Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. 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 896545194  51 LGRKPRRLDRVYAQVQAVG-PEPLLYPLDLEGAGPDDYAELAQALQRELGRLDGLLVCAAHFPGLTPFELADPASFARAI 129
Cdd:cd05340   34 LGRNEEKLRQVADHINEEGgRQPQWFILDLLTCTSENCQQLAQRIAVNYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV* 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 130 HVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSGLYPGPLRTA 209
Cdd:cd05340  114 QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTA 193

                        170
                 ....*....|..
gi 896545194 210 LRARAYSvDQDP 221
Cdd:cd05340  194 MRASAFP-TEDP 204

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194   30 GGGLGSAAAVAAAAAGATVVLLGRKPRRLDRVYAQVQAVGPEPLLYPLDLEgagpdDYAELAQALQR---ELGRLDGLLV 106
Cdd:pfam00106   9 SSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVT-----DRAQVKALVEQaveRLGRLDILVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194  107 CAAHfPGLTPFELADPASFARAIHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITS 186
Cdd:pfam00106  84 NAGI-TGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRS 162

                         170       180
                  ....*....|....*....|....*.
gi 896545194  187 LHDELGRSPVRVSGLYPGPLRTALRA 212
Cdd:pfam00106 163 LALELAPHGIRVNAVAPGGVDTDMTK 188

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. 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 896545194  51 LGRKPRRLDRVYAQVQAVG-PEPLLYPLDLEGAGPDDYAELAQALQRELGRLDGLLVCAAHFPGLTPFELADPASFARAI 129
Cdd:cd05340   34 LGRNEEKLRQVADHINEEGgRQPQWFILDLLTCTSENCQQLAQRIAVNYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV* 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 130 HVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSGLYPGPLRTA 209
Cdd:cd05340  114 QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRTA 193

                        170
                 ....*....|..
gi 896545194 210 LRARAYSvDQDP 221
Cdd:cd05340  194 MRASAFP-TEDP 204

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 896545194  49 VLLGRKPRRLDRVYAQVQAVGPEPLLYPLDLegAGPDDYAELAQALQRELGRLDGLLVCAAHFPGlTPFELADPASFARA 128
Cdd:COG1028   34 VITDRDAEALEAAAAELRAAGGRALAVAADV--TDEAAVEALVAAAVAAFGRLDILVNNAGITPP-GPLEELTEEDWDRV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 129 IHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSGLYPGPLRT 208
Cdd:COG1028  111 LDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDT 190

                        170
                 ....*....|.
gi 896545194 209 ALRARAYSVDQ 219
Cdd:COG1028  191 PMTRALLGAEE 201

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194  49 VLLGRKPRRLDRVyaqVQAVGPEPLLYPLDLegAGPDDYAELAQALQRELGRLDGLLVCAAHFPgLTPFELADPASFARA 128
Cdd:COG4221   33 VLAARRAERLEAL---AAELGGRALAVPLDV--TDEAAVEAAVAAAVAEFGRLDVLVNNAGVAL-LGPLEELDPEDWDRM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 129 IHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSGLYPGPLRT 208
Cdd:COG4221  107 IDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDT 186

                        170
                 ....*....|...
gi 896545194 209 ALRARAYSVDQDP 221
Cdd:COG4221  187 EFLDSVFDGDAEA 199

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194   74 LYPLDLegAGPDDYAELAQALQRELGRLDGLLVCAAHFPGL-TPFELADPASFARAIHVTLTAPAWLAQACLPLLRqrED 152
Cdd:pfam13561  47 VLPCDV--TDEEQVEALVAAAVEKFGRLDILVNNAGFAPKLkGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMK--EG 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 896545194  153 AALVF-AVDAPERVGQAYwGGYGVAQHGLRGLITSLHDELGRSPVRVSGLYPGPLRT 208
Cdd:pfam13561 123 GSIVNlSSIGAERVVPNY-NAYGAAKAALEALTRYLAVELGPRGIRVNAISPGPIKT 178

short chain dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194  63 AQVQAVGPEPLLYPLDLEGAGPDDYAELAQALQRELGRLDGLLVCAAHFPGLTPFELADPASFARAIHVTLTAPAWLAQA 142
Cdd:PRK12829  49 AATAARLPGAKVTATVADVADPAQVERVFDTAVERFGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARA 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896545194 143 CLPLLRQRE-DAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSGLYPGPLRTALRARA 214
Cdd:PRK12829 129 AVPLLKASGhGGVIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRV 201

