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 149043379  22 GRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPLGH 101
Cdd:cd05333  127 RSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGR 206

                         90       100       110
                 ....*....|....*....|....*....|....
gi 149043379 102 MGDPEDVADVVAFLASEDSGYITGASVEVSGGLF 135
Cdd:cd05333  207 LGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) 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: TGxxxGxG in classical SDRs. 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 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. 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-151 and Lys-155, and well as Asn-111 (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 149043379  22 GRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPLGH 101
Cdd:cd05333  127 RSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGR 206

                         90       100       110
                 ....*....|....*....|....*....|....
gi 149043379 102 MGDPEDVADVVAFLASEDSGYITGASVEVSGGLF 135
Cdd:cd05333  207 LGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379   23 RGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPLGHM 102
Cdd:TIGR01830 127 SGRIINISSVVGLMGNAGQANYAASKAGVIGFTKSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRF 206

                          90       100       110
                  ....*....|....*....|....*....|...
gi 149043379  103 GDPEDVADVVAFLASEDSGYITGASVEVSGGLF 135
Cdd:TIGR01830 207 GQPEEVANAVAFLASDEASYITGQVIHVDGGMY 239

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379   23 RGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMP--EKVKDKVTAMIPLG 100
Cdd:pfam13561 122 GGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLG 201

                          90       100       110
                  ....*....|....*....|....*....|....
gi 149043379  101 HMGDPEDVADVVAFLASEDSGYITGASVEVSGGL 134
Cdd:pfam13561 202 RLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) 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: TGxxxGxG in classical SDRs. 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 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. 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-151 and Lys-155, and well as Asn-111 (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 149043379  22 GRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPLGH 101
Cdd:cd05333  127 RSGRIINISSVVGLIGNPGQANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKVKEKILKQIPLGR 206

                         90       100       110
                 ....*....|....*....|....*....|....
gi 149043379 102 MGDPEDVADVVAFLASEDSGYITGASVEVSGGLF 135
Cdd:cd05333  207 LGTPEEVANAVAFLASDDASYITGQVLHVNGGMY 240

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379   23 RGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPLGHM 102
Cdd:TIGR01830 127 SGRIINISSVVGLMGNAGQANYAASKAGVIGFTKSLAKELASRNITVNAVAPGFIDTDMTDKLSEKVKKKILSQIPLGRF 206

                          90       100       110
                  ....*....|....*....|....*....|...
gi 149043379  103 GDPEDVADVVAFLASEDSGYITGASVEVSGGLF 135
Cdd:TIGR01830 207 GQPEEVANAVAFLASDEASYITGQVIHVDGGMY 239

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 149043379  22 GRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMP--EKVKDKVTAMIPL 99
Cdd:COG1028  133 GGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLgaEEVREALAARIPL 212

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 149043379 100 GHMGDPEDVADVVAFLASEDSGYITGASVEVSGGLFM 136
Cdd:COG1028  213 GRLGTPEEVAAAVLFLASDAASYITGQVLAVDGGLTA 249

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379   22 GRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPLGH 101
Cdd:TIGR01829 128 GWGRIINISSVNGQKGQFGQTNYSAAKAGMIGFTKALAQEGATKGVTVNTISPGYIATDMVMAMREDVLNSIVAQIPVKR 207

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 149043379  102 MGDPEDVADVVAFLASEDSGYITGASVEVSGGLFM 136
Cdd:TIGR01829 208 LGRPEEIAAAVAFLASEEAGYITGATLSINGGLYM 242

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379   23 RGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMP--EKVKDKVTAMIPLG 100
Cdd:pfam13561 122 GGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKTLAASGIPgfDELLAAAEARAPLG 201

                          90       100       110
                  ....*....|....*....|....*....|....
gi 149043379  101 HMGDPEDVADVVAFLASEDSGYITGASVEVSGGL 134
Cdd:pfam13561 202 RLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235

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 149043379  22 GRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQK-MPEKVKDKVTAMIPLG 100
Cdd:cd05233  124 GGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKlGPEEAEKELAAAIPLG 203

                         90       100       110
                 ....*....|....*....|....*....|
gi 149043379 101 HMGDPEDVADVVAFLASEDSGYITGASVEV 130
Cdd:cd05233  204 RLGTPEEVAEAVVFLASDEASYITGQVIPV 233

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379   7 LRSALALVTGAGSGigrGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMP 86
Cdd:PRK12829 126 ARAAVPLLKASGHG---GVIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVI 202

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 149043379  87 -----------EKVKDKVTAMIPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGGL 134
Cdd:PRK12829 203 earaqqlgiglDEMEQEYLEKISLGRMVEPEDIAATALFLASPAARYITGQAISVDGNV 261

3-ketoacyl-ACP reductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379  22 GRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPLGH 101
Cdd:PRK12938 131 GWGRIINISSVNGQKGQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRR 210

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 149043379 102 MGDPEDVADVVAFLASEDSGYITGASVEVSGGLFM 136
Cdd:PRK12938 211 LGSPDEIGSIVAWLASEESGFSTGADFSLNGGLHM 245

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379  13 LVTGAGSGIGRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKV--- 89
Cdd:PRK07231 123 AAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPtpe 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 149043379  90 -KDKVTAMIPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGGLF 135
Cdd:PRK07231 203 nRAKFLATIPLGRLGTPEDIANAALFLASDEASWITGVTLVVDGGRC 249

acetoacetyl-CoA reductase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379  24 GSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPLGHMG 103
Cdd:PRK12935 136 GRIISISSIIGQAGGFGQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVRQKIVAKIPKKRFG 215

