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Conserved domains on  [gi|1203982|gb|AAA89174|]
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NAD+-dependent 15-hydroxyprostaglandin dehydrogenase [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143139)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to alcohol dehydrogenase that catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones; 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-254 8.62e-108

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: 311.54  E-value: 8.62e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGVNNEK----------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  156 HGIVGFTRSAALAANlMNSGVRLNAICPGFVNTAILESIEKEEnmgqyieykdhiKDMIKYYGILDPPLIANGLITLIED 235
Cdd:cd05323 159 HGVVGFTRSLADLLE-YKTGVRVNAICPGFTNTPLLPDLVAKE------------AEMLPSAPTQSPEVVAKAIVYLIED 225

                       250
                ....*....|....*....
gi 1203982  236 DALNGAIMKITTSKGIHFQ 254
Cdd:cd05323 226 DEKNGAIWIVDGGKLIEIE 244
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-254 8.62e-108

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: 311.54  E-value: 8.62e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGVNNEK----------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  156 HGIVGFTRSAALAANlMNSGVRLNAICPGFVNTAILESIEKEEnmgqyieykdhiKDMIKYYGILDPPLIANGLITLIED 235
Cdd:cd05323 159 HGVVGFTRSLADLLE-YKTGVRVNAICPGFTNTPLLPDLVAKE------------AEMLPSAPTQSPEVVAKAIVYLIED 225

                       250
                ....*....|....*....
gi 1203982  236 DALNGAIMKITTSKGIHFQ 254
Cdd:cd05323 226 DEKNGAIWIVDGGKLIEIE 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-199 1.58e-71

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 217.87  E-value: 1.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA--LGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     86 DILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:pfam00106  79 DILVNNAGITglgpfselSDEDWERVIDVNLTGVFNLTRAVLPAMIKG---SGGRIVNISSVAGLVPYPGGSAYSASKAA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1203982    158 IVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEEN 199
Cdd:pfam00106 156 VIGFTRS--LALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-204 6.79e-63

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: 197.70  E-value: 6.79e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:COG1028   6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRA--AGGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:COG1028  84 LDILVNNAGITPpgpleeltEEDWDRVLDVNLKGPFLLTRAALPHMRER---GGGRIVNISSIAGLRGSPGQAAYAASKA 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 1203982  157 GIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 204
Cdd:COG1028 161 AVVGLTRS--LALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREAL 206
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-214 8.29e-56

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 179.59  E-value: 8.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpqKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG--EARVLVFDVSDEAAVRALIEAAVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNN--------EKNWEKTLQINLvsviSGTYLG----LDYMSKQNGGEggiIINMSSLAGLMPVAQQ 148
Cdd:PRK05653  79 AFGALDILVNNAGITRdallprmsEEDWDRVIDVNL----TGTFNVvraaLPPMIKARYGR---IVNISSVSGVTGNPGQ 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1203982   149 PVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKeenmgqyiEYKDHIKDMI 214
Cdd:PRK05653 152 TNYSAAKAGVIGFTK--ALALELASRGITVNAVAPGFIDTDMTEGLPE--------EVKAEILKEI 207
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 5-192 1.20e-27

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: 107.02  E-value: 1.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNL-EAGVQCKAALHEQFE------PQKTLFIQCDVADQQQLRDTFRK 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLCAdDPAVGYPLATRAELDavaaacPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     78 VVDHFGRLDILVNNAGV--NNEKNWEKT-------LQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQ 148
Cdd:TIGR04504  81 AVERWGRLDAAVAAAGViaGGRPLWETTdaeldllLDVNLRGVWNLARAAVPAMLARPDPRGGRFVAVASAAATRGLPHL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1203982    149 PVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:TIGR04504 161 AAYCAAKHAVVGLVRG--LAADLGGTGVTANAVSPGSTRTAMLA 202
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 6-192 1.48e-21

mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function.


Pssm-ID: 468513 [Multi-domain]  Cd Length: 256  Bit Score: 90.50  E-value: 1.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGV-------QCKAALHEQFEPQKTLFIqCDVADQQQLRDTFRKV 78
Cdd:NF040491   1 RVALVTGAARGIGAATVRRLAARGYAVVAVDACAGDPApyplgteADLDALVASSPGRVETVV-ADVRDRAALAAAVALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    79 VDHFGRLDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQP 149
Cdd:NF040491  80 LDRWGRLDAAVAAAAViaggrplweTPPEELDALWDVDVRGVWNLAAAAVPALLAGPDPRGCRFVAVASAAGHRGLFHLA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   150 VYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:NF040491 160 AYCAAKHAVVGLVR--GLAADLAGTGVTACAVSPGSTDTPMLA 200
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-153 8.37e-07

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: 47.86  E-value: 8.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982       6 KVALVTGAAQGIGRAFAEALLLKGA-KVALV------DWNLEAGVQCKAALHEQfepqkTLFIQCDVADQQQLRDTFRKV 78
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLsrsgpdAPGAAALLAELEAAGAR-----VTVVACDVADRDALAAVLAAI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      79 VDHFGRLDILVNNAGVNN--------EKNWEKTLQ------INLVSVISGtyLGLDYMskqnggeggiiINMSSLAGLMP 144
Cdd:smart00822  76 PAVEGPLTGVIHAAGVLDdgvlasltPERFAAVLApkaagaWNLHELTAD--LPLDFF-----------VLFSSIAGVLG 142


                   ....*....
gi 1203982     145 VAQQPVYCA 153
Cdd:smart00822 143 SPGQANYAA 151
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-254 8.62e-108

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: 311.54  E-value: 8.62e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPG--AAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGVNNEK----------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  156 HGIVGFTRSAALAANlMNSGVRLNAICPGFVNTAILESIEKEEnmgqyieykdhiKDMIKYYGILDPPLIANGLITLIED 235
Cdd:cd05323 159 HGVVGFTRSLADLLE-YKTGVRVNAICPGFTNTPLLPDLVAKE------------AEMLPSAPTQSPEVVAKAIVYLIED 225

                       250
                ....*....|....*....
gi 1203982  236 DALNGAIMKITTSKGIHFQ 254
Cdd:cd05323 226 DEKNGAIWIVDGGKLIEIE 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-199 1.58e-71

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 217.87  E-value: 1.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGA--LGGKALFIQGDVTDRAQVKALVEQAVERLGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     86 DILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:pfam00106  79 DILVNNAGITglgpfselSDEDWERVIDVNLTGVFNLTRAVLPAMIKG---SGGRIVNISSVAGLVPYPGGSAYSASKAA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1203982    158 IVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEEN 199
Cdd:pfam00106 156 VIGFTRS--LALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 8-246 6.05e-65

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: 202.51  E-value: 6.05e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAAlheQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDI 87
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAI---EALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   88 LVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggIIINMSSLAGLMPVAQQPVYCASKHGIV 159
Cdd:cd05233  78 LVNNAGIARpgpleeltDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGG---RIVNISSVAGLRPLPGQAAYAASKAALE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  160 GFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKdmikyygILDPPLIANGLITLIEDDA-- 237
Cdd:cd05233 155 GLTRS--LALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGR-------LGTPEEVAEAVVFLASDEAsy 225


                ....*....
gi 1203982  238 LNGAIMKIT 246
Cdd:cd05233 226 ITGQVIPVD 234
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 5-204 6.79e-63

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: 197.70  E-value: 6.79e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:COG1028   6 GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRA--AGGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:COG1028  84 LDILVNNAGITPpgpleeltEEDWDRVLDVNLKGPFLLTRAALPHMRER---GGGRIVNISSIAGLRGSPGQAAYAASKA 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 1203982  157 GIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 204
Cdd:COG1028 161 AVVGLTRS--LALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREAL 206
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-208 5.15e-59

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: 187.31  E-value: 5.15e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFepqktLFIQCDVADQQQLRDTFRKVVD 80
Cdd:COG4221   1 MSDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRA-----LAVPLDVTDEAAVEAAVAAAVA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:COG4221  76 EFGRLDVLVNNAGVAllgpleelDPEDWDRMIDVNVKGVLYVTRAALPAMRARG---SGHIVNISSIAGLRPYPGGAVYA 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 1203982  153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKD 208
Cdd:COG4221 153 ATKAAVRGLSES--LRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEG 206
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-192 5.74e-58

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 185.07  E-value: 5.74e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:COG0300   1 MSLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRA--AGARVEVVALDVTDPDAVAALAEAVLA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:COG0300  79 RFGPIDVLVNNAGVGgggpfeelDLEDLRRVFEVNVFGPVRLTRALLPLMRARG---RGRIVNVSSVAGLRGLPGMAAYA 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1203982  153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:COG0300 156 ASKAALEGFSES--LRAELAPTGVRVTAVCPGPVDTPFTA 193
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-214 8.29e-56

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 179.59  E-value: 8.29e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpqKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG--EARVLVFDVSDEAAVRALIEAAVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNN--------EKNWEKTLQINLvsviSGTYLG----LDYMSKQNGGEggiIINMSSLAGLMPVAQQ 148
Cdd:PRK05653  79 AFGALDILVNNAGITRdallprmsEEDWDRVIDVNL----TGTFNVvraaLPPMIKARYGR---IVNISSVSGVTGNPGQ 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1203982   149 PVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKeenmgqyiEYKDHIKDMI 214
Cdd:PRK05653 152 TNYSAAKAGVIGFTK--ALALELASRGITVNAVAPGFIDTDMTEGLPE--------EVKAEILKEI 207
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-188 7.48e-52

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 169.68  E-value: 7.48e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKA--GGKAIGVAMDVTDEEAINAGIDYAVETF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAG---VNN------EKnWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK12429  80 GGVDILVNNAGiqhVAPiedfptEK-WKKMIAIMLDGAFLTTKAALPIMKAQGGGR---IINMASVHGLVGSAGKAAYVS 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   154 SKHGIVGFTRSAALAAnlMNSGVRLNAICPGFVNT 188
Cdd:PRK12429 156 AKHGLIGLTKVVALEG--ATHGVTVNAICPGYVDT 188
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-194 2.76e-50

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 165.37  E-value: 2.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQckaALHEQFEPQ--KTLFIQCDVADQQQLRDTFRKV 78
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAE---ALVAEIGALggKALAVQGDVSDAESVERAVDEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    79 VDHFGRLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPV 150
Cdd:PRK05557  78 KAEFGGVDILVNNAGITRDNLlmrmkeedWDRVIDTNLTGVFNLTKAVARPMMKQRSGR---IINISSVVGLMGNPGQAN 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   151 YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESI 194
Cdd:PRK05557 155 YAASKAGVIGFTKS--LARELASRGITVNAVAPGFIETDMTDAL 196
FabG-like PRK07231
SDR family oxidoreductase;
1-193 5.47e-50

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 164.62  E-value: 5.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqckAALHEQFE-PQKTLFIQCDVADQQQLRDTFRKVV 79
Cdd:PRK07231   1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAA----ERVAAEILaGGRAIAVAADVSDEADVEAAVAAAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    80 DHFGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMPVAQQPV 150
Cdd:PRK07231  77 ERFGSVDILVNNAGTThrngplldvDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG---GGAIVNVASTAGLRPRPGLGW 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   151 YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:PRK07231 154 YNASKGAVITLTKA--LAAELGPDKIRVNAVAPVVVETGLLEA 194
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-245 7.48e-49

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 161.55  E-value: 7.48e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVAL-VDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVV 79
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIKE--EGGDAIAVKADVSSEEDVENLVEQIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    80 DHFGRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMPVAQQPVY 151
Cdd:PRK05565  79 EKFGKIDILVNNAGISNfglvtdmtDEEWDRVIDVNLTGVMLLTRYALPYMIKRK---SGVIVNISSIWGLIGASCEVLY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   152 CASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEEnmgqyieyKDHIKDMIKYYGILDPPLIANGLIT 231
Cdd:PRK05565 156 SASKGAVNAFTK--ALAKELAPSGIRVNAVAPGAIDTEMWSSFSEED--------KEGLAEEIPLGRLGKPEEIAKVVLF 225

                        250
                 ....*....|....*.
gi 1203982   232 LIEDDA--LNGAIMKI 245
Cdd:PRK05565 226 LASDDAsyITGQIITV 241
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 12-205 2.87e-48

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: 159.90  E-value: 2.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     12 GAA--QGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALHEQFepqKTLFIQCDVADQQQLRDTFRKVVDHFGRLDILV 89
Cdd:pfam13561   1 GAAneSGIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEEL---GAAVLPCDVTDEEQVEALVAAAVEKFGRLDILV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     90 NNAGVNN----------EKNWEKTLQINLVSVISGTYLGLDYMskqngGEGGIIINMSSLAGLMPVAQQPVYCASKHGIV 159
Cdd:pfam13561  77 NNAGFAPklkgpfldtsREDFDRALDVNLYSLFLLAKAALPLM-----KEGGSIVNLSSIGAERVVPNYNAYGAAKAALE 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1203982    160 GFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIE 205
Cdd:pfam13561 152 ALTRY--LAVELGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAE 195
PRK12826 PRK12826
SDR family oxidoreductase;
5-188 3.83e-48

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 160.08  E-value: 3.83e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqckAALHEQFEPQ--KTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK12826   6 GRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDA----AATAELVEAAggKARARQVDVRDRAALKAAVAAGVEDF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGL-MPVAQQPVYCA 153
Cdd:PRK12826  82 GRLDILVANAGIFPltpfaemdDEQWERVIDVNLTGTFLLTQAALPALIRAGGGR---IVLTSSVAGPrVGYPGLAHYAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   154 SKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNT 188
Cdd:PRK12826 159 SKAGLVGFTRALAL--ELAARNITVNSVHPGGVDT 191
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 3-241 1.41e-47

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: 158.32  E-value: 1.41e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepqkTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDA-----ARFFHLDVTDEDGWTAVVDTAREAF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCAS 154
Cdd:cd05341  78 GRLDVLVNNAGILTGGTvetttleeWRRLLDINLTGVFLGTRAVIPPMKEAGGGS---IINMSSIEGLVGDPALAAYNAS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  155 KHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAIL-ESIEKEENMGQYIEYKDHikdmikyyGILDPPLIANGLITLI 233
Cdd:cd05341 155 KGAVRGLTKSAALECATQGYGIRVNSVHPGYIYTPMTdELLIAQGEMGNYPNTPMG--------RAGEPDEIAYAVVYLA 226

                       250
                ....*....|
gi 1203982  234 EDDA--LNGA 241
Cdd:cd05341 227 SDESsfVTGS 236
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 6-237 3.69e-46

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: 154.63  E-value: 3.69e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQckAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAE--TVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:cd05333  79 DILVNNAGITrdnllmrmSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGR---IINISSVVGLIGNPGQANYAASKAG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  158 IVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKeenmgqyiEYKDHIKDMI--KYYGilDPPLIANGLITLIED 235
Cdd:cd05333 156 VIGFTKS--LAKELASRGITVNAVAPGFIDTDMTDALPE--------KVKEKILKQIplGRLG--TPEEVANAVAFLASD 223


                ..
gi 1203982  236 DA 237
Cdd:cd05333 224 DA 225
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 4-192 4.02e-44

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: 149.90  E-value: 4.02e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd08940  81 GVDILVNNAGIQHvapiedfpTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGR---IINIASVHGLVASANKSAYVAAK 157

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 1203982  156 HGIVGFTRSAALAAnlMNSGVRLNAICPGFVNTAILE 192
Cdd:cd08940 158 HGVVGLTKVVALET--AGTGVTCNAICPGWVLTPLVE 192
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 4-190 3.21e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 147.50  E-value: 3.21e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALheqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK06841  14 SGKVAVVTGGASGIGHAIAELFAAKGARVALLDRS-EDVAEVAAQL----LGGNAKGLVCDVSDSQSVEAAVAAVISAFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLgldyMSKQNGGE-----GGIIINMSSLAGLMPVAQQPV 150
Cdd:PRK06841  89 RIDILVNSAGVAllapaedvSEEDWDKTIDINL----KGSFL----MAQAVGRHmiaagGGKIVNLASQAGVVALERHVA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 1203982   151 YCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK06841 161 YCASKAGVVGMTK--VLALEWGPYGITVNAISPTVVLTEL 198
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-188 5.36e-43

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 146.71  E-value: 5.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepqkTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK07067   2 MRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPA-----AIAVSLDVTRQDSIDRIVAAAVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGV--------NNEKNWEKTLQINlvsvISGTYLGLDYMSKQ--NGGEGGIIINMSSLAGLMPVAQQPV 150
Cdd:PRK07067  77 RFGGIDILFNNAALfdmapildISRDSYDRLFAVN----VKGLFFLMQAVARHmvEQGRGGKIINMASQAGRRGEALVSH 152

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   151 YCASKHGIVGFTRSAALAanLMNSGVRLNAICPGFVNT 188
Cdd:PRK07067 153 YCATKAAVISYTQSAALA--LIRHGINVNAIAPGVVDT 188
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 5-210 5.80e-43

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 147.13  E-value: 5.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepqKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK12829  11 GLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLPGA----KVTATVADVADPAQVERVFDTAVERFGG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNN---------EKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK12829  87 LDVLVNNAGIAGptggideitPEQWEQTLAVNLNGQFYFARAAVPLLKAS--GHGGVIIALSSVAGRLGYPGRTPYAASK 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESI---------EKEENMGQyiEYKDHI 210
Cdd:PRK12829 165 WAVVGLVKS--LAIELGPLGIRVNAILPGIVRGPRMRRViearaqqlgIGLDEMEQ--EYLEKI 224
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-198 7.58e-43

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 146.17  E-value: 7.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK12825   2 GSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALG-RRAQAVQADVTDKAALEAAVAAAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK12825  81 RFGRIDILVNNAGIFedkpladmSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGR---IVNISSVAGLPGWPGRSNYA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 1203982   153 ASKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIEKEE 198
Cdd:PRK12825 158 AAKAGLVGLTKALAR--ELAEYGITVNMVAPGDIDTDMKEATIEEA 201
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 3-188 2.55e-42

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 145.47  E-value: 2.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALheqfepQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL------GLVVGGPLDVTDPASFAAFLDAVEADL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK07825  77 GPIDVLVNNAGVmpvgpfldEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGH---VVNVASLAGKIPVPGMATYCAS 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 1203982   155 KHGIVGFTrsAALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07825 154 KHAVVGFT--DAARLELRGTGVHVSVVLPSFVNT 185
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 4-198 2.89e-42

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: 144.83  E-value: 2.89e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd05366   1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAG-YNAVAVGADVTDKDDVEALIDQAVEKFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGgeGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05366  80 SFDVMVNNAGIApitplltiTEEDLKKVYAVNVFGVLFGIQAAARQFKKLGH--GGKIINASSIAGVQGFPNLGAYSASK 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 1203982  156 HGIVGFTRSAalAANLMNSGVRLNAICPGFVNTAILESIEKEE 198
Cdd:cd05366 158 FAVRGLTQTA--AQELAPKGITVNAYAPGIVKTEMWDYIDEEV 198
PRK06172 PRK06172
SDR family oxidoreductase;
1-192 3.65e-42

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 144.51  E-value: 3.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK06172   3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREA--GGEALFVACDVTRDAEVKALVEQTIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGV---------NNEKNWEKTLQINLvsviSGTYLGLDY----MSKQNGGEggiIINMSSLAGLMPVAQ 147
Cdd:PRK06172  81 AYGRLDYAFNNAGIeieqgrlaeGSEAEFDAIMGVNV----KGVWLCMKYqiplMLAQGGGA---IVNTASVAGLGAAPK 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 1203982   148 QPVYCASKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILE 192
Cdd:PRK06172 154 MSIYAASKHAVIGLTKSAAI--EYAKKGIRVNAVCPAVIDTDMFR 196
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
4-206 7.33e-42

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 144.10  E-value: 7.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSK--DGGKAIAVKADVSDRDQVFAAVRQVVDTFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK08643  79 DLNVVVNNAGVApttpietiTEEQFDKVYNINVGGVIWGIQAAQEAFKKL--GHGGKIINATSQAGVVGNPELAVYSSTK 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1203982   156 HGIVGFTRSAalAANLMNSGVRLNAICPGFVNTAILESIEKE--ENMGQYIEY 206
Cdd:PRK08643 157 FAVRGLTQTA--ARDLASEGITVNAYAPGIVKTPMMFDIAHQvgENAGKPDEW 207
PRK07326 PRK07326
SDR family oxidoreductase;
1-188 1.21e-41

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 142.84  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNK---GNVLGLAADVRDEADVQRAVDAIVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQnggeGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK07326  79 AFGGLDVLIANAGVGHFAPveeltpeeWRLVIDTNLTGAFYTIKAAVPALKRG----GGYIINISSLAGTNFFAGGAAYN 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 1203982   153 ASKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNT 188
Cdd:PRK07326 155 ASKFGLVGFSEAAML--DLRQYGIKVSTIMPGSVAT 188
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 5-210 2.33e-41

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: 142.50  E-value: 2.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05347   5 GKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEK--EGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSL---AGLMPVaqqPVYCA 153
Cdd:cd05347  83 IDILVNNAGIIrrhpaeefPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGK---IINICSLlseLGGPPV---PAYAA 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 1203982  154 SKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEykDHI 210
Cdd:cd05347 157 SKGGVAGLTK--ALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDIL--KRI 209
PRK07063 PRK07063
SDR family oxidoreductase;
5-193 3.20e-41

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 142.50  E-value: 3.20e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK07063   7 GKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFGP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSS------LAGLMPvaqqpv 150
Cdd:PRK07063  87 LDVLVNNAGINvfadplamTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGS---IVNIASthafkiIPGCFP------ 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   151 YCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:PRK07063 158 YPVAKHGLLGLTR--ALGIEYAARNVRVNAIAPGYIETQLTED 198
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 4-214 3.35e-41

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: 142.16  E-value: 3.35e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLE----AGVQCKAALHEQfepQKTLFIQCDVADQQQLRDTFRKVV 79
Cdd:cd05364   2 SGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAErleeTRQSCLQAGVSE---KKILLVVADLTEEEGQDRIISTTL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   80 DHFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggiIINMSSLAGLMPVAQQPVY 151
Cdd:cd05364  79 AKFGRLDILVNNAGILakgggedqDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGE----IVNVSSVAGGRSFPGVLYY 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1203982  152 CASKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIEKEENmgQYIEYKDHIKDMI 214
Cdd:cd05364 155 CISKAALDQFTRCTAL--ELAPKGVRVNSVSPGVIVTGFHRRMGMPEE--QYIKFLSRAKETH 213
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 4-193 2.30e-39

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: 137.42  E-value: 2.30e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQckaalhEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGET------VAKLGDNCRFVPVDVTSEKDVKAALALAKAKFG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGV-------NNEKN-------WEKTLQINLVSVISGTYLGLDYMSKQ---NGGEGGIIINMSSLAGLMPVA 146
Cdd:cd05371  75 RLDIVVNCAGIavaaktyNKKGQqphslelFQRVINVNLIGTFNVIRLAAGAMGKNepdQGGERGVIINTASVAAFEGQI 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 1203982  147 QQPVYCASKHGIVGFTrsAALAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:cd05371 155 GQAAYSASKGGIVGMT--LPIARDLAPQGIRVVTIAPGLFDTPLLAG 199
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 4-194 7.34e-39