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. 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 896545194  76 PLDLegagPDDYAELAQALQRELG--RLDGLLVCAAHFPGLTPFELADPASFARAIHVTLTAPAWLAQACLPLLRQREDA 153
Cdd:cd05325   53 ELDV----TDEIAESAEAVAERLGdaGLDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARA 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896545194 154 ALVFaVDApeRVG------QAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSGLYPGPLRT 208
Cdd:cd05325  129 KIIN-ISS--RVGsigdntSGGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRT 186

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194  30 GGGLGSAAAVAAAAAGATVVLLGRKPRRLDRVYAQVQAVGPEPLLYPLDLegAGPDDYAELAQALQRELGRLDgLLVCAA 109
Cdd:PRK06181  10 SEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDV--SDAEACERLIEAAVARFGGID-ILVNNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 110 HFPGLTPF-ELADPASFARAIHVTLTAPAWLAQACLPLLRQReDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLH 188
Cdd:PRK06181  87 GITMWSRFdELTDLSVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHALHGFFDSLR 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 896545194 189 DELGRSPVRVSGLYPGPLRTALRARAYSVDQDP 221
Cdd:PRK06181 166 IELADDGVAVTVVCPGFVATDIRKRALDGDGKP 198

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. 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 896545194  34 GSAAAVAAAAAGATVVLLGRKPRRLDRVYAQVQAVGPEPLLYPLDLEgagpdDYAELAQALQR---ELGRLDgLLVCAAH 110
Cdd:cd08934   16 GEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVT-----DEQQVDAAVERtveALGRLD-ILVNNAG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 111 FPGLTPFELADPASFARAIHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDE 190
Cdd:cd08934   90 IMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEGLRQE 169

                        170       180
                 ....*....|....*....|.
gi 896545194 191 LGRSPVRVSGLYPGPLRTALR 211
Cdd:cd08934  170 VTERGVRVVVIEPGTVDTELR 190

pteridine reductase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194  84 PDDYAELAQALQRELGRLDGLLVCAAHF-PglTPFELADPASFARAIHVTLTAPAWLAQACLPLLRQREdAALVFAVDA- 161
Cdd:PRK09135  69 PDALPELVAACVAAFGRLDALVNNASSFyP--TPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR-GAIVNITDIh 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 896545194 162 PERVGQAYwGGYGVAQHGLRGLITSLHDELgrSP-VRVSGLYPGP 205
Cdd:PRK09135 146 AERPLKGY-PVYCAAKAALEMLTRSLALEL--APeVRVNAVAPGA 187

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194  52 GRKPRRLDRVYAQVQAVGPePLLYPLDLEGagPDDYAELAQALQRELGRLDGLLVCAAHFP---GLTPFELADPASFARA 128
Cdd:COG0623   38 YQGEALKKRVEPLAEELGS-ALVLPCDVTD--DEQIDALFDEIKEKWGKLDFLVHSIAFAPkeeLGGRFLDTSREGFLLA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 129 IHV---TLTApawLAQACLPLLRqrEDAALVfAV--DAPERVgqayWGGY---GVAQHGLRGLITSLHDELGRSPVRVSG 200
Cdd:COG0623  115 MDIsaySLVA---LAKAAEPLMN--EGGSIV-TLtyLGAERV----VPNYnvmGVAKAALEASVRYLAADLGPKGIRVNA 184

                 ....*...
gi 896545194 201 LYPGPLRT 208
Cdd:COG0623  185 ISAGPIKT 192

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. 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 896545194  30 GGGLGSAAAVAAAAAGATVVLLGRKPRRLDRVYAQvqavGPEPLLYPLDLegAGPDDYAELAQALQRELGRLDGLLVCAA 109
Cdd:cd08932    9 SRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS----GGDVEAVPYDA--RDPEDARALVDALRDRFGRIDVLVHNAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 110 hFPGLTPFELADPASFARAIHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHD 189
Cdd:cd08932   83 -IGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALAHALRQ 161

                        170       180
                 ....*....|....*....|.
gi 896545194 190 ELGRSPVRVSGLYPGPLRTAL 210
Cdd:cd08932  162 EGWDHGVRVSAVCPGFVDTPM 182

