Patent Publication Number: US-2021189439-A1

Title: Multifunctional Fatty Acid Derivatives And Biosynthesis Thereof

Description:
FIELD 
     The disclosure relates to the field of specialty chemicals and methods for their synthesis. The disclosure provides novel multifunctional fatty acid derivative compounds such as e.g., fatty triols, dihydroxy fatty acids, etc. derivatives thereof. The disclosure further provides biochemical pathways, recombinant microorganisms and methods for the biological production of various multifunctional fatty acid derivatives. 
     BACKGROUND 
     Hydrocarbon based organic chemicals are employed by almost every industry. The many commercial and industrial uses of hydrocarbon based organic chemicals include e.g., emollients and thickeners in cosmetics and foods, pharmaceuticals, industrial solvents, surfactants, plasticizers, lubricants, emulsifiers, building blocks of polymers, etc., (see e.g., H. Maag (1984) Journal of the American Oil Chemists&#39; Society 61(2): 259-267). Thus, hydrocarbon based organic chemicals play an indispensable role in modern society. 
     Historically, most organic chemicals have been obtained as by-products from the petrochemical industry. Although more than 90 percent of the organic chemical industry is based on petroleum, the production of organic chemicals from petroleum has many disadvantages and limitations. In particular, the synthesis of medium- to long-chain hydrocarbons (C6 to C18) with multiple hydroxy(—OH), oxo (═O), amino- (—NH 2 ) or carboxyl (CO 2 H) groups in selective positions is extremely difficult and in many cases impractical or impossible starting from petrochemical feedstocks. 
     Clearly then, what is needed in the art are novel functionalized organic chemical compounds and methods for making them. In particular, a need exists for the production of medium- to long-chain hydrocarbons (C6 to C18) that have pre-designed, or “tailored,” specifications and properties useful for the preparation detergents, lubricants, pharmaceuticals, polymers and other valuable applications. 
     Fortunately, as will be clear from the detailed description that follows, the present disclosure provides for this and other needs. 
     SUMMARY 
     One aspect of the disclosure provides a multifunctional molecule having a chemical formula according to 
     
       
         
         
             
             
         
       
     
     wherein
         R1=-OH; —O 2 H; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3      R2=-H; —OH;   R3=-H; —OH;   R4=-H; —OH;   R5=-CH 3 ; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3 ;       

     wherein
         m=1-10 and n=0-9 and       

     wherein
         if R1 is OH or —O 2 H then 3&lt;m+n≤10; and if R1 is other than OH or —O 2 H, then 2&lt;m+n≤10, and       

     wherein
         the multifunctional molecule has at least three functional groups comprising a heteroatom, and       

     wherein
         at least two of R2, R3 and R4 are OH; or when R5 is other than CH 3 , CH 2  or C 3 H 7  CH 2 H 5  then at least one of R2, R3 and R4 are OH; and       

     wherein
         when R5=CH 3  and R4=H then n=0 or 1; and       

     wherein
         when R2=H, then R4 does not=H; and       

     wherein
         when R3=H, then n+m=p and p=3-10; unless R1=-OH or —O 2 H in which case when R3-H then n+m=p and p=4-10; and       

     wherein
         when the multifunctional molecule comprises a double bond that is not terminal, the double bond is in a position corresponding to an omega7 (ω-7) position; and wherein   the multifunctional molecule is not 1,3,12-dodecane triol; is not 3,11-dihydroxy-tetradecanoic acid; is not 3,11-dihydroxy-tetradecanoic acid methyl ester and is not naturally occurring.       

     In one embodiment, the multifunctional fatty acid derivative molecule is a multifunctional alcohol. In one embodiment, the multifunctional fatty acid derivative molecule has R1=CH 2 OH and R2=OH. In one embodiment, the multifunctional fatty acid derivative molecule is a member selected from the group consisting of 1,3,11-dodecane triol, 1,3, 10-dodecane triol, 1,3,9-dodecane triol, 1,3,12-dodecene triol, 1,3,11-dodecene triol, 1,3,10-dodecene triol, 1,3,9-dodecene triol, 1,3,11,12-dodecane tetrol, 1,3,10,12-dodecane tetrol, 1,3,9,12 dodecane tetrol, 1,3,7-decane triol, 1,3,8-decane triol, 1,3,9-decane triol. 
     In one embodiment, the multifunctional fatty acid derivative molecule is a multifunctional fatty acid ester. In one embodiment, the multifunctional fatty acid derivative molecule has R1=CO 2 CH 3  and R2=OH. In one embodiment, the multifunctional fatty acid derivative molecule is a member selected from the group consisting of 3,12-dihydroxy dodecanoic acid methyl ester, 3,14-dihydroxy tetradecanoic acid methyl ester, 3,16-dihydroxy hexadecanoic acid methyl ester, 3,12-dihydroxy dodecenoic acid methyl ester, 3,14-dihydroxy tetradecenoic acid methyl ester, 3,16-dihydroxy hexadecenoic acid methyl ester, 3,11-dihydroxy dodecanoic acid methyl ester, 3,10-dihydroxy dodecanoic acid methyl ester, 3,9-dihydroxy dodecanoic acid methyl ester, 3,11-dihydroxy dodecenoic acid methyl ester, 3,10-dihydroxy dodecenoic acid methyl ester, 3,9-dihydroxy dodecenoic acid methyl ester, 3,13-dihydroxy tetradecanoic acid methyl ester, 3,12-dihydroxy tetradecanoic acid methyl ester, 3,13-dihydroxy tetradecenoic acid methyl ester, 3,12-dihydroxy tetradecenoic acid methyl ester, 3,11-dihydroxy tetradecenoic acid methyl ester, 3,15-dihydroxy hexadecanoic acid methyl ester, 3,14-dihydroxy hexadecanoic acid methyl ester, 3,13-dihydroxy hexadecanoic acid methyl ester, 3,15-dihydroxy hexadecenoic acid methyl ester, 3,14-dihydroxy hexadecenoic acid methyl ester and 3,13-dihydroxy hexadecenoic acid methyl ester. 
     In one embodiment, the multifunctional fatty acid derivative molecule has R1=CO 2 CH 2 CH 3  and R2=OH. In one embodiment, the multifunctional fatty acid derivative molecule is a member selected from the group consisting of 3,12-dihydroxy dodecanoic acid ethyl ester, 3,14-dihydroxy tetradecanoic acid ethyl ester, 3,16-dihydroxy hexadecanoic acid ethyl ester, 3,12-dihydroxy dodecenoic acid ethyl ester, 3,14-dihydroxy tetradecenoic acid ethyl ester, 3,16-dihydroxy hexadecenoic acid ethyl ester, 3,11-dihydroxy dodecanoic acid ethyl ester, 3,10-dihydroxy dodecanoic acid ethyl ester, 3,9-dihydroxy dodecanoic acid ethyl ester, 3,11-dihydroxy dodecenoic acid ethyl ester, 3,10-dihydroxy dodecenoic acid ethyl ester, 3,9-dihydroxy dodecenoic acid ethyl ester, 3,13-dihydroxy tetradecanoic acid ethyl ester, 3,12-dihydroxy tetradecanoic acid ethyl ester, 3,11-dihydroxy tetradecanoic acid ethyl ester, 3,13-dihydroxy tetradecenoic acid ethyl ester, 3,12-dihydroxy tetradecenoic acid ethyl ester, 3,11-dihydroxy tetradecenoic acid ethyl ester, 3,15-dihydroxy hexadecanoic acid ethyl ester, 3,14-dihydroxy hexadecanoic acid ethyl ester, 3,13-dihydroxy hexadecanoic acid ethyl ester, 3,15-dihydroxy hexadecenoic acid ethyl ester, 3,14-dihydroxy hexadecenoic acid ethyl ester and 3,13-dihydroxy hexadecenoic acid ethyl ester. 
     In one embodiment, the multifunctional fatty acid derivative molecule is a multifunctional fatty acid. In one embodiment, n≠4. In one embodiment, the multifunctional fatty acid derivative molecule has R2=H. 
     In one aspect, the disclosure provides a multifunctional fatty acid derivative molecule wherein the multifunctional fatty acid derivative molecule is a multifunctional fatty acid selected from the group consisting of: 10,14-dihydroxyhexadecanoic acid, 10,13-dihydroxyhexadecanoic acid, 9,10,15-trihydroxy hexadecanoic acid; 9,10,14-trihydroxy hexadecanoic acid; and 9,10,13-trihydroxy hexadecanoic acid. 
     In one aspect the disclosure provides a multifunctional fatty acid derivative molecule wherein the multifunctional fatty acid derivative molecule is an unsaturated multifunctional fatty acid selected from the group consisting of: 9,10,15 trihydroxy hexadecenoic acid; 9,10,14 trihydroxy hexadecenoic acid; 9,10,13 trihydroxy hexadecenoic acid; 9,10,15 trihydroxy octadecenoic acid; 7,10,16-trihydroxy-(8e)-hexadecenoic acid; and 7,10,14-trihydroxy-(8e)-hexadecenoic acid. 
     In one aspect the disclosure provides multifunctional fatty acid derivative molecule wherein the multifunctional fatty acid derivative molecule is a multifunctional polyol selected from the group consisting of 1,12,16-hexadecene triol, 1,9,10 hexadecane triol; 1,7,10 hexadecene triol and 1,7,10-(8e)-octadecene triol. 
     In one aspect the disclosure provides a carbonate derivative of a multifunctional fatty acid derivative molecule. In one embodiment, the carbonate derivative has a chemical structural formula according to: 
     
       
         
         
             
             
         
       
     
     In one embodiment, the carbonate derivative has a chemical structural formula according to: 
     
       
         
         
             
             
         
       
     
     In one aspect the disclosure provides a method for preparing a multifunctional fatty acid derivative molecule having an acyl chain length of 8-16 carbons the method comprising: culturing a recombinant microbe that comprises a heterologous enzyme pathway capable of producing a bifunctional fatty acid derivative molecule, and at least one heterologous hydroxylating enzyme, in a culture medium comprising a simple carbon source. In one embodiment, the at least one heterologous hydroxylating enzyme is selected from a heterologous hydroxylase enzyme and a heterologous hydratase enzyme or a combination thereof. In one embodiment, the heterologous hydroxylase enzyme is a member selected from the group consisting of omega-hydroxylases (ω-hydroxylases), mid-chain hydroxylases, and subterminal hydroxylases. In one embodiment, the recombinant microbe is selected from recombinant microbes that comprise: a heterologous enzyme pathway capable of producing a 3-hydroxy fatty acid; a heterologous enzyme pathway capable of producing a 3-hydroxy fatty ester; a heterologous enzyme pathway capable of producing a 1,3-fatty diol; a heterologous enzyme pathway capable of producing a hydroxy fatty acid; a heterologous enzyme pathway capable of producing a hydroxy fatty ester; and a heterologous enzyme pathway capable of producing a fatty diol. In one embodiment, the recombinant microbe is a recombinant bacterial cell. 
     In one aspect, the disclosure provides method for preparing 1,3,12 dodecanetriol, (z5)1,3,12 dodecenetriol or a combination thereof, the method comprising: culturing in a culture medium comprising a simple carbon source, a recombinant microbe that comprises: a heterologous enzyme pathway capable of producing a 1,3-fatty diol, and at least one heterologous hydroxylating enzyme, wherein the heterologous enzyme pathway capable of producing a 1,3-fatty diol comprises: (i) a heterologous plant FatB1 thioesterase and (ii) a heterologous CarB carboxylic acid reductase; and wherein the at least one heterologous hydroxylating enzyme is a heterologous co-hydroxylase selected from a cyp153A family co-hydroxylase and an alkB ω-hydroxylase or a combination thereof. In one embodiment, the cyp153A family comprises a cyp153A ω-hydroxylase protein selected from the group consisting of: SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46 and SEQ ID NO:48. In one embodiment, the cyp153A protein is a chimeric hybrid-fusion protein selected from the group consisting of: a SEQ ID NO:4, SEQ ID NO:6 and SEQ ID NO:8. In one embodiment, 
     the heterologous enzyme pathway capable of producing a 1,3-fatty diol further comprises a heterologous alcohol dehydrogenase. In one embodiment, the heterologous alcohol dehydrogenase is a heterologous AlrA dehydrogenase from  Acinetobacter baylyi . In one embodiment, the at least one heterologous hydroxylating enzyme is a heterologous alkB ω-hydroxylase. In one embodiment, the at least one heterologous hydroxylating enzyme is a cyp153A family ω-hydroxylase. In one embodiment, the at least one heterologous hydroxylating enzyme is the heterologous ω-hydroxylase cyp153A from  Marinobacter aquaeolei . In one embodiment, the at least one heterologous hydroxylating enzyme is a heterologous ω-hydroxylase cyp153A chimeric hybrid-fusion protein selected from the group consisting of: a SEQ ID NO:4, SEQ ID NO:6 and SEQ ID NO:8 In one embodiment, the at least one heterologous hydroxylating enzyme is the combination of a heterologous cyp153A family ω-hydroxylase and an alkB ω-hydroxylase. In one embodiment, the cyp153A family ω-hydroxylase is a cyp153A ω-hydroxylase from  Marinobacter aquaeolei , and the heterologous alkB ω-hydroxylase is an alkB ω-hydroxylase from  Pseudomonas putida . In one embodiment, the heterologous enzyme pathway capable of producing a 1,3-fatty diol comprises a heterologous FatB1 thioesterase from  Umbellaria californica , and a heterologous CarB carboxylic acid reductase from  Mycobacterium smegmatis ; and the at least one heterologous hydroxylating enzyme is a heterologous cyp153A family ω-hydroxylase from  Mannobacier aquaeolei , an alkB from  Pseudomonas putida  or a combination thereof. In one embodiment, the wherein the heterologous enzyme pathway capable of producing a 1,3-fatty diol further comprises a heterologous AlrA dehydrogenase from  Acinetobacter baylyi.    
     In one aspect the disclosure provides a method for making a multifunctional fatty acid derivative molecule having a chemical formula according to: 
     
       
         
         
             
             
         
       
     
     wherein
         R1=-OH; —O 2 H; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3      R2=-H; —OH;   R3=-H; —OH;   R4=-H; —OH;   R5=-CH 3 ; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3 ;       

     wherein
         m=1-10 and n=0-9 and       

     wherein
         if R1 is OH or —O 2 H then 3&lt;m+n≤10; and if R1 is other than OH or —O 2 H, then 2&lt;m+n≤10, and       

     wherein
         the multifunctional molecule has at least three functional groups comprising a heteroatom, and       

     wherein
         at least two of R2, R3 and R4 are OH; or when R5 is other than CH 3 , CH 2  or C 3 H 7  CH 2 H 5  then at least one of R2, R3 and R4 are OH; and       

     wherein
         when R5=CH 3  and R4=H then n=0 or 1; and       

     wherein
         when R2=H, then R4 does not=H; and       

     wherein
         when R3=H, then n+m=p and p=3-10; unless R1=-OH or —O 2 H in which case when R3-H then n+m=p and p=4-10; and       

     wherein
         when the multifunctional molecule comprises a double bond that is not terminal, the double bond is in a position corresponding to an omega7 (co-7) position; and       

     wherein
         the multifunctional molecule is not 1,3,12-dodecane triol; is not 3,11-dihydroxy-tetradecanoic acid; is not 3,11-dihydroxy-tetradecanoic acid methyl ester and is not naturally occurring,
           the method comprising:
               culturing
                   a recombinant microbe that comprises a heterologous enzyme pathway capable of producing a bifunctional fatty acid derivative molecule, and at least one heterologous hydroxylating enzyme,   
                   in a culture medium comprising a simple carbon source,   
               
           wherein
           the heterologous enzyme pathway capable of producing bifunctional fatty acid derivative molecule is selected from:   a heterologous enzyme pathway capable of producing a 3-hydroxy fatty acid;   a heterologous enzyme pathway capable of producing a 3-hydroxy fatty ester;   a heterologous enzyme pathway capable of producing a 1,3-fatty diol   a heterologous enzyme pathway capable of producing a hydroxy fatty acid;   a heterologous enzyme pathway capable of producing a hydroxy fatty ester; and   a heterologous enzyme pathway capable of producing a fatty diol; and   
           wherein
           the at least one heterologous hydroxylating enzyme is selected from a heterologous hydroxylase enzyme and a heterologous hydratase enzyme or a combination thereof.   
               

     In one embodiment, the heterologous hydroxylase enzyme is a member selected from the group consisting of omega-hydroxylases (co-hydroxylases), mid-chain hydroxylases, and subterminal hydroxylases. In one embodiment, the heterologous enzyme pathway capable of producing bifunctional fatty acid derivative molecule is the heterologous enzyme pathway capable of producing a 1,3-fatty diol. In one embodiment, the heterologous enzyme pathway capable of producing a 1,3-fatty diol comprises; a heterologous thioesterase and a heterologous carboxylic acid reductase. In one embodiment, the heterologous the heterologous enzyme pathway capable of producing a 1,3-fatty diol further comprises; a heterologous alcohol dehydrogenase. In one embodiment, the heterologous the heterologous enzyme pathway capable of producing a 1,3-fatty diol further comprises: a heterologous PhaG thioesterase from  Pseudomonas putida , a heterologous CarB carboxylic acid reductase from  Mycobacterium smegmatis , and a heterologous AlrA alcohol dehydrogenase from  Acinetobacter baylyi . In one embodiment, the heterologous hydroxylase enzyme is a cyp102A subterminal-hydroxylase from  Bacillus licheniformis , and the method produces multifunctional molecules selected from the group consisting of 1,3,9 decanetriol, 1,3,8 decanetriol, 1,3,7 decanetriol, 1,3,11 dodecanetriol, 1,3,10 dodecanetriol, 1,3,9 dodecanetriol, (z5)1,3,11 dodecenetriol, (z5)1,3,10 dodecenetriol and (z5)1,3,9 dodecenetriol. 
     In one aspect the disclosure provides method for preparing a multifunctional fatty acid derivative molecule selected from the group consisting of 9,10,16-trihydroxyhexadecanoic acid and 9,10,18-trihydroxyoctadecanoic acid, the method comprising: culturing a recombinant microbe that expresses a heterologous biochemical pathway comprising: (i) a delta 12 fatty acid epoxygenase and an epoxide hydrolase, (ii) a heterologous FatA thioesterase and (iii) a cyp153A ω-hydroxylase from  Marinobacter aquaeolei  in a culture medium comprising a simple carbon source. 
     In one aspect the disclosure provides a method for preparing a multifunctional fatty acid derivative molecule selected from the group consisting of 9,10,16-trihydroxyhexadecanoic acid methyl ester and 9,10,18-trihydroxyoctadecanoic acid methyl ester, the method comprising: culturing a recombinant microbe that expresses a heterologous biochemical pathway comprising: (i) a delta 12 fatty acid epoxygenase and an epoxide hydrolase, (ii) a heterologous FatA thioesterase, (iii) an acyl-CoA synthetase, (iv) an ester synthase and (v) a cyp153A ω-hydroxylase from  Marinobacter aquaeolei  in a culture medium comprising a simple carbon source and methanol. 
     In one aspect the disclosure provides method for preparing a multifunctional fatty acid derivative molecule selected from the group consisting of 9,10,16-trihydroxyhexadecanoic acid ethyl ester and 9,10,18-trihydroxyoctadecanoic acid ethyl ester, the method comprising: culturing a recombinant microbe that expresses a heterologous biochemical pathway comprising: (i) a delta 12 fatty acid epoxygenase and an epoxide hydrolase, (ii) a heterologous FatA thioesterase, (iii) an acyl-CoA synthetase, (iv) a ester synthase and (v) a cyp153A ω-hydroxylase from  Marinobacter aquaeolei  in a culture medium comprising a simple carbon source and ethanol. 
     In one aspect the disclosure provides method for preparing a multifunctional fatty acid derivative molecule selected from the group consisting of 1, 9,10,16-hexadecanetetrol and 1, 9,10,18-octadecanetetrol, the method comprising: culturing a recombinant microbe that expresses a heterologous biochemical pathway comprising of (i) a delta 12 fatty acid epoxygenase and an epoxide hydrolase, (ii) a heterologous acyl-ACP reductase (AAR) and (iii) a cyp153A ω-hydroxylase from  Marinobacter aquaeolei  in a culture medium comprising a simple carbon source. 
     In one aspect the disclosure provides multifunctional fatty acid derivative molecule having a general formula according to: 
     
       
         
         
             
             
         
       
     
     wherein
         ω indicates the reduced end of the fatty acid derivative molecule and a indicates the carboxyl end of the fatty acid derivative molecule, and
 
wherein
   R1=-OH; —O 2 H; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3      R2=-H; —OH; —NH 2      R3=-H; —OH; —NH 2      R4=-H; —OH; —NH 2      R5=-CH 3 ; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3 ;       

     wherein
         m=1-10 and n=0-9 and wherein   if R1 is OH or —O 2 H then . . . 3&lt;m+n≤10; and if R1 is other than OH or —O 2 H, then 2&lt;m+n≤10, and       

     wherein
         the multifunctional molecule has at least three functional groups comprising a heteroatom, and       

     wherein
         when R5=CH 3  and R4=H then n=0 or 1; and       

     wherein
         when R2=CH 3 , then R4 does not=H; and       

     wherein
         when R3=H, then n+m=p and p=2-10; and       

     wherein
         when the multifunctional molecule comprises a double bond that is not terminal, the double bond is in a position corresponding to an omega7 (co-7) position; and       

     wherein
         the multifunctional molecule is not 1,3,12-dodecane triol; is not 3,11-dihydroxy-tetradecanoic acid; is not 3,11-dihydroxy-tetradecanoic acid methyl ester and is not naturally occurring.       

     In one embodiment, R2=NH 2 . In one embodiment, R1=CO 2 H. In one embodiment, the multifunctional molecule is selected from the group consisting of: 3-amino, 12-hydroxy-dodecanoic acid and 3-amino, 12-hydroxy-dodecenoic acid. In one embodiment, R1=CH 2 OH. In one embodiment, the multifunctional molecule is selected from the group consisting of: 3 amino dodecene 1,12 diol and 3-amino-dodecane 1,12-diol. In one embodiment, R5=CH 2 NH 2 . In one embodiment, the multifunctional molecule is selected from the group consisting of: 12-amino dodecane-1,3-diol, 12-amino dodecane-1,9-diol, (z5)12-amino dodecene-1,3-diol, (z5)12-amino dodecene-1,9-diol, 3-hydroxy, 12-amino dodecanoic acid and (z5)3-hydroxy, 12-amino dodecenoic acid. 
     In one aspect the disclosure provides a method for preparing a multifunctional molecule comprising an amino group, the method comprising: culturing a recombinant microbe that expresses a heterologous biochemical pathway comprising a heterologous thioesterase, and at least one heterologous hydroxylating enzyme, a heterologous alcohol dehydrogenase or oxidase and a heterologous transaminase, in a culture medium comprising a simple carbon source. In one embodiment, the thioeserase has enzyme activity according to EC3.1.2. In one embodiment, the thioeserase is selected from FatB1 from  Umbellularia californica  (Q41635) or PhaG from  Pseudomonas putida  (AAN67031). 
     In one aspect the disclosure provides a method for preparing 3-hydroxy, 12-amino dodecanoic acid, 3-amino, 12-hydroxy dodecanoic acid, (z5)3-hydroxy, 12-amino dodecenoic acid and (z5) 3-amino, 12-hydroxy dodecenoic acid, the method comprising: culturing, a recombinant microbe comprising a heterologous FatB1 thioesterase from  Umbellularia californica , an AlkJ alcohol oxidase from  Pseudomonas putida , a CV_2025 transaminase from  Chromobacterium violaceum  and a cyp153A ω-hydroxylase from  Marinobacter aquaeolei  on a simple carbon source. 
     In one aspect the disclosure provides a method for preparing 12-amino dodecane-1,3-diol, 3-amino dodecane-1,12-diol, 12-amino dodecane-1,9-diol, (z5) 12-amino dodecene-1,3-diol, (z5)3-amino dodecene-1,12-diol and (z5) 12-amino dodecene-1,9-diol, the method comprising: culturing, a recombinant microbe comprising a heterologous FatB1 thioesterase from  Umbellularia californica , an heterologous AlkJ alcohol oxidase from  Pseudomonas putida , a heterologous CV 2025 transaminase such as from  Chromobacterium violaceum , a heterologous CarB carboxylic acid reductase from  Mycobacterium smegmatis  and a heterologous cyp153A ω-hydroxylase from Mannobacier  aquaeolei  on a simple carbon source. 
    
    
     
       BRIEF DESCRIPTION OF THE FIGURES 
         FIG. 1  Illustrates some biochemical pathways that convert 3-hydroxy acyl-ACPs into trifunctional fatty acid derivatives. In particular,  FIG. 1A  Illustrates schematically production of a trifunctional fatty acid derivative from a 3-hydroxy fatty acid.  FIG. 1B  Illustrates schematically production of a trifunctional fatty acid derivative from a 3-hydroxy fatty ester. 
         FIG. 1C  Illustrates schematically production of a trifunctional fatty acid derivative from a 1,3-diol. Although  FIG. 1  depicts the enzymatic hydroxylations as the last steps of the biochemical pathway, they can occur at earlier steps of the pathways, e.g. in  FIG. 1C  the fatty acid intermediate may be hydroxylated before it is converted to a fatty alcohol by carboxylic acid reductase (CAR). 
         FIG. 2  Illustrates biochemical pathways that convert acyl-ACPs into trifunctional fatty acid derivatives. In particular,  FIG. 2A  Illustrates schematically production of a trifunctional fatty acid derivative from a fatty acid.  FIG. 2B  Illustrates schematically production of a trifunctional fatty acid derivative from a fatty ester.  FIG. 2C  Illustrates schematically production of a trifunctional fatty acid derivative from a fatty alcohol. Although  FIG. 2  depicts the enzymatic hydroxylations as the last steps of the biochemical pathway, they can occur at earlier steps of the pathways, e.g. in  FIG. 2C  the fatty acid intermediate may be hydroxylated before it is converted to a fatty alcohol by carboxylic acid reductase (CAR). 
         FIG. 3  Illustrates an exemplary biochemical pathway to produce fatty triols employing a ω-hydroxylase. Fatty acid derivatives with 12 carbon atoms are depicted. 
         FIG. 4  Illustrates an exemplary biochemical pathway to produce fatty triols employing a “subterminal”-hydroxylase. Fatty acid derivatives with 12 carbon atoms are depicted. 
         FIG. 5  Illustrates GC/MS chromatographs of extracts from recombinant  E. coli  strains.  FIG. 5A  Illustrates GC/MS chromatographs of extracts from recombinant  E. coli  without expression of a cyp153A ω-hydroxylase when fed with C12 diols.  FIG. 5B  Illustrates GC/MS chromatographs of extracts from recombinant  E. coli  with expression of a cyp153 A ω-hydroxylase when fed with C12 diols, which were efficiently converted to C12 triols. 
         FIG. 6A  and  FIG. 6B  Illustrates the mass spectrum and ion fragmentation pattern of (z5) 1,3,12-trimethylsilyloxy dodecene (peak at 12.33 minutes), which is derivatized (z5)1,3,12 dodecane triol. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp153 A ω-hydroxylase. 
         FIG. 7A  and  FIG. 7B  Illustrates the mass spectrum and ion fragmentation pattern of 1,3,12-trimethylsilyloxy dodecane (peak at 12.48 minutes), which is derivatized (z5)1,3,12 dodecane triol. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp153 A ω-hydroxylase 
         FIG. 8  Illustrates a GC/MS chromatograph of an extract from recombinant  E. coli  strains with expression of a cyp153A ω-hydroxylase when fed with 3-hydroxy dodecanoic acid, which was efficiently converted to 3,12-dihydroxy dodecanoic acid. 
         FIG. 9  Illustrates the mass spectrum and ion fragmentation pattern of 3,12-trimethylsilyloxy dodecanoic acid (peak at 13.25 minutes), which is derivatized 3,12-dihydroxy dodecanoic acid. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp153 A ω-hydroxylase. 
         FIG. 10A  and  FIG. 10B  Illustrates GC/MS chromatographs of extracts from recombinant  E. coli  strains without (A) and with (B) expression of a cyp102A “subterminal”-hydroxylase when fed with C12 diols, which were efficiently converted to various C12 triols 
         FIG. 11A  and  FIG. 11B  Illustrates the mass spectrum and ion fragmentation pattern of (z5) 1,3,9-trimethylsilyloxy dodecene (peak A in  FIG. 10 ), which is derivatized (z5)[3]9-dodecenetriol. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp102A “subterminal” hydroxylase 
         FIG. 12A  and  FIG. 12B  Illustrates the mass spectrum and ion fragmentation pattern of 1,3,9-trimethylsilyloxy dodecane (peakB in  FIG. 10 ), which is derivatized 1,3,9-dodecanetriol. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp102A “subterminal” hydroxylase 
         FIG. 13A  and  FIG. 13B  Illustrates the mass spectrum and ion fragmentation pattern of (z5) 1,3,10-trimethylsilyloxy dodecene (peak C in  FIG. 10 ), which is derivatized (z5) 1,3,10-dodecenetriol. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp102A “subterminal” hydroxylase 
         FIG. 14A  and  FIG. 14B  Illustrates the mass spectrum and ion fragmentation pattern of (Z5)1,3,11-trimethylsilyloxy dodecene (peak D in  FIG. 10 ), which is derivatized (z5) 1,3,11-dodecenetriol. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp102A “subterminal” hydroxylase 
         FIG. 15A  and  FIG. 15B  Illustrates the mass spectrum and ion fragmentation pattern of 1,3,10-trimethylsilyloxy dodecane (peak E in  FIG. 10 ), which is derivatized 1,3,10-dodecanetriol. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp102A “subterminal” hydroxylase 
         FIG. 16A  and  FIG. 16B  Illustrates the mass spectrum and ion fragmentation pattern of 1,3,11-trimethylsilyloxy dodecane (peak F in  FIG. 10 ), which is derivatized 1,3,11-dodecanetriol. The mass spectrum is from an extract of a recombinant  E. coli  strain expressing a cyp102A “subterminal” hydroxylase. 
         FIG. 17A  and  FIG. 17B  Illustrates peaks indicative of 10,16-dihydroxy hexadecanoic acid production in a recombinant  E. coli  strain grown on a simple carbon source. 
         FIG. 18A  and  FIG. 18B  Illustrates mass spectrum and ion fragmentation pattern of trimethylsilyl-10,16-dihydroxy hexadecanoic acid. 
         FIG. 19A  and  FIG. 19B  Illustrates mass spectrum and ion fragmentation pattern from trimethylsilyl derivatized 10,13 dihydroxy hexadecanoic acid. 
         FIG. 20A  and  FIG. 20B  Illustrates mass spectrum and ion fragmentation pattern of trimethyl silyl derivatized 10,14-dihydroxy hexadecanoic acid. 
         FIG. 21A  and  FIG. 21B  Illustrates mass spectrum and ion fragmentation pattern of trimethyl silyl derivatized 10,15-dihydroxy hexadecanoic acid. 
     
    
    
     DETAILED DESCRIPTION 
     Definitions 
     As used herein and in the appended claims, singular articles such as “a” and “an” and “the” and similar referents in the context of describing the elements are to be construed to cover both the singular and the plural, unless otherwise indicated herein or clearly contradicted by context. 
     As used herein, “about” is understood by persons of ordinary skill in the art and may vary to some extent depending upon the context in which it is used. If there are uses of the term which are not clear to persons of ordinary skill in the art given the context in which the term “about” is used, “about” will mean up to plus or minus 10% of the particular term. 
     As will be understood by one skilled in the art, for any and all purposes, all ranges disclosed herein also encompass any and all possible subranges and combinations of subranges thereof. Furthermore, as will be understood by one skilled in the art, a range includes each individual member. Thus, for example, a group having 1-3 atoms refers to groups having 1, 2, or 3 atoms. Similarly, a group having 1-5 atoms refers to groups having 1, 2, 3, 4, or 5 atoms, and so forth. 
     Unless defined otherwise, technical and scientific terms used herein have the same meaning as commonly understood by a person of ordinary skill in the art. In particular, this disclosure utilizes routine techniques in the field of recombinant genetics, organic chemistry, fermentation and biochemistry. Basic texts disclosing the general terms in molecular biology and genetics include e.g., Lackie,  Dictionary of Cell and Molecular Biology , Elsevier (5 th  ed. 2013). Basic texts disclosing methods in recombinant genetics and molecular biology include e.g., Sambrook et al., Molecular Cloning-A Laboratory Manual, Cold Spring Harbor Press 4 th  Edition (Cold Spring Harbor, N.Y. 2012) and Current Protocols in Molecular Biology Volumes 1-3, John Wiley &amp; Sons, Inc. (1994-1998) and Supplements 1-115 (1987-2016). Basic texts disclosing the general methods and terms in biochemistry include e.g.,  Lehninger Principles of Biochemistry  sixth edition, David L. Nelson and Michael M. Cox eds. W.H. Freeman (2012). Basic texts disclosing the general methods and terminology of fermentation include e.g.,  Principles of Fermentation Technology,  3rd Edition by Peter F Stanbury, Allan Whitaker and Stephen J Hall. Butterworth-Heinemann (2016). Basic texts disclosing the general methods and terms organic chemistry include e.g., Favre, Henri A. and Powell, Warren H.  Nomenclature of Organic Chemistry. IUPAC Recommendations and Preferred Name  2013. Cambridge, UK: The Royal Society of Chemistry, 2013 ; Practical Synthetic Organic Chemistry; Reactions, Principles, and Techniques , Stephane Caron ed., John Wiley and Sons Inc. (2011);  Organic Chemistry,  9th Edition—Francis Carey and Robert Giuliano, McGraw Hill (2013). 
     Those of skill in the art will appreciate that compounds of the present technology may exhibit the phenomena of tautomerism, conformational isomerism, geometric isomerism and/or stereoisomerism. As the formula drawings within the specification and claims can represent only one of the possible tautomeric, conformational isomeric, stereochemical or geometric isomeric forms, it should be understood that the present technology encompasses any tautomeric, conformational isomeric, stereochemical and/or geometric isomeric forms of the compounds having one or more of the utilities described herein, as well as a mixture of these various different forms. 
     “Tautomers” refers to isomeric forms of a compound that are in equilibrium with each other. The presence and concentrations of the isomeric forms will depend on the environment the compound is found in and may be different depending upon, for example, whether the compound is a solid or is in an organic or aqueous solution. For example, in aqueous solution, quinazolinones may exhibit the following isomeric forms, which are referred to as tautomers of each other: 
     
       
         
         
             
             
         
       
     
     As another example, guanidines may exhibit the following isomeric forms in protic organic solution, also referred to as tautomers of each other: 
     
       
         
         
             
             
         
       
     
