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Conserved domains on  [gi|61556948|ref|NP_001013116|]
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dehydrogenase/reductase (SDR family) member 7-like 1 [Rattus norvegicus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143187)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; 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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0051287
SCOP:  4000029

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
47-305 3.35e-107

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: 312.98  E-value: 3.35e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGA---PSPHVVPLDMSDLEDAEQVVEEALK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd05332  78 LFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 207 LALRGFFDVLRTELfDYPGITLSMICPGPVHSNIFQNAFTGDFTET-RLPKIPLFKMETSRCVQLILVSLANDLEDIWIA 285
Cdd:cd05332 158 HALQGFFDSLRAEL-SEPNISVTVVCPGLIDTNIAMNALSGDGSMSaKMDDTTANGMSPEECALEILKAIALRKREVFYA 236
                       250       260
                ....*....|....*....|.
gi 61556948 286 NQPVLLRAYVWQYVP-FRDWI 305
Cdd:cd05332 237 RQVPLLAVYLRQLFPgLFDWL 257
 
Name Accession Description Interval E-value
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
47-305 3.35e-107

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: 312.98  E-value: 3.35e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGA---PSPHVVPLDMSDLEDAEQVVEEALK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd05332  78 LFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 207 LALRGFFDVLRTELfDYPGITLSMICPGPVHSNIFQNAFTGDFTET-RLPKIPLFKMETSRCVQLILVSLANDLEDIWIA 285
Cdd:cd05332 158 HALQGFFDSLRAEL-SEPNISVTVVCPGLIDTNIAMNALSGDGSMSaKMDDTTANGMSPEECALEILKAIALRKREVFYA 236
                       250       260
                ....*....|....*....|.
gi 61556948 286 NQPVLLRAYVWQYVP-FRDWI 305
Cdd:cd05332 237 RQVPLLAVYLRQLFPgLFDWL 257
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
46-284 1.12e-67

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 212.04  E-value: 1.12e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVL 125
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAG----ARVEVVALDVTDPDAVAALAEAVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 126 QEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:COG0300  78 ARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAAS 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948 206 KLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGDftetrlpkiPLFKMETSRCVQLILVSLANDLEDIWI 284
Cdd:COG0300 158 KAALEGFSESLRAELAPT-GVRVTAVCPGPVDTPFTARAGAPA---------GRPLLSPEEVARAILRALERGRAEVYV 226
PRK06181 PRK06181
SDR family oxidoreductase;
49-272 1.94e-58

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 189.03  E-value: 1.94e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGG----EALVVPTDVSDAEACERLIEAAVARF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVAHASLVENTN-MDIFKVLIEVNYLGTVSLTKCVLPHMMERnQGKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:PRK06181  77 GGIDILVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKH 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61556948  208 ALRGFFDVLRTELFDyPGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPLFK-METSRCVQLIL 272
Cdd:PRK06181 156 ALHGFFDSLRIELAD-DGVAVTVVCPGFVATDIRKRALDGDGKPLGKSPMQESKiMSAEECAEAIL 220
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
50-247 7.48e-54

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 174.72  E-value: 7.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948    50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALG----GKALFIQGDVTDRAQVKALVEQAVERLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:pfam00106  77 RLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAV 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 61556948   210 RGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTG 247
Cdd:pfam00106 157 IGFTRSLALELAPH-GIRVNAVAPGGVDTDMTKELRED 193
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
49-236 5.54e-33

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 122.48  E-value: 5.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948    49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:TIGR01963   1 GKTALVTGAASGIGLAIARALAAAGANVVVNDFGEEGAEAAAKVAGDAGG----SVIYLPADVTKEDEIADMIAAAAAEF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:TIGR01963  77 GGLDILVNNAGIQHVAPIEEFPPEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHGLVASPFKSAYVAAKHG 156
                         170       180
                  ....*....|....*....|....*...
gi 61556948   209 LRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:TIGR01963 157 LIGLTKVLALEVAEH-GITVNAICPGYV 183
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
50-204 2.05e-05

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: 44.40  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948     50 KVVWITGASSGIGEELAFQLSKLGVC-LVLSARRGQELERVKRRCLENGNLKEkDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAALLAELEAAGA-RVTVVACDVADRDALAAVLAAIPAVE 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61556948    129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERnqgkIVVMKSLVGIVPRPLCSGYAA 204
Cdd:smart00822  80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF----FVLFSSIAGVLGSPGQANYAA 151
 