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. 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 896545194  44 AGATVVLLGRKPRRLDRVYAQVQAVGPEPLLYPLDLegAGPDDYAELAQALQRELGRLDgLLVCAA---HFPGLTPFELA 120
Cdd:cd05347   28 AGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDV--SDEEAIKAAVEAIEEDFGKID-ILVNNAgiiRRHPAEEFPEA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 121 DpasFARAIHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSG 200
Cdd:cd05347  105 E---WRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNA 181

                        170
                 ....*....|....*.
gi 896545194 201 LYPGPLRTALRARAYS 216
Cdd:cd05347  182 IAPGYFATEMTEAVVA 197

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194  32 GLGSAAAVAAAAAGATVVLLGRKPRRLDRVYAQVQAVGPEPLLYPLDLegAGPDDYAELAQALQRELGRLDGLLVCAAHF 111
Cdd:PRK07774  17 GIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDV--SDPDSAKAMADATVSAFGGIDYLVNNAAIY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 112 PGLTPFEL--ADPASFARAIHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVgqaYWGGYGVAQHGLRGLITSLHD 189
Cdd:PRK07774  95 GGMKLDLLitVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWL---YSNFYGLAKVGLNGLTQQLAR 171

                        170       180
                 ....*....|....*....|
gi 896545194 190 ELGRSPVRVSGLYPGPLRTA 209
Cdd:PRK07774 172 ELGGMNIRVNAIAPGPIDTE 191

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. 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 896545194  52 GRKPRRLDRVYAQVQAVGPEPLLYPLDLegAGPDDYAELAQALQRELGRLDGLLVCAahfpGLTPFELAD-----PASFA 126
Cdd:cd05337   33 LPDDDQATEVVAEVLAAGRRAIYFQADI--GELSDHEALLDQAWEDFGRLDCLVNNA----GIAVRPRGDlldltEDSFD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 127 RAIHVTLTAPAWLAQACL------PLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSG 200
Cdd:cd05337  107 RLIAINLRGPFFLTQAVArrmveqPDRFDGPHRSIIFVTSINAYLVSPNRGEYCISKAGLSMATRLLAYRLADEGIAVHE 186

                        170
                 ....*....|....*..
gi 896545194 201 LYPGPLRTALRARAYSV 217
Cdd:cd05337  187 IRPGLIHTDMTAPVKEK 203

SDR family oxidoreductase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194  86 DYAELAQAL----QRELGRLDGLLVCAAhFPGLTPFELADPASFARAIHVTLTAPAWLAQACLPLLRQREDAALVFAVDA 161
Cdd:PRK08267  59 DRAAWDAALadfaAATGGRLDVLFNNAG-ILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSA 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 896545194 162 PERVGQAYWGGYGVAQHGLRGLITSLHDELGRSPVRVSGLYPGPLRTAL 210
Cdd:PRK08267 138 SAIYGQPGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAM 186

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 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 896545194  48 VVLLGRK-----PRRLDRVYAqvQAVGPEPL----------LYPLDLEGAGPDDYAELAQALQRELGRLDGLLVCAAHfp 112
Cdd:cd05374    9 SSGIGLAlalalAAQGYRVIA--TARNPDKLeslgellndnLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNNAGY-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 113 GLT-PFELADPASFARAIHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDEL 191
Cdd:cd05374   85 GLFgPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALSESLRLEL 164

                        170
                 ....*....|....*...
gi 896545194 192 GRSPVRVSGLYPGPLRTA 209
Cdd:cd05374  165 APFGIKVTIIEPGPVRTG 182

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) 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 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 896545194  46 ATVVLLGRKPRRLDRVYAQVQAVGPEPLLYPLDLegAGPDDYAELAQALQRELGRLDgLLVCAAHFPGLTPFELADPASF 125
Cdd:cd05360   25 AKVVLAARSAEALHELAREVRELGGEAIAVVADV--ADAAQVERAADTAVERFGRID-TWVNNAGVAVFGRFEDVTPEEF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896545194 126 ARAIHVTLTAPAWLAQACLPLLRQREDAALVFAVDAPERVGQAYWGGYGVAQHGLRGLITSLHDELGRS--PVRVSGLYP 203
Cdd:cd05360  102 RRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLRAELAHDgaPISVTLVQP 181

                 ....*
gi 896545194 204 GPLRT 208
Cdd:cd05360  182 TAMNT 186