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Conserved domains on  [gi|767958463|ref|XP_011517393|]
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hydroxysteroid dehydrogenase-like protein 2 isoform X1 [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10176796)

SDR family NAD(P)-dependent oxidoreductase, similar to human hydroxysteroid dehydrogenase-like 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 8-248 1.76e-170

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.


:

Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 471.16  E-value: 1.76e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQHCA 167
Cdd:cd09762   81 AVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKNHTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 168 YTIAKYGMSMYVLGMAEEFK-GEIAVNALWPKTAIHTAAMDMLGGPGIESQCRKVDIIADAAYSIFQKPKS-FTGNFVID 245
Cdd:cd09762  161 YTMAKYGMSMCVLGMAEEFKpGGIAVNALWPRTAIATAAMNMLGGVDVAACCRKPEIMADAAYAILTKPSSeFTGNFLID 240


                 ...
gi 767958463 246 ENI 248
Cdd:cd09762  241 EEV 243
 
Name Accession Description Interval E-value
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 8-248 1.76e-170

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.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 471.16  E-value: 1.76e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQHCA 167
Cdd:cd09762   81 AVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKNHTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 168 YTIAKYGMSMYVLGMAEEFK-GEIAVNALWPKTAIHTAAMDMLGGPGIESQCRKVDIIADAAYSIFQKPKS-FTGNFVID 245
Cdd:cd09762  161 YTMAKYGMSMCVLGMAEEFKpGGIAVNALWPRTAIATAAMNMLGGVDVAACCRKPEIMADAAYAILTKPSSeFTGNFLID 240


                 ...
gi 767958463 246 ENI 248
Cdd:cd09762  241 EEV 243
PRK08278 PRK08278
SDR family oxidoreductase;
5-269 2.11e-158

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 441.65  E-value: 2.11e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK08278   1 MMSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKLPGTIHTAAEEIEAAGGQALPLVGDVRDEDQVAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQ 164
Cdd:PRK08278  81 VAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPLNLDPKWFAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 165 HCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPKTAIHTAAM-DMLGGPGIESQCRKVDIIADAAYSIFQKP-KSFTGN 241
Cdd:PRK08278 161 HTAYTMAKYGMSLCTLGLAEEFRDDgIAVNALWPRTTIATAAVrNLLGGDEAMRRSRTPEIMADAAYEILSRPaREFTGN 240

                        250       260
                 ....*....|....*....|....*...
gi 767958463 242 FVIDENILKEEGIENFDVYAIKPAVFPM 269
Cdd:PRK08278 241 FLIDEEVLREAGVTDFSRYAVDPGAPLM 268
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 7-212 7.00e-54

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


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 175.36  E-value: 7.00e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:COG1028    3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDA-------EALEAAAAELRAAGGRALAVAADVTDEAAVEALVA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHC 166
Cdd:COG1028   76 AAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRG--SPGQA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767958463 167 AYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPkTAIHTAAMDMLGGP 212
Cdd:COG1028  154 AYAASKAAVVGLTRSLALELAPRgIRVNAVAP-GPIDTPMTRALLGA 199
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 12-197 1.77e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 146.99  E-value: 1.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEK-------LEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHCAYTIA 171
Cdd:pfam00106  75 LGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVP--YPGGSAYSAS 152

                         170       180
                  ....*....|....*....|....*..
gi 767958463  172 KYGMSMYVLGMAEEFKG-EIAVNALWP 197
Cdd:pfam00106 153 KAAVIGFTRSLALELAPhGIRVNAVAP 179
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 15-216 3.53e-20

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]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 87.38  E-value: 3.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   15 ITGASRGIGKAIALKAAKDGANIVI----AAKTAQPHPklLGTiytaAEEIEAV----GGKALPCIVDVRDEQQISAAVE 86
Cdd:TIGR04504   6 VTGAARGIGAATVRRLAADGWRVVAvdlcADDPAVGYP--LAT----RAELDAVaaacPDQVLPVIADVRDPAALAAAVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   87 KAIKKFGGIDILVNNASAISLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPylkkskvaHILNISPPlnlnpvwfkQH 165
Cdd:TIGR04504  80 LAVERWGRLDAAVAAAGVIAGGRPLwETTDAELDLLLDVNLRGVWNLARAAVP--------AMLARPDP---------RG 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  166 C------------------AYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIHTAAMDMLGGPGIES 216
Cdd:TIGR04504 143 GrfvavasaaatrglphlaAYCAAKHAVVGLVRGLAADLGGTgVTANAVSPgstRTAMLAATARLYGLTDVEE 215
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 12-102 5.47e-06

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 45.94  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463    12 TVFITGASRGIGKAIALKAAKDGA-NIVIAAKTAQPHPKLLgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAA----ALLAELEAAGARVTVVACDVADRDALAAVLAAIPA 77

                           90
                   ....*....|..
gi 767958463    91 KFGGIDILVNNA 102
Cdd:smart00822  78 VEGPLTGVIHAA 89
 
Name Accession Description Interval E-value
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 8-248 1.76e-170

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.


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 471.16  E-value: 1.76e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQHCA 167
Cdd:cd09762   81 AVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLNPKWFKNHTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 168 YTIAKYGMSMYVLGMAEEFK-GEIAVNALWPKTAIHTAAMDMLGGPGIESQCRKVDIIADAAYSIFQKPKS-FTGNFVID 245
Cdd:cd09762  161 YTMAKYGMSMCVLGMAEEFKpGGIAVNALWPRTAIATAAMNMLGGVDVAACCRKPEIMADAAYAILTKPSSeFTGNFLID 240


                 ...
gi 767958463 246 ENI 248
Cdd:cd09762  241 EEV 243
PRK08278 PRK08278
SDR family oxidoreductase;
5-269 2.11e-158

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 441.65  E-value: 2.11e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK08278   1 MMSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEPHPKLPGTIHTAAEEIEAAGGQALPLVGDVRDEDQVAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQ 164
Cdd:PRK08278  81 VAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPLNLDPKWFAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 165 HCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPKTAIHTAAM-DMLGGPGIESQCRKVDIIADAAYSIFQKP-KSFTGN 241
Cdd:PRK08278 161 HTAYTMAKYGMSLCTLGLAEEFRDDgIAVNALWPRTTIATAAVrNLLGGDEAMRRSRTPEIMADAAYEILSRPaREFTGN 240

                        250       260
                 ....*....|....*....|....*...
gi 767958463 242 FVIDENILKEEGIENFDVYAIKPAVFPM 269
Cdd:PRK08278 241 FLIDEEVLREAGVTDFSRYAVDPGAPLM 268
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 8-248 3.28e-130

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.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 369.41  E-value: 3.28e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQ-----PHPKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQIS 82
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASegdngSAKSLPGTIEETAEEIEAAGGQALPIVVDVRDEDQVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWF 162
Cdd:cd05338   81 ALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 163 kqHCAYTIAKYGMSMYVLGMAEEFKG-EIAVNALWPKTAIHTAAMDMLGGPGIESQCRKVDIIADAAYSIFQKPK-SFTG 240
Cdd:cd05338  161 --DVAYAAGKAGMSRLTLGLAAELRRhGIAVNSLWPSTAIETPAATELSGGSDPARARSPEILSDAVLAILSRPAaERTG 238


                 ....*...
gi 767958463 241 NFVIDENI 248
Cdd:cd05338  239 LVVIDEEL 246
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 7-212 7.00e-54

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


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 175.36  E-value: 7.00e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:COG1028    3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDA-------EALEAAAAELRAAGGRALAVAADVTDEAAVEALVA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHC 166
Cdd:COG1028   76 AAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRG--SPGQA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767958463 167 AYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPkTAIHTAAMDMLGGP 212
Cdd:COG1028  154 AYAASKAAVVGLTRSLALELAPRgIRVNAVAP-GPIDTPMTRALLGA 199
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 13-221 2.99e-47

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.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 157.83  E-value: 2.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEAL--------AELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHCAYTIAK 172
Cdd:cd05233   73 GRLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRP--LPGQAAYAASK 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767958463 173 YGMSMYVLGMAEEFKGE-IAVNALWPkTAIHTAAMDMLGGPGIESQCRKV 221
Cdd:cd05233  151 AALEGLTRSLALELAPYgIRVNAVAP-GLVDTPMLAKLGPEEAEKELAAA 199
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-237 3.79e-45

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 153.10  E-value: 3.79e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:COG0300    2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEAL-------AAELRAAGARVEVVALDVTDPDAVAALAE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHC 166
Cdd:COG0300   75 AVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRG--LPGMA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958463 167 AYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIHTAAMDMLGGPGIEsqcrkVDIIADAAYSIFQKPKS 237
Cdd:COG0300  153 AYAASKAALEGFSESLRAELAPTgVRVTAVCPgpvDTPFTARAGAPAGRPLLS-----PEEVARAILRALERGRA 222
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 12-235 9.84e-44

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


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 148.79  E-value: 9.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtIYTAAEEIeavGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:COG4221    7 VALITGASSGIGAATARALAAAGARVVLAARRAER-------LEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHCAYTIA 171
Cdd:COG4221   77 FGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRP--YPGGAVYAAT 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958463 172 KYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIHTAAMDMLGGPGIESQCR----KVDIIADAAYSIFQKP 235
Cdd:COG4221  155 KAAVRGLSESLRAELRPTgIRVTVIEPgavDTEFLDSVFDGDAEAAAAVYEGleplTPEDVAEAVLFALTQP 226
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 12-197 1.77e-43

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 146.99  E-value: 1.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEK-------LEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHCAYTIA 171
Cdd:pfam00106  75 LGRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVP--YPGGSAYSAS 152

                         170       180
                  ....*....|....*....|....*..
gi 767958463  172 KYGMSMYVLGMAEEFKG-EIAVNALWP 197
Cdd:pfam00106 153 KAAVIGFTRSLALELAPhGIRVNAVAP 179
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 8-197 1.28e-37

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 133.40  E-value: 1.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAE------ALVAEIGALGGKALAVQGDVSDAESVERAVDE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNAsAIsltnTLDTPTKRLDL-----MMNVNTRGTYLASKACIPYLKKSKVAHILNISpplNLNPVW- 161
Cdd:PRK05557  77 AKAEFGGVDILVNNA-GI----TRDNLLMRMKEedwdrVIDTNLTGVFNLTKAVARPMMKQRSGRIINIS---SVVGLMg 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958463 162 -FKQhCAYTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK05557 149 nPGQ-ANYAASKAGVIGFTKSLARELasRG-ITVNAVAP 185
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-197 1.21e-36

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 130.86  E-value: 1.21e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   4 NTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQISA 83
Cdd:PRK12939   1 MASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEAREL-------AAALEAAGGRAHAIAADLADPASVQR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLnlnPVW-F 162
Cdd:PRK12939  74 FFDAAAAALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDT---ALWgA 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767958463 163 KQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK12939 151 PKLGAYVASKGAVIGMTRSLARELGGRgITVNAIAP 186
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
7-228 3.19e-36

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 129.51  E-value: 3.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEE-------AAEALAAELRAAGGEARVLVFDVSDEAAVRALIE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAisltnTLDTPTKRL-----DLMMNVNTRGTYLASKACIPYLKKSKVAHILNISP--PLNLNP 159
Cdd:PRK05653  75 AAVEAFGALDILVNNAGI-----TRDALLPRMseedwDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSvsGVTGNP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 160 VWfkqhCAYTIAKYGmsmyVLGMAEEFKGEIA-----VNALWPkTAIHTAAMDMLGGPGIESQCRKVDI--------IAD 226
Cdd:PRK05653 150 GQ----TNYSAAKAG----VIGFTKALALELAsrgitVNAVAP-GFIDTDMTEGLPEEVKAEILKEIPLgrlgqpeeVAN 220


                 ..
gi 767958463 227 AA 228
Cdd:PRK05653 221 AV 222
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-199 2.39e-34

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 124.42  E-value: 2.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK07666   5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEE-------NLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHCA 167
Cdd:PRK07666  78 LKNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKG--AAVTSA 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767958463 168 YTIAKYGmsmyVLGMAEEF-----KGEIAVNALWPKT 199
Cdd:PRK07666 156 YSASKFG----VLGLTESLmqevrKHNIRVTALTPST 188
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 7-197 3.51e-34

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 124.61  E-value: 3.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAA-------AAEALQKAGGKAIGVAMDVTDEEAINAGID 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpVWFKQHC 166
Cdd:PRK12429  74 YAVETFGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGL--VGSAGKA 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767958463 167 AYTIAKYGmsmyVLGMA-----EEFKGEIAVNALWP 197
Cdd:PRK12429 152 AYVSAKHG----LIGLTkvvalEGATHGVTVNAICP 183
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-203 4.09e-34

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 124.18  E-value: 4.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAktaqpHPKLLGTIYTAaEEIEAVGGKALPCIVDVRDEQQISAAV 85
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAY-----DINEEAAQELL-EEIKEEGGDAIAVKADVSSEEDVENLV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpplnlnPVWFKQ- 164
Cdd:PRK05565  75 EQIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNIS------SIWGLIg 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767958463 165 -HC--AYTIAKYGMSMYVLGMAEEF-KGEIAVNALWPKtAIHT 203
Cdd:PRK05565 149 aSCevLYSASKGAVNAFTKALAKELaPSGIRVNAVAPG-AIDT 190
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 8-215 1.26e-33

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. 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.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 122.70  E-value: 1.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtIYTAAEEIEAV-GGKALPCIVDVRDEQQISAAVE 86
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEV-------LEAAAEEISSAtGGRAHPIQCDVRDPEAVEAAVD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAisltNTLdTPTKRL-----DLMMNVNTRGTYLASKACIPYLKKSKV-AHILNISPPLNLNPV 160
Cdd:cd05369   74 ETLKEFGKIDILINNAAG----NFL-APAESLspngfKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGS 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958463 161 WFKQHCAytIAKYGMSMYVLGMAEEF-KGEIAVNALWPKTAIHTAAMDMLGGPGIE 215
Cdd:cd05369  149 PFQVHSA--AAKAGVDALTRSLAVEWgPYGIRVNAIAPGPIPTTEGMERLAPSGKS 202
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 12-187 9.45e-33

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.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 120.41  E-value: 9.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANiVIAakTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05374    2 VVLITGCSSGIGLALALALAAQGYR-VIA--TARNPDKL-------ESLGELLNDNLEVLELDVTDEESIKAAVKEVIER 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNAsAISLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFkqHCAYTI 170
Cdd:cd05374   72 FGRIDVLVNNA-GYGLFGPLeETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPF--LGPYCA 148

                        170
                 ....*....|....*..
gi 767958463 171 AKYGMSMYVLGMAEEFK 187
Cdd:cd05374  149 SKAALEALSESLRLELA 165
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 8-152 1.39e-32

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.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 119.95  E-value: 1.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEAL-------ADELEAEGGKALVLELDVTDEQQVDAAVER 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd08934   74 TVEALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNIS 138
PRK06138 PRK06138
SDR family oxidoreductase;
6-199 1.43e-32

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 120.26  E-value: 1.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllgtiyTAAEEIEA---VGGKALPCIVDVRDEQQIS 82
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDA-----------EAAERVAAaiaAGGRAFARQGDVGSAEAVE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpVWF 162
Cdd:PRK06138  70 ALVDFVAARWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLAL--AGG 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767958463 163 KQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPKT 199
Cdd:PRK06138 148 RGRAAYVASKGAIASLTRAMALDHATDgIRVNAVAPGT 185
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 8-207 4.66e-32

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.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 119.03  E-value: 4.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEV------VEEIKAVGGKAIAVQADVSKEEDVVALFQS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVA-HILNISPPLNLNPvWfKQHC 166
Cdd:cd05358   75 AIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKgKIINMSSVHEKIP-W-PGHV 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767958463 167 AYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIHTAAMD 207
Cdd:cd05358  153 NYAASKGGVKMMTKTLAQEYAPKgIRVNAIAPgaiNTPINAEAWD 197
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 8-197 6.03e-32

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.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 118.61  E-value: 6.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEE-------KAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpVWFKQHCA 167
Cdd:cd05347   76 IEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSE--LGGPPVPA 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767958463 168 YTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:cd05347  154 YAASKGGVAGLTKALATEWaRHGIQVNAIAP 184
PRK12826 PRK12826
SDR family oxidoreductase;
5-210 1.14e-31

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 117.71  E-value: 1.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK12826   1 TRDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAA-------TAELVEAAGGKARARQVDVRDRAALKAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISP---PLNLNPVW 161
Cdd:PRK12826  74 VAAGVEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSvagPRVGYPGL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767958463 162 fkqhCAYTIAKYGmsmyVLGM----AEEFKGE-IAVNALWPkTAIHTAAMDMLG 210
Cdd:PRK12826 154 ----AHYAASKAG----LVGFtralALELAARnITVNSVHP-GGVDTPMAGNLG 198
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 8-197 1.17e-30

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.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 114.89  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiytAAEEIEA-VGGKALPCIVDVRDEQQISAAVE 86
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGG-----------AAQAVVAqIAGGALALRVDVTDEQQVAALFE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwfKQH 165
Cdd:cd08944   70 RAVEEFGGLDLLVNNAGAMHLTPAIiDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGD--PGY 147

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:cd08944  148 GAYGASKAAIRNLTRTLAAELRHAgIRCNALAP 180
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-217 7.25e-30

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 113.04  E-value: 7.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK12825   1 MGSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAE------ELVEAVEALGRRAQAVQADVTDKAALEAA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNAsAIsltnTLDTPTKRLDL-----MMNVNTRGTYLASKACIPYLKKSKVAHILNISpPLNLNP 159
Cdd:PRK12825  75 VAAAVERFGRIDILVNNA-GI----FEDKPLADMSDdewdeVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNIS-SVAGLP 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463 160 VWFKQhCAYTIAKYGMsmyvLGMA-----EEFKGEIAVNALWPkTAIHTAAMDMLGGPGIESQ 217
Cdd:PRK12825 149 GWPGR-SNYAAAKAGL----VGLTkalarELAEYGITVNMVAP-GDIDTDMKEATIEEAREAK 205
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 8-197 1.08e-29

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 112.53  E-value: 1.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVI--AAKTAQPHpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAV 85
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVnyAGSAAAAD--------ELVAEIEAAGGRAIAVQADVADAAAVTRLF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISppLNLNPVWFKQH 165
Cdd:PRK12937  75 DAAETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG--GRIINLS--TSVIALPLPGY 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK12937 151 GPYAASKAAVEGLVHVLANELRGRgITVNAVAP 183
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 20-211 1.98e-29

