atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   3 RIAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADTGATPSVLDVENSTTaeIAGALKGHDAVVWSAGAGGGNP 82
Cdd:cd05243    1 KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAGAEVVVGDLTDAES--LAAALEGIDAVISAAGSGGKGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  83 ARTYAVDRDAAIRSMDAAAQAGVNRYVMVSYLGARRDHGVPAdhGFFPYAEAKAAADEYLRGTGLAWTILGPGGLTDKP- 161
Cdd:cd05243   79 PRTEAVDYDGNINLIDAAKKAGVKRFVLVSSIGADKPSHPLE--ALGPYLDAKRKAEDYLRASGLDYTIVRPGGLTDDPa 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 323470308 162 GTGMITVSPaEGDR---STSRSNTAIVAAAVLDLPQTAGKTIEFCDG 205
Cdd:cd05243  157 GTGRVVLGG-DGTRldgPISRADVAEVLAEALDTPAAIGKTFELGGG 202

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   3 RIAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADTGATPSVLDVENSTTaeIAGALKGHDAVVWSAGAGGGNP 82
Cdd:cd05243    1 KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAGAEVVVGDLTDAES--LAAALEGIDAVISAAGSGGKGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  83 ARTYAVDRDAAIRSMDAAAQAGVNRYVMVSYLGARRDHGVPAdhGFFPYAEAKAAADEYLRGTGLAWTILGPGGLTDKP- 161
Cdd:cd05243   79 PRTEAVDYDGNINLIDAAKKAGVKRFVLVSSIGADKPSHPLE--ALGPYLDAKRKAEDYLRASGLDYTIVRPGGLTDDPa 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 323470308 162 GTGMITVSPaEGDR---STSRSNTAIVAAAVLDLPQTAGKTIEFCDG 205
Cdd:cd05243  157 GTGRVVLGG-DGTRldgPISRADVAEVLAEALDTPAAIGKTFELGGG 202

Putative NADH-flavin reductase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   3 RIAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADtGATPSVLDVENstTAEIAGALKGHDAVVWSAGAGGGNP 82
Cdd:COG2910    1 KIAVIGATGRVGSLIVREALARGHEVTALVRNPEKLPDEHP-GLTVVVGDVLD--PAAVAEALAGADAVVSALGAGGGNP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  83 artYAVDRDAAIRSMDAAAQAGVNRYVMVSYLGARRDHGVPA------DHGFFPYAEAKAAADEYLRGTGLAWTILGPGG 156
Cdd:COG2910   78 ---TTVLSDGARALIDAMKAAGVKRLIVVGGAGSLDVAPGLGldtpgfPAALKPAAAAKAAAEELLRASDLDWTIVRPAA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 323470308 157 LTDKPGTGMITVS---PAEGDRSTSRSNTAIVAAAVLDLPQTAGKTIEFCD 204
Cdd:COG2910  155 LTDGERTGRYRLGgdgLLVDASSISRADVAVALLDELEDPAHIRQRFTVAY 205

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   3 RIAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADTGATPSVLDVENSTTaeIAGALKGHDAVVWSAGAGGGNP 82
Cdd:cd05243    1 KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAGAEVVVGDLTDAES--LAAALEGIDAVISAAGSGGKGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  83 ARTYAVDRDAAIRSMDAAAQAGVNRYVMVSYLGARRDHGVPAdhGFFPYAEAKAAADEYLRGTGLAWTILGPGGLTDKP- 161
Cdd:cd05243   79 PRTEAVDYDGNINLIDAAKKAGVKRFVLVSSIGADKPSHPLE--ALGPYLDAKRKAEDYLRASGLDYTIVRPGGLTDDPa 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 323470308 162 GTGMITVSPaEGDR---STSRSNTAIVAAAVLDLPQTAGKTIEFCDG 205
Cdd:cd05243  157 GTGRVVLGG-DGTRldgPISRADVAEVLAEALDTPAAIGKTFELGGG 202