Name Accession Description Interval E-value
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
47-305 3.35e-107

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: 312.98  E-value: 3.35e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGA---PSPHVVPLDMSDLEDAEQVVEEALK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd05332  78 LFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 207 LALRGFFDVLRTELfDYPGITLSMICPGPVHSNIFQNAFTGDFTET-RLPKIPLFKMETSRCVQLILVSLANDLEDIWIA 285
Cdd:cd05332 158 HALQGFFDSLRAEL-SEPNISVTVVCPGLIDTNIAMNALSGDGSMSaKMDDTTANGMSPEECALEILKAIALRKREVFYA 236
                       250       260
                ....*....|....*....|.
gi 61556948 286 NQPVLLRAYVWQYVP-FRDWI 305
Cdd:cd05332 237 RQVPLLAVYLRQLFPgLFDWL 257
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
46-284 1.12e-67

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 212.04  E-value: 1.12e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVL 125
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAG----ARVEVVALDVTDPDAVAALAEAVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 126 QEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:COG0300  78 ARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAAS 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948 206 KLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGDftetrlpkiPLFKMETSRCVQLILVSLANDLEDIWI 284
Cdd:COG0300 158 KAALEGFSESLRAELAPT-GVRVTAVCPGPVDTPFTARAGAPA---------GRPLLSPEEVARAILRALERGRAEVYV 226
PRK06181 PRK06181
SDR family oxidoreductase;
49-272 1.94e-58

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 189.03  E-value: 1.94e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGG----EALVVPTDVSDAEACERLIEAAVARF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVAHASLVENTN-MDIFKVLIEVNYLGTVSLTKCVLPHMMERnQGKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:PRK06181  77 GGIDILVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKH 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61556948  208 ALRGFFDVLRTELFDyPGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPLFK-METSRCVQLIL 272
Cdd:PRK06181 156 ALHGFFDSLRIELAD-DGVAVTVVCPGFVATDIRKRALDGDGKPLGKSPMQESKiMSAEECAEAIL 220
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
48-248 5.55e-56

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: 181.53  E-value: 5.55e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  48 ADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENgnlkekdILVLPLDLADTSSHDIATKTVLQE 127
Cdd:COG4221   4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGR-------ALAVPLDVTDEAAVEAAVAAAVAE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 128 FGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:COG4221  77 FGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKA 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 61556948 208 ALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGD 248
Cdd:COG4221 157 AVRGLSESLRAELRPT-GIRVTVIEPGAVDTEFLDSVFDGD 196
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
50-247 7.48e-54

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 174.72  E-value: 7.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948    50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALG----GKALFIQGDVTDRAQVKALVEQAVERLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:pfam00106  77 RLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAV 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 61556948   210 RGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTG 247
Cdd:pfam00106 157 IGFTRSLALELAPH-GIRVNAVAPGGVDTDMTKELRED 193
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
50-244 1.13e-50

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: 168.18  E-value: 1.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGvCLVL-SARRGQELErvkrrclENGNLKEKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQG-YRVIaTARNPDKLE-------SLGELLNDNLEVLELDVTDEESIKAAVKEVIERF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:cd05374  73 GRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAA 152
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 61556948 209 LRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNA 244
Cdd:cd05374 153 LEALSESLRLELAPF-GIKVTIIEPGPVRTGFADNA 187
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
52-262 8.21e-50

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: 165.53  E-value: 8.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  52 VWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekdILVLPLDLADTSSHDIATKTVLQEFGRI 131
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGN-----AVAVQADVSDEEDVEALVEEALEEFGRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 132 DILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALRG 211
Cdd:cd05233  76 DILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 61556948 212 FFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPLFKM 262
Cdd:cd05233 156 LTRSLALELAPY-GIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRL 205
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
47-259 1.12e-49

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: 165.73  E-value: 1.12e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:COG1028   4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGG----RALAVAADVTDEAAVEALVAAAVA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:COG1028  80 AFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASK 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 61556948 207 LALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTG-DFTETRLPKIPL 259
Cdd:COG1028 160 AAVVGLTRSLALELAPR-GIRVNAVAPGPIDTPMTRALLGAeEVREALAARIPL 212
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
51-258 3.92e-42