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 111.37  E-value: 1.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   20 RGIGKAIALKAAKDGANIVIAAktaqPHPKLLGTiytAAEEIEAVGGKALPCivDVRDEQQISAAVEKAIKKFGGIDILV 99
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTD----LNEALAKR---VEELAEELGAAVLPC--DVTDEEQVEALVAAAVEKFGRLDILV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  100 NNAsAISL---TNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNIS--------PPLNlnpvwfkqhcAY 168
Cdd:pfam13561  77 NNA-GFAPklkGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSsigaervvPNYN----------AY 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767958463  169 TIAKYGMSMYVLGMAEEF--KGeIAVNALWPkTAIHTAAMDMLGG 211
Cdd:pfam13561 144 GAAKAALEALTRYLAVELgpRG-IRVNAISP-GPIKTLAASGIPG 186
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 8-197 3.83e-29

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 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. 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.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 111.38  E-value: 3.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphPKLLGTIytaaEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTIL--PQLPGTA----EEIEARGGKCIPVRCDHSDDDEVEALFER 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 -AIKKFGGIDILVNNA-SAISLTNTLDT------PTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNp 159
Cdd:cd09763   75 vAREQQGRLDILVNNAyAAVQLILVGVAkpfweePPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLE- 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958463 160 vwFKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:cd09763  154 --YLFNVAYGVGKAAIDRMAADMAHELKPHgVAVVSLWP 190
FabG-like PRK07231
SDR family oxidoreductase;
7-215 4.13e-29

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 111.08  E-value: 4.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAvGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAER-------VAAEILA-GGRAIAVAADVSDEADVEAAVA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNAsAISLTNT--LDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNP----V 160
Cdd:PRK07231  74 AALERFGSVDILVNNA-GTTHRNGplLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPrpglG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958463 161 WfkqhcaYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIHTAAMdmlGGPGIE 215
Cdd:PRK07231 153 W------YNASKGAVITLTKALAAELGPDkIRVNAVAPvvvETGLLEAFM---GEPTPE 202
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
6-197 2.67e-27

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 106.42  E-value: 2.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAV 85
Cdd:PRK08226   2 GKLTGKTALITGALQGIGEGIARVFARHGANLILLDISP--------EIEKLADELCGRGHRCTAVVADVRDPASVAAAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpPLNLNPVWFKQH 165
Cdd:PRK08226  74 KRAKEKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMS-SVTGDMVADPGE 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:PRK08226 153 TAYALTKAAIVGLTKSLAVEYaQSGIRVNAICP 185
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 8-197 4.95e-27

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 105.43  E-value: 4.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVI----AAKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISA 83
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVnyasSKAAAE----------EVVAEIEAAGGKAIAVQADVSDPSQVAR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISPPLNLNPVWFk 163
Cdd:cd05362   71 LFDAAEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG--GRIINISSSLTAAYTPN- 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767958463 164 qHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:cd05362  148 -YGAYAGSKAAVEAFTRVLAKELGGRgITVNAVAP 181
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
3-142 1.31e-26

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 109.16  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIA----AKTAQphpkllgtiytAAEEIEAvGGKALPCIVDVRDE 78
Cdd:PRK08324 415 PKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLAdldeEAAEA-----------AAAELGG-PDRALGVACDVTDE 482

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958463  79 QQISAAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKK 142
Cdd:PRK08324 483 AAVQAAFEEAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKA 546
PRK07814 PRK07814
SDR family oxidoreductase;
7-229 1.81e-26

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 104.48  E-value: 1.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTES-------QLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPY-LKKSKVAHILNISPPLNLNPVwfKQH 165
Cdd:PRK07814  80 QAVEAFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLmLEHSGGGSVINISSTMGRLAG--RGF 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEFKGEIAVNALWPKTaIHTAAMDMLGG-PGIESQCRK----------VDIIADAAY 229
Cdd:PRK07814 158 AAYGTAKAALAHYTRLAALDLCPRIRVNAIAPGS-ILTSALEVVAAnDELRAPMEKatplrrlgdpEDIAAAAVY 231
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 6-197 1.91e-26

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). 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.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 103.94  E-value: 1.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVI----AAKTAQPHPKLLGTIytAAEEIEAVGGKALPCIVDVRDEQQI 81
Cdd:cd05353    1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlgGDRKGSGKSSSAADK--VVDEIKAAGGKAVANYDSVEDGEKI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  82 saaVEKAIKKFGGIDILVNNASAI---SLTNTLDtptKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNL- 157
Cdd:cd05353   79 ---VKTAIDAFGRVDILVNNAGILrdrSFAKMSE---EDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLy 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767958463 158 -NpvwFKQhCAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:cd05353  153 gN---FGQ-ANYSAAKLGLLGLSNTLAIEGaKYNITCNTIAP 190
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 8-205 2.40e-26

classical (c) SDR, subgroup 11; 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.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 103.64  E-value: 2.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGTiytaAEEIEAVGGKALP--CIV-DVRDEQQISAA 84
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAE---RLEET----RQSCLQAGVSEKKilLVVaDLTEEEGQDRI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKvAHILNISpplnlnPVWFKQ 164
Cdd:cd05364   74 ISTTLAKFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVS------SVAGGR 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767958463 165 HC----AYTIAKYGMSMYVLGMAEEF--KGeIAVNALWP---KTAIHTAA 205
Cdd:cd05364  147 SFpgvlYYCISKAALDQFTRCTALELapKG-VRVNSVSPgviVTGFHRRM 195
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 12-142 4.14e-26

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 103.22  E-value: 4.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05366    4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNLEE------AAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEK 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKK 142
Cdd:cd05366   78 FGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKK 128
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 13-217 7.05e-26

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


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 102.43  E-value: 7.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVI----AAKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKA 88
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVInyrkSKDAAA----------EVAAEIEELGGKAVVVRADVSQPQDVEEMFAAV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  89 IKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpplNLNPVWFKQH-CA 167
Cdd:cd05359   71 KERFGRLDVLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAIS---SLGSIRALPNyLA 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767958463 168 YTIAKYGMSMYVLGMAEEF-KGEIAVNALWPkTAIHTAAMDMLggPGIESQ 217
Cdd:cd05359  148 VGTAKAALEALVRYLAVELgPRGIRVNAVSP-GVIDTDALAHF--PNREDL 195
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 7-197 9.12e-26

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 102.33  E-value: 9.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKA-------EELEEAAAHLEALGIDALWIAADVADEADIERLAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIP-YLKKSKVAHILNISPPLNL--NPVWFK 163
Cdd:PRK08213  82 ETLERFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKrSMIPRGYGRIINVASVAGLggNPPEVM 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958463 164 QHCAYTIAKYGmsmyVLGMAEEFKGE-----IAVNALWP 197
Cdd:PRK08213 162 DTIAYNTSKGA----VINFTRALAAEwgphgIRVNAIAP 196
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 12-197 1.03e-25

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 101.58  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05357    2 VALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSE------AEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS------PPLNlnpvwfkqH 165
Cdd:cd05357   76 FGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIdamtdrPLTG--------Y 147

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEFKGEIAVNALWP 197
Cdd:cd05357  148 FAYCMSKAALEGLTRSAALELAPNIRVNGIAP 179
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 8-197 1.10e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 101.96  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAE---RLDE----VAAEIDDLGRRALAVPTDITDEDQCANLVAL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAI-SLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKqhc 166
Cdd:PRK07890  76 ALERFGRVDALVNNAFRVpSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYG--- 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 167 AYTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK07890 153 AYKMAKGALLAASQSLATELgpQG-IRVNSVAP 184
PRK06181 PRK06181
SDR family oxidoreductase;
12-233 1.15e-25

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 102.36  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGTiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK06181   3 VVIITGASEGIGRALAVRLARAGAQLVLAARNET---RLASL----AQELADHGGEALVVPTDVSDAEACERLIEAAVAR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNAsAISLTNTLDTpTKRLDLM---MNVNTRGTYLASKACIPYLKKSKvAHILNISPPLNLNPVWFKQhcAY 168
Cdd:PRK06181  76 FGGIDILVNNA-GITMWSRFDE-LTDLSVFervMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRS--GY 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958463 169 TIAKYGMsmyvLGMAEEFKGE-----IAVNALWP---KTAIHTAAMDMLGGPGIESQCRKVDII--ADAAYSIFQ 233
Cdd:PRK06181 151 AASKHAL----HGFFDSLRIEladdgVAVTVVCPgfvATDIRKRALDGDGKPLGKSPMQESKIMsaEECAEAILP 221
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 12-152 1.27e-25

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.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 101.47  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05333    2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAA-------ETVEEIKALGGNAAALEADVSDREAVEALVEKVEAE 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958463  92 FGGIDILVNNAsAIsltnTLDTPTKRL-----DLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd05333   75 FGPVDILVNNA-GI----TRDNLLMRMseedwDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINIS 135
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 13-207 1.92e-25

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.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 100.92  E-value: 1.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSA-------EALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQhcAYTIAK 172
Cdd:cd05360   76 GRIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQA--AYSASK 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767958463 173 YGmsmyVLGMAEEFKGEIAV-NALWPKTAIHTAAMD 207
Cdd:cd05360  154 HA----VRGFTESLRAELAHdGAPISVTLVQPTAMN 185
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 8-207 2.27e-25

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 101.29  E-value: 2.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTaqphPKLLGTIYTAAEEIEAVGGKAlpcivDVRDEQQISAAVEK 87
Cdd:PRK12829   9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVS----EAALAATAARLPGAKVTATVA-----DVADPAQVERVFDT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPT-KRLDLMMNVNTRGTYLASKACIPYLKKSK-VAHILNIS---PPLNLnPVWf 162
Cdd:PRK12829  80 AVERFGGLDVLVNNAGIAGPTGGIDEITpEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALSsvaGRLGY-PGR- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767958463 163 kQHcaYTIAKYGMSMYVLGMAEEF-KGEIAVNALWPkTAIHTAAMD 207
Cdd:PRK12829 158 -TP--YAASKWAVVGLVKSLAIELgPLGIRVNAILP-GIVRGPRMR 199
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 6-212 2.49e-25

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 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.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 100.93  E-value: 2.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIytaaeeieavGGKALPCIVDVRDEQQISAAV 85
Cdd:cd05345    1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI----------GEAAIAIQADVTKRADVEAMV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAISL-TNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNP----V 160
Cdd:cd05345   71 EAALSKFGRLDILVNNAGITHRnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPrpglT 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767958463 161 WfkqhcaYTIAKYGMSMYVLGMAEEF-KGEIAVNALWPkTAIHTAAMDMLGGP 212
Cdd:cd05345  151 W------YNASKGWVVTATKAMAVELaPRNIRVNCLCP-VAGETPLLSMFMGE 196
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 10-184 3.03e-25

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical 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 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.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 100.41  E-value: 3.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGTIYtAAEEIEAVGGKALPCI-VDVRDEQQISAAVEKA 88
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSES---KLEEAVE-EIEAEANASGQKVSYIsADLSDYEEVEQAFAQA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  89 IKKFGGIDILVNNA-SAISLtNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHCA 167
Cdd:cd08939   77 VEKGGPPDLVVNCAgISIPG-LFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVG--IYGYSA 153

                        170
                 ....*....|....*..
gi 767958463 168 YTIAKYGmsmyVLGMAE 184
Cdd:cd08939  154 YCPSKFA----LRGLAE 166
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 8-152 9.24e-25

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. 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.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 99.58  E-value: 9.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllgtiytaaEEIEAV------GGKALPCIV--DVRDEQ 79
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARRE--------------ERLEEVksecleLGAPSPHVVplDMSDLE 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  80 QISAAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd05332   67 DAEQVVEEALKLFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVS 139
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 5-207 1.15e-24

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 99.02  E-value: 1.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIytaAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK12827   1 MASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAV---AAGIEAAGGKALGLAFDVRDFAATRAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVA-HILNISpPLNLNPVWFK 163
Cdd:PRK12827  78 LDAGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGgRIVNIA-SVAGVRGNRG 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767958463 164 QhCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPkTAIHTAAMD 207
Cdd:PRK12827 157 Q-VNYAASKAGLIGLTKTLANELAPRgITVNAVAP-GAINTPMAD 199
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 13-215 1.42e-24

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. 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.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 98.80  E-value: 1.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEA-------VAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAiSLTNTLDTPTKRLDLM--MNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWfkQHCAYTI 170
Cdd:cd05365   75 GGITILVNNAGG-GGPKPFDMPMTEEDFEwaFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNV--RIAAYGS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767958463 171 AKYGMSMYVLGMAEEF-KGEIAVNALWPKtAIHTAAMDMLGGPGIE 215
Cdd:cd05365  152 SKAAVNHMTRNLAFDLgPKGIRVNAVAPG-AVKTDALASVLTPEIE 196
PRK07774 PRK07774
SDR family oxidoreductase;
6-197 1.43e-24

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 99.05  E-value: 1.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIA---AKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQIS 82
Cdd:PRK07774   2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVAdinAEGAE----------RVAKQIVADGGTAIAVQVDVSDPDSAK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNAS---AISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPplnlNP 159
Cdd:PRK07774  72 AMADATVSAFGGIDYLVNNAAiygGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSS----TA 147

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958463 160 VWFKQHcAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK07774 148 AWLYSN-FYGLAKVGLNGLTQQLARELGGMnIRVNAIAP 185
PRK07454 PRK07454
SDR family oxidoreductase;
12-249 1.44e-24

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 98.88  E-value: 1.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK07454   8 RALITGASSGIGKATALAFAKAGWDLALVARSQDALEAL-------AAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAiSLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQHCAYTI 170
Cdd:PRK07454  81 FGCPDVLINNAGM-AYTGPLlEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNA--FPQWGAYCV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 171 AKYGMSMYVLGMAEEFKGE-I--------AVN-ALWPKTAIHtAAMD---MLggpgiesqcrKVDIIADAAYSIFQKPKS 237
Cdd:PRK07454 158 SKAALAAFTKCLAEEERSHgIrvctitlgAVNtPLWDTETVQ-ADFDrsaML----------SPEQVAQTILHLAQLPPS 226

                        250
                 ....*....|..
gi 767958463 238 ftgnFVIDENIL 249
Cdd:PRK07454 227 ----AVIEDLTL 234
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 13-184 1.60e-24

classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 98.35  E-value: 1.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllGTIYTAAEEieaVGGKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:cd08929    3 ALVTGASRGIGEATARLLHAEGYRVGICARDE-------ARLAAAAAQ---ELEGVLGLAGDVRDEADVRRAVDAMEEAF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAISLTN--TLDTPTKRLDLMMNvNTRGTYLASKACIPYLKKSKvAHILNISPPLNLNPvwFKQHCAYTI 170
Cdd:cd08929   73 GGLDALVNNAGVGVMKPveELTPEEWRLVLDTN-LTGAFYCIHKAAPALLRRGG-GTIVNVGSLAGKNA--FKGGAAYNA 148

                        170
                 ....*....|....
gi 767958463 171 AKYGMsmyvLGMAE 184
Cdd:cd08929  149 SKFGL----LGLSE 158
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 8-203 4.13e-24

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 97.87  E-value: 4.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEAN------DVAEEIKKAGGEAIAVKGDVTVESDVVNLIQT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVA-HILNISPPLNLNPVWFKQHc 166
Cdd:PRK08936  79 AVKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIKgNIINMSSVHEQIPWPLFVH- 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767958463 167 aYTIAKYGMSMYVLGMAEEF-KGEIAVNALWPKtAIHT 203
Cdd:PRK08936 158 -YAASKGGVKLMTETLAMEYaPKGIRVNNIGPG-AINT 193
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 12-216 4.20e-24

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. 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, 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.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 96.92  E-value: 4.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAakTAQPHPKLLGtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05324    2 VALVTGANRGIGFEIVRQLAKSGPGTVIL--TARDVERGQA----AVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNAsAISLTNTLDTPTKR--LDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPL-NLNPvwfkqhcAY 168
Cdd:cd05324   76 YGGLDILVNNA-GIAFKGFDDSTPTReqARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLgSLTS-------AY 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767958463 169 TIAKYGMSMYVLGMAEEFKGE-IAVNAL---WPKTaihtaamDMLGGPGIES 216
Cdd:cd05324  148 GVSKAALNALTRILAKELKETgIKVNACcpgWVKT-------DMGGGKAPKT 192
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 12-152 4.97e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 99.23  E-value: 4.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK07109  10 VVVITGASAGVGRATARAFARRGAKVVLLARGE-------EGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958463  92 FGGIDILVNNAsAISLTNTLDTPT----KRldlMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK07109  83 LGPIDTWVNNA-MVTVFGPFEDVTpeefRR---VTEVTYLGVVHGTLAALRHMRPRDRGAIIQVG 143
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 7-204 5.58e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 97.42  E-value: 5.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllgTIYTAAEEIEavGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSE--------DVAEVAAQLL--GGNAKGLVCDVSDSQSVEAAVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpVWFKQHC 166
Cdd:PRK06841  82 AVISAFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGV--VALERHV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767958463 167 AYTIAKYGmsmyVLGMAEEFKGE-----IAVNALWPkTAIHTA 204
Cdd:PRK06841 160 AYCASKAG----VVGMTKVLALEwgpygITVNAISP-TVVLTE 197
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
7-152 6.08e-24

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 97.10  E-value: 6.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVI----AAKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQIS 82
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVnyarSRKAAE----------ETAEEIEALGRKALAVKANVGDVEKIK 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK08063  71 EMFAQIDEEFGRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLS 140
PRK05650 PRK05650
SDR family oxidoreductase;
13-197 6.38e-24

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 97.80  E-value: 6.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTaqpHPKLLGTiytaAEEIEAVGGKA--LPCivDVRDEQQISAAVEKAIK 90
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVN---EEGGEET----LKLLREAGGDGfyQRC--DVRDYSQLTALAQACEE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQhcAYTI 170
Cdd:PRK05650  74 KWGGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMS--SYNV 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 171 AKYGmsmyVLGMAEEFKGE-----IAVNALWP 197
Cdd:PRK05650 152 AKAG----VVALSETLLVEladdeIGVHVVCP 179
PRK07326 PRK07326
SDR family oxidoreductase;
8-184 7.29e-24

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 96.62  E-value: 7.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTaqphpklLGTIYTAAEEIEAvGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARD-------QKELEEAAAELNN-KGNVLGLAADVRDEADVQRAVDA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKvAHILNISPPLNLNPvwFKQHCA 167
Cdd:PRK07326  76 IVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNF--FAGGAA 152

                        170
                 ....*....|....*..
gi 767958463 168 YTIAKYGmsmyVLGMAE 184
Cdd:PRK07326 153 YNASKFG----LVGFSE 165
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 12-152 9.65e-24

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 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.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 96.54  E-value: 9.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKG-------AEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd05339   74 VGDVTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIA 134
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 5-197 1.13e-23

