrin IX monomethyl ester (DV-MPE) > (3,8-divinyl)-magnesium-protoporphyrin IX (DV-Mg-Proto) as substrates.
Subcellular locations: Plastid, Chloroplast |
DCVR_ORYSI | Oryza sativa subsp. indica | MAALLLSSHLTAASSSSTTSPTARPAPSFVSFRAANAAPKGARRGWPFLASSVEPPPAASAAQPFRSLAPSETTVLVTGATGYIGRYVVRELLRRGHPVVAVARPRSGLRGRNGPDEVVADLAPARVVFSDVTDAGALRADLSPHGPIHAAVCCLASRGGGVRDSWRVDYRATLHTLQAARGLGAAHFVLLSAVCVQKPLLEFQRAKLRFEGELAAEASRDPSFTYSIVRPTAFFKSLGGQVETVKNGQPYVMFGDGKLCACKPISEEDLAAFIADCISDEGKANKILPIGGPGKALTPLEQGEMLFRLLGREPRFIKVPIQVMDAAIWVLDALAKVFPGVEDAAEFGKIGRYYASESMLVLDPDTGEYSDEMTPSYGSDTLEQFFERVIREGMAGQELGEQTIF | Catalyzes the conversion of divinyl chlorophyllide to monovinyl chlorophyllide. Reduces the 8-vinyl group of the tetrapyrrole to an ethyl group using NADPH as the reductant. Can use (3,8-divinyl)-chlorophyllide a (DV-Chlidea) > (3,8-divinyl)-chlorophyll a (DV-Chla) > (3,8-divinyl)-protochlorophyllide a (DV-Pchlidea) > (3,8-divinyl)-magnesium-protoporphyrin IX monomethyl ester (DV-MPE) > (3,8-divinyl)-magnesium-protoporphyrin IX (DV-Mg-Proto) as substrates.
Subcellular locations: Plastid, Chloroplast |
DCVR_ORYSJ | Oryza sativa subsp. japonica | MAALLLSSHLTAASSSSTTSPTARPAPSFVSFRAANAAPKGARRGWPFLASSVEPPPAASAAQPFRSLAPSETTVLVTGATGYIGRYVVRELLRRGHPVVAVARPRSGLRGRNGPDEVVADLAPARVVFSDVTDAGALRADLSPHGPIHAAVCCLASRGGGVRDSWRVDYRATLHTLQAARGLGAAHFVLLSAVCVQKPLLEFQRAKLRFEGELAAEASRDPSFTYSIVRPTAFFKSLGGQVETVKNGQPYVMFGDGKLCACKPISEEDLAAFIADCISDEGKANKILPIGGPGKALTPLEQGEMLFRLLGREPRFIKVPIQVMDAAIWVLDALAKVFPGVEDAAEFGKIGRYYASESMLVLDPDTGEYSDEMTPSYGSDTLEQFFERVIREGMAGQELGEQTIF | Catalyzes the conversion of divinyl chlorophyllide to monovinyl chlorophyllide. Reduces the 8-vinyl group of the tetrapyrrole to an ethyl group using NADPH as the reductant. Can use (3,8-divinyl)-chlorophyllide a (DV-Chlidea) > (3,8-divinyl)-chlorophyll a (DV-Chla) > (3,8-divinyl)-protochlorophyllide a (DV-Pchlidea) > (3,8-divinyl)-magnesium-protoporphyrin IX monomethyl ester (DV-MPE) > (3,8-divinyl)-magnesium-protoporphyrin IX (DV-Mg-Proto) as substrates.
Subcellular locations: Plastid, Chloroplast |
DEF1_TRIKH | Triticum kiharae | RTCQSQSHKFKGACFSDTNCDSVCRTENFPRGQCNQHHVERKCYCERDC | Has weak antifungal activity against F.graminearum and F.verticillioides below 30 ug/ml, but not against A.consortiale B.cinerea, H.sativum, F.culmorum, C.graminicola and D.maydis. |
DEF1_VICFA | Vicia faba | LLGRCKVKSNRFHGPCLTDTHCSTVCRGEGYKGGDCHGLRRRCMCLC | Fabatins have antibacterial activity against Gram-positive and Gram-negative bacteria. High activity against P.aeruginosa. No activity against S.cerevisiae and C.albicans. |
DEF1_VIGUN | Vigna unguiculata | RVCESQSHGFKGACTGDHNCALVCRNEGFSGGNCRGFRRRCFCTLKC | Inhibits trypsin but not chymotrypsin. |
DEF1_WHEAT | Triticum aestivum | KICRRRSAGFKGPCMSNKNCAQVCQQEGWGGGNCDGPFRRCKCIRQC | Inhibits protein translation in cell-free systems. |
DEF21_SORBI | Sorghum bicolor | RVCRRRSAGFKGLCMSDHNCAQVCLQEGWGGGNCDGVMRQCKCIRQC | null |
DEK1_MAIZE | Zea mays | MEGEGHHGVVLACSICGFLFAVLSPFSFWVLWAVNWRPWRLYSWIYARKWPTYVQGPQLSTLCSLLTLCAWLVVISPIAVLLVWGSVLIALMERNIIGLAVIMAGVALLLSFYSIMLWWRTQWQSSEAVAYLLLLAVCLLCAYDFCAIYVTAGASASELNSPSGFFFGVSVISLAINMLFICKILFNVSGFDVDEYVRRSYKFAYSDCVEVAPVSCSPEPPDPSELYMTKSSRVKHLGLLYISSLLVLVGYSILYGLTSKEARWLGALTSVAVVILDWNLGLCSFRFELLKSRMIVLFVAGTSRAFLVSFGVHYWYLGHCISYAFVASVLLSAAVSSWLSISNPSVARIDALRSTVIKLREGFRRKGQNSSSNSSEGCGSSVKRSSGSVEAGQNGNAMDSMYRSNSQSDGVNWSSIPFDRSNSCQEGRSSDKNIDSARASLAHRSNSCLSAVQDSETAVVSVDRHGDPITSLVCSSSGLESHGCEPSGSATTSGNQQLLDLNLAAIFQDRLNDPRISSMLKKNGGLGDVELANLLQDKGLDPNFSYMLKDKVMDPRILALLQRSSLDADREHQDDVDVTATDSDRLDTTIANQISLSEELRRSGLEKWLNISRLIFHHLAGSPIRAFIVFTVMFIIETATVAIYRPETIKVINATHEQFEFGFSILLLSPVVCSIMAFIWSLRAEEMLMTSKPQKYGFIAWLLSTCVGLFLSFLSKSSVILGLSLTVPLMVACLSFAVPIWIRNGYSFWIPGREFANRENVSQAPGEKERALFVITIAVFTASIIGLGAIVSAKPLDALGYKGWDADKNSSYSPYATSMYLGWALSSTIAVITTGLIPIVAWFATYRFSPSSAICVGLFATVLVSFCGASYWGVVNSREDGVPLKADFLAALLPLLCIPAFFSLFTGLYKWKDDDWKISRGVYLFVGMGMLLLFGAVAAVIVTIRPWTVGVACLVAILFLVFVIGVIHYWTSNNFYLTRTQMLLVCSIAFLLALAAFLMGLFHGKPFVGASIGYFSFIFLLTGRALTVLLSPPIVVYSPRVLPVYVYDAHADSAKNVSYAFLILYGIALATEVWGVIASLIMNPPFVGAGVSATTLVIAFSFAVSRPCLTLKMMEDAVHFLSKDTVVQAMSRSANKTRNAISGTYSAPQRSASSAALLVGDPALTLDRAGNFVLPRADVMKLRDRLRNEEIAAGSFLCGVKDCLLICPQSLSNIDYRRNMCAHARILALEEAIDTEWVYMWDKFGGYLLLLLGLTAKAEQIQDEVRLRLFLDSIGLSDLSAKEIKKWMPEDRRQFELIQESYIREKEMEEEALMQRREEEGKGRERRRALLEREERKWKELEISLLSSIPNTGSRDAAAMAAAVRAVGGDSALEDSFARDRVSSIANHIRKAQLARRAEQTGIPGTICILDDEPRSTGRHCGELDLCLCQSQKVTLSIAVMVQPVSGPVCLFGSEFQKVCWEILVAGSEQGMEAGQVGLRLVTKGERMTTVAKEWNIGASSIADGRWHLVTVTLDADLGEATSFIDGVYDGYQNGLPLPTDNGIWEPGTDIWVGARPPMDLDAFGRSDSEGSDSKMQIMDAFLWGRCLSEDEVTVLHTAMSPAEYGFFDLAPGDAWHGSYSARVDDWESEEAYELYDQGDVEWDGQYSSGRKRPVHDAVAIDLDSFARRPRKPRFETRDEVNQRMLSVERAVRDALIAKGERNFTDQEFPPEDRSLFVDPMNPPLKLQVVSEWMRPSDIAKDISISCQPCLFSGSVNSSDVCQGRLGDCWFLSAVAVLTEMSRISEVIITPEYNDEGIYTVRFCIQGEWVAVVVDDWIPCESPGKPAFATSRKQNELWVSILEKAYAKLHGSYEALEGGLVQDALVDLTGGAGEEIDMRSPQAQLDLASGRLWSQLLHFKQEGFLLGAGSPSGSDAHISSSGIVQGHAYSILQVREVDGHKLIQIRNPWANEVEWNGPWSDSSPEWTERMKHKLMHVPQSKNGVFWMSWQDFQIHFRSIYVCRVYPPEMRYSVHGQWRGYNAGGCQDYDSWHQNPQYRLRVTGRDALYPVHVFITLTQGVGFSRKTNGFRNYQSSHDSSMFYIGMRILKTQGCRAAYNIYMHESAGGTDYVNSREISCELVLDPYPKGYTIVPTTIHPGEEAPFVLSVFSKASIRLEAV | Essential protease involved in epiderm development. Required for aleurone cell development in the endosperm probably by maintaining and restricting the aleurone and embryonic epidermal L1 cell-layer fates as well as meristems organization. Involved in the maintenance of adaxial/abaxial axis information in developing leaves, probably by regulating cell proliferation and expansion. Does not need calcium ions to be active.
Subcellular locations: Endoplasmic reticulum membrane, Cytoplasm, Cell membrane, Endosome membrane
Expressed in most tissues at low levels ranging from 30 to 55 ppm. Present in all endosperm cells at transcript level, but confined to aleurones at protein level. |
DEK1_ORYSJ | Oryza sativa subsp. japonica | MEEEEHRGVVLVCSICGFLFAVLGPLSFWILWAVNWRPWRLYSWIYARKWPAYVQGPQLSTLCSFFTLFAWLVVVSPITVLLVWGGILIALLERNIIGLAVIMVGVALLLSFYSIMLWWRTQWQSSKAVAYLLLLAVGLLCAYEFCAVYVTTGASASELNSPSGFFFGVSAISLAINMLFISKILFNGSGFDVDEYVRRLYKFAYSDCVEVAPVSCSPDPPDPSELYMTKSSRVLHLGLLYLCSLMVLVVYSILYGLTSKEARWLGALTSVAVVILDWNLGLCSFRFELLKSRMIALFVAGTSRVFLICFGVHYWYLGHCISYAFVASVLLAAAVSCWLSISNPSVARIDALRSTVIKLREGFRRKGQTSSSNSSDGCGSSVKRSSGSVEAGPHGNATDSMYRSNSQSDCVNWNNVPFDRSNSCQEGQSSDKNIDSGRASLAHRSNSCLSAVAVQDPETAVVSADRHGDPTASLVVCSSSGLESQGCESSGSATASGNQQLLDLNLAAIFQDRLNDPRITSMLKRNGGLGDVELANLLQDKGLDPNFSYMMKDKVMDPRILALLQRSSLDADREHQDDVDVTGTDSDRLDTTIANQISLSEELRRSGLENWLNLSRLMFHQVAGSPIRAFVVFTLIFIIETVTVAVHRPKPIKVINATHEQFEFGFSILLLSPVVCSIMAFIWSLCAEEMTMTSKPRKYGFIAWLLSTCVGLLLSFLSKSSVILGLSLTVPLMVACLSFAIPIWMRNGYRFWIPGGELDSRENIRQAPGKKERALFAISITVFTASVIGLGAIVSAKPLDALGYKGWDADKKSFYSPYATSMYLGWALSSTIAVLATGVIPIVAWFATYRFSPSSAICVGLFATVLVSFCGVSYWGVVNSRQDGVPLKADFLAALLPLLCIPAVFSLFTGMYKWKDDDWKISRGVYLFVGMGVLLLLGAISAVIVTIRPWTVGVACLLVILFLVFAIGVIHYWTSNNFYLTRTQMLLVCSLAFLLALAAFLMGLFQEKPFVGASIGYFSFLFLLTGRALTVLLSPPIVVYSPRVLPVYVYDAHADSAKNVSYAFLILYGIALATEVWGVIASLILNPPFIGAAISAITLVIAFSFAVSRPCLTLKMLEDAVHFLSKDTVVQAMSRSANKTRNAISGTYSAPQRSASSAALLVGDPAITLDRAGNFVLPRADVMKLRDRLRNEEITAGSFFCGVKNCLMIGSPVDVDYRRNMCAHARILALEEAIDTEWVYMWDKFGGYLLLLLGLTAKAEQIQDEVRLRLFLDSIGLSDLSAKEIKKWMPEDRRHFELIQESYIREKEMEEEVLMQRREEEGKGRERRKALLEREERKWKELEISLLSSIPNAGSRDAAAMAAAVRAVGGDSALEDSFARDRVSSIARHIRKAQLARRAEQTGIPDTVCILDDEPRSTGRHCGEIDLCLCESKKVSFSIAVMVQPVSGPVCLFGTEFQKKVCWEILVAGSEQGMEAGQVGLRLVTKGERMTTVAKEWNIGASSIADGRWHLVTVTIDADLGEATSFIDGVYDGYQNALPLPRNNGIWEPGTDIWVGARPPTDLDAFGRSDSEGSDSKMQIMDAFLWGRCLTEDEVAMLHTAICSAEYGLFDLAAEDAWHGSYSARVDDWESEEANFELYDQEDVEWDGQYSSGRKRHARDSVAIDIDSFARRPRKPRFETREEVNQRMLSVERAVREALIAKGERNFTDQEFPPDDRSLFVDPMNPSLKLQVVSEWMRPSDIAKEVSISSQPCLFSGSVNSSDVCQGRLGDCWFLSAVAVLTEMARISEVIITPEYNEEGIYTVRFCIQGEWVAVVVDDWIPCESPGKPAFATSRKQNELWVSILEKAYAKLHGSYEALEGGLVQDALVDLTGGAGEEIDMRSPQAQIDLASGRLWSQLLHFKQEGFLLGAGSPSGSDAHISSSGIVQGHAYSILQVREVDGHKLVQIRNPWANEVEWNGPWSDSSQEWTERMKHKLKHVPQSKNGVFWMSWQDFQIHFRSIYVCRVYPPEMRYSVHGQWRGYSAGGCQDYDSWHQNPQYRLRVTGRDALYPVHVFITLTQGVGFSRKTNGFRNYQSSHDSSMFYIGMRILKTRGCRAAYNIYMHESVGGTDYVNSREISCELVLEPYPKGYTIVPTTIHPGEEAPFVLSVFTKAPIKLEAV | Essential protease involved in epiderm development. Required for aleurone cell development in the endosperm probably by maintaining and restricting the aleurone and embryonic epidermal L1 cell-layer fates as well as meristems organization. Involved in the maintenance of adaxial/abaxial axis information in developing leaves, probably by regulating cell proliferation and expansion. Does not need calcium ions to be active.