                         90       100       110
                 ....*....|....*....|....*....|...
gi 149043379 104 DPEDVADVVAFLAsEDSGYITGASVEVSGGLFM 136
Cdd:PRK12935 216 QADEIAKGVVYLC-RDGAYITGQQLNINGGLYM 247

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. 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 149043379  24 GSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQK-----------MPEKVKDK 92
Cdd:cd05344  130 GRIVNISSLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRRllearaekegiSVEEAEKE 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 149043379  93 VTAMIPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGGL 134
Cdd:cd05344  210 VASQIPLGRVGKPEELAALIAFLASEKASYITGQAILVDGGL 251

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 149043379  24 GSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQ---KMPEKVKDkVTAMIPLG 100
Cdd:cd05358  134 GKIINMSSVHEKIPWPGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAeawDDPEQRAD-LLSLIPMG 212

                         90       100       110
                 ....*....|....*....|....*....|....
gi 149043379 101 HMGDPEDVADVVAFLASEDSGYITGASVEVSGGL 134
Cdd:cd05358  213 RIGEPEEIAAAAAWLASDEASYVTGTTLFVDGGM 246

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379   23 RGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKV---KDK------- 92
Cdd:TIGR02415 129 GGKIINAASIAGHEGNPILSAYSSTKFAVRGLTQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEETseiAGKpigegfe 208

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 149043379   93 -VTAMIPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGGL 134
Cdd:TIGR02415 209 eFSSEIALGRPSEPEDVAGLVSFLASEDSDYITGQSILVDGGM 251

SDR family oxidoreductase UcpA;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379  22 GRGSIINISSIVGK-VGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKM--------PEKVKDK 92
Cdd:PRK08226 132 KDGRIVMMSSVTGDmVADPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIarqsnpedPESVLTE 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 149043379  93 VTAMIPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGG 133
Cdd:PRK08226 212 MAKAIPLRRLADPLEVGELAAFLASDESSYLTGTQNVIDGG 252

(S)-acetoin forming diacetyl reductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379  24 GSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKV-----KDKVTAM-- 96
Cdd:PRK08643 132 GKIINATSQAGVVGNPELAVYSSTKFAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVgenagKPDEWGMeq 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 149043379  97 ----IPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGGL 134
Cdd:PRK08643 212 fakdITLGRLSEPEDVANCVSFLAGPDSDYITGQTIIVDGGM 253

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 149043379  22 GRGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKmpeKVKDKVTAMIP--- 98
Cdd:cd08944  128 GGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLA---KLAGFEGALGPggf 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 149043379  99 -------LGHMGDPEDVADVVAFLASEDSGYITGASVEVSGG 133
Cdd:cd08944  205 hllihqlQGRLGRPEDVAAAVVFLLSDDASFITGQVLCVDGG 246

short chain dehydrogenase; Validated

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379   1 MASQLRLRSALALVTGAGSGigrGSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATP 80
Cdd:PRK06484 114 TGAYLVAREALRLMIEQGHG---AAIVNVASGAGLVALPKRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQ 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149043379  81 MTQKMPEKVKDKVTAM---IPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGG 133
Cdd:PRK06484 191 MVAELERAGKLDPSAVrsrIPLGRLGRPEEIAEAVFFLASDQASYITGSTLVVDGG 246

3-hydroxybutyrate dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379  24 GSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKM-----------PEKVKDK 92
Cdd:PRK12429 133 GRIINMASVHGLVGSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQipdlakergisEEEVLED 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 149043379  93 VTA-MIPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGGLFM 136
Cdd:PRK12429 213 VLLpLVPQKRFTTVEEIADYALFLASFAAKGVTGQAWVVDGGWTA 257

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 149043379  22 GRGSIINISSIVGKV-GNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKM------PEKVKDKVT 94
Cdd:cd05368  120 KDGSIINMSSVASSIkGVPNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERiqaqpdPEEALKAFA 199

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 149043379  95 AMIPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGG 133
Cdd:cd05368  200 ARQPLGRLATPEEVAALAVYLASDESAYVTGTAVVIDGG 238

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149043379  24 GSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMT--------QKMPEKVKDKVTA 95
Cdd:PRK08589 134 GSIINTSSFSGQAADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVdkltgtseDEAGKTFRENQKW 213

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 149043379  96 MIPLGHMGDPEDVADVVAFLASEDSGYITGASVEVSGGL 134
Cdd:PRK08589 214 MTPLGRLGKPEEVAKLVVFLASDDSSFITGETIRIDGGV 252

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. 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 149043379  22 GRGSIINISSIVGKVGNIGQTN--YASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKMPEKVKDKVTAMIPL 99
Cdd:cd05352  136 GKGSLIITASMSGTIVNRPQPQaaYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWESYIPL 215

                         90       100       110
                 ....*....|....*....|....*....|....
gi 149043379 100 GHMGDPEDVADVVAFLASEDSGYITGASVEVSGG 133
Cdd:cd05352  216 KRIALPEELVGAYLYLASDASSYTTGSDLIIDGG 249

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with 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 149043379  24 GSIINISSIVGKVGNIGQTNYASSKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPM-TQKMPEKVKDKVTAMIPLGHM 102
Cdd:cd05355  156 SSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLiPSSFPEEKVSEFGSQVPMGRA 235

                         90       100       110
                 ....*....|....*....|....*....|.
gi 149043379 103 GDPEDVADVVAFLASEDSGYITGASVEVSGG 133
Cdd:cd05355  236 GQPAEVAPAYVFLASQDSSYVTGQVLHVNGG 266