human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. 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 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTTHPHPKLPGTIYTAAEEIEAVGGKALPCIVDVRDEQQISDAVEK 87
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  88 AVEKFGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPVWFKQHCA 167
Cdd:cd09762    81 AVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKNHTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961 168 YTIAKYGMSMCVLGMAEEFK-GEIAVNALWPKTAIHTAAMDMLGGSGIESQCRKVDIIADAAYAIFKKPK-NFTGNFVID 245
Cdd:cd09762   161 YTMAKYGMSMCVLGMAEEFKpGGIAVNALWPRTAIATAAMNMLGGVDVAACCRKPEIMADAAYAILTKPSsEFTGNFLID 240

                  ...
gi 1984068961 246 ENI 248
Cdd:cd09762   241 EEV 243

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. 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 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTTHPHPKLPGTIYTAAEEIEAVGGKALPCIVDVRDEQQISDAVEK 87
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  88 AVEKFGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPVWFKQHCA 167
Cdd:cd09762    81 AVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKNHTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961 168 YTIAKYGMSMCVLGMAEEFK-GEIAVNALWPKTAIHTAAMDMLGGSGIESQCRKVDIIADAAYAIFKKPK-NFTGNFVID 245
Cdd:cd09762   161 YTMAKYGMSMCVLGMAEEFKpGGIAVNALWPRTAIATAAMNMLGGVDVAACCRKPEIMADAAYAILTKPSsEFTGNFLID 240

                  ...
gi 1984068961 246 ENI 248
Cdd:cd09762   241 EEV 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 1984068961   7 RLAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTthphpklPGTIYTAAEEIEAVGGKALPCIVDVRDEQQISDAVE 86
Cdd:COG1028     3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRD-------AEALEAAAAELRAAGGRALAVAADVTDEAAVEALVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  87 KAVEKFGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPvwFKQHC 166
Cdd:COG1028    76 AAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRG--SPGQA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1984068961 167 AYTIAKYGMSMCVLGMAEEFKGE-IAVNALWPkTAIHTAAMDMLGG 211
Cdd:COG1028   154 AYAASKAAVVGLTRSLALELAPRgIRVNAVAP-GPIDTPMTRALLG 198

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961 311 EETFRIVKDSLSD-DVVKATQGIYLFELSGEDGGTWFLDLKsKGGNVGYGEPSDQADVVMSMSTDDFVKMFSGKLKPTMA 389
Cdd:COG3255     1 DEWAEALCEKLNAaDAAAGWDGVVQFVITGEGGGAYYLVID-DGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTA 79

                          90       100
                  ....*....|....*....|....*
gi 1984068961 390 FMSGRLKIKGNMALAIKLEKLVSQM 414
Cdd:COG3255    80 FMTGKLKVEGDMGLAMKLMSLFKAL 104

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. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  15 ITGASRGIGKAIALKAAKDGANIVIAAKTTHPhpklPGTIYTAA--EEIEAV----GGKALPCIVDVRDEQQISDAVEKA 88
Cdd:TIGR04504   6 VTGAARGIGAATVRRLAADGWRVVAVDLCADD----PAVGYPLAtrAELDAVaaacPDQVLPVIADVRDPAALAAAVALA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  89 VEKFGGIDILVNNASAISLTNTL-ETPTKRMDLMMSVNTRGTYLASKACIPylkkskvaHILNLSPPlnlnpvwfkQHC- 166
Cdd:TIGR04504  82 VERWGRLDAAVAAAGVIAGGRPLwETTDAELDLLLDVNLRGVWNLARAAVP--------AMLARPDP---------RGGr 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1984068961 167 -----------------AYTIAKYGMSMCVLGMAEEFKGE-IAVNALWP---KTAIHTAAMDMLGGSGIES 216
Cdd:TIGR04504 145 fvavasaaatrglphlaAYCAAKHAVVGLVRGLAADLGGTgVTANAVSPgstRTAMLAATARLYGLTDVEE 215

human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human HSDL2 and related protens. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. 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 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTTHPHPKLPGTIYTAAEEIEAVGGKALPCIVDVRDEQQISDAVEK 87
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  88 AVEKFGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPVWFKQHCA 167
Cdd:cd09762    81 AVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKNHTA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961 168 YTIAKYGMSMCVLGMAEEFK-GEIAVNALWPKTAIHTAAMDMLGGSGIESQCRKVDIIADAAYAIFKKPK-NFTGNFVID 245
Cdd:cd09762   161 YTMAKYGMSMCVLGMAEEFKpGGIAVNALWPRTAIATAAMNMLGGVDVAACCRKPEIMADAAYAILTKPSsEFTGNFLID 240