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 136.29  E-value: 7.34e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepqkTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK08265   5 AGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGER-----ARFIATDITDDAAIERAVATVVARFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNA------GVNNEKN-WEKTLQINLVSVISGTYLGLDYMSKQnggeGGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:PRK08265  80 RVDILVNLActylddGLASSRAdWLAALDVNLVSAAMLAQAAHPHLARG----GGAIVNFTSISAKFAQTGRWLYPASKA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 1203982   157 GIVGFTRSAA--LAANlmnsGVRLNAICPGFVNTAILESI 194
Cdd:PRK08265 156 AIRQLTRSMAmdLAPD----GIRVNSVSPGWTWSRVMDEL 191
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 5-203 1.05e-38

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 136.70  E-value: 1.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06701  46 GKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEK-EGVKCLLIPGDVSDEAFCKDAVEETVRELGR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK06701 125 LDILVNNAAFQypqqslediTAEQLDKTFKTNIYSYFHMTKAALPHLKQ-----GSAIINTGSITGYEGNETLIDYSATK 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQY 203
Cdd:PRK06701 200 GAIHAFTRS--LAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEKVSQF 245
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 5-238 1.26e-38

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: 135.54  E-value: 1.26e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFePQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05352   8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKY-GVKTKAYKCDVSSQESVEKTFKQIQKDFGK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLGLDYMSKQ--NGGEGGIIInMSSLAGLMPVAQQP--VYC 152
Cdd:cd05352  87 IDILIANAGITvhkpaldyTYEQWNKVIDVNL----NGVFNCAQAAAKIfkKQGKGSLII-TASMSGTIVNRPQPqaAYN 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKeenmgqyiEYKDHIKDMIKYYGILDPPLIANGLITL 232
Cdd:cd05352 162 ASKAAVIHLAKS--LAVEWAKYFIRVNSISPGYIDTDLTDFVDK--------ELRKKWESYIPLKRIALPEELVGAYLYL 231


                ....*.
gi 1203982  233 IEDDAL 238
Cdd:cd05352 232 ASDASS 237
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 6-245 2.98e-38

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: 134.57  E-value: 2.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd05330   4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFGRI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGVNNEKN---------WEKTLQINLvsviSGTYLGLDYMSKQNGGEG-GIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05330  84 DGFFNNAGIEGKQNltedfgadeFDKVVSINL----RGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQSGYAAAK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  156 HGIVGFTRSAALAANlmNSGVRLNAICPGFVNTAILESIEK-------EENMGQYIEYkdhikDMIKYYGilDPPLIANG 228
Cdd:cd05330 160 HGVVGLTRNSAVEYG--QYGIRINAIAPGAILTPMVEGSLKqlgpenpEEAGEEFVSV-----NPMKRFG--EPEEVAAV 230

                       250
                ....*....|....*....
gi 1203982  229 LITLIEDDA--LNGAIMKI 245
Cdd:cd05330 231 VAFLLSDDAgyVNAAVVPI 249
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
6-245 5.26e-38

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 133.74  E-value: 5.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWnleAGVQCKAALHE--QFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYF---SGNDCAKDWFEeyGFTEDQVRLKELDVTDTEECAEALAEIEEEEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNEK--------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK12824  80 PVDILVNNAGITRDSvfkrmshqEWNDVINTNLNSVFNVTQPLFAAMCEQGYGR---IINISSVNGLKGQFGQTNYSAAK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   156 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENmgqyieykDHIKDMIKYYGILDPPLIANGLITLIED 235
Cdd:PRK12824 157 AGMIGFTK--ALASEGARYGITVNCIAPGYIATPMVEQMGPEVL--------QSIVNQIPMKRLGTPEEIAAAVAFLVSE 226

                        250
                 ....*....|..
gi 1203982   236 DA--LNGAIMKI 245
Cdd:PRK12824 227 AAgfITGETISI 238
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-237 8.32e-38

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: 133.28  E-value: 8.32e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALvdwNLEAGVQCKAALHEQFEPQ--KTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:cd05358   3 GKVALVTGASSGIGKAIAIRLATAGANVVV---NYRSKEDAAEEVVEEIKAVggKAIAVQADVSKEEDVVALFQSAIKEF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVNNE--------KNWEKTLQINLvsviSGTYLG----LDYMSKQNggEGGIIINMSSLAGLMPVAQQPV 150
Cdd:cd05358  80 GTLDILVNNAGLQGDasshemtlEDWNKVIDVNL----TGQFLCareaIKRFRKSK--IKGKIINMSSVHEKIPWPGHVN 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  151 YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEEnmgqyiEYKDHIKDMIKYYGILDPPLIANGLI 230
Cdd:cd05358 154 YAASKGGVKMMTKT--LAQEYAPKGIRVNAIAPGAINTPINAEAWDDP------EQRADLLSLIPMGRIGEPEEIAAAAA 225


                ....*..
gi 1203982  231 TLIEDDA 237
Cdd:cd05358 226 WLASDEA 232
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-205 2.01e-37

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 132.40  E-value: 2.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK12939   6 AGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAA--GGRAHAIAADLADPASVQRFFDAAAAALG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNEK--------NWEKTLQINLvsviSGTYLgldyMSKQNG-----GEGGIIINMSSLAGLMPVAQQPV 150
Cdd:PRK12939  84 GLDGLVNNAGITNSKsateldidTWDAVMNVNV----RGTFL----MLRAALphlrdSGRGRIVNLASDTALWGAPKLGA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1203982   151 YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIE 205
Cdd:PRK12939 156 YVASKGAVIGMTRS--LARELGGRGITVNAIAPGLTATEATAYVPADERHAYYLK 208
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-237 2.32e-37

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 132.05  E-value: 2.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALvdwNLEAGVQCKAALHEQF--EPQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAENLVNELgkEGHDVYAVQADVSKVEDANRLVEEAVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKqngGEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK12935  81 HFGKVDILVNNAGITrdrtfkklNREDWERVIDVNLSSVFNTTSAVLPYITE---AEEGRIISISSIIGQAGGFGQTNYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEenmgqyIEYKDHIKDMIKYYGILDPplIANGLITL 232
Cdd:PRK12935 158 AAKAGMLGFTKS--LALELAKTNVTVNAICPGFIDTEMVAEVPEE------VRQKIVAKIPKKRFGQADE--IAKGVVYL 227


                 ....*
gi 1203982   233 IEDDA 237
Cdd:PRK12935 228 CRDGA 232
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 6-208 2.64e-37

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: 130.95  E-value: 2.64e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqFEPqktlfIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGD-VEA-----VPYDARDPEDARALVDALRDRFGRI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:cd08932  75 DVLVHNAGIGrpttlregSDAELEAHFSINVIAPAELTRALLPALREAGSGR---VVFLNSLSGKRVLAGNAGYSASKFA 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 1203982  158 IVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENM--GQYIEYKD 208
Cdd:cd08932 152 LRALAH--ALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFppEEMIQPKD 202
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-245 5.29e-37

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 131.44  E-value: 5.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALvdwnLEAGVQCKAalhEQFEPQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAV----LYNSAENEA---KELREKGVFTIKCDVGNRDQVKKSKEVVEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPV-Y 151
Cdd:PRK06463  76 EFGRVDVLVNNAGImylmpfeeFDEEKYNKMIKINLNGAIYTTYEFLPLLKLS---KNGAIVNIASNAGIGTAAEGTTfY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   152 CASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAIL------ESIEKEENMgqyieYKDhiKDMIKYYGIldPPLI 225
Cdd:PRK06463 153 AITKAGIIILTRR--LAFELGKYGIRVNAVAPGWVETDMTlsgksqEEAEKLREL-----FRN--KTVLKTTGK--PEDI 221

                        250       260
                 ....*....|....*....|..
gi 1203982   226 ANGLITLIEDDA--LNGAIMKI 245
Cdd:PRK06463 222 ANIVLFLASDDAryITGQVIVA 243
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 5-191 8.38e-37

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: 130.65  E-value: 8.38e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqckAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05326   4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAG----QAVAAELGDPDISFVHCDVTVEADVRAAVDTAVARFGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGV----------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCAS 154
Cdd:cd05326  80 LDIMFNNAGVlgapcysileTSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGS---IVSVASVAGVVGGLGPHAYTAS 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 1203982  155 KHGIVGFTRSAalAANLMNSGVRLNAICPGFVNTAIL 191
Cdd:cd05326 157 KHAVLGLTRSA--ATELGEHGIRVNCVSPYGVATPLL 191
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 3-201 1.20e-36

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 130.52  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDwnleagvqckaaLHE-QFEPQKTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNAD------------IHGgDGQHENYQFVPTDVSSAEEVNHTVAEIIEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAGVN-----------------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMP 144
Cdd:PRK06171  75 FGRIDGLVNNAGINiprllvdekdpagkyelNEAAFDKMFNINQKGVFLMSQAVARQMVKQH---DGVIVNMSSEAGLEG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1203982   145 VAQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMG 201
Cdd:PRK06171 152 SEGQSCYAATKAALNSFTRS--WAKELGKHNIRVVGVAPGILEATGLRTPEYEEALA 206
PRK06138 PRK06138
SDR family oxidoreductase;
1-194 1.80e-36

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 129.89  E-value: 1.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAG---GRAFARQGDVGSAEAVEALVDFVAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLGLDY----MSKQNGGEggiIINMSSLAGLMPVAQQ 148
Cdd:PRK06138  78 RWGRLDVLVNNAGFGcggtvvttDEADWDAVMRVNV----GGVFLWAKYaipiMQRQGGGS---IVNTASQLALAGGRGR 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 1203982   149 PVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI 194
Cdd:PRK06138 151 AAYVASKGAIASLTR--AMALDHATDGIRVNAVAPGTIDTPYFRRI 194
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 5-192 1.95e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 129.85  E-value: 1.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqcKAALHEQfepqKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAG---KAAADEV----GGLFVPTDVTDEDAVNALFDTAAETYGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNNEKN----------WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVA-QQPVYCA 153
Cdd:PRK06057  80 VDIAFNNAGISPPEDdsilntgldaWQRVQDVNLTSVYLCCKAALPHMVRQGKGS---IINTASFVAVMGSAtSQISYTA 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   154 SKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:PRK06057 157 SKGGVLAMSRE--LGVQFARQGIRVNALCPGPVNTPLLQ 193
PRK05855 PRK05855
SDR family oxidoreductase;
5-193 2.12e-36

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 135.88  E-value: 2.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALHEQFEPQKTLFiQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDID-EAAAERTAELIRAAGAVAHAY-RVDVSDADAMEAFAEWVRAEHGV 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:PRK05855 393 PDIVVNNAGIgmaggfldTSAEDWDRVLDVNLWGVIHGCRLFGRQMVER--GTGGHIVNVASAAAYAPSRSLPAYATSKA 470

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1203982   157 GIVGFtrSAALAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:PRK05855 471 AVLML--SECLRAELAAAGIGVTAICPGFVDTNIVAT 505
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 5-188 2.60e-36

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: 129.32  E-value: 2.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHeqFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELR--AGGAGVLAVVADLTDPEDIDRLVEKAGDAFGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAG---------VNNEKnWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05344  79 VDILVNNAGgpppgpfaeLTDED-WLEAFDLKLLSVIRIVRAVLPGMKER---GWGRIVNISSLTVKEPEPNLVLSNVAR 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 1203982  156 HGIVGFTRSAALAanLMNSGVRLNAICPGFVNT 188
Cdd:cd05344 155 AGLIGLVKTLSRE--LAPDGVTVNSVLPGYIDT 185
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-195 2.98e-36

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: 129.27  E-value: 2.98e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqckAALHEQFEPQkTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAA----RATAAEIGPA-ACAISLDVTDQASIDRCVAALVDRW 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVNN-----EKNWEKTLQINLVSViSGTYLGLDYMSKQ--NGGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05363  76 GSIDILVNNAALFDlapivDITRESYDRLFAINV-SGTLFMMQAVARAmiAQGRGGKIINMASQAGRRGEALVGVYCATK 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1203982  156 HGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIE 195
Cdd:cd05363 155 AAVISLTQSAGL--NLIRHGINVNAIAPGVVDGEHWDGVD 192
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 6-215 5.96e-36

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: 128.50  E-value: 5.96e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVAlvdwnleAGVQCKAAL-HEQFEPQKTLF-IQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVI-------ATARNPDKLeSLGELLNDNLEvLELDVTDEESIKAAVKEVIERFG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05374  74 RIDVLVNNAGYGlfgpleetSIEEVRELFEVNVFGPLRVTRAFLPLMRKQ---GSGRIVNVSSVAGLVPTPFLGPYCASK 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIK 215
Cdd:cd05374 151 AALEALSES--LRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPEISPYAPERKEIK 208
PRK07831 PRK07831
SDR family oxidoreductase;
5-198 1.05e-35

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 128.23  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAA-QGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK07831  17 GKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGRVEAVVCDVTSEAQVDALIDAAVERLG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK07831  97 RLDVLVNNAGLGGQTPvvdmtddeWSRVLDVTLTGTFRATRAALRYMRAR--GHGGVIVNNASVLGWRAQHGQAHYAAAK 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   156 HGIVGFTRSAALAAnlMNSGVRLNAICPGFVNTAILESIEKEE 198
Cdd:PRK07831 175 AGVMALTRCSALEA--AEYGVRINAVAPSIAMHPFLAKVTSAE 215
PRK06181 PRK06181
SDR family oxidoreductase;
5-190 1.37e-35

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 127.79  E-value: 1.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADH--GGEALVVPTDVSDAEACERLIEAAVARFGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNNEKNWEKT---------LQINLVSVISGTYLGLDYMsKQNGGEggiIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK06181  79 IDILVNNAGITMWSRFDELtdlsvfervMRVNYLGAVYCTHAALPHL-KASRGQ---IVVVSSLAGLTGVPTRSGYAASK 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK06181 155 HALHGFFDS--LRIELADDGVAVTVVCPGFVATDI 187
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 5-202 2.65e-35

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: 126.50  E-value: 2.65e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALheQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd08934   3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADEL--EAEGGKALVLELDVTDEQQVDAAVERTVEALGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:cd08934  81 LDILVNNAGImllgpvedADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGT---IVNISSVAGRVAVRNSAVYNATKF 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 1203982  157 GIVGFtrSAALAANLMNSGVRLNAICPGFVNTA----ILESIEKEENMGQ 202
Cdd:cd08934 158 GVNAF--SEGLRQEVTERGVRVVVIEPGTVDTElrdhITHTITKEAYEER 205
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 5-192 2.99e-35

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 126.37  E-value: 2.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQ--KTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVAAGIEAAggKALGLAFDVRDFAATRAALDAGVEEF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVNNEK--------NWEKTLQINLVSVISGTYLGLDYMSKQNGgeGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK12827  86 GRLDILVNNAGIATDAafaelsieEWDDVIDVNLDGFFNVTQAALPPMIRARR--GGRIVNIASVAGVRGNRGQVNYAAS 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   155 KHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:PRK12827 164 KAGLIGLTK--TLANELAPRGITVNAVAPGAINTPMAD 199
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 5-215 1.36e-34

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: 124.50  E-value: 1.36e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN------LEAGVQCKAalheqfepqktlfIQCDVADQQQLRDTFRKv 78
Cdd:cd05368   2 GKVALITAAAQGIGRAIALAFAREGANVIATDINeeklkeLERGPGITT-------------RVLDVTDKEQVAALAKE- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   79 vdhFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMP-VAQQP 149
Cdd:cd05368  68 ---EGRIDVLFNCAGFvhhgsildCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGS---IINMSSVASSIKgVPNRF 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1203982  150 VYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIekeenMGQYIEYKDHIKDMIK 215
Cdd:cd05368 142 VYSTTKAAVIGLTKS--VAADFAQQGIRCNAICPGTVDTPSLEER-----IQAQPDPEEALKAFAA 200
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 3-192 1.76e-34

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 125.01  E-value: 1.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLN-QDGANAVADEINK-AGGKAIGVAMDVTNEDAVNAGIDKVAERF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggEGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK13394  83 GSVDILVSNAGIQivnpienySFADWKKMQAIHVDGAFLTTKAALKHMYKDD--RGGVVIYMGSVHSHEASPLKSAYVTA 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   155 KHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:PRK13394 161 KHGLLGLAR--VLAKEGAKHNVRSHVVCPGFVRTPLVD 196
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-193 5.09e-34

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: 123.37  E-value: 5.09e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALheqfePQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQI-----AGGALALRVDVTDEQQVAALFERAVEEF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVNNE---------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCA 153
Cdd:cd08944  76 GGLDLLVNNAGAMHLtpaiidtdlAVWDQTMAINLRGTFLCCRHAAPRMIARGGGS---IVNLSSIAGQSGDPGYGAYGA 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1203982  154 SKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:cd08944 153 SKAAIRNLTRT--LAAELRHAGIRCNALAPGLIDTPLLLA 190
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-245 1.06e-33

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: 122.50  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALheqfePQKTLFIQCDVADqqqlRDTFRKVVD 80
Cdd:cd05345   1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI-----GEAAIAIQADVTK----RADVEAMVE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   81 H----FGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMPVAQ 147
Cdd:cd05345  72 AalskFGRLDILVNNAGIThrnkpmlevDEEEFDRVFAVNVKSIYLSAQALVPHMEEQG---GGVIINIASTAGLRPRPG 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  148 QPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI---EKEENMGQYieykdhiKDMIKYYGILDPPL 224
Cdd:cd05345 149 LTWYNASKGWVVTATK--AMAVELAPRNIRVNCLCPVAGETPLLSMFmgeDTPENRAKF-------RATIPLGRLSTPDD 219

                       250       260
                ....*....|....*....|...
gi 1203982  225 IANGLITLIEDDA--LNGAIMKI 245
Cdd:cd05345 220 IANAALYLASDEAsfITGVALEV 242
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-197 1.48e-33

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 127.27  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFepqktLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDH-----HALAMDVSDEAQIREGFEQLHREFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNNE----------KNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK06484  80 IDVLVNNAGVTDPtmtatldttlEEFARLQAINLTGAYLVAREALRLMIEQ--GHGAAIVNVASGAGLVALPKRTAYSAS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   155 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKE 197
Cdd:PRK06484 158 KAAVISLTRS--LACEWAAKGIRVNAVLPGYVRTQMVAELERA 198
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
5-199 2.23e-33

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 122.22  E-value: 2.23e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEA----------GVQCKAalheqfepqktlfIQCDVADQQQLRDT 74
Cdd:PRK08226   6 GKTALITGALQGIGEGIARVFARHGANLILLDISPEIekladelcgrGHRCTA-------------VVADVRDPASVAAA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    75 FRKVVDHFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMpVA 146
Cdd:PRK08226  73 IKRAKEKEGRIDILVNNAGVcrlgsfldMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGR---IVMMSSVTGDM-VA 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1203982   147 Q--QPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEEN 199
Cdd:PRK08226 149 DpgETAYALTKAAIVGLTK--SLAVEYAQSGIRVNAICPGYVRTPMAESIARQSN 201
PRK07069 PRK07069
short chain dehydrogenase; Validated
 8-194 2.50e-33

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 121.74  E-value: 2.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     8 ALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAA-LHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAeINAAHGEGVAFAAVQDVTDEAQWQALLAQAADAMGGLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    87 ILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKqngGEGGIIINMSSLAGLMPVAQQPVYCASKHGI 158
Cdd:PRK07069  82 VLVNNAGVGSFGAieqieldeWRRVMAINVESIFLGCKHALPYLRA---SQPASIVNISSVAAFKAEPDYTAYNASKAAV 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 1203982   159 VGFTRSAALAANLMNSGVRLNAICPGFVNTAILESI 194
Cdd:PRK07069 159 ASLTKSIALDCARRGLDVRCNSIHPTFIRTGIVDPI 194
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-204 2.67e-33

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 121.77  E-value: 2.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALV--DWNLEAGVQckaaLHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK06935  14 DGKVAIVTGGNTGLGQGYAVALAKAGADIIITthGTNWDETRR----LIEK-EGRKVTFVQVDLTKPESAEKVVKEALEE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK06935  89 FGKIDILVNNAGTirraplleYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGK---IINIASMLSFQGGKFVPAYTA 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1203982   154 SKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 204
Cdd:PRK06935 166 SKHGVAGLTK--AFANELAAYNIQVNAIAPGYIKTANTAPIRADKNRNDEI 214
PRK07454 PRK07454
SDR family oxidoreductase;
6-193 3.16e-33

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 120.83  E-value: 3.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRST--GVKAAAYSIDLSNPEAIAPGIAELLEQFGCP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    86 DILVNNAGV--NNE------KNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:PRK07454  85 DVLINNAGMayTGPllemplSDWQWVIQLNLTSVFQCCSAVLPGMRAR---GGGLIINVSSIAARNAFPQWGAYCVSKAA 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 1203982   158 IVGFTRsaALAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:PRK07454 162 LAAFTK--CLAEEERSHGIRVCTITLGAVNTPLWDT 195
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-190 3.46e-33

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: 121.15  E-value: 3.46e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPqKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAP-SPHVVPLDMSDLEDAEQVVEEALKLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVNNEKNW--------EKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCAS 154
Cdd:cd05332  80 GGLDILINNAGISMRSLFhdtsidvdRKIMEVNYFGPVALTKAALPHLIERSQGS---IVVVSSIAGKIGVPFRTAYAAS 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 1203982  155 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAI 190
Cdd:cd05332 157 KHALQGFFDS--LRAELSEPNISVTVVCPGLIDTNI 190
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 6-188 6.18e-33

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: 119.92  E-value: 6.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQckAALHEQFEpqKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRVGICARD-EARLA--AAAAQELE--GVLGLAGDVRDEADVRRAVDAMEEAFGGL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGVNNEKN--------WEKTLQINLvsvISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:cd08929  76 DALVNNAGVGVMKPveeltpeeWRLVLDTNL---TGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFG 152

                       170       180       190
                ....*....|....*....|....*....|.
gi 1203982  158 IVGFTRSAALaaNLMNSGVRLNAICPGFVNT 188
Cdd:cd08929 153 LLGLSEAAML--DLREANIRVVNVMPGSVDT 181
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 5-196 1.02e-32

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: 120.33  E-value: 1.02e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQkTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd08933   9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGS-CKFVPCDVTKEEDIKTLISVTVERFGR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVNNEKNW-EKT--------LQINLVSVISGTYLGLDYMSKQNGGeggiIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd08933  88 IDCLVNNAGWHPPHQTtDETsaqefrdlLNLNLISYFLASKYALPHLRKSQGN----IINLSSLVGSIGQKQAAPYVATK 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 1203982  156 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEK 196
Cdd:cd08933 164 GAITAMTK--ALAVDESRYGVRVNCISPGNIWTPLWEELAA 202
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-197 1.48e-32

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 119.67  E-value: 1.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpqKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK08213  12 GKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGI--DALWIAADVADEADIERLAEETLERFGH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN---------NEKnWEKTLQINlvsvISGTYL-----GLDYMSKQNGGEggiIINMSSLAGL-------M 143
Cdd:PRK08213  90 VDILVNNAGATwgapaedhpVEA-WDKVMNLN----VRGLFLlsqavAKRSMIPRGYGR---IINVASVAGLggnppevM 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1203982   144 P-VAqqpvYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT----AILESIEKE 197
Cdd:PRK08213 162 DtIA----YNTSKGAVINFTR--ALAAEWGPHGIRVNAIAPGFFPTkmtrGTLERLGED 214
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-200 1.80e-32