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 96.40  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVggkalpcivDVRDEQQISAA 84
Cdd:PRK12828   2 EHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI---------DLVDPQAARRA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISP--PLNLNPVWf 162
Cdd:PRK12828  73 VDEVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAgaALKAGPGM- 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767958463 163 kqhCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK12828 152 ---GAYAAAKAGVARLTEALAAELLDRgITVNAVLP 184
PRK05867 PRK05867
SDR family oxidoreductase;
8-197 2.99e-23

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 95.49  E-value: 2.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLD-------ALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKK-----------SKVAHILNIsppln 156
Cdd:PRK05867  80 VTAELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKqgqggviintaSMSGHIINV----- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767958463 157 lnPVWFKQHCAytiAKYGMSMYVLGMAEEFK-GEIAVNALWP 197
Cdd:PRK05867 155 --PQQVSHYCA---SKAAVIHLTKAMAVELApHKIRVNSVSP 191
PRK08589 PRK08589
SDR family oxidoreductase;
6-211 7.12e-23

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 94.84  E-value: 7.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAV 85
Cdd:PRK08589   2 KRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVS--------ETVDKIKSNGGKAKAYHVDISDEQQVKDFA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAISLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPyLKKSKVAHILNISP----PLNLNpv 160
Cdd:PRK08589  74 SEIKEQFGRVDVLFNNAGVDNAAGRIhEYPVDVFDKIMAVDMRGTFLMTKMLLP-LMMEQGGSIINTSSfsgqAADLY-- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767958463 161 wfkqHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPKTaIHTAAMDMLGG 211
Cdd:PRK08589 151 ----RSGYNAAKGAVINFTKSIAIEYGRDgIRANAIAPGT-IETPLVDKLTG 197
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 6-217 1.05e-22

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 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.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 93.99  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIeavGGKALPCIVDVRDEQQISAAV 85
Cdd:cd05341    1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQA-------AAAEL---GDAARFFHLDVTDEDGWTAVV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwfKQH 165
Cdd:cd05341   71 DTAREAFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGD--PAL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEFKGE---IAVNALWP---KTAIHTAAMDMLGGPGIESQ 217
Cdd:cd05341  149 AAYNASKGAVRGLTKSAALECATQgygIRVNSVHPgyiYTPMTDELLIAQGEMGNYPN 206
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 10-197 1.07e-22

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. 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.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 94.05  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIVIAAKtAQPHPkllgtIYTAAEEIEAV-GGKALPCIVDVRDEQQISAAVEKA 88
Cdd:cd08940    2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGF-GDAAE-----IEAVRAGLAAKhGVKVLYHGADLSKPAAIEDMVAYA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  89 IKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpVWFKQHCAY 168
Cdd:cd08940   76 QRQFGGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGL--VASANKSAY 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958463 169 TIAKYGmsmyVLGMAEEFKGEIA-----VNALWP 197
Cdd:cd08940  154 VAAKHG----VVGLTKVVALETAgtgvtCNAICP 183
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 12-151 1.15e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 93.97  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK07677   3 VVIITGGSSGMGKAMAKRFAEEGANVVITGRTKE-------KLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEK 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPY-LKKSKVAHILNI 151
Cdd:PRK07677  76 FGRIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYwIEKGIKGNIINM 136
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-197 1.25e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 94.71  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVI--------AAKTAQphpkllgtiytaaeEIEAVGGKALPCIVDVR 76
Cdd:PRK06701  41 SGKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIvyldehedANETKQ--------------RVEKEGVKCLLIPGDVS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  77 DEQQISAAVEKAIKKFGGIDILVNNASAISLTNTLDTPT-KRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISP-- 153
Cdd:PRK06701 107 DEAFCKDAVEETVRELGRLDILVNNAAFQYPQQSLEDITaEQLDKTFKTNIYSYFHMTKAALPHLKQG--SAIINTGSit 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767958463 154 PLNLNpvwfKQHCAYTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK06701 185 GYEGN----ETLIDYSATKGAIHAFTRSLAQSLvqKG-IRVNAVAP 225
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 10-145 1.75e-22

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of 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 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.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 93.23  E-value: 1.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAI 89
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPE--------IAEKVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAV 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958463  90 KKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKV 145
Cdd:cd08943   73 LEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGI 128
PRK07201 PRK07201
SDR family oxidoreductase;
6-152 2.17e-22

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 96.56  E-value: 2.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAV 85
Cdd:PRK07201 367 GPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGE-------ALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTV 439

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  86 EKAIKKFGGIDILVNNAS-AI--SLTNTLDtptkRL-DL--MMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK07201 440 KDILAEHGHVDYLVNNAGrSIrrSVENSTD----RFhDYerTMAVNYFGAVRLILGLLPHMRERRFGHVVNVS 508
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
14-142 2.59e-22

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 92.87  E-value: 2.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  14 FITGASRGIGKAIALKAAKDGANIVIA---AKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:PRK08643   6 LVTGAGQGIGFAIAKRLVEDGFKVAIVdynEETAQ----------AAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVD 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767958463  91 KFGGIDILVNNAsAISLTNTLDTPT-KRLDLMMNVNTRGTYLASKACIPYLKK 142
Cdd:PRK08643  76 TFGDLNVVVNNA-GVAPTTPIETITeEQFDKVYNINVGGVIWGIQAAQEAFKK 127
PRK07063 PRK07063
SDR family oxidoreductase;
5-197 4.25e-22

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 92.42  E-value: 4.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAV--GGKALPCIVDVRDEQQIS 82
Cdd:PRK07063   2 MNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAER-------AAAAIARDvaGARVLAVPADVTDAASVA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISP--PLNLNPv 160
Cdd:PRK07063  75 AAVAAAEEAFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASthAFKIIP- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767958463 161 wfkqHC-AYTIAKYGmsmyVLGMAEEFKGEIA-----VNALWP 197
Cdd:PRK07063 154 ----GCfPYPVAKHG----LLGLTRALGIEYAarnvrVNAIAP 188
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 7-228 6.30e-22

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 91.94  E-value: 6.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK07576   6 DFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQE-------KVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKvAHILNISPPLNLNPVWFKQH- 165
Cdd:PRK07576  79 QIADEFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG-ASIIQISAPQAFVPMPMQAHv 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958463 166 CAytiAKYGMSMYVLGMAEEFKGE-IAVNALWPKTAIHTAAMDMLgGPGIESQCR-----------KVDIIADAA 228
Cdd:PRK07576 158 CA---AKAGVDMLTRTLALEWGPEgIRVNSIVPGPIAGTEGMARL-APSPELQAAvaqsvplkrngTKQDIANAA 228
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 3-215 6.86e-22

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 91.83  E-value: 6.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQIS 82
Cdd:PRK06113   4 SDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINAD-------AANHVVDEIQQLGGQAFACRCDITSEQELS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAiSLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwf 162
Cdd:PRK06113  77 ALADFALSKLGKVDILVNNAGG-GGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKN-- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958463 163 KQHCAYTIAKYGMSMYVLGMAEEFkGE--IAVNALWPKtAIHTAAMDMLGGPGIE 215
Cdd:PRK06113 154 INMTSYASSKAAASHLVRNMAFDL-GEknIRVNGIAPG-AILTDALKSVITPEIE 206
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 8-197 7.08e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 92.05  E-value: 7.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQE-------LVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS---PPLNLNPVwfkq 164
Cdd:PRK07097  81 IEKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICsmmSELGRETV---- 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958463 165 hCAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:PRK07097 157 -SAYAAAKGGLKMLTKNIASEYgEANIQCNGIGP 189
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 12-152 1.35e-21

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.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 91.18  E-value: 1.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05344    3 VALVTAASSGIGLAIARALAREGARVAICARNRENLER-------AASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDA 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd05344   76 FGRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNIS 136
PRK08628 PRK08628
SDR family oxidoreductase;
13-152 1.52e-21

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 90.79  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtiYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:PRK08628  10 VIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPD--------DEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKF 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  93 GGIDILVNNASA---ISLTNTLDTPTKRLDLmmnvNTRGTYLASKACIPYLKKSKVAhILNIS 152
Cdd:PRK08628  82 GRIDGLVNNAGVndgVGLEAGREAFVASLER----NLIHYYVMAHYCLPHLKASRGA-IVNIS 139
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 8-175 2.81e-21

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 90.34  E-value: 2.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQD-------GANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNAsAISLTNTLDT-PTKRLDLMMNVNTRGTYLASKACIPYLKKSKV-AHILNISPPLNLNPVWFKQh 165
Cdd:PRK13394  78 VAERFGSVDILVSNA-GIQIVNPIENySFADWKKMQAIHVDGAFLTTKAALKHMYKDDRgGVVIYMGSVHSHEASPLKS- 155

                        170
                 ....*....|
gi 767958463 166 cAYTIAKYGM 175
Cdd:PRK13394 156 -AYVTAKHGL 164
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-152 3.10e-21

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.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 90.43  E-value: 3.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIA-AKTAQPHPKllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISA 83
Cdd:cd05355   21 SGKLKGKKALITGGDSGIGRAVAIAFAREGADVAINyLPEEEDDAE------ETKKLIEEEGRKCLLIPGDLGDESFCRD 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAIKKFGGIDILVNNASAISLTNTLDT-PTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNIS 152
Cdd:cd05355   95 LVKEVVKEFGKLDILVNNAAYQHPQESIEDiTTEQLEKTFRTNIFSMFYLTKAALPHLKKG--SSIINTT 162
PRK06124 PRK06124
SDR family oxidoreductase;
8-197 4.05e-21

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 89.77  E-value: 4.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAA-------TLEAAVAALRAAGGAAEALAFDIADEEAVAAAFAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPlnLNPVWFKQHCA 167
Cdd:PRK06124  82 IDAEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSI--AGQVARAGDAV 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767958463 168 YTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK06124 160 YPAAKQGLTGLMRALAAEFGPHgITSNAIAP 190
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 6-197 4.44e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 89.60  E-value: 4.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAV 85
Cdd:PRK07478   2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQL-------VAEIRAEGGEAVALAGDVRDEAYAKALV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNA---------SAISLTNTLDTptkrldlmMNVNTRGTYLASKACIPYLKK----------SKVA 146
Cdd:PRK07478  75 ALAVERFGGLDIAFNNAgtlgemgpvAEMSLEGWRET--------LATNLTSAFLGAKHQIPAMLArgggsliftsTFVG 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767958463 147 HilnispplnlnPVWFKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK07478 147 H-----------TAGFPGMAAYAASKAGLIGLTQVLAAEYGAQgIRVNALLP 187
PRK07035 PRK07035
SDR family oxidoreductase;
5-197 4.95e-21

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 89.30  E-value: 4.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAgctvFITGASRGIGKAIALKAAKDGANIVIAAKtaqphpKLLGtIYTAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK07035   7 TGKIA----LVTGASRGIGEAIAKLLAQQGAHVIVSSR------KLDG-CQAVADAIVAAGGKAEALACHIGEMEQIDAL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAIS-LTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFK 163
Cdd:PRK07035  76 FAHIRERHGRLDILVNNAAANPyFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQ 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958463 164 QhcAYTIAKYGmsmyVLGMAEEFKGE-----IAVNALWP 197
Cdd:PRK07035 156 G--IYSITKAA----VISMTKAFAKEcapfgIRVNALLP 188
PRK06947 PRK06947
SDR family oxidoreductase;
12-202 6.52e-21

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 89.09  E-value: 6.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIA-AKTAQphpkllgtiytAAEE----IEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK06947   4 VVLITGASRGIGRATAVLAAARGWSVGINyARDAA-----------AAEEtadaVRAAGGRACVVAGDVANEADVIAMFD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAH---ILNISPPLNL--NPv 160
Cdd:PRK06947  73 AVQSAFGRLDALVNNAGIVAPSMPLaDMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRlgSP- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767958463 161 wfKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIH 202
Cdd:PRK06947 152 --NEYVDYAGSKGAVDTLTLGLAKELGPHgVRVNAVRPgliETEIH 195
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-193 9.38e-21

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 88.61  E-value: 9.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiyTAAEE-IEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVVVNYHQSE----------DAAEAlADELGDRAIALQADVTDREQVQAMFATATE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFG-GIDILVNNASAISLTN-----TLDTPT-KRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwFK 163
Cdd:PRK08642  77 HFGkPITTVVNNALADFSFDgdarkKADDITwEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPV-VP 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767958463 164 QHcAYTIAKYGMSMYVLGMAEEFKGE-IAVN 193
Cdd:PRK08642 156 YH-DYTTAKAALLGLTRNLAAELGPYgITVN 185
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 6-151 1.20e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 88.52  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGA-NIVIAAKTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK06198   2 GRLDGKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQ-------AAELEALGAKAVFVQADLSDVEDCRRV 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVA-HILNI 151
Cdd:PRK06198  75 VAAADEAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEgTIVNI 142
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 7-197 1.98e-20

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. 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.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 87.98  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEieavGGKALPCivDVRDEQQISAAVE 86
Cdd:cd08933    6 RYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPG----SCKFVPC--DVTKEEDIKTLIS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLD-TPTKRLDLMMNVNTRGTYLASKACIPYLKKSKvAHILNISPPLNLnpVWFKQH 165
Cdd:cd08933   80 VTVERFGRIDCLVNNAGWHPPHQTTDeTSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVGS--IGQKQA 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 166 CAYTIAKYGMSMYVLGMA-EEFKGEIAVNALWP 197
Cdd:cd08933  157 APYVATKGAITAMTKALAvDESRYGVRVNCISP 189
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 13-197 3.25e-20

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.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 86.97  E-value: 3.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAakTAQPHpkllgtiyTAAEEIEAVGGKALPCIV---DVRDE-QQISAAVEKA 88
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIA--TCRDP--------SAATELAALGASHSRLHIlelDVTDEiAESAEAVAER 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  89 IKkFGGIDILVNNASAISLTNTLDTPTKR-LDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPP---LNLNPvwFKQ 164
Cdd:cd05325   71 LG-DAGLDVLINNAGILHSYGPASEVDSEdLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRvgsIGDNT--SGG 147

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958463 165 HCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:cd05325  148 WYSYRASKAALNMLTKSLAVELKRDgITVVSLHP 181
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 15-216 3.53e-20

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]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 87.38  E-value: 3.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   15 ITGASRGIGKAIALKAAKDGANIVI----AAKTAQPHPklLGTiytaAEEIEAV----GGKALPCIVDVRDEQQISAAVE 86
Cdd:TIGR04504   6 VTGAARGIGAATVRRLAADGWRVVAvdlcADDPAVGYP--LAT----RAELDAVaaacPDQVLPVIADVRDPAALAAAVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   87 KAIKKFGGIDILVNNASAISLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPylkkskvaHILNISPPlnlnpvwfkQH 165
Cdd:TIGR04504  80 LAVERWGRLDAAVAAAGVIAGGRPLwETTDAELDLLLDVNLRGVWNLARAAVP--------AMLARPDP---------RG 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  166 C------------------AYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIHTAAMDMLGGPGIES 216
Cdd:TIGR04504 143 GrfvavasaaatrglphlaAYCAAKHAVVGLVRGLAADLGGTgVTANAVSPgstRTAMLAATARLYGLTDVEE 215
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 12-152 4.69e-20

classical (c) SDR, subgroup 5; 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.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 86.57  E-value: 4.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05346    2 TVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQEL------ADELGAKFPVKVLPLQLDVSDRESIEAALENLPEE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958463  92 FGGIDILVNNAS-AISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd05346   76 FRDIDILVNNAGlALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLG 137
PRK06128 PRK06128
SDR family oxidoreductase;
5-197 7.86e-20

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 87.22  E-value: 7.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIaaktaqphpKLLGTIYTAAEE----IEAVGGKALPCIVDVRDEQQ 80
Cdd:PRK06128  50 FGRLQGRKALITGADSGIGRATAIAFAREGADIAL---------NYLPEEEQDAAEvvqlIQAEGRKAVALPGDLKDEAF 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  81 ISAAVEKAIKKFGGIDILVNNAS-AISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISPPLNLNP 159
Cdd:PRK06128 121 CRQLVERAVKELGGLDILVNIAGkQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPG--ASIINTGSIQSYQP 198

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958463 160 VwfKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK06128 199 S--PTLLDYASTKAAIVAFTKALAKQVAEKgIRVNAVAP 235
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-197 1.00e-19

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 85.99  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiyTAAEEIEAVGGKALPCivDVRDEQQISAAV 85
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAE----------NEAKELREKGVFTIKC--DVGNRDQVKKSK 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwFKQH 165
Cdd:PRK06463  71 EVVEKEFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTA-AEGT 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:PRK06463 150 TFYAITKAGIIILTRRLAFELgKYGIRVNAVAP 182
PRK09135 PRK09135
pteridine reductase; Provisional
 13-197 1.08e-19

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 85.75  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytaAEEIEAV-GGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADAL------AAELNALrPGSAAALQADLLDPDALPELVAACVAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAhILNISPPLNLNPvwFKQHCAYTIA 171
Cdd:PRK09135  83 FGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGA-IVNITDIHAERP--LKGYPVYCAA 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 172 KYGMSMYVLGMAEEFKGEIAVNA------LWP 197
Cdd:PRK09135 160 KAALEMLTRSLALELAPEVRVNAvapgaiLWP 191
PRK06398 PRK06398
aldose dehydrogenase; Validated
 8-208 2.16e-19

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 85.27  E-value: 2.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANiVIAAKTAQPHpkllgtiYTAAEEIEavggkalpciVDVRDEQQISAAVEK 87
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSN-VINFDIKEPS-------YNDVDYFK----------VDVSNKEQVIKGIDY 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpVWFKQHCA 167
Cdd:PRK06398  66 VISKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSF--AVTRNAAA 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767958463 168 YTIAKYGMSMYVLGMAEEFKGEIAVNALWPKTaIHTAAMDM 208
Cdd:PRK06398 144 YVTSKHAVLGLTRSIAVDYAPTIRCVAVCPGS-IRTPLLEW 183
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 14-152 2.38e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 85.47  E-value: 2.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  14 FITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKFG 93
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTA----------TLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958463  94 GIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK08263  77 RLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQIS 135
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-197 4.04e-19

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 84.24  E-value: 4.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK12745   4 VALVTGGRRGIGLGIARALAAAGFDLAINDRPDDE------ELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNA--SAISLTNTLDTPTKRLDLMMNVNTRGTYL----ASKACI--PYLKKSKVAHILNISpplNLNPVWFK 163
Cdd:PRK12745  78 WGRIDCLVNNAgvGVKVRGDLLDLTPESFDRVLAINLRGPFFltqaVAKRMLaqPEPEELPHRSIVFVS---SVNAIMVS 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767958463 164 -QHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK12745 155 pNRGEYCISKAGLSMAAQLFAARLAEEgIGVYEVRP 190
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 9-199 4.30e-19