Subcellular locations: Endoplasmic reticulum membrane, Cytoplasm, Cell membrane, Endosome membrane
Ubiquitously expressed with higher levels in embryos, vasculatures, leaf primordia, leaf margins, and shoot apical meristem (SAM). |
DLDH_PEA | Pisum sativum | MAMANLARRKGYSLLSSETLRYSFSLRSRAFASGSDENDVVIIGGGPGGYVAAIKAAQLGFKTTCIEKRGALGGTCLNVGCIPSKALLHSSHMYHEAKHSFANHGVKVSNVEIDLAAMMGQKDKAVSNLTRGIEGLFKKNKVTYVKGYGKFVSPSEISVDTIEGENTVVKGKHIIIATGSDVKSLPGVTIDEKKIVSSTGALALSEIPKKLVVIGAGYIGLEMGSVWGRIGSEVTVVEFASEIVPTMDAEIRKQFQRSLEKQGMKFKLKTKVVGVDTSGDGVKLTVEPSAGGEQTIIEADVVLVSAGRTPFTSGLNLDKIGVETDKLGRILVNERFSTNVSGVYAIGDVIPGPMLAHKAEEDGVACVEYLAGKVGHVDYDKVPGVVYTNPEVASVGKTEEQVKETGVEYRVGKFPFMANSRAKAIDNAEGLVKIIAEKETDKILGVHIMAPNAGELIHEAAIALQYDASSEDIARVCHAHPTMSEAIKEAAMATYDKPIHI | Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. The pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular locations: Mitochondrion matrix |
DMAS1_HORVU | Hordeum vulgare | MGAGDRTVAGMPRIGMGTAVQGPKPDPIRRAVLRAIEIGYRHFDTAAHYETEAPIGEAAAEAVRSGAVASRDDLFITSKLWCSDAHGDRVVPALRHTLRNLQMEYVDLYLVHWPVSMKPGRFKAPFTAEDFVPFDMRAVWEAMEECHRLGLAKAIGVANFSCKKLDTLLSFATIPPTVNQVEVNPVWQQRKLREFCRGKGIQLCAYSPLGAKGTHWGSDAVMDAGVLQDIAASRGKSVAQVCLRWVYEQGDCLIVKSFDEARMRENLDVDGWELTEEERRRIAEIPQRKINLGKRYVSDHGPYKSLEELWDGEI | Catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. Involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. |
DMAS1_MAIZE | Zea mays | MSATGRAPCGLPRIGLGTAVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVASREDLFVTSKVWCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTHWGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQRKINQGRRYVSEHGPYKSFEELWDGEI | Catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. Involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. |
DNM1A_ORYSJ | Oryza sativa subsp. japonica | MAKSPRSVVTTGTKRRRAKVHKEDEPVENENLESEFDVSKKESNGATEPGNEPVASKRPKRAAACSNFKEKSLDLSEKDSIITIKESRVEEKEIEAVNLTRTGPEDGQPCRKIIDFILHDGDGNLQPFEMSEVDDIFITALIMPLDDDLEKDRGKGICCSGFGRIENWAISGYDEGAAVIWVSTETSDYKCVKPASSYRSYFEHFSEKARVCVEVYKKLARSVGGNPQVDLEELIAGVVRSINSNRSFNGTVTKDFVISSGEFIYKQLIGLDHTAGNDDEMLATLPVLVALKDECKSRAGFTHLPAMPSNGTLRIKDGQDKGLTEDEDAKLARLLQEEEEWKMMKQRGKRGTSQKNIYIKICETEIANDYPLPAYYKPYNQEMDEYIFDSDIGMYSDDVPVRILDNWALYNSDSRLISLELIPMKAGAENDIVVFGSGFMREDDGSCCSTAELAQLHSSSSKSGREDPGVPIYLSPIKEWVVEFGGSMICITIRTDVAWYKLRQPTKQYAPWCEPVLKTARLAVSIITLLKEQSRASKLSFAEVIKKVAEFDSRHPAFISSKAPTVERYVVVHGQIILQQFADFPDESVKRCAFITGLLAKMEESRHTKLAIKKKSQQMRGENLNPSAKMGPILRKKLMRATTTMLISKIWGEYYATYFPGDTKEEDQNEPKEIDDDQEENEDNDAEEEVNVQDEKATRTPPSTRSRKSSADTRKEIKWEGQTAGKTVSGEVLYKCVIVQDLSISVGATVTTEDDSGETIMCFVEYMYEKLDGKNMIHGIILQEGSQTVLGNAANDREVFLTNDCLEFEASDIKELVTVNIQSLPWGHKYRKENSEAKRIEKAKAEERKRKGLPVEYICKSLYWPEKGGFFSLPYDKIGNGTGICSSCERKPVGNEFKLLSESSFVFENITYNIHDFLYIRPEFFSQGEGHETYKAGRNVGLKPYAVCHLLSVHGPAGSRKANPESTKVKVRRFYRPDDISSTKAYSSDIREVYYSEDIISVPVVMIEGKCEVRLKDDLPNSDLPAVVEHVFCCEYLYDPANGALKQLPPNVRLVTLTRKVPASKKNKGKQICDIELGGSDKPKDGQSENCLATLDIFAGCGGLSEGLQRSGLSLTKWAIEYEEPAGDAFGENHPEAAVFVENCNVILKAIMDKCGDSDDCISTSEAAERAAKLSEDKIKNLPVPGEVEFINGGPPCQGFSGMNRFNQSPWSKVQCEMILAFLSFAEYFRPRFFLLENVRNFVSFNKGQTFRLTLASLLEMGYQVRFGILEAGAYGVAQSRKRAFIWAAAPGETLPEWPEPMHVFASPELKITLPDGKFYAAVKSTAAGAPFRSITVRDTIGDLPAVENGAGKPTIQYGSGPVSWFQKKIRSDMASLNDHISKEMNELNLIRCKHIPKRPGCDWHDLPDEKVKLSTGQMVDLIPWCLPNTAKRHNQWKGLYGRLDWEGNFPTSVTDPQPMGKVGMCFHPEQDRIITVRECARSQGFPDSYRFAGNIQNKHRQIGNAVPPPLAYALGRKLKQAIDAKR | Probably methylates CpG residues and maintains DNA methylation (, ). May be involved in methylation-dependent gene silencing . May play a minor role in the maintenance of DNA methylation .
Subcellular locations: Nucleus
Expressed in roots and inflorescences . Expressed in roots, panicles, anthers, pistils, endosperm and imbibed embryos . Expressed in tissues containing actively replicating and dividing cells, such as shoot and root meristems . |
DNM1B_ORYSJ | Oryza sativa subsp. japonica | MVKSPCSPVTTGKKRCRAKPQKKDEDTTDKGKLDEGPLDATKEMNGVGKGDSRAACKRPRRAAACSDFKEKSVRLSDKSSVVATNGNKMEEEEMDAVKLTKLGPEVQRPCRKLIDFILHDADGKLQPFEMSEIDDFFITALIMPMDDDLEKDRQKGVRCEGFGRIEDWAISGYDEGTAVVWVSTEVADYECVKPAGNYKSYYDHFYEKAQVCVEVYRKLARSVGGNPNLGLEELLASVVRSINAIKGYSGTLSKDFVISNGEFVYNQLIGLDETANTDDEKFATLPVLLALRDGCKSRVEVSKLQPNISNGSLKINDAECKEVSEDDDEKLARLLQQEEEWKMMKQRGKRGTTSQKNVYIKISEAEIANDYPLPAYYKPSSQEMDEYIFDSEDSFYSDVPVRILNNWALYNADSRLIPLELIPMKAGAENDIVVFGSGFMREDDGSCCSTAESAKLSSSSSSNHQDAGVSIYLSPIKEWVIEFGGSMICITIRTDVAWYKLRQPTKQYAPWCEPVLKTARLSVSIITLLKEQSRASKLSFADVIKKVAEFDKGSPAFVSSNVALVERYIVVHGQIILQQFSDFPDETIRRSAFATGLLMKMEQRRHTKLVMKKKVQVMRGENLNPSATMGPASRRKVMRATTTRLINRIWSDYYTHHFPEDSKDADVNEAKEIDDELEENEDEDAEEEAQIEEENVSKTPPSTRSRKLVSQTCKEIRWEGEAIGKTPSGEALYKCAYVRELRINLGRTVALEDDSGELVMCFVEYMFQKLNGAKMVHGRLLQKGSETVLGNAANERDLFLTNECLEFELEDIKELMSVNLQSLPWGHKYRKENAEADRIERAKAEDRKKKGLPMEYLCKSLYWPEKGAFFSLPHDKLGLGNGFCSSCQQKEPDCDELQILSKNSFIYRNITYNVNDYLYIRPDFFSQEEDRATFKGGRNVGLKPYVVCHLLDVHEPAGSRKIHPASTKISVRRFYRPDDISSAKAYVSDIREVYYSENIVKVPVDMIEGKCEVKKKIDISNSDVPVMVEHEFFCEHFYDPATGALKQLPPNVKLMSVQQKATGALKKNKGKQICESDQVDSDKCTKVSKENRLATLDIFAGCGGLSEGLQQAGVSFTKWAIEYEEPAGEAFTKNHPEAAVFVDNCNVILKAIMDKCGDADDCISTSEAAEQAAKFSQDNIMNLPVPGEVEFINGGPPCQGFSGMNRFNQSPWSKVQCEMILAFLSFAEYFRPRFFLLENVRNFVSFNKGQTFRLTVASLLEMGYQVRFGILEAGTFGVAQSRKRAFIWAAAPGETLPDWPEPMHVFASPELKINLPDGKYYAAAKSTAGGAPFRAITVRDTIGDLPKVENGASKLLLEYGGEPISWFQKKIRGNTIALNDHISKEMNELNLIRCQRIPKRPGCDWHDLPDEKVKLSSGQLVDLIPWCLPNTAKRHNQWKGLYGRLDWEGNFPTSVTDPQPMGKVGMCFHPDQDRIITVRECARSQGFPDNYQFAGNIQSKHRQIGNAVPPPLAFALGRKLKEAVDAKRQ | Major CG methylase that methylates chromatin CpG residues and maintains DNA methylation (, ). Plays a major role in genomic imprinting, regulation of embryogenesis and seed viability (, ). Maintains DNA methylation at the FIE1 gene locus in the embryo .
Subcellular locations: Nucleus
Expressed in roots and inflorescences . Expressed in roots, panicles, anthers, pistils, endosperm and imbibed embryos . Expressed in tissues containing actively replicating and dividing cells, such as shoot and root meristems . |
DPE1_ORYSJ | Oryza sativa subsp. japonica | MATLSLPLPHLTQAIPARARPRPRPLRGIPARLLSCRAAMAVAPDKEEAAAVALDKAVKVAVAAPDRAAVAAVGVGEELPEGYDQMMPAVEEARRRRAGVLLHPTSLRGPHGIGDLGDEAVAFLAWLRDAGCTLWQVLPLVPPGRKSGEDGSPYSGQDANCGNTLLISLEELVKDGLLMENELPDPLDMEYVEFDTVANLKEPLIAKAAERLLLSRGELRTQYDCFKKNPNISGWLEDAALFAAIDRSIDALSWYEWPEPLKNRHLRALEDIYQKQKDFIEIFMAQQFLFQRQWQRIRKYAKKLGISIMGDMPIYVGYHSADVWANRKSFLLDKNGFPTFVSGVPPDAFSETGQLWNSPLYDWKAMEAGGFEWWIKRINRALDLYDEFRIDHFRGLAGFWAVPSESKVALVGSWRAGPRNAFFDALFKAVGRINIIAEDLGVITEDVVDLRKSIEAPGMAVLQFAFGGGSDNPHLPHNHEFDQVVYTGTHDNDTVIGWWQTLPEEEKQTVFKYLPEANRTEISWALITAALSSVARTSMVTMQDILGLDSSARMNTPATQKGNWRWRMPSSVSFDSLSPEAAKLKELLGLYNRL | Chloroplastic alpha-glucanotransferase involved in maltotriose metabolism.
Subcellular locations: Plastid, Chloroplast, Plastid, Amyloplast |
DPE2_ORYSJ | Oryza sativa subsp. japonica | MTNLSGKKSLNTVTLVFKLPYYTQWGQSLLIAGSEPALGSWNVKQGLSLSPVHQGNELIWSGRVSVATGFTCQYNYYVVDDNKNVLRSESGEKRKLVLPEGVQDGDVVEIRDWWQDASEALFLRSAFKNVIFNGSENAKRELKTTSLNKSLEPEDIVVQFIVSCPRLGAGSTVVVTGSNPQLGRWQTQDGLKLNYVGDSIWKANCLLRKSEFPIKYKYCKISEAGVSSLEFGPNREADVDLSSPKPSRYVLLSDGALRESPWRGAGVAVPIFSIRSNEDLGVGEFLDLKLLVDWAVNSGFHLVQLLPINDTSVHGMWWDSYPYSSLSVFALHPLYLRVQALSDAIPGDIKDEISQAKKQLDKKDVDYEASLASKLSIARKIFKLEKDKVLNSSSFKQFLSENEEWLKPYAAFCFLRDFFETSDHSQWGRFSQFSKEKLDKLVSEGTLHHDVICFHYYIQYHLYMQLSEAAAYARKKKVILKGDLPIGVDRNSVDTWVYPTLFRMNTATGAPPDYFDKNGQNWGFPTYNWEEMSKDNYGWWRARLTQMAKYFTAYRIDHILGFFRIWELPDHAATGLVGKFRPSIALSQEELLSEGLWDFDRMSRPYILQETLEEKFGSFWTVIAANFLNEYKKQHYEFKEDCNTEKKIIAKLKNSSEKSLWLEKEDSIRRGLFDLLQNIVLIRDPEDSTKFYPRFNQEDTSSFNDLDEHSKNILRRLYYDYYFARQENLWRQNALKTLPVLLNSSDMLACGEDLGLIPACVHPVMQELGLIGLRIQRMPSEPNLEFGIPSQYSYMTVCAPSCHDCSTLRAWWEEDGGRRSRFYQTVIGSDDEPPSRCTPEVANFIVKQHFDAPSMWAIFPLQDLLALKDKYTTRPAKEETINDPTNPKHYWRFRLHVTLDSLLDDKDIQATIKELVTSSGRSFPGKVDGAEESGEKLAKVQLNGKP | Cytosolic alpha-glucanotransferase essential for the cytosolic metabolism of maltose, an intermediate on the pathway by which starch is converted to sucrose in leaves at night.