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 119.29  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN----LEAGVQCKAAlheqfePQKTLFIQCDVADQQQLRDTFR 76
Cdd:PRK08217   1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNqeklEEAVAECGAL------GTEVRGYAANVTDEEDVEATFA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    77 KVVDHFGRLDILVNNAGVNNE-----------------KNWEKTLQINLvsviSGTYL-GLDYMSKQ-NGGEGGIIINMS 137
Cdd:PRK08217  75 QIAEDFGQLNGLINNAGILRDgllvkakdgkvtskmslEQFQSVIDVNL----TGVFLcGREAAAKMiESGSKGVIINIS 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   138 SL--AGLMpvaQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAIL-----ESIEKEENM 200
Cdd:PRK08217 151 SIarAGNM---GQTNYSASKAGVAAMTVT--WAKELARYGIRVAAIAPGVIETEMTaamkpEALERLEKM 215
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-245 1.88e-32

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 124.19  E-value: 1.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfepqKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGD-----EHLSVQADITDEAAVESAFAQIQARWGR 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNNE---------KNWEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK06484 344 LDVLVNNAGIAEVfkpsleqsaEDFTRVYDVNLSGAFACARAAARLMSQ-----GGVIVNLGSIASLLALPPRNAYCASK 418

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQyieykDHIKDMIKYYGILDPPLIANGLITLIED 235
Cdd:PRK06484 419 AAVTMLSRS--LACEWAPAGIRVNTVAPGYIETPAVLALKASGRADF-----DSIRRRIPLGRLGDPEEVAEAIAFLASP 491

                        250
                 ....*....|..
gi 1203982   236 DA--LNGAIMKI 245
Cdd:PRK06484 492 AAsyVNGATLTV 503
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 5-205 2.60e-32

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: 119.09  E-value: 2.60e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVA---DQQQLRDTfrkVVDH 81
Cdd:cd05329   6 GKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREK--GFKVEGSVCDVSsrsERQELMDT---VASH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   82 F-GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMsKQNGgeGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:cd05329  81 FgGKLNILVNNAGTNirkeakdyTEEDYSLIMSTNFEAAYHLSRLAHPLL-KASG--NGNIVFISSVAGVIAVPSGAPYG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 1203982  153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILES-IEKEENMGQYIE 205
Cdd:cd05329 158 ATKGALNQLTRS--LACEWAKDNIRVNAVAPWVIATPLVEPvIQQKENLDKVIE 209
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 3-185 2.86e-32

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 119.62  E-value: 2.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAA--GGEALAVKADVLDKESLEQARQQILEDF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVNN-----------------------EKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSL 139
Cdd:PRK08277  86 GPCDILINGAGGNHpkattdnefhelieptktffdldEEGFEFVFDLNLLGTLLPTQVFAKDMVGR---KGGNIINISSM 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 1203982   140 AGLMPVAQQPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGF 185
Cdd:PRK08277 163 NAFTPLTKVPAYSAAKAAISNFTQ--WLAVHFAKVGIRVNAIAPGF 206
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 5-203 4.16e-32

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: 118.93  E-value: 4.16e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALV--DWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:cd05355  26 GKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEE--EGRKCLLIPGDLGDESFCRDLVKEVVKEF 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAGLMPVAQQPVYCA 153
Cdd:cd05355 104 GKLDILVNNAAYQhpqesiediTTEQLEKTFRTNIFSMFYLTKAALPHLKK-----GSSIINTTSVTAYKGSPHLLDYAA 178

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 1203982  154 SKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQY 203
Cdd:cd05355 179 TKGAIVAFTRG--LSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKVSEF 226
PRK09242 PRK09242
SDR family oxidoreductase;
4-205 4.17e-32

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 118.70  E-value: 4.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK09242   8 DGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDHWD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK09242  88 GLHILVNNAGGNirkaaidyTEDEWRGIFETNLFSAFELSRYAHPLLKQH---ASSAIVNIGSVSGLTHVRSGAPYGMTK 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILES-IEKEENMGQYIE 205
Cdd:PRK09242 165 AALLQMTRN--LAVEWAEDGIRVNAVAPWYIRTPLTSGpLSDPDYYEQVIE 213
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 6-208 1.08e-31

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: 116.57  E-value: 1.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGA-KVALVDWNLEAGVQCKAALHEQFepQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEG--LSVRFHQLDVTDDASIEAAADFVEEKYGG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAqqpvYCASK 155
Cdd:cd05324  79 LDILVNNAGIafkgfddstPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGR---IVNVSSGLGSLTSA----YGVSK 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 1203982  156 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAilesiekeenMGQYIEYKD 208
Cdd:cd05324 152 AALNALTR--ILAKELKETGIKVNACCPGWVKTD----------MGGGKAPKT 192
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-184 1.89e-31

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: 116.53  E-value: 1.89e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALhEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05369   3 GKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEI-SSATGGRAHPIQCDVRDPEAVEAAVDETLKEFGK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVN--------NEKNWEKTLQINLVsvisGTYlgldYMSKQNG------GEGGIIINMSSLAGLMPVAQQPV 150
Cdd:cd05369  82 IDILINNAAGNflapaeslSPNGFKTVIDIDLN----GTF----NTTKAVGkrlieaKHGGSILNISATYAYTGSPFQVH 153

                       170       180       190
                ....*....|....*....|....*....|....
gi 1203982  151 YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPG 184
Cdd:cd05369 154 SAAAKAGVDALTRS--LAVEWGPYGIRVNAIAPG 185
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 4-201 2.62e-31

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: 116.22  E-value: 2.62e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQcKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd05362   2 AGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAE-EVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGV--------NNEKNWEKTLQINlvsvISGTYLGLDYMSKqNGGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05362  81 GVDILVNNAGVmlkkpiaeTSEEEFDRMFTVN----TKGAFFVLQEAAK-RLRDGGRIINISSSLTAAYTPNYGAYAGSK 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 1203982  156 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAIL------ESIEKEENMG 201
Cdd:cd05362 156 AAVEAFTR--VLAKELGGRGITVNAVAPGPVDTDMFyagkteEAVEGYAKMS 205
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 8-199 2.67e-31

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: 115.91  E-value: 2.67e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGAKVALVDW-NLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRkSKDAAAEVAAEIEEL--GGKAVVVRADVSQPQDVEEMFAAVKERFGRLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   87 ILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHGI 158
Cdd:cd05359  79 VLVSNAAAGafrplselTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGR---IVAISSLGSIRALPNYLAVGTAKAAL 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 1203982  159 VGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEEN 199
Cdd:cd05359 156 EALVRY--LAVELGPRGIRVNAVSPGVIDTDALAHFPNRED 194
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-189 3.97e-31

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 115.45  E-value: 3.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDwnleagVQCKAALHEQFEpqktlFIQCDvadqqqLRDTFRKVVDHFGR 84
Cdd:PRK06550   5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVD------KQDKPDLSGNFH-----FLQLD------LSDDLEPLFDWVPS 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK06550  68 VDILCNTAGIlddykplldTSLEEWQHIFDTNLTSTFLLTRAYLPQMLER---KSGIIINMCSIASFVAGGGGAAYTASK 144

                        170       180       190
                 ....*....|....*....|....*....|....
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTA 189
Cdd:PRK06550 145 HALAGFTKQ--LALDYAKDGIQVFGIAPGAVKTP 176
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 5-188 4.19e-31

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: 115.43  E-value: 4.19e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAAL--HEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIeaEANASGQKVSYISADLSDYEEVEQAFAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVNNEKNWE--------KTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:cd08939  81 GPPDLVVNCAGISIPGLFEdltaeefeRGMDVNYFGSLNVAHAVLPLMKEQ---RPGHIVFVSSQAALVGIYGYSAYCPS 157

                       170       180       190
                ....*....|....*....|....*....|....
gi 1203982  155 KHGIVGFtrSAALAANLMNSGVRLNAICPGFVNT 188
Cdd:cd08939 158 KFALRGL--AESLRQELKPYNIRVSVVYPPDTDT 189
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 7-195 9.22e-31

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: 114.65  E-value: 9.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALHEQFEPQKTLFIqCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDIN-EKGAEETANNVRKAGGKVHYYK-CDVSKREEVYEAAKKIKKEVGDVT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   87 ILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHGI 158
Cdd:cd05339  79 ILINNAGVvsgkklleLPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGH---IVTIASVAGLISPAGLADYCASKAAA 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 1203982  159 VGFTRSAALAANLMN-SGVRLNAICPGFVNTAILESIE 195
Cdd:cd05339 156 VGFHESLRLELKAYGkPGIKTTLVCPYFINTGMFQGVK 193
PRK06194 PRK06194
hypothetical protein; Provisional
 5-193 9.45e-31

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 115.88  E-value: 9.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPqkTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06194   6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAE--VLGVRTDVSDAAQVEALADAALERFGA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYM---SKQNGGEGGIIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK06194  84 VHLLFNNAGVgagglvweNSLADWEWVLGVNLWGVIHGVRAFTPLMlaaAEKDPAYEGHIVNTASMAGLLAPPAMGIYNV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 1203982   154 SKHGIVGFTRSaaLAANLMNSGVRLNA--ICPGFVNTAILES 193
Cdd:PRK06194 164 SKHAVVSLTET--LYQDLSLVTDQVGAsvLCPYFVPTGIWQS 203
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-245 1.52e-30

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 114.43  E-value: 1.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVAlvdwnleagVQCKAALHEQFEPQK--------TLFIQCDVADQQQLR 72
Cdd:PRK06077   2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVV---------VNAKKRAEEMNETLKmvkenggeGIGVLADVSTREGCE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    73 DTFRKVVDHFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSSLAGLMP 144
Cdd:PRK06077  73 TLAKATIDRYGVADILVNNAGLGlfspflnvDDKLIDKHISTDFKSVIYCSQELAKEMR-----EGGAIVNIASVAGIRP 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   145 VAQQPVYCASKHGIVGFTRSAALAanlMNSGVRLNAICPGFVNTAILESIEKEENMGQYiEYKDHIKDMIKyygILDPPL 224
Cdd:PRK06077 148 AYGLSIYGAMKAAVINLTKYLALE---LAPKIRVNAIAPGFVKTKLGESLFKVLGMSEK-EFAEKFTLMGK---ILDPEE 220

                        250       260
                 ....*....|....*....|.
gi 1203982   225 IANGLITLIEDDALNGAIMKI 245
Cdd:PRK06077 221 VAEFVAAILKIESITGQVFVL 241
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-184 1.69e-30

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: 113.97  E-value: 1.69e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQkTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNR-VIALELDITSKESIKELIESYLEKFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGVNN-----------EKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLM--------- 143
Cdd:cd08930  80 RIDILINNAYPSPkvwgsrfeefpYEQWNEVLNVNLGGAFLCSQAFIKLFKKQG---KGSIINIASIYGVIapdfriyen 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 1203982  144 PVAQQPV-YCASKHGIVGFTRsaALAANLMNSGVRLNAICPG 184
Cdd:cd08930 157 TQMYSPVeYSVIKAGIIHLTK--YLAKYYADTGIRVNAISPG 196
PRK07774 PRK07774
SDR family oxidoreductase;
1-189 1.84e-30

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 114.07  E-value: 1.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK07774   2 GRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVA--DGGTAIAVQVDVSDPDSAKAMADATVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNNE-----------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPvaqQP 149
Cdd:PRK07774  80 AFGGIDYLVNNAAIYGGmkldllitvpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGA---IVNQSSTAAWLY---SN 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 1203982   150 VYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTA 189
Cdd:PRK07774 154 FYGLAKVGLNGLTQQ--LARELGGMNIRVNAIAPGPIDTE 191
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 7-188 1.92e-30

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: 113.63  E-value: 1.92e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:cd05360   2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVREL--GGEAIAVVADVADAAQVERAADTAVERFGRID 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   87 ILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggIIINMSSLAGLMPVAQQPVYCASKHGI 158
Cdd:cd05360  80 TWVNNAGVAvfgrfedvTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGG---ALINVGSLLGYRSAPLQAAYSASKHAV 156

                       170       180       190
                ....*....|....*....|....*....|
gi 1203982  159 VGFTRSAALAANLMNSGVRLNAICPGFVNT 188
Cdd:cd05360 157 RGFTESLRAELAHDGAPISVTLVQPTAMNT 186
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-188 2.17e-30

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 113.74  E-value: 2.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALheqfePQKTLFI-QCDVADQQQLRDTFRKVV 79
Cdd:PRK12828   3 HSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGV-----PADALRIgGIDLVDPQAARRAVDEVN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    80 DHFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVY 151
Cdd:PRK12828  78 RQFGRLDALVNIAGAfvwgtiadGDADTWDRMYGVNVKTTLNASKAALPALTASGGGR---IVNIGAGAALKAGPGMGAY 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1203982   152 CASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK12828 155 AAAKAGVARLTE--ALAAELLDRGITVNAVLPSIIDT 189
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 5-192 3.74e-30

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: 113.38  E-value: 3.74e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPqkTLF-IQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd05343   6 GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYP--TLFpYQCDLSNEEQILSMFSAIRTQHQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGiIINMSSLAG--LMPVAQQPVYCA 153
Cdd:cd05343  84 GVDVCINNAGLarpepllsGKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGH-IININSMSGhrVPPVSVFHFYAA 162

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 1203982  154 SKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:cd05343 163 TKHAVTALTEGLRQELREAKTHIRATSISPGLVETEFAF 201
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 3-188 4.47e-30

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 115.02  E-value: 4.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVqckAALHEQFEPQ--KTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARG-EEGL---EALAAEIRAAggEALAVVADVADAEAVQAAADRAEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK07109  82 ELGPIDTWVNNAMVTvfgpfedvTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRG---AIIQVGSALAYRSIPLQSAYC 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   153 ASKHGIVGFTRSaaLAANLM--NSGVRLNAICPGFVNT 188
Cdd:PRK07109 159 AAKHAIRGFTDS--LRCELLhdGSPVSVTMVQPPAVNT 194
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 4-237 4.50e-30

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 113.28  E-value: 4.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQcKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK08936   6 EGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEAN-DVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNggEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK08936  85 TLDVMINNAGIENAvpshemslEDWNKVINTNLTGAFLGSREAIKYFVEHD--IKGNIINMSSVHEQIPWPLFVHYAASK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAIleSIEKEENMGQYieykDHIKDMIKYYGILDPPLIANGLITLIED 235
Cdd:PRK08936 163 GGVKLMTET--LAMEYAPKGIRVNNIGPGAINTPI--NAEKFADPKQR----ADVESMIPMGYIGKPEEIAAVAAWLASS 234


                 ..
gi 1203982   236 DA 237
Cdd:PRK08936 235 EA 236
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 4-189 5.98e-30

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: 113.32  E-value: 5.98e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd08935   4 KNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITAL--GGRAIALAADVLDRASLERAREEIVAQFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGVNN----------------------EKNWEKTLQINLVsvisGTYLGLDYMSKQ-NGGEGGIIINMSSLA 140
Cdd:cd08935  82 TVDILINGAGGNHpdattdpehyepeteqnffdldEEGWEFVFDLNLN----GSFLPSQVFGKDmLEQKGGSIINISSMN 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 1203982  141 GLMPVAQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTA 189
Cdd:cd08935 158 AFSPLTKVPAYSAAKAAVSNFTQW--LAVEFATTGVRVNAIAPGFFVTP 204
PRK08267 PRK08267
SDR family oxidoreductase;
9-193 5.99e-30

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 113.11  E-value: 5.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     9 LVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVqckAALHEQFEPQKTLFIQCDVADqqqlRDTFRKVVDHF-----G 83
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDIN-EAGL---AALAAELGAGNAWTGALDVTD----RAAWDAALADFaaatgG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK08267  77 RLDVLFNNAGIlrggpfedIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGA---RVINTSSASAIYGQPGLAVYSATK 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   156 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:PRK08267 154 FAVRGLTE--ALDLEWRRHGIRVADVMPLFVDTAMLDG 189
PRK06398 PRK06398
aldose dehydrogenase; Validated
 5-222 6.41e-30

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 113.00  E-value: 6.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDwnleagvqckaaLHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06398   6 DKVAIVTGGSQGIGKAVVNRLKEEGSNVINFD------------IKEP-SYNDVDYFKVDVSNKEQVIKGIDYVISKYGR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:PRK06398  73 IDILVNNAGIEsygaihavEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD---KGVIINIASVQSFAVTRNAAAYVTSKH 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1203982   157 GIVGFTRSAAL-AANLmnsgVRLNAICPGFVNTAILESIEKEEnMGqyiEYKDHIKDMIKYYGILDP 222
Cdd:PRK06398 150 AVLGLTRSIAVdYAPT----IRCVAVCPGSIRTPLLEWAAELE-VG---KDPEHVERKIREWGEMHP 208
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 1.00e-29

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 111.70  E-value: 1.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALHEQFEpQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK07666   3 QSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLART-EENLKAVAEEVEAYG-VKVVIATADVSDYEEVTAAIEQLKN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK07666  81 ELGSIDILINNAGISKFGKfleldpaeWEKIIQVNLMGVYYATRAVLPSMIERQSGD---IINISSTAGQKGAAVTSAYS 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 1203982   153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07666 158 ASKFGVLGLTES--LMQEVRKHNIRVTALTPSTVAT 191
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 6-200 1.06e-29

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: 111.39  E-value: 1.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVqckAALHEQFEPQKTLFIQCDVADqqqlRDTFRKVVDHF--- 82
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGWFVGLYDID-EDGL---AALAAELGAENVVAGALDVTD----RAAWAAALADFaaa 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 --GRLDILVNNAGVNNEKNWEKT--------LQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:cd08931  73 tgGRLDALFNNAGVGRGGPFEDVplaahdrmVDINVKGVLNGAYAALPYLKAT---PGARVINTASSSAIYGQPDLAVYS 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 1203982  153 ASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENM 200
Cdd:cd08931 150 ATKFAVRGLTE--ALDVEWARHGIRVADVWPWFVDTPILTKGETGAAP 195
PLN02253 PLN02253
xanthoxin dehydrogenase
 5-190 1.16e-29

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 112.61  E-value: 1.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PLN02253  18 GKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGE---PNVCFFHCDVTVEDDVSRAVDFTVDKFGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNNEK----------NWEKTLQINLVsvisGTYLGLDY----MSKQNGGEggiIINMSSLAGLMPVAQQPV 150
Cdd:PLN02253  95 LDIMVNNAGLTGPPcpdirnvelsEFEKVFDVNVK----GVFLGMKHaariMIPLKKGS---IVSLCSVASAIGGLGPHA 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 1203982   151 YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PLN02253 168 YTGSKHAVLGLTRS--VAAELGKHGIRVNCVSPYAVPTAL 205
PRK07035 PRK07035
SDR family oxidoreductase;
5-188 1.26e-29

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 112.03  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALHEQFEP-QKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK07035   8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDG---CQAVADAIVAAgGKAEALACHIGEMEQIDALFAHIRERHG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN---------NEKNWEKTLQINlvsvISGTYlgldYMSKQNG-----GEGGIIINMSSLAGLMPVAQQP 149
Cdd:PRK07035  85 RLDILVNNAAANpyfghildtDLGAFQKTVDVN----IRGYF----FMSVEAGklmkeQGGGSIVNVASVNGVSPGDFQG 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   150 VYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07035 157 IYSITKAAVISMTK--AFAKECAPFGIRVNALLPGLTDT 193
PRK05650 PRK05650
SDR family oxidoreductase;
9-193 1.54e-29

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 112.06  E-value: 1.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     9 LVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDIL 88
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREA--GGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    89 VNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHGIVG 160
Cdd:PRK05650  82 VNNAGVASGgffeelslEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGR---IVNIASMAGLMQGPAMSSYNVAKAGVVA 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 1203982   161 FtrSAALAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:PRK05650 159 L--SETLLVELADDEIGVHVVCPSFFQTNLLDS 189
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 5-184 2.85e-29

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 111.28  E-value: 2.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMAYGFGADATSEQSVLALSRGVDEIFGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN--------NEKNWEKTLQINLVsvisGTYLGLDYMSKQ--NGGEGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK12384  82 VDLLVYNAGIAkaafitdfQLGDFDRSLQVNLV----GYFLCAREFSRLmiRDGIQGRIIQINSKSGKVGSKHNSGYSAA 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 1203982   155 KHGIVGFTRSAALaaNLMNSGVRLNAICPG 184
Cdd:PRK12384 158 KFGGVGLTQSLAL--DLAEYGITVHSLMLG 185
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 1-203 3.51e-29

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 110.71  E-value: 3.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK06113   7 LRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQL--GGQAFACRCDITSEQELSALADFALS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNNEK-------NWEKTLQINLVSVISGTYLGLDYMSKqNGgeGGIIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK06113  85 KLGKVDILVNNAGGGGPKpfdmpmaDFRRAYELNVFSFFHLSQLVAPEMEK-NG--GGVILTITSMAAENKNINMTSYAS 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1203982   154 SKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESI---EKEENMGQY 203
Cdd:PRK06113 162 SKAAASHLVRN--MAFDLGEKNIRVNGIAPGAILTDALKSVitpEIEQKMLQH 212
PRK06124 PRK06124
SDR family oxidoreductase;
5-188 4.19e-29

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 110.57  E-value: 4.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN---LEAGVQCKAALHEQFEPqktlfIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNaatLEAAVAALRAAGGAAEA-----LAFDIADEEAVAAAFARIDAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAGVNNEKNWEKT--------LQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK06124  86 HGRLDILVNNVGARDRRPLAELddaairalLETDLVAPILLSRLAAQRMKRQGYGR---IIAITSIAGQVARAGDAVYPA 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   154 SKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK06124 163 AKQGLTGLMR--ALAAEFGPHGITSNAIAPGYFAT 195
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 6-194 4.26e-29

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: 110.71  E-value: 4.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQ-FEPQKTLfiqCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd08945   4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAgVEADGRT---CDVRSVPEIEALVAAAVARYGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLdymskQNGGEG----GIIINMSSLAGLMPVAQQPVYC 152
Cdd:cd08945  81 IDVLVNNAGRSgggataelADELWLDVVETNLTGVFRVTKEVL-----KAGGMLergtGRIINIASTGGKQGVVHAAPYS 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 1203982  153 ASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI 194
Cdd:cd08945 156 ASKHGVVGFTK--ALGLELARTGITVNAVCPGFVETPMAASV 195
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 1-200 4.32e-29

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: 110.25  E-value: 4.32e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqcKAALHEQFEPQKTlfIQCDVADQQQLRDTFRKVVD 80
Cdd:COG3967   1 MKLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEK----LEEAAAANPGLHT--IVLDVADPASIAALAEQVTA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   81 HFGRLDILVNNAGV-------NNEKNWEK---TLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPV 150
Cdd:COG3967  75 EFPDLNVLINNAGImraedllDEAEDLADaerEITTNLLGPIRLTAAFLPHLKAQ---PEAAIVNVSSGLAFVPLAVTPT 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 1203982  151 YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEENM 200
Cdd:COG3967 152 YSATKAALHSYTQS--LRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRA 199
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 4-188 4.79e-29

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 110.76  E-value: 4.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEagvqcKAALHEQFEpqktlFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPA-----RAAPIPGVE-----LLELDVTDDASVQAAVDEVIARAG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN-----NEKNWEKTLQI---NLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK06179  73 RIDVLVNNAGVGlagaaEESSIAQAQALfdtNVFGILRMTRAVLPHMRAQGSGR---IINISSVLGFLPAPYMALYAASK 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK06179 150 HAVEGYSES--LDHEVRQFGIRVSLVEPAYTKT 180
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 6-245 6.26e-29