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).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 84.06  E-value: 4.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   9 AGCTVFITGASRGIGKAIALKAAKDGANiVIAAktaqphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQisaaVEKA 88
Cdd:cd05368    1 DGKVALITAAAQGIGRAIALAFAREGAN-VIAT-----------DINEEKLKELERGPGITTRVLDVTDKEQ----VAAL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  89 IKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpPLNLNPVWFKQHCAY 168
Cdd:cd05368   65 AKEEGRIDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMS-SVASSIKGVPNRFVY 143

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 169 TIAKYGMSMYVLGMAEEFKGE-IAVNALWPKT 199
Cdd:cd05368  144 STTKAAVIGLTKSVAADFAQQgIRCNAICPGT 175
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 5-197 5.16e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 84.00  E-value: 5.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTiyTAAEEIEavggkalpciVDVRDEqqisAA 84
Cdd:PRK07060   4 AFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGE--TGCEPLR----------LDVGDD----AA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVA-HILNISPPLNLnpVWFK 163
Cdd:PRK07060  68 IRAALAAAGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGgSIVNVSSQAAL--VGLP 145

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767958463 164 QHCAYTIAKYGMSMYVLGMAEEFkGE--IAVNALWP 197
Cdd:PRK07060 146 DHLAYCASKAALDAITRVLCVEL-GPhgIRVNSVNP 180
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 12-205 5.85e-19

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. 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 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.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 83.66  E-value: 5.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllgtiYTAAEE-IEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:cd05349    2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRS----------TESAEAvAAEAGERAIAIQADVRDRDQVQAMIEEAKN 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNASAISLTNTLDTPT------KRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQ 164
Cdd:cd05349   72 HFGPVDTIVNNALIDFPFDPDQRKTfdtidwEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYH 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767958463 165 HcaYTIAKYGMSMYVLGMAEEFKGE-IAVNAL---WPKTAIHTAA 205
Cdd:cd05349  152 D--YTTAKAALLGFTRNMAKELGPYgITVNMVsggLLKVTDASAA 194
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-229 5.91e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 86.44  E-value: 5.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytaaeeiEAVGGKALPCIVDVRDEQQIS 82
Cdd:PRK06484 262 PSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLA----------EALGDEHLSVQADITDEAAVE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAIS-LTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVahILNISPPLNLNPvw 161
Cdd:PRK06484 332 SAFAQIQARWGRLDVLVNNAGIAEvFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGGV--IVNLGSIASLLA-- 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 162 FKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPKTaIHTAAMDML---GGPGIESQCRKVDI--------IADAAY 229
Cdd:PRK06484 408 LPPRNAYCASKAAVTMLSRSLACEWAPAgIRVNTVAPGY-IETPAVLALkasGRADFDSIRRRIPLgrlgdpeeVAEAIA 486
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
5-135 8.38e-19

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 83.54  E-value: 8.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIeavGGKALPCIVDVRDEQQISAA 84
Cdd:PRK07067   1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARL-------AALEI---GPAAIAVSLDVTRQDSIDRI 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKA 135
Cdd:PRK07067  71 VAAAVERFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQA 121
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 12-197 9.01e-19

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.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 82.80  E-value: 9.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKtaQPHpkllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd08932    2 VALVTGASRGIGIEIARALARDGYRVSLGLR--NPE---------DLAALSASGGDVEAVPYDARDPEDARALVDALRDR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISP-----PLNLNPVwfkqhc 166
Cdd:cd08932   71 FGRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSlsgkrVLAGNAG------ 144

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 167 aYTIAKYGMSMYVLGMA-EEFKGEIAVNALWP 197
Cdd:cd08932  145 -YSASKFALRALAHALRqEGWDHGVRVSAVCP 175
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 8-152 9.38e-19

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 83.52  E-value: 9.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIA--AKTAQPHPKLLgtiytaaeeieavggkALPCivDVRDEQQISAAV 85
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNAdiHGGDGQHENYQ----------------FVPT--DVSSAEEVNHTV 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958463  86 EKAIKKFGGIDILVNNAsAISLTNTLDTPT----------KRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK06171  69 AEIIEKFGRIDGLVNNA-GINIPRLLVDEKdpagkyelneAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMS 144
PRK07069 PRK07069
short chain dehydrogenase; Validated
 14-152 1.06e-18

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 83.22  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  14 FITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllGTIYTAAEEIEAVG-GKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDINDAA-----GLDAFAAEINAAHGeGVAFAAVQDVTDEAQWQALLAQAADAM 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK07069  78 GGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNIS 137
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 13-228 1.47e-18

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. 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.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 82.35  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHP-KLLGTIYTaaeeieavGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05323    3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAaAELQAINP--------KVKATFVQCDVTSWEQLAAAFKKAIEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNA---SAISLTNTLDTPTKRLDLmMNVN----TRGTYLAskacIPYLKKSKV---AHILNISPPLNLNPVw 161
Cdd:cd05323   75 FGRVDILINNAgilDEKSYLFAGKLPPPWEKT-IDVNltgvINTTYLA----LHYMDKNKGgkgGVIVNIGSVAGLYPA- 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958463 162 fKQHCAYTIAKYGMSMYV--LGMAEEFKGEIAVNALWP---KTAIHTAAMDMLGGPGIESQCRKVDIIADAA 228
Cdd:cd05323  149 -PQFPVYSASKHGVVGFTrsLADLLEYKTGVRVNAICPgftNTPLLPDLVAKEAEMLPSAPTQSPEVVAKAI 219
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-210 1.54e-18

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 82.85  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKtaqphpKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAK------KRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVahILNISPPLNLNPvwFKQHCA 167
Cdd:PRK06077  78 TIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGGA--IVNIASVAGIRP--AYGLSI 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767958463 168 YTIAKYGMSMYVLGMAEEFKGEIAVNALWP---KTAIHTAAMDMLG 210
Cdd:PRK06077 154 YGAMKAAVINLTKYLALELAPKIRVNAIAPgfvKTKLGESLFKVLG 199
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 5-197 1.89e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 82.47  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllGTIYTAAEEieaVGGKALPciVDVRDEQQISAA 84
Cdd:PRK06057   2 SQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDP-------EAGKAAADE---VGGLFVP--TDVTDEDAVNAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNAsAISLTN---TLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVW 161
Cdd:PRK06057  70 FDTAAETYGSVDIAFNNA-GISPPEddsILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767958463 162 FKQhCAYTIAKYGmsmyVLGMAEEFKGEIA-----VNALWP 197
Cdd:PRK06057 149 TSQ-ISYTASKGG----VLAMSRELGVQFArqgirVNALCP 184
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-200 2.16e-18

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 82.48  E-value: 2.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTN--------WDETRRLIEKEGRKVTFVQVDLTKPESAEKVVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQhc 166
Cdd:PRK06935  84 EALEEFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVP-- 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767958463 167 AYTIAKYGmsmyVLGMAEEFKGEIA-----VNALWP---KTA 200
Cdd:PRK06935 162 AYTASKHG----VAGLTKAFANELAayniqVNAIAPgyiKTA 199
PRK07831 PRK07831
SDR family oxidoreductase;
3-202 2.73e-18

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 82.00  E-value: 2.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTGRLAGCTVFITGAS-RGIGKAIALKAAKDGANIVIAaktaQPHPKLLGTiytAAEEIEAVGG----KALPCivDVRD 77
Cdd:PRK07831  10 PGHGLLAGKVVLVTAAAgTGIGSATARRALEEGARVVIS----DIHERRLGE---TADELAAELGlgrvEAVVC--DVTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  78 EQQISAAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAH-ILNISPPLN 156
Cdd:PRK07831  81 EAQVDALIDAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGvIVNNASVLG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767958463 157 lnpvWFKQH--CAYTIAKYG-MSMYVLGMAEEFKGEIAVNALWPKTAIH 202
Cdd:PRK07831 161 ----WRAQHgqAHYAAAKAGvMALTRCSALEAAEYGVRINAVAPSIAMH 205
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 7-243 3.13e-18

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. 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.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 82.01  E-value: 3.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiytAAEEIEAVGGKALPCIV-DVRDEQQISAAV 85
Cdd:cd05348    1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAE-----------KVAELRADFGDAVVGVEgDVRSLADNERAV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAIS-LTNTLDTPTKRL----DLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpplnlNPV 160
Cdd:cd05348   70 ARCVERFGKLDCFIGNAGIWDySTSLVDIPEEKLdeafDELFHINVKGYILGAKAALPALYATEGSVIFTVS-----NAG 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 161 WFKQHCA--YTIAKYGMSMYVLGMAEEFKGEIAVNALWPkTAIHTaamDMLGGPGIESQCRKVDI--IADAAYSI----- 231
Cdd:cd05348  145 FYPGGGGplYTASKHAVVGLVKQLAYELAPHIRVNGVAP-GGMVT---DLRGPASLGQGETSISTppLDDMLKSIlplgf 220

                        250
                 ....*....|..
gi 767958463 232 FQKPKSFTGNFV 243
Cdd:cd05348  221 APEPEDYTGAYV 232
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 12-152 3.52e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 82.27  E-value: 3.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiytAAEEIEAV-GGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:PRK06180   6 TWLITGVSSGFGRALAQAALAAGHRVVGTVRSEA-----------ARADFEALhPDRALARLLDVTDFDAIDAVVADAEA 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958463  91 KFGGIDILVNNA-----SAISltntlDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK06180  75 TFGPIDVLVNNAgygheGAIE-----ESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNIT 136
PRK06484 PRK06484
short chain dehydrogenase; Validated
 13-197 3.85e-18

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 84.13  E-value: 3.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVE----------RARERADSLGPDHHALAMDVSDEAQIREGFEQLHREF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAI--SLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKV-AHILNISPPLNL--NPvwfkQHCA 167
Cdd:PRK06484  78 GRIDVLVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHgAAIVNVASGAGLvaLP----KRTA 153

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 168 YTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK06484 154 YSASKAAVISLTRSLACEWaaKG-IRVNAVLP 184
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 8-151 5.88e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 80.95  E-value: 5.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAE-------RAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEH 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNI 151
Cdd:PRK08085  80 IEKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINI 143
PRK09242 PRK09242
SDR family oxidoreductase;
7-197 6.25e-18

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 80.95  E-value: 6.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkLLGTIYTAAEEiEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK09242   6 RLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDAD----ALAQARDELAE-EFPEREVHGLAADVSDDEDRRAILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwfkqhc 166
Cdd:PRK09242  81 WVEDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHV------ 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767958463 167 aYTIAKYGMSMYVL-----GMAEEFKGE-IAVNALWP 197
Cdd:PRK09242 155 -RSGAPYGMTKAALlqmtrNLAVEWAEDgIRVNAVAP 190
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 8-188 7.66e-18

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) 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.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 80.43  E-value: 7.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREE-----------RLAEAKKELPNIHTIVLDVGDAESVEALAEA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASA---ISLTNTLDTPTKrLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwFKQ 164
Cdd:cd05370   72 LLSEYPNLDILINNAGIqrpIDLRDPASDLDK-ADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVP--MAA 148

                        170       180
                 ....*....|....*....|....
gi 767958463 165 HCAYTIAKYGMSMYVLGMAEEFKG 188
Cdd:cd05370  149 NPVYCATKAALHSYTLALRHQLKD 172
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 8-197 7.73e-18

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-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.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 80.60  E-value: 7.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGG-KALPCivDVRDEQQISAAVE 86
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACAD-------AAEELSAYGEcIAIPA--DLSSEEGIEALVA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKV----AHILNISPPLNLNPVWf 162
Cdd:cd08942   75 RVAERSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSG- 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767958463 163 KQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:cd08942  154 LENYSYGASKAAVHQLTRKLAKELAGEhITVNAIAP 189
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 7-151 7.95e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 81.14  E-value: 7.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIaaktaqphpkllGTIYTAAEEIEAVG-GKALPCIVDVRDEQQISAAV 85
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAI------------GDLDEALAKETAAElGLVVGGPLDVTDPASFAAFL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958463  86 EKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNI 151
Cdd:PRK07825  70 DAVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNV 135
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 7-152 8.46e-18

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 80.59  E-value: 8.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLlgtiytaaEEIEAvggkALPCIV----DVRDEQQIS 82
Cdd:COG3967    2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREE---KL--------EEAAA----ANPGLHtivlDVADPASIA 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  83 AAVEKAIKKFGGIDILVNNAsAISLTNTLDTPTKRLDL---MMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:COG3967   67 ALAEQVTAEFPDLNVLINNA-GIMRAEDLLDEAEDLADaerEITTNLLGPIRLTAAFLPHLKAQPEAAIVNVS 138
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 12-197 9.70e-18

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. 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.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 80.73  E-value: 9.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKT---AQphpkllgtiyTAAEEIEAVGGKA----LPCivDVRDEQQISAA 84
Cdd:cd05327    3 VVVITGANSGIGKETARELAKRGAHVIIACRNeekGE----------EAAAEIKKETGNAkvevIQL--DLSSLASVRQF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLdtpTKR-LDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISP---------- 153
Cdd:cd05327   71 AEEFLARFPRLDILINNAGIMAPPRRL---TKDgFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSiahragpidf 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767958463 154 --PLNLNPVWFKQHCAYTIAKYGMSMYVLGMAEEFKG-EIAVNALWP 197
Cdd:cd05327  148 ndLDLENNKEYSPYKAYGQSKLANILFTRELARRLEGtGVTVNALHP 194
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 10-187 1.02e-17

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. 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.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 79.95  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGTiytaAEEIEAVGGKALPCIV-DVRDEQQISAAVEKA 88
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQE---KLDAV----AKEIEEKYGVETKTIAaDFSAGDDIYERIEKE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  89 IKkfgGIDI--LVNNAsAISLT---NTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFK 163
Cdd:cd05356   74 LE---GLDIgiLVNNV-GISHSipeYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLL 149

                        170       180
                 ....*....|....*....|....
gi 767958463 164 QHcaYTIAKYGMSMYVLGMAEEFK 187
Cdd:cd05356  150 AT--YSASKAFLDFFSRALYEEYK 171
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 5-101 1.07e-17

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 80.37  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK12823   3 NQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVH--------EVAAELRAAGGEALALTADLETYAGAQAA 74

                         90
                 ....*....|....*..
gi 767958463  85 VEKAIKKFGGIDILVNN 101
Cdd:PRK12823  75 MAAAVEAFGRIDVLINN 91
PRK08264 PRK08264
SDR family oxidoreductase;
8-151 1.09e-17

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 79.93  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGAniviaaktaqphpkllGTIYTAAEEIEAV---GGKALPCIVDVRDEQQISAA 84
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGA----------------AKVYAAARDPESVtdlGPRVVPLQLDVTDPASVAAA 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463  85 VEKAikkfGGIDILVNNASAISLTNTLDTPT-KRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNI 151
Cdd:PRK08264  68 AEAA----SDVTILVNNAGIFRTGSLLLEGDeDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNV 131
PRK06949 PRK06949
SDR family oxidoreductase;
8-197 1.42e-17

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 80.19  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGtiytaaeEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRA-------EIEAEGGAAHVVSLDVTDYQSIKAAVAH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNaSAISLTNTL-DTPTKRLDLMMNVNTRGT-YLASKACIPYLKKSKVA-------HILNISPPLNLN 158
Cdd:PRK06949  80 AETEAGTIDILVNN-SGVSTTQKLvDVTPADFDFVFDTNTRGAfFVAQEVAKRMIARAKGAgntkpggRIINIASVAGLR 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767958463 159 PvwFKQHCAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:PRK06949 159 V--LPQIGLYCMSKAAVVHMTRAMALEWgRHGINVNAICP 196
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 5-197 1.59e-17

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the 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.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 79.86  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAgctvFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:cd05343    5 RGRVA----LVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEAL------AAECQSAGYPTLFPYQCDLSNEEQILSM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKV--AHILNISPPLNLNPVWF 162
Cdd:cd05343   75 FSAIRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGHRVPPV 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767958463 163 KQHCAYTIAKYGMSMYVLGMAEEF---KGEIAVNALWP 197
Cdd:cd05343  155 SVFHFYAATKHAVTALTEGLRQELreaKTHIRATSISP 192
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 5-197 1.83e-17

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 80.00  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiytAAEEIEAVGGKALPCIV-DVRDEQQISA 83
Cdd:PRK06200   1 MGWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAE-----------KLASLRQRFGDHVLVVEgDVTSYADNQR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAIKKFGGIDILVNNAsAI--SLTNTLDTPTKRL----DLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpplnl 157
Cdd:PRK06200  70 AVDQTVDAFGKLDCFVGNA-GIwdYNTSLVDIPAETLdtafDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLS----- 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767958463 158 NPVWFKQHCA--YTIAKYGmsmyVLGM----AEEFKGEIAVNALWP 197
Cdd:PRK06200 144 NSSFYPGGGGplYTASKHA----VVGLvrqlAYELAPKIRVNGVAP 185
PRK12743 PRK12743
SDR family oxidoreductase;
15-208 2.65e-17

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 79.31  E-value: 2.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  15 ITGASRGIGKAIALKAAKDGANIVIA----AKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:PRK12743   7 VTASDSGIGKACALLLAQQGFDIGITwhsdEEGAK----------ETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASK-ACIPYLKKSKVAHILNISPPLNLNPVwfKQHCAYT 169
Cdd:PRK12743  77 RLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQiAARHMVKQGQGGRIINITSVHEHTPL--PGASAYT 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767958463 170 IAKYGMSMYVLGMAEEF-KGEIAVNALWPKtAIHTAAMDM 208
Cdd:PRK12743 155 AAKHALGGLTKAMALELvEHGILVNAVAPG-AIATPMNGM 193
PRK05855 PRK05855
SDR family oxidoreductase;
5-128 3.83e-17

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 81.18  E-value: 3.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVI-------AAKTAqphpkllgtiytaaEEIEAVGGKALPCIVDVRD 77
Cdd:PRK05855 310 RGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVAsdideaaAERTA--------------ELIRAAGAVAHAYRVDVSD 375

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767958463  78 EQQISAAVEKAIKKFGGIDILVNNAsAISLT-NTLDTPTKRLDLMMNVNTRG 128
Cdd:PRK05855 376 ADAMEAFAEWVRAEHGVPDIVVNNA-GIGMAgGFLDTSAEDWDRVLDVNLWG 426
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 1-197 4.31e-17