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: 145.60  E-value: 3.92e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  51 VVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEFGR 130
Cdd:cd05360   2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGG----EAIAVVADVADAAQVERAADTAVERFGR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 131 IDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALR 210
Cdd:cd05360  78 IDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVR 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 61556948 211 GFFDVLRTEL-FDYPGITLSMICPGPVHSNIFQNAftgdftETRLPKIP 258
Cdd:cd05360 158 GFTESLRAELaHDGAPISVTLVQPTAMNTPFFGHA------RSYMGKKP 200
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
50-242 5.88e-40

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: 139.81  E-value: 5.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRclengnlkEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS--------GGDVEAVPYDARDPEDARALVDALRDRFG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:cd08932  73 RIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFAL 152
                       170       180       190
                ....*....|....*....|....*....|...
gi 61556948 210 RGFFDVLRTELFDYpGITLSMICPGPVHSNIFQ 242
Cdd:cd08932 153 RALAHALRQEGWDH-GVRVSAVCPGFVDTPMAQ 184
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
47-244 1.05e-39

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: 139.85  E-value: 1.05e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAG-VSEKKILLVVADLTEEEGQDRIISTTLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMErNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd05364  80 KFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIK-TKGEIVNVSSVAGGRSFPGVLYYCISK 158
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 61556948 207 LALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNA 244
Cdd:cd05364 159 AALDQFTRCTALELAPK-GVRVNSVSPGVIVTGFHRRM 195
PRK07109 PRK07109
short chain dehydrogenase; Provisional
47-258 1.43e-39

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 141.98  E-value: 1.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGG----EALAVVADVADAEAVQAAADRAEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK07109  82 ELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAK 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 61556948  207 LALRGFFDVLRTELF-DYPGITLSMICPGPVHSNIFQNAftgdftETRLPKIP 258
Cdd:PRK07109 162 HAIRGFTDSLRCELLhDGSPVSVTMVQPPAVNTPQFDWA------RSRLPVEP 208
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
49-282 1.47e-39

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: 139.31  E-value: 1.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASGQKVSYISADLSDYEEVEQAFAQAVEKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:cd08939  81 GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFA 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61556948 209 LRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPLFKMETSRCVQLILVSLANDLEDI 282
Cdd:cd08939 161 LRGLAESLRQELKPY-NIRVSVVYPPDTDTPGFEEENKTKPEETKAIEGSSGPITPEEAARIIVKGLDRGYDDV 233
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
50-288 4.95e-38

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: 135.49  E-value: 4.95e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRClenGNLKEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADEL---GAKFPVKVLPLQLDVSDRESIEAALENLPEEFR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVA----HASLVENTNMDIfkvLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:cd05346  78 DIDILVNNAGLAlgldPAQEADLEDWET---MIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCAT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 206 KLALRGFFDVLRTELFDYPgITLSMICPGPVHsnifqnaftGDFTETRlpkiplFKMETSRC--VQLILVSL-ANDLEDI 282
Cdd:cd05346 155 KAAVRQFSLNLRKDLIGTG-IRVTNIEPGLVE---------TEFSLVR------FHGDKEKAdkVYEGVEPLtPEDIAET 218

                ....*...
gi 61556948 283 --WIANQP 288
Cdd:cd05346 219 ilWVASRP 226
PRK06182 PRK06182
short chain dehydrogenase; Validated
50-234 3.11e-37

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 133.93  E-value: 3.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRgqeLERVKrrclengNLKEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARR---VDKME-------DLASLGVHPLSLDVTDEASIKAAVDTIIAEEG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:PRK06182  74 RIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFAL 153
                        170       180
                 ....*....|....*....|....*
gi 61556948  210 RGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK06182 154 EGFSDALRLEVAPF-GIDVVVIEPG 177
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
51-306 9.46e-37

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: 131.98  E-value: 9.46e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  51 VVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEFGR 130
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGG----KVHYYKCDVSKREEVYEAAKKIKKEVGD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 131 IDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALR 210
Cdd:cd05339  77 VTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 211 GFFDVLRTELFDY--PGITLSMICPGPVHSNIFQNAFTgdftetrlPKIPLFKM-ETSRCVQLILVSLandlediwIANQ 287
Cdd:cd05339 157 GFHESLRLELKAYgkPGIKTTLVCPYFINTGMFQGVKT--------PRPLLAPIlEPEYVAEKIVRAI--------LTNQ 220
                       250
                ....*....|....*....
gi 61556948 288 PVLLRAYVWQYVPFRDWIL 306
Cdd:cd05339 221 QMLYLPFYAYFLPILKRTL 239
PRK06914 PRK06914
SDR family oxidoreductase;
50-240 1.15e-35