Subcellular locations: Cytoplasm, Cytosol |
DPOD1_ORYSJ | Oryza sativa subsp. japonica | MSSGGRGGKRRGAPPPGPSGAAAKRAHPGGTPQPPPPAATAAAPVAEEEDMMDEDVFLDETILAEDEEALLLLDRDEALASRLSRWRRPALPADLASGCSRNVAFQQLEIDYVIGESHKVLLPNSSGPAAILRIFGVTREGHSVCCQVHGFEPYFYISCPMGMGPDDISRFHQTLEGRMKDSNRNSNVPRFVKRIELVQKQTIMHYQPQQSQPFLKIVVALPTMVASCRGILERGITIEGLGSKSFLTYESNILFALRFMIDCNIVGGNWIEVPAGKYMKAARIMSYCQLELDCLYSDLVSHAAEGEHSKMAPFRILSFDIECAGRKGHFPEPTHDPVIQIANLVTLQGEGQPFVRNVMTLKSCSPIVGVDVMSFDTERDVLLAWRDFIREVDPDIIIGYNICKFDLPYLIERAEVLKIVEFPILGRIRNSRVRVRDTTFSSRQYGMRESKDVAVEGRVQFDLLQAMQRDYKLSSYSLNSVSAHFLGEQKEDVHHSIISDLQNGNSETRRRLAVYCLKDAYLPQRLLDKLMYIYNYVEMARVTGVPISFLLSRGQSIKVLSQLLRKAKQKNLVIPNIKGQASGQDTFEGATVLEARAGFYEKPIATLDFASLYPSIMMAYNLCYCTLVPPEDARKLNLPPESVNKTPSGETFVKPDVQKGILPEILEELLAARKRAKADLKEAKDPFERAVLDGRQLALKISANSVYGFTGATVGQLPCLEISSSVTSYGRQMIEHTKKLVEDKFTTLGGYEHNAEVIYGDTDSVMVQFGVSTVEDAMKLGREAADYISGTFIKPIKLEFEKIYFPYLLISKKRYAGLYWTNPEKFDKMDTKGIETVRRDNCLLVKNLVTECLHKILVDRDVPGAVQYVKNTISDLLMNRVDLSLLVITKGLTKTGEDYAVKAAHVELAERMRKRDAATAPTVGDRVPYVIIKAAKGAKAYERSEDPIYVLDNNIPIDPQYYLENQISKPLLRIFEPILKNASRELLHGSHTRAVSISTPSNSGIMKFAKKQLTCLGCKAVISGSNQTLCFHCKGREAELYCKTVGNVSELEMLFGRLWTQCQECQGSLHQDVLCTSRDCPIFYRRRKAQKDMAEARVQLQRWDF | This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction.
Subcellular locations: Nucleus |
DPOD1_SOYBN | Glycine max | MTQEEEFMDEDVFINETLVSEDEESLILRDIEQRQALANRLSKWTRPPLSAGYVAQSRSVLFQQLEIDYVIAESHGELLPNSSGPVAIIRIFGVTKEGHSVCCNVHGFEPYFYICCPPGMGPDDISHFHQTLEGRMREANRNSNVGKFVRRIEMVQRRSIMYYQQSNSQPFLKIVVALPTMVASCRGILDRGIQLDGLGMKSFLTYESNVLFALRFMIDCNIVGGNWIGIPAGKYKKTAKSLSYCQLEFDCLYSELISHAPEGEYSKMAPFRILSFDIECAGRKGHFPEPTHDPVIQIANLVTLQGEDQPFIRNVMTLKSCSPIVGVDVMPFETEREVLLAWRDFIREVDPDIIIGYNICKFDLPYLIERALNLKIAEFPILGRIRNSRVRVKDTTFSSRQYGTRESKEVAVEGRVTFDLLQVMQRDYKLSSYSLNSVSSHFLSEQKEDVHHSIISDLQNGNAETRRRLAVYCLKDAYLPQRLLDKLMFIYNYVEMARVTGVPISFLLSRGQSIKVLSQLLRRARQKNLVIPNAKQAGSEQGTFEGATVLEARAGFYEKPIATLDFASLYPSIMMAYNLCYCTLVIPEDARKLNIPPESVNRTPSGETFVKSNLQKGILPEILEELLTARKRAKADLKEAKDPLEKAVLDGRQLALKISANSVYGFTGATIGQLPCLEISSSVTSYGRQMIEHTKKLVEDKFTTLNGYEHNAEVIYGDTDSVMVQFGVSAVEEAMNLGREAAEHISGTFTKPIKLEFEKVYYPYLLISKKRYAGLFWTKPDNFDKMDTKGIETVRRDNCLLVKNLVNDCLHKILIDRDIPGAVQYVKNAISDLLMNRMDLSLLVITKGLTKTGDDYEVKAAHVELAERMRKRDAATAPNVGDRVPYVIIKAAKGAKAYERSEDPIYVLENNIPIDPHYYLENQISKPILRIFEPILKNASKELLHGSHTRSISISTPSNSGILRFAKKQLPALVVKLYLARVITLSVHIAKEGRLSCTVKQYLKCLSWRCFLGGCGHSVRSAKVHFIRMFSAPVGIVQFSIDEKRHRKIWVKQSCNWTDGTSKFCQEFDLADLFEPMDTNTIWCLPQS | This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction.
Subcellular locations: Nucleus |
DPOD2_ORYSJ | Oryza sativa subsp. japonica | MERKQAEYSNLDERYAIQGEKYQGQQYSHIYFTRLHHMRNLLHALVPSWKPHLPVTTVLGLEEGKDCIIVGTLYKHMKLKPSILDEYSKERSAIPLVKPHNFMHPDDHLILEDESGRVTLAGAIPPAAYVTGVVIALHGKETSAGNFLVEDILEAGIPPQITLPSINEDKYVVFVSGLSIGSEKFNPLQFQLLIDHITGHLGDENEQSIASNIVRVVVAGNSVHISPRFFNGQAVASKDQSRIAEPIKELDIMLTQLVASLPVDMMPGSNDPANFSLPQQPLHRCLFAGAATYNTFSSCSNPHQFELDSVRFIGTSGQNIDDLYKYSDAKDKLEFVERTLRWRHLAPTAPNSLGCYPYTDKDPFLVESCPHVYFVGNQDKYETQLLQGLEKQKVRLICIPRFCDSGVAVMLNLRNLECSTLSFSTSFDA | The function of the small subunit is not yet clear.
Subcellular locations: Nucleus |
DRP90_SOYBN | Glycine max | MSEHSFAFAYTVFFMVSVATMSELSSRRYELTQSEKRVIPTRHSTMKSCPWVVFHTRATLTRSFPCLCSNLNPSTTSCLAIFSEHSYVVVF | Possible role in gene regulation during soybean nodule differentiation. |
DRTS_MAIZE | Zea mays | MAAVLANGDSQGRPQRNYQVVVAGTRDMGIGKDGVLPWKLPGDLKFFKELTLTTSDPVKKNAVIMGRKTWESIPVKSRPLPGRLNVILTRSGSFDFATVENVVICGSMESALELLASTPYCLSIEKVFVIGGGQVLREYLKGPACEAIHLTDIQSSIECDTFIPPVDFSVFQPWYSSFPVIESNIRHSFVSFVRVRKSVAETHESNGKESTEVDTKNDKFETENFSFLPKMVYDRHEEYQYLNLVEDIIRSGAQKNDRTGTGTLSKFGCQMRFNLRKNFPLLTTKRVFWRGVVEELLWFISGSTNAKVLQEKGIHIWDGNASREYLNSVGLAHREEGDLGPIYGFQWRHFGAEYTDMHADYTGKGFDQLMDVIDKIKNDPEDRRIILSAWNPSDLKKMALPPCHMFAQFYVENGELSCQMYQRSADMGLGVPFNIASYSLLTYMIAQVCDLSPGDFVHVIGDAHVYRNHVRALEEQIQKMPKPFPILKINPSKKDIDSFMASDFKLVGYDPHQKIEMKMAV | Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP (By similarity). |
DRTS_ORYSJ | Oryza sativa subsp. japonica | MGIGKDGTLPWKLPGDLKFFKDITVTTSDPSKKNAVVMGRKTWESIPLKFRPLPGRLNVILTRSGSFDFATAENVVICGSLDSALQLLATTPYCLTVEKTFIIGGGEILRQSLNAPACEAIHLTDIESSIECDTFIPPIDLSMFHPWYSSFPVVENGIKHSFISFVRVTKSIAEANDSSGKELTGNDSKKVKFEIENFSFLPKMIFERHEEYQYLNLVQDIIRNGAKKNDRTGTGTVSKFGCQMRFNLRRNFPLLTTKRVFWRGVLEELLWFISGSTNAKVLQEKGIHIWDGNASRQYLDSIGLTQREEGDLGPVYGFQWRHFGAEYTDMHADYVGKGFDQLMDVIDKIKNNPDDRRIILSAWNPTDLKKMALPPCHMFAQFYVENGELSCQMYQRSADMGLGVPFNIASYSLLTCMIAQVCDLSPGDFVHVIGDAHVYRTHVEALEEQMRKQPKPFPILKINPVKKDIDSFVTSDFKLVRYDPHHKIEMKMAV | Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP (By similarity). |
DRTS_SOYBN | Glycine max | MPSDSSVISNGHSNGSVNPLPNLQRTYQVVVAATQDWGIGKDGKLPWRLPTDLKFFKEITMKTSEPGKKNAIVMGRKTWESIPLEYRPLSGRLNVVLTRSGSFDIATAENVVICGSMSSALELLAASPYSLSIEKVFVIGGGQIFREALNVPGCEAIHLTEIQSSIECDTFMPPVDFTIFRPWYSSFPKVENNIRYSFTTYVRVRSSAAESAGQNIDPLLDNNSESMKFEVKDFSFLPKMISERHEEYLYLKLVQDIIAEGTTKGDRTGTGTLSKFGCQMRFNLRGNFPLLTTKKVFWRGVVEELLWFISGSTNAKVLQEKGIHIWDGNASREYLDGVGLTEREEGDLGPVYGFQWRHFGARYTDMHHDYSGQGFDQLLDVINKIKRNPDDRRIILSAWNPVDLKLMALPPCHMFAQFYVAHGELSCQMYQRSADMGLGIPFNIASYALLTCMIAHVCDLIPGDFIHVIGDAHIYRNHVRPLQEQLHNQPKPFPTLKINPKKKDIDSFVAADFKLIGYDPHQKIDMKLSV | Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP (By similarity). |
DWRF8_MAIZE | Zea mays | MKREYQDAGGSGGDMGSSKDKMMAAAAGAGEQEEEDVDELLAALGYKVRSSDMADVAQKLEQLEMAMGMGGVGGAGATADDGFVSHLATDTVHYNPSDLSSWVESMLSELNAPPAPLPPATPAPRLASTSSTVTSGAAAGAGYFDLPPAVDSSSSTYALKPIPSPVAAPSADPSTDSAREPKRMRTGGGSTSSSSSSSSSMDGGRTRSSVVEAAPPATQASAAANGPAVPVVVVDTQEAGIRLVHALLACAEAVQQENFSAAEALVKQIPMLASSQGGAMRKVAAYFGEALARRVYRFRPPPDSSLLDAAFADLLHAHFYESCPYLKFAHFTANQAILEAFAGCRRVHVVDFGIKQGMQWPALLQALALRPGGPPSFRLTGVGPPQPDETDALQQVGWKLAQFAHTIRVDFQYRGLVAATLADLEPFMLQPEGDDTDDEPEVIAVNSVFELHRLLAQPGALEKVLGTVRAVRPRIVTVVEQEANHNSGTFLDRFTESLHYYSTMFDSLEGAGAGSGQSTDASPAAAGGTDQVMSEVYLGRQICNVVACEGAERTERHETLGQWRSRLGGSGFAPVHLGSNAYKQASTLLALFAGGDGYRVEEKDGCLTLGWHTRPLIATSAWRVAAAAAP | Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway.
Subcellular locations: Nucleus |
DXS2_ORYSJ | Oryza sativa subsp. japonica | MALQASSSPSMFRAIPTNTNASCRRKLQVRASAAAAAANGGGDGKVMMRKEAASGAWKIDYSGEKPATPLLDTVNYPVHMKNLSTPELEQLAAELRAEIVHTVSKTGGHLSSSLGVVELAVALHHVFDTPEDKIIWDVGHQAYPHKILTGRRSRMHTIRQTSGLAGFPKRDESAHDAFGAGHSSTSISAALGMAVARDLLGKKNHVISVIGDGAMTAGQAYEAMNNSGYLDSNMIVVLNDNKQVSLPTATLDGPATPVGALSKALTKLQSSTKLRRLREAAKTVTKQIGGQAHEVAAKVDEYARGMVSASGSTLFEELGLYYIGPVDGHSVDDLVAIFNKVKSMPAPGPVLVHIVTEKGKGYPPAEAAADRMHGVVKFDPTTGRQFKSKCSTLSYTQYFAEALIREAEADDKVVGIHAAMGGGTGLNYFHKRFPERCFDVGIAEQHAVTFAAGLAAEGLKPFCAIYSSFLQRGYDQVVHDVDLQRLPVRFAMDRAGLVGADGPTHCGAFDVAYMACLPNMVVMAPADEAELMHMVATAAAIDDRPSCFRFPRGNGIGAVLPPNHKGTPLEVGKGRVLVGGNRVALLGYGTMVQACMKAAEALKEHGIYVTVADARFCKPLDTGLIRELAAEHEVLVTVEEGSIGGFGSHVAHYLSLSGLLDGPLKLRSMFLPDRYIDHGAPVDQLEEAGLTPRHIAATVLSLLGRPLEALQLS | Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). Is a limiting enzyme for plastidic isoprenoid biosynthesis and essential for chloroplast development (By similarity).
Subcellular locations: Plastid, Chloroplast |
EF1A_MAIZE | Zea mays | MGKEKTHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIHFVPISGFEGDNMIERSTNLDWYKGPTLLEALDLINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHEALQEALPGDNVGFNVKNVAVKDLKRGYVASGSKDDPAKEAASFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAELVTKIDRRSGKELEKEPKFLKNGDAGMVKMVPTKPMVVETFSQYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKAAAKKK | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular locations: Cytoplasm |
EIX1_SOLLC | Solanum lycopersicum | MDKWKYARLAQFLFTLSLLFLETSFGLGGNKTLCLDKERDALLEFKRGLTDSFDHLSTWGDEEDKQECCKWKGIECDRRTGHVTVIDLHNKFTCSAGASACFAPRLTGKLSPSLLELEYLNYLDLSVNEFERSEIPRFIGSLKRLEYLNLSASFFSGVIPIQFQNLTSLRTLDLGENNLIVKDLRWLSHLSSLEFLSLSSSNFQVNNWFQEITKVPSLKELDLSGCGLSKLVPSQADLANSSLISLSVLHLCCNEFSSSSEYSWVFNLTTSLTSIDLLYNQLSGQIDDRFGTLMYLEHLDLANNLKIEGGVPSSFGNLTRLRHLDMSNTQTVQWLPELFLRLSGSRKSLEVLGLNENSLFGSIVNATRFSSLKKLYLQKNMLNGSFMESAGQVSTLEYLDLSENQMRGALPDLALFPSLRELHLGSNQFRGRIPQGIGKLSQLRILDVSSNRLEGLPESMGQLSNLESFDASYNVLKGTITESHLSNLSSLVDLDLSFNSLALKTSFNWLPPFQLQVISLPSCNLGPSFPKWLQNQNNYTVLDISLASISDTLPSWFSSFPPDLKILNLSNNQISGRVSDLIENTYGYRVIDLSYNNFSGALPLVPTNVQIFYLHKNQFFGSISSICRSRTSPTSLDLSHNQFSGELPDCWMNMTSLAVLNLAYNNFSGEIPHSLGSLTNLKALYIRQNSLSGMLPSFSQCQGLQILDLGGNKLTGSIPGWIGTDLLNLRILSLRFNRLHGSIPSIICQLQFLQILDLSANGLSGKIPHCFNNFTLLYQDNNSGEPMEFIVQGFYGKFPRRYLYIGDLLVQWKNQESEYKNPLLYLKTIDLSSNELIGGVPKEIADMRGLKSLNLSRNELNGTVIEGIGQMRMLESLDMSRNQLSGVIPQDLANLTFLSVLDLSNNQLSGRIPSSTQLQSFDRSSYSDNAQLCGPPLQECPGYAPPSPLIDHGSNNNPQEHDEEEEFPSLEFYISMVLSFFVAFWGILGCLIVNSSWRNAYFKFLTDTTSWLDMISRVWFARLKKKLRRAR | Involved in plant defense. Confers resistance to the fungal pathogen T.viride through recognition of the EIX elicitor protein.