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 79.17  E-value: 4.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   1 MLPNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQ 80
Cdd:PRK08277   1 MMPNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAV-------VAEIKAAGGEALAVKADVLDKES 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  81 ISAAVEKAIKKFGGIDILVN-------NASAISLTNTLDTPTKRL-DL-------MMNVNTRGTYLASKACIPYLKKSKV 145
Cdd:PRK08277  74 LEQARQQILEDFGPCDILINgaggnhpKATTDNEFHELIEPTKTFfDLdeegfefVFDLNLLGTLLPTQVFAKDMVGRKG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463 146 AHILNISP-----PLNLNPvwfkqhcAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK08277 154 GNIINISSmnaftPLTKVP-------AYSAAKAAISNFTQWLAVHFAKVgIRVNAIAP 204
PRK06139 PRK06139
SDR family oxidoreductase;
5-214 5.27e-17

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 79.76  E-value: 5.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK06139   2 MGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEE-------ALQAVAEECRALGAEVLVVPTDVTDADQVKAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIsppLNLNPvWFKQ 164
Cdd:PRK06139  75 ATQAASFGGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINM---ISLGG-FAAQ 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767958463 165 --HCAYTIAKYGMSmyvlGMAEEFKGEIAVnalWPKtaIHT-----AAMDMlggPGI 214
Cdd:PRK06139 151 pyAAAYSASKFGLR----GFSEALRGELAD---HPD--IHVcdvypAFMDT---PGF 195
PRK06182 PRK06182
short chain dehydrogenase; Validated
 12-152 9.08e-17

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 78.08  E-value: 9.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGAniviaaktaqphpkllgTIYTAA------EEIEAVGGKALPciVDVRDEQQISAAV 85
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQGY-----------------TVYGAArrvdkmEDLASLGVHPLS--LDVTDEASIKAAV 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958463  86 EKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK06182  66 DTIIAEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINIS 132
PRK07074 PRK07074
SDR family oxidoreductase;
12-199 1.00e-16

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 77.89  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAaeeieavggKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK07074   4 TALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDA---------RFVPVACDLTDAASLAAALANAAAE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASA---ISLTNTlDTPTKRLDLMMNVNtrGTYLASKACIPYLKKSKVAHILNISpplNLNPVWFKQHCAY 168
Cdd:PRK07074  75 RGPVDVLVANAGAaraASLHDT-TPASWRADNALNLE--AAYLCVEAVLEGMLKRSRGAVVNIG---SVNGMAALGHPAY 148

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 169 TIAKYGMSMYVLGMAEEF-KGEIAVNALWPKT 199
Cdd:PRK07074 149 SAAKAGLIHYTKLLAVEYgRFGIRANAVAPGT 180
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-197 1.02e-16

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 77.61  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   1 MLPNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIViAAKTAQPhpklLGTIytaaEEIEAVGGKALPCIVDVRDEQQ 80
Cdd:PRK08993   1 MILDAFSLEGKVAVVTGCDTGLGQGMALGLAEAGCDIV-GINIVEP----TETI----EQVTALGRRFLSLTADLRKIDG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  81 ISAAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIP-YLKKSKVAHILNISPPLNLN- 158
Cdd:PRK08993  72 IPALLERAVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKhFIAQGNGGKIINIASMLSFQg 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767958463 159 ----PvwfkqhcAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:PRK08993 152 girvP-------SYTASKSGVMGVTRLMANEWaKHNINVNAIAP 188
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 7-230 1.55e-16

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. 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, 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.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 77.11  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAaKTAQPHPKLLgtiytaAEEIEAVGGKALPCivDVRDEQQISAAVE 86
Cdd:cd05326    1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIA-DIDDDAGQAV------AAELGDPDISFVHC--DVTVEADVRAAVD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNT--LDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpplNLNPVW--F 162
Cdd:cd05326   72 TAVARFGRLDIMFNNAGVLGAPCYsiLETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVA---SVAGVVggL 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463 163 KQHcAYTIAKYGmsmyVLGMAEEFKGEIA-----VNALWPKTaihTAAMDMLGGPGIESQcrKVDIIADAAYS 230
Cdd:cd05326  149 GPH-AYTASKHA----VLGLTRSAATELGehgirVNCVSPYG---VATPLLTAGFGVEDE--AIEEAVRGAAN 211
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 8-247 1.55e-16

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 77.50  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDK-------VAKEITALGGRAIALAADVLDRASLERAREE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASA--------------ISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISP 153
Cdd:cd08935   76 IVAQFGTVDILINGAGGnhpdattdpehyepETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 154 PLNLNPvwFKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIHTAAMDMLGGPGIEsqcRKVDIIADAAY 229
Cdd:cd08935  156 MNAFSP--LTKVPAYSAAKAAVSNFTQWLAVEFATTgVRVNAIAPgffVTPQNRKLLINPDGSYTD---RSNKILGRTPM 230

                        250       260
                 ....*....|....*....|
gi 767958463 230 SIFQKPKSFTGN--FVIDEN 247
Cdd:cd08935  231 GRFGKPEELLGAllFLASEK 250
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 7-207 1.60e-16

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).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 76.99  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIE---AVGGKALPCivDVRDEQQISA 83
Cdd:cd05352    5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEE-------KAEELAkkyGVKTKAYKC--DVSSQESVEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFK 163
Cdd:cd05352   76 TFKQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNRPQ 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767958463 164 QHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIhTAAMD 207
Cdd:cd05352  156 PQAAYNASKAAVIHLAKSLAVEWAKYfIRVNSISPgyiDTDL-TDFVD 202
PRK09134 PRK09134
SDR family oxidoreductase;
11-197 1.83e-16

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 76.89  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  11 CTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVAVHYNRSRDEAEAL------AAEIRALGRRAVALQADLADEAEVRALVARASA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNI--SPPLNLNPVWFkqhcAY 168
Cdd:PRK09134  84 ALGPITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNMidQRVWNLNPDFL----SY 159

                        170       180
                 ....*....|....*....|....*....
gi 767958463 169 TIAKYGMSMYVLGMAEEFKGEIAVNALWP 197
Cdd:PRK09134 160 TLSKAALWTATRTLAQALAPRIRVNAIGP 188
PRK06172 PRK06172
SDR family oxidoreductase;
7-209 1.98e-16

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 76.71  E-value: 1.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK06172   4 TFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEE-------TVALIREAGGEALFVACDVTRDAEVKALVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNAS-AISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpvwfkqh 165
Cdd:PRK06172  77 QTIAAYGRLDYAFNNAGiEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGL-------- 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767958463 166 caytIAKYGMSMY------VLGMA-----EEFKGEIAVNALWPkTAIHTaamDML 209
Cdd:PRK06172 149 ----GAAPKMSIYaaskhaVIGLTksaaiEYAKKGIRVNAVCP-AVIDT---DMF 195
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-197 2.64e-16

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). 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.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 76.33  E-value: 2.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytaaEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:cd05329    3 NLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECL-------TEWREKGFKVEGSVCDVSSRSERQELMD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGG-IDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwfKQH 165
Cdd:cd05329   76 TVASHFGGkLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAV--PSG 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:cd05329  154 APYGATKGALNQLTRSLACEWaKDNIRVNAVAP 186
PRK06114 PRK06114
SDR family oxidoreductase;
7-152 6.12e-16

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 75.59  E-value: 6.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTD------DGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVA 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK06114  79 RTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIA 144
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 7-197 6.26e-16

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 75.43  E-value: 6.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENL------VNELGKEGHDVYAVQADVSKVEDANRLVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAisltnTLDTPTKRL-----DLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNlNPVW 161
Cdd:PRK12935  77 EAVNHFGKVDILVNNAGI-----TRDRTFKKLnredwERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIG-QAGG 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767958463 162 FKQhCAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:PRK12935 151 FGQ-TNYSAAKAGMLGFTKSLALELaKTNVTVNAICP 186
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 6-212 8.41e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 75.48  E-value: 8.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllGTIYTAAE----EIEAVGGKALPCIVDVRDEQQI 81
Cdd:PRK07791   2 GLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGVGLDGS--ASGGSAAQavvdEIVAAGGEAVANGDDIADWDGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  82 SAAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLK-KSKV-----AHILNISPPL 155
Cdd:PRK07791  80 ANLVDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRaESKAgravdARIINTSSGA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958463 156 NLNPVWFKQHcaYTIAKYGMSMYVLGMAEEFK--GeIAVNALWP--KTAIHTAAM-DMLGGP 212
Cdd:PRK07791 160 GLQGSVGQGN--YSAAKAGIAALTLVAAAELGryG-VTVNAIAPaaRTRMTETVFaEMMAKP 218
PRK09072 PRK09072
SDR family oxidoreductase;
7-151 8.94e-16

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 74.98  E-value: 8.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIytaaeeieAVGGKALPCIVDVRDEQQIsAAVE 86
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARL--------PYPGRHRWVVADLTSEAGR-EAVL 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958463  87 KAIKKFGGIDILVNNAsAISLTNTLD--TPTkRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNI 151
Cdd:PRK09072  73 ARAREMGGINVLINNA-GVNHFALLEdqDPE-AIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNV 137
PRK08267 PRK08267
SDR family oxidoreductase;
12-201 9.04e-16

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 74.97  E-value: 9.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDG-------ANIVIAAKTAQPHPKllGTIYTAAeeieavggkalpciVDVRDeqqiSAA 84
Cdd:PRK08267   3 SIFITGAASGIGRATALLFAAEGwrvgaydINEAGLAALAAELGA--GNAWTGA--------------LDVTD----RAA 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKF-----GGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPplnlnp 159
Cdd:PRK08267  63 WDAALADFaaatgGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSS------ 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958463 160 vwfkqhCAYT-----IAKYGMS-MYVLGMAEEFKGE-----IAVNALWP---KTAI 201
Cdd:PRK08267 137 ------ASAIygqpgLAVYSATkFAVRGLTEALDLEwrrhgIRVADVMPlfvDTAM 186
PRK05866 PRK05866
SDR family oxidoreductase;
3-152 9.11e-16

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 75.55  E-value: 9.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTG-RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkLLGTIytaAEEIEAVGG--KALPCivDVRDEQ 79
Cdd:PRK05866  32 PRQPvDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARRED----LLDAV---ADRITRAGGdaMAVPC--DLSDLD 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958463  80 QISAAVEKAIKKFGGIDILVNNAsAISLTNTLDTPTKR---LDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK05866 103 AVDALVADVEKRIGGVDILINNA-GRSIRRPLAESLDRwhdVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVA 177
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 10-197 1.30e-15

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream 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 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.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 74.54  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAI 89
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEE----------RGADFAEAEGPNLFFVHGDVADETLVKFVVYAML 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  90 KKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAhILNISPPLNLNPVWFKQhcAYT 169
Cdd:cd09761   71 EKLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGR-IINIASTRAFQSEPDSE--AYA 147

                        170       180
                 ....*....|....*....|....*...
gi 767958463 170 IAKYGMSMYVLGMAEEFKGEIAVNALWP 197
Cdd:cd09761  148 ASKGGLVALTHALAMSLGPDIRVNCISP 175
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 3-152 2.22e-15

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 73.76  E-value: 2.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTGRLAGCTVFITGASRGIGKAIALKAAKDGANiVIAAKTAqphpkllgtiytaaeEIEAVGGKALPCIVDVRDEQQIS 82
Cdd:PRK08220   1 MNAMDFSGKTVWVTGAAQGIGYAVALAFVEAGAK-VIGFDQA---------------FLTQEDYPFATFVLDVSDAAAVA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK08220  65 QVCQRLLAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVG 134
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 8-197 3.08e-15

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 73.27  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTaqphPKLLGTIYTAAEEIEavggkalPCIVDVRDEQqisaAVEK 87
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRT----QADLDSLVRECPGIE-------PVCVDLSDWD----ATEE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKV-AHILNISPPLNLNPvwFKQHC 166
Cdd:cd05351   70 ALGSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRA--LTNHT 147

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 167 AYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:cd05351  148 VYCSTKAALDMLTKVMALELgPHKIRVNSVNP 179
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 12-152 3.75e-15

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). 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.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 73.14  E-value: 3.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGAnIVIAAKTAQPHPKLLgtiytaAEEIEAVGGKALPCIV-DVRDEQQISAAVEKAIK 90
Cdd:cd08930    4 IILITGAAGLIGKAFCKALLSAGA-RLILADINAPALEQL------KEELTNLYKNRVIALElDITSKESIKELIESYLE 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958463  91 KFGGIDILVNNAsAISLTNTL----DTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd08930   77 KFGRIDILINNA-YPSPKVWGsrfeEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIA 141
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 7-152 4.32e-15

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 73.12  E-value: 4.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytAAeeieAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAV------AA----SLGERARFIATDITDDAAIERAVA 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463  87 KAIKKFGGIDILVNNAsAISLTNTLDTPtkRLDLM--MNVNTRGTYLASKACIPYLKKSKVAhILNIS 152
Cdd:PRK08265  73 TVVARFGRVDILVNLA-CTYLDDGLASS--RADWLaaLDVNLVSAAMLAQAAHPHLARGGGA-IVNFT 136
PRK07806 PRK07806
SDR family oxidoreductase;
6-103 4.56e-15

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 72.83  E-value: 4.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAV 85
Cdd:PRK07806   2 GDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKV------VAEIEAAGGRASAVGADLTDEESVAALM 75

                         90
                 ....*....|....*...
gi 767958463  86 EKAIKKFGGIDILVNNAS 103
Cdd:PRK07806  76 DTAREEFGGLDALVLNAS 93
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 12-237 6.75e-15

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). 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.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 72.42  E-value: 6.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIytaaeeIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDI------IRDAGGSAKAVPTDARDEDEVIALFDLIEEE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHI--------LNISPPLnlnpvwfk 163
Cdd:cd05373   75 IGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIiftgatasLRGRAGF-------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 164 qhCAYTIAKYGMSMYVLGMAEEFKgeiavnalwPKtAIHTAAMDMLGG---PGIESQCRKV------------DIIADAA 228
Cdd:cd05373  147 --AAFAGAKFALRALAQSMARELG---------PK-GIHVAHVIIDGGidtDFIRERFPKRderkeedgildpDAIAEAY 214


                 ....*....
gi 767958463 229 YSIFQKPKS 237
Cdd:cd05373  215 WQLHTQPRS 223
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 3-152 7.30e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 73.08  E-value: 7.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtIYTAAEEIEAvGGKALPCIVDVRDEQQIS 82
Cdd:PRK05872   2 PPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAE-------LAALAAELGG-DDRVLTVVADVTDLAAMQ 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKvAHILNIS 152
Cdd:PRK05872  74 AAAEEAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVS 142
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 7-197 1.02e-14

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 72.18  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSE--------LVHEVLAEILAAGDAAHVHTADLETYAGAQGVVR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLD-TPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNpvwfKQH 165
Cdd:cd08937   73 AAVERFGRVDVLINNVGGTIWAKPYEhYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRG----IYR 148

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:cd08937  149 IPYSAAKGGVNALTASLAFEHARDgIRVNAVAP 181
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 3-135 1.10e-14

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 73.80  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiyTAAEEIEAVGGKALPCIV-----DVRD 77
Cdd:COG3347  418 PKPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGE----------AAEAAAAELGGGYGADAVdatdvDVTA 487

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463  78 EQQISAAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKA 135
Cdd:COG3347  488 EAAVAAAFGFAGLDIGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARA 545
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 12-204 1.55e-14

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.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 71.72  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIaakTAQPHPKLLGTIytaAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd05337    3 VAIVTGASRGIGRAIATELAARGFDIAI---NDLPDDDQATEV---VAEVLAAGRRAIYFQADIGELSDHEALLDQAWED 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNA--SAISLTNTLDTPTKRLDLMMNVNTRGTYL----ASKACIPYLKKSKVAH--ILNISpplNLNPVWFK 163
Cdd:cd05337   77 FGRLDCLVNNAgiAVRPRGDLLDLTEDSFDRLIAINLRGPFFltqaVARRMVEQPDRFDGPHrsIIFVT---SINAYLVS 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767958463 164 QHCA-YTIAKYGMSMYVLGMAEEFKGE-IAVNALWPKTaIHTA 204
Cdd:cd05337  154 PNRGeYCISKAGLSMATRLLAYRLADEgIAVHEIRPGL-IHTD 195
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 12-189 1.61e-14

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an 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.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 71.28  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAktaqphpklLGTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAikk 91
Cdd:cd05354    5 TVLVTGANRGIGKAFVESLLAHGAKKVYAA---------VRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQA--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 fGGIDILVNNASAISLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpVWFKQHCAYTI 170
Cdd:cd05354   73 -KDVDVVINNAGVLKPATLLeEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASL--KNFPAMGTYSA 149

                        170
                 ....*....|....*....
gi 767958463 171 AKYGMSMYVLGMAEEFKGE 189
Cdd:cd05354  150 SKSAAYSLTQGLRAELAAQ 168
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 8-135 2.45e-14

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. 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.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 71.11  E-value: 2.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAaktaqpHPKLLGTIYTAAEeieaVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIA------DINLEAARATAAE----IGPAACAISLDVTDQASIDRCVAA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKA 135
Cdd:cd05363   71 LVDRWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQA 118
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 12-159 2.89e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 71.09  E-value: 2.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIV-----IAAKTAQPHPKLLgtiytaaeeieavggkalpcIVDVRDEQQISAAVE 86
Cdd:PRK06179   6 VALVTGASSGIGRATAEKLARAGYRVFgtsrnPARAAPIPGVELL--------------------ELDVTDDASVQAAVD 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNP 159
Cdd:PRK06179  66 EVIARAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLP 138
PRK06914 PRK06914
SDR family oxidoreductase;
14-152 4.92e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 70.44  E-value: 4.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  14 FITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIyTAAEEIEAVGGKALpcivDVRDEQQISAaVEKAIKKFG 93
Cdd:PRK06914   7 IVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQA-TQLNLQQNIKVQQL----DVTDQNSIHN-FQLVLKEIG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958463  94 GIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINIS 139
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 13-211 7.77e-14

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. 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.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 69.47  E-value: 7.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVGGKAlpcivDVRDEQQISAAVEKAIKKF 92
Cdd:cd05330    6 VLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKA-----DVSDEAQVEAYVDATVEQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAISLTN-TLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwfKQHCAYTIA 171
Cdd:cd05330   81 GRIDGFFNNAGIEGKQNlTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGV--GNQSGYAAA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767958463 172 KYGMSMYVLGMAEEF-KGEIAVNALWPKtAIHTA----AMDMLGG 211
Cdd:cd05330  159 KHGVVGLTRNSAVEYgQYGIRINAIAPG-AILTPmvegSLKQLGP 202
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-152 9.34e-14