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 130.14  E-value: 1.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGNLKEKdILVLPLDLADTSS-HDIatKTVLQEF 128
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQ-ATQLNLQQN-IKVQQLDVTDQNSiHNF--QLVLKEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:PRK06914  80 GRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYA 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 61556948  209 LRGFFDVLRTELFDYpGITLSMICPGPVHSNI 240
Cdd:PRK06914 160 LEGFSESLRLELKPF-GIDVALIEPGSYNTNI 190
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
47-236 1.44e-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: 128.81  E-value: 1.44e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGG----KALVLELDVTDEQQVDAAVERTVE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd08934  77 ALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATK 156
                       170       180       190
                ....*....|....*....|....*....|
gi 61556948 207 LALRGFFDVLRTELFDyPGITLSMICPGPV 236
Cdd:cd08934 157 FGVNAFSEGLRQEVTE-RGVRVVVIEPGTV 185
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
47-259 3.78e-35

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 128.00  E-value: 3.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQEL-ERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVL 125
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaEALVAEIGALG----GKALAVQGDVSDAESVERAVDEAK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK05557  79 AEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAAS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQnAFTGDFTETRLPKIPL 259
Cdd:PRK05557 159 KAGVIGFTKSLARELASR-GITVNAVAPGFIETDMTD-ALPEDVKEAILAQIPL 210
PRK06179 PRK06179
short chain dehydrogenase; Provisional
50-244 1.54e-34

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 126.94  E-value: 1.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGvCLVL----SARRGQELERVKrrclengnlkekdilVLPLDLADTSSHDIATKTVL 125
Cdd:PRK06179   5 KVALVTGASSGIGRATAEKLARAG-YRVFgtsrNPARAAPIPGVE---------------LLELDVTDDASVQAAVDEVI 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK06179  69 ARAGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAAS 148
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNA 244
Cdd:PRK06179 149 KHAVEGYSESLDHEVRQF-GIRVSLVEPAYTKTNFDANA 186
PRK05993 PRK05993
SDR family oxidoreductase;
50-244 1.85e-34

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 127.07  E-value: 1.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERvkrrcLENGNLKekdilVLPLDLADTSSHDIATKTVLQEF- 128
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA-----LEAEGLE-----AFQLDYAEPESIAALVAQVLELSg 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:PRK05993  75 GRLDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFA 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 61556948  209 LRGFFDVLRTELFDyPGITLSMICPGPVHSNIFQNA 244
Cdd:PRK05993 155 IEGLSLTLRMELQG-SGIHVSLIEPGPIETRFRANA 189
PRK06180 PRK06180
short chain dehydrogenase; Provisional
50-235 1.07e-33

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 125.03  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQelervKRRCLENGNlkEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK06180   5 KTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEA-----ARADFEALH--PDRALARLLDVTDFDAIDAVVADAEATFG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:PRK06180  78 PIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFAL 157
                        170       180
                 ....*....|....*....|....*.
gi 61556948  210 RGFFDVLRTELFDYpGITLSMICPGP 235
Cdd:PRK06180 158 EGISESLAKEVAPF-GIHVTAVEPGS 182
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
49-236 5.54e-33

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 122.48  E-value: 5.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948    49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:TIGR01963   1 GKTALVTGAASGIGLAIARALAAAGANVVVNDFGEEGAEAAAKVAGDAGG----SVIYLPADVTKEDEIADMIAAAAAEF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:TIGR01963  77 GGLDILVNNAGIQHVAPIEEFPPEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHGLVASPFKSAYVAAKHG 156
                         170       180
                  ....*....|....*....|....*...
gi 61556948   209 LRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:TIGR01963 157 LIGLTKVLALEVAEH-GITVNAICPGYV 183
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
47-262 7.78e-33

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 121.81  E-value: 7.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG----EARVLVFDVSDEAAVRALIEAAVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK05653  79 AFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAK 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 61556948  207 LALRGFFDVLRTELFDYpGITLSMICPGPVHSNIfqNAFTGDF-TETRLPKIPLFKM 262
Cdd:PRK05653 159 AGVIGFTKALALELASR-GITVNAVAPGFIDTDM--TEGLPEEvKAEILKEIPLGRL 212
PRK07201 PRK07201
SDR family oxidoreductase;
43-231 1.80e-32