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: 109.67  E-value: 6.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNA-LRNSAVLVQADLSDFAACADLVAAAFRAFGRC 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGV--------NNEKNWEKTLQINLvsvISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:cd05357  80 DVLVNNASAfyptplgqGSEDAWAELFGINL---KAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  158 IVGFTRSAA--LAANlmnsgVRLNAICPGFVNtailesiekeENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIED 235
Cdd:cd05357 157 LEGLTRSAAleLAPN-----IRVNGIAPGLIL----------LPEDMDAEYRENALRKVPLKRRPSAEEIADAVIFLLDS 221

                       250
                ....*....|
gi 1203982  236 DALNGAIMKI 245
Cdd:cd05357 222 NYITGQIIKV 231
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 5-237 6.85e-29

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: 109.59  E-value: 6.85e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepqkTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPN-----LFFVHGDVADETLVKFVVYAMLEKLGR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVNNEKN--------WEKTLQINLVSVISGTYLGLDYMSKQNggegGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:cd09761  76 IDVLVNNAARGSKGIlssllleeWDRILSVNLTGPYELSRYCRDELIKNK----GRIINIASTRAFQSEPDSEAYAASKG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  157 GIVGFTRsaALAANLmNSGVRLNAICPGFVNTAilesiEKEENMGQYIEYKDHIKDMIKYYGilDPPLIANGLITLIEDD 236
Cdd:cd09761 152 GLVALTH--ALAMSL-GPDIRVNCISPGWINTT-----EQQEFTAAPLTQEDHAQHPAGRVG--TPKDIANLVLFLCQQD 221


                .
gi 1203982  237 A 237
Cdd:cd09761 222 A 222
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 6-188 1.01e-28

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: 109.29  E-value: 1.01e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFePQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKF-PVKVLPLQLDVSDRESIEAALENLPEEFRDI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:cd05346  80 DILVNNAGLalgldpaqeADLEDWETMIDTNVKGLLNVTRLILPIMIARNQG---HIINLGSIAGRYPYAGGNVYCATKA 156

                       170       180       190
                ....*....|....*....|....*....|..
gi 1203982  157 GIVGFtrSAALAANLMNSGVRLNAICPGFVNT 188
Cdd:cd05346 157 AVRQF--SLNLRKDLIGTGIRVTNIEPGLVET 186
PRK06914 PRK06914
SDR family oxidoreductase;
4-254 1.10e-28

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 110.11  E-value: 1.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRdTFRKVVDHFG 83
Cdd:PRK06914   2 NKKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNIKVQQLDVTDQNSIH-NFQLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLM-PVAQQPvYCAS 154
Cdd:PRK06914  81 RIDLLVNNAGYANGgfveeipvEEYRKQFETNVFGAISVTQAVLPYMRKQKSGK---IINISSISGRVgFPGLSP-YVSS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   155 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKE-----ENMGQYIEY----KDHIKDMIKYYGilDPPLI 225
Cdd:PRK06914 157 KYALEGFSES--LRLELKPFGIDVALIEPGSYNTNIWEVGKQLaenqsETTSPYKEYmkkiQKHINSGSDTFG--NPIDV 232

                        250       260
                 ....*....|....*....|....*....
gi 1203982   226 ANGLITLIEDDALNgaiMKITTSKGIHFQ 254
Cdd:PRK06914 233 ANLIVEIAESKRPK---LRYPIGKGVKLM 258
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 7-232 1.63e-28

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: 108.81  E-value: 1.63e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALheQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAI--QQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGIT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   87 ILVNNAG---------VNNEKNWEKTLQINLVSVISGTYLGLDYMsKQNGgeGGIIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:cd05365  79 ILVNNAGgggpkpfdmPMTEEDFEWAFKLNLFSAFRLSQLCAPHM-QKAG--GGAILNISSMSSENKNVRIAAYGSSKAA 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1203982  158 IVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKEEnmgqyIEYKDHIKDMIKYYGilDPPLIANGLITL 232
Cdd:cd05365 156 VNHMTRN--LAFDLGPKGIRVNAVAPGAVKTDALASVLTPE-----IERAMLKHTPLGRLG--EPEDIANAALFL 221
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-183 2.02e-28

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 113.79  E-value: 2.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK08324 422 GKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP---DRALGVACDVTDEAAVQAAFEEAALAFGG 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGV--------NNEKNWEKTLQINLvsviSGTYLGLDY----MSKQngGEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK08324 499 VDIVVSNAGIaisgpieeTSDEDWRRSFDVNA----TGHFLVAREavriMKAQ--GLGGSIVFIASKNAVNPGPNFGAYG 572

                        170       180       190
                 ....*....|....*....|....*....|.
gi 1203982   153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICP 183
Cdd:PRK08324 573 AAKAAELHLVRQ--LALELGPDGIRVNGVNP 601
PRK07856 PRK07856
SDR family oxidoreductase;
4-188 3.86e-28

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 108.10  E-value: 3.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKValvdwnleagVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK07856   5 TGRVVLVTGGTRGIGAGIARAFLAAGATV----------VVCGRRAPETVDGRPAEFHAADVRDPDQVAALVDAIVERHG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAG--------VNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGgeGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK07856  75 RLDVLVNNAGgspyalaaEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPG--GGSIVNIGSVSGRRPSPGTAAYGAAK 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   156 HGIVGFTRSAAL--AANlmnsgVRLNAICPGFVNT 188
Cdd:PRK07856 153 AGLLNLTRSLAVewAPK-----VRVNAVVVGLVRT 182
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 4-184 4.13e-28

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: 107.86  E-value: 4.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALV-----------DWNLEAGVQCKAALHEQfEPQKTLFIQCDVADQQQLR 72
Cdd:cd05338   2 SGKVAFVTGASRGIGRAIALRLAKAGATVVVAaktasegdngsAKSLPGTIEETAEEIEA-AGGQALPIVVDVRDEDQVR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   73 DTFRKVVDHFGRLDILVNNAGV----NNE----KNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMP 144
Cdd:cd05338  81 ALVEATVDQFGRLDILVNNAGAiwlsLVEdtpaKRFDLMQRVNLRGTYLLSQAALPHMVKA---GQGHILNISPPLSLRP 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 1203982  145 VAQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPG 184
Cdd:cd05338 158 ARGDVAYAAGKAGMSRLTLG--LAAELRRHGIAVNSLWPS 195
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 5-191 5.72e-28

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: 108.08  E-value: 5.72e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVNN------EKNWEKTLQINlvsvisgtYLG--------LDYMSKQNGGEggiIINMSSLAGLM------- 143
Cdd:cd05327  81 LDILINNAGIMApprrltKDGFELQFAVN--------YLGhflltnllLPVLKASAPSR---IVNVSSIAHRAgpidfnd 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 1203982  144 -------PVAQQPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAIL 191
Cdd:cd05327 150 ldlennkEYSPYKAYGQSKLANILFTR--ELARRLEGTGVTVNALHPGVVRTELL 202
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 8-194 5.79e-28

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: 107.03  E-value: 5.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfEPQKTLFIqCDVADQQQLRDTFRKVVDHFGRLDI 87
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNP-NPSVEVEI-LDVTDEERNQLVIAELEAELGGLDL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   88 LVNNAGVNNEKNWE--------KTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHGIV 159
Cdd:cd05350  79 VIINAGVGKGTSLGdlsfkafrETIDTNLLGAAAILEAALPQFRAKGRGH---LVLISSVAALRGLPGAAAYSASKAALS 155

                       170       180       190
                ....*....|....*....|....*....|....*
gi 1203982  160 GFTRSaaLAANLMNSGVRLNAICPGFVNTAILESI 194
Cdd:cd05350 156 SLAES--LRYDVKKRGIRVTVINPGFIDTPLTANM 188
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 5-192 1.20e-27

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: 107.02  E-value: 1.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNL-EAGVQCKAALHEQFE------PQKTLFIQCDVADQQQLRDTFRK 77
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDLCAdDPAVGYPLATRAELDavaaacPDQVLPVIADVRDPAALAAAVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     78 VVDHFGRLDILVNNAGV--NNEKNWEKT-------LQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQ 148
Cdd:TIGR04504  81 AVERWGRLDAAVAAAGViaGGRPLWETTdaeldllLDVNLRGVWNLARAAVPAMLARPDPRGGRFVAVASAAATRGLPHL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1203982    149 PVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:TIGR04504 161 AAYCAAKHAVVGLVRG--LAADLGGTGVTANAVSPGSTRTAMLA 202
PRK08589 PRK08589
SDR family oxidoreductase;
3-202 1.57e-27

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 106.79  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKtlfIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIKSNGGKAKA---YHVDISDEQQVKDFASEIKEQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVNNEKN---------WEKTLQINLvsviSGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK08589  81 GRVDVLFNNAGVDNAAGriheypvdvFDKIMAVDM----RGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1203982   154 SKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIE--KEENMGQ 202
Cdd:PRK08589 157 AKGAVINFTKSIAI--EYGRDGIRANAIAPGTIETPLVDKLTgtSEDEAGK 205
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-193 1.87e-27

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: 105.47  E-value: 1.87e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfepqkTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:cd05370   1 MKLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN------IHTIVLDVGDAESVEALAEALLS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   81 HFGRLDILVNNAGVNNEKNWEK----------TLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMPVAQQPV 150
Cdd:cd05370  75 EYPNLDILINNAGIQRPIDLRDpasdldkadtEIDTNLIGPIRLIKAFLPHLKKQP---EATIVNVSSGLAFVPMAANPV 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 1203982  151 YCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:cd05370 152 YCATKAALHSYTL--ALRHQLKDTGVEVVEIVPPAVDTELHEE 192
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-199 2.47e-27

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 105.74  E-value: 2.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLeagvqcKAALHEQFEPqktlfIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK08220   4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAF------LTQEDYPFAT-----FVLDVSDAAAVAQVCQRLLA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGV--------NNEKNWEKTLQINlvsvISGTYlgldYMSKQ-----NGGEGGIIINMSSLAGLMPVAQ 147
Cdd:PRK08220  73 ETGPLDVLVNAAGIlrmgatdsLSDEDWQQTFAVN----AGGAF----NLFRAvmpqfRRQRSGAIVTVGSNAAHVPRIG 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1203982   148 QPVYCASKHGIVGFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIEKEEN 199
Cdd:PRK08220 145 MAAYGASKAALTSLAKCVGL--ELAPYGVRCNVVSPGSTDTDMQRTLWVDED 194
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-188 3.09e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 105.86  E-value: 3.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     2 HVNGKVALVTGAAQGIGRAFAEALLLKGAK-VALVDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK06198   3 RLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEAL--GAKAVFVQADLSDVEDCRRVVAAADE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNNEKN--------WEKTLQINLvsviSGTYL---GLDYMSKQNGGEGGI--IINMSSLAGlmpvaq 147
Cdd:PRK06198  81 AFGRLDALVNAAGLTDRGTildtspelFDRHFAVNV----RAPFFlmqEAIKLMRRRKAEGTIvnIGSMSAHGG------ 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   148 QP---VYCASKHGIVGFTRSAALAanLMNSGVRLNAICPGFVNT 188
Cdd:PRK06198 151 QPflaAYCASKGALATLTRNAAYA--LLRNRIRVNGLNIGWMAT 192
PRK06114 PRK06114
SDR family oxidoreductase;
3-188 3.58e-27

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 105.63  E-value: 3.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQcKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLA-ETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKqNGgeGGIIINMSSLAGLMpVAQ---QPVY 151
Cdd:PRK06114  85 GALTLAVNAAGIANanpaeemeEEQWQTVMDINLTGVFLSCQAEARAMLE-NG--GGSIVNIASMSGII-VNRgllQAHY 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1203982   152 CASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK06114 161 NASKAGVIHLSKS--LAMEWVGRGIRVNSISPGYTAT 195
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-183 4.86e-27

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 106.40  E-value: 4.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDwnLEAGVQCKAALHE-QFEPQKTLFIQCDVADQQQLRDTFRKVVDh 81
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVND--VASALDASDVLDEiRAAGAKAVAVAGDISQRATADELVATAVG- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDY---MSKQNGGE-GGIIINMSSLAGLMPVAQQP 149
Cdd:PRK07792  87 LGGLDIVVNNAGITrdrmlfnmSDEEWDAVIAVHLRGHFLLTRNAAAYwraKAKAAGGPvYGRIVNTSSEAGLVGPVGQA 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 1203982   150 VYCASKHGIVGFTRSAALAanLMNSGVRLNAICP 183
Cdd:PRK07792 167 NYGAAKAGITALTLSAARA--LGRYGVRANAICP 198
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 1-202 5.23e-27

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 104.82  E-value: 5.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVdwnlEAGVQCKA-ALHEQFEPQ--KTLFIQCDVADQQQLRDTFRK 77
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVN----YAGSAAAAdELVAEIEAAggRAIAVQADVADAAAVTRLFDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    78 VVDHFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMskqngGEGGIIINMSSLAGLMPVAQQP 149
Cdd:PRK12937  77 AETAFGRIDVLVNNAGVmplgtiadFDLEDFDRTIATNLRGAFVVLREAARHL-----GQGGRIINLSTSVIALPLPGYG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1203982   150 VYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQ 202
Cdd:PRK12937 152 PYAASKAAVEGLVH--VLANELRGRGITVNAVAPGPVATELFFNGKSAEQIDQ 202
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-188 5.50e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 104.80  E-value: 5.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNleagVQCKAALHEQF--EPqktlfIQCDVADQQQLRDTFrkv 78
Cdd:PRK07060   5 FDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARN----AAALDRLAGETgcEP-----LRLDVGDDAAIRAAL--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    79 vDHFGRLDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLGLDYMSKQ--NGGEGGIIINMSSLAGLMPVAQQ 148
Cdd:PRK07060  73 -AAAGAFDGLVNCAGIAslesaldmTAEGFDRVMAVNA----RGAALVARHVARAmiAAGRGGSIVNVSSQAALVGLPDH 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 1203982   149 PVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07060 148 LAYCASKAALDAITRV--LCVELGPHGIRVNSVNPTVTLT 185
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 4-184 5.77e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 105.51  E-value: 5.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqcKAALHEQFePQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTAT----LADLAEKY-GDRLLPLALDVTDRAAVFAAVETAVEHFG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK08263  77 RLDIVVNNAGYGlfgmieevTESEARAQIDTNFFGALWVTQAVLPYLREQRSGH---IIQISSIGGISAFPMSGIYHASK 153

                        170       180
                 ....*....|....*....|....*....
gi 1203982   156 HGIVGFtrSAALAANLMNSGVRLNAICPG 184
Cdd:PRK08263 154 WALEGM--SEALAQEVAEFGIKVTLVEPG 180
PRK05717 PRK05717
SDR family oxidoreductase;
4-188 7.21e-27

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 104.59  E-value: 7.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepqkTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK05717   9 NGRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGEN-----AWFIAMDVADEAQVAAGVAEVLGQFG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNEKN----------WEKTLQINLvsviSGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK05717  84 RLDALVCNAAIADPHNttleslslahWNRVLAVNL----TGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAA 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   154 SKHGIVGFTRsaALAANLmNSGVRLNAICPGFVNT 188
Cdd:PRK05717 160 SKGGLLALTH--ALAISL-GPEIRVNAVSPGWIDA 191
PRK07832 PRK07832
SDR family oxidoreductase;
6-195 1.07e-26

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 104.74  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWN---LEAGVQCKAALHEQFEPQKTLfiqcDVADQQQLRDTFRKVVDHF 82
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDadgLAQTVADARALGGTVPEHRAL----DISDYDAVAAFAADIHAAH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKqnGGEGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK07832  77 GSMDVVMNIAGISawgtvdrlTHEQWRRMVDVNLMGPIHVIETFVPPMVA--AGRGGHLVNVSSAAGLVALPWHAAYSAS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 1203982   155 KHGIVGFtrSAALAANLMNSGVRLNAICPGFVNTAILESIE 195
Cdd:PRK07832 155 KFGLRGL--SEVLRFDLARHGIGVSVVVPGAVKTPLVNTVE 193
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
5-208 1.77e-26

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 103.65  E-value: 1.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNleagvQCKAALHEQFEPQ----KTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK08063   4 GKVALVTGSSRGIGKAIALRLAEEGYDIAVNYAR-----SRKAAEETAEEIEalgrKALAVKANVGDVEKIKEMFAQIDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNA--GVN------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK08063  79 EFGRLDVFVNNAasGVLrpamelEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGK---IISLSSLGSIRYLENYTTVG 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1203982   153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT----------AILESIEKEENMGQYIEYKD 208
Cdd:PRK08063 156 VSKAALEALTRY--LAVELAPKGIAVNAVSGGAVDTdalkhfpnreELLEDARAKTPAGRMVEPED 219
PRK07074 PRK07074
SDR family oxidoreductase;
6-188 2.32e-26

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 103.31  E-value: 2.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAAL-HEQFEPqktlfIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALgDARFVP-----VACDLTDAASLAAALANAAAERGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGV--------NNEKNWEKTLQINLvsviSGTYLG----LDYMSKQNGGEggiIINMSSLAGlMPVAQQPVYC 152
Cdd:PRK07074  78 VDVLVANAGAaraaslhdTTPASWRADNALNL----EAAYLCveavLEGMLKRSRGA---VVNIGSVNG-MAALGHPAYS 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 1203982   153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07074 150 AAKAGLIHYTKL--LAVEYGRFGIRANAVAPGTVKT 183
PRK08628 PRK08628
SDR family oxidoreductase;
1-188 3.27e-26

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 103.11  E-value: 3.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK08628   3 LNLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRS-APDDEFAEELRAL--QPRAEFVQVDLTDDAQCRDAVEQTVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNNEKNWE-------KTLQINLVSVISGTYLGLDYMSKQNGGeggiIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK08628  80 KFGRIDGLVNNAGVNDGVGLEagreafvASLERNLIHYYVMAHYCLPHLKASRGA----IVNISSKTALTGQGGTSGYAA 155

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   154 SKHGIVGFTRSAALAanLMNSGVRLNAICPGFVNT 188
Cdd:PRK08628 156 AKGAQLALTREWAVA--LAKDGVRVNAVIPAEVMT 188
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 7-243 7.50e-26

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: 101.59  E-value: 7.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    7 VALVTGAAQGIGRAFAEALLLKG--AKVALVDWNLEAGVQCKAALheqFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEEL---RPGLRVTTVKADLSDAAGVEQLLEAIRKLDGE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDymSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05367  78 RDLLINNAGSlgpvskiefIDLDELQKYFDLNLTSPVCLTSTLLR--AFKKRGLKKTVVNVSSGAAVNPFKGWGLYCSSK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  156 HGIVGFTRsaALAANLmnSGVRLNAICPGFVNT----AILESIEKEENMGQYIEYKDHIKdmikyygILDPPLIANGLIT 231
Cdd:cd05367 156 AARDMFFR--VLAAEE--PDVRVLSYAPGVVDTdmqrEIRETSADPETRSRFRSLKEKGE-------LLDPEQSAEKLAN 224

                       250
                ....*....|...
gi 1203982  232 LIEDDA-LNGAIM 243
Cdd:cd05367 225 LLEKDKfESGAHV 237
PRK07062 PRK07062
SDR family oxidoreductase;
3-189 9.97e-26

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 102.04  E-value: 9.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEARF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAG---VNNEKN-----WEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK07062  86 GGVDMLVNNAGqgrVSTFADttddaWRDELELKYFSVINPTRAFLPLLRAS---AAASIVCVNSLLALQPEPHMVATSAA 162

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   155 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTA 189
Cdd:PRK07062 163 RAGLLNLVKS--LATELAPKGVRVNSILLGLVESG 195
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 3-189 2.82e-25

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 101.20  E-value: 2.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHeqfEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK05872   7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELG---GDDRVLTVVADVTDLAAMQAAAEEAVERF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQnggeGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK05872  84 GGIDVVVANAGIASggsvaqvdPDAFRRVIDVNLLGVFHTVRATLPALIER----RGYVLQVSSLAAFAAAPGMAAYCAS 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   155 KHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTA 189
Cdd:PRK05872 160 KAGVEAFAN--ALRLEVAHHGVTVGSAYLSWIDTD 192
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 5-183 3.13e-25

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: 100.16  E-value: 3.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHeqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQ---GGPRALGVQCDVTSEAQVQSAFEQAVLEFGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:cd08943  78 LDIVVSNAGIatsspiaeTSLEDWNRSMDINLTGHFLVSREAFRIMKSQ--GIGGNIVFNASKNAVAPGPNAAAYSAAKA 155

                       170       180
                ....*....|....*....|....*..
gi 1203982  157 GIVGFTRSAALaaNLMNSGVRLNAICP 183
Cdd:cd08943 156 AEAHLARCLAL--EGGEDGIRVNTVNP 180
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 4-184 4.52e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 100.37  E-value: 4.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgVQCKAALHeqfePQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAA-RADFEALH----PDRALARLLDVTDFDAIDAVVADAEATFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNEKNWEKT--------LQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK06180  78 PIDVLVNNAGYGHEGAIEESplaemrrqFEVNVFGAVAMTKAVLPGMRARRRGH---IVNITSMGGLITMPGIGYYCGSK 154

                        170       180
                 ....*....|....*....|....*....
gi 1203982   156 HGIVGFtrSAALAANLMNSGVRLNAICPG 184
Cdd:PRK06180 155 FALEGI--SESLAKEVAPFGIHVTAVEPG 181
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-188 9.15e-25

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 102.22  E-value: 9.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDwnleagV-QCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK08261 210 GKVALVTGAARGIGAAIAEVLARDGAHVVCLD------VpAAGEALAAVANRVGGTALALDITAPDAPARIAEHLAERHG 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN--------NEKNWEKTLQINLVS--VISGTYLGLDYMskqngGEGGIIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK08261 284 GLDIVVHNAGITrdktlanmDEARWDSVLAVNLLAplRITEALLAAGAL-----GDGGRIVGVSSISGIAGNRGQTNYAA 358

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1203982   154 SKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK08261 359 SKAGVIGLVQ--ALAPLLAERGITINAVAPGFIET 391
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-237 1.45e-24

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: 98.31  E-value: 1.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGAKVALVDwnleagvqCKAALHEQFEPQKTLFiQCDVADQQQLRDTFRKVVDHFGRLDI 87
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALD--------LPFVLLLEYGDPLRLT-PLDVADAAAVREVCSRLLAEHGPIDA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   88 LVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHGIV 159
Cdd:cd05331  72 LVNCAGVlrpgatdpLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGA---IVTVASNAAHVPRISMAAYGASKAALA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  160 GFTRSAALaaNLMNSGVRLNAICPGFVNTAILESIEKEEN-MGQYIEYK-DHIKDMIKYYGILDPPLIANGLITLIEDDA 237
Cdd:cd05331 149 SLSKCLGL--ELAPYGVRCNVVSPGSTDTAMQRTLWHDEDgAAQVIAGVpEQFRLGIPLGKIAQPADIANAVLFLASDQA 226
PRK12743 PRK12743
SDR family oxidoreductase;
6-188 3.05e-24

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 97.80  E-value: 3.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRS-HGVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    86 DILVNNAGVNNEK--------NWEKTLQINLvsviSGTYLGLDYMSKQ--NGGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK12743  82 DVLVNNAGAMTKApfldmdfdEWRKIFTVDV----DGAFLCSQIAARHmvKQGQGGRIINITSVHEHTPLPGASAYTAAK 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 1203982   156 HGIVGFTRSAALaaNLMNSGVRLNAICPGFVNT 188
Cdd:PRK12743 158 HALGGLTKAMAL--ELVEHGILVNAVAPGAIAT 188
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 5-190 3.15e-24