Putative NADH-flavin reductase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   3 RIAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADtGATPSVLDVENstTAEIAGALKGHDAVVWSAGAGGGNP 82
Cdd:COG2910    1 KIAVIGATGRVGSLIVREALARGHEVTALVRNPEKLPDEHP-GLTVVVGDVLD--PAAVAEALAGADAVVSALGAGGGNP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  83 artYAVDRDAAIRSMDAAAQAGVNRYVMVSYLGARRDHGVPA------DHGFFPYAEAKAAADEYLRGTGLAWTILGPGG 156
Cdd:COG2910   78 ---TTVLSDGARALIDAMKAAGVKRLIVVGGAGSLDVAPGLGldtpgfPAALKPAAAAKAAAEELLRASDLDWTIVRPAA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 323470308 157 LTDKPGTGMITVS---PAEGDRSTSRSNTAIVAAAVLDLPQTAGKTIEFCD 204
Cdd:COG2910  155 LTDGERTGRYRLGgdgLLVDASSISRADVAVALLDELEDPAHIRQRFTVAY 205

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   3 RIAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVaDTGATPSVLDVENSTtaEIAGALKGHDAVVWSAGAGGGNP 82
Cdd:cd05244    1 KIAIIGATGRTGSAIVREALARGHEVTALVRDPAKLPAE-HEKLKVVQGDVLDLE--DVKEALEGQDAVISALGTRNDLS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  83 ARTYAVDRDAAIrsMDAAAQAGVNRYVMVS--YLGARRDHGVPA-DHGFFPYAEAKAAADEY-----LRGTGLAWTILGP 154
Cdd:cd05244   78 PTTLHSEGTRNI--VSAMKAAGVKRLIVVGgaGSLDDRPKVTLVlDTLLFPPALRRVAEDHArmlkvLRESGLDWTAVRP 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 323470308 155 GGLTDKPGTG-MITVSPAEGDRSTSRSNTAIVAAAVLD 191
Cdd:cd05244  156 PALFDGGATGgYYRVELLVDAKGGSRISRADLAIFMLD 193

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   4 IAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADTGATPSVLDVENSttAEIAGALKGHDAVVWSAGAGGGNPA 83
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEPVAVVEGDLRDL--DSLSDAVQGVDVVIHLAGAPRDTRD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  84 RTyAVDRDAAIRSMDAAAQAGVNRYVMVSYLGA-RRDHGVPADHGFFPYAEAKAAADEYLRGTGLAWTILGPGGLTDKPG 162
Cdd:cd05226   79 FC-EVDVEGTRNVLEAAKEAGVKHFIFISSLGAyGDLHEETEPSPSSPYLAVKAKTEAVLREASLPYTIVRPGVIYGDLA 157

                 ....*.
gi 323470308 163 TGMITV 168
Cdd:cd05226  158 RAIANA 163

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   3 RIAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADTGATPSVL----DVENSTTaeIAGALKGHDAVVWSAGAG 78
Cdd:cd05271    2 VVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEAYARRLLVMGDLGQVLfvefDLRDDES--IRKALEGSDVVINLVGRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  79 GGNPARTY-AVDRDAAIRSMDAAAQAGVNRYVMVSYLGArrdhgvpADHGFFPYAEAKAAADEYLRGTGLAWTILGPG-- 155
Cdd:cd05271   80 YETKNFSFeDVHVEGPERLAKAAKEAGVERLIHISALGA-------DANSPSKYLRSKAEGEEAVREAFPEATIVRPSvv 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308 156 -GLTDKPGTGMITVS------PAEGDRSTSRSNTAI--VAAAV---LDLPQTAGKTIEFC 203
Cdd:cd05271  153 fGREDRFLNRFAKLLaflpfpPLIGGGQTKFQPVYVgdVAEAIaraLKDPETEGKTYELV 212