Subcellular locations: Cell membrane |
EIX2_SOLLC | Solanum lycopersicum | MGKRTNPRHFLVTWSLLLLETAFGLTSREVNKTLCIEKERDALLEFKRGLNDDFGRLSTWGDEEECCNWKGIECDKRTGHVIVLDLHSEVTCPGHACFAPILTGKVSPSLLELEYLNFLDLSVNGFENSEIPRFIGSLKRLEYLNLSSSDFSGEIPAQFQNLTSLRILDLGNNNLIVKDLVWLSHLSSLEFLRLGGNDFQARNWFREITKVPSLKELDLSVCGLSKFVPSPADVANSSLISLSVLHLCCNEFSTSSEYSWLFNFSTSLTSIDLSHNQLSRQIDDRFGSLMYLEHLNLANNFGAEGGVPSSFGNLTRLHYLDMSNTQTYQWLPELFLRLSGSRKSLEVLGLNDNSLFGSIVNVTRFSSLKKLYLQKNMLNGFFMERVGQVSSLEYLDLSDNQMRGPLPDLALFPSLRELHLGSNQFQGRIPQGIGKLSQLRIFDVSSNRLEGLPESMGQLSNLERFDASYNVLKGTITESHFSNLSSLVDLDLSFNLLSLNTRFDWVPPFQLQFIRLPSCNMGPSFPKWLQTQNNYTLLDISLANISDMLPSWFSNLPPELKILNLSNNHISGRVSEFIVSKQDYMIIDLSSNNFSGHLPLVPANIQIFYLHKNHFSGSISSICRNTIGAATSIDLSRNQFSGEVPDCWMNMSNLAVLNLAYNNFSGKVPQSLGSLTNLEALYIRQNSFRGMLPSFSQCQLLQILDIGGNKLTGRIPAWIGTDLLQLRILSLRSNKFDGSIPSLICQLQFLQILDLSENGLSGKIPQCLNNFTILRQENGSGESMDFKVRYDYIPGSYLYIGDLLIQWKNQESEYKNALLYLKIIDLSSNKLVGGIPKEIAEMRGLRSLNLSRNDLNGTVVEGIGQMKLLESLDLSRNQLSGMIPQGLSNLTFLSVLDLSNNHLSGRIPSSTQLQSFDRSSYSGNAQLCGPPLEECPGYAPPIDRGSNTNPQEHDDDDEFSSLEFYVSMVLGFFVTFWGILGCLIVNRSWRNAYFTFLTDMKSWLHMTSRVCFARLKGKLRN | Involved in plant defense. Confers resistance to the fungal pathogen T.viride through recognition of the EIX elicitor protein.
Subcellular locations: Cell membrane |
EJ2_SOLLC | Solanum lycopersicum | MGRGRVELKRIENKINRQVTFAKRRNGLLKKAYELSVLCDAEVALIIFSNRGKLYEFCSTSSMVKTIEKYQRCSYATLEANQSVTDTQNNYHEYLRLKARVELLQRSQRNFLGEDLGTLSSKDLEQLENQLESSLKQIRSRKTQFMLDQLADLQQKEQMLAESNRLLRRKLEESVAGFPLRLCWEDGGDHQLMHQQNRLPNTEGFFQPLGLHSSSPHFGYNPVNTDEVNAAATAHNMNGFIHGWML | MADS-box transcription factor that acts redundantly with J2 to control meristem maturation and inflorescence architecture.
Subcellular locations: Nucleus |
ERD15_SOYBN | Glycine max | MEVISASSLNPNAPMFVPLAYRTVEDFSDQWWNLVHSSPWFRDYWLRECFQDPQFQNDDAFDFDFDLDLQDEDEKERKEGKEVVSLGVLKWRSCGGGWAQAPRYVEKAPKFVKPKVSPRAIHQPR | DNA-binding protein that binds to the NRP-B promoter to activate the NRP-B-mediated cell death response . Functions as an upstream component of stress-induced NRP-B-mediated signaling to connect stress in the endoplasmic reticulum (ER) to an osmotic stress-induced cell death signal . Exhibits transactivation activity in yeast .
Subcellular locations: Nucleus |
ETFQO_ORYSJ | Oryza sativa subsp. japonica | MQRVLRAAAAGIGHASGHRAPRWGAAAAAARWLSGGREAMSYDVVVVGAGPAGLAAAIRLKQLCRDADTDLSVCVLEKGSEVGAHVLSGNVFEPRALDELIPKWRQEDTPIRVPVSSDKFWLLTKNKAWTLPSPFDNKGNYVISLSQMVRWMASKAEELGVEVYPGFAASEILYDENQIVTGVATNDVGIAKDGSKRETFQPGVELRGRMTLLAEGCRGSLSEKIIRNHKLRESGQGQHQTYALGIKEVWEIEEGKHKPGSVIHTVGWPLDSKTYGGSFMYHLDDRQLAIGLVVALNYQNPFMSPYDEFQKFKQHPAVRTILDGGTVLQYGARTLNEGGFQSIPNPVFPGGAIIGCSAGFLNVPKIKGTHTAMKSGMLAAEATFKTLVEGSSMELYWENLKKSWIWEELYRARNYRPAFEYGFIPGIALSALERYVFKGKSPFTLKHGIPDHEATDMASLHSPIQYPKPDGQISFDVPTSLYRSSTNHEHDQPPHLRLRDPTVPERVNLPLYAGPESHYCPARVYEYVTDEKGDQKLHINAQNCLHCKACDIKDPKQNIEWTVPEGGGGPGYTVM | Accepts electrons from ETF and reduces ubiquinone.
Subcellular locations: Mitochondrion inner membrane |
F16P1_ORYSI | Oryza sativa subsp. indica | MAAAATTSSHLLLLSRQQAAASLQCGLSFRRQPGRLAGGSSAPSVRCMAAVDTASAPAATEASKKSSYEITTLTTWLLKQEQAGTIDGEMTIVLASISTACKQIASLVQRAPISNLTGVQGAVNVQGEDQKKLDVVSNEVFSNCLKSSGRTGVIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDECLADIADDQNLDQVEQRCIVSVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVYVFTLDPMYGEFVLTQEKVQIPKAGKIYAFNEGNYALWDDKLKSYMDSLKEPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDQKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIMPTEIHQRVPLYIGSVEEVEKVEKFLA | Catalyzes the irreversible reaction from fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate, to regenerate the primary CO(2) acceptor molecule, ribulose-1,5-bisphosphate (Probable). Involved in the regulation of photosynthetic performance and sucrose synthesis (Ref.2).
Subcellular locations: Plastid, Chloroplast stroma |
F16P1_ORYSJ | Oryza sativa subsp. japonica | MAAAATTSSHLLLLSRQQAAASLQCGLSFRRQPGRLAGGSSAPSVRCMAAVDTASAPAATEASKKSSYEITTLTTWLLKQEQAGTIDGEMTIVLASISTACKQIASLVQRAPISNLTGVQGAVNVQGEDQKKLDVVSNEVFSNCLKSSGRTGVIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDECLADIADDQNLDQVEQRCIVSVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVYVFTLDPMYGEFVLTQEKVQIPKAGKIYAFNEGNYALWDDKLKSYMDSLKEPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDQKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIMPTEIHQRVPLYIGSVEEVEKVEKFLA | Catalyzes the irreversible reaction from fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate, to regenerate the primary CO(2) acceptor molecule, ribulose-1,5-bisphosphate. Involved in the regulation of photosynthetic performance and sucrose synthesis.
Subcellular locations: Plastid, Chloroplast stroma |
F16P1_PEA | Pisum sativum | MAAATASSQLIFSKPYSPSRLCPFQLCVFDAKSVLSSSRRKHVNGSGVRCMAVKEATSETKKRSGYEIITLTSWLLQQEQKGIIDAELTIVLSSISMACKQIASLVQRANISNLTGTQGAVNIQGEDQKKLDVISNEVFSNCLRSSGRTGIIASEEEDVAVAVEESYSGNYIVVFDPLDGSSNLDAAVSTGSIFGIYSPNDECLPDFGDDSDDNTLGTEEQRCIVNVCQPGSNLLAAGYCMYSSSVAFVLTIGKGVFVFTLDPLYGEFVLTQENLQIPKSGEIYSFNEGNYKLWDENLKKYIDDLKEPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRVLDIQPTEIHQRVPLYIGSTEEVEKVEKYLA | Subcellular locations: Plastid, Chloroplast stroma |
F16P1_SOYBN | Glycine max | MAAATASTQLIFSKPCSPSRLCPFQLCVFDTKQVLSSGRRRHVGGSGVRCMAVGEAATTGTKKRSGYELQTLTSWLLKQEQAGVIDAELTIVLSSISMACKQIASLVQRANISNLTGVQGAVNVQGEDQKKLDVVSNEVFSNCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAASTGSNFWIYSPNDECLADIDDDPTLDTTEQRCIVNVCQPGSNLLAAGYCMYSSSIIFVLTLGNGVFVFTLDPMYGEFVLTQENLQIPRAGKIYAFNEGNYQLWDEKLKKYIDDLKDPGQSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPINFIVEQAGGKGTDGLQVLRLQGTEIHQRVPLYIGEEVEKVEKYLA | Subcellular locations: Plastid, Chloroplast |
F16P1_SPIOL | Spinacia oleracea | MASIGPATTTAVKLRSSIFNPQSSTLSPSQQCITFTKSLHSFPTATRHNVASGVRCMAAVGEAATETKARTRSKYEIETLTGWLLKQEMAGVIDAELTIVLSSISLACKQIASLVQRAGISNLTGIQGAVNIQGEDQKKLDVVSNEVFSSCLRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPNDECIVDSDHDDESQLSAEEQRCVVNVCQPGDNLLAAGYCMYSSSVIFVLTIGKGVYAFTLDPMYGEFVLTSEKIQIPKAGKIYSFNEGNYKMWDDKLKKYMDDLKEPGESQKPYSSRYIGSLVGDFHRTLLYGGIYGYPRDAKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQPTEIHQRVPLYIGSVEEVEKLEKYLA | Subcellular locations: Plastid, Chloroplast |
F16P1_WHEAT | Triticum aestivum | MAAATTTTSRPLLLSRQQAAASSLQCRLPRRPGSSLFAGQGQASTPNVRCMAVVDTASAPAPAAARKRSSYDMITLTTWLLKQEQEGVIDNEMTIVLSSISTACKQIASLVQRAPISNLTGVQGATNVQGEDQKKLDVISNEVFSNCLRWSGRTGVIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIYSPSDECHIGDDATLDEVTQMCIVNVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVYVFTLDPMYGEFVLTQEKVQIPKSGKIYSFNEGNYALWDDKLKKYMDSLKEPGTSGKPYSARYIGSLVGDFHRTMLYGGIYGYPSDQKSKNGKLRLLYECAPMSFIAEQAGGKGSDGHQRVLDIMPTAVHQRVPLYVGSVEEVEKVEKFLSSE | Subcellular locations: Plastid, Chloroplast
In photosynthetically active tissues, and in the shoot and root apical meristems. |
F16P2_BETVU | Beta vulgaris | MDHAADATRTDLMTITRFVLNEQSKRPESRGDFTILMSHIVLGCKFVCSAVNKAGLAKLIGLAGETNIQGEEQKKLDVLSNEVFIKALISSGRTCILVSEEDEEATFVEPSLRGKYCVVFDPLDGCSNIDCGVSIGTIFGIYMVKDLNNATLDDVLQPGKNMVAAGYCMYGSSCTLVMSTGSGVNGFTHDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTTKYVEKCKFPKDGSSPKSLRYIGSMVADVHRTLLYGGIFMYPGDKKSPNGKLRVLYEVFPMSFLMEQAGGQAFTGEQRALDLVPKNIHDRSPVFLGSYDDVEDIKALYAAEQKNA | Subcellular locations: Cytoplasm |
FAN1_ORYSJ | Oryza sativa subsp. japonica | MLTGRESLVRLIGRRRRSPLPAALALAVPPSRSLQDDAADAEREAAAGGSSSGGGDAAGAAGWVACPVCGESIRGTDYCVNTHLDICLTRGTKRKLTQSTLLDFSFSRKATDDYALNNLNTSDEAEHMEPTDGNVSSDGAFFSLNNDKVNSKGSANASSPGCLHGSPDISETCDTCLPPNVLLPYTENTANNGVVKKCLSHMPSTDATSSTIGLLSVTDSSNSVVVDTVIVGRRFHENIELQEGASITLLRDPQNAKDPDAIKVLYAGYECEQMLGYLPRELAKVLAPLLDRHYIECEGCVVGVPEQQLDHVPIQLKCQKYTDENETYDDLKHPQFLWENFICAVGNGNLLQPSSTRYQTNFSSMITDVMANHSHLFSDKEKSFLDSFQLLPDDGQRLFVRIYTRKGPWFRMSSISYREISDLGQAAMELKLAGYIDMISCMDDLSNYDLKEVIDVLSVPEMKEILKELQKNNVSCTRRHELLSTLLYLYRNGTCTILPKRILKWTGTCIRTSDVADELLWRVQRLFFLNGDQDLSFFLLVDLGLVRFPVYACTISHRVFQEISDLLQYEEAIQVAQVMDQSLDNSNMEMVTRCIELSENRLSTAPKEENATRAEPPPSFFSRFSASSVYSKILTLGVSVYERDRRYTDAIRVLKRLLSTVASDRKRGYWALRLSVDLEHMNRSNESLSIAEAGVIDPWVRAGSKIALQRRVVRLSKPPRRWKVPSYANAVTTNIKEVNIEGRPLNCETGAKNVFYGYDGELCGVEQLALQYYADEGGGWRGTHSEGGIWMTIFGLLMWDAIFSDVPDVFQTKFQTAPLDLETDEFYRSRKDLIESQLKKIQDGIAEEILISSWELHQGTSCRGVNWDRHSLTDLRAAVVCTGGHRLASLLRHLALDYRSWSSGMPDLLLWRFLDERGGGEAKLVEVKGPRDQLSEQQRAWILVLMDFGFDVEVCKVSPVSKRR | Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions. |
FARS_MAIZE | Zea mays | MDATAFHPSLWGDFFVKYKPPTAPKRGHMTERAELLKEEVRKTLKAAANQITNALDLIITLQRLGLDHHYENEISELLRFVYSSSDYDDKDLYVVSLRFYLLRKHGHCVSSDVFTSFKDEEGNFVVDDTKCLLSLYNAAYVRTHGEKVLDEAITFTRRQLEASLLDPLEPALADEVHLTLQTPLFRRLRILEAINYIPIYGKEAGRNEAILELAKLNFNLAQLIYCEELKEVTLWWKQLNVETNLSFIRDRIVECHFWMTGACCEPQYSLSRVIATKMTALITVLDDMMDTYSTTEEAMLLAEAIYRWEENAAELLPRYMKDFYLYLLKTIDSCGDELGPNRSFRTFYLKEMLKVLVRGSSQEIKWRNENYVPKTISEHLEHSGPTVGAFQVACSSFVGMGDSITKESFEWLLTYPELAKSLMNISRLLNDTASTKREQNAGQHVSTVQCYMLKHGTTMDEACEKIKELTEDSWKDMMELYLTPTEHPKLIAQTIVDFARTADYMYKETDGFTFSHTIKDMIAKLFVDPISLF | Sesquiterpene cyclase catalyzing mainly the production of beta-farnesene and alpha-bergamotene in equal amounts from farnesyl diphosphate ( ). Mediates also the biosynthesis of minor sesquiterpene hydrocarbons including alpha-muurolene, beta-bisabolene, zingiberene, sesquiphellandrene, sesquisabinene A, germacrene D, delta-cadinene, alpha-copaene and (E)-beta-caryophyllene (, ). Involved in indirect defense by producing volatile signals attracting natural enemies of herbivores ( ).