     Because of the limits of representing compounds by structural formulas, it is to be understood that all chemical formulas of the compounds described herein represent all tautomeric forms of compounds and are within the scope of the present technology. 
     Stereoisomers of compounds (also known as optical isomers) include all chiral, diastereomeric, and racemic forms of a structure, unless the specific stereochemistry is expressly indicated. Thus, compounds used in the present technology include enriched or resolved optical isomers at any or all asymmetric atoms as are apparent from the depictions. Both racemic and diastereomeric mixtures, as well as the individual optical isomers can be isolated or synthesized so as to be substantially free of their enantiomeric or diastereomeric partners, and these stereoisomers are all within the scope of the present technology. 
     Geometric isomers can be represented by the symbol which denotes a bond that can be a single, double or triple bond as described herein. Provided herein are various geometric isomers and mixtures thereof resulting from the arrangement of substituents around a carbon-carbon double bond. Substituents around a carbon-carbon double bond are designated as being in the “Z” or “E” configuration wherein the terms “Z” and “E” are used in accordance with IUPAC standards. Unless otherwise specified, structures depicting double bonds encompass both the “E” and “Z” isomers. 
     Substituents around a carbon-carbon double bond alternatively can be referred to as “cis” or “trans,” where “cis” represents substituents on the same side of the double bond and “trans” represents substituents on opposite sides of the double bond. The term “cis” represents substituents on the same side of the plane of the ring, and the term “trans” represents substituents on opposite sides of the plane of the ring. Mixtures of compounds wherein the substituents are disposed on both the same and opposite sides of plane of the ring are designated “cis/trans.” 
     In certain embodiments, the pharmaceutically acceptable form thereof is an isomer. “Isomers” are different compounds that have the same molecular formula. “Stereoisomers” are isomers that differ only in the way the atoms are arranged in space. As used herein, the term “isomer” includes any and all geometric isomers and stereoisomers. For example, “isomers” include cis- and trans-isomers, E- and Z-isomers, R- and S-enantiomers, diastereomers, (d)-isomers, (l)-isomers, racemic mixtures thereof, and other mixtures thereof, as falling within the scope of this disclosure. 
     “Enantiomers” are a pair of stereoisomers that are non-superimposable mirror images of each other. A mixture of a pair of enantiomers in any proportion can be known as a “racemic” mixture. The term “(+−)” is used to designate a racemic mixture where appropriate. “Diastereoisomers” are stereoisomers that have at least two asymmetric atoms, but which are not mirror-images of each other. The absolute stereochemistry is specified according to the Cahn-Ingold-Prelog R-S system. When a compound is a pure enantiomer, the stereochemistry at each chiral carbon can be specified by either R or S. Resolved compounds whose absolute configuration is unknown can be designated (+) or (−) depending on the direction (dextro- or levorotatory) which they rotate plane polarized light at the wavelength of the sodium D line. Certain of the compounds described herein contain one or more asymmetric centers and can thus give rise to enantiomers, diastereomers, and other stereoisomeric forms that can be defined, in terms of absolute stereochemistry, as (R)- or (S)-. The present chemical entities, pharmaceutical compositions and methods are meant to include all such possible isomers, including racemic mixtures, optically pure forms and intermediate mixtures. Optically active (R)- and (S)-isomers can be prepared, for example, using chiral synthons or chiral reagents, or resolved using conventional techniques. The optical activity of a compound can be analyzed via any suitable method, including but not limited to chiral chromatography and polarimetry, and the degree of predominance of one stereoisomer over the other isomer can be determined. 
     The term “fatty acid” as used herein, refers to an aliphatic carboxylic acid having the formula RCOOH wherein R is an aliphatic group having at least 4 carbons, typically between about 4 and about 28 carbon atoms. The aliphatic R group can be saturated or unsaturated, branched or unbranched. Unsaturated “fatty acids” may be monounsaturated or polyunsaturated. 
     A “fatty acid” or “fatty acids”, as used herein, can be produced within a cell through the process of fatty acid biosynthesis, through the reverse of fatty acid degradation or beta-oxidation, or they can be fed to a cell. As is well known in the art, fatty acid biosynthesis is generally a malonyl-CoA dependent synthesis of acyl-ACPs or acyl CoAs, while the reverse of beta-oxidation results is acetyl-CoA dependent and results in the synthesis of acyl-CoAs. Fatty acids fed to cell are converted to acyl-CoAs and can be converted to acyl-ACPs. Fatty acids can be synthesized in a cell by natural fatty acid biosynthetic pathways or can be synthesized from heterologous fatty acid biosynthetic pathways that comprise a combination of fatty acid biosynthetic and/or degradation enzymes that result in the synthesis of acyl-CoAs and/or Acyl-ACPs. 
     Fatty acid biosynthesis and degradation occur in all life forms, including prokaryotes, single cell eukaryotes, higher eukaryotes, and Archaea. The tools and methods disclosed herein are useful in the production of fatty acid derivatives that are derived through any one or more of fatty acid synthesis, degradation, or feeding in any organism that naturally produces alkyl thioesters. 
     The term “fatty acid derivative” as used herein, refers to a product derived from a fatty acid. Thus, a “fatty acid derivative” includes “fatty acids” as defined above. In general, “fatty acid derivatives” include malonyl-CoA derived compounds including acyl-ACP or acyl-ACP derivatives. “Fatty acid derivatives” also include malonyl-CoA derived compounds such as acyl-CoA or acyl-CoA derivatives. Thus, a “fatty acid derivatives” include alky-thioesters and acyl-thioesters. Further, a “fatty acid derivative” includes a molecule/compound that is derived from a metabolic pathway that includes a fatty acid derivative enzyme. Exemplary fatty acid derivatives include fatty acids, fatty acid esters (e.g., waxes, fatty acid esters, fatty acid methyl esters (FAME), fatty acid ethyl esters (FAEE)), fatty alcohol acetate esters (FACE), fatty amines, fatty aldehydes, fatty alcohols, hydrocarbons e.g., alkanes, alkenes, etc, ketones, terminal olefins, internal olefins, 3-hydroxy fatty acid derivatives, bifunctional fatty acid derivatives (e.g., ?-hydroxy fatty acids, 1,3 fatty-diols, ?-diols, -3-hydroxy triols, ?-hydroxy FAME, ?-OH FAEE, etc.), and unsaturated fatty acid derivatives, including unsaturated compounds of each of the above mentioned fatty acid derivatives. Fatty acid derivatives also include multifunctional fatty acid derivatives, as defined below. 
     The term “multifunctional fatty acid derivatives” or equivalently “multifunctional molecules” as used herein, refers to fatty acid derivative molecules having a carbon chain length of between 8 and 16 carbons that have at least three functional groups which comprise a heteroatom. Exemplary functional groups which comprise a heteroatom include e.g. a hydroxy or equivalently, hydroxyl (—OH), oxo ( ), carboxyl (CO2H), amino (NH2), O-acetyl (CO2C2H 3 ), methoxy (OCH3) or ester (CO2CH3, CO2C2H5, CO2C3H7, CO2C2H3) group. 
     “Multifunctional fatty acid derivatives” disclosed herein may be saturated or unsaturated multifunctional fatty acid derivatives. Typically, unsaturated “multifunctional fatty acid derivatives” or “multifunctional molecules” that are not exclusively terminal olefins have a double bond located at the omega-7 (-7) position on the hydrocarbon chain. That is to say, the double bond is located between the seventh and eighth carbons from the reduced end of the fatty acid from which the multifunctional fatty acid derivative is derived. For example, (9E)-1,3,16-trihydroxy-hexadecene has a 16-hydroxyl group that is added by a hydroxylase to the reducing end of (9E)-1,3 dihydroxy hexadecane, a fatty diol unsaturated at the omega-7 position. 
     The expression “fatty acid derivative composition” as used herein, refers to a composition of fatty acid derivatives, for example a fatty acid composition produced by an organism. A “fatty acid derivative composition” may comprise a single fatty acid derivative species or may comprise a mixture of fatty acid derivative species. In some exemplary embodiments, the mixture of fatty acid derivatives includes more than one type of fatty acid derivative product (e.g., fatty acids, fatty acid esters, fatty alcohols, fatty alcohol acetates, fatty aldehydes, fatty amine, bifunctional fatty acid derivatives, and multifunctional fatty acid derivatives, etc.). In other exemplary embodiments, the mixture of fatty acid derivatives includes a mixture of fatty acid esters (or another fatty acid derivative) with different chain lengths, saturation and/or branching characteristics. In other exemplary embodiments, the mixture of fatty acid derivatives comprises predominantly one type of fatty acid derivative e.g., a multifunctional fatty acid derivative composition. In still other exemplary embodiments, the mixture of fatty acid derivatives comprises a mixture of more than one type of fatty acid derivative product e.g., fatty acid derivatives with different chain lengths, saturation and/or branching characteristics. In still other exemplary embodiments, the mixture of fatty acid derivatives comprises a mixture of fatty esters and 3-hydroxy esters. In still other exemplary embodiments, a fatty acid derivative composition comprises a mixture of fatty alcohols and fatty aldehydes, in particular a mixture of multifunctional fatty alcohols or fatty aldehydes. In still other exemplary embodiments, a fatty acid derivative composition comprises a mixture of FAME and/or FAEE, in particular a mixture of multifunctional FAME and/or FAEE. In still other exemplary embodiments, a fatty acid derivative composition comprises a mixture of fatty alcohol acetate esters (FACE), in particular a mixture of multifunctional fatty alcohol acetate esters (FACE). In other exemplary embodiments, the mixture of fatty acid derivatives includes a mixture of multifunctional fatty acid derivatives with different chain lengths, saturation and/or functional group characteristics. In other exemplary embodiments, the mixture of fatty acid derivatives comprises predominantly one type of fatty acid derivative e.g., a multifunctional fatty acid derivative composition comprising predominantly 1,3,12-dodecane triol. 
     The term “malonyl-CoA derived compound” as used herein refers to any compound or chemical entity (i.e., intermediate or end product) that is made via a biochemical pathway wherein malonyl-CoA functions as intermediate and/or is made upstream of the compound or chemical entity. For example, a malonyl-CoA derived compound may include, but is not limited to, a fatty acid derivative such as, for example, a fatty acid; a fatty ester including, but not limited to a fatty acid methyl ester (FAME) and/or a fatty acid ethyl ester (FAEE); a fatty alcohol; a fatty aldehyde; a fatty amine; an alkane; an olefin or alkene; a hydrocarbon; a beta hydroxy fatty acid derivative, a bifunctional fatty acid derivative, a multifunctional fatty acid derivative and/or an unsaturated fatty acid derivative. 
     As used herein “alkyl-thioester” or equivalently an “acyl thioester” is a compound in which the carbonyl carbon of an acyl chain and the sulfydryl group of an organic thiol forms a thioester bond. Representative organic thiols include Cystein, beta-cysteine, glutathione, mycothiol, pantetheine, Coenzyme A (CoA) and the acyl carrier protein (ACP). Thus “acyl-ACP” refers to an alkyl thioester formed between the carbonyl carbon of an acyl chain and the sulfhydryl group of the phosphopantetheinyl moiety of an ACP. An “Acyl-CoA” refers to an alkyl thioester formed between the carbonyl carbon of an acyl chain and the sulfhydryl group of the phosphopantetheinyl moiety of CoA. In some exemplary embodiments an alkyl thioester, such as acyl-ACP or acyl CoA, is an intermediate in the synthesis of fully saturated acyl-thioesters. In other exemplary embodiments an alkyl thioester, such as acyl-ACP or acyl CoA, is an intermediate in the synthesis of unsaturated acyl thioesters. In some exemplary embodiments, the carbon chain of the acyl group of an acyl thiester has 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or 28 carbons. In other exemplary embodiments, the carbon chain of the acyl group of acyl-thioester is a medium-chain and has 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 16 carbons. In other exemplary embodiments the carbon chain of the acyl group of acyl-thioester is 10 carbons in length. In still other exemplary embodiments, the carbon chain of the acyl group of acyl-thioester is 12 carbons in length. In still other exemplary embodiments, the carbon chain of the acyl group of acyl-thioester is 14 carbons in length. In still other exemplary embodiments, the carbon chain of the acyl group of acyl-thioester is 16 carbons in length. Each of these acyl-thioesters are substrates for fatty acid derivative enzymes such as e.g., thioesterases, acyl ACP reductases, ester synthases and their engineered variants that convert the acyl-thioester to fatty acid derivatives. 
     As used herein, the expression “fatty acid derivative biosynthetic pathway” refers to a biochemical pathway that produces fatty acid derivatives. The enzymes that comprise a “fatty acid derivative biosynthetic pathway” are thus referred to herein as “fatty acid derivative biosynthetic polypeptides” or equivalently “fatty acid derivative enzymes”. As discussed supra, the term “fatty acid derivative,” includes a molecule/compound derived from a biochemical pathway that includes a fatty acid derivative enzyme. Thus, a thioesterase enzyme (e.g., an enzyme having thioesterase activity EC 3.1.1.14) is a “fatty acid derivative biosynthetic peptide” or equivalently a “fatty acid derivative enzyme.” In addition to a thioesterase, a fatty acid derivative biosynthetic pathway may include additional fatty acid derivative enzymes to produce fatty acid derivatives having desired characteristics. Thus the term “fatty acid derivative enzymes” or equivalently “fatty acid derivative biosynthetic polypeptides” refers to, collectively and individually, enzymes that may be expressed or overexpressed to produce fatty acid derivatives. Non-limiting examples of “fatty acid derivative enzymes” or equivalently “fatty acid derivative biosynthetic polypeptides” include e.g., fatty acid synthetases, thioesterases, acyl-CoA synthetases, acyl-CoA reductases, acyl ACP reductases, alcohol dehydrogenases, alcohol O-acyltransferases, fatty alcohol-forming acyl-CoA reductases, fatty acid decarboxylases, fatty aldehyde decarbonylases and/or oxidative deformylases, carboxylic acid reductases, fatty alcohol O-acetyl transferases, ester synthases, etc. “Fatty acid derivative enzymes” or equivalently “fatty acid derivative biosynthetic polypeptides” convert substrates into fatty acid derivatives. In exemplary embodiments, a suitable substrate for a fatty acid derivative enzyme may be a first fatty acid derivative, which is converted by the fatty acid derivative enzyme into a different, second fatty acid derivative. 
     The term “polyol” as used herein, refers to compounds, typically fatty alcohols, which have more than one hydroxy group. Thus, as referred to herein, a polyol may have two hydroxy groups, three hydroxy groups, four hydroxy groups, etc. In general, a “polyol” that has two hydroxy groups is referred to herein as a “diol”, a “polyol” that has three hydroxy groups is referred to herein as a “triol”, a “polyol” that has four hydroxy groups is referred to herein as a “tetrol” and so on. 
     The expression “hydroxy group”, “hydroxyl group”, “alcohol group” are used interchangeably herein and refer to a chemical functional group containing one oxygen atom covalently bonded to one hydrogen atom (—OH). 
     Sequence Accession numbers throughout this description were obtained from databases provided by the NCBI (National Center for Biotechnology Information) maintained by the National Institutes of Health, U.S.A. (which are identified herein as “NCBI Accession Numbers” or alternatively as “GenBank Accession Numbers” or alternatively a simply “Accession Numbers”), and from the UniProt Knowledgebase (UniProtKB) and Swiss-Prot databases provided by the Swiss Institute of Bioinformatics (which are identified herein as “UniProtKB Accession Numbers”). 
     The term “enzyme classification (EC) number” refers to a number that denotes a specific polypeptide sequence or enzyme. EC numbers classify enzymes according to the reaction they catalyze. EC numbers are established by the nomenclature committee of the international union of biochemistry and molecular biology (IUBMB), a description of which is available on the IUBMB enzyme nomenclature website on the world wide web. 
     As used herein, the term “isolated,” with respect to products (such as multifunctional fatty acid derivatives disclosed herein) refers to products that are separated from cellular components, cell culture media, or chemical or synthetic precursors. The multifunctional fatty acid derivatives disclosed herein produced by the methods disclosed herein can be relatively immiscible in the fermentation broth, as well as in the cytoplasm. Therefore, in exemplary embodiments, the multifunctional fatty acid derivatives disclosed herein collect in an organic phase extracellularly and are thereby “isolated”. 
     As used herein, the terms “polypeptide” and “protein” are used interchangeably to refer to a polymer of amino acid residues that is typically 12 or more amino acids in length. Polypeptides less than 12 amino acids in length are referred to herein as “peptides”. The terms apply to amino acid polymers in which one or more amino acid residue is an artificial chemical mimetic of a corresponding naturally occurring amino acid, as well as to naturally occurring amino acid polymers and non-naturally occurring amino acid polymers. The term “recombinant polypeptide” refers to a polypeptide that is produced by recombinant techniques, wherein generally DNA or RNA encoding the expressed protein is inserted into a suitable expression vector that is in turn used to transform a host cell to produce the polypeptide. In some exemplary embodiments, DNA or RNA encoding an expressed peptide, polypeptide or protein is inserted into the host chromosome via homologous recombination or other means well known in the art, and is so used to transform a host cell to produce the peptide or polypeptide. Similarly, the terms “recombinant polynucleotide” or “recombinant nucleic acid” or “recombinant DNA” are produced by recombinant techniques that are known to those of skill in the art (see e.g., methods described in Sambrook et al. (supra) and/or Current Protocols in Molecular Biology (supra). 
     When referring to two nucleotide or polypeptide sequences, the “percentage of sequence identity” between the two sequences is determined by comparing the two optimally aligned sequences over a comparison window, wherein the portion of the polynucleotide sequence in the comparison window may comprise additions or deletions (i.e., gaps) as compared to the reference sequence (which does not comprise additions or deletions) for optimal alignment of the two sequences. The “percentage of sequence identity” is calculated by determining the number of positions at which the identical nucleic acid base or amino acid residue occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison and multiplying the result by 100 to yield the percentage of sequence identity. 
     Thus, the expression “percent identity,” or equivalently “percent sequence identity” in the context of two or more nucleic acid sequences or peptides or polypeptides, refers to two or more sequences or subsequences that are the same or have a specified percentage of nucleotides or amino acids that are the same (e.g., about 50% identity, preferably 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or higher identity over a specified region, when compared and aligned for maximum correspondence over a comparison window or designated region) as measured e.g., using a BLAST or BLAST 2.0 sequence comparison algorithm with default parameters (see e.g., Altschul et al. (1990)  J. Mol. Biol.  215(3):403-410) and/or the NCBI web site at ncbi.nlm.nih.gov/BLAST/) or by manual alignment and visual inspection. Percent sequence identity between two nucleic acid or amino acid sequences also can be determined using e.g., the Needleman and Wunsch algorithm that has been incorporated into the GAP program in the GCG software package, using either a Blossum 62 matrix or a PAM250 matrix, and a gap weight of 16, 14, 12, 10, 8, 6, or 4 and a length weight of 1, 2, 3, 4, 5, or 6 (Needleman and Wunsch (1970)  J. Mol. Biol.  48:444-453). The percent sequence identity between two nucleotide sequences also can be determined using the GAP program in the GCG software package, using a NWSgapdna.CMP matrix and a gap weight of 40, 50, 60, 70, or 80 and a length weight of 1, 2, 3, 4, 5, or 6. One of ordinary skill in the art can perform initial sequence identity calculations and adjust the algorithm parameters accordingly. A set of parameters that may be used if a practitioner is uncertain about which parameters should be applied to determine if a molecule is within a homology limitation of the claims, are a Blossum 62 scoring matrix with a gap penalty of 12, a gap extend penalty of 4, and a frameshift gap penalty of 5. Additional methods of sequence alignment are known in the biotechnology arts (see, e.g., Rosenberg (2005)  BMC Bioinformatics  6:278; Altschul et al. (2005)  FEBS J.  272(20):5101-5109). 
     Two or more nucleic acid or amino acid sequences are said to be “substantially identical,” when they are aligned and analyzed as discussed above and are found to share about 50% identity, preferably 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or higher identity over a specified region. Two nucleic acid sequences or polypeptide sequences are said to be “identical” if the sequence of nucleotides or amino acid residues, respectively, in the two sequences are the same when aligned for maximum correspondence as described above. This definition also refers to, or may be applied to, the compliment of a test sequence. Identity is typically calculated over a region that is at least about 25 amino acids or nucleotides in length, or more preferably over a region that is 50-100 amino acids or nucleotides in length, or over the entire length of a given sequence. 
     The expressions “hybridizes under low stringency, medium stringency, high stringency, or very high stringency conditions” describes conditions for hybridization and washing. Guidance for performing hybridization reactions can be found e.g., in Current Protocols in Molecular Biology, John Wiley &amp; Sons, N.Y. (1989), 6.3.1-6.3.6. Aqueous and non-aqueous methods are described in the cited reference and either method can be used. Specific hybridization conditions referred to herein are as follows: (1) low stringency hybridization conditions—6× sodium chloride/sodium citrate (SSC) at about 45° C., followed by two washes in 0.2×SSC, 0.1% SDS at least at 50° C. (the temperature of the washes can be increased to 55° C. for low stringency conditions); (2) medium stringency hybridization conditions—6×SSC at about 45° C., followed by one or more washes in 0.2×SSC, 0.1% SDS at 60° C.; (3) high stringency hybridization conditions—6×SSC at about 45° C., followed by one or more washes in 0.2.×SSC, 0.1% SDS at 65° C.; and (4) very high stringency hybridization conditions—0.5M sodium phosphate, 7% SDS at 65° C., followed by one or more washes at 0.2×SSC, 1% SDS at 65° C. Very high stringency conditions (4) are the preferred conditions unless otherwise specified. 
     The term “endogenous” as used herein refers to a substance e.g., a nucleic acid, protein, etc. that is produced from within a cell. Thus, an “endogenous” polynucleotide or polypeptide refers to a polynucleotide or polypeptide produced by the cell. In some exemplary embodiments an “endogenous” polypeptide or polynucleotide is encoded by the genome of the parental cell (or host cell). In other exemplary embodiments, an “endogenous” polypeptide or polynucleotide is encoded by an autonomously replicating plasmid carried by the parental cell (or host cell). In some exemplary embodiments, an “endogenous” gene is a gene that was present in the cell when the cell was originally isolated from nature i.e., the gene is “native to the cell”. In other exemplary embodiments, an “endogenous” gene has been altered through recombinant techniques e.g., by altering the relationship of control and coding sequences. Thus, a “heterologous” gene may, in some exemplary embodiments, be “endogenous” to a host cell. 
     The term “endogenous” as used herein refers to a substance e.g., a nucleic acid, protein, etc. that is produced from within a cell. Thus, an “endogenous” polynucleotide or polypeptide refers to a polynucleotide or polypeptide produced by the cell. In some exemplary embodiments an “endogenous” polypeptide or polynucleotide is encoded by the genome of the parental cell (or host cell). In other exemplary embodiments, an “endogenous” polypeptide or polynucleotide is encoded by an autonomously replicating plasmid carried by the parental cell (or host cell). In some exemplary embodiments, an “endogenous” gene is a gene that was present in the cell when the cell was originally isolated from nature i.e., the gene is “native to the cell”. In other exemplary embodiments, an “endogenous” gene has been altered through recombinant techniques e.g., by altering the relationship of control and coding sequences. Thus, a “heterologous” gene may, in some exemplary embodiments, be “endogenous” to a host cell. 
     In contrast, an “exogenous” polynucleotide or polypeptide, or other substance (e.g., fatty acid derivative, small molecule compound, etc.) refers to a polynucleotide or polypeptide or other substance that is not produced by the parental cell and which is therefore added to a cell, a cell culture or assay from outside of the cell. 
     As used herein the term “native” refers to the form of a nucleic acid, protein, polypeptide or a fragment thereof that is isolated from nature or a nucleic acid, protein, polypeptide or a fragment thereof that is without intentionally introduced mutations. 
     As used herein, the term “fragment” of a polypeptide refers to a shorter portion of a full-length polypeptide or protein ranging in size from two amino acid residues to the entire amino acid sequence minus one amino acid residue. In certain embodiments of the disclosure, a fragment refers to the entire amino acid sequence of a domain of a polypeptide or protein (e.g., a substrate binding domain or a catalytic domain). 
     The term “gene” as used herein, refers to nucleic acid sequences e.g., DNA sequences, which encode either an RNA product or a protein product, as well as operably-linked nucleic acid sequences that affect expression of the RNA or protein product (e.g., expression control sequences such as e.g., promoters, enhancers, ribosome binding sites, translational control sequences, etc). The term “gene product” refers to either the RNA e.g., tRNA, mRNA and/or protein expressed from a particular gene. 
     The term “expression” or “expressed” as used herein in reference to a gene, refers to the production of one or more transcriptional and/or translational product(s) of a gene. In exemplary embodiments, the level of expression of a DNA molecule in a cell is determined on the basis of either the amount of corresponding mRNA that is present within the cell or the amount of protein encoded by that DNA produced by the cell. The term “expressed genes” refers to genes that are transcribed into messenger RNA (mRNA) and then translated into protein, as well as genes that are transcribed into other types of RNA, such as e.g., transfer RNA (tRNA), ribosomal RNA (rRNA), and regulatory RNA, which are not translated into protein. 
     The level of expression of a nucleic acid molecule in a cell or cell free system is influenced by “expression control sequences” or equivalently “regulatory sequences”. “Expression control sequences” or “regulatory sequences” are known in the art and include, for example, promoters, enhancers, polyadenylation signals, transcription terminators, nucleotide sequences that affect RNA stability, internal ribosome entry sites (IRES), and the like, that provide for the expression of the polynucleotide sequence in a host cell. In exemplary embodiments, “expression control sequences” interact specifically with cellular proteins involved in transcription (see e.g., Maniatis et al., Science, 236: 1237-1245 (1987); Goeddel, Gene Expression Technology: Methods in Enzymology, Vol. 185, Academic Press, San Diego, Calif. (1990)). In exemplary methods, an expression control sequence is operably linked to a polynucleotide sequence. By “operably linked” is meant that a polynucleotide sequence and an expression control sequence(s) are functionally connected so as to permit expression of the polynucleotide sequence when the appropriate molecules (e.g., transcriptional activator proteins) contact the expression control sequence(s). In exemplary embodiments, operably linked promoters are located upstream of the selected polynucleotide sequence in terms of the direction of transcription and translation. In some exemplary embodiments, operably linked enhancers can be located upstream, within, or downstream of the selected polynucleotide. 
     As used herein, the phrase “the expression of said nucleotide sequence is modified relative to the wild type nucleotide sequence”, refers to a change e.g., an increase or decrease in the level of expression of an native nucleotide sequence or a change e.g., an increase or decrease in the level of the expression of a heterologous or non-native polypeptide-encoding nucleotide sequence as compared to a control nucleotide sequence e.g., wild-type control. In some exemplary embodiments, the phrase “the expression of said nucleotide sequence is modified relative to the wild type nucleotide sequence,” refers to a change in the pattern of expression of a nucleotide sequence as compared to a control pattern of expression e.g., constitutive expression as compared to developmentally timed expression. 
     The term “overexpressed” as used herein, refers to a gene whose expression is elevated in comparison to a “control” level of expression. In exemplary embodiments, “overexpression” of a gene is caused by an elevated rate of transcription as compared to the native transcription rate for that gene. In other exemplary embodiments, overexpression is caused by an elevated rate of translation of the gene compared to the native translation rate for that gene. Methods of testing for overexpression are well known in the art, for example transcribed RNA levels can be assessed using rtPCR and protein levels can be assessed using SDS page gel analysis. 
     In other embodiments, the polypeptide, polynucleotide, or hydrocarbon having an altered level of expression is “attenuated” or has a “decreased level of expression.” As used herein, “attenuate” and “decreasing the level of expression” mean to express or cause to be expressed a polynucleotide, polypeptide, or hydrocarbon in a cell at a lesser concentration than is normally expressed in a corresponding control cell (e.g., wild type cell) under the same conditions. 
     A polynucleotide or polypeptide can be attenuated using any method known in the art. For example, in some exemplary embodiments, the expression of a gene or polypeptide encoded by the gene is attenuated by mutating the regulatory polynucleotide sequences which control expression of the gene. In other exemplary embodiments, the expression of a gene or polypeptide encoded by the gene is attenuated by overexpressing a repressor protein, or by providing an exogenous regulatory element that activates a repressor protein. In still other exemplary embodiments, DNA- or RNA-based gene silencing methods are used to attenuate the expression of a gene or polynucleotide. In some embodiments, the expression of a gene or polypeptide is completely attenuated, e.g., by deleting all or a portion of the polynucleotide sequence of a gene. 
     The degree of overexpression or attenuation can be 1.5-fold or more, e.g., 2-fold or more, 3-fold or more, 5-fold or more, 10-fold or more, or 15-fold or more. Alternatively, or in addition, the degree of overexpression or attenuation can be 500-fold or less, e.g., 100-fold or less, 50-fold or less, 25-fold or less, or 20-fold or less. Thus, the degree of overexpression or attenuation can be bounded by any two of the above endpoints. For example, the degree of overexpression or attenuation can be 1.5-500-fold, 2-50-fold, 10-25-fold, or 15-20-fold. 
     As used herein, “modified activity” or an “altered level of activity” of a protein/polypeptide e.g., of a variant ChFatB2 enzyme, in a recombinant host cell refers to a difference in one or more characteristics in the activity the protein/polypeptide as compared to the characteristics of an appropriate control protein e.g., the corresponding parent protein or corresponding wild type protein. Thus, in exemplary embodiments, a difference in activity of a protein having “modified activity” as compared to a corresponding control protein is determined by measuring the activity of the modified protein in a recombinant host cell and comparing that to a measure of the same activity of a corresponding control protein in an otherwise isogenic host cell. Modified activities can be the result of, for example, changes in the structure of the protein (e.g., changes to the primary structure, such as e.g., changes to the protein&#39;s nucleotide coding sequence that result in changes in substrate specificity, changes in observed kinetic parameters, changes in solubility, etc.); changes in protein stability (e.g., increased or decreased degradation of the protein) etc. In some exemplary embodiments, a polypeptide having “modified activity” is a mutant or a variant ChFatB2 thioesterase disclosed herein. 
     The term “recombinant” as used herein, refers to a genetically modified polynucleotide, polypeptide, cell, tissue, or organism. When used with reference to a cell, the term “recombinant” indicates that the cell has been modified by the introduction of a heterologous nucleic acid or protein or has been modified by alteration of a native nucleic acid or protein, or that the cell is derived from a cell so modified and that the derived cell comprises the modification. Thus, for example, “recombinant cells” or equivalently “recombinant host cells” may be modified to express genes that are not found within the native (non-recombinant) form of the cell or may be modified to abnormally express native genes e.g., native genes may be overexpressed, underexpressed or not expressed at all. In exemplary embodiments, a “recombinant cell” or “recombinant host cell” is engineered to express a heterologous enzyme pathway capable of producing a bifunctional fatty acid derivative molecule. A recombinant cell can be derived from a microorganism such as a bacterium, a virus or a fungus. In addition, a recombinant cell can be derived from a plant or an animal cell. In exemplary embodiments, a “recombinant host cell” or “recombinant cell” is used to produce one or more multifunctional fatty acid derivatives including, but not limited to, multifunctional fatty acids, multifunctional fatty esters (e.g., waxes, fatty acid esters, fatty esters, fatty acid methyl esters (FAME), fatty acid ethyl esters (FAEE)), multifunctional fatty acyl acetate esters (FAce), multifunctional fatty alcohols (e.g., polyols), multifunctional fatty aldehydes, multifunctional fatty amines, multifunctional terminal olefins, multifunctional ketones, etc. Therefore, in some exemplary embodiments a “recombinant host cell” is a “production host” or equivalently, a “production host cell”. In some exemplary embodiments, the recombinant cell includes one or more polynucleotides, each polynucleotide encoding a polypeptide having fatty acid biosynthetic enzyme activity, wherein the recombinant cell produces a multifunctional fatty acid derivative composition when cultured in the presence of a carbon source under conditions effective to express the polynucleotides. 
     When used with reference to a polynucleotide, the term “recombinant” indicates that the polynucleotide has been modified by comparison to the native or naturally occurring form of the polynucleotide or has been modified by comparison to a naturally occurring variant of the polynucleotide. In an exemplary embodiment, a recombinant polynucleotide (or a copy or complement of a recombinant polynucleotide) is one that has been manipulated by the hand of man to be different from its naturally occurring form. Thus, in an exemplary embodiment, a recombinant polynucleotide is a mutant form of a native gene or a mutant form of a naturally occurring variant of a native gene wherein the mutation is made by intentional human manipulation e.g., made by saturation mutagenesis using mutagenic oligonucleotides, through the use of UV radiation, mutagenic chemicals, chemical synthesis etc. Such a recombinant polynucleotide might comprise one or more point mutations, deletions and/or insertions relative to the native or naturally occurring variant form of the gene. Similarly, a polynucleotide comprising a promoter operably linked to a second polynucleotide (e.g., a coding sequence) is a “recombinant” polynucleotide. Thus, a recombinant polynucleotide comprises polynucleotide combinations that are not found in nature. A recombinant protein (discussed supra) is typically one that is expressed from a recombinant polynucleotide, and recombinant cells, tissues, and organisms are those that comprise recombinant sequences (polynucleotide and/or polypeptide). 
     As used herein, the term “microorganism” refers generally to a microscopic organism. Microorganisms can be prokaryotic or eukaryotic. Exemplary prokaryotic microorganisms include e.g., bacteria, archaea, cyanobacteria, etc. An exemplary bacterium is  Escherichia coli . Exemplary eukaryotic microorganisms include e.g., yeast, protozoa, algae, etc. In exemplary embodiments, a “recombinant microorganism” is a microorganism that has been genetically altered and thereby expresses or encompasses a heterologous nucleic acid sequence and/or a heterologous protein. 
     A “production host” or equivalently a “production host cell” is a cell used to produce products. As disclosed herein, a “production host” is typically modified to express or overexpress selected genes, or to have attenuated expression of selected genes. Thus, a “production host” or a “production host cell” is a “recombinant host” or equivalently a “recombinant host cell”. Non-limiting examples of production hosts include plant, animal, human, bacteria, yeast, cyanobacteria, algae, and/or filamentous fungi cells. An exemplary “production host” is a recombinant  Escherichia coli  cell. 
     The term “acetyl-CoA derived compound” refers to any compound or chemical entity (i.e., intermediate or end product) that is made via a biochemical pathway wherein acetyl-CoA functions as intermediate and/or is made upstream of the compound or chemical entity. For example, a acetyl-CoA derived compound may include, but is not limited to, a fatty acid derivative such as, for example, a fatty acid; a fatty ester including, but not limited to a fatty acid methyl ester (FAME) and/or a fatty acid ethyl ester (FAEE); a fatty alcohol; a fatty aldehyde; a fatty amine; an alkane; an olefin or alkene; a hydrocarbon; a 3-hydroxy fatty acid derivative, a bifunctional fatty acid derivative, a multifunctional fatty acid derivative, an unsaturated fatty acid derivative, etc. 
     As used herein, the terms “purify,” “purified,” or “purification” mean the removal or isolation of a molecule from its environment by, for example, isolation or separation. “Substantially purified” molecules are at least about 60% free (e.g., at least about 65% free, at least about 70% free, at least about 75% free, at least about 80% free, at least about 85% free, at least about 90% free, at least about 95% free, at least about 96% free, at least about 97% free, at least about 98% free, at least about 99% free) from other components with which they are associated. As used herein, these terms also refer to the removal of contaminants from a sample. For example, the removal of contaminants can result in an increase in the percentage of malonyl-CoA derived compounds including multifunctional fatty acid derivatives or other compounds in a sample. For example, when a malonyl-CoA derived compound including a multifunctional fatty acid derivative or other compound is produced in a recombinant host cell, the malonyl-CoA derived compound including the multifunctional fatty acid derivative or other compound can be purified by the removal of host cell proteins. After purification, the percentage of malonyl-CoA derived compounds including multifunctional fatty acid derivatives or other compounds in the sample is increased. The terms “purify,” “purified,” and “purification” are relative terms which do not require absolute purity. Thus, for example, when a malonyl-CoA derived compound (including a multifunctional fatty acid derivative disclosed herein or other compound) is produced in recombinant host cells, a malonyl-CoA derived compound (including a purified multifunctional fatty acid derivative or other compound) is a malonyl-CoA derived compound (including a multifunctional fatty acid derivative or other compound) that is substantially separated from other cellular components (e.g., nucleic acids, polypeptides, lipids, carbohydrates, or other hydrocarbons). 
     As used herein, the term “attenuate” means to weaken, reduce, or diminish. For example, a polypeptide can be attenuated by modifying the polypeptide to reduce its activity (e.g., by modifying a nucleotide sequence that encodes the polypeptide). 
     As used herein, the term “carbon source” refers to a substrate or compound suitable to be used as a source of carbon for prokaryotic or simple eukaryotic cell growth. Carbon sources can be in various forms, including, but not limited to polymers, carbohydrates, acids, alcohols, aldehydes, ketones, amino acids, peptides, and gases (e.g., CO and C02). Exemplary carbon sources include, but are not limited to, monosaccharides, such as glucose, fructose, mannose, galactose, xylose, and arabinose; oligosaccharides, such as fructo-oligosaccharide and galacto-oligosaccharide; polysaccharides such as starch, cellulose, pectin, and xylan; disaccharides, such as sucrose, maltose, cellobiose, and turanose; cellulosic material and variants such as hemicelluloses, methyl cellulose and sodium carboxymethyl cellulose; succinate, lactate, and acetate; alcohols, such as ethanol, methanol, and glycerol, or mixtures thereof. The carbon source can also be a product of photosynthesis, such as glucose. In certain embodiments, the carbon source is biomass. In other embodiments, the carbon source is glucose. In other embodiments the carbon source is sucrose. In other embodiments the carbon source is glycerol. In other embodiments, the carbon source is a simple carbon source. In other embodiments, the carbon source is a renewable carbon source. In other embodiment, the carbon source is natural gas. In other embodiments the carbon source comprises one or more components of natural gas, such as methane, ethane, or propane. In other embodiments, the carbon source is flu gas or synthesis gas. In still other embodiments, the carbon source comprises one or more components of flu or synthesis gas such as carbon monoxide, carbon dioxide, hydrogen, etc. As used herein, the term “carbon source” or “simple carbon source” specifically excludes oleochemicals such as e.g., saturated or unsaturated fatty acids. 
     As used herein, the term “biomass” refers to any biological material from which a carbon source is derived. In some embodiments, a biomass is processed into a carbon source, which is suitable for bioconversion. In other embodiments, the biomass does not require further processing into a carbon source. The carbon source can be converted into a composition comprising multifunctional fatty acid derivatives. 
     An exemplary source of biomass is plant matter or vegetation, such as corn, sugar cane, or switchgrass. Another exemplary source of biomass is metabolic waste products, such as animal matter (e.g., cow manure). Further exemplary sources of biomass include algae and other marine plants. Biomass also includes waste products from industry, agriculture, forestry, and households, including, but not limited to, glycerol, fermentation waste, ensilage, straw, lumber, sewage, garbage, cellulosic urban waste, and food leftovers (e.g., soaps, oils and fatty acids). The term “biomass” also can refer to sources of carbon, such as carbohydrates (e.g., monosaccharides, disaccharides, or polysaccharides). 
     I. Introduction 
     Hydrocarbon molecules with multiple functional groups have many industrial applications, e.g. as high performance chemicals, lubricants, personal care products, fragrances, adjuvants, polymers, etc. These functional groups provide useful properties themselves, for instance adding hydrophilicity for use in formulations, or as handles for a next step in chemistry, for instance polymerization. Thus, such molecules are useful for the preparation detergents, lubricants, pharmaceuticals, polymers and other valuable applications 
     Unfortunately however, the synthesis of hydrocarbon molecules, especially medium- to long-chain hydrocarbons (C6 to C18) with multiple hydroxy(—OH), oxo (=O), amino-(-NH2) or carboxyl (CO2H) groups in selective positions is extremely difficult and in many cases impractical starting from petrochemical feedstocks. 
     Thus, what is needed in the art are novel functionalized hydrocarbon compounds and methods for making them. In particular, a need exists for the production of medium- to long-chain hydrocarbons (C6 to C18) that have pre-designed, or “tailored,” specifications and properties. Further, there is a desire to source such compounds from renewable and sustainable resources. Fortunately, the instant disclosure provides for this and other needs. 
     II. Multifunctional Fatty Acid Derivative Molecules and Derivatives Thereof 
     A. General Methods 
     This disclosure utilizes routine techniques in the field of recombinant genetics. Basic texts disclosing the general methods and terms in molecular biology and genetics include e.g., Sambrook et al.,  Molecular Cloning, a Laboratory Manual , Cold Spring Harbor Press 4th edition (Cold Spring Harbor, N.Y. 2012); Current Protocols in Molecular Biology Volumes 1-3, John Wiley &amp; Sons, Inc. (1994-1998). This disclosure also utilizes routine techniques in the field of biochemistry. Basic texts disclosing the general methods and terms in biochemistry include e.g.,  Lehninger Principles of Biochemistry  sixth edition, David L. Nelson and Michael M. Cox eds. W.H. Freeman (2012). This disclosure also utilizes routine techniques in industrial fermentation. Basic texts disclosing the general methods and terms in fermentation include e.g.,  Principles of Fermentation Technology,  3rd Edition by Peter F. Stanbury, Allan Whitaker and Stephen J. Hall. Butterworth-Heinemann (2016);  Fermentation Microbiology and Biotechnology,  2nd Edition, E. M. T. El-Mansi, C. F. A. Bryce, Arnold L. Demain and A. R. Allman eds. CRC Press (2007). This disclosure also utilizes routine techniques in the field of organic chemistry. Basic texts disclosing the general methods and terms in organic chemistry include e.g.,  Practical Synthetic Organic Chemistry: Reactions, Principles, and Techniques , Stephane Caron ed., John Wiley and Sons Inc. (2011);  The Synthetic Organic Chemist&#39;s Companion , Michael C. Pirrung, John Wiley and Sons Inc. (2007);  Organic Chemistry,  9th Edition—Francis Carey and Robert Giuliano, McGraw Hill (2013). 
     For nucleic acids, sizes are given in either kilobases (kb) or base pairs (bp). Estimates are typically derived from agarose or acrylamide gel electrophoresis, from sequenced nucleic acids, or from published DNA sequences. For proteins, sizes are given in kilodaltons (kDa) or amino acid residue numbers. Protein sizes may be estimated from gel electrophoresis, from sequenced proteins, from derived amino acid sequences, or from published protein sequences. 
     Oligonucleotides that are not commercially available can be chemically synthesized e.g., according to the solid phase phosphoramidite triester method first described by Beaucage &amp; Caruthers, Tetrahedron Letts. 22:1859-1862 (1981), using an automated synthesizer, as described in Van Devanter et al., Nucleic Acids Res. 12:6159-6168 (1984). Purification of oligonucleotides is e.g., by either native acrylamide gel electrophoresis or by anion-exchange HPLC as described in Pearson &amp; Reanier, J. Chrom. 255:137-149 (1983). 
     The sequence of cloned genes and synthetic oligonucleotides can be verified after cloning using, e.g., the chain termination method for sequencing double-stranded templates of Wallace et al., Gene 16:21-26 (1981). 
     B. Multifunctional Molecules 
     In an exemplary embodiment, the disclosure provides “multifunctional fatty acid derivatives” or equivalently “multifunctional molecules”. Typically, multifunctional fatty acid derivatives have a carbon chain length of between 6 and 16 carbons and have at least three functional groups which comprise a heteroatom. Exemplary functional groups which comprise a heteroatom include e.g. a hydroxyl or equivalently, hydroxyl (—OH), oxo (CHO), carboxyl (CO 2 H), amino (CH 2 NH 2 ), O-acetyl (CO 2 C 2 H 3 ), methoxy (COCH 3 ) or ester (CO 2 CH 3 , CO 2 C 2 H 5 , CO 2 C 3 H 7 , CO 2 C 2 H 3 ) group 
     In an exemplary embodiment, the present disclosure provides novel multifunctional fatty acid derivative molecules having a general formula according to Scheme 1. 
     
       
         
         
             
             
         
       
     
     wherein
         ω indicates the reduced end of the fatty acid derivative molecule and a indicates the carboxyl end of the fatty acid derivative molecule, and
 
wherein
   R1=-OH; —O 2 H; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3      R2=-H; —OH;   R3=-H; —OH;   R4=-H; —OH;   R5=-CH 3 ; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3 ;       

     wherein
         m=1-10 and n=0-9 and wherein   if R1 is OH or —O 2 H then . . . 3&lt;m+n≤10; and if R1 is other than OH or —O 2 H, then 2&lt;m+n≤10, and       

     wherein
         the multifunctional molecule has at least three functional groups comprising a heteroatom, and       

     wherein
         at least two of R2, R3 and R4 are OH; or when R5 is other than CH 3 , CH 2  then at least one of R2, R3 and R4 are OH; and       

     wherein
         when R5=CH 3  and R4=H then n=0 or 1; and       

     wherein
         when R2=CH 3 , then R4 does not=H; and       

     wherein
         when R3=H, then n+m=p and p=3-10; unless R1=-OH or —O 2 H in which case when R3-H then n+m=p and p=4-10; and       

     wherein
         when the multifunctional molecule comprises a double bond that is not terminal, the double bond is in a position corresponding to an omega7 (ω-7) position; and       

     wherein
         the multifunctional molecule is not 1,3,12-dodecane triol; is not 3,11-dihydroxy-tetradecanoic acid; is not 3,11-dihydroxy-tetradecanoic acid methyl ester and is not naturally occurring.       

     As will be apparent to one of skill in the art, when —OH groups are present at positions R2, R3 and/or R4, chiral center(s) are formed at the carbons to which the —OH groups are bound. Thus, the multifunctional molecules disclosed herein are useful as synthons for the production of chirally important compounds such as pharmaceuticals, nutraceuticals, pesticides, herbicides, flavors, fragrances, solvents, bioactive compounds, etc. 
     Double bonds, if present, can be either (Z) or (E). The presence of a double bond adds another layer of functionality to the molecules disclosed herein conferring on the molecules the ability to participate in chemical reactions involving a double bond including e.g., polymerization, alkylation, metathesis, etc. Chemical reactions utilizing the carbon-carbon double bond are known in the art (see e.g.,  Practical Synthetic Organic Chemistry: Reactions, Principles, and Techniques , Stephane Caron ed. (supra)). 
     Thus, the multifunctional molecules disclosed herein provide novel molecules with new functionalities that can be used to address old problems in an improved way and/or which can find new uses altogether. 
     (i) Molecules having R1=CH 2 OH and R2=OH in Scheme 1 
     Referring to the general formula provided by Scheme 1 (above) when R1=CH 2 OH and R2=OH the disclosure provides multifunctional polyol molecules having chemical structural formulas as follows: 
     
       
         
         
             
             
         
       
     
     Formula I is referred to herein as 1,3,11-dodecane triol. With reference to Scheme 1, 1,3,11-dodecane triol, is described as R1=CH 2 OH; R2=OH; R3=H; R4=OH; R5=CH 3 ; and m+n=p=6. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula II 
     
       
         
         
             
             
         
       
     
     The molecule of Formula II is referred to herein as 1,3,10-dodecane triol. With reference to Scheme 1, 1,3,10-dodecane triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=6. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula III 
     
       
         
         
             
             
         
       
     
     Formula III is referred to herein as 1,3,9-dodecane triol. With reference to Scheme 1, 1,3,9-dodecane triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=5. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula IV. 
     
       
         
         
             
             
         
       
     
     Formula IV is referred to herein as 1,3,12-dodecene triol. With reference to Scheme 1, the molecule of Formula IV, 1,3,12-dodecene triol, is described as R1=CH 2 OH; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=6. In an exemplary embodiment, 1,3,12-dodecene triol, the double bond is in cis and therefore the molecule of Formula V is (z5)1,3,12-dodecene triol. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula V. 
     
       
         
         
             
             
         
       
     
     Formula V is referred to herein as 1,3,11-dodecene triol. With reference to Scheme 1, the molecule of Formula V, 1,3,11-dodecene triol, is described as R1=CH 2 OH; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=6. In an exemplary embodiment, 1,3,11-dodecene triol, the double bond is in cis and therefore the molecule of Formula V is (z5)1,3,11-dodecene triol. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula VI. 
     
       
         
         
             
             
         
       
     
     Formula VI is referred to herein as 1,3,10-dodecene triol. With reference to Scheme 1, the molecule of Formula V, 1,3,10-dodecene triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 m=6. In an exemplary embodiment, 1,3,10-dodecene triol, the double bond is in cis and therefore the molecule of Formula V is (z5)1,3,10-dodecene triol. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula VII. 
     
       
         
         
             
             
         
       
     
     Formula VII is referred to herein as 1,3,9-dodecene triol. With reference to Scheme 1, the molecule of Formula V, 1,3,9-dodecene triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=5. In an exemplary embodiment, 1,3,9-dodecene triol, the double bond is in cis and therefore the molecule of Formula V is (z5)1,3,9-dodecene triol. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula VIII. 
     
       
         
         
             
             
         
       
     
     Formula VIII is referred to herein as 1,3,11,12-dodecane tetrol. With reference to Scheme 1, 1,3,11,12-dodecane tetrol is described as R1=CH 2 OH; R2=OH; R3=H; R4=OH; R5=CH 2 OH; n+m=6. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula IX. 
     
       
         
         
             
             
         
       
     
     Formula IX is referred to herein as 1,3,10,12-dodecane tetrol. With reference to Scheme 1, 1,3,10,12-dodecane tetrol, is described as R1=CH 2 OH; R2=O; R3=OH; R4=H; R5=CH 2 OH; n=0 and m=6. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula X. 
     
       
         
         
             
             
         
       
     
     Formula X is referred to herein as 1,3,9,12-dodecane tetrol. With reference to Scheme 1, 1,3,9,12-dodecane tetrol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 2 OH; n=1 and m=5. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula XI. 
     
       
         
         
             
             
         
       
     
     Formula XI is referred to herein as 1,3,7-decane triol. With reference to Scheme 1, 1,3,7-decane triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=3. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula XII. 
     
       
         
         
             
             
         
       
     
     Formula XII is referred to herein as 1,3,8-decane triol. With reference to Scheme 1, 1,3,8-decane triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=4. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula XIII. 
     
       
         
         
             
             
         
       
     
     Formula XIII is referred to herein as 1,3,9-decane triol. With reference to Scheme 1, 1,3,9-decane triol, is described as R1=CH 2 OH; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=4. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula XIV. 
     
       
         
         
             
             
         
       
     
     Formula XIV is referred to herein as 1,3,7-decene triol. 1,3,7-decene triol is the tautomer of keto-1,8-dihydroxydecane. With reference to Scheme 1, 1,3,7-decene triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=3. In an exemplary embodiment, 1,3,7-decene triol, the double bond is in cis and therefore the molecule of Formula XIV is (z3)1,3,7-decene triol. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula XV. 
     
       
         
         
             
             
         
       
     
     Formula XV is referred to herein as 1,3,8-decene triol. With reference to Scheme 1, 1,3,8-decene triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=4. In an exemplary embodiment, 1,3,8-decene triol, the double bond is in cis and therefore the molecule of Formula XV is (z3)1,3,8-decene triol. 
     In another exemplary embodiment, the disclosure provides a multifunctional molecule having a chemical structural formula according to Formula XVI. 
     
       
         
         
             
             
         
       
     
     Formula XVI is referred to herein as 1,3,9-decene triol. With reference to Scheme 1, 1,3,9-decene triol, is described as R1=CH 2 OH; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=4. In an exemplary embodiment, 1,3,9-decene triol, the double bond is in cis and therefore the molecule of Formula XV is (z3)1,3,9-decene triol. 
     (ii) Molecules Having R1=CO 2 CH 3  or CO 2 CH 2 CH 3  and R2=OH in Scheme 1 
     The disclosure also provides multifunctional fatty acid methyl ester and ethyl esters. 
     Methyl Esters 
     Thus, referring to the general formula provided by Scheme 1 (above) when R1=CO 2 CH 3  and R2=OH the disclosure provides multifunctional molecules fatty acid methyl esters having chemical structural formulas as follows: 
     In one embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XVII. 
     
       
         
         
             
             
         
       
     
     Formula XVII is referred to herein as 3,12-dihydroxy dodecanoic acid methyl ester. With reference to Scheme 1, 3,12-dihydroxy dodecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XVIII. 
     
       
         
         
             
             
         
       
     
     Formula XVIII is referred to herein as 3,14-dihydroxy tetradecanoic acid methyl ester. With reference to Scheme 1, 3,14-dihydroxy tetradecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=8. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XIX. 
     
       
         
         
             
             
         
       
     
     Formula XIX is referred to herein as 3,16-dihydroxy hexadecanoic acid methyl ester. With reference to Scheme 1, 3,16-dihydroxy hexadecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=10. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XX. 
     
       
         
         
             
             
         
       
     
     Formula XX is referred to herein as 3,12-dihydroxy dodecenoic acid methyl ester. With reference to Scheme 1, 3,12-dihydroxy dodecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=6. In an exemplary embodiment, 3,12-dihydroxy dodecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XX is (z5) 3,12-dihydroxy dodecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXI. 
     
       
         
         
             
             
         
       
     
     Formula XXI is referred to herein as 3,14-dihydroxy tetradecenoic acid methyl ester. With reference to Scheme 1, 3,14-dihydroxy tetradecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=8. In an exemplary embodiment, 3,12-dihydroxy tetradecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXI is (z7) 3,14-dihydroxy tetradecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXII. 
     
       
         
         
             
             
         
       
     
     Formula XXII is referred to herein as 3,16-dihydroxy hexadecenoic acid methyl ester. With reference to Scheme 1, 3,16-dihydroxy hexadecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=10. In an exemplary embodiment, 3,16-dihydroxy hexadecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXII is (z9) 3,16-dihydroxy hexadecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXIII. 
     
       
         
         
             
             
         
       
     
     Formula XXIII is referred to herein as 3,11-dihydroxy dodecanoic acid methyl ester. With reference to Scheme 1, 3,11-dihydroxy dodecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXIV. 
     
       
         
         
             
             
         
       
     
     Formula XXIV is referred to herein as 3,10-dihydroxy dodecanoic acid methyl ester. With reference to Scheme 1, 3,10-dihydroxy dodecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXV. 
     
       
         
         
             
             
         
       
     
     Formula XXV is referred to herein as 3,9-dihydroxy dodecanoic acid methyl ester. With reference to Scheme 1, 3,9-dihydroxy dodecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=O and m=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXVI. 
     
       
         
         
             
             
         
       
     
     Formula XXVI is referred to herein as 3,11-dihydroxy dodecenoic acid methyl ester. With reference to Scheme 1, 3,11-dihydroxy dodecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=6. In an exemplary embodiment, 3,11-dihydroxy dodecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXVI is (z5) 3,11-dihydroxy dodecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXVII. 
     
       
         
         
             
             
         
       
     
     Formula XXVII is referred to herein as 3,10-dihydroxy dodecenoic acid methyl ester. With reference to Scheme 1, 3,10-dihydroxy dodecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=6. In an exemplary embodiment, 3,10-dihydroxy dodecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXVII is (z5) 3,10-dihydroxy dodecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXVIII. 
     
       
         
         
             
             
         
       
     
     Formula XXVIII is referred to herein as 3,9-dihydroxy dodecenoic acid methyl ester. With reference to Scheme 1, 3,9-dihydroxy dodecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=5. In an exemplary embodiment, 3,9-dihydroxy dodecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXVIII is (z5) 3,9-dihydroxy dodecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXIX. 
     
       
         
         
             
             
         
       
     
     Formula XXIX is referred to herein as 3,13-dihydroxy tetradecanoic acid methyl ester. With reference to Scheme 1, 3,13-dihydroxy tetradecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=8. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXX. 
     
       
         
         
             
             
         
       
     
     Formula XXX is referred to herein as 3,12-dihydroxy tetradecanoic acid methyl ester. With reference to Scheme 1, 3,12-dihydroxy tetradecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=8. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXI. 
     
       
         
         
             
             
         
       
     
     Formula XXXI is referred to herein as 3,13-dihydroxy tetradecenoic acid methyl ester. With reference to Scheme 1, 3,13-dihydroxy tetradecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n+m=8. In an exemplary embodiment, 3,13-dihydroxy tetradecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXXI is (z7) 3,13-dihydroxy tetradecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXII. 
     
       
         
         
             
             
         
       
     
     Formula XXXII is referred to herein as 3,12-dihydroxy tetradecenoic acid methyl ester. With reference to Scheme 1, 3,12-dihydroxy tetradecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=8. In an exemplary embodiment, 3,12-dihydroxy tetradecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXXII is (z7) 3,12-dihydroxy tetradecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXIII. 
     
       
         
         
             
             
         
       
     
     Formula XXXIII is referred to herein as 3,11-dihydroxy tetradecenoic acid methyl ester. With reference to Scheme 1, 3,11-dihydroxy tetradecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=7. In an exemplary embodiment, 3,11-dihydroxy tetradecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXXIII is (z7) 3,11-dihydroxy tetradecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXIV. 
     
       
         
         
             
             
         
       
     
     Formula XXXIV is referred to herein as 3,15-dihydroxy hexadecanoic acid methyl ester. With reference to Scheme 1, 3,15-dihydroxy hexadecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=10. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXV. 
     
       
         
         
             
             
         
       
     
     Formula XXXV is referred to herein as 3,14-dihydroxy hexadecanoic acid methyl ester. With reference to Scheme 1, 3,14-dihydroxy hexadecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=10. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXVI. 
     
       
         
         
             
             
         
       
     
     Formula XXXVI is referred to herein as 3,13-dihydroxy hexadecanoic acid methyl ester. With reference to Scheme 1, 3,13-dihydroxy hexadecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=9. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXVII. 
     
       
         
         
             
             
         
       
     
     Formula XXXVII is referred to herein as 3,15-dihydroxy hexadecenoic acid methyl ester. With reference to Scheme 1, 3,15-dihydroxy hexadecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=10. In an exemplary embodiment, 3,15-dihydroxy hexadecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXXVIII is (z9) 3,15-dihydroxy hexadecenoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXVIII. 
     
       
         
         
             
             
         
       
     
     Formula XXXVIII is referred to herein as 3,14-dihydroxy hexadecanoic acid methyl ester. With reference to Scheme 1, 3,14-dihydroxy hexadecanoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=10. In an exemplary embodiment, 3,13-dihydroxy hexadecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXXVIII is (z9) 3,14-dihydroxy hexadecanoic acid methyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XXXIX. 
     
       
         
         
             
             
         
       
     
     Formula XXXIX is referred to herein as 3,13-dihydroxy hexadecenoic acid methyl ester. With reference to Scheme 1, 3,13-dihydroxy hexadecenoic acid methyl ester is described as R1=CO 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=9. In an exemplary embodiment, 3,13-dihydroxy hexadecenoic acid methyl ester has the double bond is in cis and therefore the molecule of Formula XXXIX is (z9) 3,13-dihydroxy hexadecenoic acid methyl ester. 
     Ethyl Esters 
     As noted above, the disclosure also provides multifunctional fatty acid methyl ester and ethyl esters. Exemplary methyl esters are disclosed above. Now, referring to the general formula provided by Scheme 1 (above) when R1=CO 2 CH 2 CH 3  and R2=OH the disclosure provides multifunctional fatty acid ethyl ester molecules having chemical structural formulas as follows: 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XL. 
     
       
         
         
             
             
         
       
     
     Formula XL is referred to herein as 3,12-dihydroxy dodecanoic acid ethyl ester. With reference to Scheme 1, 3,12-dihydroxy dodecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLI. 
     
       
         
         
             
             
         
       
     
     Formula XLI is referred to herein as 3,14-dihydroxy tetradecanoic acid ethyl ester. With reference to Scheme 1, 3,14-dihydroxy tetradecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=8. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLII. 
     
       
         
         
             
             
         
       
     
     Formula XLII is referred to herein as 3,16-dihydroxy hexadecanoic acid ethyl ester. With reference to Scheme 1, 3,16-dihydroxy hexadecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=10. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLIII. 
     
       
         
         
             
             
         
       
     
     Formula XLIII is referred to herein as 3,12-dihydroxy dodecenoic acid ethyl ester. With reference to Scheme 1, 3,12-dihydroxy dodecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=6. In an exemplary embodiment, 3,12-dihydroxy dodecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula XLIII is (z5) 3,12-dihydroxy dodecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLIV. 
     
       
         
         
             
             
         
       
     
     Formula XLIV is referred to herein as 3,14-dihydroxy tetradecenoic acid ethyl ester. With reference to Scheme 1, 3,14-dihydroxy tetradecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=8. In an exemplary embodiment, 3,14-dihydroxy tetradecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula XLIV is (z7) 3,14-dihydroxy tetradecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLV. 
     
       
         
         
             
             
         
       
     
     Formula XLV is referred to herein as 3,16-dihydroxy hexadecenoic acid ethyl ester. With reference to Scheme 1, 3,16-dihydroxy hexadecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=H; R5=CH 2 OH; n+m=10. In an exemplary embodiment, 3,16-dihydroxy hexadecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula XLV is (z9) 3,16-dihydroxy hexadecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLVI. 
     
       
         
         
             
             
         
       
     
     Formula XLVI is referred to herein as 3,11-dihydroxy dodecanoic acid ethyl ester. With reference to Scheme 1, 3,11-dihydroxy dodecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLVII. 
     
       
         
         
             
             
         
       
     
     Formula XLVII is referred to herein as 3,10-dihydroxy dodecanoic acid ethyl ester. With reference to Scheme 1, 3,10-dihydroxy dodecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n+m=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLVIII. 
     
       
         
         
             
             
         
       
     
     Formula XLVIII is referred to herein as 3,9-dihydroxy dodecanoic acid ethyl ester. With reference to Scheme 1, 3,9-dihydroxy dodecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=5. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XLIX. 
     
       
         
         
             
             
         
       
     
     Formula XLIX is referred to herein as 3,11-dihydroxy dodecenoic acid ethyl ester. With reference to Scheme 1, 3,11-dihydroxy dodecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=6. In an exemplary embodiment, 3,11-dihydroxy dodecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula XLIX is (z5) 3,11-dihydroxy dodecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula L. 
     
       
         
         
             
             
         
       
     
     Formula L is referred to herein as 3,10-dihydroxy dodecenoic acid ethyl ester. With reference to Scheme 1, 3,10-dihydroxy dodecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=6. In an exemplary embodiment, 3,10-dihydroxy dodecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula L is (z5) 3,10-dihydroxy dodecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LI. 
     
       
         
         
             
             
         
       
     
     Formula LI is referred to herein as 3,9-dihydroxy dodecenoic acid ethyl ester. With reference to Scheme 1, 3,9-dihydroxy dodecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=5. In an exemplary embodiment, 3,9-dihydroxy dodecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula LI is (z5) 3,9-dihydroxy dodecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LII. 
     
       
         
         
             
             
         
       
     
     Formula LII is referred to herein as 3,13-dihydroxy tetradecanoic acid ethyl ester. With reference to Scheme 1, 3,13-dihydroxy tetradecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=8. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LIII. 
     
       
         
         
             
             
         
       
     
     Formula LIII is referred to herein as 3,12-dihydroxy tetradecanoic acid ethyl ester. With reference to Scheme 1, 3,12-dihydroxy tetradecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=8. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LIV. 
     
       
         
         
             
             
         
       
     
     Formula LIV is referred to herein as 3,11-dihydroxy tetradecanoic acid methyl ester. With reference to Scheme 1, 3,11-dihydroxy tetradecanoic acid methyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=7. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LV. 
     
       
         
         
             
             
         
       
     
     Formula LV is referred to herein as 3,13-dihydroxy tetradecenoic acid ethyl ester. With reference to Scheme 1, 3,13-dihydroxy tetradecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=8. In an exemplary embodiment, 3,13-dihydroxy tetradecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula LV is (z7) 3,13-dihydroxy tetradecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LVI. 
     
       
         
         
             
             
         
       
     
     Formula LVI is referred to herein as 3,12-dihydroxy tetradecenoic acid ethyl ester. With reference to Scheme 1, 3,12-dihydroxy tetradecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=8. In an exemplary embodiment, 3,12-dihydroxy tetradecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula LVI is (z7) 3,12-dihydroxy tetradecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LVII. 
     
       
         
         
             
             
         
       
     
     Formula LVII is referred to herein as 3,11-dihydroxy tetradecenoic acid ethyl ester. With reference to Scheme 1, 3,11-dihydroxy tetradecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=7. In an exemplary embodiment, 3,11-dihydroxy tetradecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula LVII is (z7) 3,11-dihydroxy tetradecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LVIII. 
     
       
         
         
             
             
         
       
     
     Formula LVIII is referred to herein as 3,15-dihydroxy hexadecanoic acid ethyl ester. With reference to Scheme 1, 3,15-dihydroxy hexadecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=10. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LIX. 
     
       
         
         
             
             
         
       
     
     Formula LIX is referred to herein as 3,14-dihydroxy hexadecanoic acid ethyl ester. With reference to Scheme 1, 3,14-dihydroxy hexadecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=10. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LX. 
     
       
         
         
             
             
         
       
     
     Formula LX is referred to herein as 3,13-dihydroxy hexadecanoic acid ethyl ester. With reference to Scheme 1, 3,13-dihydroxy hexadecanoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=9. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXI. 
     
       
         
         
             
             
         
       
     
     Formula LXI is referred to herein as 3,15-dihydroxy hexadecenoic acid ethyl ester. With reference to Scheme 1, 3,15-dihydroxy hexadecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=H; R4=OH; R5=CH 3 ; n+m=7. In an exemplary embodiment, 3,15-dihydroxy hexadecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula LXI is (z9) 3,15-dihydroxy hexadecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXII. 
     
       
         
         
             
             
         
       
     
     Formula LXII is referred to herein as 3,14-dihydroxy hexadecenoic acid ethyl ester. With reference to Scheme 1, 3,14-dihydroxy hexadecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=0 and m=10. In an exemplary embodiment, 3,14-dihydroxy hexadecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula LXII is (z9) 3,14-dihydroxy hexadecenoic acid ethyl ester. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXIII. 
     
       
         
         
             
             
         
       
     
     Formula LXIII is referred to herein as 3,13-dihydroxy hexadecenoic acid ethyl ester. With reference to Scheme 1, 3,13-dihydroxy hexadecenoic acid ethyl ester is described as R1=CO 2 CH 2 CH 3 ; R2=OH; R3=OH; R4=H; R5=CH 3 ; n=1 and m=9. In an exemplary embodiment, 3,13-dihydroxy hexadecenoic acid ethyl ester has the double bond is in cis and therefore the molecule of Formula LXIII is (z9) 3,13-dihydroxy hexadecenoic acid ethyl ester. 
     (iii) Molecules having R1=COOH and R2=H in Scheme 1 
     In an embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having having R1=COOH and R2=H in Scheme 1, wherein n=0-3. Thus, in one embodiment R1=COOH and R2=H in Scheme 1, and n=0. In another embodiment, R1=COOH and R2=H in Scheme 1, and n=1. In another embodiment, R1=COOH and R2=H in Scheme 1, and n=2. In another embodiment, R1=COOH and R2=H in Scheme 1, and n=3. 
     In another embodiment, R1=COOH and R2=H in Scheme 1, and n≠4. 
     (iv) Novel Molecules Disclosed Herein not Described by Scheme 1 
     In addition to the molecules disclosed above which are conveniently described by Scheme 1, the disclosure further provides the following novel molecules which do not fit Scheme 1. 
     Thus, in one embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXVI. 
     
       
         
         
             
             
         
       
     
     Formula LXVI is referred to herein as 10,14-dihydroxy hexadecanoic acid. The molecule 10,14-dihydroxy hexadecanoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXVII. 
     
       
         
         
             
             
         
       
     
     Formula LXVII is referred to herein as 10,13-dihydroxy hexadecanoic acid. The molecule 10,13-dihydroxy hexadecanoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXVIII. 
     
       
         
         
             
             
         
       
     
     Formula LXVIII is referred to herein as 1,12,16-hexadecene triol. The molecule 1,12,16-hexadecene triol is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXIX. 
     
       
         
         
             
             
         
       
     
     Formula LXIX is referred to herein as 1,9,10-hexadecane triol. The molecule 1,9,10-hexadecane triol is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXX. 
     
       
         
         
             
             
         
       
     
     Formula LXX is referred to herein as 9,10,15 trihydroxy hexadecanoic acid. The molecule 9,10,15 trihydroxy hexadecanoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXI. 
     
       
         
         
             
             
         
       
     
     Formula LXXI is referred to herein as 9,10,14 trihydroxy hexadecanoic acid. The molecule 9,10,14 trihydroxy hexadecanoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXII. 
     
       
         
         
             
             
         
       
     
     Formula LXXII is referred to herein as 9,10,13 trihydroxy hexadecanoic acid. The molecule 9,10,13 trihydroxy hexadecanoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXIII. 
     
       
         
         
             
             
         
       
     
     Formula LXXIII is referred to herein as 9,10,15 trihydroxy hexadecanoic acid. The molecule 9,10,15 trihydroxy hexadecanoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXIV. 
     
       
         
         
             
             
         
       
     
     Formula LXXIV is referred to herein as 1,7,10-(8e)-hexadecene triol. The molecule 1,7,10-(8e)-hexadecene triol is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXV. 
     
       
         
         
             
             
         
       
     
     Formula LXXV is referred to herein as 1,7,10-(8e)-octadecene triol. The molecule 1,7,10-(8e)-octadecene triol is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXVI. 
     
       
         
         
             
             
         
       
     
     Formula LXXVI is referred to herein as 7,10,16 trihydroxy-(8e)-hexadecenoic acid. The molecule 7,10,16 trihydroxy-(8e)-hexadecenoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXVII. 
     
       
         
         
             
             
         
       
     
     Formula LXXVII is referred to herein as 7,10,18-trihydroxy-(8e)-octadecenoic acid. The molecule 7,10,18-trihydroxy-(8e)-octadecenoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXVIII. 
     
       
         
         
             
             
         
       
     
     Formula LXXVIII is referred to herein as 7,10,14-trihydroxy-(8e)-hexadecenoic acid. The molecule 7,10,14-trihydroxy-(8e)-hexadecenoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXIX. 
     
       
         
         
             
             
         
       
     
     Formula LXXIX is referred to herein as 7,10,13-trihydroxy-(8e)-octadecenoic acid. The molecule 7,10,13-trihydroxy-(8e)-octadecenoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXX. 
     
       
         
         
             
             
         
       
     
     Formula LXXX is referred to herein as 7,10,15-trihydroxy-(8e)-octadecenoic acid. The molecule 7,10,15-trihydroxy-(8e)-octadecenoic acid is not described with reference to Scheme 1. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXXI. 
     
       
         
         
             
             
         
       
     
     Formula LXXXI is referred to herein as 7,10,14-trihydroxy-(8e)-octadecenoic acid. The molecule 7,10,14-trihydroxy-(8e)-octadecenoic acid is not described with reference to Scheme 1. 
     Scheme 2 
     In another embodiment, the present disclosure provides novel multifunctional fatty acid derivative molecules having a general formula according to Scheme 2. 
     
       
         
         
             
             
         
       
     
     wherein
         ω indicates the reduced end of the fatty acid derivative molecule and a indicates the carboxyl end of the fatty acid derivative molecule, and
 
wherein
   R1=-OH; —O 2 H; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3      R2=-H; —OH; —NH 2      R3=-H; —OH; —NH 2      R4=-H; —OH; —NH 2      R5=-CH 3 ; —CH 2 ; —CH 2 OH; —CHO; —CH 2 NH 2 ; —CO 2 H; —CO 2 CH 3 ; —CO 2 C 2 H 5 ; —CO 2 C 3 H 7 ; —CO 2 C 2 H 3 ;       

     wherein
         m=1-10 and n=0-9 and wherein   if R1 is OH or —O 2 H then . . . 3&lt;m+n≤10; and if R1 is other than OH or —O 2 H, then 2&lt;m+n≤10, and       

     wherein
         the multifunctional molecule has at least three functional groups comprising a heteroatom, and       

     wherein
         when R5=CH 3  and R4=H then n=0 or 1; and       

     wherein
         when R2=CH 3 , then R4 does not=H; and       

     wherein
         when R3=H, then n+m=p and p=3-10; unless R1=-OH or —O 2 H in which case when R3-H then n+m=p and p=4-10; and       

     wherein
         when the multifunctional molecule comprises a double bond that is not terminal, the double bond is in a position corresponding to an omega7 (ω-7) position; and       

     wherein
         the multifunctional molecule is not 1,3,12-dodecane triol; is not 3,11-dihydroxy-tetradecanoic acid; is not 3,11-dihydroxy-tetradecanoic acid methyl ester and is not naturally occurring.       