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   3 RIAIIGGHGKVALH-LSALLTEEGHSVTSFIRnPDHAQDVADTGATPSVLDVENSTTAEIAGALKGHDAVVwSAgAGGGN 81
Cdd:cd05259    1 KIAIAGATGTLGGPiVSALLASPGFTVTVLTR-PSSTSSNEFQPSGVKVVPVDYASHESLVAALKGVDAVI-SA-LGGAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  82 PARtyavdrdaAIRSMDAAAQAGVNRYvMVSYLGArrDHGVPADHGFFPYAEAKAAADEYLR--GTGLAWTILGPGGLTD 159
Cdd:cd05259   78 IGD--------QLKLIDAAIAAGVKRF-IPSEFGV--DYDRIGALPLLDLFDEKRDVRRYLRakNAGLPWTYVSTGMFLD 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 323470308 160 KPGTGMITVSPAEGDR-------------STSRSNTAIVAAAVLDLPQTAGKTI 200
Cdd:cd05259  147 YLLEPLFGVVDLANRTatiygdgetkfafTTLEDIGRAVARALTHPDRTLNRVV 200

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308    4 IAIIGGHGKVALHLSALLTEEGHSVTSFIRNP--DHAQDVADTGATPSVLDVENSttAEIAGALKGHDAVVWSAGAGGGN 81
Cdd:pfam05368   1 ILVFGATGQQGGSVVRASLKAGHKVRALVRDPksELAKSLKEAGVELVKGDLDDK--ESLVEALKGVDVVFSVTGFWAGK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323470308   82 partyAVDRDAAIrsMDAAAQAGVNRYVMVSYLGA-RRDHGVPADHGFFpyaEAKAAADEYLRGTGLAWTILGPG 155
Cdd:pfam05368  79 -----EIEDGKKL--ADAAKEAGVKHFIPSSFGNDnDISNGVEPAVPHF---DSKAEIERYIRALGIPYTFVYAG 143

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   4 IAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADTGATpSVLDVENSTTAEIAGALKGHDAV---VWSAGAGGG 80
Cdd:cd05245    1 VLVTGATGYVGGRLVPRLLQEGHQVRALVRSPEKLADRPWSERV-TVVRGDLEDPESLRAALEGIDTAyylVHSMGSGGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  81 NPARtyavDRDAAIRSMDAAAQAGVNRYVMVSYLGarrdhgvPADHGFFPYAEAKAAADEYLRGTGL------AWTILGP 154
Cdd:cd05245   80 FEEA----DRRAARNFARAARAAGVKRIIYLGGLI-------PKGEELSPHLRSRAEVGEILRAGGVpvtelrAAVIIGS 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323470308 155 GG--------LTDK-PgtgmITVSPaegdrSTSRSNTAIVA--------AAVLDLPQTAGKTIE 201
Cdd:cd05245  149 GSasfemvryLVERlP----VMITP-----RWVNTPCQPIAirdvleylVAALDRPATAGETFE 203

atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only a partial match to a prototypical glycine-rich NAD(P)-binding motif consensus, GXXG, which conserves part of the motif of extended SDR. Furthermore, they lack the characteristic active site residues of the SDRs. This subgroup is related to phenylcoumaran benzylic ether reductase, an NADPH-dependent aromatic alcohol reductase. One member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   2 TRIAIIGGHGKVALHLSALLTEEGH-SVTSFIRNPDHAQDVADTGATPSVLDVENSttAEIAGALKGHDaVVWSAGAGGG 80
Cdd:cd05267    1 KKVLILGANGEIAREATTMLLENSNvELTLFLRNAHRLLHLKSARVTVVEGDALNS--DDLKAAMRGQD-VVYANLGGTD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308  81 NPARTYAVdrdaaIRSMDAAaqaGVNRYVMVSYLGARRDhgVPADHGFF-------PYAEAKAAADeYLRGTGLAWTILG 153
Cdd:cd05267   78 LDQQAENV-----VQAMKAV---GVKRLIWTTSLGIYDE--VPGKFGEWnkefignYLAPYRKSAA-VIENSDLDYTLLR 146