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: 97.29  E-value: 3.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFePQKTLFIQCDVADQqqlRDTFRKVVDHFGR 84
Cdd:cd05356   1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKY-GVETKTIAADFSAG---DDIYERIEKELEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDI--LVNNAGVN----------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:cd05356  77 LDIgiLVNNVGIShsipeyfletPEDELQDIINVNVMATLKMTRLILPGMVKR---KKGAIVNISSFAGLIPTPLLATYS 153

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 1203982  153 ASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:cd05356 154 ASKAFLDFFSR--ALYEEYKSQGIDVQSLLPYLVATKM 189
PRK09135 PRK09135
pteridine reductase; Provisional
 1-184 3.52e-24

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 97.31  E-value: 3.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK09135   2 MTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADALAAELNALRPGSAAALQADLLDPDALPELVAACVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNA--------GVNNEKNWEKTLQINL-----VSVISGTYLgldymsKQNGGEggiIINMSSLAGLMPVAQ 147
Cdd:PRK09135  82 AFGRLDALVNNAssfyptplGSITEAQWDDLFASNLkapffLSQAAAPQL------RKQRGA---IVNITDIHAERPLKG 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   148 QPVYCASKHGIVGFTRSAA--LAANlmnsgVRLNAICPG 184
Cdd:PRK09135 153 YPVYCAAKAALEMLTRSLAleLAPE-----VRVNAVAPG 186
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 3-198 3.99e-24

(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: 97.39  E-value: 3.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQF-------EPQKTLFIQCDVADQQQLRDTf 75
Cdd:cd05353   3 FDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSSSAADKvvdeikaAGGKAVANYDSVEDGEKIVKT- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   76 rkVVDHFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQ 147
Cdd:cd05353  82 --AIDAFGRVDILVNNAGIlrdrsfakMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGR---IINTSSAAGLYGNFG 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 1203982  148 QPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGfVNTAILESIEKEE 198
Cdd:cd05353 157 QANYSAAKLGLLGLSNT--LAIEGAKYNITCNTIAPA-AGSRMTETVMPED 204
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-188 4.24e-24

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 97.34  E-value: 4.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQckAALHE-QFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELA--ATQQElRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN----------NEKNWEKTLQINLvsviSGTYL-------GLDYMSKQNGGEGGIIINMSSLAGLMPVAQ 147
Cdd:PRK12745  81 IDCLVNNAGVGvkvrgdlldlTPESFDRVLAINL----RGPFFltqavakRMLAQPEPEELPHRSIVFVSSVNAIMVSPN 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 1203982   148 QPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK12745 157 RGEYCISKAGLSMAAQ--LFAARLAEEGIGVYEVRPGLIKT 195
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-190 5.08e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 96.92  E-value: 5.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqcKAALHEQFEPQ--KTLFIQCDVADQQQLRDTFRKV 78
Cdd:PRK07478   2 MRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAE----LDQLVAEIRAEggEAVALAGDVRDEAYAKALVALA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    79 VDHFGRLDILVNNAGVNNE---------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGL---MPva 146
Cdd:PRK07478  78 VERFGGLDIAFNNAGTLGEmgpvaemslEGWRETLATNLTSAFLGAKHQIPAMLARGGGS---LIFTSTFVGHtagFP-- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   147 QQPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK07478 153 GMAAYAASKAGLIGLTQ--VLAAEYGAQGIRVNALLPGGTDTPM 194
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-197 1.65e-23

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: 95.61  E-value: 1.65e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpQKTLFIQCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAG-RRAIYFQADIGELSDHEALLDQAWEDFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   87 ILVNNAGVN----------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGI---IINMSSLAGLMPVAQQPVYCA 153
Cdd:cd05337  82 CLVNNAGIAvrprgdlldlTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFDGPhrsIIFVTSINAYLVSPNRGEYCI 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 1203982  154 SKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKE 197
Cdd:cd05337 162 SKAGLSMATR--LLAYRLADEGIAVHEIRPGLIHTDMTAPVKEK 203
PRK09186 PRK09186
flagellin modification protein A; Provisional
 4-184 1.70e-23

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 95.83  E-value: 1.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK09186   3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLVELDITDQESLEEFLSKSAEKYG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNeKNWEKT------------LQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVA----- 146
Cdd:PRK09186  83 KIDGAVNCAYPRN-KDYGKKffdvslddfnenLSLHLGSSFLFSQQFAKYFKKQ---GGGNLVNISSIYGVVAPKfeiye 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   147 ----QQPV-YCASKHGIVGFTRsaALAANLMNSGVRLNAICPG 184
Cdd:PRK09186 159 gtsmTSPVeYAAIKAGIIHLTK--YLAKYFKDSNIRVNCVSPG 199
PRK06949 PRK06949
SDR family oxidoreductase;
5-190 3.66e-23

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 94.83  E-value: 3.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALheQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06949   9 GKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEI--EAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNneknwekTLQiNLVSVISGTYlglDYM----------------------SKQNGGE--GGIIINMSSLA 140
Cdd:PRK06949  87 IDILVNNSGVS-------TTQ-KLVDVTPADF---DFVfdtntrgaffvaqevakrmiarAKGAGNTkpGGRIINIASVA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 1203982   141 GLMPVAQQPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK06949 156 GLRVLPQIGLYCMSKAAVVHMTR--AMALEWGRHGINVNAICPGYIDTEI 203
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 3-201 4.17e-23

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 94.60  E-value: 4.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpqktlFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVK-----IFPANLSDRDEVKALGQKAEADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK12936  79 EGVDILVNNAGITkdglfvrmSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGR---IINITSVVGVTGNPGQANYCAS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 1203982   155 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAI---LESIEKEENMG 201
Cdd:PRK12936 156 KAGMIGFSKS--LAQEIATRNVTVNCVAPGFIESAMtgkLNDKQKEAIMG 203
PRK09730 PRK09730
SDR family oxidoreductase;
6-190 7.53e-23

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 93.76  E-value: 7.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVAlVDW--NLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVA-VNYqqNLHAAQEVVNLITQA--GGKAFVLQADISDENQVVAMFTAIDQHDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNNEKNWEKTL---QIN--LVSVISGTYL----GLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPV-YCA 153
Cdd:PRK09730  79 PLAALVNNAGILFTQCTVENLtaeRINrvLSTNVTGYFLccreAVKRMALKHGGSGGAIVNVSSAASRLGAPGEYVdYAA 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1203982   154 SKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK09730 159 SKGAIDTLTT--GLSLEVAAQGIRVNCVRPGFIYTEM 193
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 3-208 9.32e-23

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: 93.70  E-value: 9.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEA---CADAAEELSAYGECIAIPADLSSEEGIEALVARVAERS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSK-QNGGEGGIIINMSSLAGLM-PVAQQPVYC 152
Cdd:cd08942  81 DRLDVLVNNAGATwgapleafPESGWDKVMDINVKSVFFLTQALLPLLRAaATAENPARVINIGSIAGIVvSGLENYSYG 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1203982  153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPG--------FV--NTAILESIEKEENMGQYIEYKD 208
Cdd:cd08942 161 ASKAAVHQLTRK--LAKELAGEHITVNAIAPGrfpskmtaFLlnDPAALEAEEKSIPLGRWGRPED 224
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-204 1.38e-22

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 93.05  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVdwnleaGVQCKAALHEQFEP--QKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGV------GVAEAPETQAQVEAlgRKFHFITADLIQQKDIDSIVSQAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK12481  80 VMGHIDILINNAGIirrqdlleFGNKDWDDVININQKTVFFLSQAVAKQFVKQ--GNGGKIINIASMLSFQGGIRVPSYT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1203982   153 ASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 204
Cdd:PRK12481 158 ASKSAVMGLTR--ALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAI 207
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 4-188 3.97e-22

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: 92.03  E-value: 3.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALHEqfepQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:cd05348   3 KGEVALITGGGSGLGRALVERFVAEGAKVAVLDRS-AEKVAELRADFG----DAVVGVEGDVRSLADNERAVARCVERFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   84 RLDILVNNAGVNN------EKNWEK-------TLQINLVSVISGTYLGLDYMSKqngGEGGIIINMSSlAGLMPVAQQPV 150
Cdd:cd05348  78 KLDCFIGNAGIWDystslvDIPEEKldeafdeLFHINVKGYILGAKAALPALYA---TEGSVIFTVSN-AGFYPGGGGPL 153

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 1203982  151 YCASKHGIVGFTRsaALAANLMNSgVRLNAICPGFVNT 188
Cdd:cd05348 154 YTASKHAVVGLVK--QLAYELAPH-IRVNGVAPGGMVT 188
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 5-184 4.49e-22

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 91.93  E-value: 4.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN---LEAGVQCKAALHEqfepqkTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelvHEVAAELRAAGGE------ALALTADLETYAGAQAAMAAAVEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLA--GLMPVaqqPv 150
Cdd:PRK12823  82 FGRIDVLINNVGGTiwakpfeeyEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQG---GGAIVNVSSIAtrGINRV---P- 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 1203982   151 YCASKHGIVGFTrsAALAANLMNSGVRLNAICPG 184
Cdd:PRK12823 155 YSAAKGGVNALT--ASLAFEYAEHGIRVNAVAPG 186
PRK07814 PRK07814
SDR family oxidoreductase;
3-205 6.80e-22

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 91.76  E-value: 6.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVaLVDWNLEAGVQCKAALHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADV-LIAARTESQLDEVAEQIRA-AGRRAHVVAADLAHPEATAGLAGQAVEAF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAG--------VNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGgeGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK07814  86 GRLDIVVNNVGgtmpnpllSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSG--GGSVINISSTMGRLAGRGFAAYGTA 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1203982   155 KHGIVGFTRSAALAanlMNSGVRLNAICPGFVNTAILESIEKEENMGQYIE 205
Cdd:PRK07814 164 KAALAHYTRLAALD---LCPRIRVNAIAPGSILTSALEVVAANDELRAPME 211
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 1-188 1.04e-21

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 91.17  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEagvQCkAALHEQFePQKTLFIQCDV---ADQQQLRDTfrk 77
Cdd:PRK06200   2 GWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAE---KL-ASLRQRF-GDHVLVVEGDVtsyADNQRAVDQ--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    78 VVDHFGRLDILVNNAGVNN-------------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggiIINMSSLAGLMP 144
Cdd:PRK06200  74 TVDAFGKLDCFVGNAGIWDyntslvdipaetlDTAFDEIFNVNVKGYLLGAKAALPALKASGGS----MIFTLSNSSFYP 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   145 VAQQPVYCASKHGIVGFTRsaALAANLMnSGVRLNAICPGFVNT 188
Cdd:PRK06200 150 GGGGPLYTASKHAVVGLVR--QLAYELA-PKIRVNGVAPGGTVT 190
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-204 1.33e-21

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 90.70  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAeaLLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK08993  10 GKVAVVTGCDTGLGQGMA--LGLAEAGCDIVGINIVEPTETIEQVTA--LGRRFLSLTADLRKIDGIPALLERAVAEFGH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:PRK08993  86 IDILVNNAGLirredaieFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQ--GNGGKIINIASMLSFQGGIRVPSYTASKS 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 1203982   157 GIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYI 204
Cdd:PRK08993 164 GVMGVTR--LMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEI 209
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
 6-192 1.48e-21

mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function.


Pssm-ID: 468513 [Multi-domain]  Cd Length: 256  Bit Score: 90.50  E-value: 1.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGV-------QCKAALHEQFEPQKTLFIqCDVADQQQLRDTFRKV 78
Cdd:NF040491   1 RVALVTGAARGIGAATVRRLAARGYAVVAVDACAGDPApyplgteADLDALVASSPGRVETVV-ADVRDRAALAAAVALA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    79 VDHFGRLDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQP 149
Cdd:NF040491  80 LDRWGRLDAAVAAAAViaggrplweTPPEELDALWDVDVRGVWNLAAAAVPALLAGPDPRGCRFVAVASAAGHRGLFHLA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   150 VYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILE 192
Cdd:NF040491 160 AYCAAKHAVVGLVR--GLAADLAGTGVTACAVSPGSTDTPMLA 200
PRK05867 PRK05867
SDR family oxidoreductase;
3-194 2.24e-21

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 90.09  E-value: 2.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgVQcKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHF 82
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDA-LE-KLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAG-LMPVAQQ-PVYC 152
Cdd:PRK05867  85 GGIDIAVCNAGIITvtpmldmpLEEFQRLQNTNVTGVFLTAQAAAKAMVKQ--GQGGVIINTASMSGhIINVPQQvSHYC 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 1203982   153 ASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI 194
Cdd:PRK05867 163 ASKAAVIHLTK--AMAVELAPHKIRVNSVSPGYILTELVEPY 202
PRK06139 PRK06139
SDR family oxidoreductase;
1-188 2.64e-21

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 91.32  E-value: 2.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEagvqckaALHEQFEP-----QKTLFIQCDVADQQQLRDTF 75
Cdd:PRK06139   3 GPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEE-------ALQAVAEEcralgAEVLVVPTDVTDADQVKALA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    76 RKVVDHFGRLDILVNNAGVNNEKNWEKT--------LQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLmpvAQ 147
Cdd:PRK06139  76 TQAASFGGRIDVWVNNVGVGAVGRFEETpieaheqvIQTNLIGYMRDAHAALPIFKKQG---HGIFINMISLGGF---AA 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 1203982   148 QP---VYCASKHGIVGFtrSAALAANLMN-SGVRLNAICPGFVNT 188
Cdd:PRK06139 150 QPyaaAYSASKFGLRGF--SEALRGELADhPDIHVCDVYPAFMDT 192
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 5-200 2.87e-21

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: 89.91  E-value: 2.87e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALheQFEPQKTLFIQCDVA---DQQQLRDTfrkVVDH 81
Cdd:cd08936  10 NKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATL--QGEGLSVTGTVCHVGkaeDRERLVAT---AVNL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   82 FGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIinmSSLAGLMPVAQQPVYC 152
Cdd:cd08936  85 HGGVDILVSNAAVNpffgnildsTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIV---SSVAAFHPFPGLGPYN 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 1203982  153 ASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT----AILESIEKEENM 200
Cdd:cd08936 162 VSKTALLGLTK--NLAPELAPRNIRVNCLAPGLIKTsfssALWMDKAVEESM 211
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 3-183 3.07e-21

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 90.12  E-value: 3.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNL-----EAGVQCKAALHEQFEPQ--KTLFIQCDVADQQQLRDTF 75
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIGVgldgsASGGSAAQAVVDEIVAAggEAVANGDDIADWDGAANLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    76 RKVVDHFGRLDILVNNAGV--------NNEKNWEKTLQINLvsviSGTYLGLDYM-------SKQNGGEGGIIINMSSLA 140
Cdd:PRK07791  84 DAAVETFGGLDVLVNNAGIlrdrmianMSEEEWDAVIAVHL----KGHFATLRHAaaywraeSKAGRAVDARIINTSSGA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   141 GLMPVAQQPVYCASKHGIVGFTRSAalAANLMNSGVRLNAICP 183
Cdd:PRK07791 160 GLQGSVGQGNYSAAKAGIAALTLVA--AAELGRYGVTVNAIAP 200
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 4-197 3.28e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 89.58  E-value: 3.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqckaalheqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK06523   8 AGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRPDD-----------LPEGVEFVAADLTTAEGCAAVARAVLERLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAG----------VNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGeggIIINMSSLAGLMPVAQQPV-YC 152
Cdd:PRK06523  77 GVDILVHVLGgssapaggfaALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSG---VIIHVTSIQRRLPLPESTTaYA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 1203982   153 ASKHGIVgfTRSAALAANLMNSGVRLNAICPGFVNT----AILESIEKE 197
Cdd:PRK06523 154 AAKAALS--TYSKSLSKEVAPKGVRVNTVSPGWIETeaavALAERLAEA 200
PRK06947 PRK06947
SDR family oxidoreductase;
6-190 4.41e-21

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 89.09  E-value: 4.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRA-AGGRACVVAGDVANEADVIAMFDAVQSAFGRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    86 DILVNNAGVNNEK------NWEKTLQINLVSVIsGTYL----GLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPV-YCAS 154
Cdd:PRK06947  82 DALVNNAGIVAPSmpladmDAARLRRMFDTNVL-GAYLcareAARRLSTDRGGRGGAIVNVSSIASRLGSPNEYVdYAGS 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 1203982   155 KhGIVGfTRSAALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK06947 161 K-GAVD-TLTLGLAKELGPHGVRVNAVRPGLIETEI 194
PRK06500 PRK06500
SDR family oxidoreductase;
5-188 4.86e-21

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 88.86  E-value: 4.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfepqKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06500   6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGE-----SALVIRADAGDVAAQKALAQALAEAFGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN--------NEKNWEKTLQINLvsviSGTYLGLDYMSKQNGGEGGIIINMSSLAGL-MPvaQQPVYCASK 155
Cdd:PRK06500  81 LDAVFINAGVAkfapledwDEAMFDRSFNTNV----KGPYFLIQALLPLLANPASIVLNGSINAHIgMP--NSSVYAASK 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK06500 155 AALLSLAKT--LSGELLPRGIRVNAVSPGPVQT 185
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 6-188 1.23e-20

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: 87.90  E-value: 1.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfepQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAAEAG----ERAIAIQADVRDRDQVQAMIEEAKNHFGPV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   86 DILVNNA-------GVNNEK----NWEkTLQINLVSVISGTY----LGLDYMSKQNGGEggiIINMSSlaglmPVAQQPV 150
Cdd:cd05349  77 DTIVNNAlidfpfdPDQRKTfdtiDWE-DYQQQLEGAVKGALnllqAVLPDFKERGSGR---VINIGT-----NLFQNPV 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 1203982  151 -----YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:cd05349 148 vpyhdYTTAKAALLGFTRN--MAKELGPYGITVNMVSGGLLKV 188
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
6-197 2.89e-20

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 86.99  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVAlvdwnleAGVQCKAALHEQF-EPQKTL---FI--QCDVADQQQLRDTFRKVV 79
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVV-------AGCGPNSPRRVKWlEDQKALgfdFIasEGNVGDWDSTKAAFDKVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    80 DHFGRLDILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVY 151
Cdd:PRK12938  77 AEVGEIDVLVNNAGITRDvvfrkmtrEDWTAVIDTNLTSLFNVTKQVIDGMVERGWGR---IINISSVNGQKGQFGQTNY 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 1203982   152 CASKHGIVGFTrsAALAANLMNSGVRLNAICPGFVNTAILESIEKE 197
Cdd:PRK12938 154 STAKAGIHGFT--MSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPD 197
PRK06123 PRK06123
SDR family oxidoreductase;
6-190 4.07e-20

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 86.37  E-value: 4.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVAL-VDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06123   3 KVMIITGASRGIGAATALLAAERGYAVCLnYLRNRDAAEAVVQAIRRQ--GGEALAVAADVADEADVLRLFEAVDRELGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNNEK---------NWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPV-YCAS 154
Cdd:PRK06123  81 LDALVNNAGILEAQmrleqmdaaRLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVNVSSMAARLGSPGEYIdYAAS 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 1203982   155 KHGIVGFTrsAALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK06123 161 KGAIDTMT--IGLAKEVAAEGIRVNAVRPGVIYTEI 194
PRK07201 PRK07201
SDR family oxidoreductase;
3-166 7.07e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 88.85  E-value: 7.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfePQKTLFI-QCDVADQQQLRDTFRKVVDH 81
Cdd:PRK07201 369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRA---KGGTAHAyTCDLTDSAAVDHTVKDILAE 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAG----------VNNEKNWEKTLQINL---VSVISGTylgLDYMSKQNGGEggiIINMSSLAGLmpvAQQ 148
Cdd:PRK07201 446 HGHVDYLVNNAGrsirrsvensTDRFHDYERTMAVNYfgaVRLILGL---LPHMRERRFGH---VVNVSSIGVQ---TNA 516

                        170       180
                 ....*....|....*....|.
gi 1203982   149 P---VYCASKHGIVGFTRSAA 166
Cdd:PRK07201 517 PrfsAYVASKAALDAFSDVAA 537
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 5-184 1.16e-19

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: 85.59  E-value: 1.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05322   2 NQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYG-EKAYGFGADATNEQSVIALSKGVDEIFKR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVNNE--------KNWEKTLQINLVsvisGTYLGLDYMSKQ--NGGEGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:cd05322  81 VDLLVYSAGIAKSakitdfelGDFDRSLQVNLV----GYFLCAREFSKLmiRDGIQGRIIQINSKSGKVGSKHNSGYSAA 156

                       170       180       190
                ....*....|....*....|....*....|
gi 1203982  155 KHGIVGFTRSAALaaNLMNSGVRLNAICPG 184
Cdd:cd05322 157 KFGGVGLTQSLAL--DLAEHGITVNSLMLG 184
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 9-245 1.19e-19

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: 85.24  E-value: 1.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    9 LVTGAAQGIGRAFAEALLLKGAKValvdwnleAGVQCKAAlheqfepqktlFIQCDVADQQQLRDTFRKVV-DHFGRLDI 87
Cdd:cd05328   3 VITGAASGIGAATAELLEDAGHTV--------IGIDLREA-----------DVIADLSTPEGRAAAIADVLaRCSGVLDG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   88 LVNNAGVNNEKNWEKTLQINlvsvisgtYLGLDYMSKQ-----NGGEGGIIINMSSLAGLMP------------------ 144
Cdd:cd05328  64 LVNCAGVGGTTVAGLVLKVN--------YFGLRALMEAllprlRKGHGPAAVVVSSIAGAGWaqdklelakalaagtear 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982  145 ---VAQQ------PVYCASKHGIVGFTRSAALAAnLMNSGVRLNAICPGFVNTAILESIEKEENmgqyieYKDHIKDMIK 215
Cdd:cd05328 136 avaLAEHagqpgyLAYAGSKEALTVWTRRRAATW-LYGAGVRVNTVAPGPVETPILQAFLQDPR------GGESVDAFVT 208

                       250       260       270
                ....*....|....*....|....*....|...
gi 1203982  216 YYG-ILDPPLIANGLITLIEDDA--LNGAIMKI 245
Cdd:cd05328 209 PMGrRAEPDEIAPVIAFLASDAAswINGANLFV 241
PRK06128 PRK06128
SDR family oxidoreductase;
5-207 1.41e-19

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 86.07  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK06128 135 LDILVNIAGKQtavkdiadiTTEQFDATFKTNVYAMFWLCKAAIPHLPP-----GASIINTGSIQSYQPSPTLLDYASTK 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1203982   156 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILES----IEKEENMGQYIEYK 207
Cdd:PRK06128 210 AAIVAFTK--ALAKQVAEKGIRVNAVAPGPVWTPLQPSggqpPEKIPDFGSETPMK 263
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 5-188 1.57e-19

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: 84.83  E-value: 1.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNlEAGVQCKAALHEQFEPqktlfIQCDVADQQQLRDTFRKVvdhfGR 84
Cdd:cd05351   7 GKRALVTGAGKGIGRATVKALAKAGARVVAVSRT-QADLDSLVRECPGIEP-----VCVDLSDWDATEEALGSV----GP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:cd05351  77 VDLLVNNAAVAilqpflevTKEAFDRSFDVNVRAVIHVSQIVARGMIAR--GVPGSIVNVSSQASQRALTNHTVYCSTKA 154

                       170       180       190
                ....*....|....*....|....*....|..
gi 1203982  157 GIVGFTRSAALaaNLMNSGVRLNAICPGFVNT 188
Cdd:cd05351 155 ALDMLTKVMAL--ELGPHKIRVNSVNPTVVMT 184
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 5-188 1.87e-19