                  ...
gi 1984068961 246 ENI 248
Cdd:cd09762   241 EEV 243

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. 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 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTTH-----PHPKLPGTIYTAAEEIEAVGGKALPCIVDVRDEQQIS 82
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASegdngSAKSLPGTIEETAEEIEAAGGQALPIVVDVRDEDQVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  83 DAVEKAVEKFGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPVWF 162
Cdd:cd05338    81 ALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961 163 kqHCAYTIAKYGMSMCVLGMAEEFKG-EIAVNALWPKTAIHTAAMDMLGGSGIESQCRKVDIIADAAYAIFKKPK-NFTG 240
Cdd:cd05338   161 --DVAYAAGKAGMSRLTLGLAAELRRhGIAVNSLWPSTAIETPAATELSGGSDPARARSPEILSDAVLAILSRPAaERTG 238

                  ....*...
gi 1984068961 241 NFVIDENI 248
Cdd:cd05338   239 LVVIDEEL 246

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 1984068961  13 IFITGASRGIGKAIALKAAKDGANIVIAAKTTHPHpklpgtiyTAAEEIEAVGGKALPCIVDVRDEQQISDAVEKAVEKF 92
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEAL--------AELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  93 GGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPvwFKQHCAYTIAK 172
Cdd:cd05233    73 GRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRP--LPGQAAYAASK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961 173 YGMSMCVLGMAEEFKGE-IAVNALWPkTAIHTAAMDMLGGSGIESQCRKV---------DIIADA-AYAIFKKPKNFTGN 241
Cdd:cd05233   151 AALEGLTRSLALELAPYgIRVNAVAP-GLVDTPMLAKLGPEEAEKELAAAiplgrlgtpEEVAEAvVFLASDEASYITGQ 229

                  ..
gi 1984068961 242 FV 243
Cdd:cd05233   230 VI 231

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 1984068961  12 TIFITGASRGIGKAIALKAAKDGANIVIAAKTTHphpKLPgtiyTAAEEIeavGGKALPCIVDVRDEQQISDAVEKAVEK 91
Cdd:COG4221     7 VALITGASSGIGAATARALAAAGARVVLAARRAE---RLE----ALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  92 FGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPvwFKQHCAYTIA 171
Cdd:COG4221    77 FGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRP--YPGGAVYAAT 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1984068961 172 KYGMSMCVLGMAEEFKGE-IAVNALWP---KTAIHTAAMDMLGGSGIESQCR----KVDIIADAAYAIFKKPKN 237
Cdd:COG4221   155 KAAVRGLSESLRAELRPTgIRVTVIEPgavDTEFLDSVFDGDAEAAAAVYEGleplTPEDVAEAVLFALTQPAH 228

3-ketoacyl-(acyl-carrier-protein) reductase; Validated

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTTHPHPKlpgtiyTAAEEIEAVGGKALPCIVDVRDEQQISDAVEK 87
Cdd:PRK05557    3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAE------ALVAEIGALGGKALAVQGDVSDAESVERAVDE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  88 AVEKFGGIDILVNNAsAISLTNTLEtptkRMDL-----MMSVNTRGTYLASKACIPYLKKSKVAHILNLSpplNLNPVW- 161
Cdd:PRK05557   77 AKAEFGGVDILVNNA-GITRDNLLM----RMKEedwdrVIDTNLTGVFNLTKAVARPMMKQRSGRIINIS---SVVGLMg 148

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1984068961 162 -FKQhCAYTIAKYGMSMCVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK05557  149 nPGQ-ANYAASKAGVIGFTKSLARELasRG-ITVNAVAP 185

3-oxoacyl-ACP reductase FabG;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961   7 RLAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTthphpklPGTIYTAAEEIEAVGGKALPCIVDVRDEQQISDAVE 86
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSN-------EEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  87 KAVEKFGGIDILVNNASAisltnTLETPTKRM-----DLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSP--PLNLNP 159
Cdd:PRK05653   75 AAVEAFGALDILVNNAGI-----TRDALLPRMseedwDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSvsGVTGNP 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1984068961 160 VWfkqhCAYTIAKYGmsmcVLGMAEEFKGEIA-----VNALWPkTAIHTAAMDMLG 210
Cdd:PRK05653  150 GQ----TNYSAAKAG----VIGFTKALALELAsrgitVNAVAP-GFIDTDMTEGLP 196