     As will be apparent to one of skill in the art, when groups comprising a heteroatom are present at positions R2, R3 and/or R4, chiral center(s) are formed at the carbons to which the —OH groups are bound. Thus, the multifunctional molecules disclosed herein are useful as synthons for the production of chirally important compounds such as pharmaceuticals, nutraceuticals, pesticides, herbicides, flavors, fragrances, solvents, bioactive compounds, etc. Double bonds, if present, can be either (Z) or (E). 
     (i) Molecules Having R1=COOH and R2=-NH 2  in Scheme 2 
     Referring to the general formula provided by Scheme 2 (above) when R1=COOH and R2=NH 2  the disclosure provides multifunctional molecules having chemical structural formulas as follows: 
     
       
         
         
             
             
         
       
     
     Formula LXXXII is referred to herein as 3-amino, 12-hydroxy-dodecanoic acid. With reference to Scheme 2, 3-amino, 12-hydroxy-dodecanoic acid is described as R1=CO 2 H; R2=NH 2 ; R3=H; R4=H; R5=CH 2  OH; and m+n=p=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXXIII. 
     
       
         
         
             
             
         
       
     
     Formula LXXXIII is referred to herein as 3-amino, 12-hydroxy-dodecenoic acid. With reference to Scheme 2, 3-amino, 12-hydroxy dodecenoic acid is described as R1=CO 2 H; R2=NH 2 ; R3=H; R4=H; R5=CH 2  OH; and m+n=p=6. 
     (ii) Molecules Having R1=CH 2 OH and R2=-NH 2  in Scheme 2 
     Referring to the general formula provided by Scheme 2 (above) when R1=COOH and R2=NH 2  the disclosure provides multifunctional molecules having chemical structural formulas as follows: 
     
       
         
         
             
             
         
       
     
     Formula LXXXIV is referred to herein as 3-amino dodecene 1,12-diol. With reference to Scheme 2, 3-amino dodecene 1,12-diol is described as R1=CH 2 OH; R2=NH 2 ; R3=H; R4=H; R5=CH 2  OH; and m+n=p=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXXV. 
     
       
         
         
             
             
         
       
     
     Formula LXXXV is referred to herein as 3-amino dodecane 1,12-diol. With reference to Scheme 2, 3-amino dodecane 1,12-diol is described as R1=CO 2 H; R2=NH 2 ; R3=H; R4=H; R5=CH 2  OH; and m+n=p=6. 
     (iii) Molecules Having R1=COOH and R5=-CH 2 NH 2  in Scheme 2 
     Referring to the general formula provided by Scheme 2 (above) when R1=COOH and R5=CH 2 NH 2  the disclosure provides multifunctional molecules having chemical structural formulas as follows: 
     
       
         
         
             
             
         
       
     
     Formula LXXXVI is referred to herein as 3-hydroxy, 12-amino-dodecanoic acid. With reference to Scheme 2, 3-hydroxy, 12-amino-dodecanoic acid is described as R1=CO 2 H; R2=OH; R3=H; R4=H; R5=CH 2 NH 2 ; and m+n=p=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXXVII. 
     
       
         
         
             
             
         
       
     
     Formula LXXXV is referred to herein as 3-hydroxy, 12-amino dodecenoic acid. With reference to Scheme 2, 33-hydroxy, 12-amino dodecenoic acid is described as R1=CO 2 H; R2=OH; R3=H; R4=H; R5=CH 2 NH 2 ; and m+n=p=6. 
     (iv) Molecules Having R1=CH 2 OH and R5=CH 2 NH 2  in Scheme 2 
     Referring to the general formula provided by Scheme 2 (above) when R1=COOH and R5=CH 2 NH 2  the disclosure provides multifunctional molecules having chemical structural formulas as follows: 
     
       
         
         
             
             
         
       
     
     Formula LXXXVIII is referred to herein as 12-amino dodecene 1,3-diol. With reference to Scheme 2, 12-amino dodecene 1,3-diol is described as R1=CH 2 OH; R2=OH; R3=H; R4=H; R5=CH 2 NH 2 ; and m+n=p=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula LXXXIX. 
     
       
         
         
             
             
         
       
     
     Formula LXXXIX is referred to herein as 12-amino dodecene 1,9-diol. With reference to Scheme 2, 12-amino dodecene 1,9-diol is described as R1=CH 2 OH; R2=H; R3=OH; R4=H; R5=CH 2 NH 2 ; and m=5 n=2. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XC. 
     
       
         
         
             
             
         
       
     
     Formula XC is referred to herein as 12-amino dodecane 1,3-diol. With reference to Scheme 2, 12-amino dodecane 1,3-diol is described as R1=CH 2 OH; R2=OH; R3=H; R4=H; R5=CH 2 NH 2 ; and m+n=p=6. 
     In another embodiment, the disclosure provides a multifunctional fatty acid derivative molecule having a chemical structural formula according to Formula XCI. 
     
       
         
         
             
             
         
       
     
     Formula XCI is referred to herein as 12-amino-dodecane-1,9-diol. With reference to Scheme 2, 12-amino-dodecane-1,9-diol is described as R1=CH 2 OH; R2=H; R3=OH; R4=H; R5=CH 2 NH 2 ; and m=5 n=1. 
     1. Physical Properties Multifunctional fatty Acid Derivative Molecules 
     All of the multifunctional fatty acid derivative molecules (MFM) disclosed herein comprise a chiral center at R2, R3, and R4 when R2, R3 and/or R4 are hydroxyl groups. Additionally, the unsaturated MFM disclosed herein, also comprise a double bond. Thus, the MFM disclosed herein are able to undergo a wide array of chemical reactions to form a large variety of molecules. Thus, the MFM disclosed herein find use as unique chemicals which further provide for a number of unique and useful derivative molecules. 
     a. Hydroxyl Groups 
     In exemplary embodiments, the multifunctional molecules disclosed herein comprise hydroxyl functional groups. As is generally known in the art, the chemistry of polyols is much the same as that of alcohols. Thus, because of the polar nature of the —OH bond multifunctional molecules as disclosed herein readily form hydrogen bonds with other multifunctional molecules bearing hydroxyl groups or other hydrogen-bonding systems (e.g. water). Thus, multifunctional molecules bearing hydroxyl groups generally have relatively high melting and boiling points by comparison with analogous alkanes and relatively high solubility in aqueous media. (see e.g.,  Organic Chemistry  ninth edition Francis Carey and Robert Giuliano (2013) supra). 
     The hydroxyl functional groups may participate in the large number of chemical reactions characteristic of hydroxyl groups. Thus, in one exemplary embodiment, the hydroxyl functional groups participate in nucleophilic substitution reactions wherein the hydroxyl acts as a leaving group or where —OH or —O— functions as a nucleophile e.g., substitution with a halide. 
     In other exemplary embodiments, the hydroxyl functional groups participate in nucleophilic addition reactions wherein the hydroxyl group acts as the nucleophile thereby forming acetals with aldehydes or ketones. Exemplary nucleophilic addition reactions include e.g., glycosylation reactions, which are discussed in more detail herein below. 
     In still other exemplary embodiments, the hydroxyl functional groups participate in nucleophilic acyl substitution reactions wherein the hydroxyl group acts as the nucleophile to form esters with carboxylic acids and carboxylic acid derivatives e.g., to form fatty esters. 
     In still other exemplary embodiments, the hydroxyl functional groups participate in elimination reactions wherein the hydroxyl group is removed as water and a carbon double bond (alkene) is formed. 
     In still other exemplary embodiments, the hydroxyl functional groups participate in oxidation reactions wherein the hydroxyl group is converted to a carbonyl group (C═O) thus producing a carbonyl compound. In oxidation reactions the resulting carbonyl compound may be an aldehyde, a ketone, or a carboxylic acid depending on the the oxidizing agent used (see e.g.,  Organic Chemistry  9th Edition, Francis Carey and Robert Giuliano (2013) supra). 
     Thus, the multiple hydroxyl functional groups of the multifunctional molecules disclosed herein make a wide variety of reactions possible and this in turn offers the possibility of numerous derivatives having unique and useful properties. 
     For example in some embodiments, a recombinant microbe that expresses a heterologous biochemical pathway comprising a thioesterase, at least one hydroxylating enzyme, an alcohol dehydrogenase or oxidase and a transaminase produces multifunctional fatty acid molecules with an amino group. Suitable thioesterases include any polypeptides that, when expressed in a microorganism in the presence of a carbon source, catalyze the production of fatty acids including 3-hydroxy fatty acids, e.g., enzymes having an Enzyme Commission number (EC 3.1.2.). Exemplary thioesterases include e.g., FatB1 from  Umbellularia californica  (Q41635) or PhaG from  Pseudomonas putida  (AAN67031). 
     Thus, in one embodiment, a recombinant microbe comprising a thioesterase such as FatB1 from  Umbellularia californica , an alcohol oxidase such as AlkJ from  Pseudomonas putida , a transaminase such as CV_2025 from  Chromobacterium violaceum  and a ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecules: 3-hydroxy, 12-amino dodecanoic acid; 3-amino, 12-hydroxy dodecanoic acid; (z5)3-hydroxy, 12-amino dodecenoic acid and (z5) 3-amino 12-hydroxy dodecenoic acid when the recombinant microbe is grown on a simple carbon source. 
     In another embodiment, a recombinant microbe comprising an thioesterase such as FatB1 from  Umbellularia californica , an alcohol oxidase such as AlkJ from  Pseudomonas putida , a transaminase such as CV_2025 from  Chromobacterium violaceum , a carboxylic acid reductase such as CarB from  Mycobacterium smegmatis  and an ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecules 12-amino dodecane-1,3-diol; 3-amino dodecane-1,12-diol; 12-amino dodecane-1,9-diol; (z5)12-amino dodecene-1,3-diol; (z5)3-amino dodecene-1,12-diol and (z5)12-amino dodecene-1,9-diol. 
     Table 5 herein below discloses heterologous enzymes suitable for converting hydroxyl groups in multifunctional molecules into other functional groups. Further, Table 5 discloses the reactions catalyzed by the enzymes. Exemplary functional groups to which hydroxyl groups can be converted include e.g., oxo, carboxyl, amino, 0-acetyl, methoxy, ester, etc. Exemplary enzymes suitable for making these modifications includes dehydrogenases, oxidases, transaminases, acetyl-transferases, methyltransferases and ester synthases. 
     b. Chirality 
     Chiral molecules, such as multifunctional molecules disclosed herein, which may have a chiral center at R1, R2, R3 and/or R4, are building blocks for the synthesis of compounds e.g., pharmaceuticals, nutraceuticals, etc., which are affected by stereochemistry. Since most isomers of chiral drugs exhibit marked differences in biological activities such as e.g., pharmacology, toxicology, pharmacokinetics, biorecognition, metabolism, etc., chirality is an important property to consider e.g., in drug design. Indeed, selecting the appropriate enantiomer can have profound effect on the biological properties of a molecule. Thus, the novel multifunctional molecules disclosed herein provide building blocks for the synthesis of compounds such as e.g., pharmaceuticals, which are affected by stereochemistry. 
     The 3-hydroxy functionality of the multifunctional fatty acid derivative molecules disclosed herein may form a stereo center at the carbon bearing the hydroxy functionality, thereby providing a point of chirality for the molecule. 
     The stereoisomer of a multifunctional fatty acid derivative molecule that is produced by a microorganism depends on the selectivity of the fatty acid biosynthesis pathway (FAS) from which it is produced. By manipulating which FAS enzymes are responsible for synthesis of a multifunctional fatty acid derivative molecule the chirality of the resulting multifunctional fatty acid derivative molecule can be controlled. 
     For example, in an exemplary embodiment, the native  E. coli  FAS is exploited to produce the (R) enantiomer of multifunctional fatty acid derivative molecule. In this embodiment, the chiral center of the multifunctional fatty acid derivative molecule is created by the activity of by 3-ketoacyl-ACP reductase, an enzyme encoded by the FabG gene in  E. coli . The activity of 3-ketoacyl-ACP reductase produces (R)-3-hydroxyl acyl ACP which can then enter engineered enzymatic pathway(s). 
     In other exemplary embodiments, the beta-oxidation pathway is exploited to produce the (S) enantiomer of a multifunctional fatty acid derivative molecule. In this embodiment, the (S) enantiomer of the multifunctional fatty acid derivative molecule is prepared by causing an accumulation of (S)-3-hydroxy acyl CoA which is an intermediate in the degradation of fatty acids through the beta-oxidation pathway. The excess (S)-3-hydroxy-acyl CoA is then converted to the (S) enantiomer of the multifunctional fatty acid derivative molecule through the action of fatty alcohol forming polypeptides, thioesterases or ester synthases. 
     Therefore, in an exemplary embodiment, to prepare the (S) enantiomer of an multifunctional fatty acid derivative molecule, available free fatty acids are first converted to acyl-CoAs by acyl-CoA synthase, a reaction catalyzed by FadD in  E. coli  (and homologs in other microorganisms). The resulting acyl-CoAs are then oxidized to trans-2-enoyl-CoA by fatty acyl-CoA dehydrogenase, a reaction catalyzed by FadE in  E. coli  (and homologs in other microorganisms). The resulting trans-2-enoyl-CoA is then hydrated to (S)-3-hydroxy-acyl-CoA by 2-trans-enoyl-CoA hydratase/(S)-3-hydroxy-acyl-CoA dehydratase, a reaction catalyzed by FadB in  E. coli  (and homologs in other microorganisms). 
     In the wild-type beta-oxidation pathway, (S)-3-hydroxy-acyl-CoA is then further oxidized to 3-keto-acyl-CoA by 3-keto-acyl-CoA dehydrogenase, a reaction also catalyzed by FadB in  E. coli  (and homologs in other microorganisms). The resulting 3-keto-acyl-CoA is thiolyzed to acyl-CoA and acetyl-CoA by 3-ketoacyl-CoA thiolase, a reaction catalyzed by FadA in  E. coli  (and homologs in other microorganisms). 
     In one exemplary embodiment, accumulation of (S)-3-hydroxy-acyl-CoA, is caused by selectively blocking the dehydrogenase activity of 3-keto-acyl-CoA dehydrogenase (FadB) to prevent the oxidation of (S)-3-hydroxy-acyl-CoA to 3-keto-acyl-CoA. In exemplary embodiments, selective blocking of the (S)-3-hydroxy-acyl-CoA dehydrogenase activity of FadB is achieved by mutation of Histidine 450 in the  E. coli  FadB gene (see e.g., He XY and Yang SY (1996) Biochemistry 35(29):9625-9630). (S)-3-hydroxy-acyl CoA accumulated in the cell is then converted to the (S) enantiomer of the multifunctional fatty acid derivative molecule, through the action of fatty alcohol forming polypeptides, thioesterases or ester synthases such as those disclosed e.g., in WO 2016/011430 A1. 
     Determination/confirmation of the resulting enantiomer configuration is achieved by any method known in the art e.g., by non-chromatographic techniques as polarimetry, by nuclear magnetic resonance, isotopic dilution, calorimetry, and enzyme techniques. These techniques require pure samples, and no separation of enantiomers is involved. Quantitation (which does not require pure samples) and separation of enantiomers can be done simultaneously by chiral chromatography such as gas chromatography (GC) or high performance liquid chromatography (HPLC) using chiral columns (see e.g.,  Stereochemistry of Organic Compounds , Ernest L. Elil and Sanuel H. Wilen, 1994, John Wiley &amp; Sons, Inc.). The chiral purity of products can be identified using chiral chromatographic methods such as chiral HPLC or LC/MS (see e.g., US Patent Application Publication Nos. US2008/0248539A1 and US2013/0052699A1). 
     c. Metathesis 
     As discussed above, the double bond of an unsaturated multifunctional fatty acid derivative molecule, may be in either (E) configuration or (Z) configuration. 
     In general, unsaturated fatty acid derivative molecules produced utilizing microbes as disclosed hereinabove carry the double bond in (Z) configuration. However, as will be discussed herein below, methods are available to rearrange the (Z) double bond of an unsaturated fatty acid derivative molecule such that the double bond is produced in (E) configuration. 
     Multifunctional fatty acid derivative molecules produced as disclosed herein have a double bond predominantly in (Z) configuration. In some exemplary embodiments an unsaturated multifunctional fatty acid derivative molecule has a non-terminal double bond between the seventh and eighth carbons from the reduced end of the multifunctional fatty acid derivative molecule (in the co-7 position). In exemplary embodiments, the double bond in the co-7 position is in cis (Z) configuration. 
     U.S. Pat. No. 9,163,267 teaches methods for producing an olefin by contacting a composition comprising at least one omega-7-olefinic fatty acid or derivative thereof with a cross metathesis catalyst under conditions allowing a cross metathesis transformation, wherein the at least one omega-7-olefinic fatty acid or derivative thereof was produced in a genetically engineered microorganism. Thus, in exemplary embodiments, methods such as those disclosed in U.S. Pat. No. 9,163,267 are used to prepare a (E) isomer of an unsaturated (Z)-multifunctional fatty acid derivative e.g., (E) isomer of (z5) 1,3,12 dodecenetriol, made using engineered microbes as disclosed herein above. As is well known in the art, in cross metathesis reactions, the (Z)-(E) selectivity is typically biased towards the formation of the (E)-isomer (see e.g., Naeimeh Bahri-Laleh et al., (2011) Beilstein J. Org. Chem. 7:40-45). 
     2. Assaying for Multifunctional Fatty Acid Derivatives 
     In exemplary embodiments, multifunctional fatty acid derivatives are identified by assaying for the production of multifunctional fatty acid derivatives (e.g., 1,3,10 dodecanetriol, (z5) 1,3,12 dodecenetriol, 1,3,11 dodecane triol, etc.) by a recombinant microbial host strain. In exemplary embodiments, Gas-Chromatography with Flame-Ionization Detection (GC-FID) is used to assay the multifunctional acid derivative. GC-FID is known in the art (see e.g., Adlard, E. R.; Handley, Alan J. (2001).  Gas chromatographic techniques and applications . London: Sheffield Academic). However, any appropriate method for quantitation and analysis may be used e.g., mass spectrometry (MS), Gas Chromatography-mass spectrometry (GC-MS), liquid chromatography-mass spectrometry (LC-MS), thin layer chromatography (TLC), etc. 
     3. Multifunctional Fatty Acid Derivative Molecules as Building Blocks for Polyols, Surfactants, Polyesters and Polyurethanes 
     Multifunctional fatty acid derivatives such as the multifunctional molecules disclosed herein, have applications as e.g., polyols, surfactants, and/or monomers in a variety of polymers, including but not limited to polyesters and polyurethanes. 
     In exemplary embodiments, the hydroxyl functional groups of multifunctional molecules are used to prepare polyurethanes in at least two different broad sets of chemistry: isocyanate-based polyurethanes and non-isocyanate polyurethanes. 
     In exemplary embodiments, multifunctional molecules act as polyols in standard isocyanate-based polyurethanes; or with mixed functionalities, available hydroxyl group(s) are reacted with isocyanates. As is known in the art, isocyanate reactions are promoted by ultraviolet light or by catalysts such as e.g., dibutyltin dilaurate or bismuth octanoate by methods known in the art (see e.g., Y. Li et al., Bio-based Polyols and Polyurethanes, Springer Briefs in Green Chemistry for Sustainability, DOI 10.1007/978-3-319-21539-6_2). Many different isocyanates, ranging from linear to aromatic, may be used; and techniques for preparing the polymer may or may not go through a pre-polymer phase, for instance prepping the available hydroxy groups, triol, or polyol with isocyanate groups (see e.g., U.S. Pat. No. 4,532,316). The available hydroxy groups of the multifunctional molecules disclosed herein may first be derivatized, for example by co-polymerizing with ethylene oxide by methods known in the art (see e.g., Anionic Polymerization: Principles, Practice, Strength, Consequences, Springer (2015) Nikos Hadjichristidis, Akira Hirao Eds.) thereby providing polyether polyols. The resulting polyether polyols may be used as-is in various applications, e.g., as building blocks of polyurethanes. Multifunctional molecules with mixed functionalities, for instance both hydroxyl and carboxylic groups, provide building blocks for copolymers, e.g., polyester polyurethanes. 
     In other embodiments certain specific arrangements of two or more hydroxyl groups in the multifunctional molecules disclosed herein provide chemical advantages in producing non-isocyanate polyurethanes. In particular, in exemplary embodiments a 1,3-hydroxy arrangement, for example as illustrated by 1,3,12-triol, is reacted with dimethyl carbonate or carbon dioxide to prepare a 6-membered cyclic carbonate ring to provide a molecule according to Formula XCII. 
     
       
         
         
             
             
         
       
     
     The resulting 6-membered cyclic carbonate has a 30x reactivity versus a 5-membered cyclic carbonate from a 1,2-hydroxy moiety and is thus preferable in use (Maisonneuve et al, Chem. Rev., 2015). Catalysts useful for the preparation of carbonate derivatives on the hydroxyl groups of multifunctional molecules are readily selected by a person having ordinary skill in the art. Exemplary catalysts include e.g., 1,5,7-triazabicyclo[4.4.0]dec-5-ene with dimethyl carbonate (see e.g., Mutlu et al, Green Chem., 2012 pp. 1728-1735); various imidazolium or thiazolium carbene catalysts in the presence of cesium carbonate, dibromomethane, and CO 2  at atmospheric pressure (see e.g., Bobbink et al, Chem. Commun., 2016,52, 10787-10790); and CeO 2  with 2-cyanopyridine in the presence of CO 2  (see e.g., Honda et al, ACS Catal., 2014). 
     In exemplary embodiments, selective protection of the 1,3-hydroxy portion of the 1,3,12-triol allows for further chemistry on the C12 (terminal) hydroxyl group. Thus, for example, standard chemical conversion of the C12 OH group to an amine group in an alkylation with ammonia (see e.g., Bahn et al., ChemCatChem, 2011 pp. 1853-1864) is used. The resulting 1,3-carbonate and 12-amine provides a molecule according to Formula XCIII, which in exemplary embodiments, is self-polymerized as a non-isocyanate polyurethane. 
     
       
         
         
             
             
         
       
     
     Non-isocyanate polyurethanes are useful to the world because they allow the performance and properties of polyurethanes, used in such diverse applications from construction materials to medical devices, produced without the use of carcinogenic isocyanates. This enables safer working conditions for producers, commercial users, and even everyday consumers who may be exposed when using polyurethane products such as coatings and adhesives. It also has potential benefits of reducing environmental isocyanate exposure due to spills and waste removal. 
     The 1,3-hydroxy arrangement in the 1,3,12-triol has the advantage over 1,2-hydroxy arrangement in analogous structures in that there is less steric hindrance by the alcohol reaction centers. The derivatization of all three hydroxy groups on the 1,3,12-triol creates unusual branched structures—“three pointed stars”—that can form networks in solutions and polymer solids. 
     The 1,3,12-triol itself, or derivatives, may be useful in metal-ion chelation, useful in applications such as water treatment and catalyst development. 
     The arrangement of hydroxyl groups on the 1,3,12-triol molecule gives three places of hydrogen bonding, which in turn has implications for applied uses. For instance, it was observed that the 1,3,12-triol when mixed with 2-ethyl hexanol at a 60:40 triol:solvent ratio created a gel-like material that solidified. This thickening property is anticipated to act across a variety of solvents, at least with similar hydrogen bonding capability or dipole moment, and even in aqueous formulations. Thickening properties are useful in personal care formulations (such as lotions and shampoos), oil field applications (recovery methods), home and industrial cleaning products, and potential other fuel (semi-solid fuels) and industrial uses (low-volatiles cleaning, solid lubricants, etc.). 
     The 1,3,12-triol as-is or derivatized with polar groups may have further applications beyond thickening. In personal care applications, the 1,3,12-triol or its water-soluble derivatives may act as a humectant (retaining moisture on the skin) and as surface active ingredient for emulsifying and gentle cleaning. Gentle cleaning has the aim of removal of pollutive particles, external residues, excess oils, dead cell debris, and disruptive microbes without “stripping” the skin of protective oils and ceramides. In oil field recovery, surfactants with differentiated interfacial tension properties can help efficiently recover oil in conditions of high salinity and low temperatures (see e.g., Iglauer et al., Colloids and Surfaces A: Physiochemical and Engineering Aspects, 2009). Examples of derivatizing the 1,3,12-triol include water-soluble polyurethanes using standard polyurethane chemistries as described above; polyglycosides where mono-, di-, or polysaccharides are bound to one or more of the oxygens from the 1,3,12-triol; ethoxylation of the primary or all alcohols of the triol; or polyethylene glycol groups added to the alcohols of the 1,3,12-triol. 
     Chemistries for forming polyesters are well known in the art (see e.g., van der Ende, A. et al (2010) Macromolecules, 2010, 43 (13), pp 5665-5671 ; Modern Polyesters: Chemistry and Technology of Polyesters and Copolyesters , John Wiley &amp; Sons, (2005) John Scheirs, Timothy E. Long Eds.) Exemplary chemistries include, but are not limited to, reactions catalyzed by heat and acid; lipase enzyme catalyzed polycondensation; the use of scandium triflates as catalysts, etc (see e.g., Diaz, A. et al., Macromolecules 2005, 38, 1048-1050). 
     In exemplary embodiments, 1,3,12-triol is reacted with diacids such as adipic acid to form “brush” polyesters (see e.g., W. Chen, et al. Macromolecules, 2017, 50 (11), pp 4089-4113). The resulting “brush” polyester from 1,3,12-triol have less crystallinity and, if highly networked, potentially more strength, rigidity, solvent-resistance, and scratch resistance than a polyester produced with alpha-omega diols. 
     In other exemplary embodiments, the 1,3,12-triol is a starting intermediate for differentiated performance properties in a wide variety of polymer applications. For example a multifunctional molecule e.g., 1,3,12-triol, is used in controlled mixed hydrophobic-hydrophilic copolymers for the creation of reverse micelles and dendrimer structures with highly specialized chelating and drug-delivery applications. 
     II. Preparation of Multi-functional Fatty Acid Derivative Molecules 
     1. Introduction 
     Multi-functional molecules can be made by any method known in the art. Typically, multifunctional molecules are prepared from petrochemicals or oleochemicals, but such routes for preparation and synthesis of multifunctional molecules have many disadvantages and limitations. In particular, the synthesis of medium- to long-chain hydrocarbons (C 8  to C 16 ) with multiple hydroxy(—OH), oxo (=O), amino-(-NH 2 ) or carboxyl (CO 2 H) groups in selective positions is extremely difficult and in many cases impractical starting from petrochemical feedstock. 
     Therefore, multifunctional molecules as disclosed herein are typically made using recombinant host cells e.g., using microbes e.g., bacterial cells, yeast cells, etc. that are engineered to produce multi-functional fatty acid derivative molecules. Accordingly, as disclosed herein, recombinant host cells are engineered and constructed to utilize nucleic acids and their corresponding polypeptides of enzymatic function in order to provide heterologous enzyme pathways for the in vivo production of the multifunctional fatty acid derivatives disclosed herein. Petrochemical or oleochemical feedstocks are not required, as the disclosed recombinant microbes use simple carbon sources to produce multifunctional fatty acid derivatives having desired carbon chain lengths and having specific functional groups placed in specific positions. 
     Therefore, in exemplary embodiments, the disclosed recombinant microbes use simple carbon sources to produce multifunctional fatty acid derivatives having specific functional groups placed in specific positions. In one exemplary embodiment, the disclosed recombinant microbes use simple carbon sources to produce multifunctional fatty acid derivatives having carbon chain lengths of ten (10) carbons to sixteen (16) carbons in length and having specific functional groups placed in specific positions (see e.g., Scheme 1, supra). In other exemplary embodiments, the disclosed recombinant microbes use simple carbon sources to produce multifunctional fatty acid derivatives having carbon chain lengths of between ten (10) carbons and sixteen (16) carbons in length and having functional groups placed in specific positions. 
     As will be discussed in detail below, the biosynthesis of multifunctional fatty acid derivatives takes advantage of the ability of the microbes fatty acid biosynthesis machinery to incorporate oxygen into medium to long carbon chains during fatty acid biosynthesis. In addition, oxygen molecules, e.g., hydroxyl groups, are incorporated into medium- to long-chain fatty acid derivatives by certain hydroxylases (also known as oxygenases) and hydratases. The hydroxylation reactions are usually regio- and stereo-selective thereby providing multifunctional fatty acid derivatives with chiral hydroxyl groups (R or S) in specific positions. 
     In exemplary embodiments, the incorporated hydroxyl groups are converted to other functional groups by employing additional enzymes to convert these hydroxyl groups into other functional groups, e.g. oxo (CHO), carboxyl (CO 2 H), amino (CH 2 NH 2 ), O-acetyl (CO 2 C 2 H 3 ), methoxy (COCH 3 ) or ester (CO 2 C 2 H 5 , CO 2 C 3 H 7 ) groups. 
     Enzymes useful for making converting incorporated hydroxyl groups to other functional groups are disclosed herein below in Table 5. 
     Typically, the carbon chain length of the multifunctional molecules disclosed herein is between 8 and 16 carbons. In exemplary embodiments, the carbon chain (or equivalently, acyl chain) length of the multifunctional molecules disclosed herein is between 10 and 16 carbons. In exemplary embodiments, the multifunctional molecules disclosed herein comprise one double bond in either cis-(Z) or trans-(E) configuration. When the double bond is not terminal, the double bond is in the omega-7 (ω-7) position. 
     2. Host Cells and Host Cell Cultures 
     In view of the present disclosure, the person having ordinary skill in the art will appreciate that any of the embodiments contemplated herein may be practiced with any host cell or microorganism that can be genetically modified via the introduction of one or more nucleic acid sequences that code for the appropriate fatty acid biosynthetic enzymes. Accordingly, the recombinant microorganisms disclosed herein function as host cells and comprise one or more polynucleotide sequences that include an open reading frame that encode one or more fatty acid biosynthetic enzymes together with operably-linked regulatory sequences that facilitate expression of the fatty acid biosynthetic polypeptide(s) in the host cell. 
     Exemplary microorganisms that provide suitable host cells, include but are not limited to cells from the genus  Escherichia, Bacillus, Lactobacillus, Zymomonas, Rhodococcus, Pseudomonas, Aspergillus, Trichoderma, Neurospora, Fusarium, Humicola, Rhizomucor, Kluyveromyces, Pichia, Mucor, Myceliophtora, Penicillium, Phanerochaete, Pleurotus, Trametes, Chrysosporium, Saccharomyces, Stenotrophamonas, Schizosaccharomyces, Yarrowia , or  Streptomyces . In some exemplary embodiments, the host cell is a Gram-positive bacterial cell. In other exemplary embodiments, the host cell is a Gram-negative bacterial cell. In some embodiments, the host cell is an  E. coli  cell. In other exemplary embodiments, the host cell is a  Bacillus lentus  cell, a  Bacillus brevis  cell, a  Bacillus stearothermophilus  cell, a  Bacillus  lichenoformis cell, a  Bacillus alkalophilus  cell, a  Bacillus coagulans  cell, a  Bacillus circulans  cell, a  Bacillus pumilis  cell, a  Bacillus thuringiensis  cell, a  Bacillus clausii  cell, a  Bacillus megaterium  cell, a  Bacillus subtilis  cell, or a  Bacillus amyloliquefaciens  cell. 
     In still other exemplary embodiments, the host cell is a  Trichoderma koningii  cell, a  Trichoderma viride  cell, a  Trichoderma reesei  cell, a  Trichoderma longibrachiatum  cell, an  Aspergillus awamori  cell, an  Aspergillus  fumigates cell, an  Aspergillus foetidus  cell, an  Aspergillus nidulans  cell, an  Aspergillus niger  cell, an  Aspergillus oryzae  cell, a  Humicola insolens  cell, a  Humicola lanuginose  cell, a  Rhodococcus opacus  cell, a  Rhizomucor miehei  cell, or a  Mucor michei  cell. In still other exemplary other embodiments, the host cell is a  Streptomyces lividans  cell or a  Streptomyces murinus  cell. In yet other embodiments, the host cell is an Actinomycetes cell. In some exemplary embodiments, the host cell is a  Saccharomyces cerevisiae  cell. 
     In still other exemplary embodiments, the host cell is a cell from a eukaryotic plant, algae, cyanobacterium, green-sulfur bacterium, green non-sulfur bacterium, purple sulfur bacterium, purple non-sulfur bacterium, extremophile, yeast, fungus, engineered organisms thereof, or a synthetic organism. In some exemplary embodiments, the host cell is a cell from  Arabidopsis thaliana, Panicum virgatums, Miscanthus giganteus, Zea mays, Botryococcuse braunii, Chalamydomonas reinhardtii, Dunaliela salina, Thermosynechococcus elongatus, Synechococcus elongatus , Synechococcus sp.,  Synechocystis  sp.,  Chlorobium tepidum, Chloroflexus auranticus, Chromatiumm vinosum, Rhodospirillum rubrum, Rhodobacter capsulatus, Rhodopseudomonas palusris, Clostridium ljungdahlii, Clostridiuthermocellum , or  Pencillium chrysogenum . In some other exemplary embodiments, the host cell is from  Pichia pastories, Saccharomyces cerevisiae, Yarrowia lipolytica, Schizosaccharomyces pombe, Pseudomonas fluorescens, Pseudomonas putida  or  Zymomonas mobilis . In still further exemplary embodiments, the host cell is a cell from  Synechococcus  sp. PCC 7002 , Synechococcus  sp. PCC 7942, or  Synechocystis  sp. PCC6803. In some exemplary embodiments, the host cell is a CHO cell, a COS cell, a VERO cell, a BHK cell, a HeLa cell, a Cvl cell, an MDCK cell, a 293 cell, a 3T3 cell, or a PC12 cell. In some exemplary embodiments, the host cell is an  E. coli  cell. In some exemplary embodiments, the  E. coli  cell is a strain B, a strain C, a strain K, or a strain W  E. coli  cell. 
     a. Expression of Heterologous Enzymatic Activities in Microorganisms 
     The expression of enzymatic activities in microorganisms and microbial cells for the production of fatty acid derivative molecules is taught e.g., in the following U.S. Pat. Nos. 9,133,406; 9,340,801; 9,200,299; 9,068,201; 8,999,686; 8,658,404; 8,597,922; 8,535,916; 8,530,221; 8,372,610; 8,323,924; 8,313,934; 8,283,143; 8,268,599; 8,183,028; 8,110,670; 8,110,093; and 8,097,439. 
     Therefore, in exemplary embodiments, the host cells or host microorganisms that are used to express polypeptides for biosynthesis of multifunctional fatty acid derivative molecules express heterologous thioesterase activity (E.C. 3.1.2.14, EC 3.1.2.20, etc.) for the production of fatty acids. 
     In other exemplary embodiments, the host cells or host microorganisms that are used to express polypeptides for biosynthesis of multifunctional fatty acid derivative molecules express ester synthase activity (E.C. 2.3.1.75) for the production of fatty esters. In another exemplary embodiment, the host cell has ester synthase activity (E.C. 2.3.1.75) and acyl-CoA synthase (FadD) (E.C. 6.2.1.3) activity for the production of fatty esters. 
     In another exemplary embodiment, the host cell has acyl-ACP reductase (AAR) (E.C. 1.2.1.80) activity and/or alcohol dehydrogenase activity (E.C. 1.1.1.1.) and/or fatty alcohol acyl-CoA reductase (FAR) (E.C. 1.1.1.-) activity and/or carboxylic acid reductase (CAR) (EC 1.2.99.6) activity for the production of fatty alcohols. In another exemplary embodiment, the host cell has acyl-CoA reductase (E.C. 1.2.1.50) activity, and acyl-CoA synthase (FadD) (E.C. 6.2.1.3) activity, for the production of fatty alcohols. In another exemplary embodiment, the host cell has acyl-ACP reductase (AAR) (E.C. 1.2.1.80) activity and alcohol dehydrogenase activity (E.C. 1.1.1.1.) for the production of fatty alcohols. 
     In another exemplary embodiment, the host cell has acyl-ACP reductase (AAR) (E.C. 1.2.1.80) activity for the production of fatty aldehydes. In another exemplary embodiment, the host cell has acyl-ACP reductase (AAR) (E.C. 1.2.1.80) activity and decarbonylase activity (aldehyde forming oxygenase) for the production of alkanes and alkenes. 
     In another exemplary embodiment, the host cell has OleA activity for the production of ketones. In another exemplary embodiment, the host cell has OleBCD activity for the production of internal olefins. In another exemplary embodiment, the host cell has decarboxylase activity for making terminal olefins. 
     In some exemplary embodiments, host cells or microorganisms that are used to express polypeptides for biosynthesis of multifunctional fatty acid derivative molecules comprise certain native enzyme activities that are upregulated or overexpressed in order to produce one or more particular fatty acid derivative(s) such as e.g., fatty esters, fatty alcohols, fatty amines, fatty aldehydes, bifunctional fatty acid derivatives, diacids, etc. 
     Typically, the multifunctional fatty acid derivatives disclosed herein are recovered from the culture medium and/or are isolated from the host cells. In one exemplary embodiment, the multifunctional fatty acid derivatives are recovered from the culture medium (extracellular). In another exemplary embodiment, the multifunctional fatty acid derivatives are isolated from the host cells (intracellular). In another exemplary embodiment, the multifunctional fatty acid derivatives are recovered from the culture medium and isolated from the host cells. 
     A fatty acid derivative composition produced by a host cell can be analyzed using methods known in the art, for example, Gas-Chromatography with Flame Ionization Detection (GC-FID) in order to determine the distribution of particular multifunctional fatty acid derivatives as well as chain lengths and degree of saturation of the components of the fatty acid derivative composition. Similarly, other compounds can be analyzed through methods well known in the art. 
     b. Genetic Alterations for Fine Tuning Recombinant Host Cells 
     In some exemplary embodiments, host cells comprise optional genetic manipulations and alterations can be used to enhance or otherwise fine tune the production of multifunctional fatty acid derivative molecules. As will be appreciated by a person having ordinary skill in the art, optional genetic manipulations can be used interchangeably from one host cell to another, depending on what other heterologous enzymes and what native enzymatic pathways are present in the host cell. Some optional genetic manipulations are discussed below. 
     FadE 
     FadE (Acyl-CoA dehydrogenase) catalyzes the first step the first step in fatty acid utilization/degradation (p-oxidation cycle) which is the oxidation of acyl-CoA to 2-enoyl-CoA (see e.g., Campbell, J. W. and Cronan, J. E. Jr (2002) J. Bacteriol. 184(13): 3759-3764, Lennen, R. M. and Pfleger, B. F (2012) Trends Biotechnol. 30(12):659-667). Since fadE initiates the p-oxidation cycle, when  E. coli  lacks FadE, it cannot grow on fatty acids as a carbon source (see e.g., Campbell, J. W. and Cronan supra). 
     However, when  E. coli  is grown on a carbon source other than fatty acids e.g., grown on sugar, acetate, etc., fadE attenuation is optional because under such conditions fadE expression is repressed by FadR. Therefore, when cells are grown on a simple carbon source such as e.g., glucose, the fadE gene product is already attenuated. Accordingly, when grown on a carbon source other than fatty acids, a fadE mutation/deletion is optional. 
     fhuA 
     The gene fhuA codes for the TonA protein, which is an energy-coupled transporter and receptor in the outer membrane of  E. coli  (see e.g., V. Braun (2009) J Bacteriol. 191(11):3431-3436). The fhuA deletion allows the cell to become more resistant to phage attack. This phenotype can be beneficial in certain fermentation conditions. Its deletion is optional. 
     entD 
     For example, the entD gene codes for a phosphopantetheinyl transferase. Overexpression of native  E. coli  entD, a phosphopantetheinyl transferase, enables the activation of CarB from apo-CarB to holo-CarB, thereby allowing conversion of free fatty acids into fatty aldehydes, which can then be converted to fatty alcohols by a fatty aldehyde reductase see e.g., U.S. Pat. No. 9,340,801. 
     Overexpression of Non-Native and/or Native and/or Variants of Genes Involved in the Synthesis of Acyl-ACP 
     In some embodiments, the fatty acid biosynthetic pathway in the production host uses the precursors acetyl-CoA and malonyl-CoA.  E. coli  or other host organisms engineered to overproduce these components can serve as the starting point for subsequent genetic engineering steps to provide the specific output product (such as, fatty acids, fatty esters, hydrocarbons, fatty alcohols). Several different modifications can be made, either in combination or individually, to the host strain to obtain increased acetyl-CoA/malonyl-CoA/fatty acid and fatty acid derivative production see e.g., US Patent Application Publication 2010/0199548. 
     Other exemplary modifications of a host cell include e.g., overexpression of non-native and/or native and/or variants of genes involved in the synthesis of acyl-ACP. In general, by increasing acyl-ACP synthesis increases the amount of acyl-ACP, which is the substrate of thioesterases, estersynthases and acyl-ACP reductases. Exemplary enzymes that increase acyl-ACP production include e.g., enzymes that make up the “fatty acid synthase” (FAS). As is known in the art (see e.g., US 2010/0199548) FAS enzymes are a group of enzymes that catalyze the initiation and elongation of acyl chains. The acyl carrier protein (ACP) along with the enzymes in the FAS pathway control the length, degree of saturation, and branching of the fatty acids produced. Enzymes that comprise FAS include e.g., AccABCD, FabD, FabH, FabG, FabA, FabZ, FabI, FabK, FabL, FabM, FabQ, FabV, FabX,FabB, and FabF. Depending upon the desired product one or more of these genes can be attenuated or over-expressed. 
     Therefore, in exemplary embodiments a host strain may overexpress of one or more of the FAS genes. Exemplary FAS genes that may be overexpressed include e.g., fadR from  Escherichia coli  (NP_415705.1) fabA from  Salmonella typhimurium  (NP_460041), fabD from  Salmonella typhimurium  (NP_460164), fabG from  Salmonella typhimurium  (NP_460165), fabH from  Salmonella typhimurium  (NP_460163), fabV from  Vibrio cholera  (YP_001217283), and fabF from  Clostridium acetobutylicum  (NP_350156). In some exemplary embodiments, the overexpression of one or more of these genes, which code for enzymes and regulators in fatty acid biosynthesis, serves to further increase the titer of fatty-acid derivative compounds under particular culture conditions. In some exemplary embodiments, the wild-type  E. coli  strains MG1655 or W3110 (see e.g., Blattner, et al. (1997) 277(5331): 1453-1462; Jensen, K. F. (1993)  J. Bact.,  175(11): 3401-3407) are used as host strains. 
     3. Methods of Making Recombinant Host Cells and Cultures 
     Any method known in the art can be used to engineer host cells to produce fatty acid derivatives and/or fatty acid derivative compositions or other compounds. Methods for engineering host cells are well known in the art and are readily appreciated and accessible to the skilled practitioner. See e.g., Sambrook et al. (supra); Current Protocols in Molecular Biology (supra). 
     Generally, a polynucleotide (or gene) sequence is provided to the host cell by way of a recombinant vector that comprises a promoter operably linked to the fatty acid biosynthetic polynucleotide sequence of interest. Once a polynucleotide sequence(s) encoding fatty acid biosynthetic pathway polypeptide has been prepared and isolated, various methods may be used to construct expression cassettes, vectors and other DNA constructs. The skilled artisan is well aware of the genetic elements that must be present on an expression construct/vector in order to successfully transform, select and propagate the expression construct in host cells. Techniques for manipulation of nucleic acids such as subcloning nucleic acid sequences into expression vectors, labeling probes, DNA hybridization, and the like are described generally in e.g., Sambrook, et al., supra; Current Protocols in Molecular Biology, supra. 
     A number of recombinant vectors are available to those of skill in the art for use in the stable transformation/transfection of bacteria and other microorganisms (see e.g., Sambrook, et al., supra). Appropriate vectors are readily chosen by one of skill in the art. 
     Once an appropriate vector is identified and constructed, the appropriate transformation technique is readily chosen by the skilled practitioner. Exemplary transformation/transfection methods available to those skilled in the art include e.g., electroporation, calcium chloride transformation and etc., such methods being well known to the skilled artisan (see e.g., Sambrook, supra). In exemplary embodiments, polynucleotide sequences, comprising open reading frames encoding proteins and operably-linked regulatory sequences can be integrated into a chromosome of the recombinant host cells, incorporated in one or more plasmid expression system resident in the recombinant host cells, or both. 
     As will be appreciated by those skilled in the art, the design of the expression vector can depend on such factors as e.g., the choice of the host cell to be transformed, the level of expression of polypeptide desired, etc. 
     4. Recombinant Microbes Comprising a Heterologous Enzyme Pathway Capable of Producing Bifunctional Fatty Acid Derivative Molecules for the Production of Multifunctional Fatty Acid Derivative Molecules 
     As discussed above, a recombinant host cell comprising heterologous fatty acid biosynthetic polypeptides is used to produce particular types of multifunctional fatty acid derivatives. Thus, in some exemplary embodiments, the disclosure provides recombinant microbes that comprise heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative molecule and at least one heterologous hydroxylating enzyme. Therefore, in exemplary embodiments, a method for preparing a multifunctional molecule comprises: growing a recombinant microbe that comprises a heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative molecule and at least one heterologous hydroxylating enzyme in a culture medium that comprises a simple carbon source. 
     Exemplary disclosures that provide microbial strains that that comprise heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative molecule are known in the art see e.g., U.S. Patent Application Publication No. 2016/0130616 (LS48); U.S. Patent Application Publication No. 2017/0204436 (LS52); U.S. Patent Application Publication No. 2014/0215904 (LS35 β-OH esters), etc. 
     Some exemplary heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative molecule are illustrated in  FIG. 1  and  FIG. 2 . In  FIG. 1  and  FIG. 2  one of skill in the art can see that if a pathway capable of producing a bifunctional fatty acid derivative molecule is combined with one additional hydroxylating enzyme, a trifunctional fatty acid derivative is produced. Furthermore, if a pathway capable of producing a bifunctional fatty acid derivative molecule is combined with further hydroxylating enzymes, then tetrafunctional fatty acid derivatives are produced. In some embodiments, tetrafunctional fatty acid derivatives are also produced if a pathway from  FIG. 1  and/or  FIG. 2  includes a hydroxylase that can hydroxylate in two different positions. 
     In particular, in exemplary embodiments, a recombinant host cell comprising heterologous enzyme pathway capable of producing a bifunctional fatty acid derivative molecules produces 3-hydroxy fatty acids from 3-hydroxy acyl-ACPs. See e.g.,  FIG. 1A . Addition of at least one heterologous hydroxylating enzyme to the recombinant host cell provides a host cell that, when grown on a simple carbon source produces multifunctional fatty acid derivative molecules. 
     In other exemplary embodiments, a recombinant host cell comprising heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative produces 3-hydroxy fatty esters from 3-hydroxy acyl-ACPs. See e.g.,  FIG. 1B . Addition of at least one heterologous hydroxylating enzyme to the recombinant host cell provides a host cell that, when grown on a simple carbon source produces multifunctional fatty acid derivative molecules. 
     In still other exemplary embodiments, a recombinant host cell comprising heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative produces 1,3-fatty diols from 3-hydroxy acyl-ACPs. See e.g.,  FIG. 1C . Addition of at least one heterologous hydroxylating enzyme to the recombinant host cell provides a host cell that, when grown on a simple carbon source produces multifunctional fatty acid derivative molecules. 
     In still other exemplary embodiments, a recombinant host cell comprising heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative produces hydroxy-fatty acids from fatty acids. See e.g.,  FIG. 2A . Addition of at least one heterologous hydroxylating enzyme to the recombinant host cell provides a host cell that, when grown on a simple carbon source produces multifunctional fatty acid derivative molecules. 
     In still other exemplary embodiments, a recombinant host cell comprising heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative produces hydroxy-fatty esters from a fatty esters. See e.g.,  FIG. 2B . Addition of at least one heterologous hydroxylating enzyme to the recombinant host cell provides a host cell that, when grown on a simple carbon source produces multifunctional fatty acid derivative molecules. 
     In still other exemplary embodiments, a recombinant host cell comprising heterologous enzyme pathway(s) capable of producing a bifunctional fatty acid derivative produces fatty diols from fatty alcohols. See e.g.,  FIG. 2C . Addition of at least one heterologous hydroxylating enzyme to the recombinant host cell provides a host cell that, when grown on a simple carbon source produces multifunctional fatty acid derivative molecules. 
     If a pathway from  FIG. 1  or  FIG. 2  is combined with an additional hydroxylating enzyme e.g., a hydroxylase or a hydratase, then tetrafunctional fatty acid derivatives with four functional groups are produced. Tetrafunctional fatty acid derivatives can also be produced if a pathway from  FIG. 1  and  FIG. 2  includes a hydroxylase that can hydroxylate in two different positions. 
     Although  FIG. 1  and  FIG. 2  depict the enzymatic hydroxylation as the last step of the biochemical pathway, hydroxylation can occur at an earlier step of the pathways, e.g. in  FIG. 1C  the 3OH fatty acid intermediate may be hydroxylated before it is converted to a fatty alcohol by carboxylacid reductase (CAR). 
     a. Multifunctional Fatty Acid Derivatives from 3-Hydroxy Fatty Acids 
       FIG. 1A  illustrates and exemplary pathway for the production of multifunctional fatty acid derivative molecules from 3-hydroxy-acyl-ACPs (3OH-acyl-ACPs) via 3-hydroxy fatty acids. Thus, in addition to a heterologous biochemical pathway that generates 3-hydroxy fatty acids a recombinant cell need only comprise one additional hydroxylating enzyme to synthesize a trifunctional fatty acid derivative. 
     Thus, in exemplary embodiments, a recombinant microbe that expresses a heterologous biochemical pathway comprising a thioesterase, and at least one hydroxylating enzyme, produces multifunctional fatty acid molecules. Suitable thioesterases include any polypeptides that, when expressed in a microorganism in the presence of a carbon source, catalyze the production of fatty acids including 3-hydroxy fatty acids, e.g., enzymes having an Enzyme Commission number (EC 3.1.2.). Exemplary thioesterases include e.g., FatB1 from  Umbellularia californica  (Q41635) or PhaG from  Pseudomonas putida  (AAN67031). 
     Therefore in an exemplary embodiment, a recombinant microbe comprising a thioesterase such as FatB1 from  Umbellularia californica  and an ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecules 3,10-dihydoxy decanoic acid, 3,12-dihydoxy dodecanoic acid, 3,14-dihydoxy tetradecanoic acid, (z5)3,12-dihydoxy dodecenoic acid and (z7)3,14-dihydoxy tetradecanoic acid when the recombinant microbe is grown on a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe expressing a heterologous biochemical pathway comprising an ester synthase such as FatB1 from  Umbellularia californica  and a “subterminal” hydroxylase such as cyp102A from a  Bacillus  produces the trifunctional molecules 3,9-dihydoxy dodecanoic acid; 3,8-dihydoxy dodecanoic acid; 3,7-dihydoxy decanoic acid; 3,11-dihydoxy dodecanoic acid; 3,10-dihydoxy dodecanoic acid; 3,9-dihydoxy dodecanoic acid; 3,13-dihydoxy tetradecanoic acid; 3,12-dihydoxy tetradecanoic acid; 3,11-dihydoxy tetradecanoic acid; (z5)3,11-dihydoxy dodecenoic acid; (z5)3,10-dihydoxy dodecenoic acid; (z5)3,9-dihydoxy dodecenoic acid; (z7)3,13-dihydoxy tetradecenoic acid; (z7)3,12-dihydoxy tetradecenoic acid; (z7)3,11-dihydoxy tetradecenoic acid, when the recombinant microbe is grown on a simple carbon source. 
     b. Multifunctional Fatty Acid Derivatives from 3-Hydroxy Fatty Esters 
       FIG. 1B  shows biochemical pathways that convert 3-hydroxy-acyl-ACPs (3OH-acyl-ACPs) into trifunctional fatty acid derivatives via 3-hydroxy fatty methyl or ethyl esters. Thus, in addition to a heterologous biochemical pathway that generates 3-hydroxy fatty methyl or ethyl esters a recombinant cell need only comprise one additional hydroxylating enzyme to synthesize a trifunctional fatty acid derivative. 
     Thus, in exemplary embodiments, a recombinant microbe that expresses a heterologous biochemical pathway comprising an ester synthase and at least one hydroxylating enzyme, produces multifunctional fatty acid ester molecules. Suitable ester synthases include any polypeptides that, when expressed in a microorganism in the presence of a carbon source and an alcohol, catalyze the production of fatty esters, e.g., fatty acid methyl and ethyl esters, including 3-hydroxy esters e.g., enzymes having an Enzyme Commission number (EC 2.3.1.75). Exemplary ester synthases include e.g., ester synthase polypeptide, such as e.g., ES9, a wax ester synthase from  Marinobacter hydrocarbonoclasticus  DSM 8798 (UniProtKB A3RE51, GenBank AB021021, see e.g., U.S. Pat. No. 8,530,221, PCT Publication WO2011038132, U.S. Pat. No. 9,133,406), or ES376 (another wax ester synthase from  Marinobacter hydrocarbonoclasticus  DSM 8798). 
     Therefore in an exemplary embodiment, a recombinant microbe comprising an ester synthase such as ES9 and a ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecules 3,12-dihydoxy dodecanoic acid methyl ester, 3,14-dihydoxy tetradecanoic acid methyl ester, 3,16-dihydoxy hexadecanoic acid methyl ester, (z5)3,12-dihydoxy dodecenoic acid methyl ester, (z7)3,14-dihydoxy tetradecanoic acid methyl ester and (z9)3,16-dihydoxy hexadecanoic acid methyl ester when the recombinant microbe is grown on a simple carbon source with methanol added. 
     In another exemplary embodiment, a recombinant microbe expressing a heterologous biochemical pathway comprising an ester synthase such as ES9 from  Marinobacter hydrocarbinoclasticus  and an ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecules 3,12-dihydoxy dodecanoic acid ethyl ester, 3,14-dihydoxy tetradecanoic acid ethyl ester, 3,16-dihydoxy hexadecanoic acid ethyl ester, (z5)3,12-dihydoxy dodecenoic acid ethyl ester, (z7)3,14-dihydoxy tetradecanoic acid ethyl ester and (z9)3,16-dihydoxy hexadecanoic acid ethyl ester when the recombinant microbe is grown on a simple carbon source with ethanol added. 
     In another exemplary embodiment, a recombinant microbe expressing a heterologous biochemical pathway comprising an ester synthase such as ES9 from  Marinobacter hydrocarbinoclasticus  and a “subterminal” hydroxylase such as cyp102A from  Bacillus licheniformis  produces the trifunctional molecules 3,11-dihydoxy dodecanoic acid methyl ester, 3,10-dihydoxy dodecanoic acid methyl ester, 3,9-dihydoxy dodecanoic acid methyl ester, 3,13-dihydoxy tetradecanoic acid methyl ester, 3,12-dihydoxy tetradecanoic acid methyl ester, 3,11-dihydoxy tetradecanoic acid methyl ester, 3,15-dihydoxy hexadecanoic acid methyl ester, 3,14-dihydoxy hexadecanoic acid methyl ester, 3,13-dihydoxy hexadecanoic acid methyl ester, (z5)3,11-dihydoxy dodecenoic acid methyl ester, (z5)3,10-dihydoxy dodecenoic acid methyl ester, (z5)3,9-dihydoxy dodecenoic acid methyl ester, (z7)3,13-dihydoxy tetradecenoic acid methyl ester, (z7)3,12-dihydoxy tetradecenoic acid methyl ester, (z7)3,11-dihydoxy tetradecenoic acid methyl ester, (z9)3,15-dihydoxy hexadecenoic acid methyl ester, (z9)3,14-dihydoxy hexadecenoic acid methyl ester, (z9)3,13-dihydoxy hexadecenoic acid methyl ester when the recombinant microbe is grown on a simple carbon source and methanol is added. 
     For example, a recombinant microbe that expresses a heterologous biochemical pathway comprising an ester synthase such as ES9 from  Marinobacter hydrocarbinoclasticus  and a “subterminal” hydroxylase such as cyp102A from  Bacillus lichenformis  produces the trifunctional molecules 3,11-dihydoxy dodecanoic acid ethyl ester, 3,10-dihydoxy dodecanoic acid ethyl ester, 3,9-dihydoxy dodecanoic acid ethyl ester, 3,13-dihydoxy tetradecanoic acid ethyl ester, 3,12-dihydoxy tetradecanoic acid ethyl ester, 3,11-dihydoxy tetradecanoic acid ethyl ester, 3,15-dihydoxy hexadecanoic acid ethyl ester, 3,14-dihydoxy hexadecanoic acid ethyl ester, 3,13-dihydoxy hexadecanoic acid ethyl ester, (z5)3,11-dihydoxy dodecenoic acid ethyl ester, (z5)3,10-dihydoxy dodecenoic acid ethyl ester, (z5)3,9-dihydoxy dodecenoic acid ethyl ester, (z7)3,13-dihydoxy tetradecenoic acid ethyl ester, (z7)3,12-dihydoxy tetradecenoic acid ethyl ester, (z7)3,11-dihydoxy tetradecenoic acid ethyl ester, (z9)3,15-dihydoxy hexadecenoic acid ethyl ester, (z9)3,14-dihydoxy hexadecenoic acid ethyl ester, (z9)3,13-dihydoxy hexadecenoic acid ethyl ester when the recombinant microbe is grown on a simple carbon source and ethanol is added. 
     c. Multifunctional Fatty Acid Derivatives from 1,3-Fatty Diols 
       FIG. 1C  illustrates biochemical pathways for the conversion of 3-hydroxy-acyl-ACPs into trifunctional fatty acid derivatives via 1,3 fatty diols. 
     Methods for the production of 1,3-fatty diols are known in the art (see e.g., US Patent Application Publication 2017/0204436). As will be shown below, the addition of only one additional hydroxylating enzyme provides for the synthesis of trifunctional fatty acid derivatives. Further combination with another hydroxylating enzyme e.g., a hydroxylase or hydratase, produces tetrafunctional fatty acid derivatives with four functional groups. Tetrafunctional fatty acid derivatives can also be produced if a pathway includes a hydroxylase that can hydroxylate in two different positions. 
     Thus, in an exemplary embodiment, a recombinant microbe expressing a heterologous a biochemical pathway that converts 3-hydroxy-acyl-ACPs into trifunctional fatty acid derivatives via 1,3 fatty diols comprises a thioesterase such as FatB1 from  Umbellularia californica , a carboxylic acid reductase such as CarB from  Mycobacterium smegmatis , an alcohol dehydrogenase such as AlrA from  Acinetobacter baylyi  and a w-hydroxylase such as cyp153A from  Marinobacter aquaeolei . The recombinant microbe produces the trifunctional molecules 1,3,12 dodecanetriol and (z5)1,3,12 dodecenetriol when the recombinant microbe is grown on a simple carbon source (see e.g.,  FIG. 3 ). The heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     In another exemplary embodiment, a recombinant microbe expressing a heterologous biochemical pathway comprising a thioesterase such as FatB1 from  Umbellularia californica , a carboxylic acid reductase such as CarB from  Mycobacterium smegmatis , an alcohol dehydrogenase such as AlrA from  Acinetobacter  baylyi and a ω-hydroxylase such as alkB from  Pseudomonas putida  produces the trifunctional molecules 1,3,12 dodecanetriol and (z5)1,3,12 dodecenetriol when the recombinant microbe is grown on a simple carbon source (see e.g.,  FIG. 3 ). Here again, the heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a thioesterase such as FatB1 from  Umbellularia californica , a carboxylic acid reductase such as CarB from  Mycobacterium smegmatis , an alcohol dehydrogenase such as AlrA from  Acinetobacter  baylyi and a “subterminal” hydroxylase such as cyp102A from a  Bacillus  (e.g.,  Bacillus licheniformis ) produces the trifunctional molecules 1,3,11 dodecanetriol, 1,3,10 dodecanetriol, 1,3,9 dodecanetriol, (z5)1,3,11 dodecenetriol, (z5)1,3,10 dodecenetriol and (z5)1,3,9 dodecenetriol when the recombinant microbe is grown on a simple carbon source (see e.g.,  FIG. 4 ). The heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a thioesterase such as PhaG from  Pseudomonas putida , a carboxylic acid reductase such as CarB from  Mycobacterium smegmatis , an alcohol dehydrogenase such as AlrA from  Acinetobacter  baylyi and a ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecules 1,3,8 octanetriol, 1,3,10 decanetriol, 1,3,12 dodecanetriol, and (z5)1,3,12 dodecenetriol when the recombinant microbe is grown on a simple carbon source. The heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous a biochemical pathway comprising of a thioesterase such as PhaG from  Pseudomonas putida , a carboxylacid reductase such as CarB from  Mycobacterium smegmatis , an alcohol dehydrogenase such as AlrA from  Acinetobacter baylyi  and a “subterminal” hydroxylase such as cyp102A from  Bacillus lichenformis  can produce from a simple carbon source the trifunctional molecules 1,3,7 octanetriol, 1,3,5 octanetriol, 1,3,5 octanetriol, 1,3,9 decanetriol, 1,3,8 decanetriol, 1,3,7 decanetriol, 1,3,11 dodecanetriol, 1,3,10 dodecanetriol, 1,3,9 dodecanetriol, (z5)1,3,11 dodecenetriol, (z5)1,3,10 dodecenetriol and (z5)1,3,9 dodecenetriol. The heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising an acyl-ACP reductase such as AAR from  Synechococcus elongatus , an alcohol dehydrogenase such as AlrA from  Acinetobacter baylyi  and a ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecules 1,3,14 tetradecanetriol, 1,3,16 hexadecanetriol, (z7)1,3,14 tetradecenetriol and (z9)1,3,16 hexadecenetriol when the recombinant microbe is grown on a simple carbon source. The heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising an acyl-ACP reductase such as AAR from  Synechococcus elongatus , an alcohol dehydrogenase such as AlrA from  Acinetobacter baylyi  and a “subterminal” hydroxylase such as cyp102A from a  Bacillus  produces the trifunctional molecules 1,3,13 tetradecanetriol, 1,3,12 tetradecanetriol, 1,3,11 tetradecanetriol, 1,3,15 hexadecanetriol, 1,3,14 hexadecanetriol, 1,3,13 hexadecanetriol, (z7)1,3,13 tetradecenetriol, (z7)1,3,12 tetradecenetriol, (z7)1,3,11 tetradecenetriol, (z9)1,3,15 hexadecenetriol, (z9)1,3,14 hexadecenetriol and (z9)1,3,13 hexadecenetriol when the recombinant microbe is grown on a simple carbon source. The heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     Multifunctional fatty acid derivatives can also be derived from bifunctional 3-oxo fatty acids (R1: —COOH, R2: ═O), however 3-oxo fatty acids may spontaneously decarboxylate to form the corresponding methyl-ketone (R1: H, R2: ═O; carbon chain is one carbon shorter). 
     d. Multifunctional Fatty Acid Derivatives from Fatty Acids, Fatty Esters and Alcohols 
     It is not a requirement to incorporate hydroxylation at both R1 and R2 (scheme 1) for producing multifunctional fatty acid derivatives. Biochemical pathways towards multifunctional fatty acid derivatives without hydroxylation at R2, i.e., via acyl-ACPs and not 3-hydroxy acyl-ACPs, are disclosed in  FIG. 2 . Such pathways to the production of multifunctional fatty acid derivatives employ two hydroxylases or hydratases that hydroxylate at different positions of the carbon chain to produce trifunctional fatty acid derivatives. In some embodiments, only one hydroxylase that can hydroxylate two positions can be employed. 
     i. Multifunctional Fatty Acid Derivatives from Fatty Acids 
     Thus, in an exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a thioesterase such as FatA from  Arabidopsis thaliana , a fatty acid hydratase such as OhyA1 or OhyA2 from  Stenotrophomonas maltophilia  and a ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecule 10,16-dihydroxyhexadecanoic acid when the microbe is grown on a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a thioesterase such as FatA from  Arabidopsis thaliana , a fatty acid hydratase such as OhyA1 or OhyA2 from  Stenotrophomonas maltophilia  and a ω-hydroxylase such as cyp102A from  Bacilllus lichenformis  produces the trifunctional molecules 10,15-dihydroxyhexadecanoic acid, 10,14-dihydroxyhexadecanoic acid and 10,13-dihydroxyhexadecanoic acid when the microbe is grown on a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising an epoxygenase such as delta 12 fatty acid epoxygenase from  Stokasia laevis  and epoxide hydrolase from  Caenorhabditis elegans , and a thioesterase such as FatA from  Arabidopsis thaliana  produces the trifunctional molecules 9,10-dihydroxyhexadecanoic and 9,10-dihydroxyoctadecanoic acid when the recombinant microbe is grown on a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising an epoxygenase such as delta 12 fatty acid epoxygenase from  Stokasia laevis  and epoxide hydrolase from  Caenorhabditis elegans , a thioesterase such as FatA from  Arabidopsis thaliana  and a ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the tetrafunctional molecules 9,10,16-trihydroxyhexadecanoic acid and 9,10,18-trihydroxyoctadecanoic acid when the recombinant microbe is grown on a from a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising an epoxygenase such as delta 12 fatty acid epoxygenase from  Stokasia laevis  and epoxide hydrolase from  Caenorhabditis elegans , a thioesterase such as FatA from  Arabidopsis thaliana  and a “subterminal” hydroxylase such as cyp102A from  Bacillus lichenformis  produces the tetrafunctional molecules 9,10,15-trihydroxyhexadecanoic acid; 9,10,14-trihydroxyhexadecanoic acid; 9,10,13-trihydroxyhexadecanoic acid; 9,10,15-trihydroxyoctadecanoic acid; 9,10,14-trihydroxyoctadecanoic acid; 9,10,13-trihydroxyoctadecanoic acid when the recombinant microbe is grown on a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a 10S-Dioxygenase and 7,10-Diol Synthase such as PA2077 and PA2078 from  Pseudomonas aeruginosa  and a thioesterase such as FatA3 from  Arabidopsis thaliana  produces the trifunctional molecules 7,10-dihydroxy-(8e)-hexadecenoic acid and 7,10-dihydroxy-(8e)-octadecenoic acid when the recombinant microbe is grown on a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a 10S-Dioxygenase and 7,10-Diol Synthase such as PA2077 and PA2078 from  Pseudomonas aeruginosa , a thioesterase such as FatA3 from  Arabidopsis thaliana  and a ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the tetrafunctional molecules 7,10,16-trihydroxy-(8e)-hexadecenoic acid and 7,10,18-trihydroxy-(8e)-octadecenoic acid when the recombinant microbe is grown on a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a 10S-Dioxygenase and 7,10-Diol Synthase such as PA2077 and PA2078 from  Pseudomonas aeruginosa , a thioesterase such as FatA3 from  Arabidopsis thaliana  and a “subterminal” hydroxylase such as cyp102A from  Bacillus licheniformis  produces the tetrafunctional molecules 7,10,15-trihydroxy-(8e)-hexadecenoic acid; 7,10, 14-trihydroxy-(8e)-hexadecenoic acid; 7,10,13-trihydroxy-(8e)-hexadecenoic acid; 7,10,15-trihydroxy-(8e)-octadecenoic acid; 7,10,14-trihydroxy-(8e)-octadecenoic acid and 7,10,13-trihydroxy-(8e)-octadecenoic acid when the recombinant microbe is grown on a simple carbon source. 
     ii. Multifunctional Fatty Acid Derivatives from Fatty Alcohols 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous a biochemical pathway comprising a thioesterase such as FatA3 from  Arabidopsis thaliana , a fatty acid hydratase such as OhyA1 or OhyA2 from  Stenotrophomonas maltophilia , a carboxylic acid reductase such as CarB from  Mycobacterium smegmatis , an alcohol dehydrogenase such as AlrA from  Acinetobacter baylyi  and a ω-hydroxylase such as cyp153A from  Marinobacter aquaeolei  produces the trifunctional molecule 1,10,16-hexadecanetriol when the recombinant microbe is grown on a simple carbon source. The heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a thioesterase such as FatA3 from  Arabidopsis thaliana , a fatty acid hydratase such as OhyA1 or OhyA2 from  Stenotrophomonas maltophilia , a carboxylic acid reductase such as CarB from  Mycobacterium smegmatis , an alcohol dehydrogenase such as AlrA from  Acinetobacter baylyi  and a ω-hydroxylase such as cyp102A from  Bacilllus lichenformis  produces the trifunctional molecules 1,10,15-hexadecanetriol, 1,10,14-hexadecanetriol and 1,10,13-hexadecanetriol when the recombinant microbe is grown on a simple carbon source. The heterologous expression of the alcohol dehydrogenase is optional, because most microbes express endogenous alcohol dehydrogenases. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising an epoxygenase such as delta 12 fatty acid epoxygenase from  Stokasia laevis  and epoxide hydrolase from  Caenorhabditis elegans , an acyl-ACP reductase such as AAR from  Synechococcus elongatus  and an alcohol dehydrogenase such as AlrA from  Acinetobacter baylyi  produces the trifunctional molecules 1,9,10-hexadecanetriol and 1,9,10-octadecanetriol when the recombinant microbe is grown on a simple carbon source. 
     In another exemplary embodiment, a recombinant microbe that expresses a heterologous biochemical pathway comprising a 10S-Dioxygenase and 7,10-Diol Synthase such as PA2077 and PA2078 from  Pseudomonas aeruginosa , an acyl-ACP reductase such as AAR from  Synechococcus elongatus  and an alcohol dehydrogenase such as AlrA from  Acinetobacter  baylyi produces the trifunctional molecules 1,7,10-(8e)-hexadecenetriol acid and 1,7,10-(8e)-octadecenetriol when the recombinant microbe is grown on a simple carbon source. 
     Although  FIG. 2  depicts the enzymatic hydroxylations as the last steps of the biochemical pathway, they can occur at earlier steps of the pathways, e.g. in  FIG. 2C  the fatty acid intermediate may be hydroxylated before it is converted to a fatty alcohol by carboxylic acid reductase (CAR). 
     5. Heterologous Hydroxylating Enzymes 
     In exemplary embodiments, ω-hydroxylases are used for hydroxylation at R5 in Scheme 1. Some exemplary ω-hydroxylases/o-oxygenases (EC 1.14.15.3) and their redox partners are provided in Tables 1A and 1B. In general, the ω-hydroxylases/o-oxygenases (EC 1.14.15.3) are non-heme di-iron oxygenases (e.g., alkB from  Pseudomonas putida  GPo1) or heme-type P450 oxygenases (e.g., cyp153A from  Marinobacter aquaeolei ) also known as cytochrome P450s. 
     Cytochromes P450s are proteins encoded by a superfamily of genes that convert a broad variety of substrates and catalyze a variety of chemical reactions. 
     An exemplary cytochrome P450 is cyp153A. Cyp153A is a sub-family of soluble bacterial cytochrome P450s that hydroxylate hydrocarbon chains with high selectivity for the ω-position (see e.g., van Beilen et al. (2006) Appl. Environ. Microbiol. 72:59-65; Funhoff et al. (2006) J. Bacteriol. 188:5220-5227; Scheps et al. (2011) Org. Biomol. Chem. 9:6727-6733; Honda-Malca et al. (2012) Chem. Commun. 48:5115-5117). 
     As with all cytochrome P450s, Cyp153A ω-hydroxylases require electrons for their catalytic activity, which are provided via specific redox proteins such as ferredoxin and ferredoxin reductase. Typically, the redox proteins are discrete proteins interacting with cyp153A. 
     A self-sufficient hybrid (chimeric) cyp153A oxygenase (i.e., an oxygenase that does not require discrete ferredoxin and ferredoxin reductase proteins for activity) has been created by fusing cyp153A from  Alcanivorax borkumensis  SK2 (see e.g., Kubota et al. (2005) Biosci. Biotechnol. Biochem. 69:2421-2430; Fujita et al. (2009) Biosci. Biotechnol. Biochem. 73:1825-1830) with the reductase domain from P450RhF, which includes flavin mononucleotide (FMN) and NADPH-binding sites and a [2FeS] ferredoxin center (see e.g., Hunter et al. (2005) FEBS Lett. 579:2215-2220). The resulting P450RhF belongs to the class-I P450-fused PFOR (see e.g., DeMot and Parret (2003) Trends Microbiol. 10: 502). Exemplary natural P450-Reductase fusion proteins are provided in Tables 1C and 1D. 
     Another CYP153A-reductase hybrid fusion proteins was prepared using a gene from  Marinobacter aquaeoli  coding for the CYP153A (G307A) P450 catalytic domain, where a glycine (G) was substituted for an alanine (A) at position 307, and a gene coding for the c-terminal FMN- and Fe/S-containing reductase domain of P450RhF from  Rhodococcus  sp. NCIMB9784 (see e.g. US Patent Application Publication 2016/0130616). The resulting polypeptides are CYP153A-RhF1 (SEQ ID NO:4) and CYP153A-RhF2 hybrid fusion polypeptide (SEQ ID NO:6). When this CYP153A-reductase hybrid fusion protein was expressed in  E. coli  cells with a simple carbon source such as glucose, fatty acid derivatives were efficiently converted to ω-hydroxy fatty acid derivatives source. 
     Other exemplary ω-hydroxylases (EC 1.14.15.3) and their redox partners that can be used to generate similar CYP153A-reductase hybrid fusion polypeptides are provided in Tables 1A, 1B and Table 7. 
     