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: 84.89  E-value: 1.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN---LEAGVQCKAALHEqfepqkTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:cd08937   4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSelvHEVLAEILAAGDA------AHVHTADLETYAGAQGVVRAAVER 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   82 FGRLDILVNNAGVN---------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLA--GLMPVAqqpv 150
Cdd:cd08937  78 FGRVDVLINNVGGTiwakpyehyEEEQIEAEIRRSLFPTLWCCRAVLPHMLER---QQGVIVNVSSIAtrGIYRIP---- 150

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 1203982  151 YCASKHGIVGFTrsAALAANLMNSGVRLNAICPGFVNT 188
Cdd:cd08937 151 YSAAKGGVNALT--ASLAFEHARDGIRVNAVAPGGTEA 186
PRK09072 PRK09072
SDR family oxidoreductase;
1-190 3.34e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 84.22  E-value: 3.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALHEQFEPQKTLFIQCDVADqQQLRDTFRKVVD 80
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEK---LEALAARLPYPGRHRWVVADLTS-EAGREAVLARAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK09072  77 EMGGINVLINNAGVNhfalledqDPEAIERLLALNLTAPMQLTRALLPLLRAQ---PSAMVVNVGSTFGSIGYPGYASYC 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   153 ASKHGIVGFtrSAALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK09072 154 ASKFALRGF--SEALRRELADTGVRVLYLAPRATRTAM 189
PRK08264 PRK08264
SDR family oxidoreductase;
1-188 3.91e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 83.40  E-value: 3.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGA-KVAlvdwnleAGVQCKAALHEQFEpqKTLFIQCDVADqqqlRDTFRKVV 79
Cdd:PRK08264   2 MDIKGKVVLVTGANRGIGRAFVEQLLARGAaKVY-------AAARDPESVTDLGP--RVVPLQLDVTD----PASVAAAA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    80 DHFGRLDILVNNAGVN---------NEKNWEKTLQINlvsvisgtYLGLDYMS-------KQNGgeGGIIINMSSLAGLM 143
Cdd:PRK08264  69 EAASDVTILVNNAGIFrtgslllegDEDALRAEMETN--------YFGPLAMArafapvlAANG--GGAIVNVLSVLSWV 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 1203982   144 PVAQQPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK08264 139 NFPNLGTYSASKAAAWSLTQ--ALRAELAPQGTRVLGVHPGPIDT 181
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 3.97e-19

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 83.97  E-value: 3.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQ--GIGRAFAEALLLKGAKVALVDWN-LEAGVQCKAALHEQFEPQKTLF---IQC-----DVADQQ 69
Cdd:PRK12748   1 LPLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYWSpYDKTMPWGMHDKEPVLLKEEIEsygVRCehmeiDLSQPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    70 QLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINL-----VSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMP 144
Cdd:PRK12748  81 APNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLdkhyaVNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSLGP 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   145 VAQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK12748 161 MPDELAYAATKGAIEAFTKS--LAPELAEKGITVNAVNPGPTDT 202
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-198 5.28e-19

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: 83.23  E-value: 5.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    3 VNGKVALVTGAAQGIGRAFAEALLLKGAKvalvdwNLEAGVQCKAALHEQFE--PQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAK------KVYAAVRDPGSAAHLVAkyGDKVVPLRLDVTDPESIKAAAAQAKD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   81 hfgrLDILVNNAGVNNEKNW---------EKTLQINLVSVISGTYLGLDYMsKQNGgeGGIIINMSSLAGLMPVAQQPVY 151
Cdd:cd05354  75 ----VDVVINNAGVLKPATLleegalealKQEMDVNVFGLLRLAQAFAPVL-KANG--GGAIVNLNSVASLKNFPAMGTY 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 1203982  152 CASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEE 198
Cdd:cd05354 148 SASKSAAYSLTQ--GLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPK 192
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-189 1.98e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 82.03  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK07097  10 GKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRE--LGIEAHGYVCDVTDEDGVQAMVSQIEKEVGV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKH 156
Cdd:PRK07097  88 IDILVNNAGIIKRipmlemsaEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGK---IINICSMMSELGRETVSAYAAAKG 164

                        170       180       190
                 ....*....|....*....|....*....|...
gi 1203982   157 GIVGFTRSaaLAANLMNSGVRLNAICPGFVNTA 189
Cdd:PRK07097 165 GLKMLTKN--IASEYGEANIQCNGIGPGYIATP 195
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
6-245 2.00e-18

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 82.04  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDwnlEAGVQCKAALHEQFEPQKTlFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISIS---RTENKELTKLAEQYNSNLT-FHSLDLQDVHELETNFNEILSSIQED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    86 DI----LVNNAG----VNNEKNWE-----KTLQINLVS--VISGTYLgldymsKQNGGEGG--IIINMSSLAGLMPVAQQ 148
Cdd:PRK06924  78 NVssihLINNAGmvapIKPIEKAEseeliTNVHLNLLApmILTSTFM------KHTKDWKVdkRVINISSGAAKNPYFGW 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   149 PVYCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNT---AILESIEKE--ENMGQYIEYKDHIKdmikyygILDPP 223
Cdd:PRK06924 152 SAYCSSKAGLDMFTQTVATEQEEEEYPVKIVAFSPGVMDTnmqAQIRSSSKEdfTNLDRFITLKEEGK-------LLSPE 224

                        250       260
                 ....*....|....*....|...
gi 1203982   224 LIANGLITLIEDDAL-NGAIMKI 245
Cdd:PRK06924 225 YVAKALRNLLETEDFpNGEVIDI 247
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 5-188 1.13e-17

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: 80.20  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAGV------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLA---GLMPVA----QQP-- 149
Cdd:cd09807  81 LDVLINNAGVmrcpysKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKS---APSRIVNVSSLAhkaGKINFDdlnsEKSyn 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 1203982  150 ---VYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:cd09807 158 tgfAYCQSKLANVLFTRE--LARRLQGTGVTVNALHPGVVRT 197
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-188 1.61e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 79.43  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIqcDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK07523  10 GRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAF--DVTDHDAVRAAIDAFEAEIGP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSS----LA--GLMPvaqqpv 150
Cdd:PRK07523  88 IDILVNNAGMQFrtpledfpADAFERLLRTNISSVFYVGQAVARHMIARGAGK---IINIASvqsaLArpGIAP------ 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   151 YCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07523 159 YTATKGAVGNLTK--GMATDWAKHGLQCNAIAPGYFDT 194
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 4-198 2.38e-17

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: 79.03  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVqckAALHEQFEPQ--KTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:cd09763   2 SGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQL---PGTAEEIEARggKCIPVRCDHSDDDEVEALFERVARE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   82 F-GRLDILVNNA------GVNN---------EKNWEKTLQINLVSVISGTYLGLDYMSKQNggeGGIIINMSSLAGLMPV 145
Cdd:cd09763  79 QqGRLDILVNNAyaavqlILVGvakpfweepPTIWDDINNVGLRAHYACSVYAAPLMVKAG---KGLIVIISSTGGLEYL 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 1203982  146 aQQPVYCASKHGIVGFTrsAALAANLMNSGVRLNAICPGFVNT-AILESIEKEE 198
Cdd:cd09763 156 -FNVAYGVGKAAIDRMA--ADMAHELKPHGVAVVSLWPGFVRTeLVLEMPEDDE 206
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 7-184 3.24e-17

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: 78.82  E-value: 3.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVD----HF 82
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTCQADLSNSATLFSRCEAIIDacfrAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     83 GRLDILVNNA----------GVNNEKNWE-KTLQINLVSVISGT----YLGLDYMSKQNGGEGG-------IIINMSSLA 140
Cdd:TIGR02685  83 GRCDVLVNNAsafyptpllrGDAGEGVGDkKSLEVQVAELFGSNaiapYFLIKAFAQRQAGTRAeqrstnlSIVNLCDAM 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1203982    141 GLMPVAQQPVYCASKHGIVGFTRSAALaaNLMNSGVRLNAICPG 184
Cdd:TIGR02685 163 TDQPLLGFTMYTMAKHALEGLTRSAAL--ELAPLQIRVNGVAPG 204
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 3-199 3.42e-17

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: 78.39  E-value: 3.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFI-QCDVADQQQLRDTFRKVVDH 81
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFIlDLLTCTSENCQQLAQRIAVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   82 FGRLDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:cd05340  82 YPRLDGVLHNAGLlgdvcplseQNPQVWQDV*QVNVNATFMLTQALLPLLLKS---DAGSLVFTSSSVGRQGRANWGAYA 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 1203982  153 ASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEEN 199
Cdd:cd05340 159 VSKFATEGL*Q--VLADEYQQRNLRVNCINPGGTRTAMRASAFPTED 203
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 5.27e-17

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 78.21  E-value: 5.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQckaALHEQFePQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK08642   1 MQISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAE---ALADEL-GDRAIALQADVTDREQVQAMFATATE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGR-LDILVNNA-------GVNNEK----NWEKTLQiNLVSVISGTYL----GLDYMSKQNGGEggiIINMSSlaglmP 144
Cdd:PRK08642  77 HFGKpITTVVNNAladfsfdGDARKKaddiTWEDFQQ-QLEGSVKGALNtiqaALPGMREQGFGR---IINIGT-----N 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 1203982   145 VAQQPV-----YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK08642 148 LFQNPVvpyhdYTTAKAALLGLTRN--LAAELGPYGITVNMVSGGLLRT 194
PRK08219 PRK08219
SDR family oxidoreductase;
6-198 9.90e-17

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 76.90  E-value: 9.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALllkgakvaLVDWNLEAGVQCKAALHE---QFEPQKTLfiQCDVADQqqlrDTFRKVVDHF 82
Cdd:PRK08219   4 PTALITGASRGIGAAIAREL--------APTHTLLLGGRPAERLDElaaELPGATPF--PVDLTDP----EAIAAAVEQL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLdymsKQNGGEGGIIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK08219  70 GRLDVLVHNAGVadlgpvaeSTVDEWRATLEVNVVAPAELTRLLL----PALRAAHGHVVFINSGAGLRANPGWGSYAAS 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   155 KHGIVGFTRsaALAANLMNSgVRLNAICPGFVNTAILESIEKEE 198
Cdd:PRK08219 146 KFALRALAD--ALREEEPGN-VRVTSVHPGRTDTDMQRGLVAQE 186
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 5-184 2.09e-16

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 76.26  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALhEQFEPQkTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEI-EQFPGQ-VLTVQMDVRNPEDVQKMVEQIDEKFGR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN--------NEKNWEKTLQInlvsVISGTYlgldYMSKQNG------GEGGIIINMSSL------AGLMP 144
Cdd:PRK07677  79 IDALINNAAGNficpaedlSVNGWNSVIDI----VLNGTF----YCSQAVGkywiekGIKGNIINMVATyawdagPGVIH 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 1203982   145 VAqqpvycASKHGIVGFTRSAALAANlMNSGVRLNAICPG 184
Cdd:PRK07677 151 SA------AAKAGVLAMTRTLAVEWG-RKYGIRVNAIAPG 183
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 5-194 2.90e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 75.95  E-value: 2.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQ-FEPQKTLFiqcDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK08085   9 GKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEgIKAHAAPF---NVTHKQEVEAAIEHIEKDIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK08085  86 PIDVLINNAGIQRrhpftefpEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGK---IINICSMQSELGRDTITPYAASK 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   156 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESI 194
Cdd:PRK08085 163 GAVKMLTR--GMCVELARHNIQVNGIAPGYFKTEMTKAL 199
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 1-203 5.01e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 75.47  E-value: 5.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQktlfIQCDVADQQQLRDTfRKVVD 80
Cdd:PRK06125   3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVD----VAVHALDLSSPEAR-EQLAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAG--------VNNEKNWEKTLQINLVSVISGTYLGLDYMsKQNGgeGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK06125  78 EAGDIDILVNNAGaipgggldDVDDAAWRAGWELKVFGYIDLTRLAYPRM-KARG--SGVIVNVIGAAGENPDADYICGS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1203982   153 ASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQY 203
Cdd:PRK06125 155 AGNAALMAFTR--ALGGKSLDDGVRVVGVNPGPVATDRMLTLLKGRARAEL 203
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 6-212 1.07e-15

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: 74.42  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALL---LKGAKVALVDWNLEAGVQCKAALHEQFePQKTLFIQCDVADQQQLRDTFRKVVDhf 82
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLAsdpSKRFKVYATMRDLKKKGRLWEAAGALA-GGTLETLQLDVCDSKSVAAAVERVTE-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   83 GRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCAS 154
Cdd:cd09806  78 RHVDVLVCNAGVGllgplealSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGR---ILVTSSVGGLQGLPFNDVYCAS 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1203982  155 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTA----ILESIEKEENMGQYIEYKDHIKD 212
Cdd:cd09806 155 KFALEGLCES--LAVQLLPFNVHLSLIECGPVHTAfmekVLGSPEEVLDRTADDITTFHFFY 214
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-188 1.81e-15

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 73.67  E-value: 1.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGA--AQGIGRAFAEALLLKGAKVALVDW-----NLEAGVQCKAALHEQfEPQKTLFIQC-----DVADQQQLR 72
Cdd:PRK12859   6 NKVAVVTGVsrLDGIGAAICKELAEAGADIFFTYWtaydkEMPWGVDQDEQIQLQ-EELLKNGVKVssmelDLTQNDAPK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    73 DTFRKVVDHFGRLDILVNNAGVNNEKNWEkTLQINL------VSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVA 146
Cdd:PRK12859  85 ELLNKVTEQLGYPHILVNNAAYSTNNDFS-NLTAEEldkhymVNVRATTLLSSQFARGFDKKSGGRIINMTSGQFQGPMV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 1203982   147 QQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK12859 164 GELAYAATKGAIDALTSS--LAAEVAHLGITVNAINPGPTDT 203
PRK07577 PRK07577
SDR family oxidoreductase;
6-188 2.03e-15

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 73.22  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKValvdwnleAGVQCKAAlhEQFEPQktlFIQCDVADQQQLRDTFRKVVDHFGrL 85
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGHQV--------IGIARSAI--DDFPGE---LFACDLADIEQTAATLAQINEIHP-V 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    86 DILVNNAGVNNEKNWEK--------TLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAgLMPVAQQPVYCASKHG 157
Cdd:PRK07577  70 DAIVNNVGIALPQPLGKidlaalqdVYDLNVRAAVQVTQAFLEGMKLR---EQGRIVNICSRA-IFGALDRTSYSAAKSA 145

                        170       180       190
                 ....*....|....*....|....*....|.
gi 1203982   158 IVGFTRSAALaaNLMNSGVRLNAICPGFVNT 188
Cdd:PRK07577 146 LVGCTRTWAL--ELAEYGITVNAVAPGPIET 174
PRK06482 PRK06482
SDR family oxidoreductase;
4-166 2.47e-15

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 73.61  E-value: 2.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVAlvdwnleAGVQCKAALHEQFE--PQKTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRVA-------ATVRRPDALDDLKAryGDRLWVLQLDVTDSAAVRAVVDRAFAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAG---------VNNEKnWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK06482  74 LGRIDVVVSNAGyglfgaaeeLSDAQ-IRRQIDTNLIGSIQVIRAALPHLRRQGGGR---IVQVSSEGGQIAYPGFSLYH 149

                        170
                 ....*....|....
gi 1203982   153 ASKHGIVGFTRSAA 166
Cdd:PRK06482 150 ATKWGIEGFVEAVA 163
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 5-188 4.92e-15

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: 72.36  E-value: 4.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAA--QGIGRAFAEALLLKGAKVALVDWN--LEAGVQckaALHEQFEPqkTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:COG0623   5 GKRGLITGVAndRSIAWGIAKALHEEGAELAFTYQGeaLKKRVE---PLAEELGS--ALVLPCDVTDDEQIDALFDEIKE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   81 HFGRLDILV-------NNAGVN-----NEKNWEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSSLAGLMPVaqq 148
Cdd:COG0623  80 KWGKLDFLVhsiafapKEELGGrfldtSREGFLLAMDISAYSLVALAKAAEPLMN-----EGGSIVTLTYLGAERVV--- 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 1203982  149 PVYcaskhGIVG--------FTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:COG0623 152 PNY-----NVMGvakaaleaSVRY--LAADLGPKGIRVNAISAGPIKT 192
PRK07985 PRK07985
SDR family oxidoreductase;
3-190 5.22e-15

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 73.11  E-value: 5.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVAL--VDWNLEAGVQCKAALHEQfePQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAIsyLPVEEEDAQDVKKIIEEC--GRKAVLLPGDLSDEKFARSLVHEAHK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAG----VNNEKN-----WEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAGLMPVAQQPVY 151
Cdd:PRK07985 125 ALGGLDIMALVAGkqvaIPDIADltseqFQKTFAINVFALFWLTQEAIPLLPK-----GASIITTSSIQAYQPSPHLLDY 199

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   152 CASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK07985 200 AATKAAILNYSR--GLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 5-196 6.24e-15

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 72.68  E-value: 6.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQ-FEPQKtlfIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEgFDVHG---VMCDVRHREEVTHLADEAFRLLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGV--------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK05876  83 HVDVVFSNAGIvvggpiveMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQ--GTGGHVVFTASFAGLVPNAGLGAYGVAK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEK 196
Cdd:PRK05876 161 YGVVGLAET--LAREVTADGIGVSVLCPMVVETNLVANSER 199
PRK06182 PRK06182
short chain dehydrogenase; Validated
 6-227 6.52e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 72.69  E-value: 6.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALllkgakvalvdwnLEAGVQCKAALH--EQFEPQKTLFIQC---DVADQQQLRDTFRKVVD 80
Cdd:PRK06182   4 KVALVTGASSGIGKATARRL-------------AAQGYTVYGAARrvDKMEDLASLGVHPlslDVTDEASIKAAVDTIIA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAGVNNEKNWE--------KTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMpvaQQPV-- 150
Cdd:PRK06182  71 EEGRIDVLVNNAGYGSYGAIEdvpidearRQFEVNLFGAARLTQLVLPHMRAQRSGR---IINISSMGGKI---YTPLga 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   151 -YCASKHGIVGFtrSAALAANLMNSGVRLNAICPGFVNT----AILESIEKEENMGQYIEYKDHI-KDMIKYYG---ILD 221
Cdd:PRK06182 145 wYHATKFALEGF--SDALRLEVAPFGIDVVVIEPGGIKTewgdIAADHLLKTSGNGAYAEQAQAVaASMRSTYGsgrLSD 222


                 ....*.
gi 1203982   222 PPLIAN 227
Cdd:PRK06182 223 PSVIAD 228
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 8-188 9.98e-15

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: 71.56  E-value: 9.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGAK--VALV-DWNLEAGVQCKAALHEqfepqKTLFIQCDVAD-----QQQLRDTFRkvv 79
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNtvIATCrDPSAATELAALGASHS-----RLHILELDVTDeiaesAEAVAERLG--- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   80 dhFGRLDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKqngGEGGIIINMSSLAG---LMPVAQ 147
Cdd:cd05325  73 --DAGLDVLINNAGIlhsygpaseVDSEDLLEVFQVNVLGPLLLTQAFLPLLLK---GARAKIINISSRVGsigDNTSGG 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 1203982  148 QPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:cd05325 148 WYSYRASKAALNMLTKS--LAVELKRDGITVVSLHPGWVRT 186
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 5-188 1.62e-14

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: 70.43  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDwnleagvqckaaLHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASID------------LAENEEADASIIVLDSDSFTEQAKQVVASVARLSGK 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDILVNNAG---------VNNEKNWEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:cd05334  69 VDALICVAGgwaggsaksKSFVKNWDLMWKQNLWTSFIASHLATKHLL-----SGGLLVLTGAKAALEPTPGMIGYGAAK 143

                       170       180       190
                ....*....|....*....|....*....|...
gi 1203982  156 HGIVGFTRSAALAANLMNSGVRLNAICPGFVNT 188
Cdd:cd05334 144 AAVHQLTQSLAAENSGLPAGSTANAILPVTLDT 176
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 4-186 2.06e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 71.14  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgVQCKAALHEQFEPQkTLFIQCDVADQQQLRDTFRKVVDHFG 83
Cdd:PRK07576   8 AGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEK-VDAAVAQLQQAGPE-GLGVSADVRDYAAVEAAFAQIADEFG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN--------NEKNWEKTLQINLV---SVISGTYlglDYMSKQnggeGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK07576  86 PIDVLVSGAAGNfpapaagmSANGFKTVVDIDLLgtfNVLKAAY---PLLRRP----GASIIQISAPQAFVPMPMQAHVC 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 1203982   153 ASKHGIVGFTRSAALAANLmnSGVRLNAICPGFV 186
Cdd:PRK07576 159 AAKAGVDMLTRTLALEWGP--EGIRVNSIVPGPI 190
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 7-186 8.20e-14

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 69.02  E-value: 8.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFepqktLFIQCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNL-----YIAQLDVRNRAAIEEMLASLPAEWRNID 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    87 ILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKhg 157
Cdd:PRK10538  77 VLVNNAGLalglepahkASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGH---IINIGSTAGSWPYAGGNVYGATK-- 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 1203982   158 ivGFTR--SAALAANLMNSGVRLNAICPGFV 186
Cdd:PRK10538 152 --AFVRqfSLNLRTDLHGTAVRVTDIEPGLV 180
PRK08278 PRK08278
SDR family oxidoreductase;
1-183 1.00e-13

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 69.16  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALV------DWNLEAGVQCKAalhEQFEPQ--KTLFIQCDVADQQQLR 72
Cdd:PRK08278   2 MSLSGKTLFITGASRGIGLAIALRAARDGANIVIAaktaepHPKLPGTIHTAA---EEIEAAggQALPLVGDVRDEDQVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    73 DTFRKVVDHFGRLDILVNNAGVNNEKNWEKT--------LQINlvsvISGTYL----GLDYMSKqngGEGGIIINMSSLA 140
Cdd:PRK08278  79 AAVAKAVERFGGIDICVNNASAINLTGTEDTpmkrfdlmQQIN----VRGTFLvsqaCLPHLKK---SENPHILTLSPPL 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 1203982   141 GLMP--VAQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICP 183
Cdd:PRK08278 152 NLDPkwFAPHTAYTMAKYGMSLCTLG--LAEEFRDDGIAVNALWP 194
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 6-200 1.25e-13

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: 68.84  E-value: 1.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKV-ALVDWNLEAGVQckaALHEQFEPQKTLfIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVlAGCLTKNGPGAK---ELRRVCSDRLRT-LQLDVTKPEQIKRAAQWVKEHVGE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   85 LDI--LVNNAGVN---------NEKNWEKTLQINLVSVISGT--YLGLDYMSKqnggegGIIINMSSLAGLMPVAQQPVY 151
Cdd:cd09805  77 KGLwgLVNNAGILgfggdeellPMDDYRKCMEVNLFGTVEVTkaFLPLLRRAK------GRVVNVSSMGGRVPFPAGGAY 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 1203982  152 CASKHGIVGFtrSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENM 200
Cdd:cd09805 151 CASKAAVEAF--SDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQ 197
PRK08251 PRK08251
SDR family oxidoreductase;
6-190 1.60e-13

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 68.42  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVAL----VDwNLEAgvqCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALcarrTD-RLEE---LKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAGVNN---------EKNwEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGlMPVAQQpVYC 152
Cdd:PRK08251  79 LGGLDRVIVNAGIGKgarlgtgkfWAN-KATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRG-LPGVKA-AYA 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   153 ASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK08251 156 ASKAGVASLGEG--LRAELAKTPIKVSTIEPGYIRSEM 191
PRK07023 PRK07023
SDR family oxidoreductase;
8-194 5.47e-13