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 69.22  E-value: 9.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVI----AAKTAQphpkllgtiytAAEEIEAVGGKALPCIVDVRDEQQIS 82
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALidlnQEKLEE-----------AVAECGALGTEVRGYAANVTDEEDVE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKFGGIDILVNNASAIS---LTNTLDTP-TKRLDL-----MMNVNTRGTYL----ASKACIPyLKKSKVahIL 149
Cdd:PRK08217  71 ATFAQIAEDFGQLNGLINNAGILRdglLVKAKDGKvTSKMSLeqfqsVIDVNLTGVFLcgreAAAKMIE-SGSKGV--II 147


                 ...
gi 767958463 150 NIS 152
Cdd:PRK08217 148 NIS 150
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 7-105 1.10e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 69.30  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPC-IVDVRDeqqiSAAV 85
Cdd:PRK06125   4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDAD-------ALEALAADLRAAHGVDVAVhALDLSS----PEAR 72

                         90       100
                 ....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAI 105
Cdd:PRK06125  73 EQLAAEAGDIDILVNNAGAI 92
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 13-197 1.36e-13

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved 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.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 68.51  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytAAEEIEAVGGKALPCiVDVRDEQQISAAVEKAIKKF 92
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDEL------KAELLNPNPSVEVEI-LDVTDEERNQLVIAELEAEL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLnpVWFKQHCAYTIAK 172
Cdd:cd05350   74 GGLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAAL--RGLPGAAAYSASK 151

                        170       180
                 ....*....|....*....|....*.
gi 767958463 173 YGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:cd05350  152 AALSSLAESLRYDVKKRgIRVTVINP 177
PRK05717 PRK05717
SDR family oxidoreductase;
2-197 2.19e-13

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 68.38  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   2 LPNTGRLAgctvFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaaeeIEAVGGKALPCIVDVRDEQQI 81
Cdd:PRK05717   6 PGHNGRVA----LVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKV----------AKALGENAWFIAMDVADEAQV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  82 SAAVEKAIKKFGGIDILVNNAsaiSLTNTLDTPTKRLDL-----MMNVNTRGTYLASKACIPYLKkskvAHILNIsppLN 156
Cdd:PRK05717  72 AAGVAEVLGQFGRLDALVCNA---AIADPHNTTLESLSLahwnrVLAVNLTGPMLLAKHCAPYLR----AHNGAI---VN 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767958463 157 LNPVWFKQH----CAYTIAKYGMSMYVLGMAEEFKGEIAVNALWP 197
Cdd:PRK05717 142 LASTRARQSepdtEAYAASKGGLLALTHALAISLGPEIRVNAVSP 186
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-197 2.94e-13

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 67.79  E-value: 2.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   2 LPNTGRlagcTVFITGASR--GIGKAIALKAAKDGANIViaAKTAQPHPKLLG------TIYTAAEEIEAVGGKALPCIV 73
Cdd:PRK12748   1 LPLMKK----IALVTGASRlnGIGAAVCRRLAAKGIDIF--FTYWSPYDKTMPwgmhdkEPVLLKEEIESYGVRCEHMEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  74 DVRDEQQISAAVEKAIKKFGGIDILVNNAsAISLTNTLDTPT-KRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK12748  75 DLSQPYAPNRVFYAVSERLGDPSILINNA-AYSTHTRLEELTaEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLT 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767958463 153 PPLNLNPVwfKQHCAYTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK12748 154 SGQSLGPM--PDELAYAATKGAIEAFTKSLAPELaeKG-ITVNAVNP 197
PRK06123 PRK06123
SDR family oxidoreductase;
15-213 3.05e-13

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 67.88  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  15 ITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiyTAAEE----IEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:PRK06123   7 ITGASRGIGAATALLAAERGYAVCLNYLRNR----------DAAEAvvqaIRRQGGEALAVAADVADEADVLRLFEAVDR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNASAISLTNTLD-TPTKRLDLMMNVNTRGTYLASKACIpylKKSKVAH------ILNISP-------Pln 156
Cdd:PRK06123  77 ELGRLDALVNNAGILEAQMRLEqMDAARLTRIFATNVVGSFLCAREAV---KRMSTRHggrggaIVNVSSmaarlgsP-- 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958463 157 lnpvwfKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP---KTAIHTAAmdmlGGPG 213
Cdd:PRK06123 152 ------GEYIDYAASKGAIDTMTIGLAKEVAAEgIRVNAVRPgviYTEIHASG----GEPG 202
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-197 3.74e-13

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 67.62  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytaaEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQ---------AQVEALGRKFHFITADLIQQKDIDSIVSQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGT-YLASKACIPYLKKSKVAHILNISPPLNLN-----Pvw 161
Cdd:PRK12481  77 AVEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVfFLSQAVAKQFVKQGNGGKIINIASMLSFQggirvP-- 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767958463 162 fkqhcAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:PRK12481 155 -----SYTASKSAVMGLTRALATELsQYNINVNAIAP 186
PRK07832 PRK07832
SDR family oxidoreductase;
13-184 5.24e-13

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 67.38  E-value: 5.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtIYTAAEEIEAVGGK-ALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADG-------LAQTVADARALGGTvPEHRALDISDYDAVAAFAADIHAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNAsAISLTNTLDTPTKR-------LDLMMNVNTRGTYLAskaciPYLKKSKVAHILNISPPLNLnpVWFKQ 164
Cdd:PRK07832  76 HGSMDVVMNIA-GISAWGTVDRLTHEqwrrmvdVNLMGPIHVIETFVP-----PMVAAGRGGHLVNVSSAAGL--VALPW 147

                        170       180
                 ....*....|....*....|
gi 767958463 165 HCAYTIAKYGmsmyVLGMAE 184
Cdd:PRK07832 148 HAAYSASKFG----LRGLSE 163
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-152 5.61e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 67.10  E-value: 5.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAgctvFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGtiytAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK07523   9 TGRRA----LVTGSSQGIGYALAEGLAQAGAEVILNGRDPA---KLAA----AAESLKGQGLSAHALAFDVTDHDAVRAA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK07523  78 IDAFEAEIGPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIA 145
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-146 5.73e-13

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 67.88  E-value: 5.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIV---IAAKTAQPhpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAA 84
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVvndVASALDAS---------DVLDEIRAAGAKAVAVAGDISQRATADEL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  85 VEKAIkKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLK-KSKVA 146
Cdd:PRK07792  81 VATAV-GLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRaKAKAA 142
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 8-197 7.03e-13

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. 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.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 66.80  E-value: 7.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIytAAEEIEAVG-----GKAlpcivdvRDEQQIs 82
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATL--QGEGLSVTGtvchvGKA-------EDRERL- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 aaVEKAIKKFGGIDILVNNAsAISL--TNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSK------VAHILNISPP 154
Cdd:cd08936   78 --VATAVNLHGGVDILVSNA-AVNPffGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGggsvviVSSVAAFHPF 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767958463 155 LNLNPvwfkqhcaYTIAKYGMsmyvLGMAEEFKGEIA-----VNALWP 197
Cdd:cd08936  155 PGLGP--------YNVSKTAL----LGLTKNLAPELAprnirVNCLAP 190
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-199 7.82e-13

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 66.32  E-value: 7.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   6 GRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIEAVGgkalpcivDVRDEQQISAAV 85
Cdd:PRK05786   1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGNIHYVVG--------DVSSTESARNVI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAIsLTNTLDTPtKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISPPLNLNPVWfKQH 165
Cdd:PRK05786  73 EKAAKVLNAIDGLVVTVGGY-VEDTVEEF-SGLEEMLTNHIKIPLYAVNASLRFLKEG--SSIVLVSSMSGIYKAS-PDQ 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPKT 199
Cdd:PRK05786 148 LSYAVAKAGLAKAVEILASELLGRgIRVNGIAPTT 182
PLN02253 PLN02253
xanthoxin dehydrogenase
 7-197 8.57e-13

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 67.16  E-value: 8.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytaaeeiEAVGGKALPCIV--DVRDEQQISAA 84
Cdd:PLN02253  15 RLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVC----------DSLGGEPNVCFFhcDVTVEDDVSRA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNA--SAISLTNTLDTPTKRLDLMMNVNTRGTYL----ASKACIPyLKKSKVAHILNISPPL-NL 157
Cdd:PLN02253  85 VDFTVDKFGTLDIMVNNAglTGPPCPDIRNVELSEFEKVFDVNVKGVFLgmkhAARIMIP-LKKGSIVSLCSVASAIgGL 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767958463 158 NPvwfkqHcAYTIAKYGmsmyVLGMAEEFKGE-----IAVNALWP 197
Cdd:PLN02253 164 GP-----H-AYTGSKHA----VLGLTRSVAAElgkhgIRVNCVSP 198
PRK12742 PRK12742
SDR family oxidoreductase;
1-197 8.96e-13

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 66.32  E-value: 8.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   1 MLPNTGRlagcTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiyTAAEEIEA-VGGKALPciVDVRDEQ 79
Cdd:PRK12742   1 MGAFTGK----KVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSK----------DAAERLAQeTGATAVQ--TDSADRD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  80 QISAAVekaiKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISpPLNLNP 159
Cdd:PRK12742  65 AVIDVV----RKSGALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG--GRIIIIG-SVNGDR 137

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958463 160 VWFKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK12742 138 MPVAGMAAYAASKSALQGMARGLARDFGPRgITINVVQP 176
PRK07856 PRK07856
SDR family oxidoreductase;
8-197 1.32e-12

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 66.11  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllgtiytaAEEIEAVGGKALPCivDVRDEQQISAAVEK 87
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRA-------------PETVDGRPAEFHAA--DVRDPDQVAALVDA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKK-SKVAHILNISPPLNLNPVwfKQHC 166
Cdd:PRK07856  69 IVERHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSVSGRRPS--PGTA 146

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767958463 167 AYTIAKYGMSMYVLGMAEEFKGEIAVNALWP 197
Cdd:PRK07856 147 AYGAAKAGLLNLTRSLAVEWAPKVRVNAVVV 177
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 15-135 1.61e-12

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. 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.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 65.77  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  15 ITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKFGG 94
Cdd:cd05371    7 VTGGASGLGLATVERLLAQGAKVVILDLPNSP-----------GETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGR 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767958463  95 IDILVNNA---SAISLTNTLDTPTKRLDLM---MNVNTRGTY----LASKA 135
Cdd:cd05371   76 LDIVVNCAgiaVAAKTYNKKGQQPHSLELFqrvINVNLIGTFnvirLAAGA 126
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 8-125 2.84e-12

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 66.40  E-value: 2.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANiVIAAKTAQphpkllgtiytAAEEIEAV----GGKALPCivDVRDEQQISA 83
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAH-VVCLDVPA-----------AGEALAAVanrvGGTALAL--DITAPDAPAR 273

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767958463  84 AVEKAIKKFGGIDILVNNAsAISLTNTL-DTPTKRLDLMMNVN 125
Cdd:PRK08261 274 IAEHLAERHGGLDIVVHNA-GITRDKTLaNMDEARWDSVLAVN 315
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 12-188 3.23e-12

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. 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.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 64.61  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAkTAQPHPKLLGTiytaaeEIEAVGGKALPCIV-DVRDEQQISAAVEKAIK 90
Cdd:cd05367    1 VIILTGASRGIGRALAEELLKRGSPSVVVL-LARSEEPLQEL------KEELRPGLRVTTVKaDLSDAAGVEQLLEAIRK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNASA---ISLTNTLDtpTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAH-ILNISPPLNLNPvwFKQHC 166
Cdd:cd05367   74 LDGERDLLINNAGSlgpVSKIEFID--LDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKtVVNVSSGAAVNP--FKGWG 149

                        170       180
                 ....*....|....*....|..
gi 767958463 167 AYTIAKYGMSMYVLGMAEEFKG 188
Cdd:cd05367  150 LYCSSKAARDMFFRVLAAEEPD 171
PRK08703 PRK08703
SDR family oxidoreductase;
8-197 4.13e-12

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 64.57  E-value: 4.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKtaqpHPKLLGTIYtaaEEIEAVGGK---ALPC-IVDVRDEQ--QI 81
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVAR----HQKKLEKVY---DAIVEAGHPepfAIRFdLMSAEEKEfeQF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  82 SAAVEKAIKkfGGIDILVNNASAISLTNTLDtpTKRLDLMMN---VNTRGTYLASKACIPYLKKSKVAHILNI--SPPLN 156
Cdd:PRK08703  77 AATIAEATQ--GKLDGIVHCAGYFYALSPLD--FQTVAEWVNqyrINTVAPMGLTRALFPLLKQSPDASVIFVgeSHGET 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767958463 157 LNPVWfkqhCAYTIAKYGMSMYVLGMAEEFK--GEIAVNALWP 197
Cdd:PRK08703 153 PKAYW----GGFGASKAALNYLCKVAADEWErfGNLRANVLVP 191
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 10-152 5.11e-12

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 64.54  E-value: 5.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGG--KALPCIVDVRDEQQISAAVEK 87
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEE-------ARKEIETESGnqNIFLHIVDMSDPKQVWEFVEE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958463  88 AIKKFGGIDILVNNASAisLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd09808   74 FKEEGKKLHVLINNAGC--MVNKRELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVS 136
PRK12746 PRK12746
SDR family oxidoreductase;
8-207 6.79e-12

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 63.90  E-value: 6.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAaktaqphpklLGTIYTAAE----EIEAVGGKALPCIVDVRDEQQISA 83
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIH----------YGRNKQAADetirEIESNGGKAFLIEADLNSIDGVKK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAIKKF------GGIDILVNNAsAISLTNTLDTPTKRL-DLMMNVNTRGTYLASKACIPYLKKSkvAHILNISPP-L 155
Cdd:PRK12746  74 LVEQLKNELqirvgtSEIDILVNNA-GIGTQGTIENTTEEIfDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAeV 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767958463 156 NLNpvwFKQHCAYTIAKYGMSMYVLGMAEEFkGE--IAVNALWP---KTAIHTAAMD 207
Cdd:PRK12746 151 RLG---FTGSIAYGLSKGALNTMTLPLAKHL-GErgITVNTIMPgytKTDINAKLLD 203
PRK09730 PRK09730
SDR family oxidoreductase;
12-227 7.50e-12

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 63.72  E-value: 7.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVI----AAKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVnyqqNLHAAQ----------EVVNLITQAGGKAFVLQADISDENQVVAMFTA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPT-KRLDLMMNVNTRGTYLaskACIPYLKKSKVAH------ILNISPPLNL--N 158
Cdd:PRK09730  73 IDQHDEPLAALVNNAGILFTQCTVENLTaERINRVLSTNVTGYFL---CCREAVKRMALKHggsggaIVNVSSAASRlgA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463 159 PvwfKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPK---TAIHTAAmdmlGGPGiesqcrKVDIIADA 227
Cdd:PRK09730 150 P---GEYVDYAASKGAIDTLTTGLSLEVAAQgIRVNCVRPGfiyTEMHASG----GEPG------RVDRVKSN 209
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 12-174 1.16e-11

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 63.52  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEAVGG--KALPCIVDVRDEQQISAAVEKAI 89
Cdd:PRK12384   4 VAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANV-------AQEINAEYGegMAYGFGADATSEQSVLALSRGVD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  90 KKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYL----ASKACIPYLKKSKVAHILNISpplnlNPVWFKQH 165
Cdd:PRK12384  77 EIFGRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLcareFSRLMIRDGIQGRIIQINSKS-----GKVGSKHN 151


                 ....*....
gi 767958463 166 CAYTIAKYG 174
Cdd:PRK12384 152 SGYSAAKFG 160
PRK06194 PRK06194
hypothetical protein; Provisional
 7-102 1.45e-11

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 63.50  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK06194   3 DFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDR-------AVAELRAQGAEVLGVRTDVSDAAQVEALAD 75

                         90
                 ....*....|....*.
gi 767958463  87 KAIKKFGGIDILVNNA 102
Cdd:PRK06194  76 AALERFGAVHLLFNNA 91
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 12-197 2.10e-11

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. 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.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 62.56  E-value: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:cd08945    5 VALVTGATSGIGLAIARRLGKEGLRVFVCARGEE-------GLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPY--LKKSKVAHILNISPPLNlnpvwfKQ---HC 166
Cdd:cd08945   78 YGPIDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGG------KQgvvHA 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767958463 167 A-YTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:cd08945  152 ApYSASKHGVVGFTKALGLELaRTGITVNAVCP 184
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 8-197 3.15e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 61.81  E-value: 3.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGtIYtaaEEIEAVGGkALPCIV-------DVRDEQQ 80
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEE---KLEA-VY---DEIEAAGG-PQPAIIpldlltaTPQNYQQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  81 ISAAVEkaiKKFGGIDILVNNASAIS-LTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNP 159
Cdd:PRK08945  82 LADTIE---EQFGRLDGVLHNAGLLGeLGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767958463 160 --VWfkqhCAYTIAKY---GMsMYVLgmAEEFKG-EIAVNALWP 197
Cdd:PRK08945 159 raNW----GAYAVSKFateGM-MQVL--ADEYQGtNLRVNCINP 195
PRK07775 PRK07775
SDR family oxidoreductase;
12-188 4.46e-11

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 62.08  E-value: 4.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK07775  12 PALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEEL-------VDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwfKQHC-AYTI 170
Cdd:PRK07775  85 LGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQ---RPHMgAYGA 161

                        170
                 ....*....|....*...
gi 767958463 171 AKYGMSMYVLGMAEEFKG 188
Cdd:PRK07775 162 AKAGLEAMVTNLQMELEG 179
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 12-222 6.30e-11

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid 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.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 61.32  E-value: 6.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDganiviAAKTAQPHPKL--LGTIYTAAEEIEAVGGKALPCI-VDVRDEQQISAAVEKA 88
Cdd:cd09806    2 VVLITGCSSGIGLHLAVRLASD------PSKRFKVYATMrdLKKKGRLWEAAGALAGGTLETLqLDVCDSKSVAAAVERV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  89 ikKFGGIDILVNNAsAISLTNTLDTPTkrLDLM---MNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFKQ- 164
Cdd:cd09806   76 --TERHVDVLVCNA-GVGLLGPLEALS--EDAMasvFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDv 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463 165 HCAYTIAKYGM--SMYVLgmAEEFKGEIAVNALWPktaIHTAAMDMLGGPGIESQCRKVD 222
Cdd:cd09806  151 YCASKFALEGLceSLAVQ--LLPFNVHLSLIECGP---VHTAFMEKVLGSPEEVLDRTAD 205
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 13-151 9.74e-11

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 60.54  E-value: 9.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGAnIVIAakTAQPHPKLlgtiytaaEEIEA-VGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGH-KVIA--TGRRQERL--------QELKDeLGDNLYIAQLDVRNRAAIEEMLASLPAE 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958463  92 FGGIDILVNNAS-AISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNI 151
Cdd:PRK10538  72 WRNIDVLVNNAGlALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINI 132
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 8-205 9.79e-11