       
         
           
               
             
               
                 TABLE 1A 
               
             
            
               
                   
               
               
                 Examples of ω-Hydroxylase/ω-Oxygenase (EC 1.14.15.3) 
               
            
           
           
               
               
               
               
               
            
               
                 Gene 
                   
                   
                   
                 Hydroxy- 
               
               
                 Desig- 
                 Source  
                 Accession  
                 Redox  
                 lation 
               
               
                 nation 
                 Organism 
                 No. 
                 System 
                 Position 
               
               
                   
               
               
                 cyp153A 
                 
                   Acineto- 
                 
                 BAE78452 
                 operon with 
                 ω- 
               
               
                 (aciA) 
                 
                   bacter 
                 
                   
                 ferredoxin and 
                 hydroxylase 
               
               
                   
                 sp. OC4 
                   
                 ferredoxin 
                   
               
               
                   
                   
                   
                 reductase 
                   
               
               
                 cyp153A16 
                 
                   Myco- 
                 
                 YP_001851443 
                 operon with 
                 ω- 
               
               
                   
                 
                   bacterium 
                 
                   
                 ferredoxin and 
                 hydroxylase 
               
               
                   
                   marinum  M 
                   
                 ferredoxin 
                   
               
               
                   
                   
                   
                 reductase 
                   
               
               
                 cyp153A6 
                 
                   Myco- 
                 
                 AJ833989 
                 operon with 
                 ω- 
               
               
                   
                 
                   bacterium 
                 
                   
                 ferredoxin and 
                 hydroxylase 
               
               
                   
                 sp.  
                   
                 ferredoxin 
                   
               
               
                   
                 HXN-1500 
                   
                 reductase 
                   
               
               
                 cyp153A 
                 Marino- 
                 WP_011784142 
                 operon with 
                 ω- 
               
               
                   
                 bacter 
                   
                 ferredoxin and 
                 hydroxylase 
               
               
                   
                 aquaeolei  
                   
                 ferredoxin 
                   
               
               
                   
                 VT8 
                   
                 reductase 
                   
               
               
                 alkB 
                 
                   Pseudo- 
                 
                 CAB54050 
                 requires 
                 ω- 
               
               
                   
                 
                   monas 
                 
                   
                 rubredoxin and 
                 hydroxylase 
               
               
                   
                 
                   putida  
                 
                   
                 rubredoxin 
                   
               
               
                   
                 GPo1 
                   
                 reductase 
                   
               
               
                 alkB 
                 
                   Pseudo- 
                 
                 CAB51045 
                 requires 
                 ω- 
               
               
                   
                 
                   monas 
                 
                   
                 rubredoxin and 
                 hydroxylase 
               
               
                   
                 
                   fluorescens 
                 
                   
                 rubredoxin 
                   
               
               
                   
                 CHA0 
                   
                 reductase 
                   
               
               
                 alkM 
                 
                   Acineto- 
                 
                 YP_046098 
                 requires 
                 ω- 
               
               
                   
                 
                   bacter 
                 
                   
                 rubredoxin and 
                 hydroxylase 
               
               
                   
                 
                   baylyi 
                 
                   
                 rubredoxin 
                   
               
               
                   
                   
                   
                 reductase 
                   
               
               
                 alkB 
                   Gordonia  sp. 
                 ADT82701 
                 requires 
                 ω- 
               
               
                   
                 SoGc 
                   
                 rubredoxin and 
                 hydroxylase 
               
               
                   
                   
                   
                 rubredoxin 
                   
               
               
                   
                   
                   
                 reductase 
                   
               
               
                 alkW1 
                   Dietzia  sp. 
                 HQ850582 
                 c-terminal 
                 ω- 
               
               
                   
                 DQ12-45-1b 
                   
                 rubredoxin 
                 hydroxylase 
               
               
                   
                   
                   
                 fusion, requires 
                   
               
               
                   
                   
                   
                 rubredoxin 
                   
               
               
                   
                   
                   
                 reductase 
                   
               
               
                 alkB 
                 
                   Pseudo- 
                 
                 CAB54050 
                 requires 
                 ω- 
               
               
                   
                 
                   monas 
                 
                   
                 rubredoxin and 
                 hydroxylase 
               
               
                   
                 
                   putida  
                 
                   
                 rubredoxin 
                   
               
               
                   
                 GPo1 
                   
                 reductase 
                   
               
               
                 alkB 
                 
                   Pseudo- 
                 
                 CAB51045 
                 requires 
                 ω- 
               
               
                   
                 
                   monas 
                 
                   
                 rubredoxin and 
                 hydroxylase 
               
               
                   
                 
                   fluorescens 
                 
                   
                 rubredoxin 
                   
               
               
                   
                 CHA0 
                   
                 reductase 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 1B 
               
             
            
               
                   
               
               
                 Exemplary Redox Partners for ω-Hydroxylase/ 
               
               
                 ω-Oxygenase (EC 1.14.15.3) 
               
            
           
           
               
               
               
            
               
                 Designation/ 
                   
                   
               
               
                 Name 
                 Organism 
                 Accession # 
               
               
                   
               
               
                 ferredoxin,  
                   Acinetobacter  sp. OC4 
                 BAE78451,  
               
               
                 ferredoxin 
                   
                 BAE78453 
               
               
                 reductase 
                   
                   
               
               
                 Putidaredoxin, 
                 
                   Pseudomonas putida 
                 
                 BAA00414,  
               
               
                 putidaredoxin  
                   
                 BAA00413 
               
               
                 reductase 
                   
                   
               
               
                 (camAB) 
                   
                   
               
               
                 ferredoxin,  
                 
                   Mycobacterium  
                 
                 YP_001851444, 
               
               
                 ferredoxin 
                   marinum  M 
                 YP_001851442 
               
               
                 reductase 
                   
                   
               
               
                 ferredoxin,  
                 
                   Marinobacter aquaeoli 
                 
                 YP_957887,  
               
               
                 ferredoxin 
                 VT8 
                 YP_957889 
               
               
                 reductase 
                   
                   
               
               
                 alkG, alkT 
                 
                   Pseudomonas  
                 
                 CAB54052,  
               
               
                   
                   putida  GPo1 
                 CAB54063 
               
               
                 rubA, rubB 
                 
                   Acinetobacter  
                 
                 CAA86925,  
               
               
                   
                   baylyi  ADP1 
                 CAA86926 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 1C 
               
             
            
               
                   
               
               
                 Examples of Self-Sufficient ω-1, ω-2, ω-3-Hydroxylase/ 
               
               
                 Oxygenase (EC 1.14.14.1) Fusion Proteins 
               
            
           
           
               
               
               
               
               
            
               
                 Gene 
                   
                   
                   
                 Hydroxy- 
               
               
                 Desig- 
                 Source 
                 Accession  
                 Redox  
                 lation 
               
               
                 nation 
                 Organism 
                 No. 
                 System 
                 Position 
               
               
                   
               
               
                 cyp102A1 
                 
                   Bacillus 
                 
                 AAA87602 
                 fusion protein  
                 ω-1,-2,-3 
               
               
                 (P450- 
                 
                   megaterium 
                 
                   
                 with reductase  
                 hydroxy- 
               
               
                 BM3) 
                   
                   
                 domain 
                 lation 
               
               
                 cyp102A3 
                 
                   Bacillus 
                 
                 NP_390594 
                 fusion protein  
                 ω-1,-2,-3 
               
               
                   
                 
                   subtilis 
                 
                   
                 with reductase  
                 hydroxy- 
               
               
                   
                   
                   
                 domain 
                 lation 
               
               
                 cyp102A7 
                 
                   Bacillus 
                 
                 AAU41718 
                 fusion protein  
                 ω-1,-2,-3 
               
               
                   
                 
                   licheniformis 
                 
                   
                 with reductase  
                 hydroxy- 
               
               
                   
                   
                   
                 domain 
                 lation 
               
               
                 Cyp102D1 
                 
                   Streptomyces 
                 
                 WP_010982013 
                 fusion protein  
                 ω-1,-2,-3 
               
               
                   
                 
                   avermitilis 
                 
                   
                 with reductase  
                 hydroxy- 
               
               
                   
                   
                   
                 domain 
                 lation 
               
               
                 Cyp505A1 
                 
                   Fusarium 
                 
                 AB030037 
                 fusion protein  
                 ω-1,-2,-3 
               
               
                   
                 
                   oxysporum 
                 
                   
                 with reductase  
                 hydroxy- 
               
               
                   
                   
                   
                 domain 
                 lation 
               
               
                 Cyp505E 
                 
                   Aspergillus 
                 
                 XP_001210151 
                 fusion protein  
                 ω-1,-2, 
               
               
                   
                 
                   terreus 
                 
                   
                 with reductase  
                 -3,-7 
               
               
                   
                   
                   
                 domain 
                 hydroxy- 
               
               
                   
                   
                   
                   
                 lation 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 1D 
               
             
            
               
                   
               
               
                 Examples of Self-Sufficient Class-I P450-Fused PFOR Fusion Proteins 
               
            
           
           
               
               
               
            
               
                 Designation/Name 
                 Organism 
                 Accession # 
               
               
                   
               
               
                 P450RhF 
                   Rhodococcus  sp. NCIMB 9784 
                 AAM67416 
               
               
                 REQ_44300 
                   Rhodococcus equi  103S 
                 YP_004009071 
               
               
                 HMPREF0018_01193 
                 
                   Acinetobacter radioresistens 
                 
                 ZP_06072406 
               
               
                   
                 SH164 
                   
               
               
                 BMAA1669 
                   Burkholderia mallei  ATCC 23344 
                 YP_106239 
               
               
                 Rmet_4932 
                   Cupriavidus metallidurans  CH34 
                 YP_587063 
               
               
                 H16_B1279 
                   Ralstonia eutropha  H16 
                 YP_840799 
               
               
                   
               
            
           
         
       
     
     In exemplary embodiments hydroxylation at R3 and R4 in Scheme 1 is achieved through the use of “subterminal” hydroxylases, “mid-chain” hydroxylases and/or oleate hydratases. 
     “Subterminal” hydroxylases incorporate one OH group at one or more of the omega-1 (ω-1) position, the omega-2 (ω-2) position, the omega-3 (ω-3) position, and/or the omega-4 (ω-4) position, etc. of a fatty acid or fatty acid derivative molecule. Typically, subterminal hydroxylases are cytochrome P450 oxygenases from the cyp102 or cyp505 family (see e.g., Whitehouse et al. (2012) Chem. Soc. Rev. 41: 1218; Kitazume et al. (2000) J. Biol. Chem. 2000, 275:39734-39740) which comprises self-sufficient natural P450-reductase fusion proteins. Cyp102 and Cyp505 family subterminal hydroxylases do not require additional redox partners. 
     Fatty acid hydroxylases incorporate one OH group at one or more positions close to the center of the hydrocarbon chain. Cytochrome P450 oxygenases can be “mid-chain” fatty acid hydroxylases. Another exemplary group of fatty acid hydroxylases are closely related to plant or fungal acyl-CoA desaturases (see e.g., Broun et al. 1998, Science vol. 282, pp. 1315) and belong to the non-heme diiron protein family. Exemplary “mid-chain” fatty acid hydroxylases include e.g., FAH12 from  Ricinus communis  (see e.g., Van De Loo et al. 1995, PNAS vol. 92, pp. 6743); CpFAH from  Claviceps purpurea  (see e.g., Meesapyodsuk and Xiao Qiu, Plant Physiol., vol. 147, pp and Table 2). They require redox partners similar to the ones listed in Table 1B. 
     Fatty acid hydratases act only on unsaturated carbon atoms, e.g. they can convert oleic acid into 10-hydroxy stearic acid. Exemplary fatty acid hydratases include e.g., ohyA1 and ohyA2 from  Stenotrophomonas maltophilia  (see e.g. Joo et al. 2012, J. Biotechnol. vol. 158, pp. 17; Kang et al. 2017, AEM vol. 83, pp. 1 and see Table 3). Although fatty acid hydratases contain FAD as a cofactor, cofactor regeneration during catalysis is not required (see e.g., Engleder et al. 2015, ChemBioChem vol. 16, pp. 1730). Additional redox partner as described above for the hydroxylases/oxygenases are not required for the ohyA-type hydratases. 
     In exemplary embodiments, hydroxylation at R2 and if R1=02H in scheme 1, occurs through the action of a-hydroxylases. Exemplary α-hydoxylases include P450 enzymes of the peroxygenase cyp152 family, for example cyp153A1 from  Sphingomonas paucimobilis  (see e.g., Table 4, Matsunaga et al. 1997, JBC, vol. 272, No. 38, pp. 23592, etc.). These enzymes can utilize hydrogen peroxide as electron donor, but they can also use redox partners as described in Table 1B. 
     
       
         
           
               
             
               
                 TABLE 2 
               
             
            
               
                   
               
               
                 Examples of “mid-chain” Hydroxylase/Oxygenase (EC 1.14.19.6) 
               
            
           
           
               
               
               
            
               
                 Designation/Name 
                 Organism 
                 Accession # 
               
               
                   
               
               
                 CpFAH 
                 
                   Claviceps purpurea 
                 
                 CCE30184 
               
               
                 RcFAH12 
                 
                   Ricinus communis 
                 
                 AAC49010 
               
               
                 FaFAD1 
                 
                   Fragaria x ananassa 
                 
                 KF887973 
               
               
                 LFAH12 
                 
                   Lesquerella fendleri 
                 
                 AAC32755 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 3 
               
             
            
               
                   
               
               
                 Examples of Hydratases (EC 4.2.1.53) 
               
            
           
           
               
               
               
            
               
                 Designation/Name 
                 Organism 
                 Accession # 
               
               
                   
               
               
                 OhyA1 
                 
                   Stenotrophomonas maltophilia 
                 
                 WP_012479975 
               
               
                 OhyA2 
                 
                   Stenotrophomonas maltophilia 
                 
                 WP_017356052 
               
               
                 OhyA 
                 
                   Elizabethkingia meningoseptica 
                 
                 GQ144652 
               
               
                 LAH 
                 
                   Lactobacillus acidophilus 
                 
                 AAV42528 
               
               
                 FA-HY1 
                 
                   Lactobacillus acidophilus 
                 
                 LC030242 
               
               
                 FA-HY2 
                 
                   Lactobacillus acidophilus 
                 
                 LC030243 
               
               
                 Sn_OhyA2 
                 
                   Stenotrophomonas nitritireducens 
                 
                 WP_062168826 
               
               
                 SPH 
                 
                   Sfreptococcus pyogenes 
                 
                 ACI60731 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 4 
               
             
            
               
                   
               
               
                 Examples of α-Hydroxylases/Peroxygenases (EC 1.11.2.4) 
               
            
           
           
               
               
               
               
            
               
                   
                 Designation/Name 
                 Organism 
                 Accession # 
               
               
                   
                   
               
               
                   
                 Cyp152B1 
                 
                   Sphingomonas paucimobilis 
                 
                 BAA22987 
               
               
                   
                 Cyp152A1 
                 
                   Bacillus subtilis 
                 
                 NP_388092 
               
               
                   
                 Cyp152A 
                 
                   Bacillus clausii 
                 
                 YP_176535 
               
               
                   
                   
               
            
           
         
       
     
     The combined activity of certain dioxygenases and diol synthases (see Table 11) convert fatty acids such as oleic acid into dihydroxy fatty acids via hydroperoxy fatty acid intermediates (Estupian et al. 2014, Biochimica et Biophysica Acta 1841:1360-1371). These enzymes belong to the class of Di-Heme cytochrome C peroxidases. 
     
       
         
           
               
             
               
                 TABLE 11 
               
             
            
               
                   
               
               
                 Examples of bacterial diol synthases (EC 1.13.11.77) 
               
            
           
           
               
               
               
            
               
                 Designation/Name 
                 Organism 
                 Accession # 
               
               
                   
               
               
                 PA2077, PA2078 (10S- 
                   P. aeruginosa  PAO1 
                 NP_250767,  
               
               
                 Dioxygenase; 7,10-Diol 
                   
                 NP_250768 
               
               
                 Synthase) 
                   
                   
               
               
                 azo2594, azo2595 
                   Azoarcus  sp. BH72 
                 WP_011766321, 
               
               
                   
                   
                 WP_011766322 
               
               
                   
               
            
           
         
       
     
     The combined activity of certain epoxygenases (also known as peroxygenases or epoxidases) and epoxide hydrolases (see Table 12) convert fatty acids such as oleic acid into dihydroxy fatty acids via epoxy fatty acid intermediates (Kaprakkaden et al. 2017, Microb Cell Fact 16:85). Epoxygenases are heme-containing monooxygenases and catalyze hydroperoxide-dependent epoxidation of unsaturated fatty acids. 
     
       
         
           
               
             
               
                 TABLE 12 
               
             
            
               
                   
               
               
                 Examples of epoxygenases (EC 1.11.2.3)  
               
               
                 and epoxide hydrolases (EC 3.3.2.10) 
               
            
           
           
               
               
               
               
            
               
                   
                 Designation/ 
                   
                 Accession #  
               
               
                   
                 Name 
                 Organism 
                 or reference 
               
               
                   
                   
               
               
                   
                 AsPXG3 
                 
                   Avena sativa 
                 
                 Benaragama,  
               
               
                   
                   
                   
                 Planta (2017) 
               
               
                   
                   
                   
                 246:711-719 
               
               
                   
                 delta 12 fatty acid 
                 
                   Stokasia laevis 
                 
                 AAR23815 
               
               
                   
                 epoxygenase 
                   
                   
               
               
                   
                 AtPXG4 
                 
                   Arabidopsis thaliana 
                 
                 Benaragama,  
               
               
                   
                   
                   
                 Planta (2017) 
               
               
                   
                   
                   
                 246:711-719 
               
               
                   
                 PpoC 
                 
                   Aspergillus nidulans 
                 
                 AY613780 
               
               
                   
                 epoxide hydrolase 
                 
                   Caenorhabditis elegans 
                 
                 ABV45408 
               
               
                   
                 epoxide hydrolase-2 
                 
                   Mangifera idica 
                 
                 AQZ55557 
               
               
                   
                 BmeH 
                 
                   Bacillus megaterium 
                 
                 ADV36302 
               
               
                   
                   
               
            
           
         
       
     
     6. Heterologous Enzymes that Modify Hydroxyl Groups of Multifunctional Fatty Acid Derivative Molecules 
     In exemplary embodiments, additional enzymes are employed to convert the hydroxyl groups of multifunctional fatty acid derivatives into other functional groups, e.g. oxo (CHO), carboxyl (CO 2 H), amino (CH 2 NH 2 ),O-acetyl (CO 2 C 2 H 3 ), methoxy (COCH 3 ) or ester (CO 2 CH 3 , CO 2 C 2 H 5 , CO 2 C 3 H 7 , CO 2 C 2 H 3 ) groups. Exemplary enzymes suitable for these modifications include dehydrogenases, oxidases, transaminases, acetyl-transferases, methyl transferases and ester synthases (see e.g., Table 5). 
     
       
         
           
               
             
               
                 TABLE 5 
               
             
            
               
                   
               
               
                 Enzymes that convert hydroxyl groups in multifunctional  
               
               
                 fatty acid derivatives into other functional groups. 
               
            
           
           
               
               
               
               
            
               
                 Designation/Name 
                 Organism 
                 Accession # 
                 Enzyme Function 
               
               
                   
               
               
                 Alcohol  
                   
                   
                 C—OH ↔ C═O 
               
               
                 dehydrogenase 
                   
                   
                   
               
               
                 ADH 
                 
                   Micrococcus luteus 
                 
                 ADD83022 
                   
               
               
                 cddC 
                 
                   Rhodococcus ruber 
                 
                 AAL14237 
                   
               
               
                 AlrA 
                 
                   Acinetobacter baylyi 
                 
                 CAG70252 
                   
               
               
                 yjgB 
                 
                   Escherichia coli 
                 
                 NP_418690 
                   
               
               
                 yahK 
                 
                   Escherichia coli 
                 
                 NP_414859 
                   
               
               
                 ybbO 
                 
                   Escherichia coli 
                 
                 NP_415026 
                   
               
               
                 adhP 
                 
                   Escherichia coli 
                 
                 P39451 
                   
               
               
                 Alcohol Oxidase 
                   
                   
                 C—OH → C═O 
               
               
                 alkJ 
                   Pseudomonas putida  GPo1 
                 CAB54054 
                   
               
               
                 alkJ 
                   Alcanivorax borkumensis  AP1 
                 CAC38030 
                   
               
               
                 FAO1 
                 
                   Yarrowia lipolytica 
                 
                 YALI0B14014g 
                   
               
               
                 Aldehyde  
                   
                   
                 C—OH → C═O → COOH 
               
               
                 dehydrogenase 
                   
                   
                   
               
               
                 alkH 
                   Pseudomonas putida  GPo1 
                 CAB51050 
                   
               
               
                 alkH 
                   Alcanivorax borkumensis  AP1 
                 CAC38029 
                   
               
               
                 cddD 
                   Rhodococcus ruber  SC1 
                 AAL14238 
                   
               
               
                 FAldDH 
                 
                   Acinetobacter baylyi 
                 
                 WP_004927398 
                   
               
               
                 Maqu_3410 
                   Marinobacter aquaeolei  VT8  
                 WP_011786822 
                   
               
               
                 feaB 
                 
                   Escherichia coli 
                 
                 P80668 
                   
               
               
                 patD 
                 
                   Escherichia coli 
                 
                 P77674 
                   
               
               
                 paaZ 
                 
                   Escherichia coli 
                 
                 P77455 
                   
               
               
                 Transaminase/Amine 
                   
                   
                 C—OH → C═O↔C—NH 2   
               
               
                 dehydrogenase 
                   
                   
                   
               
               
                 CV_2025 
                 
                   Chromobacterium violaceum 
                 
                 Q7NWG4 
                   
               
               
                 gabT 
                   Pseudomonas  sp.AAC 
                 KES23458 
                   
               
               
                 ygjG 
                 
                   Escherichia coli 
                 
                 NP_417544 
                   
               
               
                 GabT 
                 
                   Pseudomonas aeruginosa 
                 
                 WP_003156103 
                   
               
               
                 GabT 
                 
                   Pseudomonas aeruginosa 
                 
                 AAG03655 
                   
               
               
                 PRK08297 
                 
                   Mycobacterium tuberculosis 
                 
                 NP_217807 
                   
               
               
                 Ald 
                 
                   Bacillus subtilis 
                 
                 BAI86717 
                   
               
               
                 gdhA 
                 
                   Escherichia coli 
                 
                 NP_416275 
                   
               
               
                 gdh 
                 
                   Peptoniphilus 
                 
                 AAA25611 
                   
               
               
                   
                 
                   asaccharolyticus 
                 
                   
                   
               
               
                 Lysine DH 
                 
                   Achromobacter denitrificans 
                 
                 AAZ94428 
                   
               
               
                 Acetyl-O-transferase 
                 2.3.1.84 
                   
                 C—OH → C—O 2 C 2 H 3   
               
               
                 atf1 
                 
                   Saccharomyces cerevisiae 
                 
                 CAA99708 
                   
               
               
                 SAAT 
                 
                   Fragaria ananassa 
                 
                 AF193789 
                   
               
               
                 Methyl-O-transferase 
                   
                   
                 C—OH → C—OCH 3   
               
               
                 FAMT 
                 
                   Mycobacterium marinum 
                 
                 NC010612 
                   
               
               
                 DmJHAMT 
                 
                   Drosophila melanogaster 
                 
                 Q9VJK8 
               
               
                   
               
            
           
         
       
         
         
           
             
               
                 
                   
                     
                       
                         III. Fermentation and Production of Multifunctional Fatty Acid Derivatives 
                       
                     
                   
                 
               
             
           
         
       
    
     As used herein, fermentation broadly refers to the conversion of organic materials into target substances by recombinant host cells. For example, this includes the conversion of a carbon source by recombinant host cells into multifunctional fatty acid derivative molecules as disclosed herein by propagating a culture of the recombinant host cells in a media comprising a carbon source. Conditions permissive for the production of target substances such as e.g., multifunctional fatty acid derivative molecules as disclosed herein, are any conditions that allow a host cell to produce a desired product, such as a multifunctional fatty acid derivative composition. Suitable conditions include, for example, typical fermentation conditions see e.g.,  Principles of Fermentation Technology,  3rd Edition (2016) supra;  Fermentation Microbiology and Biotechnology,  2nd Edition, (2007) supra. 
     Fermentation conditions can include many parameters, well known in the art, including but not limited to temperature ranges, pH levels, levels of aeration, feed rates and media composition. Each of these conditions, individually and in combination, allows the host cell to grow. Fermentation can be aerobic, anaerobic, or variations thereof (such as micro-aerobic). Exemplary culture media include broths (liquid) or gels (solid). Generally, the medium includes a carbon source (e.g., a simple carbon source derived from a renewable feedstock) that can be metabolized by a host cell directly. In addition, enzymes can be used in the medium to facilitate the mobilization (e.g., the depolymerization of starch or cellulose to fermentable sugars) and subsequent metabolism of the carbon source to produce multifunctional fatty acid derivatives. 
     For small scale production, the host cells engineered to produce multifunctional fatty acid derivative compositions are typically grown in batches of, for example, about 100 μL, 200 μL, 300 μL, 400 μL, 500 μL, 1 mL, 5 mL, 10 mL, 15 mL, 25 mL, 50 mL, 75 mL, 100 mL, 500 mL, 1 L, 2 L, 5 L, or 10 L. 
     For large scale production, the engineered host cells can be grown in cultures having a volume batches of about 10 L, 100 L, 1000 L, 10,000 L, 100,000 L, 1,000,000 L or larger; fermented; and induced to express any desired polynucleotide sequence. 
     The multifunctional fatty acid derivative compositions disclosed herein can be found in the extracellular environment of the recombinant host cell culture and can be readily isolated from the culture medium by methods known in the art. A multifunctional fatty acid derivative may be secreted by the recombinant host cell, transported into the extracellular environment or passively transferred into the extracellular environment of the recombinant host cell culture. 
     Exemplary microorganisms suitable for use as production host cells include e.g., bacteria, cyanobacteria, yeast, algae, filamentous fungi, etc. To produce fatty acid derivative compositions production host cells (or equivalently, host cells) are engineered to comprise fatty acid biosynthesis pathways that are modified relative to non-engineered or native host cells e.g., engineered as discussed above and as disclosed e.g., in U.S. Patent Application Publication 2015/0064782. Production hosts engineered to comprise modified fatty acid biosynthesis pathways are able to efficiently convert glucose or other renewable feedstocks into fatty acid derivatives. Protocols and procedures for high density fermentations for the production of various compounds have been established (see, e.g., U.S. Pat. Nos. 8,372,610; 8,323,924; 8,313,934; 8,283,143; 8,268,599; 8,183,028; 8,110,670; 8,110,093; and 8,097,439). 
     In some exemplary embodiments, a production host cell is cultured in a culture medium (e.g., fermentation medium) comprising an initial concentration of a carbon source (e.g., a simple carbon source) of about 20 g/L to about 900 g/L. In other embodiments, the culture medium comprises an initial concentration of a carbon source of about 2 g/L to about 10 g/L; of about 10 g/L to about 20 g/L; of about 20 g/L to about 30 g/L; of about 30 g/L to about 40 g/L; or of about 40 g/L to about 50 g/L. In some embodiments, the level of available carbon source in the culture medium can be monitored during the fermentation proceeding. In some embodiments, the method further includes adding a supplemental carbon source to the culture medium when the level of the initial carbon source in the medium is less than about 0.5 g/L. 
     In some exemplary embodiments, a supplemental carbon source is added to the culture medium when the level of the carbon source in the medium is less than about 0.4 g/L, less than about 0.3 g/L, less than about 0.2 g/L, or less than about 0.1 g/L. In some embodiments, the supplemental carbon source is added to maintain a carbon source level of about 1 g/L to about 25 g/L. In some embodiments, the supplemental carbon source is added to maintain a carbon source level of about 2 g/L or more (e.g., about 2 g/L or more, about 3 g/L or more, about 4 g/L or more). In certain embodiments, the supplemental carbon source is added to maintain a carbon source level of about 5 g/L or less (e.g., about 5 g/L or less, about 4 g/L or less, about 3 g/L or less). In some embodiments, the supplemental carbon source is added to maintain a carbon source level of about 2 g/L to about 5 g/L, of about 5 g/L to about 10 g/L, or of about 10 g/L to about 25 g/L. 
     In one exemplary embodiment the carbon source for the fermentation is derived from a renewable feedstock. In some embodiments, the carbon source is glucose. In other embodiments, the carbon source is glycerol. Other possible carbon sources include, but are not limited to, fructose, mannose, galactose, xylose, arabinose, starch, cellulose, pectin, xylan, sucrose, maltose, cellobiose, and turanose; cellulosic material and variants such as hemicelluloses, methyl cellulose and sodium carboxymethyl cellulose; saturated or unsaturated fatty acids, succinate, lactate, and acetate; alcohols, such as ethanol, methanol, and glycerol, or mixtures thereof. In one embodiment, the carbon source is derived from corn, sugar cane, sorghum, beet, switch grass, ensilage, straw, lumber, pulp, sewage, garbage, cellulosic urban waste, flu-gas, syn-gas, or carbon dioxide. The simple carbon source can also be a product of photosynthesis, such as glucose or sucrose. In one embodiment, the carbon source is derived from a waste product such as glycerol, flu-gas, or syn-gas; or from the reformation of organic materials such as biomass; or from natural gas or from methane, or from the reformation of these materials to syn-gas; or from carbon dioxide that is fixed photosynthetically, for example multifunctional fatty acid derivatives may be produced by recombinant cyanobacteria growing photosynthetically and using CO 2  as carbon source. In some exemplary embodiments, the carbon source is derived from biomass. An exemplary source of biomass is plant matter or vegetation, such as corn, sugar cane, or switchgrass. Another exemplary source of biomass is metabolic waste products, such as animal matter (e.g., cow manure). Further exemplary sources of biomass include algae and other marine plants. Biomass also includes waste products from industry, agriculture, forestry, and households, including, but not limited to, fermentation waste, ensilage, straw, lumber, sewage, garbage, cellulosic urban waste, municipal solid waste, and food leftovers. 
     In some exemplary embodiments, a multifunctional fatty acid derivative is produced at a concentration of about 0.5 g/L to about 40 g/L. In some embodiments, a fatty acid derivative is produced at a concentration of about 1 g/L or more (e.g., about 1 g/L or more, about 10 g/L or more, about 20 g/L or more, about 50 g/L or more, about 100 g/L or more). In some embodiments, a fatty acid derivative is produced at a concentration of about 1 g/L to about 170 g/L, of about 1 g/L to about 10 g/L, of about 40 g/L to about 170 g/L, of about 100 g/L to about 170 g/L, of about 10 g/L to about 100 g/L, of about 1 g/L to about 40 g/L, of about 40 g/L to about 100 g/L, or of about 1 g/L to about 100 g/L. 
     In other exemplary embodiments, a multifunctional fatty acid derivative is produced at a titer of about 25 mg/L, about 50 mg/L, about 75 mg/L, about 100 mg/L, about 125 mg/L, about 150 mg/L, about 175 mg/L, about 200 mg/L, about 225 mg/L, about 250 mg/L, about 275 mg/L, about 300 mg/L, about 325 mg/L, about 350 mg/L, about 375 mg/L, about 400 mg/L, about 425 mg/L, about 450 mg/L, about 475 mg/L, about 500 mg/L, about 525 mg/L, about 550 mg/L, about 575 mg/L, about 600 mg/L, about 625 mg/L, about 650 mg/L, about 675 mg/L, about 700 mg/L, about 725 mg/L, about 750 mg/L, about 775 mg/L, about 800 mg/L, about 825 mg/L, about 850 mg/L, about 875 mg/L, about 900 mg/L, about 925 mg/L, about 950 mg/L, about 975 mg/L, about 1000 mg/L, about 1050 mg/L, about 1075 mg/L, about 1100 mg/L, about 1125 mg/L, about 1150 mg/L, about 1175 mg/L, about 1200 mg/L, about 1225 mg/L, about 1250 mg/L, about 1275 mg/L, about 1300 mg/L, about 1325 mg/L, about 1350 mg/L, about 1375 mg/L, about 1400 mg/L, about 1425 mg/L, about 1450 mg/L, about 1475 mg/L, about 1500 mg/L, about 1525 mg/L, about 1550 mg/L, about 1575 mg/L, about 1600 mg/L, about 1625 mg/L, about 1650 mg/L, about 1675 mg/L, about 1700 mg/L, about 1725 mg/L, about 1750 mg/L, about 1775 mg/L, about 1800 mg/L, about 1825 mg/L, about 1850 mg/L, about 1875 mg/L, about 1900 mg/L, about 1925 mg/L, about 1950 mg/L, about 1975 mg/L, about 2000 mg/L (2 g/L), 3 g/L, 5 g/L, 10 g/L, 20 g/L, 30 g/L, 40 g/L, 50 g/L, 60 g/L, 70 g/L, 80 g/L, 90 g/L, 100 g/L or a range bounded by any two of the foregoing values. In other embodiments, a fatty acid derivative or other compound is produced at a titer of more than 100 g/L, more than 200 g/L, or more than 300 g/L. In exemplary embodiments, the titer of fatty acid derivative or other compound produced by a recombinant host cell according to the methods disclosed herein is from 5 g/L to 200 g/L, 10 g/L to 150 g/L, 20 g/L to 120 g/L and 30 g/L to 100 g/L. The titer may refer to a particular fatty acid derivative or a combination of fatty acid derivatives or another compound or a combination of other compounds produced by a given recombinant host cell culture. In exemplary embodiments, the expression of ChFatB2 thioesterase variant in a recombinant host cell such as  E. coli  results in the production of a higher titer as compared to a recombinant host cell expressing the corresponding wild type polypeptide. In one embodiment, the higher titer ranges from at least about 5 g/L to about 200 g/L. 
     In other exemplary embodiments, the host cells engineered to produce a multifunctional fatty acid derivative according to the methods of the disclosure have a yield of at least 1%, at least 2%, at least about 3%, at least about 4%, at least about 5%, at least about 6%, at least about 7%, at least about 8%, at least about 9%, at least about 10%, at least about 11%, at least about 12%, at least about 13%, at least about 14%, at least about 15%, at least about 16%, at least about 17%, at least about 18%, at least about 19%, at least about 20%, at least about 21%, at least about 22%, at least about 23%, at least about 24%, at least about 25%, at least about 26%, at least about 27%, at least about 28%, at least about 29%, or at least about 30% or a range bounded by any two of the foregoing values. In other embodiments, a fatty acid derivative or derivatives or other compound(s) are produced at a yield of more than about 30%, more than about 35%, more than about 40%, more than about 45%, more than about 50%, more than about 55%, more than about 60%, more than about 65%, more than about 70%, more than about 75%, more than about 80%, more than about 85%, more than about 90%, more than 100%, more than 200%, more than 250%, more than 300%, more than 350%, more than 400%, more than 450%, more than 500%, more than 550%, more than 600%, more than 650%, more than 700%, more than 750%, or more. Alternatively, or in addition, the yield is about 30% or less, about 27% or less, about 25% or less, or about 22% or less. In another embodiment, the yield is about 50% or less, about 45% or less, or about 35% or less. In another embodiment, the yield is about 95% or less, or 90% or less, or 85% or less, or 80% or less, or 75% or less, or 70% or less, or 65% or less, or 60% or less, or 55% or less, or 50% or less. Thus, the yield can be bounded by any two of the above endpoints. For example, the yield of a multifunctional fatty acid derivative e.g., a 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, etc. carbon multifunctional fatty acid derivative produced by the recombinant host cell according to the methods disclosed herein can be about 5% to about 15%, about 10% to about 25%, about 10% to about 22%, about 15% to about 27%, about 18% to about 22%, about 20% to about 28%, about 20% to about 30%, about 30% to about 40%, about 40% to about 50%, about 50% to about 60%, about 60% to about 70%, about 70% to about 80%, about 80% to about 90%, about 90% to about 100%, about 100% to about 200%, about 200% to about 300%, about 300% to about 400%, about 400% to about 500%, about 500% to about 600%, about 600% to about 700%, or about 700% to about 800%. The yield may refer to a particular multifunctional fatty acid derivative or a combination of fatty acid derivatives. In one embodiment, the higher yield ranges from about 10% to about 800% of theoretical yield. In addition, the yield will also be dependent on the feedstock used. 
     In some exemplary embodiments, the productivity of the host cells engineered to produce a multifunctional fatty acid derivative according to the methods of the disclosure is at least 100 mg/L/hour, at least 200 mg/L/hour, at least 300 mg/L/hour, at least 400 mg/L/hour, at least 500 mg/L/hour, at least 600 mg/L/hour, at least 700 mg/L/hour, at least 800 mg/L/hour, at least 900 mg/L/hour, at least 1000 mg/L/hour, at least 1100 mg/L/hour, at least 1200 mg/L/hour, at least 1300 mg/L/hour, at least 1400 mg/L/hour, at least 1500 mg/L/hour, at least 1600 mg/L/hour, at least 1700 mg/L/hour, at least 1800 mg/L/hour, at least 1900 mg/L/hour, at least 2000 mg/L/hour, at least 2100 mg/L/hour, at least 2200 mg/L/hour, at least 2300 mg/L/hour, at least 2400 mg/L/hour, 2500 mg/L/hour, or as high as 10 g/L/hour (dependent upon cell mass). For example, the productivity of a malonyl-CoA derived compound including a fatty acid derivative or derivatives or other compound(s) produced by a recombinant host cell according to the methods of the disclosure may be from 500 mg/L/hour to 2500 mg/L/hour, or from 700 mg/L/hour to 2000 mg/L/hour. The productivity may refer to a particular 8 and/or 10 carbon fatty acid derivative or a combination of fatty acid derivatives or other compound(s) produced by a given host cell culture. For example, the expression of a ChFatB2 thioesterase variant in a recombinant host cell such as  E. coli  results in increased productivity of an 8 and/or 10 carbon fatty acid derivatives or other compounds as compared to a recombinant host cell expressing the corresponding wild type polypeptide. In exemplary embodiments, higher productivity ranges from about 0.3 g/L/h to about 3 g/L/h to about 10 g/L/h to about 100 g/L/h to about a 1000 g/L/h. 
     As disclosed supra, in some exemplary embodiments, the host cell used in the fermentation procedures discussed herein (supra) is a mammalian cell, plant cell, insect cell, yeast cell, fungus cell, filamentous fungi cell, an algal cell, a cyanobacterial cell, and bacterial cell. 
     IV. Isolation 
     Bioproducts e.g., compositions comprising multifunctional fatty acid derivatives as disclosed herein which are produced utilizing recombinant host cells as discussed above are typically isolated from the fermentation broth by methods known in the art. 
     V. Compositions and Formulations of Multifunctional Fatty Acid Derivative Molecules 
     Bioproducts e.g., compositions comprising multifunctional fatty acid derivative molecules produced utilizing engineered microbes as discussed herein, are produced from renewable sources (e.g., from a simple carbon source derived from renewable feedstocks) and, as such, are new compositions of matter. These new bioproducts can be distinguished from organic compounds derived from petrochemical carbon on the basis of dual carbon-isotopic fingerprinting or  14 C dating. Additionally, the specific source of biosourced carbon (e.g., glucose vs. glycerol) can be determined by dual carbon-isotopic fingerprinting by methods known in the art (see, e.g., U.S. Pat. No. 7,169,588, WO 2016/011430 A1, etc.). 
     The following examples are offered to illustrate, but not to limit the invention. 
     EXAMPLES 
     Example 1 
     The following Example illustrates materials and methods for Examples 2-9 disclosed herein below. 
     Methods 
     Small Scale Fermentation Protocol: 
     40 μL LB culture (from an LB culture growing in a 96 well plate) was used to inoculate 360 μL LB media, which was then incubated for approximately 4 hours at 32° C. shaking. 80 μL of the LB seed was used to inoculate 320 μL Nlim media (Table 6). After growing at 32° C. for 2 hours, the cultures were induced with IPTG (final concentration 1 mM). The cultures were then incubated at 32° C. with shaking for 20 hours if not noted otherwise, after which they were extracted following the standard extraction protocol detailed below. 
     