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 66.58  E-value: 5.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     8 ALVTGAAQGIGRAFAEALLLKGakVALVDWNLEAGVQCKAALHEQFEpqktlFIQCDVADQQQL-----RDTFRKVVDHF 82
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPG--IAVLGVARSRHPSLAAAAGERLA-----EVELDLSDAAAAaawlaGDLLAAFVDGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLdILVNNAGV---------NNEKNWEKTLQINLVSVISgtyLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCA 153
Cdd:PRK07023  77 SRV-LLINNAGTvepigplatLDAAAIARAVGLNVAAPLM---LTAALAQAASDAAERRILHISSGAARNAYAGWSVYCA 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 1203982   154 SKHGIVGFTRSAALAAnlmNSGVRLNAICPGFVNTAILESI 194
Cdd:PRK07023 153 TKAALDHHARAVALDA---NRALRIVSLAPGVVDTGMQATI 190
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 4-190 8.53e-13

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: 66.31  E-value: 8.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALH---EQFEPQ--KTLFIQCDVADQQQLRDTFRKV 78
Cdd:cd09762   2 AGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEPHPKLPGTIYtaaEEIEAAggKALPCIVDIRDEDQVRAAVEKA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   79 VDHFGRLDILVNNAGVNNEKNWEKT--------LQINLvsviSGTYLG----LDYMSKqngGEGGIIINMSSLAGLMPV- 145
Cdd:cd09762  82 VEKFGGIDILVNNASAISLTGTLDTpmkrydlmMGVNT----RGTYLCskacLPYLKK---SKNPHILNLSPPLNLNPKw 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 1203982  146 -AQQPVYCASKHGIVGFTrsAALAANLMNSGVRLNAICPgfvNTAI 190
Cdd:cd09762 155 fKNHTAYTMAKYGMSMCV--LGMAEEFKPGGIAVNALWP---RTAI 195
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 8-190 1.50e-12

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent 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: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 64.53  E-value: 1.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGAKValvdwnLEAGvqckaalheqfepQKTLFIQCDVADQQQLRDTFRKVvdhfGRLDI 87
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEV------ITAG-------------RSSGDYQVDITDEASIKALFEKV----GHFDA 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   88 LVNNAGVNN--------EKNWEKTL------QINLVSVisgtylGLDYMSkqnggEGGIIINMSSLAGLMPVAQQPVYCA 153
Cdd:cd11731  58 IVSTAGDAEfaplaeltDADFQRGLnskllgQINLVRH------GLPYLN-----DGGSITLTSGILAQRPIPGGAAAAT 126

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 1203982  154 SKHGIVGFTRSAALAanlMNSGVRLNAICPGFVNTAI 190
Cdd:cd11731 127 VNGALEGFVRAAAIE---LPRGIRINAVSPGVVEESL 160
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 5-94 3.14e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 65.43  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLR---DTFRKvvdH 81
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAATPGADVTLQELDLTSLASVRaaaDALRA---A 92

                         90
                 ....*....|...
gi 1203982    82 FGRLDILVNNAGV 94
Cdd:PRK06197  93 YPRIDLLINNAGV 105
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 5-138 4.05e-12

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 65.71  E-value: 4.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:COG3347 425 GRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAAFGFAGLDIGG 504

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 1203982   85 LDILVNNAG-VNNEKNWEKT--LQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSS 138
Cdd:COG3347 505 SDIGVANAGiASSSPEEETRlsFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVF 561
PRK05693 PRK05693
SDR family oxidoreductase;
6-188 5.67e-12

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 64.04  E-value: 5.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKValvdWnleaGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRL 85
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEV----W----ATARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    86 DILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQNggegGIIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:PRK05693  74 DVLINNAGYGamgplldgGVEAMRRQFETNVFAVVGVTRALFPLLRRSR----GLVVNIGSVSGVLVTPFAGAYCASKAA 149

                        170       180       190
                 ....*....|....*....|....*....|.
gi 1203982   158 IVGFtrSAALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK05693 150 VHAL--SDALRLELAPFGVQVMEVQPGAIAS 178
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 7-188 2.48e-11

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: 61.82  E-value: 2.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEagvqcKAALHEQFEpqkTLFIQCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:cd05361   3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFA-----DAAERQAFE---SENPGTKALSEQKPEELVDAVLQAGGAID 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   87 ILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHG 157
Cdd:cd05361  75 VLVSNDYIprpmnpidgTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGS---IIFITSAVPKKPLAYNSLYGPARAA 151

                       170       180       190
                ....*....|....*....|....*....|.
gi 1203982  158 IVgfTRSAALAANLMNSGVRLNAICPGFVNT 188
Cdd:cd05361 152 AV--ALAESLAKELSRDNILVYAIGPNFFNS 180
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 4-189 2.76e-11

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 61.81  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALhEQFEPQKTLFIQCDV--ADQQQLRDTFRKVVDH 81
Cdd:PRK08945  11 KDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEI-EAAGGPQPAIIPLDLltATPQNYQQLADTIEEQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAGV---------NNEKNWEKTLQINLVSVISGTYLGLDYMSKqngGEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK08945  90 FGRLDGVLHNAGLlgelgpmeqQDPEVWQDVMQVNVNATFMLTQALLPLLLK---SPAASLVFTSSSVGRQGRANWGAYA 166

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1203982   153 ASKHGIVGFtrSAALAANLMNSGVRLNAICPGFVNTA 189
Cdd:PRK08945 167 VSKFATEGM--MQVLADEYQGTNLRVNCINPGGTRTA 201
PRK12742 PRK12742
SDR family oxidoreductase;
5-188 3.03e-11

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 61.70  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVdwnlEAGVQCKA-ALHEQFEPQKtlfIQCDVADqqqlRDTFRKVVDHFG 83
Cdd:PRK12742   6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRFT----YAGSKDAAeRLAQETGATA---VQTDSAD----RDAVIDVVRKSG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    84 RLDILVNNAGVN--------NEKNWEKTLQINlvsvISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASK 155
Cdd:PRK12742  75 ALDILVVNAGIAvfgdalelDADDIDRLFKIN----IHAPYHASVEAARQMPEGGRIIIIGSVNGDRMPVAGMAAYAASK 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 1203982   156 HGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK12742 151 SALQGMAR--GLARDFGPRGITINVVQPGPIDT 181
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 1-186 3.66e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 61.51  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALV---DWNL-EAGVQCKAALHeqfepqKTLFIQCDVADQQQLRDTFR 76
Cdd:PRK07890   1 MLLKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAartAERLdEVAAEIDDLGR------RALAVPTDITDEDQCANLVA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    77 KVVDHFGRLDILVNNA-------GVNNE--KNWEKTLQINLVSVISGTYLGLDYMSKQnggeGGIIINMSSLAGLMPVAQ 147
Cdd:PRK07890  75 LALERFGRVDALVNNAfrvpsmkPLADAdfAHWRAVIELNVLGTLRLTQAFTPALAES----GGSIVMINSMVLRHSQPK 150

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   148 QPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFV 186
Cdd:PRK07890 151 YGAYKMAKGALLAASQS--LATELGPQGIRVNSVAPGYI 187
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 7-236 5.16e-11

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 61.08  E-value: 5.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      7 VALVTGAAQGIGRAFAEALLL----KGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVV--- 79
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLKALRelp 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     80 --DHFGRLdILVNNAG-----------VNNEKNWEKTLQINLVSVISGTYLGLDYMsKQNGGEGGIIINMSSLAGLMPVA 146
Cdd:TIGR01500  82 rpKGLQRL-LLINNAGtlgdvskgfvdLSDSTQVQNYWALNLTSMLCLTSSVLKAF-KDSPGLNRTVVNISSLCAIQPFK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    147 QQPVYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNTailesiekeeNMGQYIEYKDHIKDMIKYY-------GI 219
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQ--VLALEEKNPNVRVLNYAPGVLDT----------DMQQQVREESVDPDMRKGLqelkakgKL 227

                         250
                  ....*....|....*..
gi 1203982    220 LDPPLIANGLITLIEDD 236
Cdd:TIGR01500 228 VDPKVSAQKLLSLLEKD 244
PRK05866 PRK05866
SDR family oxidoreductase;
3-176 6.92e-11

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 61.30  E-value: 6.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKV-----------ALVDWNLEAGVQCKAalheqfepqktlfIQCDVADQQQL 71
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVvavarredlldAVADRITRAGGDAMA-------------VPCDLSDLDAV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    72 RDTFRKVVDHFGRLDILVNNAG----------VNNEKNWEKTLQINLVS---VISGTYLGldyMSKQNGGEggiIINMSS 138
Cdd:PRK05866 105 DALVADVEKRIGGVDILINNAGrsirrplaesLDRWHDVERTMVLNYYAplrLIRGLAPG---MLERGDGH---IINVAT 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 1203982   139 ---LAGLMPvaQQPVYCASKHGIVGFTRSaaLAANLMNSGV 176
Cdd:PRK05866 179 wgvLSEASP--LFSVYNASKAALSAVSRV--IETEWGDRGV 215
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 9-194 9.12e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 60.59  E-value: 9.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     9 LVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqcKAALHEQFEPQKT----LFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK05875  11 LVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDK----LAAAAEEIEALKGagavRYEPADVTDEDQVARAVDAATAWHGR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LDILVNNAGVN---------NEKNWEKTLQINlvsvISGTYLGLDYMSKQ--NGGeGGIIINMSSLAGlmpvaqqpvycA 153
Cdd:PRK05875  87 LHGVVHCAGGSetigpitqiDSDAWRRTVDLN----VNGTMYVLKHAARElvRGG-GGSFVGISSIAA-----------S 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 1203982   154 SKH---GIVGFTRSA-----ALAAN-LMNSGVRLNAICPGFVNTAILESI 194
Cdd:PRK05875 151 NTHrwfGAYGVTKSAvdhlmKLAADeLGPSWVRVNSIRPGLIRTDLVAPI 200
PRK07024 PRK07024
SDR family oxidoreductase;
10-188 9.14e-11

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 60.33  E-value: 9.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    10 VTGAAQGIGRAFAEALLLKGAKVALV------------DWNLEAGVQCKAAlheqfepqktlfiqcDVADQQQLRDTFRK 77
Cdd:PRK07024   7 ITGASSGIGQALAREYARQGATLGLVarrtdalqafaaRLPKAARVSVYAA---------------DVRDADALAAAAAD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    78 VVDHFGRLDILVNNAGVN---------NEKNWEKTLQINLVSVIsGTYlgLDYMSKQNGGEGGIIINMSSLAGL--MPVA 146
Cdd:PRK07024  72 FIAAHGLPDVVIANAGISvgtlteereDLAVFREVMDTNYFGMV-ATF--QPFIAPMRAARRGTLVGIASVAGVrgLPGA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 1203982   147 QqpVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07024 149 G--AYSASKAAAIKYLES--LRVELRPAGVRVVTIAPGYIRT 186
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-186 1.27e-10

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 59.77  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfepQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK05786   1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKY---GNIHYVVGDVSSTESARNVIEKAAK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNAG------VNNEKNWEKTLQINLVSVISGTYLGLDYMskqngGEGGIIINMSSLAGL-MPVAQQPVYCA 153
Cdd:PRK05786  78 VLNAIDGLVVTVGgyvedtVEEFSGLEEMLTNHIKIPLYAVNASLRFL-----KEGSSIVLVSSMSGIyKASPDQLSYAV 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 1203982   154 SKHGIvgfTRSA-ALAANLMNSGVRLNAICPGFV 186
Cdd:PRK05786 153 AKAGL---AKAVeILASELLGRGIRVNGIAPTTI 183
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 5-98 2.71e-10

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: 60.07  E-value: 2.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALL-LKGAKVALV---------DWNLEAgvqcKAALHEQfePQKTLFIQCDVADQQQLRDT 74
Cdd:cd08953 205 GGVYLVTGGAGGIGRALARALArRYGARLVLLgrsplppeeEWKAQT----LAALEAL--GARVLYISADVTDAAAVRRL 278

                        90       100
                ....*....|....*....|....
gi 1203982   75 FRKVVDHFGRLDILVNNAGVNNEK 98
Cdd:cd08953 279 LEKVRERYGAIDGVIHAAGVLRDA 302
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 5-181 2.74e-10

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: 59.13  E-value: 2.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAA--QGIGRAFAEALLLKGAKVALVDWN--LEAGVQckaALHEQFePQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:cd05372   1 GKRILITGIAndRSIAWGIAKALHEAGAELAFTYQPeaLRKRVE---KLAERL-GESALVLPCDVSNDEEIKELFAEVKK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   81 HFGRLDILV-------NNAGVN-----NEKNWEKTLQINLVSVISGTYLGLDYMskqngGEGGIIINMSSLAGLMPVAQQ 148
Cdd:cd05372  77 DWGKLDGLVhsiafapKVQLKGpfldtSRKGFLKALDISAYSLVSLAKAALPIM-----NPGGSIVTLSYLGSERVVPGY 151

                       170       180       190
                ....*....|....*....|....*....|...
gi 1203982  149 PVYCASKHGIVGFTRSaaLAANLMNSGVRLNAI 181
Cdd:cd05372 152 NVMGVAKAALESSVRY--LAYELGRKGIRVNAI 182
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
5-200 3.79e-10

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 58.57  E-value: 3.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAA--QGIGRAFAEALLLKGAKVALVDWNLEAGvQCKAALHEQFEP-QKTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK07370   6 GKKALVTGIAnnRSIAWGIAQQLHAAGAELGITYLPDEKG-RFEKKVRELTEPlNPSLFLPCDVQDDAQIEETFETIKQK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNN-AGVNNE-----------KNWEKTLQINLVSVISgtylgLDYMSKQNGGEGGIIINMSSLAGLMPVAQQP 149
Cdd:PRK07370  85 WGKLDILVHClAFAGKEeligdfsatsrEGFARALEISAYSLAP-----LCKAAKPLMSEGGSIVTLTYLGGVRAIPNYN 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1203982   150 VYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT-------AILESIEKEENM 200
Cdd:PRK07370 160 VMGVAKAALEASVRY--LAAELGPKNIRVNAISAGPIRTlassavgGILDMIHHVEEK 215
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 3-203 4.36e-10

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 58.55  E-value: 4.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvQCKAALHE-QFEPQKTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKE--EAEETVYEiQSNGGSAFSIGANLESLHGVEALYSSLDNE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 F------GRLDILVNNAGVNNEKNWEKTLQI---NLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYC 152
Cdd:PRK12747  80 LqnrtgsTKFDILINNAGIGPGAFIEETTEQffdRMVSVNAKAPFFIIQQALSRLRDNSRIINISSAATRISLPDFIAYS 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1203982   153 ASKHGIVgfTRSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQY 203
Cdd:PRK12747 160 MTKGAIN--TMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQY 208
PRK06196 PRK06196
oxidoreductase; Provisional
 5-94 5.99e-10

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 58.54  E-value: 5.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEqfepqkTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:PRK06196  26 GKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGIDG------VEVVMLDLADLESVRAFAERFLDSGRR 99

                         90
                 ....*....|
gi 1203982    85 LDILVNNAGV 94
Cdd:PRK06196 100 IDILINNAGV 109
PRK09134 PRK09134
SDR family oxidoreductase;
6-184 1.08e-09

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 57.24  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVAlvdwnleagVQCKAALHEQFE--------PQKTLFIQCDVADQQQLRDTFRK 77
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVA---------VHYNRSRDEAEAlaaeiralGRRAVALQADLADEAEVRALVAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    78 VVDHFGRLDILVNNAGVNNEKN--------WEKTLQINLVSVIsgtYLGLDYMSKQNGGEGGIIINMsslaglmpvAQQP 149
Cdd:PRK09134  81 ASAALGPITLLVNNASLFEYDSaasftrasWDRHMATNLRAPF---VLAQAFARALPADARGLVVNM---------IDQR 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   150 V---------YCASKHGIVGFTRSAALAanlMNSGVRLNAICPG 184
Cdd:PRK09134 149 VwnlnpdflsYTLSKAALWTATRTLAQA---LAPRIRVNAIGPG 189
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 8-193 1.67e-09

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: 55.98  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGA-KVALVDwnleagvqckaalheqfepqktlfiqcdvadqqqlrdtfrkvvdhfgRLD 86
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGSpKVLVVS-----------------------------------------------RRD 33

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   87 ILVNNAGVNN--------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCASKHGI 158
Cdd:cd02266  34 VVVHNAAILDdgrlidltGSRIERAIRANVVGTRRLLEAARELMKAKRLGR---FILISSVAGLFGAPGLGGYAASKAAL 110

                       170       180       190
                ....*....|....*....|....*....|....*
gi 1203982  159 VGFTRSAalAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:cd02266 111 DGLAQQW--ASEGWGNGLPATAVACGTWAGSGMAK 143
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-109 2.45e-09

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 56.53  E-value: 2.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    9 LVTGAAQGIGRAFAEALLLKGAKVALVDwNLEAGVQcKAALHEQFEpqktlFIQCDVADQQQLRDTFRKVvdhfgrlDIL 88
Cdd:COG0451   3 LVTGGAGFIGSHLARRLLARGHEVVGLD-RSPPGAA-NLAALPGVE-----FVRGDLRDPEALAAALAGV-------DAV 68

                        90       100
                ....*....|....*....|...
gi 1203982   89 VNNAGV--NNEKNWEKTLQINLV 109
Cdd:COG0451  69 VHLAAPagVGEEDPDETLEVNVE 91
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
54-191 3.77e-09

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 55.78  E-value: 3.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    54 EPQKTL--FIQCDVADQQQLRDTFRKVVdhfGRLDILVNNAGVNNEKNWEKTLQINlvsvisgtYLGLDYMSKQ---NGG 128
Cdd:PRK12428  19 EPGMTLdgFIQADLGDPASIDAAVAALP---GRIDALFNIAGVPGTAPVELVARVN--------FLGLRHLTEAllpRMA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   129 EGGIIINMSSLAGLM---------------------------PVAQQPVYCASKHGIVGFTRSAAlAANLMNSGVRLNAI 181
Cdd:PRK12428  88 PGGAIVNVASLAGAEwpqrlelhkalaatasfdegaawlaahPVALATGYQLSKEALILWTMRQA-QPWFGARGIRVNCV 166

                        170
                 ....*....|
gi 1203982   182 CPGFVNTAIL 191
Cdd:PRK12428 167 APGPVFTPIL 176
PRK12744 PRK12744
SDR family oxidoreductase;
1-188 3.99e-09

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 55.90  E-value: 3.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MH-VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQ--KTLFIQCDVADQQQLRDTFRK 77
Cdd:PRK12744   3 DHsLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAEETVAAVKAAgaKAVAFQADLTTAAAVEKLFDD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    78 VVDHFGRLDILVNNAGvnneknweKTLQINLVSVISGTYlglDYMS-----------KQNG----GEGGIIINMSSLAGl 142
Cdd:PRK12744  83 AKAAFGRPDIAINTVG--------KVLKKPIVEISEAEY---DEMFavnsksafffiKEAGrhlnDNGKIVTLVTSLLG- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 1203982   143 mpvAQQPVYCA---SKHGIVGFTRSAalAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK12744 151 ---AFTPFYSAyagSKAPVEHFTRAA--SKEFGARGISVTAVGPGPMDT 194
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 5-117 1.30e-08

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: 54.14  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGR 84
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLHIVDMSDPKQVWEFVEEFKEEGKK 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 1203982   85 LDILVNNAG--VNNEKNWEKTLQINLVSVISGTYL 117
Cdd:cd09808  81 LHVLINNAGcmVNKRELTEDGLEKNFATNTLGTYI 115
PRK12746 PRK12746
SDR family oxidoreductase;
2-190 1.84e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 53.88  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     2 HVNGKVALVTGAAQGIGRAFAEALLLKGAKVAlVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQqqlrDTFRKVVDH 81
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVA-IHYGRNKQAADETIREIESNGGKAFLIEADLNSI----DGVKKLVEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 F----------GRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGG---EGGIIINMSSLAGLMPVAQQ 148
Cdd:PRK12746  78 LknelqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPllrAEGRVINISSAEVRLGFTGS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 1203982   149 PVYCASKHGIVgfTRSAALAANLMNSGVRLNAICPGFVNTAI 190
Cdd:PRK12746 158 IAYGLSKGALN--TMTLPLAKHLGERGITVNTIMPGYTKTDI 197
PRK07806 PRK07806
SDR family oxidoreductase;
2-92 3.02e-08

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 53.19  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     2 HVNGKVALVTGAAQGIGRAFAEALLLKGAKVAlVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDH 81
Cdd:PRK07806   3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVV-VNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREE 81

                         90
                 ....*....|.
gi 1203982    82 FGRLDILVNNA 92
Cdd:PRK07806  82 FGGLDALVLNA 92
PRK09291 PRK09291
SDR family oxidoreductase;
5-188 4.73e-08

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 52.69  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVAlvdwnleAGVQCKAALHEQFEPQKTL-----FIQCDVADQQQLRDTFRKVV 79
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVI-------AGVQIAPQVTALRAEAARRglalrVEKLDLTDAIDRAQAAEWDV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    80 DhfgrldILVNNAGVNNE--------KNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVY 151
Cdd:PRK09291  75 D------VLLNNAGIGEAgavvdipvELVRELFETNVFGPLELTQGFVRKMVARGKGK---VVFTSSMAGLITGPFTGAY 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1203982   152 CASKHGIVGFtrSAALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK09291 146 CASKHALEAI--AEAMHAELKPFGIQVATVNPGPYLT 180
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
5-188 5.50e-08

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 52.25  E-value: 5.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQ------GIGRAFAEAlllkGAKVALVDWNlEAGVQCKAALHEQFEPqkTLFIQCDVADQQQLRDTFRKV 78
Cdd:PRK07533  10 GKRGLVVGIANeqsiawGCARAFRAL----GAELAVTYLN-DKARPYVEPLAEELDA--PIFLPLDVREPGQLEAVFARI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    79 VDHFGRLDILVNN----------AGVNN--EKNWEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSSLAGLMPVA 146
Cdd:PRK07533  83 AEEWGRLDFLLHSiafapkedlhGRVVDcsREGFALAMDVSCHSFIRMARLAEPLMT-----NGGSLLTMSYYGAEKVVE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 1203982   147 QQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07533 158 NYNLMGPVKAALESSVRY--LAAELGPKGIRVHAISPGPLKT 197
PRK06720 PRK06720
hypothetical protein; Provisional
 1-94 1.58e-07

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 49.97  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGvqcKAALHEQFE-PQKTLFIQCDVADQQQLRDTFRKVV 79
Cdd:PRK06720  12 MKLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESG---QATVEEITNlGGEALFVSYDMEKQGDWQRVISITL 88

                         90
                 ....*....|....*
gi 1203982    80 DHFGRLDILVNNAGV 94
Cdd:PRK06720  89 NAFSRIDMLFQNAGL 103
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
9-188 1.62e-07

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 50.86  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     9 LVTGAAQGIGRAFAEALLLKG-AKVALV----DWNLEAGV-QCKAALHEQFEpqktlFIQCDVADQqqlrDTFRKVVDHF 82
Cdd:PRK07904  12 LLLGGTSEIGLAICERYLKNApARVVLAalpdDPRRDAAVaQMKAAGASSVE-----VIDFDALDT----DSHPKVIDAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 ---GRLDILVNNAGV--NNEKNWE------KTLQINLVSVIS-GTYLGlDYMSKQNGGEggiIINMSSLAGLMPVAQQPV 150
Cdd:PRK07904  83 fagGDVDVAIVAFGLlgDAEELWQnqrkavQIAEINYTAAVSvGVLLG-EKMRAQGFGQ---IIAMSSVAGERVRRSNFV 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   151 YCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK07904 159 YGSTKAGLDGFYLG--LGEALREYGVRVLVVRPGQVRT 194
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 7-226 2.71e-07