Subcellular locations: Cytoplasm |
FARS_ZEADI | Zea diploperennis | MDATAFHPSLWGDFFVKYKPPTAPKRGHMTQRAELLKEEVRKTLKAAANQIKNALDLIITLQRLGLDHHYENEISELLRFVYSSSDYDDKDLYVVSLRFYLLRKHGHCVSSDVFTSFKDEEGNFVVDDTKCLLSLYNAAYLRTHGEKVLDEAITFTRRQLEALLLDSLEPALADEVHLTLQTPLFRRLRILEAVNYIPIYGKEAGRNEAILELAKLNFNLAQLIYCEELKEITLWWKQLNVETNLSFIRDRIVECHFWMTGACCEPQYSLSRVIATKMTALITVLDDMMDTYSTTEEAMLLAEAIYRWEESAAELLPGYMKDFYLYLLKTIDSCGDELGPNRSFRTFYLKEMLKVFVRGSSQEIKWRNENYVPKTISEHLEHSGPTVGAFQVACSSFVGMGDNITKESFEWLLTYPELVKSLMNIARLLNDTASTKREQNAGHHVSTVQCYMLKHGTTMDEACDKIKELTEDSWKDMMELYLTPTEHPKLIAQTIVDFARTADYMYKETDGFTFSHTIKDMIAKLFVDPISLF | Sesquiterpene cyclase catalyzing the production of sixfold more beta-farnesene than alpha-bergamotene from farnesyl diphosphate. Involved in indirect defense by producing volatile signals attracting natural enemies of herbivores.
Subcellular locations: Cytoplasm |
FARS_ZEAMH | Zea mays subsp. huehuetenangensis | MDATAFHPSLWGDFFVKYKPPTAPKRGHMTERAELLKEEVRKTLKAAANQIKNALDLIITLQRLGLDHHYENEISELLRFVYSSSDYDDKDLYVVSLRFYLLRKHGHCVSSDVFTSFKDEEGNFVVDDTKCLLSLYNAAYFRTHGEKVLDEAIAFTRRQLEASLLDPLEPALADEVHLTLQTPLFRRLRILEAINYIPIYGKEAGRNEAILELAKLNFNLAQLIYCGELKEVTLWWKQLNVETNLSFIRDRIVECHFWMTGACCEPQYSLSRVIATKMTALITVLDDMMDTYSTTEEAMLLAEAIYRWEENAAELLPGYMKDFYLYLLKTIDSCGDELGPNRSFRTFYLKEMLKVLVRGSSQEIKWRNENYVPKTISEHLEHSGPTVGAFQVACSSFVGMGDIITKESFEWLLTYPELVKSLMNIARLLNDTASTKREQNAGQHVSTVQCYMLKHGTTMDEACEKVKELTEDSWKDMMELYLTPTEHPKLIAQTIVDFARTADYMYKETDGFTFSHTIKDMIAKLFVDPISLF | Sesquiterpene cyclase catalyzing the production of beta-farnesene and alpha-bergamotene in equal amounts from farnesyl diphosphate. Involved in indirect defense by producing volatile signals attracting natural enemies of herbivores.
Subcellular locations: Cytoplasm |
FARS_ZEAMM | Zea mays subsp. mexicana | MDATAFHPSLWGDFFVKYKPPTAPKRGHMTERAELLKEEVRKTLKAAANQIKNALDLIITLQRLGLDHHYENEISELLRFVYSSSDYDDKDLYVVSLRFYLLRKHGHCVSSDVFTSFKDEEGNFVVDDTKCLLTLYNAAYLRTHGEKVLDEAITFTRRQLEASLLDPLEPALLADEVSLTLQTPLFRRLRILEAINYIPIYGKEAGRNEAILELAKLNFNLAQLIYCEELKEVTLWWKQLNVETNLSFIRDRIVECHFWMTGACCEPQYSLSRVIATKMTALITVLDDMMDTYSTTEEAMLLAEAIYGWEENAAELLPGYMKDFYLYLLKTIDSCGDELGPNRSFRTFYLKEMLKVLVRGSSQEIKWRNENYVPKTISEHLEHSGPSVGAFQVACSSFVGMGDSITKGSFEWLLTYPELAKSLMNIARLLNDTASTKREQNAGHHVSTVQCYMLMHGTTMDEACEKIKELTEDSWKDMMELYLTPTEHPKLIAQTIVDFARTADYMYKETDGFTFSHTIKDMIAKLFVDPISLF | Sesquiterpene cyclase catalyzing the production of beta-farnesene and alpha-bergamotene in equal amounts from farnesyl diphosphate. Involved in indirect defense by producing volatile signals attracting natural enemies of herbivores.
Subcellular locations: Cytoplasm |
FARS_ZEAPE | Zea perennis | MDATAFHPSLWGDFFVKYEPPTAPKRGHMTQRAELLKEEVRKTLKAAANQIKNALDLIITLQRLGLDHHYENEISELLRFVYSSSDYDDKDLYVVSLRFYLLRKHGHRVSSDVFMSFKDEEGNFVVDDTKCLLSLYNAAYLMTHGEKVLDEAITFTRRQLEALLLDPLEPALADEVYLTLQTPLFRRLRILEAVNYIPIYGKEAGRNEAILELAKLNFNLAQLIYCEELKEVTLWWKQLNVETNLSFIRDRIVECHFWMTGACCEPRYSLSRVIATKMTALITVLDDMMDTYSTTEEAMLLAEAIYRWEENAAELLPGYMKHFYLYLLKTIDSCGGELGPNRSFRTFYLKEMLKVFVRGSSQEIKWRNENYVPKTISEHLEHSGPTVGAFQVACSSFVGMGDNITKESFEWLLTYPELVKSLMNIARLLNDTASTKREQTAGHHVSTVQCYMLKHGTTMDEACEKIKELTEDSWKDMMELYLTPTEHPKLVAQTIVDFARTADYMYKETDGFTFSHTIKDMIAKLFVDPISLF | Sesquiterpene cyclase catalyzing the production of sixfold more beta-farnesene than alpha-bergamotene from farnesyl diphosphate. Involved in indirect defense by producing volatile signals attracting natural enemies of herbivores.
Subcellular locations: Cytoplasm |
FAS1_ORYSJ | Oryza sativa subsp. japonica | MEGGKLLGVAHPEPANNIDADLRYDLGQSRMQVDGPVVLNRSAELEPSDSMAIDDVPVEASSQPAPAKQSPALMDTIVEVQKQLKRKRASSGPALAAADKDALVAGCCQELEGLLEYYREVSGHRMQFEVGNLSTNAAIGCLLEESSLGLSKLVDEIYEKLKGMEGVSATSVRSSVLLIGQRMMYGQSSPDADVLEDESETALWCWEVRDLKVIPLRMRGPLSTRRTARKKIHERITAIYSTLSVLEAPGAEAQVNDMRKASLKLSKALNLEGIKSLVERATQKSNIERGAKNTGSTAKEPMQEMVKSNNDTGIIENVDDSQLQKNTSTNEKDTQKAQKQVEKELKQKEKEEARMRKQQKKQQEEALREQKRREKEEAEMKKQQRKQEEEAQKEQKRREKEEAETRKQQKKQQEEAEKEQKRREKEAVQLKKQLAIQKQASMMERFFKNKKDSEKLEKPGGKDSGVQTTDPCTTNKEVVPLVTSIIDSSFSQKENWALEDLRRLQISGWQKLSSYNRSSRWGIRNKPKKEAFKELKLQKTSDNMLEEILSPNEDTCHNLSQENEPDKSANDVDMLPAVELQFHGTNHANPLPTRSIKRKLLQFDKSNRPAYYGTWRKKSAVVGPRCPLKMDPDLDYEVDSDDEWEEEDPGESLSDCEKDNDEVMEEDSKITDEESEDSFFVPDGYLSDNEGIQIESLLDDKDEASSSPPDQCAEVEEFRALLRQQKVLNTLTEQALRKSQPLVISNLTHEKAELLTAGDLKGTSKIEQLCLQVLSMRICPGGATIDLPVIDSSSANAEETNQLNVKSSPAAASAIPDTDLAEIVKVIGSCRDGINKLVESLHQKFPNVSKSQLKNKVREISEFVDNRWQVKKEVLSKLGLSSSPASSKKPKSIATYFSKRCLPPEEAILASPELRLKSKTTQNVNGDTDIPRINLLPSSQ | Component of the chromatin assembly factor complex (CAF-1) involved in chromatin assembly following DNA replication and DNA repair. Required for several aspects of development, including apical meristem maintenance by regulating the durations of the S- and G2-phases of the cell cycle through its chromatin assembly activity.
Subcellular locations: Nucleus
In embryo, expressed in leaf primordia, coleoptile and radicle. In seedlings, expressed in cell division zone of roots, SAM and leaf primordia. Expressed in floral organ primordia. |
FEA2_MAIZE | Zea mays | MLTATPLPHQLLATFLLVLASATQPAVPASTDRAALLAFRASLSPPSRAALSSWSGPLSPSWLGVSLHPATAPAPSVTTPSVAELSLRGLNLTGVIPAAPLALLRRLRTLDLSANALSGELPCSLPRSLLALDLSRNALSGAVPTCLPSSLPALRTLNLSANFLRLPLSPRLSFPARLAALDLSRNAISGAVPPRIVADPDNSALLLLDLSHNRFSGEIPAGIAAVRSLQGLFLADNQLSGDIPPGIGNLTYLQVLDLSNNRLSGSVPAGLAGCFQLLYLQLGGNQLSGALRPELDALASLKVLDLSNNKISGEIPLPLAGCRSLEVVDLSGNEISGELSSAVAKWLSLKFLSLAGNQLSGHLPDWMFSFPLLQWLDLSSNKFVGFIPDGGFNVSEVLNGGGGQGTPSESVLPPQLFVSASVDTVSWQLDLGYDVQATTGIDLSGNELCGEIPEGLVDMKGLEYLNLSCNYLAGQIPAGLGGMGRLHTLDFSHNGLSGEVPPGIAAMTVLEVLNLSYNSLSGPLPTTKFPGALAGNPGICSGKGCSENARTPEGKMEGSNHRGWLGGWHGENGWVSLGAFCISTMTSFYVSLATLLCSSNARNFVFRPVRVEY | Receptor-like protein that regulates shoot meristem proliferation. Based on additive and synergistic phenotypes of double mutants, it is probable that unlike CLV1 and CLV2 in A.thaliana, FAE2 and TD1 do not function exclusively in a single pathway.
Subcellular locations: Cell membrane
Expressed in ear primordia, vegetative apex and young leaf tissues. Barely detected in expanded leaf tissues and not expressed in roots. |
FER5_MAIZE | Zea mays | MATVLSSPRAPAFSFSLRAAPATTVAMTRGASSRLRAQATYNVKLITPEGEVELQVPDDVYILDYAEEEGIDLPYSCRAGSCSSCAGKVVSGSLDQSDQSFLDDSQVADGWVLTCVAYPTSDVVIETHKEDDLIS | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular locations: Plastid, Chloroplast |
FER6_MAIZE | Zea mays | MSTATAPRLPAPRSGASYHYQTTAAPAANTLSFAGHARQAARASGPRLSSRFVASAAAVLHKVKLVGPDGTEHEFEAPDDTYILEAAETAGVELPFSCRAGSCSTCAGRMSAGEVDQSEGSFLDDGQMAEGYLLTCISYPKADCVIHTHKEEDLY | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular locations: Plastid, Chloroplast |
FER_WHEAT | Triticum aestivum | MAAALSLRAPFSLRAVAPPAPRVALAPAALSLAAAKQVRGARLRAQATYKVKLVTPEGEVELEVPDDVYILDQAEEEGIDLPYSCRAGSCSSCAGKLVSGEIDQSDQSFLDDDQMEAGWVLTCHAYPKSDIVIETHKEEELTA | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular locations: Plastid, Chloroplast |
FLO6_ORYSJ | Oryza sativa subsp. japonica | MLPLLLPLPVTPPPPLPSPTLTLAPASAPRRRLVLLAAAAPHHHHHHRRRRVYRRQRAAPTQTRAPRRTLSASNAARGEEDLEEAIYEFMRRSDKPGAFPTRAELVAAGRADLAAAVDACGGWLSLGWSSGGAEAGRASSSVGVHPDYPPEAGAAAAAGGASDLAQGAVWASSREAEASPSGRQPETEEEETETKFGTGLDGMLTRLQRERERVRPPLPRSSDGAGGERDNVALMGQSGAPSHSATGGRYTPKVPDNGNIHSYHPQNGALEHNKSSKSLTNDAWRTWSLDKGGFSDFQAAEIHSTNSRKSFRHDGLDILAQDDVHGPSNGVAVHDYDINDVDSERDDIHARLQNLELDLTAALHTLRSRFDKVISDMSEGDGAKAPNGLSDDWEFEETKVMQAQEELRSIRAKIAVLEGKMALEIIEKNKIIEEKQRRLDEAEKALSELRTVYIVWSNPASEVLLTGSFDGWTSQRRMERSERGTFSLNLRLYPGRYEIKFIVDGVWRNDPLRPLVSNNGHENNLLTVT | Involved in compound starch granule formation and starch synthesis in endosperm. May act as a regulatory scaffolding protein and affect starch synthesis and compound starch granule formation through direct interaction with isoamylase 1 (ISA1). Binds starch, amylopectin and amylose through its C-terminal carbohydrate-binding domain (CBM) in vitro.
Subcellular locations: Plastid, Chloroplast
Localizes to granule-like structures in chloroplasts.