       
         
           
               
             
               
                 TABLE 6 
               
               
                   
               
               
                 N-lim Media Formulation 
               
               
                 N-lini Media Formulation 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
               
               
            
               
                 1 
                 × 
                 5 × Salt Soln. with NH4Cl 
               
               
                 1 
                 × 
                 1000 × Trace Vitamins 
               
               
                 1 
                 mg/L 
                 10 mg/mL Thiamine 
               
               
                 1 
                 mM 
                 1M MgSO4 
               
               
                 0.1 
                 mM 
                 1M CaCl2 
               
               
                 40 
                 g/L 
                 500 g/L glucose 
               
               
                 1 
                 × 
                 1000 × Trace minerals 
               
               
                 10 
                 mg/L 
                 10 g/L Fe Citrate 
               
               
                 100 
                 μg/mL 
                 100 mg/ml spectinomycin 
               
               
                 100 
                 mM 
                 2M BisTris (pH7.0) 
               
               
                 0.5 
                 mM 
                 Aminolevulinic acid 
               
               
                   
               
            
           
         
       
     
     Fatty Acid Species Standard Extraction and Analytical Protocol 
     To each well to be extracted, 80 μL of 1M HCl, followed by 400 μL of butyl acetate containing 500 mg/L 1-undecanol or 500 mg/L undecanoic acid as internal standard (IS) was added as internal standard (IS) was added. The 96 well plates were then heat-sealed using a plate sealer (ALPS-300 heater; Abgene, ThermoScientific, Rockford, Ill.), and shaken for 15 minutes at 2000 rpm using MIXMATE mixer (Eppendorf, Hamburg, Germany). After shaking, the plates were centrifuged for 10 minutes at 4500 rpm at room temperature (Allegra X-15R, rotor SX4750A, Beckman Coulter, Brea, Calif.) to separate the aqueous and organic layers. 50 μL of the organic layer was transferred to a 96 well plate (polypropylene, Corning, Amsterdam, The Netherlands) and derivatized with 50 uL of trimethylsiloxy/N,O-Bis(trimethylsilyl)trifluoroacetamide (TMS/BSTFA). The plate was subsequently heat sealed and stored at −20° C. until evaluated by either Gas Chromatography with Flame Ionization Detection (GC-FID) or Gas Chromatography-Mass Spectrometry (GC-MS). 
     The GC-MS parameters used to generate chromatograms and mass spectra for compounds identification were as follows: 1 μl sample was injected into analytical Column: DB-1HT, 15m×250 μm×0.1 μm, available from Agilent with cat #J&amp;W 122-1111E, Oven temperature: initial at 50° C., hold for 5 minutes, increase to 300° C. at 25° C./min, and hold for 5.24 minutes for a total run time of 24 minutes. Column flow: 1.2 mL/min, Inlet temperature: 300° C., Split ratio: 20:1, Software: ChemStation E.02.01.1177. MS parameters: Transfer line temperature: 300° C., MS source: 230° C., MS Quad: 150° C. Auto sampler: Combi PAL (CTC analytics) distributed by LEAP Technologies. The GC-FID parameters used to quantify each compound were carried out as follows: 1 μL of sample was injected onto an analytical column (UFC Rtx-1, 5 M×0.1 mm×0.1 μM) in a Thermo Fisher UltraFast TRACE GC (Thermo Fisher Scientific, West Palm Beach, Fla.). Oven temperature: initial at 100° C., hold for 0.2 minutes, increase to 320° C. at 100° C./min, and hold for 0.5 minutes for a total run time of 2.5 minutes using column flow of 0.5 ml/min, Inlet temperature: 300° C. and flame ionization detector temperature: 300° C. 
     The protocol detailed above represents standard conditions, which may be modified as necessary to optimize the analytical results. 
     Example 2 
     The following Example illustrates the conversion of exogenously added 1,3 dodeca(e)nediols to 1,3,12 dodeca(e)netriols by recombinant  E. coli  strains expressing various ω-hydroxylases. Most of the ω-hydroxylases are from the cyp153A family and were expressed either (i) as free standing catalytic cyp153 P450 enzymes or (ii) as chimeric hybrid fusion proteins (cyp153A P450 enzyme fused with a reductase domain). One ω-hydroxylases was an alkB-type ω-hydroxylase, which does not belong to the P450 family. 
     The genes for the cyp153 ω-hydroxylases were either amplified from genomic DNA or obtained by gene synthesis and cloned into a pACYC-derivative vector (p15A replicon, kanamycin resistance marker) such that they were under the control of the IPTG-inducible Ptrc promoter and in an operon with the CamA (putraredoxin reductase) and CamB (putredoxin) genes from  Pseudomonas . Chimeric P450 fusion proteins did not require CamAB coexpression. The alkB-type ω-hydroxylase from  Pseudomonas putida  was coexpressed in an operon with its cognate redox proteins alkG and alkT. All ω-hydroxylase plasmids were then transformed into an  E. coli  MG1655 derivative strain. The small scale fermentation protocol (see above) was followed and at the time of induction a mixture of 1,3 dodecanediol and (z5)1,3-dodecenediol (˜65/35%) was added to the cultures at a final concentration of 1 g/L. 
     Surprisingly, most strains with the ω-hydroxylases completely or partially converted 1,3-dodeca(e)nediols to 1,3,12-dodeca(e)netriols. In comparison to the control strain without expression of an ω-hydroxylases, two new peaks at RT 12.33 and RT 12.48 min (after TMS/BSTFA derivatization) appeared, while the two peaks corresponding to derivatized 1,3-dodeca(e)nediols disappeared or were significantly reduced (see  FIG. 5 ). 
     The mass spectrum of the peak at RT 12.33 min is shown in  FIG. 6  The fragmentation pattern indicated that this peak was (z5) 1,3,12-trimethylsilyloxy dodecene, which is the derivatized form of (z5) 1,3,12-decenetriol. Characteristic ion fragments are shown in  FIG. 6 . Ions at m/z=315, 219, 103 are useful diagnostic markers for this compound. Analogously, the peak at RT 12.48 min was identified as 1,3,12-trimethylsilyloxy dodecane, which is the derivatized form of 1,3,12-decanetriol. Characteristic ion fragments are shown in  FIG. 7 . Ions at m/z=419, 317, 103 are useful diagnostic markers for this compound. 
     As shown in table 7, the cyp153 P450 enzymes from  Marinobacter aquaeolei, Congregibacter litoralis, Limnobacter  sp. MED105,  Gordonia paraffinivorans, Blastomonas  sp. CACIA14H2 and  Caulobacter  sp. K31 showed the highest conversion to 1,3,12 dodeca(e)netriols. Table 7 also shows that cyp153A P450 from  M. aquaeolei  efficiently converted 1,3-dodeca(e)nediols to 1,3,12-dodeca(e)netriols as free standing catalytic P450 domain (CYP153A_Maqu) with discrete redox proteins or as chimeric fusion enzymes with either a PFROR-type reductase domain from  Rhodococcus  (CYP153A_RhF1/2) or a BM3-type reductase domain from  Bacillus  (CYP153A-BM3). In addition, the alkB-type ω-hydroxylase from  Pseudomonas putida  (alkBGT) also efficiently converted 1,3-dodeca(e)nediols to 1,3,12-dodeca(e)netriols. 
     
       
         
           
               
             
               
                 TABLE 7 
               
             
            
               
                   
               
               
                 Conversion of 1,3-dodecanediol to 1,3,12-dodecanetriol using various ω-hydroxylases 
               
            
           
           
               
               
               
               
            
               
                   
                   
                   
                 % Conversion 
               
               
                   
                   
                 Accession Number 
                 1,3-C12 diol* to 
               
               
                 ω-hydroxylase 
                 Microorganism 
                 or SEQ ID NO. 
                 1,3,12-C12 triol** 
               
               
                   
               
            
           
           
               
               
               
               
            
               
                 CYP153_mgp_HTCC2143 
                 
                   marine gamma 
                 
                 WP_007223979 
                 1.8 
               
               
                   
                 
                   proteobacterium 
                 
                   
                   
               
               
                   
                 HTCC2143 
                   
                   
               
               
                 CYP153_mgp_HTCC2080 
                 
                   marine gamma 
                 
                 WP_007235225 
                 15.8 
               
               
                   
                 
                   proteobacterium 
                 
                   
                   
               
               
                   
                 HTCC2080 
                   
                   
               
               
                 CYP153_Clit 
                 
                   Congregibacter 
                 
                 WP_008292970 
                 97.0 
               
               
                   
                 
                   litoralis 
                 
                   
                   
               
               
                 CYP153_Lim 
                   Limnobacter  sp. 
                 WP_008247244 
                 93.9 
               
               
                   
                 MED105 
                   
                   
               
               
                 CYP153_Caul 
                   Caulobacter  sp. K31 
                 ABZ74416 
                 44.3 
               
               
                 CYP153_Mmar 
                 
                   Mycobacterium 
                 
                 ACC41588 
                 1.7 
               
               
                   
                   marinum  str. M 
                   
                   
               
               
                 CYP153_mgp_HTCC2148 
                 
                   Marine gamma 
                 
                 EEB77967 
                 6.6 
               
               
                   
                 
                   proteobacterium 
                 
                   
                   
               
               
                   
                 HTCC2148 
                   
                   
               
               
                 CYP153_Pmed 
                 
                   Patulibacter 
                 
                 EHN09160 
                 6.0 
               
               
                   
                 
                   medicamentivorans 
                 
                   
                   
               
               
                 CYP153_Ppsy 
                 
                   Paraglaciecola 
                 
                 AGH45156 
                 1.7 
               
               
                   
                   psychrophila  170 
                   
                   
               
               
                 CYP153_Abro 
                 
                   Afipia broomeae 
                 
                 WP_006021902 
                 5.5 
               
               
                   
                 ATCC 49717 
                   
                   
               
               
                 CYP153_Rrub 
                 
                   Rhodococcus ruber 
                 
                 WP_003937314 
                 16.1 
               
               
                   
                 BKS 20-38 
                   
                   
               
               
                 CYP153_Gpar 
                 
                   Gordonia 
                 
                 WP_006901781 
                 70.8 
               
               
                   
                 
                   paraffinivorans 
                 
                   
                   
               
               
                 CYP153_A_OC4 
                   Acinetobacter  sp. 
                 AB221118 
                 0.0 
               
               
                   
                 OC4 
                   
                   
               
               
                 CYP153_Smac 
                 
                   Sphingopyxis 
                 
                 AJ850057 
                 0.0 
               
               
                   
                 
                   macrogoltabida 
                 
                   
                   
               
               
                 CYP153_M_HXN1500 
                   Mycobacterium  sp. 
                 AJ783967 
                 26.4 
               
               
                   
                 HXN-1500 
                   
                   
               
               
                 CYP153_Cmic 
                 
                   Candidatus 
                 
                 WP_012228788 
                 0.9 
               
               
                   
                 
                   Microthrix parvicella 
                 
                   
                   
               
               
                   
                 RN1 
                   
                   
               
               
                 CYP153_A_P52 
                   Afipia  sp. P52-10 
                 WP_034469539 
                 0.0 
               
               
                 CYP153_B_CACIA14H2 
                   Blastomonas  sp. 
                 ESZ86026 
                 47.2 
               
               
                   
                 CACIA14H2 
                   
                   
               
               
                 CYP153_CPha1 
                 
                   Candidatus 
                 
                 WP_043950289 
                 2.0 
               
               
                   
                 
                   Phaeomarinobacter 
                 
                   
                   
               
               
                   
                 
                   ectocarpi 
                 
                   
                   
               
               
                 CYP153_CPha2 
                 
                   Candidatus 
                 
                 WP_043950063 
                 15.5 
               
               
                   
                 
                   Phaeomarinobacter 
                 
                   
                   
               
               
                   
                 
                   ectocarpi 
                 
                   
                   
               
               
                 CYP153A_Maqu 
                 
                   Marinobacter 
                 
                 WP_011784142 
                 100.0 
               
               
                   
                 
                   aquaeolei 
                 
                   
                   
               
               
                 CYP153A_RhF1 
                 
                   Marinobacter 
                 
                 SEQ ID NO: 3 and 
                 74.9 
               
               
                   
                 
                   aquaeolei 
                 
                 SEQ ID NO: 4 
                   
               
               
                 CYP153A_RhF2 
                 
                   Marinobacter 
                 
                 SEQ ID NO: 5 and 
                 97.4 
               
               
                   
                 
                   aquaeolei 
                 
                 SEQ ID NO: 6 
                   
               
               
                 CYP153A-BM3 
                 
                   Marinobacter 
                 
                 SEQ ID NO: 7 and 
                 90.2 
               
               
                   
                 
                   aquaeolei 
                 
                 SEQ ID NO: 8 
                   
               
               
                 AlkB 
                 
                   Pseudomonas putida 
                 
                 CAB54050 
                 72.7 
               
               
                   
               
               
                 *C12 diol substrate is ~65% 1,3 dodecanediol and ~35% (z5)1,3 dodecenediol 
               
               
                 **C12 triol product is 1,3, 12 dodecanetriol and (5z)1,3,12 dodecenetriol 
               
            
           
         
       
     
     Example 3 
     The following Example illustrates the conversion of exogenously added 3-hydroxy dodecanoic acid to 3,12-dihydroxy dodecanoic acid by recombinant  E. coli  strains expressing various ω-hydroxylases. 
     The  E. coli  strains, ω-hydroxylases and experimental design are identical to Example 2, except that in this Example, 3-hydroxy dodecanoic acid was added at induction at a final concentration of 1 g/L (instead of 1,3 dodeca(e)nediol). 
     Surprisingly, most strains with the ω-hydroxylases completely or partially converted 3-hydroxy dodecanoic acid to 3,12-dihydroxy dodecanoic acid. In comparison to the control strain without expression of an ω-hydroxylases, one new peak at RT 13.25 minutes (after BSTFA derivatization) appeared, while the 3-hydroxy dodecanoic acid peak disappeared or was reduced (see  FIG. 8 ). 
     The mass spectrum of the peak at RT 13.25 min is shown in  FIG. 9 . The fragmentation pattern indicated that this peak was 3,12-trimethylsilyloxy-dodecanoic acid trimethylsilyl ester, which is the derivatized form of 3,12-dihydroxy dodecanoic acid. Characteristic ion fragments used to identify 3,12-trimethylsilyloxy-dodecanoic acid trimethylsilyl ester are shown in  FIG. 9 . Ions at m/z=433 and 233 are useful diagnostic markers for these compounds. The ion at m/z 433 was used to determine the chain length after loss of CH 3  (m/z=448-15) and ion at 233 was used to determine the fragment ion of —(CH3SiO)CHCH2COOSi(CH3)3 ( FIG. 9 ). 
     As shown in Table 8, the cyp153A P450 enzymes from  Marinobacter aquaeolei, Congregibacter litoralis , Limnobacter sp. MED105, Blastomonas sp. CACIA14H2 and  Caulobacter  sp. K31 showed the highest conversion to 3,12-dihydroxy dodecanoic acid. Table 8 also shows that cyp153A P450 from  M aquaeolei  efficiently converted 3-hydroxy dodecanoic acid to 3,12-dihydroxy dodecanoic acid as free standing catalytic P450 domain (CYP153A_Maqu) with discrete redox proteins and as chimeric fusion enzyme with either a PFROR-type reductase domain from  Rhodococcus  (CYP153A_RhF01/2) or a BM3-type reductase domain from  Bacillus  (CYP153A-BM3). In addition, the alKB-type ω-hydroxylase from  Pseudomonas putida  (alkBGT) also converted 3-hydroxy dodecanoic acid to 3,12-dihydroxy dodecanoic acid. 
     
       
         
           
               
             
               
                 TABLE 8 
               
             
            
               
                   
               
               
                 Conversion of 3-hydroxy dodecanoic acid to 3,12-dihydroxy  
               
               
                 dodecanoic acid using various ω-hydroxylases 
               
            
           
           
               
               
               
               
            
               
                   
                   
                   
                 % Conversion 
               
               
                   
                   
                   
                 3-OH dodecanoic acid 
               
               
                   
                   
                   
                 to 3,12 diOH 
               
               
                 ω-hydroxylase 
                 Microorganism 
                 Accession Number 
                 dodecanoic acid 
               
               
                   
               
            
           
           
               
               
               
               
            
               
                 CYP153_mgp_HTCC2143 
                 
                   marine gamma 
                 
                 WP_007223979 
                 0.0 
               
               
                   
                 
                   proteobactenum 
                 
                   
                   
               
               
                   
                 HTCC2143 
                   
                   
               
               
                 CYP153_mgp_HTCC2080 
                 
                   marine gamma 
                 
                 WP_007235225 
                 12.4 
               
               
                   
                 
                   proteobacterium 
                 
                   
                   
               
               
                   
                 HTCC2080 
                   
                   
               
               
                 CYP153_Clit 
                 
                   Congregibacter 
                 
                 WP_008292970 
                 100.0 
               
               
                   
                 
                   litoralis 
                 
                   
                   
               
               
                 CYP153_Lim 
                   Limnobacter  sp. 
                 WP_008247244 
                 94.3 
               
               
                   
                 MED105 
                   
                   
               
               
                 CYP153_Caul 
                   Caulobacter  sp. K31 
                 ABZ74416 
                 42.0 
               
               
                 CYP153_Mmar 
                 
                   Mycobacterium 
                 
                 ACC41588 
                 0.0 
               
               
                   
                   marinum  str. M 
                   
                   
               
               
                 CYP153_mgp_HTCC2148 
                 
                   Marine gamma 
                 
                 EEB77967 
                 21.5 
               
               
                   
                 
                   proteobacterium 
                 
                   
                   
               
               
                   
                 HTCC2148 
                   
                   
               
               
                 CYP153_Pmed 
                 
                   Patulibacter 
                 
                 EHN09160 
                 0.0 
               
               
                   
                 
                   medicamentivorans 
                 
                   
                   
               
               
                 CYP153_Ppsy 
                 
                   Paraglaciecola 
                 
                 AGH45156 
                 1.3 
               
               
                   
                   psychrophila  170 
                   
                   
               
               
                 CYP153_Abro 
                 
                   Afipia broomeae 
                 
                 WP_006021902 
                 12.5 
               
               
                   
                 ATCC 49717 
                   
                   
               
               
                 CYP153_Rrub 
                 
                   Rhodococcus ruber 
                 
                 WP_003937314 
                 8.3 
               
               
                   
                 BKS 20-38 
                   
                   
               
               
                 CYP153_Gpar 
                 
                   Gordonia 
                 
                 WP_006901781 
                 2.0 
               
               
                   
                 
                   paraffinivorans 
                 
                   
                   
               
               
                 CYP153_A_OC4 
                   Acinetobacter  sp. 
                 AB221118 
                 0.0 
               
               
                   
                 OC4 
                   
                   
               
               
                 CYP153_Smac 
                 
                   Sphingopyxis 
                 
                 AJ850057 
                 1.0 
               
               
                   
                 
                   macrogoltabida 
                 
                   
                   
               
               
                 CYP153_M_HXN1500 
                   Mycobacterium  sp. 
                 AJ783967 
                 0.5 
               
               
                   
                 HXN-1500 
                   
                   
               
               
                 CYP153_Cmic 
                 
                   Candidatus 
                 
                 WP_012228788 
                 2.0 
               
               
                   
                 
                   Microthrix 
                 
                   
                   
               
               
                   
                   parvicella  RN1 
                   
                   
               
               
                 CYP153_A_P52 
                   Afipia  sp. P52-10 
                 WP_034469539 
                 0.0 
               
               
                 CYP153_B_CACIA14H2 
                 Blastomonas sp. 
                 ESZ86026 
                 92.0 
               
               
                   
                 CACIA14H2 
                   
                   
               
               
                 CYP153_CPha1 
                 
                   Candidatus 
                 
                 WP_043950289 
                 0.0 
               
               
                   
                 
                   Phaeomarinobacter 
                 
                   
                   
               
               
                   
                 
                   ectocarpi 
                 
                   
                   
               
               
                 CYP153_CPha2 
                 
                   Candidatus 
                 
                 WP_043950063 
                 20.7 
               
               
                   
                 
                   Phaeomarinobacter 
                 
                   
                   
               
               
                   
                 
                   ectocarpi 
                 
                   
                   
               
               
                 CYP153A_Maqu 
                 
                   Marinobacter 
                 
                 WP_011784142 
                 100.0 
               
               
                   
                 
                   aquaeolei 
                 
                   
                   
               
               
                 CYP153A_RhF1 
                 
                   Marinobacter 
                 
                 SEQ ID NO: 3 and 
                 86.1 
               
               
                   
                 
                   aquaeolei 
                 
                 SEQ ID NO: 4 
                   
               
               
                 CYP153A_RhF2 
                 
                   Marinobacter 
                 
                 SEQ ID NO: 5 and 
                 29.4 
               
               
                   
                 
                   aquaeolei 
                 
                 SEQ ID NO: 6 
                   
               
               
                 CYP153A-BM3 
                 
                   Marinobacter 
                 
                 SEQ ID NO: 7 and 
                 86.8 
               
               
                   
                 
                   aquaeolei 
                 
                 SEQ ID NO: 8 
                   
               
               
                 AlkB 
                 
                   Pseudomonas putida 
                 
                 CAB54050 
                 23.2 
               
               
                   
               
            
           
         
       
     
     Example 4 
     The following Example illustrates the conversion of exogenously added 1,3-dodeca(e)nediols to various dodeca(e)netriols by a recombinant  E. coli  strain expressing a “subterminal” co-hydroxylase from  Bacillus lichenformis  (cyp102A1_Blic). 
     The gene for cyp102A1_Blic was amplified from genomic DNA and cloned into a pCL-derivative vector (SC101 replicon, spectinomycin resistance marker) such that it was under the control of the IPTG-inducible Ptrc. The resulting plasmid, pKM.046, was then transformed into an  E. coli  MG1655 derivative strain. The small scale fermentation protocol (see Example 1 above) was followed and at the time of induction a mixture of 1,3 dodecanediol and (z5)1,3-dodecenediol (˜65/35%) was added to the cultures at a final concentration of 1 g/L. 
     Surprisingly, the strain with cyp102A7_Blic almost completely converted 1,3-dodeca(e)nediols to various dodeca(e)netriols. In comparison to the control strain without expression of an ω-hydroxylases, six new peaks between RT 12.0 and 12.5 min (after TMS/BSTFA derivatization) appeared, while the two 1,3-dodeca(e)nediols derivatized peaks almost completely disappeared (see  FIG. 10 ). 
     After TMS/BSTFA derivatization, the six peaks were identified from shortest to longest RT as (z5) 1,3,9-trimethylsilyloxy dodecene, 1,3,9-trimethylsilyloxy dodecane, (z5) 1,3,10-trimethylsilyloxy dodecene, (z5) 1,3,11-trimethylsilyloxy dodecene, 1,3,10-trimethylsilyloxy dodecane and 1,3,11-trimethylsilyloxy dodecane which are the derivatized form of (z5) 1,3,9-dodecenetriol, 1,3,9-dodecanetriol, (z5) 1,3,10-dodecenetriol, (z5) 1,3,11-dodecenetriol, 1,3,10-dodecanetriol and 1,3,11-dodecanetriol, respectively (see  FIG. 10 ). The mass spectrum of the derivatized compounds and characteristic fragment ions used to identify these structures are shown in  FIGS. 11-16 :  FIG. 11 : (z5) 1,3,9-trimethylsilyloxy dodecene,  FIG. 12 :  1 , 3 , 9 -trimethylsilyloxy dodecane,  FIG. 13 : (z5) 1,3,10-trimethylsilyloxy dodecene,  FIG. 14 : (z5) 1,3,11-trimethylsilyloxy dodecene,  FIG. 15 : 1,3,10-trimethylsilyloxy dodecane and  FIG. 16 :  1 , 3 , 11 -trimethylsilyloxy dodecane. 
     Example 5 
     The following Example illustrates production of 1,3,12-dodecanetriol from a renewable carbohydrate feedstock such as glucose, by recombinant  E. coli  strains expressing pathway genes for the production of 1,3 diols and either a P450 ω-hydroxylase, cyp153A(G307A) from  M. aquaeolei , or a chimeric hybrid-protein in which a CYP153A P450 hydroxylase is fused with a reductase domain, cyp153A-RhF2. 
     The gene for the cyp153A(G307A) was amplified from genomic DNA and cloned into a pACYC-derivative vector (p15A replicon, kanamycin resistance marker) such that it was under the control of the IPTG-inducible Ptrc promoter and in an operon with the CamA (putraredoxin reductase) and CamB (putredoxin) genes resulting in plasmid pZR.395 (Table 9). The gene for cyp153A-RhF2 was amplified from a plasmid and cloned into a pACYC-derivative vector (p15A replicon, kanamycin resistance marker) resulting in plasmid pIR.092 (Table 9). 
     Plasmid pNH308 (Table 9), a pCL1920-derivative vector (SC101 replicon, spectinomycin resistance marker), contained the following operon controlled by the IPTG-inducible Ptrc promoter: a fatty acid reductase variant, carB8 from  Mycobacterium smegmatis , a thioesterase, fatB1 from  Umbellularia californica , an alcohol dehydrogenase, AlrA from  Acinetobacter baylyi , and variants of β-ketoacyl-ACP synthase, fabB, and of a transcriptional regulator, fadR, both from  E.coli.    
     The genome of base strain stNH1525 (Table 10) was engineered as follows: the acyl-CoA dehydrogenase (fadE) gene was attenuated. A phosphopantetheinyl transferase (entD) and a synthetic fatty acid biosynthesis operon (consisting of an enoyl-ACP reductase, an ACP-malonyltransferase, a β-ketoacyl-ACP reductase and a 3-hydroxyacyl-ACP dehydratase and two β-ketoacyl-ACP synthases) were overexpressed. Plasmids pZR.395 and pIR.092 were cotransformed with plasmid pNH.308 into stHN1525 resulting in strains sAS.548 and sZR519, respectively (Table 9). Both strains were subjected to small scale fermentation and product analysis as described in the methods (see above). 
     Both strains produced triols, which were identified as described in example 1. Strain sAS.548 produced 104 mg/L 1,3,12 dodecanetriol from glucose and strain sZR.519 produced 62 mg/L 1,3,12 dodecanetriol from glucose. Besides triols, sAS.548 and sZR.519 produced various fatty alcohols (533 and 898 mg/L, respectively) and diols (477 and 377 mg/L, respectively). 
     This example showed that  E. coli  strains engineered for producing 1,3 diols when combined with the expression of aCYP153 P450 ω-hydroxylase or achimeric hybrid-protein CYP153 P450 ω-hydroxylase produced fatty triols from glucose. 
     
       
         
           
               
             
               
                 TABLE 9 
               
             
            
               
                   
               
               
                 Plasmids used for triol or dihydroxy fatty acid production from glucose 
               
            
           
           
               
               
            
               
                 Plasmid Name 
                 Pathway Genes 
               
               
                   
               
               
                 pZR.395 
                 pACYC-trc-cyp153A(G307A)-camA-camB 
               
               
                 pIR.092 
                 pACYC-trc-cyp153A(G307A)-RhF2 
               
               
                 pZR.468 
                 pACYC-trc-cyp102A7 
               
               
                 pKM.046 
                 pCL-trc-cyp102A7 
               
               
                 pNH.308 
                 pCL-trc-carB-fatB1-alrA-fabB-fadR 
               
               
                 pNH.328 
                 pCL-trc-carB-phaG-alrA 
               
               
                 pKEV199 
                 pCL-trc-fatB1 
               
               
                 pZR.427 
                 pCL-trc-fatA3-fabB-T5-cyp153A-RhF2 
               
               
                 pKM.080 
                 pCL-trc-fatA3-fabB-T5-cyp102A7 
               
               
                 pAL.001 
                 pACYC-ohyA1_Smal 
               
               
                 pAL.002 
                 pACYC-ohyA2_Smal 
               
               
                   
               
            
           
         
       
     
     
       
         
           
               
             
               
                 TABLE 10 
               
             
            
               
                   
               
               
                 Strains used for triol or dihydroxy  
               
               
                 fatty acid production from glucose 
               
            
           
           
               
               
            
               
                 Strain Name 
                 Description 
               
               
                   
               
               
                 stNH1525 
                 Base strain, no plasmids 
               
               
                 AA.207 
                 Base strain, no plasmids 
               
               
                 TLC2 
                 Base strains, no plasmids 
               
               
                 sAS.548 
                 stNH1525 with plasmids pNH308 and pZR.395 
               
               
                 sZR.519 
                 stNH1525 with plasmids pNH308 and pIR.092 
               
               
                 sZR.521 
                 stNH1525 with plasmids pNH308 and pZR.468 
               
               
                 sZR.525 
                 AA.207 with plasmids pKEV199 and pIR.092 
               
               
                 sAL.131 
                 TLC2 with plasmids AA.233 with plasmids  
               
               
                   
                 pAL.001 and pZR.427 
               
               
                 sAL.132 
                 TLC2 with plasmids pAL.002 and pZR.427 
               
               
                 sAL.134 
                 TLC2 with plasmids pAL.001 and pKM.080 
               
               
                 sAL.135 
                 TLC2 with plasmids pAL.002 and pKM.080 
               
               
                   
               
            
           
         
       
     
     Example 6 
     The following Example illustrates production of subterminally-hydroxylated triols from a renewable carbohydrate feedstock such as glucose, by a recombinant  E. coli  strain expressing pathway genes for the production of 1,3 diols and a cyp102A7 P450 hydroxylase from  B. licheniformis , cyp102A7 Blic. 
     The gene for the cyp102A7_Blic was amplified from genomic DNA and cloned into a pACYC-derivative vector (p15A replicon, kanamycin resistance marker) such that it was under the control of the IPTG-inducible Ptrc promoter resulting in plasmid pZR.468 (Table 9). 
     Plasmids pZR.468 was cotransformed with plasmid pNH.308 into stNH1525 (see Example 5) resulting in strain sZR.521 (Table 10). The strain was subjected to small scale fermentation and product analysis as described in the methods (Example 1). 
     The strain produced triols, which were identified as described in Example 4. sZR.521 produced 122 mg/L 1,3,10-dodecanetriol and 24 mg/L 1,3,11-dodecanetriol from glucose. Besides triols, sZR.521 produced various fatty alcohols (614 mg/L) and diols (318 mg/L, respectively). 
     This example showed that  E. coli  strains engineered for producing 1,3 diols when combined with the expression of a CYP102A7 P450 hydroxylase produced fatty triols from glucose. 
     Example 7 
     The following Example illustrates production of 3,12-dihydroxy dodecanoic acid from a renewable carbohydrate feedstock such as glucose, by recombinant  E. coli  strains expressing pathway genes for the production of 3-hydroxy fatty acids and a cyp153A P450 w-hydroxylase. 
     The gene for cyp153A-RhF2 was amplified from a plasmid and cloned into a pACYC-derivative vector (p15A replicon, kanamycin resistance marker) such that it was under the control of the IPTG-inducible Ptrc promoter resulting in plasmid pIR.092 (Table 9). 
     Plasmid pKEV199 (Table 9), a pCL1920-derivative vector (SC101 replicon, spectinomycin resistance marker), contained a thioesterase, fatB1 from  Umbellularia californica , controlled by the IPTG-inducible Ptrc promoter. 
     The genome of base strain AA.207 (Table 9) was engineered as follows: the acyl-CoA dehydrogenase (fadE) gene was attenuated and a synthetic fatty acid biosynthesis operon (consisting of an enoyl-ACP reductase, an ACP-malonyltransferase, a β-ketoacyl-ACP reductase and a 3-hydroxyacyl-ACP dehydratase and two β-ketoacyl-ACP synthases) and a variant of the transcriptional regulator fadR were overexpressed. 
     Plasmid pIR.092 (see Example 5 and Table 9) was cotransformed with plasmid pKEV199 into stHN1525 resulting in strain sZR525 (Table 9). The strain was subjected to small scale fermentation and product analysis as described in the methods (see above). 
     The strains produced dihydroxy-fatty acids, which were identified as described in Example 3. Strain sZR.525 produced 6 mg/L 3,12-dihydroxy dodecanoic acid from glucose. Besides dihydroxy fatty acids, sZR.525 produced various fatty acids (411 mg/L) and 3-hydroxy fatty acids (1089 mg/L, respectively). 
     This example showed that an  E. coli  strain engineered for producing 3-hydroxy fatty acids when combined with the expression of a CYP153 P450 w-hydroxylase produced dihydroxy fatty acids from glucose. 
     Example 8 
     Production of 10,16-dihydroxy hexadecanoic acid by a recombinant  E. coli  strain from a simple carbon source. 
     This example shows the production of 10,16-dihydroxy hexadecanoic acid from a renewable carbohydrate feedstock such as glucose, by recombinant  E. coli  strains expressing pathway genes for two fatty acid-hydroxylating enzymes, the chimeric hybrid-protein cyp153A-RhF2 from  M. aquaeolei , and OhyA1 or OhyA2 from  Stenotrophomonas maltophilia.    
     Plasmid pAL.001 and pAL.002 (Table 9), pACYC-derivative vectors (p15A replicon, kanamycin resistance marker), contained the fatty acid hydroxylases ohyA1 and ohyA2 from  S. maltophilia , respectively, controlled by the IPTG-inducible Ptrc promoter. Plasmid pZR.427 (Table 9), a pCL1920-derivative vector (SC101 replicon, spectinomycin resistance marker), contained the following two operons: (i) the IPTG-inducible Ptrc promoter controlling thioesterase FatA from  A. thaliana  and  p -ketoacyl-ACP synthase, fabB, and (ii) a IPTG-inducible PT5 promoter controlling cyp153A-RhF2 from  M. aquaeolei.    
     The genome of base strain TLC2 (Table 10) was a derivative of  E. coli  MG1655 with an attenuated acyl-CoA dehydrogenase (fadE) gene. 
     Plasmid pZR.427 was cotransformed with plasmids pAL.001 or pAL.002 into TLC2 resulting in strains sAL.131 and sAL.132, respectively (Table 9). The strains were subjected to small scale fermentation and product analysis as described in the methods (see above). 
     The extracts from strains sAL.131 ( FIG. 17A ) and sAL.132 showed two new peaks at RT 12.692 and 14.415 min (after TMS/BSTFA derivatization), that were not observed in the control strain without expressing ohyA1 or ohyA2 ( FIG. 17B ). The mass spectrum and the retention time of the peak at RT 12.692 min in comparison with authentic standard sample indicated that this peak was trimethylsilyl derivative of 10-hydroxy hexadecanoic acid (10-OH C16:0 FFA). The mass spectrum of the peak at 14.415 min is shown in  FIG. 18 . The fragmentation pattern indicated that this peak was trimethylsilyl derivative of 10,16-dihydroxy hexadecanoic acid (10,16-diOH C16:0 FFA) which is derived from 10-hydroxy hexadecanoic acid (10-OH C16:0 FFA). Characteristic ion fragments are shown in  FIG. 18 . Ions at m/z=489, 331 and 275 are useful diagnostic markers for this compound. 
     Strain sAL.131 and sAL.132 produced 14 mg/L and 9 mg/L 10,16-hexadecanoic acid from glucose, respectively. Besides 10,16-hexadecanoic acid both strains also produced 10-hydroxy hexadecanoic acid, 16-hydroxy hexadecanoic acid, hexadecanoic acid, (z9)-hexadecenoic acid and small amounts of other fatty acid derivatives. 
     This example showed that  E. coli  strains engineered for producing fatty acids when combined with the expression of a CYP153A P450 ω-hydroxylase and a fatty acid hydratase produced dihydroxy fatty acids from glucose. 
     Example 9 
     Production of 10,13-, 10,14- and 10,15-dihydroxy hexadecanoic acid by a recombinant  E. coli  strain from a simple carbon source. 
     This example shows the production of 10,13-, 10,14- and 10,15-dihydroxy hexadecanoic acid from a renewable carbohydrate feedstock such as glucose, by recombinant  E. coli  strains expressing pathway genes for two fatty acid-hydroxylating enzymes, cyp102A7 from  B. licheniformis , and OhyA1 or OhyA2 from  Stenotrophomonas maltophilia.    
     Plasmid pAL.001 and pAL.002 (Table 9), pACYC-derivative vectors (p15A replicon, kanamycin resistance marker), contained the fatty acid hydroxylases ohyA1 and ohyA2 from  S. maltophilia , respectively, controlled by the IPTG-inducible Ptrc promoter. Plasmid pKM.080 (Table 9), a pCL1920-derivative vector (SC101 replicon, spectinomycin resistance marker), contained the following two operons: (i) the IPTG-inducible Ptrc promoter controlling thioesterase fatA from  A. thaliana  and  p -ketoacyl-ACP synthase, fabB, and (ii) a IPTG-inducible PT5 promoter controlling cyp102A7 from  B. licheniformis.    
     Plasmid pKM.080 was cotransformed with plasmids pAL.001 or pAL.002 into TLC2 (see Example 8 and Table 10) resulting in strains sAL.134 and sAL.135, respectively (Table 9). The strains were subjected to small scale fermentation and product analysis as described in the methods (see above). 
     In comparison to a control strain without expression of ohyA1 or ohyA2, three major new peaks at RT 12.692, 13.948 and 14.062 min (after TMS/BSTFA derivatization) appeared in extracts from strains sAL.134 and sAL.135. (data not shown). The mass spectrum scan through the peak at RT 12.692 indicated that this peak was a mixture of two products. The fragmentation patterns indicated that the major product was the trimethylsilyl derivative of 10-hydroxy hexadecanoic acid (10-OH C16:0 FFA) as confirmed using authentic standard sample and the minor product was trimethylsilyl derivative of 10,13-dihydroxy hexadecanoic acid (10,13-diOH C16:0) ( FIG. 19 ). Characteristic ions of trimethylsilyl derivative of 10,13-dihydroxy hexadecanoic acid (10,13-diOH C16:0) obtained from this scan is shown in  FIG. 19 . Characteristic ions at 331 and 145 are useful diagnostic markers for this compound. 
     The mass spectrum of the peak at 13.948 min is shown in  FIG. 20 . The fragmentation patterns indicated that this peak was the tetramethylsilyl derivative of 10,14-dihydroxy hexadecanoic acid (10,14-diOH C16:0 FFA). Characteristic ion fragments are shown in  FIG. 20 . Ions at m/z=489, 331, 275 and 131 are useful diagnostic markers for this compound. 
     The mass spectrum of the peak at RT 14.062 min is shown in  FIG. 21 . The fragmentation pattern indicated that this peak was the trimethylsilyl derivative of 10,15-dihydroxy hexadecanoic acid (10,15-diOH C16:0 FFA). Characteristic ion fragments are shown in  FIG. 21 . Ions at m/z=489, 331, 275, 117 are useful diagnostic markers for this compound. 
     Strain sAL.134 produced from glucose 17 mg/L 10,14-dihydroxy hexadecanoic acid and 28 mg/L 10,15-dihydroxy hexadecanoic acid, the amount of 10,13-dihydroxy hexadecanoic acid could not be quantified as the GC peak overlapped with 10-hydroxy hexadecanoic acid. Strain sAL.135 produced from glucose 13 mg/L 10,14-dihydroxy hexadecanoic acid and 10,15-dihydroxy hexadecanoic acid produced was under the quantitation limit, the amount of 10,13-dihydroxy hexadecanoic acid could not be quantified as the GC peak overlapped with 10-hydroxy hexadecanoic acid. 
     Both strains also produced 10-hydroxy hexadecanoic acid, 15-hydroxy hexadecanoic acid, 14-hydroxy hexadecanoic acid, 13-hydroxy hexadecanoic acid, hexadecanoic acid, (z9)-hexadecenoic acid and small amounts of other fatty acid derivatives. 
     This example showed that  E. coli  strains engineered for producing fatty acids when combined with the expression of a CYP1012A subterminal-hydroxylase and a fatty acid hydratase produced dihydroxy fatty acids from glucose. 
     As is apparent to one of skill in the art, various modifications and variations of the above aspects and embodiments can be made without departing from the spirit and scope of this disclosure. Such modifications and variations are thus within the scope of this disclosure. 
     
       
         
           
               
             
               
                 APPENDIX 1 
               
               
                   
               
               
                 SEQUENCES 
               
               
                   
               
             
            
               
                   
               
            
           
           
               
            
               
                 Cyp153A (G307A) from  Marinobacter aquaeolei  (DNA) 
               
               
                 SEQ ID NO: 1 
               
               
                 ATGCCAACACTGCCCAGAACATTTGACGACATTCAGTCCCGACTGATTAACGCCACC 
               
               
                 TCCAGGGTGGTGCCGATGCAGAGGCAAATTCAGGGACTGAAATTCTTAATGAGCGC 
               
               
                 CAAGAGGAAGACCTTCGGCCCACGCCGACCGATGCCCGAATTCGTTGAAACACCCA 
               
               
                 TCCCGGACGTTAACACGCTGGCCCTTGAGGACATCGATGTCAGCAATCCGTTTTTAT 
               
               
                 ACCGGCAGGGTCAGTGGCGCGCCTATTTCAAACGGTTGCGTGATGAGGCGCCGGTC 
               
               
                 CATTACCAGAAGAACAGCCCTTTCGGCCCCTTCTGGTCGGTAACTCGGTTTGAAGAC 
               
               
                 ATCCTGTTCGTGGATAAGAGTCACGACCTGTTTTCCGCCGAGCCGCAAATCATTCTC 
               
               
                 GGTGACCCTCCGGAGGGGCTGTCGGTGGAAATGTTCATAGCGATGGATCCGCCGAA 
               
               
                 ACACGATGTGCAGCGCAGCTCGGTGCAGGGAGTAGTGGCACCGAAAAACCTGAAGG 
               
               
                 AGATGGAGGGGCTGATCCGATCACGCACCGGCGATGTGCTTGACAGCCTGCCTACA 
               
               
                 GACAAACCCTTTAACTGGGTACCTGCTGTTTCCAAGGAACTCACAGGCCGCATGCTG 
               
               
                 GCGACGCTTCTGGATTTTCCTTACGAGGAACGCCACAAGCTGGTTGAGTGGTCGGAC 
               
               
                 AGAATGGCAGGTGCAGCATCGGCCACCGGCGGGGAGTTTGCCGATGAAAATGCCAT 
               
               
                 GTTTGACGACGCGGCAGACATGGCCCGGTCTTTCTCCAGGCTTTGGCGGGACAAGGA 
               
               
                 GGCGCGCCGCGCAGCAGGCGAGGAGCCCGGTTTCGATTTGATCAGCCTGTTGCAGA 
               
               
                 GCAACAAAGAAACGAAAGACCTGATCAATCGGCCGATGGAGTTTATCGGTAATTTG 
               
               
                 ACGCTGCTCATAGTCGcCGGCAACGATACGACGCGCAACTCGATGAGTGGTGGCCTG 
               
               
                 GTGGCCATGAACGAATTCCCCAGGGAATTTGAAAAATTGAAGGCAAAACCGGAGTT 
               
               
                 GATTCCGAACATGGTGTCGGAAATCATCCGCTGGCAAACGCCGCTGGCCTATATGCG 
               
               
                 CCGAATCGCCAAGCAGGATGTCGAACTGGGCGGCCAGACCATCAAGAAGGGTGATC 
               
               
                 GAGTTGTCATGTGGTACGCGTCGGGTAACCGGGACGAGCGCAAATTTGACAACCCC 
               
               
                 GATCAGTTCATCATTGATCGCAAGGACGCACGAAACCACATGTCGTTCGGCTATGGG 
               
               
                 GTTCACCGTTGCATGGGCAACCGTCTGGCTGAACTGCAACTGCGCATCCTCTGGGAA 
               
               
                 GAAATACTCAAGCGTTTTGACAACATCGAAGTCGTCGAAGAGCCCGAGCGGGTGCA 
               
               
                 GTCCAACTTCGTGCGGGGCTATTCCAGGTTGATGGTCAAACTGACACCGAACAGTTA 
               
               
                 A 
               
               
                   
               
               
                 Cyp153A (G307A) from  Marinobacter aquaeolei  (protein) 
               
               
                 SEQ ID NO: 2 
               
               
                 MPTLPRTFDDIQSRLINATSRVVPMQRQIQGLKFLMSAKRKTFGPRRPMPEFVETPIPDV 
               
               
                 NTLALEDIDVSNPFLYRQGQWRAYFKRLRDEAPVHYQKNSPFGPFWSVTRFEDILFVDK 
               
               
                 SHDLFSAEPQIILGDPPEGLSVEMFIAMDPPKHDVQRSSVQGVVAPKNLKEMEGLIRSRT 
               
               
                 GDVLDSLPTDKPFNWVPAVSKELTGRMLATLLDFPYEERHKLVEWSDRMAGAASATG 
               
               
                 GEFADENAMFDDAADMARSFSRLWRDKEARRAAGEEPGFDLISLLQSNKETKDLINRP 
               
               
                 MEFIGNLTLLIVAGNDTTRNSMSGGLVAMNEFPREFEKLKAKPELIPNMVSEIIRWQTPL 
               
               
                 AYMRRIAKQDVELGGQTIKKGDRVVMWYASGNRDERKFDNPDQFIIDRKDARNHMSF 
               
               
                 GYGVHRCMGNRLAELQLRILWEEILKRFDNIEVVEEPERVQSNFVRGYSRLMVKLTPNS. 
               