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: 50.07  E-value: 2.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIqCDVADQQQLRDTFRKVVDHFGRLD 86
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVP-TDARDEDEVIALFDLIEEEIGPLE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   87 ILVNNAGVNN------------EKNWEktlqinlVSVISGTYLG---LDYMSKQNGGEggiIINMSSLAGLMPVAQQPVY 151
Cdd:cd05373  80 VLVYNAGANVwfpilettprvfEKVWE-------MAAFGGFLAAreaAKRMLARGRGT---IIFTGATASLRGRAGFAAF 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1203982  152 CASKHGIVGFTRSaaLAANLMNSGVRL-NAICPGFVNTAILesiekEENMGQYIEYKDHikdmikyYGILDPPLIA 226
Cdd:cd05373 150 AGAKFALRALAQS--MARELGPKGIHVaHVIIDGGIDTDFI-----RERFPKRDERKEE-------DGILDPDAIA 211
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-188 3.28e-07

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. 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: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 50.18  E-value: 3.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    9 LVTGAAQGIGRAFAEALLLKGAKVAlvdwnLEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKvVDHFGRLDIL 88
Cdd:cd08951  11 FITGSSDGLGLAAARTLLHQGHEVV-----LHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQ-VNAIGRFDAV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   89 VNNAGVNNEKN-------WEKTLQINLVSVISGTYL-----GLDYMSK--QNGGEggiiinmSSLAGLM----PVAQQPV 150
Cdd:cd08951  85 IHNAGILSGPNrktpdtgIPAMVAVNVLAPYVLTALirrpkRLIYLSSgmHRGGN-------ASLDDIDwfnrGENDSPA 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 1203982  151 YCASKHGIVgfTRSAALAANLMNsgVRLNAICPGFVNT 188
Cdd:cd08951 158 YSDSKLHVL--TLAAAVARRWKD--VSSNAVHPGWVPT 191
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 6-153 8.37e-07

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: 47.86  E-value: 8.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982       6 KVALVTGAAQGIGRAFAEALLLKGA-KVALV------DWNLEAGVQCKAALHEQfepqkTLFIQCDVADQQQLRDTFRKV 78
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGArRLVLLsrsgpdAPGAAALLAELEAAGAR-----VTVVACDVADRDALAAVLAAI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      79 VDHFGRLDILVNNAGVNN--------EKNWEKTLQ------INLVSVISGtyLGLDYMskqnggeggiiINMSSLAGLMP 144
Cdd:smart00822  76 PAVEGPLTGVIHAAGVLDdgvlasltPERFAAVLApkaagaWNLHELTAD--LPLDFF-----------VLFSSIAGVLG 142


                   ....*....
gi 1203982     145 VAQQPVYCA 153
Cdd:smart00822 143 SPGQANYAA 151
PRK08340 PRK08340
SDR family oxidoreductase;
9-93 9.55e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 48.65  E-value: 9.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     9 LVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDIL 88
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEEN---LEKALKELKEYGEVYAVKADLSDKDDLKNLVKEAWELLGGIDAL 80


                 ....*
gi 1203982    89 VNNAG 93
Cdd:PRK08340  81 VWNAG 85
PRK08703 PRK08703
SDR family oxidoreductase;
5-188 1.06e-06

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 48.39  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWN---LEAGV-QCKAALHEqfEPQKTLFIQCDVADQQ--QLRDTFRKV 78
Cdd:PRK08703   6 DKTILVTGASQGLGEQVAKAYAAAGATVILVARHqkkLEKVYdAIVEAGHP--EPFAIRFDLMSAEEKEfeQFAATIAEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    79 VDhfGRLDILVNNAG-------VNNEK--NWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQP 149
Cdd:PRK08703  84 TQ--GKLDGIVHCAGyfyalspLDFQTvaEWVNQYRINTVAPMGLTRALFPLLKQSPDAS---VIFVGESHGETPKAYWG 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   150 VYCASKHGIVGFTRSAALAANLMNSgVRLNAICPGFVNT 188
Cdd:PRK08703 159 GFGASKAALNYLCKVAADEWERFGN-LRANVLVPGPINS 196
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 8-188 1.13e-06

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: 47.90  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPqktlfiqCDVADQQQLRDTFRKVvdhfGRLDI 87
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARP-------ADVAAELEVWALAQEL----GPLDL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   88 LVNNAG------VNNEK--NWEKTLQINLvsviSGTYLGLDYmSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIV 159
Cdd:cd11730  70 LVYAAGailgkpLARTKpaAWRRILDANL----TGAALVLKH-ALALLAAGARLVFLGAYPELVMLPGLSAYAAAKAALE 144

                       170       180
                ....*....|....*....|....*....
gi 1203982  160 GFTRSAALAANlmnsGVRLNAICPGFVNT 188
Cdd:cd11730 145 AYVEVARKEVR----GLRLTLVRPPAVDT 169
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 5-95 2.56e-06

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 48.15  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKV-ALVDWNLEAGVQckaaLHEQFEPQKTLFIQcdVADQQQLRDTFRKVvdhfg 83
Cdd:PRK07424 178 GKTVAVTGASGTLGQALLKELHQQGAKVvALTSNSDKITLE----INGEDLPVKTLHWQ--VGQEAALAELLEKV----- 246

                         90
                 ....*....|..
gi 1203982    84 rlDILVNNAGVN 95
Cdd:PRK07424 247 --DILIINHGIN 256
PRK08416 PRK08416
enoyl-ACP reductase;
2-193 2.67e-06

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 47.46  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     2 HVNGKVALVTGAAQGIGRAFAEALLLKGAKVALV-DWNLEAGVQCKAALHEQFEpQKTLFIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK08416   5 EMKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTyNSNVEEANKIAEDLEQKYG-IKAKAYPLNILEPETYKELFKKIDE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNA--------------------GVNNeknwEKTLQINlvSVISGTYLGLDYMSKQNGGEggiIINMSSLA 140
Cdd:PRK08416  84 DFDRVDFFISNAiisgravvggytkfmrlkpkGLNN----IYTATVN--AFVVGAQEAAKRMEKVGGGS---IISLSSTG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1203982   141 GLMPVAQQPVYCASKHGIVGFTRSAalAANLMNSGVRLNAICPGFVNTAILES 193
Cdd:PRK08416 155 NLVYIENYAGHGTSKAAVETMVKYA--ATELGEKNIRVNAVSGGPIDTDALKA 205
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 61-196 3.05e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 46.73  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    61 IQCDVADQQQLRDTFRKVvdhfGRLDILVNNAGVN--------NEKNWEKTL------QINLVSVisgtylGLDYMSkqn 126
Cdd:PRK07578  36 VQVDITDPASIRALFEKV----GKVDAVVSAAGKVhfaplaemTDEDFNVGLqsklmgQVNLVLI------GQHYLN--- 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982   127 ggEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAanlMNSGVRLNAICPGFVNtailESIEK 196
Cdd:PRK07578 103 --DGGSFTLTSGILSDEPIPGGASAATVNGALEGFVKAAALE---LPRGIRINVVSPTVLT----ESLEK 163
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 3-197 3.14e-06

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 47.16  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     3 VNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfEPQKTLFIQCDVADQQQLRDTFRKVVDhF 82
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSE-SNVDVSYIVADLTKREDLERTVKELKN-I 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    83 GRLDILVNNAG--------VNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEggiIINMSSLAGLMPVAQQPVYCAS 154
Cdd:PRK08339  84 GEPDIFFFSTGgpkpgyfmEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGR---IIYSTSVAIKEPIPNIALSNVV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 1203982   155 KHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNTAILESIEKE 197
Cdd:PRK08339 161 RISMAGLVRT--LAKELGPKGITVNGIMPGIIRTDRVIQLAQD 201
PRK08017 PRK08017
SDR family oxidoreductase;
6-188 3.44e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 47.00  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKValvdwnLEAgvqCK-----AALHEQ-FEPqktlfIQCDVADQQQLRDTFRKVV 79
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRV------LAA---CRkpddvARMNSLgFTG-----ILLDLDDPESVERAADEVI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    80 D-HFGRLDILVNNAGVN--------NEKNWEKTLQINLVSVISGTYLGLDYMSKQngGEGGiIINMSSLAGLMPVAQQPV 150
Cdd:PRK08017  69 AlTDNRLYGLFNNAGFGvygplstiSRQQMEQQFSTNFFGTHQLTMLLLPAMLPH--GEGR-IVMTSSVMGLISTPGRGA 145

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1203982   151 YCASKHGIVGFtrSAALAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK08017 146 YAASKYALEAW--SDALRMELRHSGIKVSLIEPGPIRT 181
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 5-188 6.60e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 46.40  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVADqqQLRDTFRKVVDHFGR 84
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSG--DIDEGVKRIKETIEG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    85 LD--ILVNNAGVN----------NEKNWEKTLQINLVSVISGTYLGLDYMSKQnggEGGIIINMSSLAGLMpVAQQP--- 149
Cdd:PLN02780 131 LDvgVLINNVGVSypyarffhevDEELLKNLIKVNVEGTTKVTQAVLPGMLKR---KKGAIINIGSGAAIV-IPSDPlya 206

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   150 VYCASKHGIVGFTRsaALAANLMNSGVRLNAICPGFVNT 188
Cdd:PLN02780 207 VYAATKAYIDQFSR--CLYVEYKKSGIDVQCQVPLYVAT 243
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 9-82 7.56e-06

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs 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. 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. 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. 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: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 46.37  E-value: 7.56e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1203982    9 LVTGAAQGIGRAFAEALLLKGAKVALVDwNLEAGvqCKAALHEQfEPQKTLFIQCDVADQQQLRDTFRK----VVDHF 82
Cdd:cd05247   3 LVTGGAGYIGSHTVVELLEAGYDVVVLD-NLSNG--HREALPRI-EKIRIEFYEGDIRDRAALDKVFAEhkidAVIHF 76
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 5-107 1.35e-05

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. 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. 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: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 45.28  E-value: 1.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLFIQCDVA---DQQQLRDTFRKVVDH 81
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWHKARVEAMTLDLAslrSVQRFAEAFKAKNSP 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 1203982   82 fgrLDILVNNAGV------NNEKNWEKTLQIN 107
Cdd:cd09809  81 ---LHVLVCNAAVfalpwtLTEDGLETTFQVN 109
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 6-94 1.45e-05

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (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. 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: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 45.59  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGA-KVALVDWNLEAGVQckAALHEQFEPQKTLFIQCDVADQQQLR---DTFRKVVdh 81
Cdd:cd09810   2 GTVVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQ--AAQEVGMPKDSYSVLHCDLASLDSVRqfvDNFRRTG-- 77

                        90
                ....*....|...
gi 1203982   82 fGRLDILVNNAGV 94
Cdd:cd09810  78 -RPLDALVCNAAV 89
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 9-186 1.49e-05

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     9 LVTGAAQGIGRAFAEALLLKGAKVAL--------VDWNLEAGVQCkaalheqfepqktlfIQCDVADQQQLRDTFRKVVD 80
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVIVsyrthypaIDGLRQAGAQC---------------IQADFSTNAGIMAFIDELKQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGRLDILVNNA--------GVNNEKNWEKTLQINlvsvISGTY---LGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQP 149
Cdd:PRK06483  71 HTDGLRAIIHNAsdwlaekpGAPLADVLARMMQIH----VNAPYllnLALEDLLRGHGHAASDIIHITDYVVEKGSDKHI 146

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1203982   150 VYCASKHGIVGFTRS--AALAANlmnsgVRLNAICPGFV 186
Cdd:PRK06483 147 AYAASKAALDNMTLSfaAKLAPE-----VKVNSIAPALI 180
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 8-126 1.71e-05

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 44.98  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      8 ALVTGAAQGIGRAFAEALLLKGAKVALVDwNLEAGVQCKAALHEQfepqktlFIQCDVADQQQLRDTFRKVvdhfgRLDI 87
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLD-RLTSASNTARLADLR-------FVEGDLTDRDALEKLLADV-----RPDA 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1203982     88 LVNNAGV----NNEKNWEKTLQINLVsvisGTYLGLDYMSKQN 126
Cdd:pfam01370  68 VIHLAAVggvgASIEDPEDFIEANVL----GTLNLLEAARKAG 106
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
5-188 4.68e-05

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 43.59  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQ------GIGRAFAEAlllkGAKVALVdWNLEAgvqckaaLHEQFEP-----QKTLFIQCDVADQQQLRD 73
Cdd:PRK08159  10 GKRGLILGVANnrsiawGIAKACRAA----GAELAFT-YQGDA-------LKKRVEPlaaelGAFVAGHCDVTDEASIDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    74 TFRKVVDHFGRLDILVNNAGVNN------------EKNWEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSslag 141
Cdd:PRK08159  78 VFETLEKKWGKLDFVVHAIGFSDkdeltgryvdtsRDNFTMTMDISVYSFTAVAQRAEKLMT-----DGGSILTLT---- 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1203982   142 lmpvaqqpVYCASK----HGIVGFTRSAA------LAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK08159 149 --------YYGAEKvmphYNVMGVAKAALeasvkyLAVDLGPKNIRVNAISAGPIKT 197
PRK08862 PRK08862
SDR family oxidoreductase;
1-189 5.45e-05

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 43.17  E-value: 5.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHeQFEPQKTLFIQCDvADQQQLRDTFRKVVD 80
Cdd:PRK08862   1 MDIKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCS-ALTDNVYSFQLKD-FSQESIRHLFDAIEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    81 HFGR-LDILVNN------AGVNNEKNWEKTlqINLVSVISGTYLGL-----DYMSKQNggEGGIIINMSS------LAGL 142
Cdd:PRK08862  79 QFNRaPDVLVNNwtssplPSLFDEQPSESF--IQQLSSLASTLFTYgqvaaERMRKRN--KKGVIVNVIShddhqdLTGV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 1203982   143 MpvaqqpvycASKHGIVGFTRSAALAANLMNsgVRLNAICPGFVNTA 189
Cdd:PRK08862 155 E---------SSNALVSGFTHSWAKELTPFN--IRVGGVVPSIFSAN 190
PRK06101 PRK06101
SDR family oxidoreductase;
7-188 8.19e-05

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 42.93  E-value: 8.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     7 VALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAgvqcKAALHEQFEPQKTLfiQCDVADQQQLRDT-----FRKVVDH 81
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSV----LDELHTQSANIFTL--AFDVTDHPGTKAAlsqlpFIPELWI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    82 FGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAGLMPVAQQPVYCASKHGIVGF 161
Cdd:PRK06101  77 FNAGDCEYMDDGKVDATLMARVFNVNVLGVANCIEGIQPHLSC-----GHRVVIVGSIASELALPRAEAYGASKAAVAYF 151

                        170       180
                 ....*....|....*....|....*..
gi 1203982   162 TRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK06101 152 ART--LQLDLRPKGIEVVTVFPGFVAT 176
PRK05854 PRK05854
SDR family oxidoreductase;
5-94 1.09e-04

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 42.75  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     5 GKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQfEPQKTLFI-QCD------VADqqqLRDTFRK 77
Cdd:PRK05854  14 GKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTA-VPDAKLSLrALDlsslasVAA---LGEQLRA 89

                         90
                 ....*....|....*...
gi 1203982    78 VvdhfGR-LDILVNNAGV 94
Cdd:PRK05854  90 E----GRpIHLLINNAGV 103
PRK12367 PRK12367
short chain dehydrogenase; Provisional
 4-110 4.77e-04

short chain dehydrogenase; Provisional


Pssm-ID: 237079  Cd Length: 245  Bit Score: 40.38  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     4 NGKVALVTGAAQGIGRAFAEALLLKGAKValVDWNLEAGVQCKAALHeqfEPQKTlfIQCDVADQQQLRDTFRKvvdhfg 83
Cdd:PRK12367  13 QGKRIGITGASGALGKALTKAFRAKGAKV--IGLTHSKINNSESNDE---SPNEW--IKWECGKEESLDKQLAS------ 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 1203982    84 rLDILVNNAGVNN-----EKNWEKTLQINLVS 110
Cdd:PRK12367  80 -LDVLILNHGINPggrqdPENINKALEINALS 110
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
1-188 7.54e-04

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 40.09  E-value: 7.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAA--QGIGRAFAEALLLKGAKVALVDWN--LEAGVQckaalheQFEPQKTLFIQCDVADQQQLRDTFR 76
Cdd:PRK06079   3 GILSGKKIVVMGVAnkRSIAWGCAQAIKDQGATVIYTYQNdrMKKSLQ-------KLVDEEDLLVECDVASDESIERAFA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    77 KVVDHFGRLDILVNNAGVNNEKNWEKTL------------QINLVSVISGTYLGLDYMSKqnggeGGIIINMSSLAGLMP 144
Cdd:PRK06079  76 TIKERVGKIDGIVHAIAYAKKEELGGNVtdtsrdgyalaqDISAYSLIAVAKYARPLLNP-----GASIVTLTYFGSERA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   145 VAQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK06079 151 IPNYNVMGIAKAALESSVRY--LARDLGKKGIRVNAISAGAVKT 192
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
1-188 8.31e-04

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 40.11  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     1 MHVNGKVALVTGAA--QGIGRAFAEALLLKGAKVALVDWN--LEAGVQCKAAlheqfEPQKTLFIQCDVADQQQLRDTFR 76
Cdd:PRK08415   1 MIMKGKKGLIVGVAnnKSIAYGIAKACFEQGAELAFTYLNeaLKKRVEPIAQ-----ELGSDYVYELDVSKPEHFKSLAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    77 KVVDHFGRLDILVN-----------NAGVNNEKN-WEKTLQINLVSVISGTYLGLDYMSkqnggEGGIIINMSSLAGLMP 144
Cdd:PRK08415  76 SLKKDLGKIDFIVHsvafapkealeGSFLETSKEaFNIAMEISVYSLIELTRALLPLLN-----DGASVLTLSYLGGVKY 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 1203982   145 VAQQPVYCASKHGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK08415 151 VPHYNVMGVAKAALESSVRY--LAVDLGKKGIRVNAISAGPIKT 192
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 9-94 8.42e-04

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: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982      9 LVTGAAQGIGRAFAEALLLKGAK---------------VALVDwNLEA-GVQCKAalheqfepqktlfIQCDVADQQQLR 72
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhlvllsrsaaprpdaQALIA-ELEArGVEVVV-------------VACDVSDPDAVA 69

                          90       100
                  ....*....|....*....|..
gi 1203982     73 DTFRKVVDHFGRLDILVNNAGV 94
Cdd:pfam08659  70 ALLAEIKAEGPPIRGVIHAAGV 91
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
 9-94 8.68e-04

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs 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. 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. 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. 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: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 40.01  E-value: 8.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    9 LVTGAAQGIGRAFAEALLLKGAKVALVDwNLEA--GVQCKAALHEQF-EPQKTLFIQCDVADQQQLRDTFRKVvdHFGRL 85
Cdd:cd05253   4 LVTGAAGFIGFHVAKRLLERGDEVVGID-NLNDyyDVRLKEARLELLgKSGGFKFVKGDLEDREALRRLFKDH--EFDAV 80


                ....*....
gi 1203982   86 DILVNNAGV 94
Cdd:cd05253  81 IHLAAQAGV 89
PRK08177 PRK08177
SDR family oxidoreductase;
6-188 1.10e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 39.24  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982     6 KVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALHEQFEpqktlfiQCDVADQQQLRDTFRKVVDHfgRL 85
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIE-------KLDMNDPASLDQLLQRLQGQ--RF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    86 DILVNNAGVNN-------EKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEgGIIINMSSLAG---LMPVAQQPVYCASK 155
Cdd:PRK08177  73 DLLFVNAGISGpahqsaaDATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQ-GVLAFMSSQLGsveLPDGGEMPLYKASK 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 1203982   156 HGIVGFTRSaaLAANLMNSGVRLNAICPGFVNT 188
Cdd:PRK08177 152 AALNSMTRS--FVAELGEPTLTVLSMHPGWVKT 182
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 9-94 1.68e-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: 39.29  E-value: 1.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    9 LVTGAAQGIGRAFAEALLLKGAK-VALVDWN-LEAGVQCKAALHEQFEPQKTLfIQCDVADQQQLRDTFRKvVDHFGRLD 86
Cdd:cd05274 154 LITGGLGGLGLLVARWLAARGARhLVLLSRRgPAPRAAARAALLRAGGARVSV-VRCDVTDPAALAALLAE-LAAGGPLA 231


                ....*...
gi 1203982   87 ILVNNAGV 94
Cdd:cd05274 232 GVIHAAGV 239
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 6-102 2.69e-03

3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other enzymes) catalyzes NADP-dependent sterol C-4 demethylation, as part of steroid biosynthesis. 3-keto reductase is a classical SDR, with a well conserved canonical active site tetrad and fairly well conserved characteristic 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: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 38.52  E-value: 2.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALL-----LKGAKVALVDWNLEAGVQCKAALHEQFEPQKTLF--IQCDVADQQQLRDTFRKV 78
Cdd:cd08941   2 KVVLVTGANSGLGLAICERLLaeddeNPELTLILACRNLQRAEAACRALLASHPDARVVFdyVLVDLSNMVSVFAAAKEL 81

                        90       100
                ....*....|....*....|....*.
gi 1203982   79 VDHFGRLDILVNNAG--VNNEKNWEK 102
Cdd:cd08941  82 KKRYPRLDYLYLNAGimPNPGIDWIG 107
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 8-98 5.03e-03

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: 37.00  E-value: 5.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    8 ALVTGAAQGIGRAFAEALLLKGAKVALVdwnleagVQCKAALHEQFEPQKtLFIQCDVADQQQLRDTFRKVvdhfgrlDI 87
Cdd:cd05226   1 ILILGATGFIGRALARELLEQGHEVTLL-------VRNTKRLSKEDQEPV-AVVEGDLRDLDSLSDAVQGV-------DV 65

                        90
                ....*....|.
gi 1203982   88 LVNNAGVNNEK 98
Cdd:cd05226  66 VIHLAGAPRDT 76
KR_fFAS_SDR_c_like cd08950
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ...
 5-32 5.64e-03

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like SDRs; KR domain of fungal-type fatty acid synthase (FAS), type I. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member, is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the Classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. 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: 187653 [Multi-domain]  Cd Length: 259  Bit Score: 37.17  E-value: 5.64e-03
                        10        20
                ....*....|....*....|....*....
gi 1203982    5 GKVALVTGAAQG-IGRAFAEALLLKGAKV 32
Cdd:cd08950   7 GKVALVTGAGPGsIGAEVVAGLLAGGATV 35
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 6-100 8.35e-03

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 36.84  E-value: 8.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1203982    6 KVALVTGAAQGIGRAFAEALLLKGAKVALVdwnlEAGVQCKAALHEQFEPQKTLFIQCDVADQQQLRDTFRKVvdhfgrl 85
Cdd:cd05271   1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVP----YRCEAYARRLLVMGDLGQVLFVEFDLRDDESIRKALEGS------- 69

                        90
                ....*....|....*.
gi 1203982   86 DILVNNAGVNNE-KNW 100
Cdd:cd05271  70 DVVINLVGRLYEtKNF 85
 
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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