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.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 60.67  E-value: 9.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGG-KALPCIVDVRD--EQQISAA 84
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEE-------KLRQVADHINEEGGrQPQWFILDLLTctSENCQQL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGGIDILVNNASAISLTNTL-DTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPV--W 161
Cdd:cd05340   75 AQRIAVNYPRLDGVLHNAGLLGDVCPLsEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRanW 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767958463 162 fkqhCAYTIAKYGMSMYVLGMAEEFKG-EIAVNALWP---KTAIHTAA 205
Cdd:cd05340  155 ----GAYAVSKFATEGL*QVLADEYQQrNLRVNCINPggtRTAMRASA 198
PRK07985 PRK07985
SDR family oxidoreductase;
5-197 1.01e-10

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 61.16  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAaktaqphpkllgtiYTAAEE---------IEAVGGKALPCIVDV 75
Cdd:PRK07985  44 SGRLKDRKALVTGGDSGIGRAAAIAYAREGADVAIS--------------YLPVEEedaqdvkkiIEECGRKAVLLPGDL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  76 RDEQQISAAVEKAIKKFGGIDILVNNA-SAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISPP 154
Cdd:PRK07985 110 SDEKFARSLVHEAHKALGGLDIMALVAgKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG--ASIITTSSI 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767958463 155 LNLNPvwfKQHCA-YTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK07985 188 QAYQP---SPHLLdYAATKAAILNYSRGLAKQVaeKG-IRVNIVAP 229
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 13-185 1.13e-10

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 60.56  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANiVIAAKTAqphpkllgtiytaAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGAT-VIALDLP-------------FVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS------PPLNLnpvwfkqhC 166
Cdd:cd05331   67 GPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVAsnaahvPRISM--------A 138

                        170
                 ....*....|....*....
gi 767958463 167 AYTIAKYGMSMYVLGMAEE 185
Cdd:cd05331  139 AYGASKAALASLSKCLGLE 157
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
15-197 1.16e-10

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 60.55  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  15 ITGASRGIGKAIALKAAKDGaNIVIAAKTAQphpkllgtiYTAAEEIEAVGGKALPCI----VDVRDEQQISAAVEKAIK 90
Cdd:PRK12824   7 VTGAKRGIGSAIARELLNDG-YRVIATYFSG---------NDCAKDWFEEYGFTEDQVrlkeLDVTDTEECAEALAEIEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNASAisltnTLDTPTKRLDL-----MMNVNTRGTYLASKACIPYLKKSKVAHILNISpPLNLNPVWFKQh 165
Cdd:PRK12824  77 EEGPVDILVNNAGI-----TRDSVFKRMSHqewndVINTNLNSVFNVTQPLFAAMCEQGYGRIINIS-SVNGLKGQFGQ- 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958463 166 CAYTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK12824 150 TNYSAAKAGMIGFTKALASEGarYG-ITVNCIAP 182
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 13-207 1.19e-10

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical 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 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.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 60.16  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGaniviaaktaqphpkllgtIYTAAEEIEAVGGKALPC----------IVDVRDEqqis 82
Cdd:cd08931    3 IFITGAASGIGRETALLFARNG-------------------WFVGLYDIDEDGLAALAAelgaenvvagALDVTDR---- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  83 AAVEKAIKKF-----GGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPplnl 157
Cdd:cd08931   60 AAWAAALADFaaatgGRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTAS---- 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958463 158 npvwfkqhCAYTIAKYGMSMY------VLGMAEEFKGE-----IAVNALWP---KTAIHTAAMD 207
Cdd:cd08931  136 --------SSAIYGQPDLAVYsatkfaVRGLTEALDVEwarhgIRVADVWPwfvDTPILTKGET 191
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 3-101 2.28e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 60.01  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   3 PNTGRLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLG---TIYTAAEEIEAVGGKALPCIVDVRDEQ 79
Cdd:PRK08303   1 PMMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRSTRARRSEYDrpeTIEETAELVTAAGGRGIAVQVDHLVPE 80

                         90       100
                 ....*....|....*....|..
gi 767958463  80 QISAAVEKAIKKFGGIDILVNN 101
Cdd:PRK08303  81 QVRALVERIDREQGRLDILVND 102
PRK07577 PRK07577
SDR family oxidoreductase;
12-197 2.41e-10

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 59.36  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPH-PkllgtiytaaeeieavgGKALPCivDVRDEQQiSAAVEKAIK 90
Cdd:PRK07577   5 TVLVTGATKGIGLALSLRLANLGHQVIGIARSAIDDfP-----------------GELFAC--DLADIEQ-TAATLAQIN 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNAsAISLTNTL---DTPTkrLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpplNLNPVWFKQHCA 167
Cdd:PRK07577  65 EIHPVDAIVNNV-GIALPQPLgkiDLAA--LQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNIC---SRAIFGALDRTS 138

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767958463 168 YTIAKYGMsmyvLGMAEEFKGEIA-----VNALWP 197
Cdd:PRK07577 139 YSAAKSAL----VGCTRTWALELAeygitVNAVAP 169
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 12-197 3.13e-10

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 58.79  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTaqPHPKLlgtiytaaEEIEAVGGKALPCivDVRDEQQISAAVEKAIKK 91
Cdd:PRK06483   4 PILITGAGQRIGLALAWHLLAQGQPVIVSYRT--HYPAI--------DGLRQAGAQCIQA--DFSTNAGIMAFIDELKQH 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKS--KVAHILNISpplnlNPVWFK---QHC 166
Cdd:PRK06483  72 TDGLRAIIHNASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHghAASDIIHIT-----DYVVEKgsdKHI 146

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767958463 167 AYTIAKYGMSMYVLGMAEEFKGEIAVNALWP 197
Cdd:PRK06483 147 AYAASKAALDNMTLSFAAKLAPEVKVNSIAP 177
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 8-99 3.20e-10

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 59.27  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGA--SRGIGKAIALKAAKDGANIVIaakTAQPhPKLLGTIYTAAEEIEAVggKALPCivDVRDEQQISAAV 85
Cdd:COG0623    3 LKGKRGLITGVanDRSIAWGIAKALHEEGAELAF---TYQG-EALKKRVEPLAEELGSA--LVLPC--DVTDDEQIDALF 74

                         90
                 ....*....|....
gi 767958463  86 EKAIKKFGGIDILV 99
Cdd:COG0623   75 DEIKEKWGKLDFLV 88
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-197 3.42e-10

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 59.03  E-value: 3.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASR--GIGKAIALKAAKDGANIVIAAKTA----QPHPKLLGTIYTAAEEIEAVGGKALPCIVDVRDEQQ 80
Cdd:PRK12859   3 QLKNKVAVVTGVSRldGIGAAICKELAEAGADIFFTYWTAydkeMPWGVDQDEQIQLQEELLKNGVKVSSMELDLTQNDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  81 ISAAVEKAIKKFGGIDILVNNAsAISLTNTLDTPT-KRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNP 159
Cdd:PRK12859  83 PKELLNKVTEQLGYPHILVNNA-AYSTNNDFSNLTaEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767958463 160 VwfKQHCAYTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK12859 162 M--VGELAYAATKGAIDALTSSLAAEVahLG-ITVNAINP 198
PRK07062 PRK07062
SDR family oxidoreductase;
8-195 4.40e-10

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 58.90  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphPKLLGTIYTAAEEIEAVGGKALPCivDVRDEQQISAAVEK 87
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDE---ERLASAEARLREKFPGARLLAARC--DVLDEADVAAFAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTP----TKRLDLMMnvntRGTYLASKACIPYLKKSKVAHILNISPPLNLNPvwfK 163
Cdd:PRK07062  81 VEARFGGVDMLVNNAGQGRVSTFADTTddawRDELELKY----FSVINPTRAFLPLLRASAAASIVCVNSLLALQP---E 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958463 164 QHCAYT-IAKYGMSMYVLGMAEEFKGE-IAVNAL 195
Cdd:PRK07062 154 PHMVATsAARAGLLNLVKSLATELAPKgVRVNSI 187
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
12-192 7.80e-10

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 58.45  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiyTAAEEIEAVggkalpcIVDVRDEQQISAAVEkaikk 91
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANL-----AALPGVEFV-------RGDLRDPEALAAALA----- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 fgGIDILVNNASAISltntldTPTKRLDLMMNVNTRGTYLASKACipylKKSKVAHILNIS---------PPLN----LN 158
Cdd:COG0451   64 --GVDAVVHLAAPAG------VGEEDPDETLEVNVEGTLNLLEAA----RAAGVKRFVYASsssvygdgeGPIDedtpLR 131

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958463 159 PVWfkqhcAYTIAKYGMSMYVLGMAEEFKGEIAV 192
Cdd:COG0451  132 PVS-----PYGASKLAAELLARAYARRYGLPVTI 160
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 8-197 1.34e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 57.39  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKllGTIYtaaeEIEAVGGKALPCIVDVRDEQQISA---A 84
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAE--ETVY----EIQSNGGSAFSIGANLESLHGVEAlysS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  85 VEKAIKKFGG---IDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISPPlnLNPVW 161
Cdd:PRK12747  76 LDNELQNRTGstkFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDN--SRIINISSA--ATRIS 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767958463 162 FKQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWP 197
Cdd:PRK12747 152 LPDFIAYSMTKGAINTMTFTLAKQLGARgITVNAILP 188
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 7-102 1.44e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 57.22  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTaQPHPKLLGTIYTAAeeieavggkalpcivDVRDEQQISAAVE 86
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARS-RPDDLPEGVEFVAA---------------DLTTAEGCAAVAR 69

                         90
                 ....*....|....*.
gi 767958463  87 KAIKKFGGIDILVNNA 102
Cdd:PRK06523  70 AVLERLGGVDILVHVL 85
PRK06500 PRK06500
SDR family oxidoreductase;
7-212 1.49e-09

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 57.27  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIeavGGKALPCIVD---VRDEQQISA 83
Cdd:PRK06500   3 RLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPA-------SLEAARAEL---GESALVIRADagdVAAQKALAQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAikkFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSkVAHILNISpplnlnpvwfk 163
Cdd:PRK06500  73 ALAEA---FGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANP-ASIVLNGS----------- 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463 164 qhcayTIAKYGM---SMY------VLGMAEEFKGE-----IAVNALWPKtAIHTAAMDMLGGP 212
Cdd:PRK06500 138 -----INAHIGMpnsSVYaaskaaLLSLAKTLSGEllprgIRVNAVSPG-PVQTPLYGKLGLP 194
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 11-178 1.61e-09

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. 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.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 57.29  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  11 CTVFITGASRGIGKAIALKAAKDGAnIVIAAKTAQPHPkllgtiytAAEEIEAVGGKALPCI-VDVRDEQQISAAVEKAI 89
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGF-TVLAGCLTKNGP--------GAKELRRVCSDRLRTLqLDVTKPEQIKRAAQWVK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  90 KKFGGIDI--LVNNASAISL-TNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKvAHILNISPPLNLNPvwFKQHC 166
Cdd:cd09805   72 EHVGEKGLwgLVNNAGILGFgGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAK-GRVVNVSSMGGRVP--FPAGG 148

                        170
                 ....*....|..
gi 767958463 167 AYTIAKYGMSMY 178
Cdd:cd09805  149 AYCASKAAVEAF 160
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 13-212 1.71e-09

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. 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.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 56.38  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGtiyTAAEeieaVGGKALPciVDVRDEQQISAAVEKAikkf 92
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAG---ALAG---LAAE----VGALARP--ADVAAELEVWALAQEL---- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 GGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLnlnpVWFKQHCAYTIAK 172
Cdd:cd11730   65 GPLDLLVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPEL----VMLPGLSAYAAAK 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767958463 173 YGMSMYVLGMAEEFKGEIAVNALWPktAIHTAAMDMLGGP 212
Cdd:cd11730  141 AALEAYVEVARKEVRGLRLTLVRPP--AVDTGLWAPPGRL 178
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 8-197 2.22e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 57.12  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpKLLGtiytAAEEIEAVGG----KALPciVDVRDEQQISA 83
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPD---KLAA----AAEEIEALKGagavRYEP--ADVTDEDQVAR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAIKKFGGIDILVNNASA---ISLTNTLDTPTKRLDLMMNVNtrGTYLASKACIPYLKKSKVAHILNISPPLNLNP- 159
Cdd:PRK05875  76 AVDAATAWHGRLHGVVHCAGGsetIGPITQIDSDAWRRTVDLNVN--GTMYVLKHAARELVRGGGGSFVGISSIAASNTh 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767958463 160 VWFKqhcAYTIAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:PRK05875 154 RWFG---AYGVTKSAVDHLMKLAADELgPSWVRVNSIRP 189
PRK09186 PRK09186
flagellin modification protein A; Provisional
 8-152 4.89e-09

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 55.77  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGAnIVIAAKTAQPHPKLLgtiytaAEEIEAVGGKALPCIV--DVRDEQQISAAV 85
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGG-IVIAADIDKEALNEL------LESLGKEFKSKKLSLVelDITDQESLEEFL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  86 EKAIKKFGGIDILVNNASAISL---TNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK09186  75 SKSAEKYGKIDGAVNCAYPRNKdygKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNIS 144
PRK07024 PRK07024
SDR family oxidoreductase;
13-102 7.14e-09

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 55.32  E-value: 7.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIytaaeeieAVGGKALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARL--------PKAARVSVYAADVRDADALAAAAADFIAAH 76

                         90
                 ....*....|
gi 767958463  93 GGIDILVNNA 102
Cdd:PRK07024  77 GLPDVVIANA 86
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
5-197 1.39e-08

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 54.25  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   5 TGRLAgctvFITGASRGIGKAIALKAAKDGANIVIAAKTAQPH-PKLLgtiytaaEEIEAVGGKALPCIVDVRDEQQISA 83
Cdd:PRK12938   2 SQRIA----YVTGGMGGIGTSICQRLHKDGFKVVAGCGPNSPRrVKWL-------EDQKALGFDFIASEGNVGDWDSTKA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  84 AVEKAIKKFGGIDILVNNASAisltnTLDTPTKRL-----DLMMNVNTRGTYLASKACIPYLKKSKVAHILNISpPLNLN 158
Cdd:PRK12938  71 AFDKVKAEVGEIDVLVNNAGI-----TRDVVFRKMtredwTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINIS-SVNGQ 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767958463 159 PVWFKQhCAYTIAKYGMSMYVLGMAEEF--KGeIAVNALWP 197
Cdd:PRK12938 145 KGQFGQ-TNYSTAKAGIHGFTMSLAQEVatKG-VTVNTVSP 183
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 1-209 1.52e-08

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 54.15  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   1 MLPNTGRLAgctvFITGASRGIGKAIALKAAKDGAniviaaktaqphpkLLGTIYTAAEEIEAVGG------KALPCIVD 74
Cdd:PRK12936   1 MFDLSGRKA----LVTGASGGIGEEIARLLHAQGA--------------IVGLHGTRVEKLEALAAelgervKIFPANLS 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  75 VRDEqqISAAVEKAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPP 154
Cdd:PRK12936  63 DRDE--VKALGQKAEADLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSV 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463 155 LNL--NPvwfkQHCAYTIAKYGMSMYVLGMAEEFKGE-IAVNALWPKTaIHTAAMDML 209
Cdd:PRK12936 141 VGVtgNP----GQANYCASKAGMIGFSKSLAQEIATRnVTVNCVAPGF-IESAMTGKL 193
PRK05693 PRK05693
SDR family oxidoreductase;
12-151 1.77e-08

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 54.41  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPhpkllgtiytaAEEIEAVGGKALPciVDVRDEQQISAAVEKAIKK 91
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAED-----------VEALAAAGFTAVQ--LDVNDGAALARLAEELEAE 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKvAHILNI 151
Cdd:PRK05693  70 HGGLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSR-GLVVNI 128
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 10-152 6.52e-08

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. 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.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 52.47  E-value: 6.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIVIAAKTaqphpklLGTIYTAAEEIEavgGKALPCIVDVRdeqQISAAVEKAI 89
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVIMACRD-------MAKCEEAAAEIR---RDTLNHEVIVR---HLDLASLKSI 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  90 KKFGG--------IDILVNNASAISL--TNTLDTptkrLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:cd09807   68 RAFAAeflaeedrLDVLINNAGVMRCpySKTEDG----FEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVS 136
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-152 8.81e-08

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 51.89  E-value: 8.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKtaQPHPKLLGTIYTAaeeieavggkalpcIVDVRDEqqisaaVEKAIKK 91
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQGAQVYGVDK--QDKPDLSGNFHFL--------------QLDLSDD------LEPLFDW 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958463  92 FGGIDILVNNASAI-SLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK06550  65 VPSVDILCNTAGILdDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMC 126
PRK05993 PRK05993
SDR family oxidoreductase;
12-219 1.17e-07

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 51.95  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGK--AIALKaaKDGANIVIAAKTAQPHPKLlgtiytAAEEIEAVggkalpcIVDVRDEQQISAAVEKAI 89
Cdd:PRK05993   6 SILITGCSSGIGAycARALQ--SDGWRVFATCRKEEDVAAL------EAEGLEAF-------QLDYAEPESIAALVAQVL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  90 KKFGG-IDILVNN-----ASAISltntlDTPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVWFK 163
Cdd:PRK05993  71 ELSGGrLDALFNNgaygqPGAVE-----DLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYR 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767958463 164 QhcAYTIAKYGMSMYVLGMAEEFKGeiavnalwpkTAIHTAAMDmlggPG-IESQCR 219
Cdd:PRK05993 146 G--AYNASKFAIEGLSLTLRMELQG----------SGIHVSLIE----PGpIETRFR 186
PRK12744 PRK12744
SDR family oxidoreductase;
8-130 1.19e-07

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 51.66  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGAN-IVIAAKTAQPHPKLLGTIytaaEEIEAVGGKALPCIVDVRDEQQISAAVE 86
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKaVAIHYNSAASKADAEETV----AAVKAAGAKAVAFQADLTTAAAVEKLFD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767958463  87 KAIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTY 130
Cdd:PRK12744  82 DAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAF 125
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 12-199 1.90e-07

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. 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.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 50.79  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIViaaktaqphpkllGTIYTAAEEieavggkALPCIV---DVRDEQQISAAVEKA 88
Cdd:cd05334    3 VVLVYGGRGALGSAVVQAFKSRGWWVA-------------SIDLAENEE-------ADASIIvldSDSFTEQAKQVVASV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  89 IKKFGGIDILVNNASAISLTNTLD-TPTKRLDLMMNVNTRGTYLASKACIPYLKKSkvAHILNISPPLNLNPVwfKQHCA 167
Cdd:cd05334   63 ARLSGKVDALICVAGGWAGGSAKSkSFVKNWDLMWKQNLWTSFIASHLATKHLLSG--GLLVLTGAKAALEPT--PGMIG 138