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTTHphpklpgTIYTAAEEIEAVGGKALPCIVDVRDEQQISDAVEK 87
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEE-------NLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  88 AVEKFGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPP--LNLNPVwfkqH 165
Cdd:PRK07666   78 LKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTagQKGAAV----T 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1984068961 166 CAYTIAKYGmsmcVLGMAEEF-----KGEIAVNALWPKtaihTAAMDM 208
Cdd:PRK07666  154 SAYSASKFG----VLGLTESLmqevrKHNIRVTALTPS----TVATDM 193

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 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTThphPKLPgtiyTAAEEIEAVGGKALPCIVDVRDEQQISDAVEK 87
Cdd:cd05347     3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNE---EKAE----EAQQLIEKEGVEATAFTCDVSDEEAIKAAVEA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  88 AVEKFGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILN---LSPPLNLNPVwfkq 164
Cdd:cd05347    76 IEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINicsLLSELGGPPV---- 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1984068961 165 hCAYTIAKYGMSMCVLGMAEEF-KGEIAVNALWP 197
Cdd:cd05347   152 -PAYAASKGGVAGLTKALATEWaRHGIQVNAIAP 184

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 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTTHPHPKLpgtiytaAEEIEAVGGKALPCIVDVRDEQQISDAVEK 87
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEAL-------ADELEAEGGKALVLELDVTDEQQVDAAVER 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1984068961  88 AVEKFGGIDILVNNASAISLTNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLS 152
Cdd:cd08934    74 TVEALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNIS 138

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 1984068961   8 LAGCTIFITGASRGIGKAIALKAAKDGANIVIAaktthphpKLPGTiytAAEEIEA-VGGKALPCIVDVRDEQQISDAVE 86
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVA--------DIDGG---AAQAVVAqIAGGALALRVDVTDEQQVAALFE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  87 KAVEKFGGIDILVNNASAISLTNTL-ETPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPVwfKQH 165
Cdd:cd08944    70 RAVEEFGGLDLLVNNAGAMHLTPAIiDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGD--PGY 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1984068961 166 CAYTIAKYGMSMCVLGMAEEFKGE-IAVNALWP---KTAIHTAAMDM 208
Cdd:cd08944   148 GAYGASKAAIRNLTRTLAAELRHAgIRCNALAPgliDTPLLLAKLAG 194

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 1984068961  12 TIFITGASRGIGKAIALKAAKDGANiVIAakTTHPHPKLPgtiytaaEEIEAVGGKALPCIVDVRDEQQISDAVEKAVEK 91
Cdd:cd05374     2 VVLITGCSSGIGLALALALAAQGYR-VIA--TARNPDKLE-------SLGELLNDNLEVLELDVTDEESIKAAVKEVIER 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  92 FGGIDILVNNAsAISLTNTLE-TPTKRMDLMMSVNTRGTYLASKACIPYLKKSKVAHILNLSPPLNLNPVWFkqHCAYTI 170
Cdd:cd05374    72 FGRIDVLVNNA-GYGLFGPLEeTSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPF--LGPYCA 148

                         170       180
                  ....*....|....*....|.
gi 1984068961 171 AKYGMSmcvlGMAEEFKGEIA 191
Cdd:cd05374   149 SKAALE----ALSESLRLELA 165

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961  20 RGIGKAIALKAAKDGANIVIaaktTHPHPKLPGTiytAAEEIEAVGGKALPCivDVRDEQQISDAVEKAVEKFGGIDILV 99
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVL----TDLNEALAKR---VEELAEELGAAVLPC--DVTDEEQVEALVAAAVEKFGRLDILV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961 100 NNAsAISL---TNTLETPTKRMDLMMSVNTRGTYLASKACIPYLKKSkvAHILNLS--------PPLNlnpvwfkqhcAY 168
Cdd:pfam13561  77 NNA-GFAPklkGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSsigaervvPNYN----------AY 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1984068961 169 TIAKYGMSMCVLGMAEEF--KGeIAVNALWPkTAIHTAAMDMLGG 211
Cdd:pfam13561 144 GAAKAALEALTRYLAVELgpRG-IRVNAISP-GPIKTLAASGIPG 186

SDR family oxidoreductase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1984068961   7 RLAGCTIFITGASRGIGKAIALKAAKDGANIVIAAKTthphpklPGTIYTAAEEIEAvGGKALPCIVDVRDEQQISDAVE 86
Cdd:PRK07231    2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRN-------EEAAERVAAEILA-GGRAIAVAADVSDEADVEAAVA 73