Expressed in leaves, stems and panicles. Expressed at lower levels in roots and developing seeds. |
FON1_ORYSJ | Oryza sativa subsp. japonica | MPPTLLLLLLLLPPSLASPDRDIYALAKLKAALVPSPSATAPPPLADWDPAATSPAHCTFSGVTCDGRSRVVAINLTALPLHSGYLPPEIALLDSLANLTIAACCLPGHVPLELPTLPSLRHLNLSNNNLSGHFPVPDSGGGASPYFPSLELIDAYNNNLSGLLPPFSASHARLRYLHLGGNYFTGAIPDSYGDLAALEYLGLNGNTLSGHVPVSLSRLTRLREMYIGYYNQYDGGVPPEFGDLGALLRLDMSSCNLTGPVPPELGRLQRLDTLFLQWNRLSGEIPPQLGDLSSLASLDLSVNDLAGEIPPSLANLSNLKLLNLFRNHLRGSIPDFVAGFAQLEVLQLWDNNLTGNIPAGLGKNGRLKTLDLATNHLTGPIPADLCAGRRLEMLVLMENGLFGPIPDSLGDCKTLTRVRLAKNFLTGPVPAGLFNLPQANMVELTDNLLTGELPDVIGGDKIGMLLLGNNGIGGRIPPAIGNLPALQTLSLESNNFSGALPPEIGNLKNLSRLNVSGNALTGAIPDELIRCASLAAVDLSRNGFSGEIPESITSLKILCTLNVSRNRLTGELPPEMSNMTSLTTLDVSYNSLSGPVPMQGQFLVFNESSFVGNPGLCGGPVADACPPSMAGGGGGAGSQLRLRWDSKKMLVALVAAFAAVAVAFLGARKGCSAWRSAARRRSGAWKMTAFQKLEFSAEDVVECVKEDNIIGKGGAGIVYHGVTRGAELAIKRLVGRGGGEHDRGFSAEVTTLGRIRHRNIVRLLGFVSNRETNLLLYEYMPNGSLGEMLHGGKGGHLGWEARARVAAEAACGLCYLHHDCAPRIIHRDVKSNNILLDSAFEAHVADFGLAKFLGGATSECMSAIAGSYGYIAPEYAYTLRVDEKSDVYSFGVVLLELITGRRPVGGFGDGVDIVHWVRKVTAELPDNSDTAAVLAVADRRLTPEPVALMVNLYKVAMACVEEASTARPTMREVVHMLSNPNSAQPNSGDLLVTF | Receptor-like kinase protein that regulates the size of the floral meristem.
Subcellular locations: Membrane
Expressed in shoot apical meristem, and after transition to the reproductive phase, detected in the inflorescence and the floral meristems. Expressed uniformly throughout the meristems. Expressed also in floral organ primordia, such as the palea, lemma, lodicules, stamens, carpels and ovules. |
FON2_ORYSI | Oryza sativa subsp. indica | MGRLFLCLVVAWCWVALLLVAPVHGRVGLPGEFSGDQRPVPATSFDLVTEPKTKQPRGVKGTRRPSWSSWSSTASRSSPPPGRGAPSAAAAAELRSVPAGPDPMHHHGSPRRPEHARSTGRP | Probable extracellular signal that regulates meristem maintenance. May function as a putative ligand for a receptor complex including FON1. Regulates the size of the floral meristem and the number of floral organs (By similarity).
Subcellular locations: Secreted |
FON2_ORYSJ | Oryza sativa subsp. japonica | MGRLFLCLVVAWCWVALLLVAPVHGRVGLPGEFSGDQRPVPATSFDLVTEPKTKQPRGVKGTRRPSWSSWSSTASRSSPPPGRGAPSAAAAAELRSVPAGPDPMHHHGSPRRPEHARSTGRP | Probable extracellular signal that regulates meristem maintenance. May function as a putative ligand for a receptor complex including FON1. Regulates the size of the floral meristem and the number of floral organs.
Subcellular locations: Secreted
Expressed in shoot apical and axillary meristems, but not in other vegetative tissues. Detected in a group of small cells at the apical region of the central zone of the meristems. |
FRI_PHAVU | Phaseolus vulgaris | MALAPSKVSPFSGFSLSDGVGAVRNPTCSVSLSFLNKKVGSRNLGVSASTVPLTGVIFEPFEEVKKEELAVPTAGQVSLARQYYADECESAINEQINVEYNASYVYHSLFAYFDRDNVALKGFARFFKESSEEEREHAEKLMKYQNTRGGRVVLHPIKNVPSEFEHVEKGDALYAMELALSLEKLVNEKLRSVHSVADRNKDPQLADFIESEFLSEQVEAIKKISEYVAQLRMVGKGHGVWHFDQSLLHDGHAA | Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).
Subcellular locations: Plastid, Chloroplast, Plastid |
G3PC_ORYSI | Oryza sativa subsp. indica | MGKIKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGQWKHSDIKIKDSKTLLLGEKPVTVFGIRNPDEIPWAEAGAEYVVESTGVFTDKEKAAAHLKGGAKKVVISAPSKDAPMFVCGVNEDKYTSDIDIVSNASCTTNCLAPLAKVIHDNFGIIEGLMTTVHAITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTVDVSVVDLTVRIEKAASYDAIKSAIKSASEGKLKGIIGYVEEDLVSTDFVGDSRSSIFDAKAGIALNDNFVKLVAWYDNEWGYSNRVIDLIRHMAKTQ | Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism (By similarity).
Subcellular locations: Cytoplasm |
G3PC_PEA | Pisum sativum | MGAKIKIGINGFGRIGRLVARVALKRDDVELVAVNDPFITTDYMTYMFKYDSVHGQWKNDELTVKDSNTLLFGQKPVTVFAHRNPEEIPWASTGADIIVESTGVFTDKDKAAAHLKGGAKKVIISAPSKDAPMFVVGVNENEYKPEFDIISNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKAAIKEESEGKLKGILGYTEDDVVSTDFIGDTRSSIFDAKAGIALNDKFVKLVSWYDNELGYSTRVVDLIVHIAKQL | Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism (By similarity).
Subcellular locations: Cytoplasm |
G6PDC_SOLTU | Solanum tuberosum | MGVQLRLNPCSSSSAATSPSTFHNGTPYFCKKFNFLPFRTQPLNWVSGIYSRIQPRKHFEVFSSNGFPLNAVSVQDVQVPLTELGSGDTTVSITVIGASGDLAKKKILPALFALFYEDCLPENFVVFGYSRTKLSDEELRNMISTTLTCRIDKRENCDAKMEHFLERCFYHSGQYNSEDDFAELDYKLKEKEGCRVSNRLFYLSIPPNIFVDVVRCASLKASSTSGWTRVIVEKPFGRDLESSSELTRSLKKYLTEEQIFRIDHYLGKELVENLSVLRFSNLVFEPLWSRNYIRNVQFIFSEDFGTEGRGGYFDHYGIIRDIMQNHLLQILALFAMETPVSLDAEDIRNEKVKVLRSMRPLQLEDVVLGQYKGHSNGAKSYPAYTDDPTVPNGSITPTFSAAALFIDNARWDGVPFLMKAGKALHTKRAEIRVQFRHVPGNLYKRNFGTDMDKATNELVLRLQPDEAIYLKINNKVPGLGMRLDRSDLNLLYKAKYRGEIPDAYERLLLDAIEGERRLFIRSDELDAAWALFTPLLKELEEKKIAPELYPYGSRGPVGAHYLAAKHNVRWGDLSGDD | Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are involved in membrane synthesis and cell division.
Subcellular locations: Plastid, Chloroplast
Green tissues, leaves and chloroplasts. |
G6PDC_SPIOL | Spinacia oleracea | MEELVSCHHLPLLCLQSSVPPNGCLTFFQDSACQRCSHSEFSNGHPLNDVSLQNDVAVNPIVAKSIDPSADLQLLPLLESVKEEPTLSIIVVGASGDLAKKKIFPALFALFYENCLPENFTVFGFSRTEMNDEELRTMISKTLTCRIDQRENCGEKMDHFLQRCFYHSGQYNSEDDFSGLDCKLKEKEAGRLQNRLFYLSIPPNIFVDVVRCVSHRASSASGWTRVIVEKPFGRDSDSSRELTRSFKQYLSEDQIFRIDHYLGKELVENLSVLRFSNLVFEPLWSRNYIRNVQLIFSEDFGTEGRGGYFDNYGIIRDIMQNHLLQILALFAMETPVSLDAEDIRNEKVKVLRSMKPLKLQDVVVGQYKGHSKGNKSYSGYTDDPTVPNNSVTPTFAAAALFIDNARWDGVPFLMKAGKALHTKRAEIRVQFRHVPGNLYKKTFGTDLDKATNELVLRVQPDEAIYLKINNKVPGLGMRLDRTDLNLCYSTRYRGEIPDAYERLLLDAIEGERRLFIRSDKLDAAWSLFTPLLKELEEKKVAPELYPYGSRGPVGAHYLAAKHNVRWGDLSGEDS | Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are involved in membrane synthesis and cell division.
Subcellular locations: Plastid, Chloroplast |
GATP1_ORYSI | Oryza sativa subsp. indica | MVIARGLLRSNASSSSSQAINLLKYVTSTGSLQGHTQNLCDASTRHFSSVPSPQSNSTEENGFKGHGMLAPFTAGWQSTDVHPLVIERSEGSYVYDIDGKKYLDSLAGLWCTALGGSEPRLAKAATEQLHKLPFYHSFWNRTTKPSLDLAKELLSMFTAREMGKVFFTNSGSEANDSQVKLVWYYNNALGRPDKKKFIARSKSYHGSTLISASLSGLPALHQKFDLPAPFVLHTDCPHYWRFHLPGETEEEFATRLANNLEELILKEGPETIAAFIAEPVMGAGGVIPPPKTYFEKVQAIVKKYDILFIADEVITAFGRLGTMFGSDMYNIKPDLVSMAKALSSAYVPIGAIMVSPEISDVIHSQSNKLGSFAHGFTYSGHPVACAVAIEALKIYQERNIPDHVKQISPRFQEGVKAFAGSPIVGEIRGVGLILGTEFADNKSPNDPFPAEWGVGAIFGAECQKRGMLVRVAGDNIMMSPPLIMTPDEVEELVSIYGDALKATEERVAELKSKKNN | Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate as amino-group acceptor, but not 2-oxoglutarate.
Subcellular locations: Mitochondrion |
GATP1_ORYSJ | Oryza sativa subsp. japonica | MVIARGLLRSNASSSSSQAINLLKYVTSTGSLQGHTQNLCDASTRHFSSVPSPQYNSTEENGFKGHGMLAPFTAGWQSTDVHPLVIERSEGSYVYDIDGKKYLDSLAGLWCTALGGSEPRLVKAATEQLHKLPFYHSFWNRTTKPSLDLAKELLSMFTAREMGKVFFTNSGSEANDSQVKLVWYYNNALGRPDKKKFIARSKSYHGSTLISASLSGLPALHQKFDLPAPFVLHTDCPHYWRFHLPGETEEEFATRLANNLEELILKEGPETIAAFIAEPVMGAGGVIPPPKTYFEKVQAIVKKYDILFIADEVITAFGRLGTMFGSDMYNIKPDLVSMAKALSSAYVPIGAIMVSPEISDVIHSQSNKLGSFAHGFTYSGHPVACAVAIEALKIYQERNIPDHVKQISPRFQEGVKAFAGSPIVGEIRGVGLILGTEFADNKSPNDPFPAEWGVGAIFGAECQKRGMLVRVAGDNIMMSPPLIMTPDEVEELVSIYGDALKATEERVAELKSKKNN | Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate as amino-group acceptor, but not 2-oxoglutarate. Not involved in the interaction with blast fungus.
Subcellular locations: Mitochondrion
Expressed in roots, stems and panicles. |
GATP1_SOLLC | Solanum lycopersicum | MAKISRLFGSTVKAAITAQAGFHGKRIPAVSSLQEHIVKSTPARYNSTQACLENDISGTDNKGFKGHDMLAPFTAGWQSTDVDPLIIEKSEGSHVYDMQGRKYIDTLAGLWCTALGGNEPRLVDAATKQLNTLPFYHSFWNRTTKPSLDLAKELLDMFTAKKMAKAFFTNSGSEANDTQVKLVWYYNNALGRPNKKKFIARAKAYHGSTLISASLTGLPALHQNFDLPAPFVLHTDCPHYWRYHLPGETEEEFSTRLAKNLEDLILKEGPETIAAFIAEPVMGAGGVIPPPATYFDKIQAVVKKYDILFIADEVICAFGRLGTMFGSDMYNIKPDLVTLAKALSSAYMPIGAVLVSPEVSDVIHSQSNKLGSFSHGFTYSGHPVACAVALEAIKIYKERNMVERVNRISPKFQEGLKAFSDSPIIGEIRGLGLILATEFANNKSPNDHFPPEWGVGAYFGAQCQKNGMLVRVAGDTIMMSPPFVVTPEELDELIRIYGKALRETEKRVEELKSQK | Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate or glyoxylate as amino-group acceptor. Cannot use beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors. Acts predominantly in vegetative tissues.
Subcellular locations: Mitochondrion
Expressed in leaves, roots, stems, flowers and fruits. |
GATP2_ORYSI | Oryza sativa subsp. indica | MNLIKHAAFAASFQGETDCTSHASARKFSTSGSSPLLDSTEGNGFKGHSMLAPFTAGWHSTDLEPLIIERSEGSYVYDSKGNKYLDTLAGLWCTALGGSEPRLVKAATDQLNKLPFYHSFWNSTAKPPLDLAEELISMFTAKEMGKVFFTNSGSEANDSQVKLVWYYNNALGRPNKKKIIAQSQAYHGSTLISASLSGLPAMHLKFDLPAPFVLHTDCPHYWRFGLPGEAEEEFATRLADNLENLILKEGPETVAAFIAEPVIGAGGVIPPPKTYFEKIQAVLQKYDVLFIADEVITGFGRLGTMFGSDLYNIKPDLVSLAKALSSAYVPIGATLVSPEISDVVHSQSNKIGFFAHGFTYSGHPVSCAVALEALKIYRERNIPAHVKQISPRFQEGIKAFAGSSIIGETRGVGLLLATEFANNKSPNDPFPVEWGVAQIFGAECKKRGMLVKVVGDEIAMSPPLIMSQREVDGLVSIYGEALKATEERVAELRSKKK | Transaminase that degrades gamma-amino butyric acid (GABA).
Subcellular locations: Mitochondrion |
GATP2_ORYSJ | Oryza sativa subsp. japonica | MNLIKHAAFAASFQGETDCTSHASARKFSTSGSSPLLDSTEGNGFKGHSMLAPFTAGWHSTDLEPLIIERSEGSYVYDSKGNKYLDTLAGLWCTALGGSEPRLVKAATDQLNKLPFYHSFWNSTAKPPLDLAEELISMFTAKEMGKVFFTNSGSEANDSQVKLVWYYNNALGRPNKKKIIAQSQAYHGSTLISASLSGLPAMHLKFDLPAPFVLHTDCPHYWRFGLPGEAEEEFATRLADNLENLILKEGPETVAAFIAEPVIGAGGVIPPPKTYFEKIQAVLQKYDVLFIADEVITGFGRLGTMFGSDLYNIKPDLVSLAKALSSAYVPIGATLVSPEISDVVHSQSNKIGFFAHGFTYSGHPVSCAVALEALKIYRERNIPAHVKQISPRFQEGIKAFAGSSIIGETRGVGLLLATEFANNKSPNDPFPVEWGVAQIFGAECKKRGMLVKVVGDEIAMSPPLIMSQREVDGLVSIYGEALKATEERVAELRSKKK | Transaminase that degrades gamma-amino butyric acid (GABA).
Subcellular locations: Mitochondrion |
GATP2_SOLLC | Solanum lycopersicum | MAKTNGFMGHDMLAPFTAAWMIDMGPLVIDKAEGSYVYGVNGKKYLDSLSGLWCTVLGGSEPRLIEAASKQLNKSAFYHSFWNRTTKPSLDLAKELINMFTANKMGKVFFTSSGSEANDTQVKLVWYYNNAIGRPNKKKIISRKNAYHGSTYMTAGLSGLPSLHLKFDLPPPYILHTDCPHYWNYHLPGETEEEYSTRLANNLENLILKEGPETVAAFIAEPVMGGAGVIIPPATYFEKIQAVLKKYDILFIADEVICGFGRLGTMFGCDKYNIKPDLVSIAKALSGGYIPIGAVLVSEEISKVIMSQSNQLGVFCHGFTYSGHPVACAVALEALKIYKEKNITEVVNKLSPKLQEGLKAFIDSPIIGEIRGTGLVLSTEFVDNKSPNDPFPPEWGVGTYFGSQCQKHGMLVSFSGDHVNMAPPFTLSLEELDEMISIYGKALKDTEKRVEELKSQKK | Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate or glyoxylate as amino-group acceptor. Cannot use beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors. May be responsible for establishing the GABA gradient in the carpel.