               
                   
               
               
                 Cyp153A-RhF1, chimeric hybrid-fusion protein (DNA) 
               
               
                 SEQ ID NO: 3 
               
               
                 ATGCCAACACTGCCCAGAACATTTGACGACATTCAGTCCCGACTGATTAACGCCACC 
               
               
                 TCCAGGGTGGTGCCGATGCAGAGGCAAATTCAGGGACTGAAATTCTTAATGAGCGC 
               
               
                 CAAGAGGAAGACCTTCGGCCCACGCCGACCGATGCCCGAATTCGTTGAAACACCCA 
               
               
                 TCCCGGACGTTAACACGCTGGCCCTTGAGGACATCGATGTCAGCAATCCGTTTTTAT 
               
               
                 ACCGGCAGGGTCAGTGGCGCGCCTATTTCAAACGGTTGCGTGATGAGGCGCCGGTC 
               
               
                 CATTACCAGAAGAACAGCCCTTTCGGCCCCTTCTGGTCGGTAACTCGGTTTGAAGAC 
               
               
                 ATCCTGTTCGTGGATAAGAGTCACGACCTGTTTTCCGCCGAGCCGCAAATCATTCTC 
               
               
                 GGTGACCCTCCGGAGGGGCTGTCGGTGGAAATGTTCATAGCGATGGATCCGCCGAA 
               
               
                 ACACGATGTGCAGCGCAGCTCGGTGCAGGGAGTAGTGGCACCGAAAAACCTGAAGG 
               
               
                 AGATGGAGGGGCTGATCCGATCACGCACCGGCGATGTGCTTGACAGCCTGCCTACA 
               
               
                 GACAAACCCTTTAACTGGGTACCTGCTGTTTCCAAGGAACTCACAGGCCGCATGCTG 
               
               
                 GCGACGCTTCTGGATTTTCCTTACGAGGAACGCCACAAGCTGGTTGAGTGGTCGGAC 
               
               
                 AGAATGGCAGGTGCAGCATCGGCCACCGGCGGGGAGTTTGCCGATGAAAATGCCAT 
               
               
                 GTTTGACGACGCGGCAGACATGGCCCGGTCTTTCTCCAGGCTTTGGCGGGACAAGGA 
               
               
                 GGCGCGCCGCGCAGCAGGCGAGGAGCCCGGTTTCGATTTGATCAGCCTGTTGCAGA 
               
               
                 GCAACAAAGAAACGAAAGACCTGATCAATCGGCCGATGGAGTTTATCGGTAATTTG 
               
               
                 ACGCTGCTCATAGTCGcCGGCAACGATACGACGCGCAACTCGATGAGTGGTGGCCTG 
               
               
                 GTGGCCATGAACGAATTCCCCAGGGAATTTGAAAAATTGAAGGCAAAACCGGAGTT 
               
               
                 GATTCCGAACATGGTGTCGGAAATCATCCGCTGGCAAACGCCGCTGGCCTATATGCG 
               
               
                 CCGAATCGCCAAGCAGGATGTCGAACTGGGCGGCCAGACCATCAAGAAGGGTGATC 
               
               
                 GAGTTGTCATGTGGTACGCGTCGGGTAACCGGGACGAGCGCAAATTTGACAACCCC 
               
               
                 GATCAGTTCATCATTGATCGCAAGGACGCACGAAACCACATGTCGTTCGGCTATGGG 
               
               
                 GTTCACCGTTGCATGGGCAACCGTCTGGCTGAACTGCAACTGCGCATCCTCTGGGAA 
               
               
                 GAAATACTCAAGCGTTTTGACAACATCGAAGTCGTCGAAGAGCCCGAGCGGGTGCA 
               
               
                 GTCCAACTTCGTGCGGGGCTATTCCAGGTTGATGGTCAAACTGACACCGAACAGTGT 
               
               
                 ACTCCATCGTCATCAACCTGTCACCATCGGCGAGCCGGCCGCTCGTGCTGTGAGCCG 
               
               
                 CACGGTGACCGTTGAGCGTCTTGATCGCATTGCCGACGATGTCCTTCGCCTGGTCCTT 
               
               
                 CGCGATGCTGGAGGTAAAACCCTCCCGACGTGGACGCCTGGCGCTCACATCGACCT 
               
               
                 GGATCTGGGtGCTCTGAGCCGTCAGTATTCGCTCTGCGGCGCTCCGGATGCTCCGTCG 
               
               
                 TACGAAATCGCCGTGCACTTAGATCCgGAAAGCCGTGGTGGAAGCCGCTATATTCAT 
               
               
                 GAACAGCTGGAAGTTGGAAGTCCGCTGCGTATGCGtGGCCCACGCAACCATTTCGCC 
               
               
                 CTGGATCCGGGtGCGGAACATTACGTGTTTGTTGCCGGGGGTATCGGCATCACGCCG 
               
               
                 GTGCTGGCAATGGCGGATCATGCCCGTGCGCGTGGTTGGTCGTACGAACTGCATTAT 
               
               
                 TGTGGTCGTAATCGTAGCGGTATGGCTTACCTGGAACGCGTCGCGGGACATGGTGAC 
               
               
                 CGCGCtGCCTTGCACGTATCTGAAGAAGGCACCCGCATTGATCTGGCGGCATTACTT 
               
               
                 GCTGAACCGGCGCCGGGCGTGCAAATCTACGCCTGCGGTCCGGGCCGTTTATTAGCG 
               
               
                 GGTCTTGAAGACGCGTCTCGTAATTGGCCGGATGGCGCGCTTCATGTGGAGCATTTC 
               
               
                 ACTTCGAGTTTAGCCGCTTTGGATCCGGATGTCGAACATGCCTTTGATTTGGAGCTG 
               
               
                 CGTGACTCTGGCCTTACCGTTCGCGTCGAGCCAACTCAGACCGTTTTAGACGCTTTG 
               
               
                 CGTGCGAACAATATCGACGTCCCGTCGGATTGCGAAGAGGGGCTGTGTGGTTCTTGC 
               
               
                 GAAGTAGCCGTTCTGGATGGCGAGGTTGATCACCGTGATACCGTTCTGACTAAGGCC 
               
               
                 GAGCGCGCCGCGAATCGTCAGATGATGACTTGCTGCAGTCGTGCATGCGGTGATCGT 
               
               
                 CTGGCGCTGCGCCTCTAA 
               
               
                   
               
               
                 Cyp153A-RhF1, chimeric hybrid-fusion protein (protein) 
               
               
                 SEQ ID NO: 4 
               
               
                 MPTLPRTFDDIQSRLINATSRVVPMQRQIQGLKFLMSAKRKTFGPRRPMPEFVETPIPDV 
               
               
                 NTLALEDIDVSNPFLYRQGQWRAYFKRLRDEAPVHYQKNSPFGPFWSVTRFEDILFVDK 
               
               
                 SHDLFSAEPQIILGDPPEGLSVEMFIAMDPPKHDVQRSSVQGVVAPKNLKEMEGLIRSRT 
               
               
                 GDVLDSLPTDKPFNWVPAVSKELTGRMLATLLDFPYEERHKLVEWSDRMAGAASATG 
               
               
                 GEFADENAMFDDAADMARSFSRLWRDKEARRAAGEEPGFDLISLLQSNKETKDLINRP 
               
               
                 MEFIGNLTLLIVAGNDTTRNSMSGGLVAMNEFPREFEKLKAKPELIPNMVSEIIRWQTPL 
               
               
                 AYMRRIAKQDVELGGQTIKKGDRVVMWYASGNRDERKFDNPDQFIIDRKDARNHMSF 
               
               
                 GYGVHRCMGNRLAELQLRILWEEILKRFDNIEVVEEPERVQSNFVRGYSRLMVKLTPNS 
               
               
                 VLHRHQPVTIGEPAARAVSRTVTVERLDRIADDVLRLVLRDAGGKTLPTWTPGAHIDLD 
               
               
                 LGALSRQYSLCGAPDAPSYEIAVHLDPESRGGSRYIHEQLEVGSPLRMRGPRNHFALDPG 
               
               
                 AEHYVFVAGGIGITPVLAMADHARARGWSYELHYCGRNRSGMAYLERVAGHGDRAAL 
               
               
                 HVSEEGTRIDLAALLAEPAPGVQIYACGPGRLLAGLEDASRNWPDGALHVEHFTSSLAA 
               
               
                 LDPDVEHAFDLELRDSGLTVRVEPTQTVLDALRANNIDVPSDCEEGLCGSCEVAVLDGE 
               
               
                 VDHRDTVLTKAERAANRQMMTCCSRACGDRLALRL. 
               
               
                   
               
               
                 Cyp153A-RhF2, chimeric hybrid-fusion protein (DNA) 
               
               
                 SEQ ID NO: 5 
               
               
                 ATGCCAACACTGCCCAGAACATTTGACGACATTCAGTCCCGACTGATTAACGCCACC 
               
               
                 TCCAGGGTGGTGCCGATGCAGAGGCAAATTCAGGGACTGAAATTCTTAATGAGCGC 
               
               
                 CAAGAGGAAGACCTTCGGCCCACGCCGACCGATGCCCGAATTCGTTGAAACACCCA 
               
               
                 TCCCGGACGTTAACACGCTGGCCCTTGAGGACATCGATGTCAGCAATCCGTTTTTAT 
               
               
                 ACCGGCAGGGTCAGTGGCGCGCCTATTTCAAACGGTTGCGTGATGAGGCGCCGGTC 
               
               
                 CATTACCAGAAGAACAGCCCTTTCGGCCCCTTCTGGTCGGTAACTCGGTTTGAAGAC 
               
               
                 ATCCTGTTCGTGGATAAGAGTCACGACCTGTTTTCCGCCGAGCCGCAAATCATTCTC 
               
               
                 GGTGACCCTCCGGAGGGGCTGTCGGTGGAAATGTTCATAGCGATGGATCCGCCGAA 
               
               
                 ACACGATGTGCAGCGCAGCTCGGTGCAGGGAGTAGTGGCACCGAAAAACCTGAAGG 
               
               
                 AGATGGAGGGGCTGATCCGATCACGCACCGGCGATGTGCTTGACAGCCTGCCTACA 
               
               
                 GACAAACCCTTTAACTGGGTACCTGCTGTTTCCAAGGAACTCACAGGCCGCATGCTG 
               
               
                 GCGACGCTTCTGGATTTTCCTTACGAGGAACGCCACAAGCTGGTTGAGTGGTCGGAC 
               
               
                 AGAATGGCAGGTGCAGCATCGGCCACCGGCGGGGAGTTTGCCGATGAAAATGCCAT 
               
               
                 GTTTGACGACGCGGCAGACATGGCCCGGTCTTTCTCCAGGCTTTGGCGGGACAAGGA 
               
               
                 GGCGCGCCGCGCAGCAGGCGAGGAGCCCGGTTTCGATTTGATCAGCCTGTTGCAGA 
               
               
                 GCAACAAAGAAACGAAAGACCTGATCAATCGGCCGATGGAGTTTATCGGTAATTTG 
               
               
                 ACGCTGCTCATAGTCGcCGGCAACGATACGACGCGCAACTCGATGAGTGGTGGCCTG 
               
               
                 GTGGCCATGAACGAATTCCCCAGGGAATTTGAAAAATTGAAGGCAAAACCGGAGTT 
               
               
                 GATTCCGAACATGGTGTCGGAAATCATCCGCTGGCAAACGCCGCTGGCCTATATGCG 
               
               
                 CCGAATCGCCAAGCAGGATGTCGAACTGGGCGGCCAGACCATCAAGAAGGGTGATC 
               
               
                 GAGTTGTCATGTGGTACGCGTCGGGTAACCGGGACGAGCGCAAATTTGACAACCCC 
               
               
                 GATCAGTTCATCATTGATCGCAAGGACGCACGAAACCACATGTCGTTCGGCTATGGG 
               
               
                 GTTCACCGTTGCATGGGCAACCGTCTGGCTGAACTGCAACTGCGCATCCTCTGGGAA 
               
               
                 GAAATACTCAAGCGTTTTGACAACATCGAAGTCGTCGAAGAGCCCGAGCGGGTGCA 
               
               
                 GTCCAACTTCGTGCGGGGCTATTCCAGGTTGATGGTCAAACTGACACCGAACAGTGT 
               
               
                 ACTCCATCGTCATCAACCTGTCACCATCGGCGAGCCGGCCGCTCGTGCTGTGAGCCG 
               
               
                 CACGGTGACCGTTGAGCGTCTTGATCGCATTGCCGACGATGTCCTTCGCCTGGTCCTT 
               
               
                 CGCGATGCTGGAGGTAAAACCCTCCCGACGTGGACGCCTGGCGCTCACATCGACCT 
               
               
                 GGATCTGGGtGCTCTGAGCCGTCAGTATTCGCTCTGCGGCGCTCCGGATGCTCCGTCG 
               
               
                 TACGAAATCGCCGTGCACTTAGATCCgGAAAGCCGTGGTGGAAGCCGCTATATTCAT 
               
               
                 GAACAGCTGGAAGTTGGAAGTCCGCTGCGTATGCGtGGCCCACGCAACCATTTCGCC 
               
               
                 CTGGATCCGGGtGCGGAACATTACGTGTTTGTTGCCGGGGGTATCGGCATCACGCCG 
               
               
                 GTGCTGGCAATGGCGGATCATGCCCGTGCGCGTGGTTGGTCGTACGAACTGCATTAT 
               
               
                 TGTGGTCGTAATCGTAGCGGTATGGCTTACCTGGAACGCGTCGCGGGACATGGTGAC 
               
               
                 CGCGCtGCCTTGCACGTATCTGAAGAAGGCACCCGCATTGATCTGGCGGCATTACTT 
               
               
                 GCTGAACCGGCGCCGGGCGTGCAAATCTACGCCTGCGGTCCGGGCCGTTTATTAGCG 
               
               
                 GGTCTTGAAGACGCGTCTCGTAATTGGCCGGATGGCGCGCTTCATGTGGAGCATTTC 
               
               
                 ACTTCGAGTTTAGCCGCTTTGGATCCGGATGTCGAACATGCCTTTGATTTGGAGCTG 
               
               
                 CGTGACTCTGGCCTTACCGTTCGCGTCGAGCCAACTCAGACCGTTTTAGACGCTTTG 
               
               
                 CGTGCGAACAATATCGACGTCCCGTCGGATTGCgaaGAGGGGCTGTGTGGTTCTTGCG 
               
               
                 AAGTAGCCGTTCTGGATGGCGAGGTTGATCACCGTGATACCGTTCTGACTAAGGCCG 
               
               
                 AGCGCGCCGCGAATCGTCAGATGATGACTTGCTGCAGTCGTGCATGCGGTGATCGTC 
               
               
                 TGGtcCTGCGCCTCTAA 
               
               
                   
               
               
                 Cyp153A-RhF2, chimeric hybrid-fusion protein (protein) 
               
               
                 SEQ ID NO: 6 
               
               
                 MPTLPRTFDDIQSRLINATSRVVPMQRQIQGLKFLMSAKRKTFGPRRPMPEFVETPIPDV 
               
               
                 NTLALEDIDVSNPFLYRQGQWRAYFKRLRDEAPVHYQKNSPFGPFWSVTRFEDILFVDK 
               
               
                 SHDLFSAEPQIILGDPPEGLSVEMFIAMDPPKHDVQRSSVQGVVAPKNLKEMEGLIRSRT 
               
               
                 GDVLDSLPTDKPFNWVPAVSKELTGRMLATLLDFPYEERHKLVEWSDRMAGAASATG 
               
               
                 GEFADENAMFDDAADMARSFSRLWRDKEARRAAGEEPGFDLISLLQSNKETKDLINRP 
               
               
                 MEFIGNLTLLIVAGNDTTRNSMSGGLVAMNEFPREFEKLKAKPELIPNMVSEIIRWQTPL 
               
               
                 AYMRRIAKQDVELGGQTIKKGDRVVMWYASGNRDERKFDNPDQFIIDRKDARNHMSF 
               
               
                 GYGVHRCMGNRLAELQLRILWEEILKRFDNIEVVEEPERVQSNFVRGYSRLMVKLTPNS 
               
               
                 VLHRHQPVTIGEPAARAVSRTVTVERLDRIADDVLRLVLRDAGGKTLPTWTPGAHIDLD 
               
               
                 LGALSRQYSLCGAPDAPSYEIAVHLDPESRGGSRYIHEQLEVGSPLRMRGPRNHFALDPG 
               
               
                 AEHYVFVAGGIGITPVLAMADHARARGWSYELHYCGRNRSGMAYLERVAGHGDRAAL 
               
               
                 HVSEEGTRIDLAALLAEPAPGVQIYACGPGRLLAGLEDASRNWPDGALHVEHFTSSLAA 
               
               
                 LDPDVEHAFDLELRDSGLTVRVEPTQTVLDALRANNIDVPSDCEEGLCGSCEVAVLDGE 
               
               
                 VDHRDTVLTKAERAANRQMMTCCSRACGDRLVLRL. 
               
               
                   
               
               
                 Cyp153A-BM3 chimeric hybrid-fusion protein (DNA) 
               
               
                 SEQ ID NO: 7 
               
               
                 ATGCCAACACTGCCCAGAACATTTGACGACATTCAGTCCCGACTGATTAACGCCACC 
               
               
                 TCCAGGGTGGTGCCGATGCAGAGGCAAATTCAGGGACTGAAATTCTTAATGAGCGC 
               
               
                 CAAGAGGAAGACCTTCGGCCCACGCCGACCGATGCCCGAATTCGTTGAAACACCCA 
               
               
                 TCCCGGACGTTAACACGCTGGCCCTTGAGGACATCGATGTCAGCAATCCGTTTTTAT 
               
               
                 ACCGGCAGGGTCAGTGGCGCGCCTATTTCAAACGGTTGCGTGATGAGGCGCCGGTC 
               
               
                 CATTACCAGAAGAACAGCCCTTTCGGCCCCTTCTGGTCGGTAACTCGGTTTGAAGAC 
               
               
                 ATCCTGTTCGTGGATAAGAGTCACGACCTGTTTTCCGCCGAGCCGCAAATCATTCTC 
               
               
                 GGTGACCCTCCGGAGGGGCTGTCGGTGGAAATGTTCATAGCGATGGATCCGCCGAA 
               
               
                 ACACGATGTGCAGCGCAGCTCGGTGCAGGGAGTAGTGGCACCGAAAAACCTGAAGG 
               
               
                 AGATGGAGGGGCTGATCCGATCACGCACCGGCGATGTGCTTGACAGCCTGCCTACA 
               
               
                 GACAAACCCTTTAACTGGGTACCTGCTGTTTCCAAGGAACTCACAGGCCGCATGCTG 
               
               
                 GCGACGCTTCTGGATTTTCCTTACGAGGAACGCCACAAGCTGGTTGAGTGGTCGGAC 
               
               
                 AGAATGGCAGGTGCAGCATCGGCCACCGGCGGGGAGTTTGCCGATGAAAATGCCAT 
               
               
                 GTTTGACGACGCGGCAGACATGGCCCGGTCTTTCTCCAGGCTTTGGCGGGACAAGGA 
               
               
                 GGCGCGCCGCGCAGCAGGCGAGGAGCCCGGTTTCGATTTGATCAGCCTGTTGCAGA 
               
               
                 GCAACAAAGAAACGAAAGACCTGATCAATCGGCCGATGGAGTTTATCGGTAATTTG 
               
               
                 ACGCTGCTCATAGTCGcCGGCAACGATACGACGCGCAACTCGATGAGTGGTGGCCTG 
               
               
                 GTGGCCATGAACGAATTCCCCAGGGAATTTGAAAAATTGAAGGCAAAACCGGAGTT 
               
               
                 GATTCCGAACATGGTGTCGGAAATCATCCGCTGGCAAACGCCGCTGGCCTATATGCG 
               
               
                 CCGAATCGCCAAGCAGGATGTCGAACTGGGCGGCCAGACCATCAAGAAGGGTGATC 
               
               
                 GAGTTGTCATGTGGTACGCGTCGGGTAACCGGGACGAGCGCAAATTTGACAACCCC 
               
               
                 GATCAGTTCATCATTGATCGCAAGGACGCACGAAACCACATGTCGTTCGGCTATGGG 
               
               
                 GTTCACCGTTGCATGGGCAACCGTCTGGCTGAACTGCAACTGCGCATCCTCTGGGAA 
               
               
                 GAAATACTCAAGCGTTTTGACAACATCGAAGTCGTCGAAGAGCCCGAGCGGGTGCA 
               
               
                 GTCCAACTTCGTGCGGGGCTATTCCAGGTTGATGGTCAAACTGACACCGAACAGTTC 
               
               
                 ACCTAGCACTGAACAGTCTGCTAAAAAAGTACGCAAAAAGGCAGAAAACGCTCATA 
               
               
                 ATACGCCGCTGCTTGTGCTATACGGTTCAAATATGGGAACAGCTGAAGGAACGGCG 
               
               
                 CGTGATTTAGCAGATATTGCAATGAGCAAAGGATTTGCACCGCAGGTCGCAACGCTT 
               
               
                 GATTCACACGCCGGAAATCTTCCGCGCGAAGGAGCTGTATTAATTGTAACGGCGTCT 
               
               
                 TATAACGGTCATCCGCCTGATAACGCAAAGCAATTTGTCGACTGGTTAGACCAAGCG 
               
               
                 TCTGCTGATGAAGTAAAAGGCGTTCGCTACTCCGTATTTGGATGCGGCGATAAAAAC 
               
               
                 TGGGCTACTACGTATCAAAAAGTGCCTGCTTTTATCGATGAAACGCTTGCCGCTAAA 
               
               
                 GGGGCAGAAAACATCGCTGACCGCGGTGAAGCAGATGCAAGCGACGACTTTGAAGG 
               
               
                 CACATATGAAGAATGGCGTGAACATATGTGGAGTGACGTAGCAGCCTACTTTAACCT 
               
               
                 CGACATTGAAAACAGTGAAGATAATAAATCTACTCTTTCACTTCAATTTGTCGACAG 
               
               
                 CGCCGCGGATATGCCGCTTGCGAAAATGCACGGTGCGTTTTCAACGAACGTCGTAGC 
               
               
                 AAGCAAAGAACTTCAACAGCCAGGCAGTGCACGAAGCACGCGACATCTTGAAATTG 
               
               
                 AACTTCCAAAAGAAGCTTCTTATCAAGAAGGAGATCATTTAGGTGTTATTCCTCGCA 
               
               
                 ACTATGAAGGAATAGTAAACCGTGTAACAGCAAGGTTCGGCCTAGATGCATCACAG 
               
               
                 CAAATCCGTCTGGAAGCAGAAGAAGAAAAATTAGCTCATTTGCCACTCGCTAAAAC 
               
               
                 AGTATCCGTAGAAGAGCTTCTGCAATACGTGGAGCTTCAAGATCCTGTTACGCGCAC 
               
               
                 GCAGCTTCGCGCAATGGCTGCTAAAACGGTCTGCCCGCCGCATAAAGTAGAGCTTG 
               
               
                 AAGCCTTGCTTGAAAAGCAAGCCTACAAAGAACAAGTGCTGGCAAAACGTTTAACA 
               
               
                 ATGCTTGAACTGCTTGAAAAATACCCGGCGTGTGAAATGAAATTCAGCGAATTTATC 
               
               
                 GCCCTTCTGCCAAGCATACGCCCGCGCTATTACTCGATTTCTTCATCACCTCGTGTCG 
               
               
                 ATGAAAAACAAGCAAGCATCACGGTCAGCGTTGTCTCAGGAGAAGCGTGGAGCGGA 
               
               
                 TATGGAGAATATAAAGGAATTGCGTCGAACTATCTTGCCGAGCTGCAAGAAGGAGA 
               
               
                 TACGATTACGTGCTTTATTTCCACACCGCAGTCAGAATTTACGCTGCCAAAAGACCC 
               
               
                 TGAAACGCCGCTTATCATGGTCGGACCGGGAACAGGCGTCGCGCCGTTTAGAGGCTT 
               
               
                 TGTGCAGGCGCGCAAACAGCTAAAAGAACAAGGACAGTCACTTGGAGAAGCACATT 
               
               
                 TATACTTCGGCTGCCGTTCACCTCATGAAGACTATCTGTATCAAGAAGAGCTTGAAA 
               
               
                 ACGCCCAAAGCGAAGGCATCATTACGCTTCATACCGCTTTTTCTCGCATGCCAAATC 
               
               
                 AGCCGAAAACATACGTTCAGCACGTAATGGAACAAGACGGCAAGAAATTGATTGAA 
               
               
                 CTTCTTGATCAAGGAGCGCACTTCTATATTTGCGGAGACGGAAGCCAAATGGCACCT 
               
               
                 GCCGTTGAAGCAACGCTTATGAAAAGCTATGCTGACGTTCACCAAGTGAGTGAAGC 
               
               
                 AGACGCTCGCTTATGGCTGCAGCAGCTAGAAGAAAAAGGCCGATACGCAAAAGACG 
               
               
                 TGTGGGCTGGGTAA 
               
               
                   
               
               
                 Cyp153A-BM3 chimeric hybrid-fusion protein (protein) 
               
               
                 SEQ ID NO: 8 
               
               
                 MPTLPRTFDDIQSRLINATSRVVPMQRQIQGLKFLMSAKRKTFGPRRPMPEFVETPIPDV 
               
               
                 NTLALEDIDVSNPFLYRQGQWRAYFKRLRDEAPVHYQKNSPEGPFWSVTRFEDILFVDK 
               
               
                 SHDLFSAEPQIILGDPPEGLSVEMFIAMDPPKHDVQRSSVQGVVAPKNLKEMEGLIRSRT 
               
               
                 GDVLDSLPTDKPFNWVPAVSKELTGRMLATLLDFPYEERHKLVEWSDRMAGAASATG 
               
               
                 GEFADENAMFDDAADMARSFSRLWRDKEARRAAGEEPGFDLISLLQSNKETKDLINRP 
               
               
                 MEFIGNLTLLIVAGNDTTRNSMSGGLVAMNEFPREFEKLKAKPELIPNMVSEIIRWQTPL 
               
               
                 AYMRRIAKQDVELGGQTIKKGDRVVMWYASGNRDERKFDNPDQFIIDRKDARNHMSF 
               
               
                 GYGVHRCMGNRLAELQLRILWEEILKRFDNIEVVEEPERVQSNFVRGYSRLMVKLTPNS 
               
               
                 SPSTEQSAKKVRKKAENAHNTPLLVLYGSNMGTAEGTARDLADIAMSKGFAPQVATLD 
               
               
                 SHAGNLPREGAVLIVTASYNGHPPDNAKQFVDWLDQASADEVKGVRYSVFGCGDKNW 
               
               
                 ATTYQKVPAFIDETLAAKGAENIADRGEADASDDFEGTYEEWREHMWSDVAAYFNLDI 
               
               
                 ENSEDNKSTLSLQFVDSAADMPLAKMHGAFSTNVVASKELQQPGSARSTRHLEIELPKE 
               
               
                 ASYQEGDHLGVIPRNYEGIVNRVTARFGLDASQQIRLEAEEEKLAHLPLAKTVSVEELLQ 
               
               
                 YVELQDPVTRTQLRAMAAKTVCPPHKVELEALLEKQAYKEQVLAKRLTMLELLEKYPA 
               
               
                 CEMKFSEFIALLPSIRPRYYSISSSPRVDEKQASITVSVVSGEAWSGYGEYKGIASNYLAE 
               
               
                 LQEGDTITCFISTPQSEETLPKDPETPLEVIVGPGTGVAPERGEVQARKQLKEQGQSLGEAH 
               
               
                 LYFGCRSPHEDYLYQEELENAQSEGIITLHTAFSRMPNQPKTYVQHVMEQDGKKLIELL 
               
               
                 DQGAHFYICGDGSQMAPAVEATLMKSYADVHQVSEADARLWLQQLEEKGRYAKDVW 
               
               
                 AG. 
               
               
                   
               
               
                 CYP153_mgp_HTCC2143 from marine gamma proteobacterium 
               
               
                 HTCC2143 (DNA) SEQ ID NO: 9 
               
               
                 ATGGGAAGCTTGGAGCGTATCTCCATGTTGGATTACGATCCTGCAACGATGCCATTA 
               
               
                 GAGGATATTGATGTATCTGACGTAGACTTATGGATCAACGACGCCAAGTGGGATTAT 
               
               
                 TTGACGCGCTTGCGTAATGACGCTCCCGTCCATTACTGTAAGAGTTCCGAATTCGGC 
               
               
                 CCTTACTGGTCCATCACGCGCTTCGATGACATCATGAAAGTAGAGAAGAATTGGGA 
               
               
                 GGTTTTCTCCTCTTTCCCTAGTATCACAATTAGTGATCCTGCTGAAGATTCGGACTTC 
               
               
                 ACTGCGCCAACCTTCATTGCCATGGACCCACCAAAGCACGACGACCAGCGTCGCGC 
               
               
                 TGTGCAAAACGTAGTGGCACCTCCAAACCTTAAAGAGTTAGAATCGACTATTCGTTC 
               
               
                 ACGCGCAGTCAACATCCTGGATTCACTTCCTATCGGAGAGACTTTTAATTGGGTTGA 
               
               
                 TCGCGTTTCAATTGAACTGACTACACAGATGTTAGCTACCTTGTTTGATTTTCCTTTT 
               
               
                 GAGGACCGTTATAAGCTGACGCATTGGAGCGATGTCACGTTTGCTCGCCTGGGAGCG 
               
               
                 GGTCTGATCGAAACAGAGGAGGAGCGTCAGCAAGAACTGATTGAGTGTTTGAACTA 
               
               
                 TTTCTTACAACTTTGGAAGGAACGTGAAGAGAACCCGGTGGGAAACGACCTTATCA 
               
               
                 GTATGATGATTCGTGGAGATGCGACTAAAAACTTAAGTCCTCAAGAGTACCTTGGGA 
               
               
                 ACATCTTACTTCTTATTGTAGGAGGGAATGACACAACCCGTAATAGCATTACAGGAG 
               
               
                 GACTGTTGGCTCTGAACGAAAATCCCGCTGAATATGAGAAACTGCGTTCCCATCCTG 
               
               
                 AACACATCCCGAACATGGTATCGGAAATCATCCGCTGGGTAACGCCTTTGGCTCACA 
               
               
                 TGCGTCGTACAGCTACTCGTGATTATGAGTTCGAAGGGCAACAGATTAAGAAGGGG 
               
               
                 GATAAAATTATCATGTGGTATGCAAGTGGCAACCGTGATGAGCGCACAATCCCCAA 
               
               
                 TCCCAACAAGTTTTTGATCGATCGCGAGCGCGCCCGTAACCACATCAGTTTCGGCTT 
               
               
                 CGGTTTGCACCGCTGCATGGGGAATCGTTTAGCTGAAATGCAACTGCGTGTCTTGTG 
               
               
                 GGAGGAAATCCAAAAACGCTTTAAGACAATTGAGGTTGTCGGAGCACCAGAACGCA 
               
               
                 TTCCTTCGTGTTTTGTCCACGGGATTTCTTCCCTGCCAGTGCGTTTACACTCTTATTAC 
               
               
                 TAA 
               
               
                   
               
               
                 CYP153_mgp_HTCC2143 from marine gamma proteobacterium 
               
               
                 HTCC2143 (protein) SEQ ID NO: 10 
               
               
                 MGSLERISMLDYDPATMPLEDIDVSDVDLWINDAKWDYLTRLRNDAPVHYCKSSEFGP 
               
               
                 YWSITRFDDIMKVEKNWEVFSSFPSITISDPAEDSDFTAPTFIAMDPPKHDDQRRAVQNV 
               
               
                 VAPPNLKELESTIRSRAVNILDSLPIGETFNWVDRVSIELTTQMLATLFDFPFEDRYKLTH 
               
               
                 WSDVTFARLGAGLIETEEERQQELIECLNYFLQLWKEREENPVGNDLISMMIRGDATKN 
               
               
                 LSPQEYLGNILLLIVGGNDTTRNSITGGLLALNENPAEYEKLRSHPEHIPNMVSEIIRWVT 
               
               
                 PLAHMRRTATRDYEFEGQQIKKGDKIIMWYASGNRDERTIPNPNKFLIDRERARNHISFG 
               
               
                 FGLHRCMGNRLAEMQLRVLWEEIQKRFKTIEVVGAPERIPSCFVHGISSLPVRLHSYY. 
               
               
                   
               
               
                 CYP153_mgp_HTCC2080 from marine gamma proteobacterium 
               
               
                 HTCC2080 (DNA) SEQ ID NO: 11 
               
               
                 ATGAACCAGGCAGTAACGCGTAAAGATGGTTTGCCAGACCCCCTGTCCACTCCTCTG 
               
               
                 GACCAATTGGACATTGCTGACCCACGTCGTTTCGAATTCGACACCTGGCAGCCATTG 
               
               
                 TTTGAGCGTCTGCGCTCCGAGGCTCCGGTCCACTACCAAGCACAGGGACCTGCAGGT 
               
               
                 CCCGCTCCCCACGGCGACTTCTGGTCTGTAACTCGTTTCGAAGATATTGTCGAGGTT 
               
               
                 GAAAAAAATTGGGAGGCGTTTAGTTCCGAGCCAAGCATCGCCATCCTTGACCCGGA 
               
               
                 ACCAGACATGTCCGTACAGATGTTCATCGCAACAGATCCACCCCTTCATGATGACCA 
               
               
                 ACGCCGTGCGGTACAAGGTGCGGTCGCACCAAAAAATTTACAGGAATTTGAGGCCC 
               
               
                 TGATTCGTCAGCGCACGCAGGAAACTCTGGATGGGCTGCCACTTGGGGAGACTTTCA 
               
               
                 ATTGGGTCGACCGTGTAAGCATCGATTTGACTACCAAAATGCTTGCGACATTATTTG 
               
               
                 ATTTCCCCCAGGAGCAGCGCCAATTATTGACTCACTGGTCCGACGCCGCGACTTCAG 
               
               
                 ATGCGCGCATCACCGCAGGGCGCGGGCTGTCGATTGATGAACGTCGTACCATCATG 
               
               
                 GGGGAGATGCTGCAAAGCTTTACCCAGCTGTGGCACGACCACAAAGCGAATGACCG 
               
               
                 TGAGTCCTTCGATTTAATCCGTATGTTACAGCGTGATCCAAAGACCCAAAATATGGT 
               
               
                 AGACGAGCCATTTTCTTACCTGGGTAACCTTATGTTACTTATCGTTGGGGGGAACGA 
               
               
                 CACAACTCGTAATTCCATGACGGGAGGTGTATTGCATTTGCATCAAAACCCCAGCGA 
               
               
                 AATGGCGAAACTGAAGGCCAATCACGGGTTGATTCCCTCGATGGTTTCGGAAATCAT 
               
               
                 CCGTTATCAGACGCCATTGCCACACATGCGCCGTACAGCCACACGCGATGTCGAATT 
               
               
                 AAACGGAACCGTTATCCCGAAAGGCGGTCGTGTGGTATTGTGGTATGTTAGCGGAA 
               
               
                 ATCGTGACTCTAATGCAATTCCCGAGGCAGACAAGTTCATCATCGATCGCCCGAATG 
               
               
                 TACGTAACCATTTGTCATTCGGGATGGGTATTCATCGCTGCATGGGGAATCGTTTGG 
               
               
                 CTGAAATGCAATTACGCATTGTTTGGGAAGAAATCCTTGAGCGTTTTGAGCGCATTG 
               
               
                 AAGTTGTAGGACCAGCAGTTCGCACTTGTAATTCCTTTGTTCGTGGCTATCACGAAC 
               
               
                 TTCCGGTTCGTCTTCACCCTAAGGTTTACTAA 
               
               
                   
               
               
                 CYP153_mgp_HTCC2080 from marine gamma proteobacterium 
               
               
                 HTCC2080 (protein) SEQ ID NO: 12 
               
               
                 MNQAVTRKDGLPDPLSTPLDQLDIADPRRFEFDTWQPLFERLRSEAPVHYQAQGPAGPA 
               
               
                 PHGDFWSVTRFEDIVEVEKNWEAFSSEPSIAILDPEPDMSVQMFIATDPPLHDDQRRAVQ 
               
               
                 GAVAPKNLQEFEALIRQRTQETLDGLPLGETFNWVDRVSIDLTTKMLATLFDFPQEQRQ 
               
               
                 LLTHWSDAATSDARITAGRGLSIDERRTIMGEMLQSFTQLWHDHKANDRESFDLIRMLQ 
               
               
                 RDPKTQNMVDEPFSYLGNLMLLIVGGNDTTRNSMTGGVLHLHQNPSEMAKLKANHGLI 
               
               
                 PSMVSEIIRYQTPLPHMRRTATRDVELNGTVIPKGGRVVLWYVSGNRDSNAIPEADKFII 
               
               
                 DRPNVRNHLSFGMGIHRCMGNRLAEMQLRIVWEEILERFERIEVVGPAVRTCNSFVRGY 
               
               
                 HELPVRLHPKVY. 
               
               
                   
               
               
                 CYP153_Clit from  Congregibacter litoralis  (DNA)  
               
               
                 SEQ ID NO: 13 
               
               
                 ATGAACGTCGCTCAAGATCTGCCTCATCCATCGGATTTAGCTTTGGAAGACATCGAC 
               
               
                 GTAAGCGATTCGCGCATCTACCAACAGGATGCATGGCGCCCCTACTTTGAACGTCTG 
               
               
                 CGCAAGGAGGACCCTGTTCACTACGTAGCAGACTCACAGTTCGGGCCTTTCTGGTCC 
               
               
                 ATCACCCGCTGGGAGGATATTGTAGCGGTGGATTCCAACTTCGAGGATTTTTCTAGT 
               
               
                 GAACCGGCCATCGTCATTGGAGACAACAGCGAAGAGCTGCCCATTGCCAATTTCATT 
               
               
                 AGCATGGACCCTCCCAAGCATGACGTTCAACGCCGCGCCGTCCAGGGCGTAGTGGC 
               
               
                 CCCAAAAAACTTGGCGGAGATGGAGGCGCTGATCCGCTCCCGCGTGGTAGAAATTT 
               
               
                 TGGATGGCTTACCTGTGGGAGAGACATTCAACTGGGTCGACCGCGTCTCGATCAATC 
               
               
                 TTACAACGCAAATGCTGGCTACACTTTTCGACTTTCCATTCGAAGAACGTTTTAAACT 
               
               
                 GACCTACTGGAGCGATTTGGGCGCCGGCAGCCCTGAAATTGCGGGTGGCGATGTCG 
               
               
                 ATCCTGAGGAACGTTTAGCTGGTTTACATGACTGCTTAGAAACATTCACTCGCATCT 
               
               
                 GGCACGAACGCAAAGACGACGGTGTCGAGACTTTGGACCTTATTCGCATGTTGCAA 
               
               
                 CGTGACCCGAATACGAAGGACATGGTCGATGATCCAATGGAATATCTTGGAAATCT 
               
               
                 GCTGCTTCTGATCATTGGTGGAAATGACACGACCCGTAATAGCGCTAGCGCTGGCGT 
               
               
                 TCTGGCGTTGAATCAAAACCCTGCCGAATATGAAAAATTGCGTGCTAACCCCGCACT 
               
               
                 TATCCCGAGTATGGTATCAGAGGTGATTCGTTGGCAGACGCCCTTAATGCACATGCG 
               
               
                 TCGCACTGCTAACAAGGATGTTGAATTTCAGGGCAAGCAGATTCGCAAAGGTGACA 
               
               
                 AGGTCGTTATGTGGTATCTTAGTGGCAACCATGATGAAACAGCTATCGAAAACCCCA 
               
               
                 ATTCCTTCATCATTGATCGTGAAAATCCTCGTAAACATATGTCTTTTGGGTTCGGGGT 
               
               
                 TCACCGCTGCATGGGTAACCGCCTTGCCGAGATGCAACTTCGTGTTCTTTGGGAGGA 
               
               
                 AATTATGCAACGTTTTTCAAAGGTAGAAGTCGTAGGGGAACCAGAGCGTGTTAAGT 
               
               
                 CCAACTTTGTGCGTGGGATTAGCAATTTGCCAGTCCGTGTGCACCCTCTTTACTAA 
               
               
                   
               
               
                 CYP153_Clit from  Congregibacter litoralis  (protein) 
               
               
                 SEQ ID NO: 14 
               
               
                 MNVAQDLPHPSDLALEDIDVSDSRIYQQDAWRPYFERLRKEDPVHYVADSQFGPFWSIT 
               
               
                 RWEDIVAVDSNFEDFSSEPAIVIGDNSEELPIANFISMDPPKHDVQRRAVQGVVAPKNLA 
               
               
                 EMEALIRSRVVEILDGLPVGETFNWVDRVSINLTTQMLATLFDFPFEERFKLTYWSDLGA 
               
               
                 GSPEIAGGDVDPEERLAGLHDCLETFTRIWHERKDDGVETLDLIRMLQRDPNTKDMVD 
               
               
                 DPMEYLGNLLLLIIGGNDTTRNSASAGVLALNQNPAEYEKLRANPALIPSMVSEVIRWQ 
               
               
                 TPLMHMRRTANKDVEFQGKQIRKGDKVVMWYLSGNHDETAIENPNSFIIDRENPRKHM 
               
               
                 SFGFGVHRCMGNRLAEMQLRVLWEEIMQRFSKVEVVGEPERVKSNFVRGISNLPVRVH 
               
               
                 PLY. 
               
               
                   
               
               
                 CYP153_Lim from  Limnobacter  sp. MED105 (DNA) SEQ ID NO: 15 
               
               
                 ATGTCAACGCAATCAAAGACATTCGACCAGATTCAAACACGCGTAATCAATGCGAC 
               
               
                 AGCAAAGGTTATTCCAATGCACTTGCAGATTCAAGGTTTAAAATTCCTTATGCGCGC 
               
               
                 GAAGAAAAAAACCATTGGGGCCCGCCGCCCAACTCCCTCCTTTGTGGAGTACCCACT 
               
               
                 GCCAGATGTCGGGACTTTACGCATTGACGATATTGATGTCTCAAACCCTTTCTTATAC 
               
               
                 CGCCAGGGTCAATGGCGCGCATATTTCAAGCGCCTTCGTGATGAAGCACCCGTTCAT 
               
               
                 TTCCAAAAGAATTCACCCTTCGGTCCGTTCTGGAGCGTTACCCGTTATGAGGATATC 
               
               
                 CTTTTCGTAGACAAACATCACGATTTATTTTCGGCAGAGCCCGTTATCATCTTAGGA 
               
               
                 GACCCACCGGAGGGTCTTTCGGTAGAGATGTTTATCGCAATGGATCCTCCTAAGCAC 
               
               
                 GATGCTCAACGTAGTTCAGTACAAGGGGTGGTGGCCCCCCAAAACTTAAAGGAGAT 
               
               
                 GGAGAGCCTGATTCGTTCACGCACGGGAGATGTGTTAGATTCCCTTCCCGTCGGCCA 
               
               
                 GCCTTTTGACTGGGTTCCCACAGTTTCGAAGGAGCTGACTGGACGCATGCTTGCGAC 
               
               
                 TCTGTTAGATTTTCCGTACGACGAGCGTGACAAGCTGATTTATTGGTCGGATCTTCTG 
               
               
                 GCTGGTGCGGCGTCCGCCACCGGGGGAGAGTTTACTGATGAGGAAGCGATGTTTGA 
               
               
                 TGCAGCGGCAGATATGGCACGCGACTTTAGCCGTTTATGGCGCGACAAACAGGCGC 
               
               
                 GCCGCGCAGCTGGGGAAGCTCCCGGCTTCGATTTAATTAGCCTGCTTCAGAGCAGCG 
               
               
                 AAGATACGCGTGACCTGATCAATCGCCCGATGGAGTTTATCGGCAACTTGGCATTGT 
               
               
                 TAATTGTTGGGGGAAACGATACAACACGTAACTCCATGAGTGGTGGCCTTCTGGCAA 
               
               
                 TGAATCAATTTCCTAAGGAGTTTAAAAAGCTGAAGGCAAACCCAGCATTGATCCCTA 
               
               
                 ATATGGTGTCGGAAATTATTCGCTGGCAGACACCTCTGGCCTACATGCGTCGTATTG 
               
               
                 CTAAACAAGATGTTGAACTTGGCGGACGCACTATCAAGAAAGGAGATCGCGTAGTC 
               
               
                 ATGTGGTATGCCTCCGGTAACCGCGACGAACGTAAGTTCACCGACCCCGATCAATTT 
               
               
                 TTGATTGATCGCAGTGGGGCCCGCAACCACTTGTCCTTCGGATATGGAGTACACCGT 
               
               
                 TGTATGGGTAATCGTCTTGCGGAGCTTCAACTGCGTATTTTGTGGGAAGAATTGTTA 
               
               
                 AAGCGTTTCGAAAATATTGAAGTTGTGGGCGAGCCTGAGCGTGTTCAATCAAACTTT 
               
               
                 GTTCGCGGATATTCAGAGATGATGGTGAAATTAACTCCACTGCGTTACTAA 
               
               
                   
               
               
                 CYP153_Lim from  Limnobacter  sp. MED105 (protein) 
               
               
                 SEQ ID NO: 16 
               
               
                 MSTQSKTFDQIQTRVINATAKVIPMHLQIQGLKFLMRAKKKTIGARRPTPSFVEYPLPDV 
               
               
                 GTLRIDDIDVSNPFLYRQGQWRAYFKRLRDEAPVHFQKNSPFGPFWSVTRYEDILFVDK 
               
               
                 HHDLFSAEPVIILGDPPEGLSVEMFIAMDPPKHDAQRSSVQGVVAPQNLKEMESLIRSRT 
               
               
                 GDVLDSLPVGQPFDWVPTVSKELTGRMLATLLDFPYDERDKLIYWSDLLAGAASATGG 
               
               
                 EFTDEEAMFDAAADMARDFSRLWRDKQARRAAGEAPGFDLISLLQSSEDTRDLINRPM 
               
               
                 EFIGNLALLIVGGNDTTRNSMSGGLLAMNQFPKEFKKLKANPALIPNMVSEIIRWQTPLA 
               
               
                 YMRRIAKQDVELGGRTIKKGDRVVMWYASGNRDERKFTDPDQFLIDRSGARNHLSFGY 
               
               
                 GVHRCMGNRLAELQLRILWEELLKRFENIEVVGEPERVQSNFVRGYSEMMVKLTPLRY 
               
               
                   
               
               
                 CYP153_Caul from  Caulobacter  sp. K31 (DNA) SEQ ID NO: 17 
               
               
                 ATGAGCGATGGTGCAATTGATTTACGCGCGGAGGCGCGCGCCAAGGCGTATGCGAT 
               
               
                 GCCCTTAGAGGATATCAACCTTGCAGATACCGAATTGTGGCGCACAGATACGGTGTG 
               
               
                 GCCGTATCTGGAGCGCTTGCGTAAGGAAGACCCCGTTCATTTACACCCTGCTCATCA 
               
               
                 CCATCCCGACGGAGCGTTTTGGAGTATTACTAAATATGCAGATATCATGGCCGTCGA 
               
               
                 CATTAATCATGAGGTATTTTCAAGTGAACCGTCGATCACCATCTTTGACCCCAAAGA 
               
               
                 GGATTTTACCCTTCCTATGTTCATTGCGATGGACCCGCCAAAGCATGATGTGCAACG 
               
               
                 CAAGACTGTCAGTCCGATTGTGAGTCCGGCAAACTTACACTTGATGGAACCTCTTAT 
               
               
                 CCGCAGTCGCATCACCAAAACGCTTGACGAACTTCCTATTGGGGAGCCATTTGATTG 
               
               
                 GGTGGATCGCGTCTCTATCGAGCTTACAACTCAGATGTTGGCGACCCTTTTCGACTTC 
               
               
                 CCATGGGACGAGCGCCGCAAACTGACACGCTGGTCCGATATTGCAACAGCAGTACC 
               
               
                 CGAAAGCGGCTTATTTGTTACGGACGATTATGAAACCGAGCGCCGCATGGAATTATT 
               
               
                 CGGGTGCGTCGATTATTTCACTCGTCTTTGGAACGAACGTGTGAATGCCCCACCTAA 
               
               
                 GGGTGATCTGATCTCTATGTTAGCCCATGGGGAGGCCACCCGTAATATGGACCGTAT 
               
               
                 GGAGTACCTTGGGAACTTATTACTTCTTATTATTGGAGGGAACGACACAACTCGTAA 
               
               
                 CACTATGACAGGCTCGATCCTGGCGATGAATCAAAACCCCGACCAATTACGCAAAT 
               
               
                 TACGTGAAAACCCGAGTCTGATTCCGTCCATGGTCAGTGAAACCATTCGCTGGCAGA 
               
               
                 CTCCACTGTCAAACATGCGCCGCACAGCCACCCAAGACTTTGAGTTAGGTGGGAAA 
               
               
                 TTGATTAAGAAAGGTGATAAAGTGCTGATCTGGTATGCCTCCGGTAATCGTGATGAA 
               
               
                 GAAGCTATCGAAAACCCAGAAGCGTACATTATTGACCGTGAGCGTCCTCGTAATCAT 
               
               
                 CTTTCGTTTGGTTTCGGTATCCACCGTTGCGTCGGGAATCGCCTGGCAGAATTGCAAT 
               
               
                 TGCGTATTCTGTGGGAAGAAATTTTACCCCGTTTTCCAGAGATTCAGGTACTGGAGG 
               
               
                 ATCCGCAGCGTGTTCCGTCAGTTCTGATTCGTGGGTACTCCTCCATGCCCGTCATGAT 
               
               
                 CCCTGCACGCTCATACTAA 
               
               
                   
               
               
                 CYP153_Caul from  Caulobacter  sp. K31 (protein) 
               
               
                 SEQ ID NO: 18 
               
               
                 MSDGAIDLRAEARAKAYAMPLEDINLADTELWRTDTVWPYLERLRKEDPVHLHPAHH 
               
               
                 HPDGAFWSITKYADIMAVDINHEVFSSEPSITIFDPKEDFTLPMFIAMDPPKHDVQRKTVS 
               
               
                 PIVSPANLHLMEPLIRSRITKTLDELPIGEPFDWVDRVSIELTTQMLATLFDFPWDERRKL 
               
               
                 TRWSDIATAVPESGLFVTDDYETERRMELFGCVDYFTRLWNERVNAPPKGDLISMLAH 
               
               
                 GEATRNMDRMEYLGNLLLLIIGGNDTTRNTMTGSILAMNQNPDQLRKLRENPSLIPSMV 
               
               
                 SETIRWQTPLSNMIRRTATQDFELGGKLIKKGDKVLIWYASGNRDEEAIENPEAYIIDRER 
               
               
                 PRNHLSFGFGIHRCVGNRLAELQLRILWEEILPRFPEIQVLEDPQRVPSVLIRGYSSMPVMI 
               
               
                 PARSY 
               
               
                   
               
               
                 CYP153_Mmar from  Mycobacterium marinum  str. M (DNA) 
               
               
                 SEQ ID NO: 19 
               
               
                 ATGTCGAACATTCGTGAAGCAGTAACGGCAAAGGCGCAAGCCACTATTCCAATGGA 
               
               
                 TCGTATTATCCAGGGAGCGCACTTGTATGATCGTACACGCCGCTGGGTAACCGGCAC 
               
               
                 GAATGGTGAGAAAATTTTCATTGAACGCCCGATCCCGCCTGCCGACGAAGTCGAGCT 
               
               
                 TACAGACATCGACTTAAGTAATCCCTTCCTTTACCGCCAGGGCCGCTGGAAGTCTTA 
               
               
                 TTACGAGCGCCTTCGTAACGAAGCGCCTGTCCACTACCAAGCGCATTCGGCCTTCGG 
               
               
                 GCCTTTCTGGTCTGTTACTCGTCACGCAGATATTGTGGCAGTCGATAAGAACCATGA 
               
               
                 AGTTTTTAGCAGTGAACCGTTTATCGTGATTGGGTCCCCACCACGCTTTTTGGATATC 
               
               
                 GCGATGTTCATCGCTATGGATCCACCCAAACATGATCGCCAACGCCAGGCAGTTCAG 
               
               
                 GGCGTCGTGGCACCAAAGAATTTACGTGAAATGGAAGGATTAATTCGCGAGCGCGT 
               
               
                 CGTGGACGTGTTGGATGCCCTGCCCCTTGGCGAACCTTTCAATTGGGTGCAGCACGT 
               
               
                 CTCAATTGAATTGACTGCGCGCATGTTAGCTACATTATTGGACTTTCCTTTTGAACAG 
               
               
                 CGTCGCAAGTTGGTCCAGTGGTCCGACTTGGCGACGAGCATGGAACAAGCAAATGG 
               
               
                 CGGTCCTAGCGATAATGACGAAATCTTCCGCGGTATGGTGGACATGGCGCGTGGGTT 
               
               
                 ATCTGCCCATTGGCGCGACAAAGCAGCACGTACTGCGGCAGGAGAACTTCCAGGAT 
               
               
                 TCGACCTTATCACTATGTTACAGAGCGACGAATCCACGAAGGACCTGATTGACCGCC 
               
               
                 CGATGGAGTTTTTAGGTAATCTTGTTCTTCTTATCGTGGGAGGTAATGATACTACCCG 
               
               
                 TAATTCTATGAGTGGTGGCGTATTGGCTCTGAACGAGTTCCCAGATCAGTTTGAGAA 
               
               
                 ACTGAAGGCTAACCCAGAACTGATTCCTAATATGGTATCTGAGATTATTCGCTGGCA 
               
               
                 AACACCGTTGGCTCACATGCGTCGCATTGCCAAAGCCGATACGGTGCTGAATGGGC 
               
               
                 AATTTATTCGCAAGGGAGACAAAGTTTTGATGTGGTATGCTTCAGGTAATCGCGATG 
               
               
                 AGCGTGTATTTGACCGCCCCGATGACTTGATTATCGACCGCGCAAATGCCCGTAACC 
               
               
                 ATATTTCGTTCGGGTTCGGAGTTCATCGCTGTATGGGAAATCGTCTTGCTGAGATGC 
               
               
                 AGTTACGCATCTTATGGGAGGAACTTTTACCACGCTTTGAGAACATTGAAGTAGTGG 
               
               
                 GGGAACCTGAGTACGTCCAATCTAATTTCGTGCGTGGGATCAGCAAACTGATGGTCC 
               
               
                 GTTTGACCCCCAAGGGCGGTGCCTACTAA 
               
               
                   
               
               
                 CYP153_Mmar from  Mycobacterium marinum  str. M (protein) 
               
               
                 SEQ ID NO: 20 
               
               
                 MSNIREAVTAKAQATIPMDRIIQGAHLYDRTRRWVTGTNGEKIFIERPIPPADEVELTDID 
               
               
                 LSNPFLYRQGRWKSYYERLRNEAPVHYQAHSAFGPFWSVTRHADIVAVDKNHEVFSSE 
               
               
                 PFIVIGSPPRFLDIAMFIAMDPPKHDRQRQAVQGVVAPKNLREMEGLIRERVVDVLDALP 
               
               
                 LGEPFNWVQHVSIELTARMLATLLDFPFEQRRKLVQWSDLATSMEQANGGPSDNDEIFR 
               
               
                 GMVDMARGLSAHWRDKAARTAAGELPGFDLITMLQSDESTKDLIDRPMEFLGNLVLLI 
               
               
                 VGGNDTTRNSMSGGVLALNEFPDQFEKLKANPELIPNMVSEIIRWQTPLAHMRRIAKAD 
               
               
                 TVLNGQFIRKGDKVLMWYASGNRDERVFDRPDDLIIDRANARNHISFGFGVHRCMGNR 
               
               
                 LAEMQLRILWEELLPRFENIEVVGEPEYVQSNFVRGISKLMVRLTPKGGAY. 
               