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767958463 168 YTIAKYGMSMYVLGMAEEFKG---EIAVNALWPKT 199
Cdd:cd05334  139 YGAAKAAVHQLTQSLAAENSGlpaGSTANAILPVT 173
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 8-195 2.76e-07

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 50.72  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGASRGIGKAIALKAAKDGANIVIaAKTAQPhpkllgTIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEK 87
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVL-GDVDKP------GLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  88 AIKKFGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIP-YLKKSKVAHILNISPPLNLNPVwfKQHC 166
Cdd:PRK05876  77 AFRLLGHVDVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrLLEQGTGGHVVFTASFAGLVPN--AGLG 154

                        170       180
                 ....*....|....*....|....*....
gi 767958463 167 AYTIAKYGmsmyVLGMAEEFKGEIAVNAL 195
Cdd:PRK05876 155 AYGVAKYG----VVGLAETLAREVTADGI 179
PRK06482 PRK06482
SDR family oxidoreductase;
12-152 3.52e-07

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 50.50  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiytAAEEIEAVGGKALP-CIVDVRDEQQISAAVEKAIK 90
Cdd:PRK06482   4 TWFITGASSGFGRGMTERLLARGDRVAATVRRPD-----------ALDDLKARYGDRLWvLQLDVTDSAAVRAVVDRAFA 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767958463  91 KFGGIDILVNNA------SAISLTNTldtptkRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNIS 152
Cdd:PRK06482  73 ALGRIDVVVSNAgyglfgAAEELSDA------QIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVS 134
PRK08219 PRK08219
SDR family oxidoreductase;
12-126 6.08e-07

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 49.16  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIAlKAAKDGANIVIAAKTAqphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEkaikK 91
Cdd:PRK08219   5 TALITGASRGIGAAIA-RELAPTHTLLLGGRPA-----------ERLDELAAELPGATPFPVDLTDPEAIAAAVE----Q 68

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767958463  92 FGGIDILVNNASAISLTNTLDTPTKRLDLMMNVNT 126
Cdd:PRK08219  69 LGRLDVLVHNAGVADLGPVAESTVDEWRATLEVNV 103
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 15-96 1.08e-06

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. 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 KRs 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.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 49.29  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  15 ITGASRGIGKAIALKAAKD-GANIVIAAKTAQPHPKLLgtIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKKFG 93
Cdd:cd08953  210 VTGGAGGIGRALARALARRyGARLVLLGRSPLPPEEEW--KAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYG 287


                 ...
gi 767958463  94 GID 96
Cdd:cd08953  288 AID 290
PRK08340 PRK08340
SDR family oxidoreductase;
13-106 2.10e-06

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 47.88  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgTIYTAAEEIEAVGGkALPCIVDVRDEQQISAAVEKAIKKF 92
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRNEE-------NLEKALKELKEYGE-VYAVKADLSDKDDLKNLVKEAWELL 74

                         90
                 ....*....|....
gi 767958463  93 GGIDILVNNASAIS 106
Cdd:PRK08340  75 GGIDALVWNAGNVR 88
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
13-189 2.14e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 47.76  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHpkllgtIYTAAEEieaVGGKALPCIVDVRDEQQISAAVEKAIKKf 92
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISRTENKE------LTKLAEQ---YNSNLTFHSLDLQDVHELETNFNEILSS- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  93 ggidILVNNASAISLTNT--LDTPTKR--------LDLMMNVNTRGTYLASKAcipYLKKSKV----AHILNISPPLNLN 158
Cdd:PRK06924  74 ----IQEDNVSSIHLINNagMVAPIKPiekaeseeLITNVHLNLLAPMILTST---FMKHTKDwkvdKRVINISSGAAKN 146

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767958463 159 PvwFKQHCAYTIAKYGMSMYVLGMAEEFKGE 189
Cdd:PRK06924 147 P--YFGWSAYCSSKAGLDMFTQTVATEQEEE 175
PRK06720 PRK06720
hypothetical protein; Provisional
 7-102 3.50e-06

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 46.12  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   7 RLAGCTVFITGASRGIGKAIALKAAKDGANIV---IAAKTAQphpkllgtiyTAAEEIEAVGGKALPCIVDVRDEQQISA 83
Cdd:PRK06720  13 KLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIvtdIDQESGQ----------ATVEEITNLGGEALFVSYDMEKQGDWQR 82

                         90
                 ....*....|....*....
gi 767958463  84 AVEKAIKKFGGIDILVNNA 102
Cdd:PRK06720  83 VISITLNAFSRIDMLFQNA 101
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 12-102 5.47e-06

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 45.94  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463    12 TVFITGASRGIGKAIALKAAKDGA-NIVIAAKTAQPHPKLLgtiyTAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAA----ALLAELEAAGARVTVVACDVADRDALAAVLAAIPA 77

                           90
                   ....*....|..
gi 767958463    91 KFGGIDILVNNA 102
Cdd:smart00822  78 VEGPLTGVIHAA 89
PRK06953 PRK06953
SDR family oxidoreductase;
12-139 7.04e-06

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 46.22  E-value: 7.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQphpkllgtiytAAEEIEAVGGKALpcIVDVRDEQQISAavekAIKK 91
Cdd:PRK06953   3 TVLIVGASRGIGREFVRQYRADGWRVIATARDAA-----------ALAALQALGAEAL--ALDVADPASVAG----LAWK 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767958463  92 FGG--IDILVNNASAIS-LTNTLDTPTKR-LDLMMNVNTRGTYLASKACIPY 139
Cdd:PRK06953  66 LDGeaLDAAVYVAGVYGpRTEGVEPITREdFDAVMHTNVLGPMQLLPILLPL 117
PRK08416 PRK08416
enoyl-ACP reductase;
10-102 2.02e-05

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 45.15  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIviaAKTAQPHPKLLGTIYTAAEEIEAVGGKALPciVDVRDEQQISAAVEKAI 89
Cdd:PRK08416   8 GKTLVISGGTRGIGKAIVYEFAQSGVNI---AFTYNSNVEEANKIAEDLEQKYGIKAKAYP--LNILEPETYKELFKKID 82

                         90
                 ....*....|...
gi 767958463  90 KKFGGIDILVNNA 102
Cdd:PRK08416  83 EDFDRVDFFISNA 95
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 12-197 2.79e-05

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. 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.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 44.49  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIV-IAAKTAQPHPKllgtiytAAEEIEAVGGKALpcivdvrDEQQISAAVEKAIK 90
Cdd:cd05361    3 IALVTHARHFAGPASAEALTEDGYTVVcHDASFADAAER-------QAFESENPGTKAL-------SEQKPEELVDAVLQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  91 KFGGIDILVNNASAISLTNTLD-TPTKRLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPPLNLNPVwfKQHCAYT 169
Cdd:cd05361   69 AGGAIDVLVSNDYIPRPMNPIDgTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPL--AYNSLYG 146

                        170       180
                 ....*....|....*....|....*....
gi 767958463 170 IAKYGMSMYVLGMAEEF-KGEIAVNALWP 197
Cdd:cd05361  147 PARAAAVALAESLAKELsRDNILVYAIGP 175
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 12-212 3.08e-05

alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, which catalyzes the NAD-dependent oxidoreduction of hydroxysteroids, is a dimeric member of the classical SDR family. 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.


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 44.41  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIV-IAAKTAqphpkllgtiytaaeEIEAvggkalpcivDVRDEQQISAAVEKAI- 89
Cdd:cd05328    1 TIVITGAASGIGAATAELLEDAGHTVIgIDLREA---------------DVIA----------DLSTPEGRAAAIADVLa 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  90 KKFGGIDILVNNASAisltntldTPTKRLDLMMNVNTRGTYLASKACIPYLKKSK------VAHILNISPPLNLNP---- 159
Cdd:cd05328   56 RCSGVLDGLVNCAGV--------GGTTVAGLVLKVNYFGLRALMEALLPRLRKGHgpaavvVSSIAGAGWAQDKLElaka 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463 160 -----------VWFKQ----HCAYTIAKYGMSMYVLGMAE--EFKGEIAVNALWP---KTAIHTAAMDMLGGP 212
Cdd:cd05328  128 laagtearavaLAEHAgqpgYLAYAGSKEALTVWTRRRAAtwLYGAGVRVNTVAPgpvETPILQAFLQDPRGG 200
PRK08251 PRK08251
SDR family oxidoreductase;
12-102 4.17e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 43.77  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIYTAAEEIeAVGGKALpcivDVRDEQQISAAVEKAIKK 91
Cdd:PRK08251   4 KILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYPGI-KVAVAAL----DVNDHDQVFEVFAEFRDE 78

                         90
                 ....*....|.
gi 767958463  92 FGGIDILVNNA 102
Cdd:PRK08251  79 LGGLDRVIVNA 89
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 10-99 4.19e-05

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site 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.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 44.11  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGAS--RGIGKAIALKAAKDGANIVIaakTAQPhPKLLGTIYTAAEEIEAVGgKALPCivDVRDEQQISAAVEK 87
Cdd:cd05372    1 GKRILITGIAndRSIAWGIAKALHEAGAELAF---TYQP-EALRKRVEKLAERLGESA-LVLPC--DVSNDEEIKELFAE 73

                         90
                 ....*....|..
gi 767958463  88 AIKKFGGIDILV 99
Cdd:cd05372   74 VKKDWGKLDGLV 85
PRK09291 PRK09291
SDR family oxidoreductase;
12-102 5.06e-05

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 43.83  E-value: 5.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAqphpkllGTIYTAAEEIEAVGGkALPCI-VDVRDEQQISAAVEKaik 90
Cdd:PRK09291   4 TILITGAGSGFGREVALRLARKGHNVIAGVQIA-------PQVTALRAEAARRGL-ALRVEkLDLTDAIDRAQAAEW--- 72

                         90
                 ....*....|..
gi 767958463  91 kfgGIDILVNNA 102
Cdd:PRK09291  73 ---DVDVLLNNA 81
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 15-104 2.00e-04

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 41.84  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   15 ITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLgtiytAAEEIEAVGGKALPCIVDVRDEQQISAAVEKAI----K 90
Cdd:TIGR02685   6 VTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTL-----AAELNARRPNSAVTCQADLSNSATLFSRCEAIIdacfR 80

                          90
                  ....*....|....
gi 767958463   91 KFGGIDILVNNASA 104
Cdd:TIGR02685  81 AFGRCDVLVNNASA 94
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 15-197 2.14e-04

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical 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.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 41.68  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  15 ITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytaAEEIEA-VGGKALPCIVDVRDEQQISAAVEKAIKKFG 93
Cdd:cd05322    7 VIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKV-------ADEINAeYGEKAYGFGADATNEQSVIALSKGVDEIFK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  94 GIDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYL----ASKACIpylKKSKVAHILNISPplNLNPVWFKQHCAYT 169
Cdd:cd05322   80 RVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLcareFSKLMI---RDGIQGRIIQINS--KSGKVGSKHNSGYS 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767958463 170 IAKYG----MSMYVLGMAEEfkgEIAVNALWP 197
Cdd:cd05322  155 AAKFGgvglTQSLALDLAEH---GITVNSLML 183
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 1-102 3.07e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 41.55  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   1 MLPNTGRLAgctvFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIyTAAEEIEAVGGKALpcivDVRDEQQ 80
Cdd:PRK06197  11 IPDQSGRVA----VVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARI-TAATPGADVTLQEL----DLTSLAS 81

                         90       100
                 ....*....|....*....|..
gi 767958463  81 ISAAVEKAIKKFGGIDILVNNA 102
Cdd:PRK06197  82 VRAAADALRAAYPRIDLLINNA 103
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 10-151 3.76e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 41.39  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  10 GCTVFITGASRGIGKAIALKAAKDGANIVIAAKtaqpHPKLLGTIYTAaeeIEAVGGKALPCIVDVRDEQQISAAVEKAI 89
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVAR----NPDKLKDVSDS---IQSKYSKTQIKTVVVDFSGDIDEGVKRIK 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  90 KKFGGID--ILVNNASaisltntLDTPTKR---------LDLMMNVNTRGTYLASKACIPYLKKSKVAHILNI 151
Cdd:PLN02780 126 ETIEGLDvgVLINNVG-------VSYPYARffhevdeelLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINI 191
PRK07041 PRK07041
SDR family oxidoreductase;
15-135 3.83e-04

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 40.79  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  15 ITGASRGIGKAIALKAAKDGANIVIAAKTAqphPKLlgtiYTAAEEIEAvGGKALPCIVDVRDEQQISAAVEKAikkfGG 94
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTIASRSR---DRL----AAAARALGG-GAPVRTAALDITDEAAVDAFFAEA----GP 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767958463  95 IDILVnnasaISLTNTLDTPTKRLDL-----MMNVNTRGTYLASKA 135
Cdd:PRK07041  70 FDHVV-----ITAADTPGGPVRALPLaaaqaAMDSKFWGAYRVARA 110
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 13-104 6.19e-04

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


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 39.69  E-value: 6.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLLGTIytaaeeieavggKALPCiVDVRDEQQISAAVEkaikkf 92
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEP------------VAVVE-GDLRDLDSLSDAVQ------ 61

                         90
                 ....*....|..
gi 767958463  93 gGIDILVNNASA 104
Cdd:cd05226   62 -GVDVVIHLAGA 72
PRK06101 PRK06101
SDR family oxidoreductase;
12-240 6.48e-04

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 40.24  E-value: 6.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANiVIAAKTAQphpKLLGTIYTAAEEIEavggkalPCIVDVRDEQQISAAVekAIKK 91
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQ-VIACGRNQ---SVLDELHTQSANIF-------TLAFDVTDHPGTKAAL--SQLP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  92 FGGiDILVNNASAISLTNTLDTPTKRLDLMMNVNTRGTYLASKACIPYLKKS-KVAHILNISPPLNLnpvwfKQHCAYTI 170
Cdd:PRK06101  70 FIP-ELWIFNAGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSCGhRVVIVGSIASELAL-----PRAEAYGA 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958463 171 AKYGMSMYVLGMAEEFKGE-IAVNALWPK------TAIHTAAMDMLGGPGIESQCRKVDIIADAAYSIFqkPKSFTG 240
Cdd:PRK06101 144 SKAAVAYFARTLQLDLRPKgIEVVTVFPGfvatplTDKNTFAMPMIITVEQASQEIRAQLARGKSHIYF--PARFTW 218
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 13-154 1.03e-03

Short-chain dehydrogenases/reductases (SDR); 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 (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs 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.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 39.42  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  13 VFITGASRGIGKAIALKAAKDGANIVIAaktaqphpkllgtiytaaeeieavggkalpciVDVRdeqqisaavekaikkf 92
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSPKVLV--------------------------------VSRR---------------- 32

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463  93 ggiDILVNNAsAISLTNTLDTPTK-RLDLMMNVNTRGTYLASKACIPYLKKSKVAHILNISPP 154
Cdd:cd02266   33 ---DVVVHNA-AILDDGRLIDLTGsRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSV 91
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 12-95 1.20e-03

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 39.08  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   12 TVFITGASRGIGKAIALKAAKDGA-NIVIAAKTAQPHPKLLGTIytaaEEIEAVGGKALPCIVDVRDEQQISAAVEKAIK 90
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGArHLVLLSRSAAPRPDAQALI----AELEARGVEVVVVACDVSDPDAVAALLAEIKA 77


                  ....*
gi 767958463   91 KFGGI 95
Cdd:pfam08659  78 EGPPI 82
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 12-152 2.26e-03

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 38.29  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKTAQPHPKLlgtiytAAEEIEAVGGkalpcivDVRDEQQISAAVEkaikk 91
Cdd:COG0702    1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAAL------AAAGVEVVQG-------DLDDPESLAAALA----- 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958463  92 fgGIDILVNNASAisltNTLDTPTKRLDLMMNVntrgtylaskacIPYLKKSKVAHILNIS 152
Cdd:COG0702   63 --GVDAVFLLVPS----GPGGDFAVDVEGARNL------------ADAAKAAGVKRIVYLS 105
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
 8-69 3.57e-03

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 38.59  E-value: 3.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767958463   8 LAGCTVFITGASrGIGKAIALKAAKDGANIVIAAKTaqphpkllgtiYTAAEEI-EAVGGKAL 69
Cdd:PLN02520 377 LAGKLFVVIGAG-GAGKALAYGAKEKGARVVIANRT-----------YERAKELaDAVGGQAL 427
PRK08862 PRK08862
SDR family oxidoreductase;
12-115 5.46e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 37.40  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGANIVIAAKtaqpHPKLLGTIYtaaEEIEAVGGKALPCIVDVRDEQQISAAVEKAIKK 91
Cdd:PRK08862   7 IILITSAGSVLGRTISCHFARLGATLILCDQ----DQSALKDTY---EQCSALTDNVYSFQLKDFSQESIRHLFDAIEQQ 79

                         90       100
                 ....*....|....*....|....*
gi 767958463  92 FG-GIDILVNNASAISLTNTLDTPT 115
Cdd:PRK08862  80 FNrAPDVLVNNWTSSPLPSLFDEQP 104
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 12-116 6.36e-03

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. 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 KRs 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.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 37.75  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463  12 TVFITGASRGIGKAIALKAAKDGA-NIVIAAKTAQPHPkllgtIYTAAEEIEAVGGKALPCIVDVRDEQQISAAVEkAIK 90
Cdd:cd05274  152 TYLITGGLGGLGLLVARWLAARGArHLVLLSRRGPAPR-----AAARAALLRAGGARVSVVRCDVTDPAALAALLA-ELA 225

                         90       100
                 ....*....|....*....|....*.
gi 767958463  91 KFGGIDILVnNASAISLTNTLDTPTK 116
Cdd:cd05274  226 AGGPLAGVI-HAAGVLRDALLAELTP 250
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
8-99 9.60e-03

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 37.00  E-value: 9.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958463   8 LAGCTVFITGAS--RGIGKAIALKAAKDGANIVIaakTAQPHPKllGTIYTAAEEIEAVGGKA--LPCivDVRDEQQISA 83
Cdd:PRK07370   4 LTGKKALVTGIAnnRSIAWGIAQQLHAAGAELGI---TYLPDEK--GRFEKKVRELTEPLNPSlfLPC--DVQDDAQIEE 76

                         90
                 ....*....|....*.
gi 767958463  84 AVEKAIKKFGGIDILV 99
Cdd:PRK07370  77 TFETIKQKWGKLDILV 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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