Subcellular locations: Cytoplasm
Expressed in leaves, roots, stems, flowers and fruits. Expressed in carpels, but not in stamens. |
GATP3_ORYSI | Oryza sativa subsp. indica | MICRSLLLLRSNAASKASSIVKHVAATGCLPEYSSEAPARYFSSESSLQVDSTEENGFKGHGMLAPFTAGWQSTDLHPLVIDRSEGSYVYDINGKKYIDALAGLWSTALGGNEPRLIKAATDQLNKLPFYHSFWNRTTKPSLDLANEILSMFTAREMGKIFFTNSGSEANDSQVKLVWYYNNALGRPNKKKFIARSKSYHGSTLVSASLSGLPALHQKFDLPAPFVLHTDCPHYWRFHLPDETEEEFATRLATNLENLILKEGPETIAAFIAEPVMGAGGVIPPPKTYFEKIQAVLKKYDILLIADEVITAFGRLGTMFGCDMYDIKPDLVSIAKALSSAYMPIGAILVSPEITDVIYSQSNKLGSFAHGFTYSGHPVSCAVAIEALKIYKERNIIEHVQKIAPRFQEGIKAFSGSPIVGEIRGLGLILGTEFVDNKSPNDPFPAEWGVGSLFGAECEKRGMLIRVAGDNIMLSPPLIMTPDEVEEIISKYGDALKATEERIAELKAKRG | Transaminase that degrades gamma-amino butyric acid (GABA).
Subcellular locations: Mitochondrion |
GATP3_ORYSJ | Oryza sativa subsp. japonica | MICRSLLLLRSNAASKASNIVKHVAATGCLPKYSSEAPARYFSSEPSLQVDSTEENGFKGHGMLAPFTAGWQSTDLHPLVIDRSEGSYVYDINGKKYIDALAGLWSTALGGNEPRLIKAATDQLNKLPFYHSFWNRTTKPSLDLANEILSMFTAREMGKIFFTNSGSEANDSQVKLVWYYNNALGRPNKKKFIARSKSYHGSTLVSASLSGLPALHQKFDLPAPFVLHTDCPHYWRFHLPDETEEEFATRLATNLENLILKEGPETIAAFIAEPVMGAGGVIPPPKTYFEKIQAVLKKYDILLIADEVITAFGRLGTMFGCDMYDIKPDLVSIAKALSSAYMPIGAILVSPEITDVIYSQSNKLGSFAHGFTYSGHPVSCAVAIEALKIYKERNIIEHVQKIAPRFQEGIKAFSGSPIVGEIRGLGLILGTEFVDNKSPNDPFPAEWGVGSLFGAECEKRGMLIRVAGDNIMLSPPLIMTPDEVEEIICKYGDALKATEERIAELKAKRG | Transaminase that degrades gamma-amino butyric acid (GABA).
Subcellular locations: Mitochondrion |
GATP3_SOLLC | Solanum lycopersicum | MAKITSLIGSGIVAATNQVGPHVKHIPAVGNLQKQIVSDQIQVRWSSTETSLKNDISATDVRGYKGHDMLAPFTAGWHSTDLEPLVIQKSEGSYVYDVNGKKYLDALAGLWCTSLGGNEPRLVAAATKQLNELAFYHSFWNRSTKPSLDLAKELLDLFTANKMAKAFFTNSGSEANDTQVKLVWYYNNALGRPDKKKFIARTKSYHGSTLISASLSGLPALHQQFDLPAPFVLHTDCPHFWRFHQPGETEEEFSTRLANNLENLILKEGPETIAAFIAEPVMGAGGVIPPPATYFEKVQAILKKYDILFIADEVICGFGRLGTMFGCEKYNIKPDLVSVAKALSSGYMPIGAVLVSPEVSDVIYSQSNKLGTFSHGFTYSGHPVSCAVALETLKIYKERNIIEQVNRISPKFQEGLKAFSDSPIIGEIRGTGLLHGTEFTDNKSPNDPFPPEWGIGAYFGARCEKHGVLVRVAGDNIMMSPPYILSLEEIDELIIKYGKALKDTENRVEELKSQKKIKSS | Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate or glyoxylate as amino-group acceptor. Cannot use beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors.
Subcellular locations: Plastid, Chloroplast
Expressed in leaves, roots, stems, flowers and fruits. |
GATP4_ORYSJ | Oryza sativa subsp. japonica | MTTPHGLLQYSSGAFSDQVPADDSAEEHGVKDHAMLAPFTAAWQTAISPPLVIERSEGCYVYDVNGTKYLDALAGLLSTALGGSEPRLVKAATEQLNKLPFYHSFWNHTTRPSLDLAKELISMFTAREMGKVFFTNSGSEANDSQVKIVWYYNNALGRPKKKNIISRTQSYHGTTFISASLSGLPTLHQDFDLPGRFVLHTDCPHYWRFHLPGETEEEFATRLADNLENLILKQGPETIAAFIAEPVIGAGGVILPPKTYFEKIQAVVKKYDILFIVDEVITGFGRLGTMFGSDLYNIKPDLVSLAKALSSAYAPIGAILVSPEISDVIHSHSNKLGTFAHGFTYSGHPVSCAVALEALKIYRERDIPGHVTHVAQRFQEGIKAFAAGSPIVGETRGVGLLIATEFTDNKSPYELFPFEWGVGEIFGQECKKRGMMVKVLGNLIAMSPPLIITREEIDKLVSIYGEALKATEERVAELKSKKN | Transaminase that degrades gamma-amino butyric acid (GABA).
Subcellular locations: Cytoplasm
Not detected in roots, stems, flowers or leaves of healthy plants. |
GCP4_MEDTR | Medicago truncatula | MLHELLLALLGYTGDLIIDRRDNNLSANTPISDECTFKLAPDISFIDPSDRELIERIITLGFYYRELERFSAKSRNLNWIRSENANPLENKEKPSVYRRALANGIVEILAVYSSSILHIEQLLLSETMPILATVTQGLNKFFSLLPPLYELILKIERGDIRGGELLNLLHKKCHCGVPELQTCIQRLLWHGHQVMYNQLASWMVYGILEDRHGEFFISRQEGRDVENSSSHQEISEKLSRLSTADASLSDWHMGFHISLDMLPEYIPMRVAESILFAGKAVRVLRNPSPSFLSQDDVYPQEPKRFPKIHGFEGRFNFQREPIINTGMRVEDLLPQSEADKIENMLLDLKESSEFHKRSFECAVDSIQAIAASHLWQLVVVRADLNGHLKALKDYFLLAKGDFFQCFLEESRQLMRLPPRQSTAEADLMVPFQLASLKTIGEEDKYFSKVSLRMPSYGITVKPSLLNVPKATSAAADGISGASISNASSEMSVDGWDGIALEYSIEWPLHLFFTQEVLSRYLKVFQYLLRLKRTQMELEKLWASVMHQYHSIFAKNKKSDQDKSPITQQRDQRFRSMWRVREHMAFLIRNLQFYIQVDVIESQWNILQSHIQDSHDFTELVGFHQEYLSALISQTFLDIGSVSRILDGIMKLCLQFCWNIENQDNFSNTSELEHIAEEFNKKSNSLYTILRSSRLAGSQRTPFLRRFLLRLNLNSFFESTAKEVMNVVRPRPTFPGLNQR | Gamma-tubulin complex is necessary for microtubule nucleation at the microtubule organizing centers (MTOCs).
Subcellular locations: Cytoplasm, Cytoskeleton, Microtubule organizing center |
GCSH_PEA | Pisum sativum | MALRMWASSTANALKLSSSSRLHLSPTFSISRCFSNVLDGLKYAPSHEWVKHEGSVATIGITDHAQDHLGEVVFVELPEPGVSVTKGKGFGAVESVKATSDVNSPISGEVIEVNTGLTGKPGLINSSPYEDGWMIKIKPTSPDELESLLGAKEYTKFCEEEDAAH | The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Subcellular locations: Mitochondrion |
GCST_SOLTU | Solanum tuberosum | MRGGLWQLGQSITRRLAQADKKTIGRRCFASDADLKKTVLYDFHVVNGGKMVPFAGWSMPIQYKDSIMDSTVNCRENGSLFDVSHMCGLSLKGKDTIPFLEKLVIADVAGLAPGTGSLTVFTNEKGGAIDDSVVTKVTNDHIYLVVNAGCRDKDLAHIEEHMKSFKSKGGDVSWHIHDERSLLALQGPLAAPVLQYLTKDDLSKMYFGEFRVLDINGAPCFLTRTGYTGEDGFEISVPSENALDLAKALLEKSEGKIRLTGLGARDSLRLEAGLCLYGNDMEQHTTPVEAGLTWAIGKRRRAEGGFLGAEVILKQIEEGPKIRRVGFFSSGPPPRSHSEIQDSNGQNIGEITSGGFSPCLKKNIAMGYVKTGNHKAGTNVKIVIRGKSYDGVVTKMPFVPTKYYKP | The glycine cleavage system catalyzes the degradation of glycine.
Subcellular locations: Mitochondrion |
GENL1_ORYSJ | Oryza sativa subsp. japonica | MGVGGSFWDLLKPYARHEGAGYLRGRRVAVDLSFWVVSHSAAIRARSPHARLPHLRTLFFRTLSLFSKMGAFPVFVVDGQPSPLKSQVRAARFFRGSGMDLAALPSTEAEASADALVQPRNAKFTRYVEDCVELLEYLGMPVLRAKGEGEALCAQLNNQGHVDACITSDSDAFLFGAKTVIKVLRSNCKEPFECYNMADIESGLGLKRKQMVAMALLVGSDHDLHGVPGFGPETALRFVQLFDEDNVLAKLYEIGKGVYPFIGVSAPNIDDLPSPSTKSLPRARSPHCSHCGHPGNKKNHIKDGCNFCLVDSLENCVEKPAGFICECPSCDKARDLKVQRRNENWQIKVCKRIAAETNFPNEEIINLYLNDDNLDNENGVPLLTWNKPDMEILVDFLSFKQNWEPAYIRQRMLPMLSTIYLREMASSQSKSFLLYDQYKFHSIQRIKIRYGHPYYLVKWKRVTRSMISNDPPSKQTELEGKNDKVEVLDGDDEVVDEEEEEPTMISETTELLDEPDVPQVLDDDKDCFLLTDEDIELVNAAFPDEAQRFQEEQRLKEAKSIARKSKLNVAGFETPKGPRPSGVQLSIKEFYRSKKGLSGDSGKDGSRKSSDVDLSKNLPKSVRRRLLFD | Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA. Possesses both single-stranded and double-stranded DNA-binding activities. Involved in early microspore development, but does not alter meiosis or tapetal cells development (, ). Possesses Holliday junction (HJ) resolvase activity in vitro. Cleaves HJ at symmetrically related sites of the branch point .
Subcellular locations: Nucleus
Highly expressed in anthers. Expressed in roots and leaves. |
GENL2_ORYSJ | Oryza sativa subsp. japonica | MGVKNLWDILESCKKKLPLHHLQNKKVCVDLSCWLVQMYSANRSPAFAKDKVYLKNLFHRIRALLALNCTLLFVTDGAIPSLKLATYRRRLGSISHAAKESDQPNSHPSISLRRNKGSEFSCMIKEAKRLGMALGIPCLDGLEEAEAQCASLDLESLCDGCFTSDSDAFLFGARTVYRDVFIGEGGYVICYEMEDIEKTLGFGRNSLISLAVLLGSDYSNGVNGFGPETACRLVKSVGDNLILDQILSNGVKATRKCKGKNSGNKVDDMCPKASSCEVGMTQDSDGQFRDVINAYLEPKCHSPDSEAVQRVCGQHPFLRPQLQKICEEYFDWSPEKTDQYILPKIAERELRRFSDLRSASSALGIKPLLSEIPVPCPVLAIVKQRKVHGNECYEVSWRNIEGLQVSVVPGDLVKSACPEKITEFLEKKGEEKKQKRRARPKKSGQAAVKDVDEQLQELLLGIEADSGGILGATASVCQTLTAAYTVAVEDVVDLSSPSPPLRKLSKSQKKMMAEDVNVAGMNMNKMESESSFSTQSSTSDVDNQLIDLSSPLAGGDNGMKGGRRALADISNVGSHSTETDGGGGGGGGVASVGHGTTIDLSSPSPAIGDRSRVHHDDDDVIHERKARDLRMFLDSIRNELY | Single-stranded DNA endonuclease activity in vitro . May not be active as double-stranded DNA endonuclease . Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA with a specific cleavage site in the 5' overhang strand exactly one nucleotide 3' of the branch point (By similarity). Structure- and sequence-specific nuclease that resolves holliday junctions (HJs) by symmetrically oriented incisions in two opposing strands near the junction point, thus leading to ligatable products; HJs are physical links between homologous DNA molecules that arise as central intermediary structures during homologous recombination and repair in meiotic and somatic cells (By similarity). Probably involved in the resolution of toxic replication structures to ensure genome stability, and to maintain telomere integrity and replication (By similarity).
Subcellular locations: Nucleus
Highly expressed in shoot apical meristem (SAM) and young leaves. Expressed in roots, flag leaf and panicles. |
GGH_SOYBN | Glycine max | MPNDSVLSLFFFVTLFTCLLSATSHDDHIFLPSQLHDDDSVSCTATDPSLNYKPVIGILTHPGDGASGRLSNATGVSYIAASYVKFVESGGARVIPLIYNESPENLNKKLDLVNGVLFTGGWAVSGPYLDTLGNIFKKALERNDAGDHFPVIAFNLGGNLVIRIVSEQTDILEPFTASSLPSSLVLWNEANAKGSLFQRFPSDLLTQLKTDCLVLHNHRYAISPRKLQYNTKLSDFFEILATSGDRDGKTFVSTARGRKYPVTVNLWQPEKNAFEWATSLKAPHTEDAIRVTQSTANFFISEARKSTNTPDAQKVRDSLIYNYKPTFGGTAGKGYDQVYLFE | Subcellular locations: Secreted, Extracellular space, Secreted, Cell wall
Extracellular or cell-wall bound.