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 323470308 154 PGGLTDKPGTGMITVSPAEGDRSTSRSNTAiVAAAVLDL 192
Cdd:cd05267  147 PAWLTNNDEIDYELTPKGEAFKGTEVSRKS-VADLITDI 184

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   4 IAIIGGHGKVALHLSALLTEEGHSVTsfirnpdhaqdvadtgatpsVLDVensttaeiagalkgHDAVVWSAGAGGG--- 80
Cdd:cd08946    1 ILVTGGAGFIGSHLVRRLLERGHEVV--------------------VIDR--------------LDVVVHLAALVGVpas 46

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323470308  81 --NPARTYAVDRDAAIRSMDAAAQAGVNRYVMVS----YLGArrDHGVPADH----GFFPYAEAKAAADEYLR 143
Cdd:cd08946   47 wdNPDEDFETNVVGTLNLLEAARKAGVKRFVYASsasvYGSP--EGLPEEEEtpprPLSPYGVSKLAAEHLLR 117

translocon at the inner envelope of chloroplast subunit 62; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 323470308  86 YAVDRDAAIRSMDAAAQAGVNRYVMVSYLGARRdHGVPAD--HGFFPYAEAKAAADEYLRGTGLAWTILGPGGL 157
Cdd:PLN03209 181 YRIDYLATKNLVDAATVAKVNHFILVTSLGTNK-VGFPAAilNLFWGVLCWKRKAEEALIASGLPYTIVRPGGM 253

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323470308   3 RIAIIGGHGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADtgatPSVLDVENSTTAEIAGAlkghDAVVWSAGA 77
Cdd:cd05242    1 KIVITGGTGFIGRALTRRLTAAGHEVVVLSRRPGKAEGLAE----VITWDGLSLGPWELPGA----DAVINLAGE 67

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   6 IIGGHGKVALHLS-ALLTEEGHSVTSFirnpdhaqDVADTGATPSVLDVEN--------STTAEIAGALKGHDAVVWSAG 76
Cdd:cd05241    4 VTGGSGFFGERLVkQLLERGGTYVRSF--------DIAPPGEALSAWQHPNieflkgdiTDRNDVEQALSGADCVFHTAA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323470308  77 A-GGGNPARTY-AVDRDAAIRSMDAAAQAGVNRYVMVSYLGARRDHGVPA---------DHGFFPYAEAKAAADE 140
Cdd:cd05241   76 IvPLAGPRDLYwEVNVGGTQNVLDACQRCGVQKFVYTSSSSVIFGGQNIHngdetlpypPLDSDMYAETKAIAEI 150

cinnamoyl-CoA reductase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323470308   4 IAIIGGHGKVALHLSALLTEEGHSVTSFIRNPD-----HAQDVADTGATPSVLDVENSTTAEIAGALKGHDAVVWSAGAG 78
Cdd:PLN02214  13 VCVTGAGGYIASWIVKILLERGYTVKGTVRNPDdpkntHLRELEGGKERLILCKADLQDYEALKAAIDGCDGVFHTASPV 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 323470308  79 GGNPARTYAVDRDAAIRSMDAAAQAGVNRYVMVSYLGA 116
Cdd:PLN02214  93 TDDPEQMVEPAVNGAKFVINAAAEAKVKRVVITSSIGA 130

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323470308   2 TRIAIIGGhGKVALHLSALLTEEGHSVTSFIRNPDHAQDVADTGATPSVL-DV---EN-STTAEIAGALKGHDAVV 72
Cdd:COG0240    1 MKIAVLGA-GSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLpGVklpENlRATSDLEEALAGADLVL 75