               
                   
               
               
                 CYP153_mgp_HTCC2148 from marine gamma proteobacterium 
               
               
                 HTCC2148 (DNA) SEQ ID NO: 21 
               
               
                 ATGCCGGAAGTTGCATTGGACAACTCCCAGGATAAACTTCAGCAGGATCGTATCGA 
               
               
                 GAACTACGACGCGACGGTCGTAGACAAGGACCCTTATGACGTTGACATCGCGGACT 
               
               
                 TCAACATGATTAACCCCCACCTTTTCTCTTCTAACACCCTTTGGCCCTGGTTCAAACG 
               
               
                 CCTGCGTGAGGAGGAGCCAGTCCATTATTGTCGCGACTCCGTATTTGGTCCGTATTG 
               
               
                 GAGCGTTACGAGTTATGATGCTATCATGAAAGTAGACACGTCACATGACATCTTTAG 
               
               
                 CTCGGAGCCGAACATTACCGTAGGCGATTTACAAGAGGACTTTCCTTTAGCAACTTT 
               
               
                 TATCGCCATGGATCGTCCGAAGCACGACGAACAACGCGCCGTAGTAAATCCTGCTG 
               
               
                 TGCGCGGACAGCAGTTGCGCGACTTTGAGCCCCTTATTCGCGAGCGCACTCAACGCG 
               
               
                 TACTGGATTCTTTACCGGTGGGCGAAGAATTCAATTGGGTGGAAAAGGTCTCTATTG 
               
               
                 AATTAACTACCTGTATGCTGGCTACCTTGTTTGACTTTCCGTTCGAGGACCGTGCCAA 
               
               
                 ATTAACCCGTTGGTCTGATGTGACGTTCGCAATCCCTGGACTGGGTGTAGTGGATAG 
               
               
                 TGAAGAACAGCGTCGTGAGGAACTTTTGGAGTGCCTTGCGGCCTTCACCGAACTTTG 
               
               
                 GAACCAACGTGTCAACGAAGAACCGCGCGGGGACTTCATTAGTCTGCTGGCTCATG 
               
               
                 GCAGCGCAACGCAGGAAATGGATCCCTTTGAATATCTGGGCAACATCCTTCTTTTGA 
               
               
                 TCATTGGTGGTAATGACACAACACGTAATTCGATGAGCGGAAGCGTGTTGTGTCAAA 
               
               
                 ACCTGTACCCAGAGCAATTTGATAAGTTAAAGGCACAACCGGAGCTGATTCCATCTA 
               
               
                 TGGTTAGTGAGACGATTCGTTGGCAAACTCCCCTGGCCTATATGCGTCGCACCGCAA 
               
               
                 ATCAAGACACAATCTTAGGGGATAAGCAAATCAAGAAAGGTGATAAGGTTTTGATG 
               
               
                 TGGTATGTGAGCGGCAATCGCGATGAATCTCACTTTGAAAATCCTGACGACTATATC 
               
               
                 ATCGATCGCCCTAACGTCCGCAGCCACCTTTCATTTGGTTTTGGGATCCATCGTTGTA 
               
               
                 TGGGCAATGCGGTCGGTGAGATGCAGTTGCGTGTCCTGTGGGAGGAGATCCTGCAA 
               
               
                 CGTTTCGACCGTATTGAGGTAGTTGGTGATGTTGAACGCGTGCCTTCCTCATTCGTAA 
               
               
                 AGGGGTATAGCAGCTTACCTGTGATTCTGCACCCTAAAAAGTACTAA 
               
               
                   
               
               
                 CYP153_mgp_HTCC2148 from marine gamma proteobacterium 
               
               
                 HTCC2148 (protein) SEQ ID NO: 22 
               
               
                 MPEVALDNSQDKLQQDRIENYDATVVDKDPYDVDIADFNMINPHLFSSNTLWPWFKRL 
               
               
                 REEEPVHYCRDSVFGPYWSVTSYDAIMKVDTSHDIFSSEPNITVGDLQEDFPLATFIAMD 
               
               
                 RPKHDEQRAVVNPAVRGQQLRDFEPLIRERTQRVLDSLPVGEEFNWVEKVSIELTTCML 
               
               
                 ATLFDFPFEDRAKLTRWSDVTFAIPGLGVVDSEEQRREELLECLAAFTELWNQRVNEEP 
               
               
                 RGDFISLLAHGSATQEMDPFEYLGNILLLIIGGNDTTRNSMSGSVLCQNLYPEQFDKLKA 
               
               
                 QPELIPSMVSETIRWQTPLAYMRRTANQDTILGDKQIKKGDKVLMWYVSGNRDESHFE 
               
               
                 NPDDYIIDRPNVRSHLSFGFGIHRCMGNAVGEMQLRVLWEEILQRFDRIEVVGDVERVP 
               
               
                 SSFVKGYSSLPVILHPKKY. 
               
               
                   
               
               
                 CYP153_Pmed from  Patulibacter medicamentivorans  (DNA) 
               
               
                 SEQ ID NO :23 
               
               
                 ATGTTTGAACAAACAACCACGAAGCGCGAGACCATGACAACGAACAGCACGTTATT 
               
               
                 CCAGCGTACAAAGGTCCGCGTGACTGACACGGTTCAAGCTACTGTCCCGGTAGACC 
               
               
                 GTGTAATCCAGTCTGTGGCCCTGACGTTGAAAGCAAAACGCTTGGCTGGGATGATGA 
               
               
                 AAGCATTGCGTTTCGAAGAACGTCCCATTCCTGATCCGGCAGATGTTCCACTGGAGG 
               
               
                 AAATCGACGTCTCTAATCCTTTTATGAACCGCCAAGGACAATGGTATCCGTATTTTG 
               
               
                 CGCGTTTACGCGAGGAGGCGCCTGTGCATTATCAACCCAAGTCGCCTTTTGGGCCGT 
               
               
                 TCTGGTCGGTTACGCGTTACGCGGACATTCAAGCGGTTGATTCAAACGCAGAGGTCT 
               
               
                 TTAGTGCAGAACCGTATATCGTCTTAGGCCCTCCACCGTTCAACGCCGAAATGTTCA 
               
               
                 TCGCCATGGACCCTCCCAAACACGACGTCCAGCGTCGTGCAGTCCAAGGTGTGGTCG 
               
               
                 CGCCGAAGAACTTAAAAGAAATGGAGAGTTTAATCCGCGAACGCGTACAGGATGTA 
               
               
                 TTAGATAATTTACCGACAGACCGCCCCTTTGATTGGGTCGAACGTGTCAGTAAAGAA 
               
               
                 ATCACAGGGCGCATGTTAGCCACCTTATTGGATTTCCCATTCGAGGAGCGCCATAAG 
               
               
                 TTGACGTATTGGAGTGACACGATCAGTGGCTCAGCAGACGCAACTGGTGGCACGAC 
               
               
                 CCATCAAGACGAGTTGTTCCCTGCCGCAGTTGATTTGGCACGCAATTTCACCGCCCT 
               
               
                 GTGGCACGATAAGGCAGCTCGTCGCGCTGCGGGCGAACCAGATGGGTTTGACCTTA 
               
               
                 TTACACTTATGCAGACATCGGAGGACACAAAAGACCTTATCAAAAAGCCGTTTGAG 
               
               
                 TTTCTGGGGAATTTGACTTTATTGATTGTTGGTGGAAATGACACAACTCGCAACTCG 
               
               
                 ATGTCAGGAGGCGTTCTGGCACTTAACCGCTTTCCAGATGAATTTGAGAAGTTGAAA 
               
               
                 GCGGACCCAAAACTGATTCCGAACATGGTATCCGAGATCATCCGTTGGCAGACTCCC 
               
               
                 TTGGCATATATGCGCCGCGTAGCTAAAAAAGACGTTCATTTTGGCGGGCAATTTATT 
               
               
                 CGCAAAGGTGACGTTGTATTAATGTGGTACGCCTCTGGGAATCGTGACGAGCGCAA 
               
               
                 GTTTGAAAACGCCGACGACTTCATCATCGACCGTAAGAATGCACGCAACCACATGT 
               
               
                 CTTTCGGATTCGGAGTCCACCGTTGCATGGGTAACCGCTTAGCTGAGATGCAGCTTC 
               
               
                 GTATCCTTTGGGAAGAGCTTTTGGAACGTTTTGACCGCATCGACGTAATTGGCGAAC 
               
               
                 CAGGGTATGTACAGTCAAACTTTGTCAAAGGGTACTCCGACATGCAGGTCCAATTAA 
               
               
                 CGCCTAAGCCCGCTCGCGAACAAACACCTGTCCGCGTTGAGGCCACTTCGGGTGCAT 
               
               
                 ACTAA 
               
               
                   
               
               
                 CYP153_Pmed from  Patulibacter medicamentivorans  (protein) 
               
               
                 SEQ ID NO: 24 
               
               
                 MFEQTTTKRETMTTNSTLFQRTKVRVTDTVQATVPVDRVIQSVALTLKAKRLAGMMK 
               
               
                 ALRFEERPIPDPADVPLEEIDVSNPFMNRQGQWYPYFARLREEAPVHYQPKSPFGPFWSV 
               
               
                 TRYADIQAVDSNAEVFSAEPYIVLGPPPFNAEMFIAMDPPKHDVQRRAVQGVVAPKNLK 
               
               
                 EMESLIRERVQDVLDNLPTDRPFDWVERVSKEITGRMLATLLDFPFEERHKLTYWSDTIS 
               
               
                 GSADATGGTTHQDELFPAAVDLARNFTALWHDKAARRAAGEPDGFDLITLMQTSEDTK 
               
               
                 DLIKKPFEFLGNLTLLIVGGNDTTRNSMSGGVLALNRFPDEFEKLKADPKLIPNMVSEIIR 
               
               
                 WQTPLAYMRRVAKKDVHFGGQFIRKGDVVLMWYASGNRDERKFENADDFIIDRKNAR 
               
               
                 NHMSFGFGVHRCMGNRLAEMQLRILWEELLERFDRIDVIGEPGYVQSNFVKGYSDMQV 
               
               
                 QLTPKPAREQTPVRVEATSGAY. 
               
               
                   
               
               
                 CYP153_Ppsy from  Paraglaciecola psychrophila  170 (DNA) 
               
               
                 SEQ ID NO: 25 
               
               
                 ATGAACTCGCTGACGAACACCACGGCTGAGCCTGTCGCGACAAGTTCTATCACACC 
               
               
                 GACCCCTGCTGTGAAATTCATCGAACAACCTATTGCCGATGTTTCTACGGTGGCTCT 
               
               
                 GGAGGACATCGATGTGTCGAATCCATTCATGTTCCGTCAGAACAAGTGGCAATCGTA 
               
               
                 CTTTAAACGTTTGCGCGATGAGTGCCCGGTTCATTATCAAAAAAATTCACCTTTCGG 
               
               
                 GGCATTCTGGTCGGTAACCCGTTTCGAGGATATTATGTTTGTGGATAAGAATCACAC 
               
               
                 GCTGTTTAGTTCCGAACCTGCCATCGTGATCGGAGACCGCCCAGCTGACTATATGCT 
               
               
                 TGACATGTTTATTGCAATGGACCCGCCTAAACATGATGCTCAGCGTCAGGCTGTGCA 
               
               
                 GAGCGCGGTTGCCCCCAAAAACCTGGCGGAGATGGAGGAACTGATTCGCGAGCGTA 
               
               
                 CAGTAGATGTCCTGAACGATCTTCCGGTAGGTGAATCGTTCGACTGGGTTGAGAAAG 
               
               
                 TAAGTGTGGAACTGACTACTCGCATGCTGGCGACACTGTTTGACTTCCCGTACGAAA 
               
               
                 AGCGCCATAAGCTGCCTTACTGGTCGGATCTTGCGTCCGGCTCCCCCGAAATGACTG 
               
               
                 GTGGCTTAGTGCAAGACGATGAACGCGTGGCAGGCATCACGGACCTTATGACAGAG 
               
               
                 TTCTCCCAGCTTTGGCACATCAAGGCGGCACAGAAAGCAGCGGGTGAACAGGGAGG 
               
               
                 CTTTGATCTTATTTCATTGATGCAGGCCAATGACAACACAAAAAACATGGTCGACAC 
               
               
                 CCCGTTAGAGTTCCTGGGTAACCTTGTGCTGCTGATTGTTGGTGGCAACGACACCAC 
               
               
                 TCGCAACAGTATGACTGGCGGCGTCGATGCGCTGAACGAGTTTCCTCAAGAGTTCAT 
               
               
                 TAAGCTGAAAAATGACCCGAGCTTAATTCCCAATATGGTATCTGAAATCATCCGCTG 
               
               
                 GCAGACTCCCCTTGCTCACATGCGTCGCATCGCGACAGAAGACGTGGAATTAAATG 
               
               
                 GGAAGACGATTAAGAAGGGAGACAAGGTTGTTATGTGGTACGTGTCCGGAAATCGT 
               
               
                 GATGAACGTGTAATTAATAATCCTGATCAATTCGTCATTGACCGCGACAAAGCCCGT 
               
               
                 AATCATCTGTCGTTTGGATTTGGGATTCATCGTTGCATGGGTAACCGCTTAGCGGAA 
               
               
                 ATGCAACTGCGCATCCTTTGGGAGGAAATCTTACAACGTTTTGAGAATATCGAAGTG 
               
               
                 ATTAACAAGCCCAAATACGTTCAGTCTAACTTCGTCAAGGGATATACGGAACTTCGT 
               
               
                 GTTAAATTGACAGCCAAAGTGTACTAA 
               
               
                   
               
               
                 CYP153_Ppsy from  Paraglaciecola psychrophila  170 
               
               
                 (protein) SEQ ID NO: 26 
               
               
                 MNSLTNTTAEPVATSSITPTPAVKFIEQPIADVSTVALEDIDVSNPFMFRQNKWQSYFKR 
               
               
                 LRDECPVHYQKNSPFGAFWSVTRFEDIMFVDKNHTLFSSEPAIVIGDRPADYMLDMFIA 
               
               
                 MDPPKHDAQRQAVQSAVAPKNLAEMEELIRERTVDVLNDLPVGESFDWVEKVSVELTT 
               
               
                 RMLATLFDFPYEKRUKLPYWSDLASGSPEMTGGLVQDDERVAGITDLMTEFSQLWHIK 
               
               
                 AAQKAAGEQGGFDLISLMQANDNTKNIVIVDTPLEFLGNLVLLIVGGNDTTRNSMTGGV 
               
               
                 DALNEFPQEFIKLKNDPSLIPNMVSEIIRWQTPLAHMRRIATEDVELNGKTIKKGDKVVM 
               
               
                 WYVSGNRDERVINNPDQFVIDRDKARNHLSFGFGIHRCMGNRLAEMQLRILWEEILQRF 
               
               
                 ENIEVINKPKYVQSNFVKGYTELRVKLTAKVY. 
               
               
                   
               
               
                 CYP153_Abro from  Afipia broomeae  ATCC 49717 (DNA) 
               
               
                 SEQ ID NO: 27 
               
               
                 ATGCACGGTACATTAGACCCCGCCCGCCATTCAGAACTTAATGCCGCACGCGAGAA 
               
               
                 AGCCTACAGTACGCCGATCGAGCAGTTTAATCCCGGCGACCCAGACCTTTTCCGCAA 
               
               
                 CGATACATTCTGGCCGTACTTCGAACGTTTGCGTAAGGAGGACCCAGTGCACTATTG 
               
               
                 TAAAGATTCTCAATTCGGGGCCTATTGGTCCGTGATGAAATATAACGATATTATGCA 
               
               
                 TGTTGAGACGAATCATCAAATTTACAGCAGTGAAGCCAGCCTTGGTGGCATTACTAT 
               
               
                 TCGCGACGCTCCTCCGGAATTCCGTCGTCCAATGTTTATTGCAATGGACCAACCAAA 
               
               
                 ACACAGCGCCCAGCGCAAGACGGTCGCTCCGATGTTTACACCCACACATTTGGATG 
               
               
                 AACTGGCCGGAACAATCCGCCAGCGTGCTGCACAATGCTTAGACGCACTTCCTCGTA 
               
               
                 ATGCAACTTTCGACTGGGTAGATCGCGTAAGCATCGAACTTACGACTCAGATGCTGG 
               
               
                 CGACTCTTTTTGATTTTCCCTGGGAGGACCGTCGCAAATTGACGCGCTGGTCCGATG 
               
               
                 TAGCTACCGCCTTGCCTGGTAACACTGACATCATCGCGTCTGAGGATGCCCGTCAAG 
               
               
                 CGGAGCTTCAGGAGTGTGCTGCATATTTCTCTCGTTTGTGGAACGAACGCATTAACG 
               
               
                 CGCCCCCCAAATCAGATCTTCTTTCAATGATGGCCCATGCCGAAGCAACTCGCGACA 
               
               
                 TGGACCCCAAGACGTTTCTTGGCAACCTGATCTTGTTGATCGTGGGAGGGAACGACA 
               
               
                 CGACACGTAATTCACTGTCCGGAGGATTATACGCTTTGAACGAAAACCCAGCCGAAT 
               
               
                 ACCAAAAGTTACGTAGTAATCACGCCTTAGTGGACTCGATGGTGCCAGAGGTGATCC 
               
               
                 GCTGGCAGACACCGTTGGCACATATGCGTCGCACAGCCCTGCAAGACACAGAGTTG 
               
               
                 CGCGGCAAGCACATTAAAAAGGGAGATAAGGTTGTCATGTGGTACGTATCTGGCAA 
               
               
                 TCGCGACGATGAAGTGATTGAAAATCCAGACAGTTTCATTATCGATCGCGCACGTCC 
               
               
                 CCGCCAACACCTGTCGTTCGGCTTTGGAATCCACCGCTGTGTCGGCATCCGTCTTGCT 
               
               
                 GAGTTACAGTTGAAGATCGTCTGGGAAGAGATCCTTAAACGCTTCGATAACATCGA 
               
               
                 GGTAGTAGAACCCCCACACCGCGTTTACTCCTCCTTTGTGAAAGGGTACGAAACACT 
               
               
                 GCCCGTGCGTTTGGCATCATACTAA 
               
               
                   
               
               
                 CYP153_Abro from  Afipia broomeae  ATCC 49717 (protein) 
               
               
                 SEQ ID NO: 28 
               
               
                 MHGTLDPARHSELNAAREKAYSTPIEQFNPGDPDLFRNDTFWPYFERLRKEDPVHYCKD 
               
               
                 SQFGAYWSVMKYNDIMHVETNHQIYSSEASLGGITIRDAPPEFRRPMFIAMDQPKHSAQ 
               
               
                 RKTVAPMFTPTHLDELAGTIRQRAAQCLDALPRNATFDWVDRVSIELTTQMLATLFDFP 
               
               
                 WEDRRKLTRWSDVATALPGNTDIIASEDARQAELQECAAYFSRLWNERINAPPKSDLLS 
               
               
                 MMAHAEATRDMDPKTFLGNLILLIVGGNDTTRNSLSGGLYALNENPAEYQKLRSNHAL 
               
               
                 VDSMVPEVIRWQTPLAHMRRTALQDTELRGKHIKKGDKVVMWYVSGNRDDEVIENPD 
               
               
                 SFIIDRARPRQHLSFGFGIHRCVGIRLAELQLKIVWEEILKRFDNIEVVEPPHRVYSSFVKG 
               
               
                 YETLPVRLASY. 
               
               
                   
               
               
                 CYP153_Rrub from  Rhodococcus ruber  BKS 20-38 (DNA) 
               
               
                 SEQ ID NO: 29 
               
               
                 ATGAAGATTCCCGAGGCTATTACAGCCAAAGTGCAATCTACGATTCCCATGGATCTG 
               
               
                 CAGATTCAGGGTGCACATTTGTACGATAAAACACGTCGCTGGGTGACGGGGACAAA 
               
               
                 TGGTGAAAAATTGTTTGTGGAGAGCCCTATCCCTCCCGTTGAGGACGTTGAGCTTGC 
               
               
                 AGATATTGATTTATCGAATCCTTTTCTTTATCGTCAAGGACGCTGGCAGTCCTACTTC 
               
               
                 GAACGCTTGCGCAACGAAGCTCCTGTCCACTATCAGCCTAACTCGGCCTTCGGTCCG 
               
               
                 TTTTGGTCCGTAACCCGTCACGCAGACATCGTCGCAGTGGATAAAAATCACGAGCTG 
               
               
                 TTCTCGGCCGAACCCTTTATCGTGATTGGAGCCCCACCGCGTTTCCTTGACATTGCCA 
               
               
                 TGTTTATCGCAATGGACCCGCCGCGCCACGATGCACAACGTGCCGCAGTACAAGGG 
               
               
                 GTGGTTGCCCCCAAGAACTTACGCGAAATGGAAGGTTTGATCCGCTCCCGTGTGCAA 
               
               
                 GAAGTTTTGGATGACCTGCCGGTAGACCAACCCTTTGATTGGGTCCAAAATGTTAGT 
               
               
                 ATCGAGTTAACGGCTCGCATGTTAGCCACATTATTGGACTTTCCGTATGAACAACGC 
               
               
                 CGTAAGTTGGTGTACTGGTCAGACCTGGCGACCTCTCTGGAGCAGGCGAACGGGGG 
               
               
                 CCCCAGCGATAATGACGAAGTGTTTCCCGGAATGCGCGATATGGCTCGTGGGTTATC 
               
               
                 AGCATTATGGCATGACAAAGCCGCTCGCATGGCTGCGGGGGAAGAACCAGGCTTTG 
               
               
                 ATCTGATCACTATGTTGCAGAGCAATGAGAACACGAAGGATCTTATCGATCGTCCTA 
               
               
                 TGGAATTTCTGGGCAATCTGGTGTTACTGATTGTAGGAGGAAACGACACGACGCGC 
               
               
                 AACTCTATGTCCGGAGGAGTCCTTGCGTTGAACCGCTTCCCAGATCAGTTCGAGAAG 
               
               
                 CTTAAGGCTAACCCAGATTTGATTCCAAATATGGGTTCAGAAATTATTCGTTGGCAA 
               
               
                 ACACCTTTGGCTTACATGCGTCGTGTTGCGAAAGCCGATACCATTTTGAACGGTCAG 
               
               
                 TTTATCCGTAAGGGGGATAAGGTTGTGATGTGGTATGCAAGTGGTAATCGTGATGAG 
               
               
                 CGCGTGTTCGAACGCCCCGATGAATTTATTATTGACCGTGCTAACGCCCGTAACCAC 
               
               
                 ATCTCTTTTGGCTTCGGGGTCCACCGTTGTATGGGTAATCGTTTGGCCGAATTGCAAT 
               
               
                 TACGTATCCTTTGGGAAGAATTATTGCCTCGCTTTGACAATATCGAGGTAGTAGGGG 
               
               
                 AGCCTGAGTACGTTCAGTCGAATTTTGTACGCGGTATTAGTAAAATGATGGTACGTC 
               
               
                 TGACCCCCAAATCCAGTGCCTACTAA 
               
               
                   
               
               
                 CYP153_Rrub from  Rhodococcus ruber  BKS 20-38 (protein) 
               
               
                 SEQ ID NO: 30 
               
               
                 MKIPEAITAKVQSTIPMDLQIQGAHLYDKTRRWVTGTNGEKLFVESPIPPVEDVELADID 
               
               
                 LSNPFLYRQGRWQSYFERLRNEAPVHYQPNSAFGPFWSVTRHADIVAVDKNHELFSAEP 
               
               
                 FIVIGAPPRFLDIAMFIAMDPPRHDAQRAAVQGVVAPKNLREMEGLIRSRVQEVLDDLP 
               
               
                 VDQPFDWVQNVSIELTARMLATLLDFPYEQRRKLVYWSDLATSLEQANGGPSDNDEVF 
               
               
                 PGMRDMARGLSALWHDKAARMAAGEEPGFDLITMLQSNENTKDLIDRPMEFLGNLVL 
               
               
                 LIVGGNDTTRNSMSGGVLALNRFPDQFEKLKANPDLIPNMGSEIIRWQTPLAYMRRVAK 
               
               
                 ADTILNGQFIRKGDKVVMWYASGNRDERVFERPDEFIIDRANARNHISFGFGVHRCMGN 
               
               
                 RLAELQLRILWEELLPRFDNIEVVGEPEYVQSNFVRGISKMMVRLTPKSSAY. 
               
               
                   
               
               
                 CYP153_Gpar from  Gordonia paraffinivorans  (DNA) 
               
               
                 SEQ ID NO: 31 
               
               
                 ATGCAGATCCTTGACCGTGTCGTCGAGACGGTGCAGGCCAATATTCCGGTCGACCGC 
               
               
                 CAGGTGCAGGCGTTACAACTGTTTCACAAAGCACGTGGTCGCCTGGTAGGGGAATC 
               
               
                 ACGTCCAGAGCCGTTTGTAGAGAAGCCCATCCCCCCAGTTGATGAAGTATCGCTGGA 
               
               
                 TGCCATTGACATGTCTAATCCCTTCATGTATCGCCAAGGCCAGTGGGCGCCATACTT 
               
               
                 CGCGCGCTTGCGTGAAGAAGCGCCAGTTCATTACCAGCCCAATTCCCGTTTTGGGCC 
               
               
                 GTTTTGGTCGGTGACCCGTTACGAAGACATCCTGACCGTCGATAAAGACCACGAGAC 
               
               
                 CTTCAGTGCAGAACCATTTATCGTAATTGGGACGCCGCCCCCTGGATTGGATGTAGA 
               
               
                 GATGTTTATTGCTATGGACCCGCCGCGCCACGATGTGCAACGCCGCGCGGTCCAGGG 
               
               
                 AGTCGTAGCCCCAAAAAACTTAAAAGAAATGGAAGGACTGATCCGCGAGCGTGTTT 
               
               
                 GTGAAGTGTTAGATAATCTTCCCGTAGGTCAGCCATTTAACTGGGTCGATCGCGTTA 
               
               
                 GTGTAGAGATCACTGCTCGCACCTTAGCGACGATCTTAGATTTCCCCTATGAGCAGC 
               
               
                 GCCGTAATTTAGTTCGCTGGAGTGACCTGGCCGCAGGATCCGAAGAAGCCACAGGT 
               
               
                 GGTGCCAGCGATCCAGACGTCGTCTACCAGGCGGCGCTTGAGATGGTACGTGCTTTC 
               
               
                 TCAGAGTTATGGCACGATAAGGCCGCACGTCGTGCCGCAGGCGAGGAACCAGGCTT 
               
               
                 TGATTTGATCTCAATGTTACAATCCAATGAGGACACCAAGGATTTGGTTAAACGTCC 
               
               
                 GATGGAATTCATTGGGAATCTTACATTACTGATTGTCGGTGGAAACGACACCACTCG 
               
               
                 CAATAGCATGTCGGGTGGAGTGTACGCGCTGAATAAGTTTCCTGGAGAGTTCGAGA 
               
               
                 AACTTAAGGCAGACCCGTCTTTGATTCCGAATATGGTTTCTGAGATCATTCGTTGGC 
               
               
                 AGACGCCCTTGGCGTACATGCGTCGCGTCGCGACTAAAGACACCATCCTTAATGGCC 
               
               
                 AATTCATTCGTAAAGGCGACAAGTTGGTGATGTGGTATGCATCCGGAAACCGCGAT 
               
               
                 GAGTCTAAGTTCGAGCGTGCGGATGAGTTGATTATCGACCGCCCCAACGCTCGTAAT 
               
               
                 CACATGGCGTTTGGGTATGGGGTGCACCGCTGCATGGGCAATCGTCTTGCCGAGCTG 
               
               
                 CAACTTCGCATCTTATGGGAAGAATTACTGGAACGCTTCGACGACATCAAGGTCTTG 
               
               
                 GAGGAACCAGAGTATGTTCAGTCTAACTTTGTTCGCGGTTACTCTAAGTTGATGGTG 
               
               
                 GAGCTGACGGCGAAGAAGACGTCTTACTAA 
               
               
                   
               
               
                 CYP153_Gpar from  Gordonia paraffinivorans  (protein) 
               
               
                 SEQ ID NO: 32 
               
               
                 MQILDRVVETVQANIPVDRQVQALQLFHKARGRLVGESRPEPFVEKPIPPVDEVSLDAID 
               
               
                 MSNPFMYRQGQWAPYFARLREEAPVHYQPNSRFGPFWSVTRYEDILTVDKDHETFSAE 
               
               
                 PFIVIGTPPPGLDVEMFIAMDPPRHDVQRRAVQGVVAPKNLKEMEGLIRERVCEVLDNL 
               
               
                 PVGQPFNWVDRVSVEITARTLATILDFPYEQRRNLVRWSDLAAGSEEATGGASDPDVV 
               
               
                 YQAALEMVRAFSELWHDKAARRAAGEEPGFDLISMLQSNEDTKDLVKRPMEFIGNLTL 
               
               
                 LIVGGNDTTRNSMSGGVYALNKFPGEFEKLKADPSLIPNMVSEIIRWQTPLAYMRRVAT 
               
               
                 KDTILNGQFIRKGDKLVMWYASGNRDESKFERADELIIDRPNARNHMAFGYGVHRCMG 
               
               
                 NRLAELQLRILWEELLERFDDIKVLEEPEYVQSNFVRGYSKLMVELTAKKTSY. 
               
               
                   
               
               
                 CYP153_A_OC4 from  Acinetobacter  sp. OC4 (DNA) 
               
               
                 SEQ ID NO: 33 
               
               
                 ATGAACTCGGTGGCAGAGATTTTTGAGAAGATTACTCAAACGGTCACTAGTACAGC 
               
               
                 AGCAGACGTTGCCACAACAGTGACTGACAAGGTGAAATCGAACGAACAGTTTCAGA 
               
               
                 CGGGAAAGCAATTCTTACACGGACAAGTTACCCGCTTCGTACCTTTGCACACACAGG 
               
               
                 TCCGCGGTATTCAGTGGATGCAAAAGGCTAAGTTCCGCGTGTTTAACGTGCAAGAGT 
               
               
                 TTCCCGCATTTATTGAGCAACCTATTCCTGAGGTCGCCACGCTTGCTCTTGCGGAAAT 
               
               
                 CGACGTTTCCAACCCCTTTTTGTACAAACAGAAGAAATGGCAGTCTTATTTCAAGCG 
               
               
                 CTTGCGTGATGAAGCGCCCGTGCATTATCAGGCGAACTCTCCCTTCGGCGCATTCTG 
               
               
                 GTCAGTCACCCGTTATGACGACATTGTCTATGTCGACAAGAATCACGAGATCTTTTC 
               
               
                 GGCTGAACCAGTAATTGCCATTGGGAATACGCCGCCCGGCTTAGGTGCAGAGATGTT 
               
               
                 TATCGCGATGGACCCACCGAAGCACGATGTCCAACGCCAGGCTGTCCAGGATGTAG 
               
               
                 TCGCACCGAAAAACTTGAAAGAATTAGAGGGCTTGATTCGCCTTCGTGTTCAGGAAG 
               
               
                 TACTGGACCAATTGCCCACGGATCAACCCTTTGATTGGGTGCAAAATGTATCCATCG 
               
               
                 AATTGACGGCGCGTATGTTGGCAACCTTGTTTGATTTTCCATACGAAAAGCGTCACA 
               
               
                 AGTTAGTAGAGTGGTCAGATCTGATGGCCGGGACTGCGGAGGCAACAGGGGGTACA 
               
               
                 GTGACTAACCTGGATGAGATTTTCGACGCTGCTGTCGACGCGGCTAAACACTTTGCT 
               
               
                 GAATTGTGGCATCGCAAAGCCGCTCAGAAGTCTGCAGGAGCGGAGATGGGTTATGA 
               
               
                 TTTGATTTCTCTTATGCAGAGTAATGAGGCAACCAAAGATTTGATCTATCGCCCCAT 
               
               
                 GGAATTTATGGGAAATCTGGTGTTATTAATCGTAGGTGGTAATGACACTACACGTAA 
               
               
                 TAGTATGACGGGTGGTGTTTATGCGTTGAATCTTTTTCCAAATGAGTTTGTAAAGTTG 
               
               
                 AAGAATAATCCCTCACTGATTCCGAATATGGTCAGCGAAATTATCCGCTGGCAAACA 
               
               
                 CCTCTGGCATATATGCGCCGCATCGCCAAGCAGGACGTCGAGTTAAATGGGCAAAC 
               
               
                 AATTAAAAAAGGTGACAAAGTGGTAATGTGGTATGTTTCGGGGAACCGTGATGAAC 
               
               
                 GTGTGATTGAGCGCCCAGATGAACTTATCATTGACCGTAAGGGTGCTCGTAATCACC 
               
               
                 TTTCTTTCGGTTTCGGAGTGCATCGCTGCATGGGAAACCGTTTAGCGGAGATGCAGC 
               
               
                 TTCGTATCTTGTGGGAAGAGCTGCTTCAACGCTTTGAAAATATCGAAGTTCTGGGGG 
               
               
                 AGCCGGAAATCGTGCAATCGAACTTTGTCCGCGGTTACGCCAAAATGATGGTGAAA 
               
               
                 CTGACCGCGAAGGCCTACTAA 
               
               
                   
               
               
                 CYP153_A_OC4 from  Acinetobacter  sp. OC4 (protein) 
               
               
                 SEQ ID NO: 34 
               
               
                 MNSVAEIFEKITQTVTSTAADVATTVTDKVKSNEQFQTGKQFLHGQVTRFVPLHTQVRG 
               
               
                 IQWMQKAKFRVFNVQEFPAFIEQPIPEVATLALAEIDVSNPFLYKQKKWQSYFKRLRDE 
               
               
                 APVHYQANSPFGAFWSVTRYDDIVYVDKNHEIFSAEPVIAIGNTPPGLGAEMFIAMDPPK 
               
               
                 HDVQRQAVQDVVAPKNLKELEGLIRLRVQEVLDQLPTDQPFDWVQNVSIELTARMLAT 
               
               
                 LFDFPYEKRHKLVEWSDLMAGTAEATGGTVTNLDEIFDAAVDAAKHFAELWHRKAAQ 
               
               
                 KSAGAEMGYDLISLMQSNEATKDLIYRPMEFMGNLVLLIVGGNDTTRNSMTGGVYALN 
               
               
                 LFPNEFVKLKNNPSLIPNMVSEIIRWQTPLAYMRRIAKQDVELNGQTIKKGDKVVMWYV 
               
               
                 SGNRDERVIERPDELIIDRKGARNHLSFGFGVHRCMGNRLAEMQLRILWEELLQRFENIE 
               
               
                 VLGEPEIVQSNFVRGYAKMMVKLTAKAY. 
               
               
                   
               
               
                 CYP153_Smac from  Sphingopyxis macrogoltabida  (DNA) 
               
               
                 SEQ ID NO: 35 
               
               
                 ATGGAGCACACCGGTCAATCTGCGGCAGCCACAATGCCACTGGATAGCATCGATGT 
               
               
                 GTCCATCCCAGAACTTTTTTATAACGATTCGGTAGGAGAGTATTTCAAGCGTTTACG 
               
               
                 CAAGGATGACCCCGTGCACTATTGTGCAGATTCCGCGTTCGGCCCATATTGGTCCAT 
               
               
                 CACTAAGTATAACGATATCATGCACGTGGACACAAACCATGACATTTTTTCTAGCGA 
               
               
                 CGCCGGATACGGGGGTATTATTATTGACGACGGCATTCAAAAGGGTGGGGACGGTG 
               
               
                 GGTTAGATTTACCGAATTTCATCGCTATGGATCGTCCCCGTCATGACGAGCAACGTA 
               
               
                 AGGCTGTGAGCCCAATCGTGGCTCCTGCGAACTTGGCTGCCCTTGAGGGAACGATCC 
               
               
                 GCGAGCGTGTCAGCAAGACTCTGGACGGTCTGCCGGTTGGTGAGGAGTTCGACTGG 
               
               
                 GTTGACCGTGTATCAATCGAGATTACTACGCAGATGTTAGCGACTTTGTTCGACTTTC 
               
               
                 CGTTCGAAGAGCGCCGTAAACTGACCCGCTGGAGTGATGTAACGACCGCCGCACCC 
               
               
                 GGAGGCGGAGTCGTGGAGAGTTGGGACCAACGTAAGACCGAATTACTTGAGTGCGC 
               
               
                 GGCCTATTTTCAGGTTCTTTGGAATGAGCGTGTGAACAAAGACCCCGGCAACGATCT 
               
               
                 TATTAGTATGCTTGCACATAGTCCTGCTACTCGTAACATGACACCTGAAGAATACTT 
               
               
                 GGGTAATGTTCTGCTTTTGATCGTAGGCGGGAACGACACCACGCGTAACTCAATGAC 
               
               
                 TGGTGGCGTATTGGCTCTGCACAAGAACCCGGATCAATTTGCAAAGCTGAAAGCTA 
               
               
                 ACCCCGCCCTTGTTGAAACGATGGTCCCCGAGATCATCCGTTGGCAAACGCCTTTAG 
               
               
                 CGCATATGCGTCGTACGGCAATTGCGGACTCGGAGCTGGGTGGTAAGACTATTCGCA 
               
               
                 AGGGTGATAAAGTCGTGATGTGGTACTATTCAGGTAACCGCGACGATGAAGTTATTG 
               
               
                 ATCGTCCCGAAGAATTCATTATTGACCGCCCTCGCCCCCGTCAACACCTTTCCTTCGG 
               
               
                 TTTCGGCATCCATCGCTGTGTTGGGAATCGCTTAGCTGAAATGCAACTTCGTATTCTG 
               
               
                 TGGGAAGAAATTCTTACGCGCTTCAGTCGCATTGAGGTGATGGCGGAACCTGAGCGT 
               
               
                 GTGCGCTCGAATTTTGTTCGCGGTTACGCGAAAATGATGGTCCGTGTTCATGCTTACT 
               
               
                 AA 
               
               
                   
               
               
                 CYP153_Smac from  Sphingopyxis macrogoltabida  (protein) 
               
               
                 SEQ ID NO: 36 
               
               
                 MEHTGQSAAATMPLDSIDVSIPELFYNDSVGEYFKRLRKDDPVHYCADSAFGPYWSITK 
               
               
                 YNDIMHVDTNHDIFSSDAGYGGIIIDDGIQKGGDGGLDLPNFIAMDRPRHDEQRKAVSPI 
               
               
                 VAPANLAALEGTIRERVSKTLDGLPVGEEFDWVDRVSIEITTQMLATLFDFPFEERRKLT 
               
               
                 RWSDVTTAAPGGGVVESWDQRKTELLECAAYFQVLWNERVNKDPGNDLISMLAHSPA 
               
               
                 TRNMTPEEYLGNVLLLIVGGNDTTRNSMTGGVLALHKNPDQFAKLKANPALVETMVPE 
               
               
                 IIRWQTPLAHMRRTAIADSELGGKTIRKGDKVVMWYYSGNRDDEVIDRPEEFIIDRPRPR 
               
               
                 QHLSFGFGIHRCVGNRLAEMQLRILWEEILTRFSRIEVMAEPERVRSNFVRGYAKMMVR 
               
               
                 VHAY. 
               
               
                   
               
               
                 CYP153_M_HXN1500 from  Mycobacterium  sp. HXN-1500 
               
               
                 (DNA) SEQ ID NO: 37 
               
               
                 ATGACGGAAATGACAGTCGCAGCCTCCGACGCGACTAATGCGGCTTATGGTATGGC 
               
               
                 CCTGGAAGATATCGATGTCAGTAACCCTGTGCTGTTCCGTGACAACACATGGCACCC 
               
               
                 TTACTTTAAACGCTTACGCGAGGAGGACCCAGTTCATTATTGCAAATCCAGTATGTT 
               
               
                 CGGGCCCTATTGGTCAGTGACAAAATATCGTGATATTATGGCCGTAGAAACCAATCC 
               
               
                 GAAGGTCTTTAGCTCTGAGGCGAAATCTGGCGGAATCACAATTATGGACGACAACG 
               
               
                 CGGCTGCTAGTCTGCCAATGTTTATTGCGATGGATCCTCCGAAACATGACGTACAAC 
               
               
                 GTAAAACGGTTTCGCCGATCGTCGCGCCAGAGAACTTGGCCACAATGGAGTCAGTG 
               
               
                 ATTCGTCAGCGCACGGCTGATTTACTTGACGGGTTACCCATTAACGAGGAGTTCGAC 
               
               
                 TGGGTCCATCGTGTCTCTATCGAGCTGACCACGAAGATGCTGGCCACGCTTTTCGAT 
               
               
                 TTCCCTTGGGACGATCGCGCCAAACTGACACGCTGGTCCGACGTTACAACTGCGCTT 
               
               
                 CCCGGAGGGGGCATTATTGATAGTGAGGAACAGCGTATGGCGGAGTTGATGGAGTG 
               
               
                 TGCGACATATTTCACTGAATTGTGGAATCAGCGTGTGAATGCCGAGCCAAAGAACG 
               
               
                 ATTTAATTTCCATGATGGCTCACAGCGAGTCAACCCGTCATATGGCTCCGGAGGAGT 
               
               
                 ACTTAGGGAATATCGTACTGCTGATTGTTGGTGGAAACGATACTACACGCAATTCGA 
               
               
                 TGACAGGGGGGGTGCTTGCGTTAAACGAATTTCCGGATGAATATCGTAAGTTATCCG 
               
               
                 CCAACCCTGCCTTGATTAGTTCGATGGTATCAGAAATCATTCGTTGGCAAACCCCAC 
               
               
                 TTAGTCACATGCGTCGTACAGCCCTGGAAGATATCGAATTTGGTGGTAAACATATCC 
               
               
                 GCCAGGGTGACAAAGTTGTGATGTGGTACGTCTCTGGTAACCGTGACCCGGAAGCT 
               
               
                 ATCGATAATCCCGACACATTCATTATTGACCGCGCTAAGCCGCGCCAGCATTTATCC 
               
               
                 TTCGGGTTCGGGATTCATCGTTGTGTAGGCAACCGTTTAGCTGAATTGCAGTTAAAT 
               
               
                 ATCCTTTGGGAGGAGATTTTAAAACGTTGGCCGGATCCACTGCAGATCCAAGTGTTA 
               
               
                 CAGGAACCCACCCGTGTTCTGAGCCCCTTCGTTAAGGGCTACGAGAGTCTGCCGGTA 
               
               
                 CGTATCAATGCGTACTAA 
               
               
                   
               
               
                 CYP153_M_HXN1500 from  Mycobacterium  sp. HXN-1500 
               
               
                 (protein) SEQ ID NO: 38 
               
               
                 MTEMTVAASDATNAAYGMALEDIDVSNPVLFRDNTWHPYFKRLREEDPVHYCKSSMF 
               
               
                 GPYWSVTKYRDIMAVETNPKVFSSEAKSGGITIMDDNAAASLPMFIAMDPPKHDVQRK 
               
               
                 TVSPIVAPENLATMESVIRQRTADLLDGLPINEEFDWVHRVSIELTTKMLATLFDFPWDD 
               
               
                 RAKLTRWSDVTTALPGGGIIDSEEQRMAELMECATYFTELWNQRVNAEPKNDLISMMA 
               
               
                 HSESTRHMAPEEYLGNIVLLIVGGNDTTRNSMTGGVLALNEFPDEYRKLSANPALISSM 
               
               
                 VSEIIRWQTPLSHMRRTALEDIEFGGKHIRQGDKVVMWYVSGNRDPEAIDNPDTFIIDRA 
               
               
                 KPRQHLSFGFGIHRCVGNRLAELQLNILWEEILKRWPDPLQIQVLQEPTRVLSPFVKGYE 
               
               
                 SLPVRINAY. 
               
               
                   
               
               
                 CYP153_Cmic from  Candidatus Microthrix parvicella  RN1 
               
               
                 (DNA) SEQ ID NO: 39 
               
               
                 ATGACCGATGACACGAAGCCGCGCATTGATTTCGACCCATCGATTCGTACGCCAGA 
               
               
                 GATGGAAATGGCCGAAGTTGGGGCGGGGGTTCCAGATGCTGCTGACTTAAAACTTA 
               
               
                 CAGACTTAAATCCCGCTAATCCACATTTGTTTAAGGAGGACCGCTGGCACGATCATT 
               
               
                 TCGCTCGCTTACGTGCGGAGGACCCGGTCCATCTTAATGAAATCGAGACTGCGGGTC 
               
               
                 GCTACTGGTCTATCACGAAGTATGACGATGTGCGCGCCGTCGACGGCGATTGGCAA 
               
               
                 ACTTTCTCGTCGGCACAAGGTATGACGTTGGGGCTGCGCCCTGATCCCGACCGCCCG 
               
               
                 AATCCGCTGGTACAAATCACCCCTTTCATTGCGATGGACCCGCCGGAGCACACAGCA 
               
               
                 CAACGTAAAACTGTTCGCAGCGTGTCTGCTCCGTCCAACCTTCGTAACTTAGAACCC 
               
               
                 TTGATCCGCGAACGTACTGTTGCAGTGCTTGATTCTTTACCCGAAGGAGAAACCTTC 
               
               
                 GACTGGGTCGATACGGTCAGTATTGAGCTGACAACCCTTTTACTTGCCACATTATTT 
               
               
                 GACTTTCCGCTTGAGGATCGTCGCAAGCTTACCCGCTGGTCCGACATTGTTTTCGCCG 
               
               
                 TGCCCGGGTCGGGTGGAGTTGTAGAAACGCAGCAACAGAAAATCGAAGAGCTTATG 
               
               
                 GAGTGCGTCACTTACTTTGAGGGGTTATGGGAAGAGCGTCGTGGTGGTGACGGGAC 
               
               
                 AGACTTAGTTTCGATGTTGGCCAACGGGGAAGCAACTAAAGACATGCCCACCATTTC 
               
               
                 GCATTTGGGTAATCTGTTGCTGTTAATCGTGGGAGGGAACGATACAACCCGCAATAC 
               
               
                 CATGACAGGTTCGGTGTACGGATTGAACAAATATCCAGATCAATATGACAAATTAA 
               
               
                 CTGCGGACCCTGGCTTGATTAGCACCTTTGTTCCGGAGATTATTCGCTGGCAGACAC 
               
               
                 CACTGTCTTATATGCGTCGCACAGCCACGAAAGATTGTACAATCCGTGATAAACAGA 
               
               
                 TCCTTGAAGGCGACCAAGTGCTTATGTGGTATATTTCTGCTAATCGTGATGAGGACG 
               
               
                 TTTTTGTAGACGCTGAGCGCATCGACTTAGACCGCTCTAATGCGGACCGCCAACTGG 
               
               
                 CGTTCGGCTACGGAATCCACTTCTGCATGGGGTCGCGTCTTGCTGAATTGCAACTGC 
               
               
                 GCATTTTATGGGAAGAGGTACTTGCACGTTTCGAACGTATTGAGCTTCAAGCCGAGC 
               
               
                 CTGAGCGCACACTTAGTTCCTTTGTTCATGGGTACACGAAACTGCCTGTAACTGTTA 
               
               
                 CTCGCCGTTACTAA 
               
               
                   
               
               
                 CYP153_Cmic from  Candidatus Microthrix parvicella  RN1 
               
               
                 (protein) SEQ ID NO: 40 
               
               
                 MTDDTKPRIDFDPSIRTPEMEMAEVGAGVPDAADLKLTDLNPANPHLFKEDRWHDHFA 
               
               
                 RLRAEDPVHLNEIETAGRYWSITKYDDVRAVDGDWQTFSSAQGMTLGLRPDPDRPNPL 
               
               
                 VQITPFIAMDPPEHTAQRKTVRSVSAPSNLRNLEPLIRERTVAVLDSLPEGETFDWVDTV 
               
               
                 SIELTTLLLATLFDFPLEDRRKLTRWSDIVFAVPGSGGVVETQQQKIEELMECVTYFEGL 
               
               
                 WEERRGGDGTDLVSMLANGEATKDMPTISHLGNLLLLIVGGNDTTRNTMTGSVYGLNK 
               
               
                 YPDQYDKLTADPGLISTFVPEIIRWQTPLSYMRRTATKDCTIRDKQILEGDQVLMWYISA 
               
               
                 NRDEDVFVDAERIDLDRSNADRQLAFGYGIHFCMGSRLAELQLRILWEEVLARFERIELQ 
               
               
                 AEPERTLSSFVHGYTKLPVTVTRRY. 
               
               
                   
               
               
                 CYP153_A_P52 from  Afipia  sp. P52-10 (DNA) SEQ ID NO: 41 
               
               
                 ATGCAATCGACGCAACGTGGGGCCCGTGATTTTGCGACACGTCTGCCATTGGACGCG 
               
               
                 ATTGACGTATCCGATCCACAACTGTATCAGGACGATACCTGGCGTCCTCTTTTCGCG 
               
               
                 CGCCTTCGCGCGGAAGACCCGGTCCACTATTGTCGCGACTCGGCGTTTGGTCCCTAC 
               
               
                 TGGAGTGTAACGACGTACGACGATATCTTGAAAGTGGAACTTGATCATTCAACGTAC 
               
               
                 TCATCCAGCTCGGAACTGGGAGGCATTCAGGTGACCGATCAACCGAAGGGAAAGGA 
               
               
                 AACTATTTCTTTCATTCGTATGGACCCACCTGGCCACACTGCGCAACGCCGTATCGTT 
               
               
                 GCTCCTATCGTCGCCCCCACACACTTGGCAAACTTTGAGCCAGTGATCCGTGAGCGC 
               
               
                 ACAGCCCGTGTTCTTGACGGCCTGCCTCGTAATGAAACCTTCGATTGGGCTGACCGC 
               
               
                 GTCTCCGTCGAACTTACCGCAATGATGTTAGCAACTCTTTTCGACTTTCCCATGGAAG 
               
               
                 AACGTCGCAAGTTAACTTACTGGTCCGACGTAGCGATTGCTAACATTAACTCGCCGG 
               
               
                 AGAGCCCTATCACATCTGAGGATGAGCGCTCGGAGAAATTAGGGGAGATGGCCGCG 
               
               
                 TGCTTCAAGGCTTTGTGGGATCGCCGTGCAGCAGTCGAGCCCAAGTTCGACCTTGTA 
               
               
                 TCAATGTTGGCGCATGGGGCAGCGACTCGTGATATGGGGGTCCGTGAATTAACAGG 
               
               
                 TACTATCGGTTTGCTGATCGTGGGGGGTAATGATACAACCCGTAATTCCATGACGGG 
               
               
                 TGGAGTACTGGCGCTTCACGACTATCCCGAGGAGGCAGAAAAGTTGCGCGGCAATC 
               
               
                 CAGCCTTAATCCCGTCGTTAGTGTCCGAAATTATTCGTTATCAATCCCCGGTTTTGCA 
               
               
                 CATGCGTCGTACGGCCCGTGTTGATGCTGAGATTGGAGGAAAGACCATCCGCGCTG 
               
               
                 GGGACAAGGTCGTCATGTGGTACATTTCCGGGAACCGTGATGAGAAAAAGATCGAG 
               
               
                 CACGCAGATCGTTTTGTGATCGACCGTGCCAAGCCCCGTCAACATTTGGCTTTCGGG 
               
               
                 GCCGGCGTTCACCGTTGTGTTGGAGATCGCCTTGCCGAATTGCAGCTGCGCATTCTTT 
               
               
                 GGGAAGCAATCCTGGAACGCGGCTTTGTTATTGACGTAGTTGGGGAACCAAAGCGT 
               
               
                 CTTTATTCCAATTTCATCCGTGGCTTTCGCTCTCTTCCCGTGCGCATTCGCACTGCCTA 
               
               
                 CTAA 
               
               
                   
               
               
                 CYP153_A_P52 from  Afipia  sp. P52-10 (protein) SEQ ID NO: 42 
               
               
                 MQSTQRGARDFATRLPLDAIDVSDPQLYQDDTWRPLFARLRAEDPVHYCRDSAFGPYW 
               
               
                 SVTTYDDILKVELDHSTYSSSSELGGIQVTDQPKGKETISFIRMDPPGHTAQRRIVAPIVAP 
               
               
                 THLANFEPVIRERTARVLDGLPRNETFDWADRVSVELTAMMLATLFDFPMEERRKLTY 
               
               
                 WSDVAIANINSPESPITSEDERSEKLGEMAACFKALWDRRAAVEPKFDLVSMLAHGAAT 
               
               
                 RDMGVRELTGTIGLLIVGGNDTTRNSMTGGVLALHDYPEEAEKLRGNPALIPSLVSEIIR 
               
               
                 YQSPVLHMRRTARVDAEIGGKTIRAGDKVVMWYISGNRDEKKIEHADRFVIDRAKPRQ 
               
               
                 HLAFGAGVHRCVGDRLAELQLRILWEAILERGFVIDVVGEPKRLYSNFIRGFRSLPVRIR 
               
               
                 TAY. 
               
