Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVML 80
Cdd:cd05351   122 MIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKML 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:cd05351   202 NRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGGFLA 243

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVML 80
Cdd:cd05351   122 MIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKML 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:cd05351   202 NRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGGFLA 243

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVML 80
Cdd:COG1028   129 MRERG-GGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALA 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:COG1028   208 ARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA 249

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGR------------A 68
Cdd:TIGR03971 138 MIERG-GGSIVLTSSTAGLKGGPGGAHYVAAKHGVVGLMRSLALELAPHGIRVNAVHPTGVNTPMIDneamyrlfrpdlD 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958656375  69 NWSDPHKAKVMLDRIPLGkFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:TIGR03971 217 TPTDAAEAFRSMNALPVP-WVEPEDISNAVLFLASDEARYVTGVTLPVDAGALA 269

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVML 80
Cdd:cd05351   122 MIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKML 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:cd05351   202 NRIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVDGGFLA 243

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVML 80
Cdd:COG1028   129 MRERG-GGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALA 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:COG1028   208 ARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA 249

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPhKAKVML 80
Cdd:cd05233   120 MKKQG-GGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEE-AEKELA 197

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVD 117
Cdd:cd05233   198 AAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234

short chain dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPhKAKVML 80
Cdd:PRK06841  135 MIAAG-GGKIVNLASQAGVVALERHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGE-KGERAK 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGF 120
Cdd:PRK06841  213 KLIPAGRFAYPEEIAAAALFLASDAAAMITGENLVIDGGY 252

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGR---ANWSDPHKAK 77
Cdd:PRK06138  127 MQRQG-GGSIVNTASQLALAGGRGRAAYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRrifARHADPEALR 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958656375  78 VMLD-RIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:PRK06138  206 EALRaRHPMNRFGTAEEVAQAALFLASDESSFATGTTLVVDGGWLA 251

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKvmL 80
Cdd:PRK12743  126 MVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPDS--R 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:PRK12743  204 PGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIVDGGFML 245

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   8 GAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVMLDRIPLGK 87
Cdd:cd05358   134 GKIINMSSVHEKIPWPGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIPMGR 213

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958656375  88 FAEVENVVDTILFLLSNRSSMTTGSALPVDGG 119
Cdd:cd05358   214 IGEPEEIAAAAAWLASDEASYVTGTTLFVDGG 245

3-oxoacyl-ACP reductase FabG;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGVpGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAkvML 80
Cdd:PRK05653  128 MIKARY-GRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAE--IL 204

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGG 119
Cdd:PRK05653  205 KEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVNGG 243

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGR------------A 68
Cdd:TIGR03971 138 MIERG-GGSIVLTSSTAGLKGGPGGAHYVAAKHGVVGLMRSLALELAPHGIRVNAVHPTGVNTPMIDneamyrlfrpdlD 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958656375  69 NWSDPHKAKVMLDRIPLGkFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:TIGR03971 217 TPTDAAEAFRSMNALPVP-WVEPEDISNAVLFLASDEARYVTGVTLPVDAGALA 269

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVML 80
Cdd:cd05331   114 MKDRR-TGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLWHDEDGAAQVI 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958656375  81 D--------RIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGG 119
Cdd:cd05331   193 AgvpeqfrlGIPLGKIAQPADIANAVLFLASDQAGHITMHDLVVDGG 239

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   8 GAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMgRANWSDPHKAK-VMLDRIPLG 86
Cdd:cd05359   128 GRIVAISSLGSIRALPNYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDA-LAHFPNREDLLeAAAANTPAG 206

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958656375  87 KFAEVENVVDTILFLLSNRSSMTTGSALPVDGGF 120
Cdd:cd05359   207 RVGTPQDVADAVGFLCSDAARMITGQTLVVDGGL 240

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   8 GAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVMLD------ 81
Cdd:PRK08220  128 GAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWVDEDGEQQVIAgfpeqf 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958656375  82 --RIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGflAT 123
Cdd:PRK08220  208 klGIPLGKIARPQEIANAVLFLASDLASHITLQDIVVDGG--AT 249

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPhKIRVNAVNPTVVMTPMgRANWSDPHKAKvml 80
Cdd:cd05357   123 RLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEGLTRSAALELAP-NIRVNGIAPGLILLPE-DMDAEYRENAL--- 197

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSsmTTGSALPVDGG 119
Cdd:cd05357   198 RKVPLKRRPSAEEIADAVIFLLDSNY--ITGQIIKVDGG 234

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   5 GVPGAIVNVSSQASQRALTNHTV-YCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMgRANWSDPHKAKVMLDRI 83
Cdd:PRK06947  133 GRGGAIVNVSSIASRLGSPNEYVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEI-HASGGQPGRAARLGAQT 211

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958656375  84 PLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGG 119
Cdd:PRK06947  212 PLGRAGEADEVAETIVWLLSDAASYVTGALLDVGGG 247

short chain dehydrogenase; Validated

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   8 GAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTP-------MGRANWSDphkakvML 80
Cdd:PRK06484  394 GVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPavlalkaSGRADFDS------IR 467

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958656375  81 DRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:PRK06484  468 RRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGGWTA 509

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSD------PH 74
Cdd:cd08944   124 MIARG-GGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGfegalgPG 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958656375  75 KAKVMLDRIpLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGG 119
Cdd:cd08944   203 GFHLLIHQL-QGRLGRPEDVAAAVVFLLSDDASFITGQVLCVDGG 246

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   2 IARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVMLD 81
Cdd:PRK06124  134 MKRQGYGRIIAITSIAGQVARAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGPWLAQ 213

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958656375  82 RIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLA 122
Cdd:PRK06124  214 RTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLAVDGGYSV 254

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGvPGAIVNVSSQASQ-RALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGR---ANWSDPHKA 76
Cdd:cd05368   116 MLARK-DGSIINMSSVASSiKGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEeriQAQPDPEEA 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958656375  77 -KVMLDRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGG 119
Cdd:cd05368   195 lKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGG 238

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   8 GAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDP-----HKAKVMLDR 82
Cdd:cd08935   148 GSIINISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPdgsytDRSNKILGR 227

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958656375  83 IPLGKFAEVENVVDTILFLLS-NRSSMTTGSALPVDGGFLA 122
Cdd:cd08935   228 TPMGRFGKPEELLGALLFLASeKASSFVTGVVIPVDGGFSA 268

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   8 GAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVMlDRIPLGK 87
Cdd:cd05362   131 GRIINISSSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYA-KMSPLGR 209

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958656375  88 FAEVENVVDTILFLLSNRSSMTTGSALPVDGGF 120
Cdd:cd05362   210 LGEPEDIAPVVAFLASPDGRWVNGQVIRANGGY 242

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPM--------GRANWSD 72
Cdd:cd05366   126 FKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMwdyideevGEIAGKP 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958656375  73 PHKAKVMLDR-IPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGG 119
Cdd:cd05366   206 EGEGFAEFSSsIPLGRLSEPEDVAGLVSFLASEDSDYITGQTILVDGG 253

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958656375   1 MIARGVpGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDP 73
Cdd:pfam00106 123 MIKGSG-GRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDE 194

L-iditol 2-dehydrogenase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656375   1 MIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPM---------GRANWS 71
Cdd:PRK07067  126 MVEQGRGGKIINMASQAGRRGEALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMwdqvdalfaRYENRP 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958656375  72 DPHKAKVMLDRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGG 119
Cdd:PRK07067  206 PGEKKRLVGEAVPLGRMGVPDDLTGMALFLASADADYIVAQTYNVDGG 253