Expressed only in young (1-15 day old) leaf, stem and root tissue. |
GINT1_ORYSI | Oryza sativa subsp. indica | MAGRRAMRPSGSSMRGVVARLAAARSPAVSFLVAAAAGAALVGGVYFWLVVSSFRLPDSRAVGCLPDGEGSWAIGMYYGKSPLELRPIELEGRSNGNSSAWPVANPVLTCATPTEGGYPSNFVADPFLYVQGDTLFLFFETKTVSTMQGDIGVARSLDQGATWEFLGIALDEAWHLSYPFVFKYENEIYMMPEGNKKKELRLYRATKFPLEWTLEKVLIDKPLIDSSLVQYDGLWWLFASDFTRHGIEKNAELEIRYSNSPLGPWSEHKQNPIYRSDKSLGARNGGRLFIFEGSLYRPGQDCSGTYGRKVKLYKIEKLTKEEYKEVPVNLGIEEAKKGRNAWNGMRYHHIDAQQLASGGWVAVMDGDRVPSGDSTRRSLFGYMGFLVAVALVTFVGFVKGAISCYIPPSFWVPLTRRSELSRILPVHRFNLKIRRYSTSIGRNISATKARLSEKTWSNTLFFCVIALIGIVNVCIAVHFLLGGNGAEEAYTHQGQHSQFTMVTMTYEARLWNLKLFVEHYSRCESVREIVVVWNKGNHPTSDAFDSTVPVRIRVEEINSLNNRFRGDPLIKTRAVLELDDDIMMTCSDVEKGFKVWREHPERMVGFYPRMIDGDPLQYRNERYARGKKGYNLILTGAAFMDSEFAFSKYWSQEAKEGRDYVHKNFNCEDLLMNFLYANASSSRTVEYVHPAWAIDTSKLSSVAISRDTQKHYDIRTKCLAKFASIYGPLPQKWLFGMREDGWDK | Essential protein. Glycosyltransferase that mediates the glycosylation of glycosylinositol phosphorylceramides (GIPCs), the major sphingolipids in the plasma membrane; acts as a HexN(Ac)-specific GIPC sugar transferase. Responsible for the glycosylation of a subgroup of GIPCs found in seeds and pollen that contain GlcNAc and GlcN (GlcN(Ac)). Maybe involved in the maintenance of cell-cell adhesion.
Subcellular locations: Membrane |
GINT1_ORYSJ | Oryza sativa subsp. japonica | MAGRRAMRPSGSSMRGVVARLAAARSPAVSFLVAAAAGAALVGGVYFWLVVSSFRLPDSRAVGCLPDGEGSWAIGMYYGKSPLELRPIELEGRSNGNSSAWPVANPVLTCATPTEGGYPSNFVADPFLYVQGDTLFLFFETKTVSTMQGDIGVARSLDQGATWEFLGIALDEAWHLSYPFVFKYENEIYMMPEGNKKKELRLYRATKFPLEWTLEKVLIDKPLIDSSLVQYDGLWWLFASDFTRHGIEKNAELEIWYSNSPLGPWSEHKQNPIYRSDKSLGARNGGRLFIFEGSLYRPGQDCSGTYGRKVKLYKIEKLTKEEYKEVPVNLGIEEAKKGRNAWNGMRYHHIDAQQLASGGWVAVMDGDRVPSGDSTRRSLFGYMGFLVAVALVTFVGFVKGAISCYIPPSFWVPLTRRSELSRILPVHRFNLKIRRYSTSIGRNISATKARLSEKTWSNTLFFCVIALIGIVNVCIAVHFLLGGNGAEEAYTHQGQHSQFTMVTMTYEARLWNLKLFVEHYSRCESVREIVVVWNKGNHPTSDAFDSTVPVRIRVEEINSLNNRFRGDPLIKTRAVLELDDDIMMTCSDVEKGFKVWREHPERMVGFYPRMIDGDPLQYRNERYARGKKGYNLILTGAAFMDSEFAFSKYWSQEAKEGRDYVHKNFNCEDLLMNFLYANASSSRTVEYVHPAWAIDTSKLSSVAISRDTQKHYDIRTKCLAKFASIYGPLPQKWLFGMREDGWDK | Essential protein. Glycosyltransferase that mediates the glycosylation of glycosylinositol phosphorylceramides (GIPCs), the major sphingolipids in the plasma membrane; acts as a HexN(Ac)-specific GIPC sugar transferase. Responsible for the glycosylation of a subgroup of GIPCs found in seeds and pollen that contain GlcNAc and GlcN (GlcN(Ac)). Maybe involved in the maintenance of cell-cell adhesion.
Subcellular locations: Membrane
Highly expressed in almost all tissues. |
GIP1_SOYBN | Glycine max | MPPPLPSLCNFNLAILFLFLTPTFQIPLIAPISKDDTTQLYTLSVFLKTPLQPTKLHLHLGSSLSWVLCDSTYTSSSSHHIPCNTPLCNSFPSNACSNNSSLCALFPENPVTRNTLLDTALIDSLALPTYDASSSLVLISDFIFSCATAHLLQGLAANALGLASLGRSNYSLPAQISTSLTSPRSFTLCLPASSANTGAAIFASTASSFLFSSKIDLTYTQLIVNPVADTVVTDNPQPSDEYFINLTSIKINGKPLYINSSILTVDQTGFGGTKISTAEPYTVLETSIYRLFVQRFVNESSAFNLTVTEAVEPFGVCYPAGDLTETRVGPAVPTVDLVMHSEDVFWRIFGGNSMVRVAKGGVDVWCLGFVDGGTRGRTPIVIGGHQLEDNLMQFDLDSNRFGFTSTLLLQDAKCSNLKVNNFANGIK | Involved in plant defense against Phytophtora sojae . Contributes positively to soybean resistance against P.sojae . Binds the P.sojae xyloglucanase XEG1 and inhibits its cell wall degrading enzyme activity and its contribution as P.sojae virulence factor . XEG1 acts as an important virulence factor during P.sojae infection but also acts as a pathogen-associated molecular pattern (PAMP) in soybean and solanaceous species, where it can trigger defense responses including cell death .
(Microbial infection) Possesses stronger binding affinity with XLP1, a truncated paralog of P.sojae XEG1 which has no enzyme activity. Is impaired in its inhibitor activity towards the P.sojae xyloglucanase XEG1 when hijacked by XLP1 binding.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL812_ORYSJ | Oryza sativa subsp. japonica | MASSSLFLLGALLVLASWQAIVAYDPSPLQDFCVADMNSPVRVNGFACKNPMDVSSEDFFNAAKFDMPRNTFNKLGSNVTNLNVMEFPGLNTLGISLARIDYAPMGVNPPHIHPRATELLTVLEGTLYVGFVTSNPNKLFSKVVCKGDVFVFPKAMIHFQMNLDHDKPAVAQSALSSQNPGVITIASAVFGSQPPISDDVLTKAFQVEKKLIDWLQSQFWENNY | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL813_ORYSJ | Oryza sativa subsp. japonica | MSSTPLLPVLLSTMILLSAVSTTTTALTQDFCVANLPLGADTPSGYQCRPAATVTAADFYSGALARPGILIRPFNTSLASAFVQQYPAVNGLGISASRVDILPGGVVPLHTHPAGSELLYVLDGALVAGFISSSDNKVYYKEVSKGGMFVFPQGLLHFQYNTGDTTAVAFAAYSSSNPGLQILDYALFANNLPTSYVVKGTFLAEAEVRRLKSKFGGSG | May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL814_ORYSJ | Oryza sativa subsp. japonica | MAKAVMMLPVLLSFLLLPFSSMALTQDFCVADLTCSDTPAGYPCKASVGAGDFAYHGLAAAGNTSNLIKAAVTPAFVGQFPGVNGLGISAARLDIAVGGVVPLHTHPAASELLFVTQGTVAAGFITSSSNTVYTRTLYAGDIMVFPQGLLHYQYNAGQSAAVALVAFSGPNPGLQITDYALFANNLPSAIVEKVTFLDDAQVKKLKSVLGGSG | May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL81_ORYSJ | Oryza sativa subsp. japonica | MASFISFLLLAALIGMASWQAIAAEPSPLQDFCVADLNSAVRVNGFACKNPTNVSADDFFKAAMLDKPRDTAVNKVGSNITLINVMEIPGLNTLGISIVRVDYAPLGLNPPHTHPRATEIFTVLEGTLYVGFVTSNPDNKLFSKVLNKGDVFVFPKGLIHFQFNLDPHKPAIATSAISSQNPGIITIANAVFRSNPPISDDILAKAFQVDKKIIDLLQA | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL82_ORYSJ | Oryza sativa subsp. japonica | MASSSFSFLLVAALLGLASWKAIASDPSPLQDFCVADLNSPVRVNGFVCKNPMNASADDFFKAAMLDKPRDTNNKVGSNVTLVNVLQLPGLNTLGISIARLDFAPLGLNPPHTHPRATEIFTVLEGTLYVGFVTSNPDNRLLSKVLNKGDVFVFPEGLIHFQFNPNPHKPAVAIAALSSQNPGVITIANAVFGSNPPISDDILMKAFQVDKKIIDLLQAQF | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL83_ORYSJ | Oryza sativa subsp. japonica | MASSSLFLLASLLVLASWQQAIAFDPSPLQDFCVADMASPVRVNGFPCKNPMNVTSDDFFNAAKFDMPRNTMNKVGSNVTNLNVINFPGLNTLGISLARIDYAPMGVNPPHVHPRATELLTVLEGTLYVGFVTSNPNRLFSKVVHKGDVFVFPKAMIHFQMNLDHNKPAVAQSALSSQNPGVITIASAIFGSTPPISDDVLVKAFQVEKKVIDWLKSQFSENNHY | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL84_ORYSJ | Oryza sativa subsp. japonica | MASSSSLYLLAALLALASWQAIAFDPSPLQDFCVADMKSPVRVNGFPCKNPMEVNSDDFFNAAKFDMPRSTMNKVGSNVTNLNVLNFPGLNTLGISLARIDYAPLGVNPPHIHPRATELLTVLEGTLYVGFVTSNPNRLFSKVVHKGDTFVFPKAMIHFQMNLDHNKPAVAQSSLNSQNPGVITIASAVFGSKPPISDDVLTKAFQVEKKVIDWLKSQFWESNY | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL85_ORYSJ | Oryza sativa subsp. japonica | MASPSSLCLLAALALISWQAMASDPSPLQDFCVADMHSPVRVNGFACLNPMEVNADHFFKAAKLDTPRKTNKVGSNVTLINVMQIPGLNTLGISIARIDYAPLGQNPPHTHPRATEILTVLEGTLYVGFVTSNPNNTLFSKVLNKGDVFVFPQGLIHFQFNPNPHQPAVAIAALSSQNPGAITIANAVFGSKPPISDEVLAKAFQVEKGTIDWLQAQFWENNHY | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL86_ORYSJ | Oryza sativa subsp. japonica | MASPSSLCLLTALLALVSWQTIASDPSPLQDFCVADEHSPVLVNGFACLDPKHVNADHFFKAAMLDTPRKTNKVGSNVTLINVMQIPGLNTLGISIARIDYAPLGQNPPHTHPRATEILTVLEGTLYVGFVTSNPNNTLFSKVLKKGDVFVFPVGLIHFQFNPNPHQPAVAIAALSSQNPGAITIANAVFGSKPPISDEVLAKAFQVEKGTIDWLQAQFWENNHY | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL87_ORYSJ | Oryza sativa subsp. japonica | MASPSSFCLLAVLLALVSWQAIASDPSPLQDFCVADKHSPVLVNGFACLDPKYVNADHFFKAAMLDTPRKTNKVGSNVTLINVMQIPGLNTLGISIARIDYAPLGENPPHTHPRATEILTVLEGTLYVGFVTSNPNNTLFSKVLNKGDVFVFPEGLIHFQFNPNPHQPAVALAALSSQNPGAITIANAVFGSKPPISDDILAKAFQVEKGTIDWLQAQFWENNHY | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL88_ORYSJ | Oryza sativa subsp. japonica | MASPSFCLLAALLALVSWQAIASDPSPLQDFCVADKHSPVLVNGFACLDPKYVTADHFFKAAMLDTPRKTNKVGSNVTLINVMQIPGLNTLGISIARIDYAPLGENPPHTHPRATEILTVLEGTLYVGFVTSNPNNTLFSKVLNKGDVFVFPEGLIHFQFNPNPHQPAVAIAALSSQNPGAITIANAVFGSKPPISDKVLAKAFQVEKGTIDWLQAQFWENNHY | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GL89_ORYSJ | Oryza sativa subsp. japonica | MASPSFCLFAALLALVSWQAIASDPSPLQDFCVADKHSPVLVNGFACLDPKYVTADHFFKAAMLDTPRKTNKVGSNVTLINVMQIPGLNTLGISIARIDYAPLGQNPPHTHPRATEILTVLEGTLHVGFVTSNPNNTLFSKVLNKGDVFVFPVGLIHFQFNPNPHQPAVAIAALSSQNPGVITIANAVFGSKPPISDEVLAKAFQVGKGTIDWLQAQFWENNHY | Plays a role in broad-spectrum disease resistance. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular locations: Secreted, Extracellular space, Apoplast |
GLGB_SOLTU | Solanum tuberosum | MEINFKVLSKPIRGSFPSFSPKVSSGASRNKICFPSQHSTGLKFGSQERSWDISSTPKSRVRKDERMKHSSAISAVLTDDNSTMAPLEEDVKTENIGLLNLDPTLEPYLDHFRHRMKRYVDQKMLIEKYEGPLEEFAQGYLKFGFNREDGCIVYREWAPAAQEDEVIGDFNGWNGSNHMMEKDQFGVWSIRIPDVDSKPVIPHNSRVKFRFKHGNGVWVDRIPAWIKYATADATKFAAPYDGVYWDPPPSERYHFKYPRPPKPRAPRIYEAHVGMSSSEPRVNSYREFADDVLPRIKANNYNTVQLMAIMEHSYYGSFGYHVTNFFAVSSRYGNPEDLKYLIDKAHSLGLQVLVDVVHSHASNNVTDGLNGFDIGQGSQESYFHAGERGYHKLWDSRLFNYANWEVLRFLLSNLRWWLEEYNFDGFRFDGITSMLYVHHGINMGFTGNYNEYFSEATDVDAVVYLMLANNLIHKIFPDATVIAEDVSGMPGLGRPVSEGGIGFDYRLAMAIPDKWIDYLKNKNDEDWSMKEVTSSLTNRRYTEKCIAYAESHDQSIVGDKTIAFLLMDKEMYSGMSCLTDASPVVDRGIALHKMIHFFTMALGGEGYLNFMGNEFGHPEWIDFPREGNNWSYDKCRRQWNLADSEHLRYKFMNAFDRAMNSLDEKFSFLASGKQIVSSMDDDNKVVVFERGDLVFVFNFHPKNTYEGYKVGCDLPGKYRVALDSDAWEFGGHGRTGHDVDHFTSPEGIPGVPETNFNGRQIPSKCCLLREHVWLITELMNACQKLKITRQTFVVSYYQQPISRRVTRNLKIRYLQISVTLTNACQKLKFTRQTFLVSYYQQPILRRVTRKLKDSLSTNIST | Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Subcellular locations: Plastid, Chloroplast, Plastid, Amyloplast |
GLO2_ORYSJ | Oryza sativa subsp. japonica | MALVTNVCEYEELAKHKLPKMVYDFYAVDAEDQWTLRENSEAFSRILFQPVVLVDVSCIDMSMSVLGYNISMPIMIAPTALHKLAHPEGELATARAAAAAETIMTLSSWSSCSIEEVNLAGPGVRFFQLSIYKDRNLVQQLIQRAEKAGYKAIVLTVDAPWLGRREADVKNRFTLPQNVMLKIFEGLDQGKIDETNGSGLAAYVASQIDRSFSWKDIKWLQTVTSLPVLVKGIITAQDTRIAIEYGAAGIIMSNHGGRQLDYLPATISCLEEVVREANGRVPVFIDSGFRRGTDVFKALALGASGVFIGRPVLFSLAIDGEAGVRNALRMLRDELEITMALSGCTSVKEITRGHVVTESDRIRRCSRL | Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2. Is a key enzyme in photorespiration in green plants.
Subcellular locations: Peroxisome |