               
                   
               
               
                 CYP153_B_CACIA14H2 from  Blastomonas  sp. CACI414H2 
               
               
                 (DNA) SEQ ID NO: 43 
               
               
                 ATGGCAACAGTGCTGAAGGAGCCCGGCGCGGCGTTGAACTACGATATGAGTGATGC 
               
               
                 GTCCTGGTATGTGGAGGATCGCTGGCAAGAACCATTCCGTCAAATGCGTGAGCAAG 
               
               
                 ACCCGATTCACTGGACTGAAAATGGCATGTTCGGTAGTTTCTGGAATGTAACTAATC 
               
               
                 ACAAAGCGATCCAACACGTCGAAGCATTGCCAGAAATTTTCAGTTCCTCCTACGAAC 
               
               
                 ATGGAGGGATTACACTGGCAGACCGTATCGACGACGGGACGGAACTGGTTATGCCA 
               
               
                 ATGTTCATTGCCATGGACCGTCCGAAACACACAGGACAACGTCGTACTGTAGCTCCG 
               
               
                 GCCTTCACCCCTACAGAAATGAAGCGTATGTCTGACGATATCCGCCGTCGCACTGCC 
               
               
                 GAAATTTTAGACGGCCTTCCATGGGACCAGCCGTTCGATTGGGTTGATCGTGTCAGT 
               
               
                 ATCGAGCTTACGACACAGATGCTGGCTATTTTGTTCGACTTCCCATGGGAGGATCGT 
               
               
                 CGTAAACTGACCGAATGGAGTGATTGGGCCGGAGATATTGAATTGATTCATTCGGA 
               
               
                 GGAAATGCGTCAAGAGCGCTTAAAACATCTGTACGATATGGGCGCGTACTTTAAAA 
               
               
                 AGCTTTGGGATGCCAAAATCAACGCAGAACCAACCCCAGATTTAATCTCTATGATGA 
               
               
                 TCCATTCCGACGCCATGAGCGAGATGGATGAATTTGAGTTTATGGGTAACTTAATCC 
               
               
                 TGTTAATCGTCGGTGGCAACGATACGACGCGTAATTCAATGTCGGGTCTTGTGTATG 
               
               
                 GCCTGCAGCAGTTCCCGGATCAACGCGAGAAGCTTGAACAAAATCCGGCGCTTATC 
               
               
                 CCTAATGCGGTGCAAGAGATCATTCGCTGGCAGACACCCTTAGCCCATATGCGCCGC 
               
               
                 ACAGCACTGGAAGATTATGACTTATTCGGCAAGACTATTCGCAAAGGAGATAAACT 
               
               
                 GGCACTTTGGTACATTTCAGGGAACCGTGACGAGAGTGTGTTTGAGGATGCGGATA 
               
               
                 AAATCATCGTAGATCGTGAAAATGCTCGCCGCCACCTTGCGTTCGGATATGGTATCC 
               
               
                 ACCGTTGTGTCGGCGCTCGTTTAGCCGAATTGCAGATTGCGATTCTGTTAGAAGAGA 
               
               
                 TGGCGAAACGTCGTATGCGTGTTAATGTCCTTGAAGAGCCAGTTCGCGTTCGCGCGT 
               
               
                 GTTTTGTGCATGGGTATCGCTCCATGCAAGTTTCCTTATCAAAGTACTACTAA 
               
               
                   
               
               
                 CYP153_B_CACIA14H2 from  Blastomonas  sp. CACI414H2 
               
               
                 (protein) SEQ ID NO: 44 
               
               
                 MATVLKEPGAALNYDMSDASWYVEDRWQEPFRQMREQDPIHWTENGMFGSFWNVTN 
               
               
                 HKAIQHVEALPEIFSSSYEHGGITLADRIDDGTELVMPMFIAMDRPKHTGQRRTVAPAFT 
               
               
                 PTEMKRMSDDIRRRTAEILDGLPWDQPFDWVDRVSIELTTQMLAILFDFPWEDRRKLTE 
               
               
                 WSDWAGDIELIHSEEMRQERLKHLYDMGAYFKKLWDAKINAEPTPDLISMMIHSDAMS 
               
               
                 EMDEFEFMGNLILLIVGGNDTTRNSMSGLVYGLQQFPDQREKLEQNPALIPNAVQEIIRW 
               
               
                 QTPLAHMRRTALEDYDLFGKTIRKGDKLALWYISGNRDESVFEDADKIIVDRENARRHL 
               
               
                 AFGYGIHRCVGARLAELQIAILLEEMAKRRIVIRVNVLEEPVRVRACFVHGYRSMQVSLS 
               
               
                 KYY. 
               
               
                   
               
               
                 CYP153_CPha1 from  Candidatus Phaeomarinobacter ectocarpi   
               
               
                 (DNA) SEQ ID NO: 45 
               
               
                 ATGACGACCGCCAATCAAACTAGCCCAAATGGAGCCATTGACGTGAACGATATCCC 
               
               
                 TTTGGCAGAGTTAGATGTGAGCCAACCTCATCTGTTTAAGAACGACACCTGGCGCCC 
               
               
                 ATGGTTCGCACGCCTGCGTGCTGAGGCGCCCGTCCATTATCTTGCCGATAGCGAAAA 
               
               
                 CGGACCTTTCTGGTCGGTCACGTCACACGATATGACTAAAGCGGTCGACGCAAACC 
               
               
                 ATAAGGTCTTCTCATCCGAGGAGGGCGGCATTGCCATCGTCGACCCACAGCCTTTGG 
               
               
                 ACGGTGAGCAATTAATGCGTGACCCTTCGTTTATCTCAATGGATGAGCCAAAGCATG 
               
               
                 CTACACAACGCAAGGCCGTGTCGCCGGCTGTAGCTCCCAAAAACCTTGCAGAGCTG 
               
               
                 GAACCTTTGATTCGCGAGCGTGCCGCTGACATCCTTGATAACCTGCCAGTCGGGGAA 
               
               
                 ACCTTTAACTGGGTCGACCGTGTTTCAGTTGAACTTACAGCGCGCATGCTTGCGACG 
               
               
                 TTGTTCGACTTCCCTTATGAACGCCGTCGTGACTTGATTCGCTGGAGTGATGTGGCCA 
               
               
                 CCGCTGTACCTAAAGTGACTGGGGAGGCAAATGACATGGGTGCCCGCCGCGATGCG 
               
               
                 CTTATTGAATGCGCTACTACATTCTACCAATTATGGCAGGAACGCGCGGCACAACCT 
               
               
                 CCGAAGTTCGACTTCGTCAGCATGTTAGCCCATGGGGAAGCGACAAAACACCTTTCA 
               
               
                 GAAGACCCATTATTGATGTTGGGGAACATCATCTTATTGATCGTGGGTGGCAATGAC 
               
               
                 ACTACACGTAATTCGATTTCCGGGGGTGTTGTTGCTTTGAACCAGTATCCAGAAGAG 
               
               
                 TATCAGAAGTTGCGTGATACTCCCGCCCTGATCCCCAATATGGTGGCGGAGACGGTA 
               
               
                 CGCTGGCAAACCCCTGTTATCCACATGCGCCGTACCGCCCTTGAGGACGTTGAGCTG 
               
               
                 GGCGGTAAGACGATCCGTAAAGGAGACAAAGTCGTGATGTGGTACCTTAGTGGTAA 
               
               
                 CCGTGATGAGGCAGTCTTCCCAGACGCAGACCGCTTGATCATTGACCGCCCAAATGC 
               
               
                 ACGCCAGCATGTATCGTTTGGATTCGGCGTGCACCGTTGCATGGGCAACCGTTTAGC 
               
               
                 TGAAATGCAACTTCGTGTCTTGTGGGAGGAGATCATGAAACGCTTTCATACAGTCGA 
               
               
                 AGTTGTGGGGGAAGTTGAGCGCCTTAGCAACAACTTTATCCGTGGGATCGCGTCAGT 
               
               
                 CCCTGTGCGTTTGCACCCGTTATACTAA 
               
               
                   
               
               
                 CYP153_CPha1 from  Candidatus Phaeomarinobacter ectocarpi   
               
               
                 (protein) SEQ ID NO: 46 
               
               
                 MTTANQTSPNGAIDVNDIPLAELDVSQPHLFKNDTWRPWFARLRAEAPVHYLADSENG 
               
               
                 PFWSVTSHDMTKAVDANHKVFSSEEGGIAIVDPQPLDGEQLMRDPSFISMDEPKHATQR 
               
               
                 KAVSPAVAPKNLAELEPLIRERAADILDNLPVGETFNWVDRVSVELTARMLATLFDFPY 
               
               
                 ERRRDLIRWSDVATAVPKVTGEANDMGARRDALIECATTFYQLWQERAAQPPKFDFVS 
               
               
                 MLAHGEATKHLSEDPLLMLGNIILLIVGGNDTTRNSISGGVVALNQYPEEYQKLRDTPAL 
               
               
                 IPNMVAETVRWQTPVIHMRRTALEDVELGGKTIRKGDKVVMWYLSGNRDEAVFPDAD 
               
               
                 RLIIDRPNARQHVSFGFGVHRCMGNRLAEMQLRVLWEEIMKRFHTVEVVGEVERLSNN 
               
               
                 FIRGIASVPVRLHPLY. 
               
               
                   
               
               
                 CYP153_CPha2 from  Candidatus Phaeomarinobacter ectocarpi   
               
               
                 (DNA) SEQ ID NO: 47 
               
               
                 ATGTCGCAAGCTGCGGCAGAGACCCCTAGCACAGTCGATCATCAGGAGCGTGCATG 
               
               
                 GTCTATGCCTCTGGAAGATATCAACGTGGCTGACGGTGCACTTTTCCAAGACGATGC 
               
               
                 TATTTGGCCCTACTTTGAACGTCTTCGCAAGGAAGCACCGGTTCATAAGGGACATAG 
               
               
                 CGACGAGTTCGGTGACTATTGGAGTGTGACTCGTTATGAAGACATTATGGCGGTGGA 
               
               
                 CACCAATCATCATGTTTTCTCCTCGGAGGGGGCCATTACCCTTGCAGATCCGTTGGA 
               
               
                 AGATTTCCGTGCTCCAATGTTCATCGCAATGGATCCCCCGAAGCACGACAAACAGCG 
               
               
                 TATTACTGTCCAACCGATCGTCGCCCCAAAAAATCTGCAAAACTGGGAGGGCTTGAT 
               
               
                 CCGTGAGCGTACCGGCTTAATTCTGGATCAACTGCCCCGCAACGAGACGTTTGATTG 
               
               
                 GGTCGATAAAGTAAGCATTGAACTTACCACTATGATGCTTGCCACGTTATTCGATTT 
               
               
                 CCCTTTCGAGGAGCGCCGTCGCTTGACCCGTTGGTCTGATGTCGCCACAGGGCGTGA 
               
               
                 TAATCCCGAAATTTATAAAAGCGAAGAACAGTGGCGTGGGGAGCTTATGGAGTGTT 
               
               
                 TAGAGGCGTTCACTGGGTTATGGAACGACCGCGTTAACTCAGACACGCCCGGAAAC 
               
               
                 GATTTAATTTCGATGCTGGCGAGCGGGGAATCTACTAAGAATATGGATCCCATGGAG 
               
               
                 TATTTAGGCAACATTATTCTGCTTATTGTCGGGGGAAATGATACTACTCGCAACTCA 
               
               
                 ATGACGGGATCTGTTTACGCCTTAAACAAGTTTGCGGGCGAATATGATAAGTTAATT 
               
               
                 GCTGATCCTTCACTGATTCCCAATCTTTCGAGCGAGATCATTCGCTGGCAAACACCA 
               
               
                 TTGGCACATATGCGTCGTACTGCACTTGAAGACATTGAGCTGAACGGCCAGATGATC 
               
               
                 AAAAAAGGAGACAAAGTGGCCATGTGGTACGTATCCGGAAACCGCGACACGGCTGT 
               
               
                 GTTCGAGAACGCTGATGACGTAATTATTGACCGCCCCAATGCACGTCGCCAGATGTC 
               
               
                 CTTCGGGTATGGGATTCACCGCTGCGTTGGAAATCGCCTTGGTGAATTACAGATTAA 
               
               
                 GATCCTGTGGGAGGAACTGCTGAAGCGTTTTCCCAAAATCGAGGTCATGGAAGAAC 
               
               
                 CAACGCGCACACGTTCACCATTCGTCAAGGGATACACGTATATGCCCGTTCGTATTC 
               
               
                 CGGCCTACTAA 
               
               
                   
               
               
                 CYP153_CPha2 from  Candidatus Phaeomarinobacter ectocarpi   
               
               
                 (protein) SEQ ID NO: 48 
               
               
                 MSQAAAETPSTVDHQERAWSMPLEDINVADGALFQDDAIWPYFERLRKEAPVHKGHSD 
               
               
                 EFGDYWSVTRYEDIMAVDTNHHVFSSEGAITLADPLEDFRAPMFIAMDPPKHDKQRITV 
               
               
                 QPIVAPKNLQNWEGLIRERTGLILDQLPRNETFDWVDKVSIELTTMMLATLFDFPFEERR 
               
               
                 RLTRWSDVATGRDNPEIYKSEEQWRGELMECLEAFTGLWNDRVNSDTPGNDLISMLAS 
               
               
                 GESTKNMDPMEYLGNIILLIVGGNDTTRNSMTGSVYALNKFAGEYDKLIADPSLIPNLSS 
               
               
                 EIIRWQTPLAHMRRTALEDIELNGQMIKKGDKVAMWYVSGNRDTAVFENADDVIIDRP 
               
               
                 NARRQMSFGYGIHRCVGNRLGELQIKILWEELLKRFPKIEVMEEPTRTRSPFVKGYTYM 
               
               
                 PVRIPAY. 
               
               
                   
               
               
                 CamA from  Pseudomonas putida  ATCC 17453 (DNA) 
               
               
                 SEQ ID NO: 49 
               
               
                 ATGAACGCAAATGATAACGTCGTAATCGTCGGGACGGGACTTGCGGGGGTAGAAGT 
               
               
                 TGCATTTGGCTTACGCGCCAGTGGATGGGAGGGTAATATTCGCCTGGTTGGAGATGC 
               
               
                 GACTGTTATTCCACACCACTTGCCCCCGTTGAGCAAAGCGTACTTAGCCGGTAAGGC 
               
               
                 GACTGCAGAGTCATTATATTTACGTACTCCGGACGCCTATGCAGCACAAAACATCCA 
               
               
                 ATTGCTTGGAGGTACGCAGGTTACAGCGATTAATCGTGACCGTCAACAAGTCATCCT 
               
               
                 GTCTGATGGCCGTGCGTTGGACTATGACCGCTTAGTGCTGGCAACTGGTGGCCGCCC 
               
               
                 GCGCCCGCTTCCTGTGGCAAGTGGTGCTGTCGGGAAAGCGAATAATTTCCGCTATCT 
               
               
                 GCGTACTCTTGAAGACGCCGAGTGCATCCGCCGCCAGTTAATCGCCGATAATCGTCT 
               
               
                 GGTGGTTATTGGTGGAGGTTACATTGGTCTGGAAGTAGCCGCGACCGCAATCAAGG 
               
               
                 CGAACATGCATGTTACATTATTGGATACGGCCGCACGTGTGCTTGAACGCGTAACCG 
               
               
                 CCCCGCCAGTATCCGCATTCTATGAACACTTACATCGCGAGGCAGGGGTTGATATCC 
               
               
                 GTACTGGGACCCAGGTCTGTGGATTTGAAATGTCGACAGATCAGCAGAAAGTTACT 
               
               
                 GCGGTCTTGTGCGAAGACGGGACCCGCCTTCCGGCGGATCTTGTGATCGCAGGAATT 
               
               
                 GGTCTGATCCCCAATTGCGAATTAGCATCCGCAGCTGGCTTACAAGTGGATAACGGC 
               
               
                 ATCGTGATTAACGAACACATGCAGACGAGTGACCCTCTTATCATGGCGGTTGGCGAC 
               
               
                 TGTGCGCGCTTTCATAGCCAACTTTACGACCGTTGGGTGCGTATTGAGTCCGTACCC 
               
               
                 AACGCGCTGGAACAAGCTCGTAAGATCGCGGCTATTTTGTGCGGTAAAGTGCCTCGT 
               
               
                 GATGAAGCAGCTCCTTGGTTCTGGAGTGACCAATACGAGATTGGATTGAAGATGGT 
               
               
                 AGGATTATCAGAAGGCTACGATCGCATTATTGTCCGCGGCTCACTTGCTCAGCCCGA 
               
               
                 TTTCTCCGTCTTCTATCTTCAGGGAGATCGCGTGTTGGCTGTCGATACAGTTAATCGT 
               
               
                 CCTGTGGAATTCAATCAAAGCAAACAGATTATCACGGATCGTTTACCCGTAGAGCCT 
               
               
                 AACTTACTGGGCGACGAAAGCGTCCCACTTAAGGAGATCATTGCAGCCGCGAAGGC 
               
               
                 TGAGTTATCGAGTGCATAA 
               
               
                   
               
               
                 CamA from  Pseudomonas putida  ATCC 17453 (protein) 
               
               
                 SEQ ID NO: 50 
               
               
                 MNANDNVVIVGTGLAGVEVAFGLRASGWEGNIRLVGDATVIPHHLPPLSKAYLAGKAT 
               
               
                 AESLYLRTPDAYAAQNIQLLGGTQVTAINRDRQQVILSDGRALDYDRLVLATGGRPRPL 
               
               
                 PVASGAVGKANNFRYLRTLEDAECIRRQLIADNRLVVIGGGYIGLEVAATAIKANMHVT 
               
               
                 LLDTAARVLERVTAPPVSAFYEHLHREAGVDIRTGTQVCGFEMSTDQQKVTAVLCEDG 
               
               
                 TRLPADLVIAGIGLIPNCELASAAGLQVDNGIVINEHMQTSDPLIMAVGDCARFHSQLYD 
               
               
                 RWVRIESVPNALEQARKIAAILCGKVPRDEAAPWFWSDQYEIGLKMVGLSEGYDRIIVR 
               
               
                 GSLAQPDFSVFYLQGDRVLAVDTVNRPVEFNQSKQIITDRLPVEPNLLGDESVPLKEIIAA 
               
               
                 AKAELSSA. 
               
               
                   
               
               
                 CamB from  Pseudomonas putida  ATCC 17453 (DNA) 
               
               
                 SEQ ID NO: 51 
               
               
                 ATGTCTAAAGTTGTCTATGTCTCCCATGACGGAACCCGTCGTGAGTTAGACGTTGCT 
               
               
                 GATGGTGTGTCACTGATGCAAGCAGCGGTCAGCAATGGAATTTATGATATTGTGGGC 
               
               
                 GACTGTGGAGGTTCTGCCTCTTGCGCCACTTGTCATGTTTACGTAAACGAAGCGTTT 
               
               
                 ACGGATAAGGTCCCTGCCGCCAACGAACGTGAGATTGGTATGTTAGAGTGCGTTACC 
               
               
                 GCCGAGTTAAAGCCGAATTCGCGTTTGTGTTGTCAGATCATTATGACACCGGAGTTA 
               
               
                 GATGGCATTGTTGTCGATGTCCCTGACCGTCAATGGTAA 
               
               
                   
               
               
                 CamB from  Pseudomonas putida  ATCC 17453 (protein) 
               
               
                 SEQ ID NO: 52 
               
               
                 MSKVVYVSHDGTRRELDVADGVSLMQAAVSNGIYDIVGDCGGSASCATCHVYVNEAF 
               
               
                 TDKVPAANEREIGMLECVTAELKPNSRLCCQIIMTPELDGIVVDVPDRQW. 
               
               
                   
               
               
                 AlkB from  Pseudomonas putida  (DNA) SEQ ID NO: 53 
               
               
                 ATGCTTGAGAAACACAGAGTTCTGGATTCCGCTCCAGAGTACGTAGATAAAAAGAA 
               
               
                 ATATCTCTGGATACTATCAACTTTGTGGCCGGCTACTCCGATGATCGGAATCTGGCTT 
               
               
                 GCAAATGAAACTGGTTGGGGGATTTTTTATGGGCTGGTATTGCTCGTATGGTACGGC 
               
               
                 GCACTTCCATTGCTTGATGCGATGTTTGGTGAGGACTTTAATAATCCGCCTGAAGAA 
               
               
                 GTGGTGCCGAAACTAGAGAAGGAGCGGTACTATCGAGTTTTGACATATCTAACAGTT 
               
               
                 CCTATGCATTACGCTGCATTAATTGTGTCAGCATGGTGGGTCGGAACTCAGCCAATG 
               
               
                 TCTTGGCTTGAAATTGGTGCGCTTGCCTTGTCACTGGGTATCGTGAACGGACTAGCG 
               
               
                 CTCAATACAGGACACGAACTCGGTCACAAGAAGGAGACTTTTGATCGTTGGATGGC 
               
               
                 CAAAATTGTGTTGGCTGTCGTAGGGTACGGTCACTTCTTTATTGAGCATAATAAGGG 
               
               
                 TCATCACCGTGATGTCGCTACACCGATGGATCCTGCAACATCCCGGATGGGAGAAA 
               
               
                 GCATTTATAAGTTTTCAATCCGTGAGATCCCAGGAGCATTTATTCGTGCTTGGGGGC 
               
               
                 TTGAGGAACAACGCCTTTCGCGCCGTGGCCAAAGCGTTTGGAGTTTCGATAATGAAA 
               
               
                 TCCTCCAACCAATGATCATCACAGTTATTCTTTACGCCGTTCTCCTTGCCTTGTTTGG 
               
               
                 ACCTAAGATGCTGGTGTTCCTGCCGATTCAAATGGCTTTCGGTTGGTGGCAGCTGAC 
               
               
                 CAGTGCGAACTATATTGAACATTACGGCTTGCTCCGTCAAAAAATGGAGGACGGTC 
               
               
                 GATATGAGCATCAAAAGCCGCACCATTCTTGGAATAGTAATCACATCGTCTCTAATC 
               
               
                 TAGTGCTGTTCCACCTTCAGCGGCACTCGGATCACCACGCGCATCCAACACGTTCTT 
               
               
                 ATCAGTCACTTCGGGATTTTCCCGGCCTGCCGGCTCTTCCGACGGGTTACCCTGGTG 
               
               
                 CATTTTTGATGGCGATGATTCCTCAGTGGTTTAGATCAGTTATGGATCCCAAGGTAG 
               
               
                 TAGATTGGGCTGGTGGTGACCTTAATAAGATCCAAATTGATGATTCGATGCGAGAAA 
               
               
                 CCTATTTGAAAAAATTTGGCACTAGTAGTGCTGGTCATAGTTCGAGTACCTCTGCGG 
               
               
                 TAGCATCGTAG 
               
               
                   
               
               
                 AlkB from  Pseudomonas putida  (Protein) SEQ ID NO: 54 
               
               
                 MLEKHRVLDSAPEYVDKKKYLWILSTLWPATPMIGIWLANETGWGIFYGLVLLVWYG 
               
               
                 ALPLLDAMFGEDFNNPPEEVVPKLEKERYYRVLTYLTVPMHYAALIVSAWWVGTQPM 
               
               
                 SWLEIGALALSLGIVNGLALNTGHELGHKKETFDRWMAKIVLAVVGYGHFFIEHNKGH 
               
               
                 HRDVATPMDPATSRMGESIYKF SIREIPGAFIRAWGLEEQRLSRRGQSVWSFDNEILQPM 
               
               
                 IITVILYAVLLALFGPKMLVFLPIQMAFGWWQLTSANYIEHYGLLRQKMEDGRYEHQKP 
               
               
                 HHSWNSNHIVSNLVLFHLQRHSDHHAEIPTRSYQSLRDFPGLPALPTGYPGAFLMAMIPQ 
               
               
                 WFRSVMDPKVVDWAGGDLNKIQIDDSMRETYLKKFGTSSAGHSSSTSAVAS. 
               
               
                   
               
               
                 AlkG from  Pseudomonas putida  (DNA) SEQ ID NO: 55 
               
               
                 ATGGCTAGCTATAAATGCCCGGATTGTAATTATGTTTATGATGAGAGTGCGGGTAAT 
               
               
                 GTGCATGAGGGGTTTTCTCCAGGTACGCCTTGGCACCTTATTCCTGAGGATTGGTGC 
               
               
                 TGCCCCGATTGCGCCGTTCGAGACAAGCTTGACTTCATGTTAATTGAGAGCGGCGTA 
               
               
                 GGTGAAAAGGGCGTCACCTCAACCCATACTTCGCCAAATTTATCCGAGGTTAGTGGC 
               
               
                 ACAAGTTTAACTGCTGAAGCAGTGGTTGCGCCGACAAGCTTAGAGAAATTGCCTAGT 
               
               
                 GCCGACGTTAAAGGCCAAGATCTATATAAAACTCAACCTCCAAGGTCTGATGCCCA 
               
               
                 AGGCGGGAAAGCATACTTGAAGTGGATATGTATTACTTGTGGCCATATATATGATGA 
               
               
                 GGCGTTGGGCGATGAGGCCGAGGGTTTTACTCCAGGTACTCGCTTTGAGGATATTCC 
               
               
                 TGATGACTGGTGCTGTCCGGATTGCGGGGCTACGAAAGAAGACTATGTGCTCTACGA 
               
               
                 GGAAAAGTGA 
               
               
                   
               
               
                 AlkG from  Pseudomonas putida  (Protein) SEQ ID NO: 56 
               
               
                 MASYKCPDCNYVYDESAGNVHEGFSPGTPWHLIPEDWCCPDCAVRDKLDFMLIESGVG 
               
               
                 EKGVTSTHTSPNLSEVSGTSLTAEAVVAPTSLEKLPSADVKGQDLYKTQPPRSDAQGGK 
               
               
                 AYLKWICITCGHIYDEALGDEAEGFTPGTRFEDIPDDWCCPDCGATKEDYVLYEEK. 
               
               
                   
               
               
                 AlkT from  Pseudomonas putida  (DNA) SEQ ID NO: 57 
               
               
                 ATGGCAATCGTTGTTGTTGGCGCTGGTACAGCTGGAGTAAATGCTGCGTTCTGGCTT 
               
               
                 CGTCAATATGGTTATAAAGGGGAAATTAGGATTTTTAGCAGGGAGTCTGTGGCGCCT 
               
               
                 TATCAGCGGCCTCCTCTATCCAAGGCTTTTCTGACAAGTGAGATTGCAGAATCCGCA 
               
               
                 GTGCCATTAAAGCCAGAAGGTTTTTATACGAATAACAATATTACCATTTCGTTAAAT 
               
               
                 ACACCGATTGTATCAATCGACGTGGGGCGTAAGATAGTTTCTTCTAAAGATGGAAAA 
               
               
                 GAATACGCGTATGAAAAATTGATTCTTGCAACACCTGCTAGCGCACGTAGGTTAACC 
               
               
                 TGCGAGGGGTCTGAACTGTCTGGGGTCTGCTATTTACGCAGTATGGAAGACGCCAAA 
               
               
                 AATTTACGTAGGAAACTTGTGGAGAGTGCGTCTGTTGTTGTGTTGGGCGGCGGAGTA 
               
               
                 ATCGGGCTTGAAGTCGCCTCAGCTGCGGTGGGCTTAGGGAAGAGGGTCACAGTGAT 
               
               
                 AGAAGCCACCCCGCGTGTAATGGCGCGCGTGGTTACGCCGGCAGCAGCAAACTTAG 
               
               
                 TCAGAGCCCGCCTGGAGGCTGAAGGAATTGAGTTCAAGCTGAATGCGAAATTAACG 
               
               
                 TCTATAAAGGGCAGGAATGGCCATGTTGAACAATGCGTACTTGAAAGTGGAGAAGA 
               
               
                 AATTCAGGCGGATCTGATTGTAGTTGGAATCGGTGCTATCCCAGAGCTAGAGCTGGC 
               
               
                 AACTGAGGCGGCCCTTGAAGTGAGTAATGGTGTTGTGGTCGATGATCAGATGTGTAC 
               
               
                 ATCGGATACAAGTATATATGCAATCGGCGACTGCGCAATGGCTAGAAATCCTTTTTG 
               
               
                 GGGAACGATGGTACGTTTAGAGACAATTCATAATGCGGTTACACACGCTCAAATTGT 
               
               
                 CGCAAGTAGCATCTGTGGCACATCAACACCAGCACCAACCCCACCACGGTTCTGGTC 
               
               
                 TGATCTTAAAGGGATGGCGCTGCAAGGACTTGGTGCTCTAAAGGACTACGATAAAC 
               
               
                 TCGTTGTTGCAATTAATAACGAAACTCTTGAACTAGAAGTCCTTGCGTACAAGCAGG 
               
               
                 AGCGACTGATTGCAACTGAGACAATAAATTTGCCTAAACGTCAAGGTGCGCTTGCA 
               
               
                 GGGAGTATAAAATTACCTGATTAG 
               
               
                   
               
               
                 AlkT from  Pseudomonas putida  (Protein) SEQ ID NO: 58 
               
               
                 MAIVVVGAGTAGVNAAFWLRQYGYKGEIRIFSRESVAPYQRPPLSKAFLTSEIAESAVPL 
               
               
                 KPEGFYTNNNITISLNTPIVSIDVGRKIVSSKDGKEYAYEKLILATPASARRLTCEGSELSG 
               
               
                 VCYLRSMEDAKNLRRKLVESASVVVLGGGVIGLEVASAAVGLGKRVTVIEATPRVMAR 
               
               
                 VVTPAAANLVRARLEAEGIEFKLNAKLTSIKGRNGHVEQCVLESGEEIQADLIVVGIGAIP 
               
               
                 ELELATEAALEVSNGVVVDDQMCTSDTSIYAIGDCAMARNPFWGTMVRLETIHNAVTH 
               
               
                 AQIVASSICGTSTPAPTPPRFWSDLKGMALQGLGALKDYDKLVVAINNETLELEVLAYK 
               
               
                 QERLIATETINLPKRQGALAGSIKLPD. 
               
               
                   
               
               
                 Cyp102A7 from  Bacillus licheniformis  (DNA) SEQ ID NO: 59 
               
               
                 ATGAACAAGTTAGATGGAATTCCAATCCCTAAAACTTACGGGCCGCTCGGCAACCTG 
               
               
                 CCTTTGCTTGACAAAAACAGGGTCTCCCAGTCACTTTGGAAAATCGCGGATGAGATG 
               
               
                 GGGCCTATCTTTCAATTTAAGTTTGCGGATGCGATTGGGGTTTTTGTGTCCAGCCATG 
               
               
                 AACTGGTTAAAGAAGTCTCTGAAGAATCCCGTTTTGACAAAAACATGGGGAAGGGG 
               
               
                 CTATTGAAAGTTCGCGAGTTCAGCGGAGACGGGCTCTTTACAAGCTGGACGGAAGA 
               
               
                 ACCCAATTGGCGGAAAGCCCACAACATCCTTCTGCCGAGCTTCAGCCAGAAAGCGA 
               
               
                 TGAAGGGATACCATCCCATGATGCAGGATATCGCCGTCCAGCTCATTCAAAAGTGGT 
               
               
                 CCCGTCTCAATCAGGATGAAAGCATTGATGTGCCGGACGATATGACGCGGCTGACG 
               
               
                 CTGGACACGATCGGCTTATGCGGGTTTAACTACCGCTTTAACAGCTTCTACCGTGAA 
               
               
                 GGGCAGCATCCGTTTATTGAGAGCATGGTCCGGGGTTTGAGCGAAGCGATGAGACA 
               
               
                 GACGAAGCGCTTCCCGCTGCAGGATAAGCTGATGATTCAAACGAAGCGCCGGTTTA 
               
               
                 ACAGCGATGTCGAGTCGATGTTTTCTCTTGTTGACCGGATCATCGCTGACCGGAAGC 
               
               
                 AGGCCGAGAGTGAAAGCGGAAATGACCTCTTGTCGCTTATGCTTCATGCGAAAGAC 
               
               
                 CCTGAGACCGGCGAAAAACTGGATGATGAGAATATCCGCTATCAAATTATTACATTT 
               
               
                 TTGATTGCCGGACACGAGACGACGAGCGGTTTATTATCGTTTGCAATCTATCTGCTC 
               
               
                 CTGAAGCATCCGGATAAGCTTAAGAAAGCGTATGAAGAAGCAGACCGCGTGCTGAC 
               
               
                 CGATCCCGTCCCATCCTACAAACAGGTTCAGCAGCTGAAATACATCCGAATGATTTT 
               
               
                 GAATGAATCGATAAGGCTTTGGCCGACGGCACCGGCTTTCTCTCTTTATGCAAAAGA 
               
               
                 AGAAACGGTTATCGGGGGAAAATATTTGATTCCAAAAGGACAGAGCGTTACAGTGC 
               
               
                 TCATCCCAAAACTGCACAGAGATCAAAGCGTCTGGGGAGAAGATGCCGAGGCATTC 
               
               
                 CGGCCTGAACGGTTCGAGCAGATGGACAGCATTCCGGCGCACGCATACAAACCGTT 
               
               
                 TGGCAACGGCCAAAGGGCATGCATCGGCATGCAGTTCGCCCTTCATGAAGCGACGC 
               
               
                 TTGTGCTCGGCATGATTCTTCAGTACTTTGATCTTGAAGATCATGCAAACTACCAATT 
               
               
                 GAAGATCAAAGAATCGCTGACATTAAAACCGGATGGTTTCACAATCCGGGTGAGGC 
               
               
                 CGAGGAAAAAAGAAGCAATGACGGCGATGCCGGGCGCTCAGCCTGAAGAGAACGG 
               
               
                 ACGGCAGGAAGAACGGCCTTCCGCACCGGCGGCGGAAAATACGCACGGAACCCCTC 
               
               
                 TTCTTGTGCTCTACGGTTCAAATCTCGGCACAGCCGAAGAGATTGCGAAGGAGCTTG 
               
               
                 CTGAAGAAGCGCGTGAGCAAGGGTTTCACAGCCGGACGGCGGAGCTTGATCAATAC 
               
               
                 GCAGGCGCCATCCCGGCAGAAGGGGCTGTTATCATTGTGACGGCTTCCTATAACGGA 
               
               
                 AACCCGCCCGATTGCGCAAAGGAATTTGTCAATTGGCTTGAGCATGATCAGACAGA 
               
               
                 CGATTTGCGTGGTGTCAAATATGCGGTATTCGGCTGCGGTAACCGCAGCTGGGCCAG 
               
               
                 CACCTACCAGCGGATTCCGCGCCTGATTGACAGCGTATTGGAAAAAAAAGGCGCCC 
               
               
                 AAAGGCTGCACAAGCTTGGAGAAGGGGATGCAGGCGATGATTTTGAAGGACAGTTT 
               
               
                 GAGTCATGGAAATATGATCTGTGGCCGCTTTTAAGAACCGAATTTTCATTGGCCGAA 
               
               
                 CCCGAGCCGAATCAAACAGAAACAGACAGGCAAGCCTTATCTGTCGAGTTCGTAAA 
               
               
                 CGCACCTGCGGCTTCGCCGCTGGCTAAAGCTTATCAGGTGTTCACAGCGAAGATATC 
               
               
                 GGCAAACCGAGAACTGCAGTGTGAAAAGAGCGGGAGAAGCACAAGGCATATTGAA 
               
               
                 ATATCGCTTCCTGAAGGCGCCGCATATCAGGAGGGAGACCATCTCGGTGTGCTACCG 
               
               
                 CAAAAtAGCGAAGTGCTGATTGGCCGCGTTTTTCAGCGGTTTGGGCTGAACGGAAAT 
               
               
                 GAACAAATTCTGATTAGCGGCCGGAATCAAGCATCACATTTGCCTTTGGAGAGGCCC 
               
               
                 GTTCATGTCAAAGACCTTTTTCAACATTGCGTCGAGCTCCAGGAACCGGCCACAAGG 
               
               
                 GCCCAGATACGCGAGCTGGCGGCTCATACTGTTTGTCCGCCTCATCAGCGCGAGCTT 
               
               
                 GAAGACCTGCTGAAAGATGACGTCTATAAGGATCAAGTGTTGAATAAGCGGCTGAC 
               
               
                 AATGCTTGACCTGCTTGAGCAATACCCGGCCTGTGAACTGCCGTTCGCCCGTTTTCTG 
               
               
                 GCGCTTCTTCCTCCGCTAAAACCGAGGTACTATTCGATTTCCAGTTCGCCGCAGCTTA 
               
               
                 ACCCGCGGCAAACAAGCATCACCGTCTCTGTCGTAAGTGGCCCGGCGTTGAGCGGC 
               
               
                 CGCGGGCATTATAAGGGAGTTGCATCGAACTATCTCGCCGGCCTTGAGCCGGGAGA 
               
               
                 CGCGATTTCGTGTTTCATCAGAGAGCCTCAGTCAGGCTTCCGGCTTCCCGAAGATCC 
               
               
                 TGAAACACCGGTGATCATGGTCGGGCCGGGCACCGGAATCGCCCCTTACCGCGGAT 
               
               
                 TTCTTCAGGCGCGCCGCATCCAGCGCGATGCCGGTGTGAAGCTCGGTGAAGCGCATT 
               
               
                 TGTACTTCGGCTGCCGCCGTCCGAACGAAGATTTTCTGTATCGAGACGAGTTGGAGC 
               
               
                 AAGCGGAAAAGGACGGAATCGTCCATCTGCATACAGCGTTTTCCCGGCTTGAGGGC 
               
               
                 CGGCCGAAAACATATGTGCAAGATTTGCTCAGAGAGGATGCAGCCTTGCTGATTCAC 
               
               
                 TTGTTGAACGAAGGCGGCCGCCTGTATGTGTGCGGAGACGGAAGCCGCATGGCTCC 
               
               
                 AGCTGTTGAACAAGCTTTGTGCGAGGCGTATCGCATAGTACAGGGTGCGAGTCGGG 
               
               
                 AAGAGTCGCAAAGCTGGCTGTCCGCACTTTTAGAAGAAGGGCGCTATGCAAAGGAT 
               
               
                 GTATGGGACGGCGGCGTTTCCCAACATAATGTGAAGGCGGACTGCATTGCAAGAAC 
               
               
                 GTAA 
               
               
                   
               
               
                 Cyp102A7 from  Bacillus licheniformis  (Protein) SEQ ID NO: 60 
               
               
                 MNKLDGIPIPKTYGPLGNLPLLDKNRVSQSLWKIADEMGPIFQFKFADAIGVFVSSHELV 
               
               
                 KEVSEESRFDKNMGKGLLKVREFSGDGLFTSWTEEPNWRKAHNILLPSFSQKAMKGYH 
               
               
                 PMMQDIAVQLIQKWSRLNQDESIDVPDDMTRLTLDTIGLCGFNYRFNSFYREGQHPFIES 
               
               
                 MVRGLSEAMRQTKRFPLQDKLMIQTKRRFNSDVESMFSLVDRIIADRKQAESESGNDLL 
               
               
                 SLMLHAKDPETGEKLDDENIRYQIITFLIAGHETTSGLLSFAIYLLLKHPDKLKKAYEEAD 
               
               
                 RVLTDPVPSYKQVQQLKYIRMILNESIRLWPTAPAFSLYAKEETVIGGKYLIPKGQSVTV 
               
               
                 LIPKLHRDQSVWGEDAEAFRPERFEQMDSIPAHAYKPFGNGQRACIGMQFALHEATLVL 
               
               
                 GMILQYFDLEDHANYQLKIKESLTLKPDGFTIRVRPRKKEAMTAMPGAQPEENGRQEER 
               
               
                 PSAPAAENTHGTPLLVLYGSNLGTAEEIAKELAEEAREQGFHSRTAELDQYAGAIPAEGA 
               
               
                 VIIVTASYNGNPPDCAKEFVNWLEHDQTDDLRGVKYAVFGCGNRSWASTYQRIPRLIDS 
               
               
                 VLEKKGAQRLHKLGEGDAGDDFEGQFESWKYDLWPLLRTEFSLAEPEPNQTETDRQAL 
               
               
                 SVEFVNAPAASPLAKAYQVFTAKISANRELQCEKSGRSTRHIEISLPEGAAYQEGDHLGV 
               
               
                 LPQNSEVLIGRVFQRFGLNGNEQILISGRNQASHLPLERPVHVKDLFQHCVELQEPATRA 
               
               
                 QIRELAAHTVCPPHQRELEDLLKDDVYKDQVLNKRLTMLDLLEQYPACELPFARFLALL 
               
               
                 PPLKPRYYSISSSPQLNPRQTSITVSVVSGPALSGRGHYKGVASNYLAGLEPGDAISCFIRE 
               
               
                 PQSGFRLPEDPETPVIMVGPGTGIAPYRGFLQARRIQRDAGVKLGEAHLYFGCRRPNEDF 
               
               
                 LYRDELEQAEKDGIVHLHTAFSRLEGRPKTYVQDLLREDAALLIHLLNEGGRLYVCGDG 
               
               
                 SRMAPAVEQALCEAYRIVQGASREESQSWLSALLEEGRYAKDVWDGGVSQHNVKADC 
               
               
                 IART. 
               
               
                   
               
               
                 OhyA1 from  Stenotrophomonas maltophilia  ATCC17679 (DNA) 
               
               
                 SEQ ID NO: 61 
               
               
                 ATGTACTACAGCAGTGGCAACTACGAAGCCTTTGCGCGCCCGCGCAAGCCCGCCGG 
               
               
                 TGTCGATGACAAGCGCGCATGGTTCGTCGGTTCGGGCCTGGCCTCGCTGGCCGGCGC 
               
               
                 CGCGTTCCTGGTGCGCGACGGCCGCATGGCCGGTGAGCGCATCACCATTCTCGAGCA 
               
               
                 GCAGCGGATTGCCGGAGGCGCGCTGGATGGCCTGAAGGTGCCTGAAAAGGGCTTCG 
               
               
                 TGATCCGCGGTGGACGCGAGATGGAAGACCACTTCGAGTGTCTGTGGGATCTGTTCC 
               
               
                 GCTCGATTCCGTCGCTGGAGATTGAAGATGCCAGCGTGCTGGACGAGTTCTACTGGC 
               
               
                 TGAACAAGGACGACCCCAACTATTCGCTGCAGCGTGCCACGATCAATCGCGGTGAG 
               
               
                 GATGCGCACACCGACGGCCTGTTCACCCTGACCGAGCAGGCGCAGAAGGACATCAT 
               
               
                 CGCGCTGTTCCTGGCCACCCGGCAGGAGATGGAGAACAAGCGCATCGACGAGGTGC 
               
               
                 TGGGCCGCGACTTCCTGGACAGCAACTTCTGGCTGTACTGGCGCACCATGTTCGCCT 
               
               
                 TCGAGGAATGGCATTCGGCGCTGGAGATGAAGCTGTACCTGCATCGCTTCATCCACC 
               
               
                 ATATCGGCGGCCTGCCGGATTTCTCGGCGCTGAAGTTCACCAAGTACAACCAGTACG 
               
               
                 AATCGCTGGTGCTGCCGCTGGTGAAGTGGCTGCAGGACCACGGCGTGGTGTTCCAGT 
               
               
                 ACGGCACCGAGGTGACCGACGTCGACTTCGATCTGGCGGCCGGCCGCAAGCAGGCC 
               
               
                 ACGCGCATCCACTGGACGCGTGACGGTGTAGCCGGTGGCGTGGATCTGAGCGCGGA 
               
               
                 TGACCTTGTGTTCATGACGATCGGTTCGTTGACCGAGAACTCGGACAACGGCGACCA 
               
               
                 CCGCACGGCTGCGCGTTTGAATGAAGGCGCGGCGCCGGCCTGGGACCTGTGGCGAC 
               
               
                 GTATTGCCGCCAGGGATCCTGCGTTCGGGCGCCCGGATGTGTTTGGCGCGCATATCC 
               
               
                 CGCAGACCAAGTGGGAATCGGCGACGGTGACCACGCTGGATGCACGCATTCCGGCC 
               
               
                 TACATCCAGAAGATCGCCAAGCGCGACCCGTTCAGTGGCAAGGTGGTGACCGGCGG 
               
               
                 CATCGTCAGTGTGCGTGACTCGCGCTGGTTGATGAGCTGGACGGTGAACCGCCAGCC 
               
               
                 GCATTTCAAGAACCAGCCCAAGGATCAGATCGTGGTCTGGGTGTATTCGCTGTTCGT 
               
               
                 GGATACGCCTGGAGACTACGTGAAGAAGCCGATGCAGGATTGCACCGGCGAGGAGA 
               
               
                 TCACCCGTGAGTGGCTGTACCACCTGGGCGTGCCGGTGGAAGAAATCGACGAATTG 
               
               
                 GCCGCGACCGGCGCGAAAACGGTGCCGGTGATGATGCCGTACATCACCGCGTTCTT 
               
               
                 CATGCCACGCCAGGCCGGTGATCGCCCGGACGTGGTGCCGGAGGGTGCGGTGAACT 
               
               
                 TCGCCTTCATCGGCCAGTTTGCCGAATCGAAGCAGCGCGACTGCATCTTCACCACCG 
               
               
                 AGTATTCGGTGCGCACACCGATGGAAGCGGTGTATACCCTGCTGGGCATCGAGCGC 
               
               
                 GGCGTGCCGGAGGTGTTCAATTCCACCTATGACGTGCGCTCGTTGCTGGCGGCGACC 
               
               
                 GGTCGCCTGCGCGATGGCAGGGAACTGGATATTCCCGGCCCGGCGTTCCTGCGCAA 
               
               
                 CCTGCTGATGAACAAGCTGGACAAGACCCAGATCGGTGGCCTCCTGCGCGAGTTCA 
               
               
                 AGCTGGTGCAGGAGGACTGA 
               
               
                   
               
               
                 OhyA1 from  Stenotrophomonas maltophilia  ATCC17679 (Protein) 
               
               
                 SEQ ID NO: 62 
               
               
                 MYYSSGNYEAFARPRKPAGVDDKRAWFVGSGLASLAGAAFLVRDGRMAGERITILEQQ 
               
               
                 RIAGGALDGLKVPEKGFVIRGGREMEDHFECLWDLFRSIPSLEIEDASVLDEFYWLNKD 
               
               
                 DPNYSLQRATINRGEDAHTDGLFTLTEQAQKDIIALFLATRQEMENKRIDEVLGRDFLDS 
               
               
                 NFWLYWRTMFAFEEWHSALEMKLYLHRFIHHIGGLPDFSALKFTKYNQYESLVLPLVK 
               
               
                 WLQDHGVVFQYGTEVTDVDFDLAAGRKQATRIHWTRDGVAGGVDLSADDLVFMTIGS 
               
               
                 LTENSDNGDHRTAARLNEGAAPAWDLWRRIAARDPAFGRPDVFGAHIPQTKWESATVT 
               
               
                 TLDARIPAYIQKIAKRDPFSGKVVTGGIVSVRDSRWLMSWTVNRQPHFKNQPKDQIVV 
               
               
                 WVYSLFVDTPGDYVKKPMQDCTGEEITREWLYHLGVPVEEIDELAATGAKTVPVMMP 
               
               
                 YITAFFMPRQAGDRPDVVPEGAVNFAFIGQFAESKQRDCIFTTEYSVRTPMEAVYTLLGI 
               
               
                 ERGVPEVFNSTYDVRSLLAATGRLRDGRELDIPGPAFLRNLLMNKLDKTQIGGLLREFK 
               
               
                 LVQED. 
               
               
                   
               
               
                 OhyA2 from  Stenotrophomonas maltophilia  S208 (DNA) 
               
               
                 SEQ ID NO: 63 
               
               
                 ATGAGCCAGCCCACCGCACCGGGACGCAACGCAGGGGCCACGCCGGCCTTCGAGCA 
               
               
                 CGAGCCGGACAGCACCGGCGGCTACTGGTCCAACCGGCCGGAGAACACACTGCCAC 
               
               
                 CGCCGGACATGATGGGGGCCTACATGCGCAACCGGCCGCTGCCGCCGGAGGACGTG 
               
               
                 GCGCAGCGCAAGGCCTACATCATCGGCACCGGCATCGCCGGGTTGGCGGCGGCGTT 
               
               
                 CTACCTGATCCGCGACGGCGGCATGCCGCCGGCCAACATCACGCTGCTGGACAGCC 
               
               
                 TGGAGATCGAAGGCGGTTCGCTGGATGGCGCGGGGGATGCCGAGCAGGGCTACCTG 
               
               
                 ATCCGCGGCGGCCGCGAGATGAACTGGAACTACGACAATTTCTGGGACCTGTTCCA 
               
               
                 GGATGTGCCGGCACTCGAACTGCCGGCCGGCTTCAGCGTGCTCGACGAGTACCGCG 
               
               
                 CCGTCAACGACAACGATCCGAACTGGTCCAAGGCGCGGCTGCTGCACCAGCAGGGC 
               
               
                 AAGGTCAAGGATTTCGCCACGTTCGGGTTGAGCCGCGGCCAGCAATGGGAGCTGGT 
               
               
                 CAAGCTGCTGCTCAAGCGCAAGGAAGACCTGGACGACGTCACCATCGAGGACTACT 
               
               
                 TCAGCGAAGGCTTTCTGCAGAGCAACTTCTGGTTCTTCTGGCGCTCGATGTTCGCCTT 
               
               
                 CGAGAACTGGCAGAGCCTGCTCGAGATGAAGCTGTACATGCATCGGTTCCTGGATG 
               
               
                 CCATCGACGGTCTGAACGACATGTCCGCGCTGGTGTTTCCCAAGTACAACCAATACG 
               
               
                 AGAGTTTTGTGGTGCCGCTGTCGCGGATGCTGCGCGCGCAGGGCGTCAACGTGCAGT 
               
               
                 TCGATACCCGCGTCCACGACCTGGAGATGGCGGTGGACGGGCAGTCACGCACCGTC 
               
               
                 ACCGCGCTGCGCTGCCGGGTGGCCGGCAACGAGACCACGCTGCCGGTTGCGGCGGG 
               
               
                 CGACCTGGTGTTCGCGCTCACCGGTTCGATGACCGAAGGCACGGCGTACGGCGACA 
               
               
                 TGGACACCGTGCCGCCGCTGGCGCGCGACCGCCGGGACCCGGGCGAGGACAGTGAC 
               
               
                 TGGGCGCTGTGGCGCAATCTCGCGCGGCAGTCGCCGATCTTCGGCAAGCCGGAGAA 
               
               
                 GTTCTACGGCGACGTGGACCGCTCGATGTGGGAGTCGGCCACGTTGACCTGCCGCCC 
               
               
                 CTCGCCGCTGGTGGACAAGATCCGCACGTTGTCGGTCAACGATCCGTACTCCGGGCG 
               
               
                 CACCGTGACCGGTGGGGTCATCACCATCACCGATTCCAACTGGGTGCTCAGCTTCAC 
               
               
                 CGTCAACCGCCAGCCGCATTTCGTGGACCAGCCCAAGGACGTGCTGGTGGTATGGG 
               
               
                 TCTATGCCCTGTTGATGGATCAGGACGGCAACCACATCAAAAAGCCGATGCCGGCG 
               
               
                 TGTACCGGACGCGAGGTGCTGGCCGAACTGTGCCACCACCTGGGCATCGGCGACCA 
               
               
                 GATCGATGCGGTGGCCGCCGCGACCAGGGTGCGGCTGGCGTTGATGCCGTACATCA 
               
               
                 CCGCGCAGTTCATGCCGCGTGCCGCTGGCGACCGTCCGCACGTGGTACCGGCCGGCT 
               
               
                 GCACCAACCTGGGCCTGCTCGGCCAGTTCGTGGAAACGCGCAACGATGTGATCTTCA 
               
               
                 CGATGGAAAGCTCGATCCGCACGGCGCGTGTGGCGGTGTACACCCTGCTGGGGCTG 
               
               
                 CGCAAGCAGGTACCGGACCTGAGCCCGACCCAGTACGACATCCGCAATCTGATCAA 
               
               
                 AGCGGCACGGGCGTTGAACAACAACGCGCCGTTCCCCGGCGAACGGCTGCTGCACC 
               
               
                 GTCTGCTCGGCAACAGTTATTACGCCCACATCCTGCCGCCGCTGCCACAGCCTGAAA 
               
               
                 AGGGCCGGGAGGCCTTCCTTGAAGAGGAGCTGTCGTGGTTGTCAGGCAAGGGCAGC 
               
               
                 GTGGTGCTGAAGGACCTGTCTGCACGGCTGGATCGGCTTGGCGAAACGCTGGGCAG 
               
               
                 GCGGCGCGCGCCCTGA 
               
               
                   
               
               
                 OhyA2 from  Stenotrophomonas maltophilia  S208 (Protein) 
               
               
                 SEQ ID NO: 64 
               
               
                 MSQPTAPGRNAGATPAFEHEPDSTGGYWSNRPENTLPPPDMMGAYMRNRPLPPEDVAQ 
               
               
                 RKAYIIGTGIAGLAAAFYLIRDGGMPPANITLLDSLEIEGGSLDGAGDAEQGYLIRGGRE 
               
               
                 MNWNYDNFWDLFQDVPALELPAGFSVLDEYRAVNDNDPNWSKARLLHQQGKVKDFA 
               
               
                 TFGLSRGQQWELVKLLLKRKEDLDDVTIEDYFSEGFLQSNFWFFWRSMFAFENWQSLL 
               
               
                 EMKLYMHRFLDAIDGLNDMSALVFPKYNQYESFVVPLSRMLRAQGVNVQFDTRVHDL 
               
               
                 EMAVDGQSRTVTALRCRVAGNETTLPVAAGDLVFALTGSMTEGTAYGDMDTVPPLAR 
               
               
                 DRRDPGEDSDWALWRNLARQSPIFGKPEKFYGDVDRSMWESATLTCRPSPLVDKIRTLS 
               
               
                 VNDPYSGRTVTGGVITITDSNWVLSFTVNRQPHFVDQPKDVLVVWVYALLMDQDGNHI 
               
               
                 KKPMPACTGREVLAELCHHLGIGDQIDAVAAATRVRLALMPYITAQFMPRAAGDRPHV 
               
               
                 VPAGCTNLGLLGQFVETRNDVIFTMESSIRTARVAVYTLLGLRKQVPDLSPTQYDIRNLI 
               
               
                 KAARALNNNAPFPGERLLHRLLGNSYYAHILPPLPQPEKGREAFLEEELSWLSGKGSVV 
               
               
                 LKDLSARLDRLGETLGRRRAP.