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 126.99  E-value: 1.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   43 PEQALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATK 122
Cdd:PRK07201 365 LRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGG----TAHAYTCDLTDSAAVDHTVK 440
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGRIDILVNNGGVAHASLVENT--NMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSlVGIVPR-PLC 199
Cdd:PRK07201 441 DILAEHGHVDYLVNNAGRSIRRSVENStdRFHDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSS-IGVQTNaPRF 519
                        170       180       190
                 ....*....|....*....|....*....|..
gi 61556948  200 SGYAASKLALRGFFDVLRTELFDyPGITLSMI 231
Cdd:PRK07201 520 SAYVASKAALDAFSDVAASETLS-DGITFTTI 550
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
54-240 3.98e-32

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: 119.63  E-value: 3.98e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEKDILVlplDLADTSS------HDIATKTvlqe 127
Cdd:cd05356   6 VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAA---DFSAGDDiyerieKELEGLD---- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 128 fgrIDILVNNGGVAHASLVENTNMDIFKV--LIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:cd05356  79 ---IGILVNNVGISHSIPEYFLETPEDELqdIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSAS 155
                       170       180       190
                ....*....|....*....|....*....|....*
gi 61556948 206 KLALRGFFDVLRTELFDYpGITLSMICPGPVHSNI 240
Cdd:cd05356 156 KAFLDFFSRALYEEYKSQ-GIDVQSLLPYLVATKM 189
PRK06139 PRK06139
SDR family oxidoreductase;
47-234 4.11e-32

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 122.14  E-value: 4.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSS-HDIATKTvl 125
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALG----AEVLVVPTDVTDADQvKALATQA-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEF-GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK06139  79 ASFgGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSA 158
                        170       180       190
                 ....*....|....*....|....*....|
gi 61556948  205 SKLALRGFFDVLRTELFDYPGITLSMICPG 234
Cdd:PRK06139 159 SKFGLRGFSEALRGELADHPDIHVCDVYPA 188
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
45-219 4.17e-32

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 119.79  E-value: 4.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGNLKekdILVLPLDLADTSSHDIATKTV 124
Cdd:PRK07666   3 QSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEE-VEAYGVK---VVIATADVSDYEEVTAAIEQL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK07666  79 KNELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSA 158
                        170
                 ....*....|....*
gi 61556948  205 SKLALRGFFDVLRTE 219
Cdd:PRK07666 159 SKFGVLGLTESLMQE 173
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
50-236 4.41e-32

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: 119.26  E-value: 4.41e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLG-VCLVLSAR---RGQEleRVKRrcLENGNLkekDILVLPLDLADTSSHDIATKTVL 125
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTARdveRGQA--AVEK--LRAEGL---SVRFHQLDVTDDASIEAAADFVE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 126 QEFGRIDILVNNGGVAHASLVENTNM-DIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIvprpLCSGYAA 204
Cdd:cd05324  74 EKYGGLDILVNNAGIAFKGFDDSTPTrEQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGS----LTSAYGV 149
                       170       180       190
                ....*....|....*....|....*....|..
gi 61556948 205 SKLALRGFFDVLRTELFDyPGITLSMICPGPV 236
Cdd:cd05324 150 SKAALNALTRILAKELKE-TGIKVNACCPGWV 180
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
50-255 5.83e-32

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: 119.87  E-value: 5.83e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLS-------KLGVCLVLSARRGQELERVKRRClengnlkEKDILVLPLDLADTSSHDIATK 122
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLAsdpskrfKVYATMRDLKKKGRLWEAAGALA-------GGTLETLQLDVCDSKSVAAAVE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 123 TVLQefGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:cd09806  74 RVTE--RHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVY 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 61556948 203 AASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFtGDFTETRLP 255
Cdd:cd09806 152 CASKFALEGLCESLAVQLLPF-NVHLSLIECGPVHTAFMEKVL-GSPEEVLDR 202
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
47-259 2.14e-31

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: 117.84  E-value: 2.14e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05347   3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEG----VEATAFTCDVSDEEAIKAAVEAIEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd05347  79 DFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASK 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 61556948 207 LALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTG-DFTETRLPKIPL 259
Cdd:cd05347 159 GGVAGLTKALATEWARH-GIQVNAIAPGYFATEMTEAVVADpEFNDDILKRIPA 211
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
47-222 2.18e-31

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: 117.96  E-value: 2.18e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRrclENGNLKekdilVLPLDLADTSSHDIATKTVLQ 126
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAA---ANPGLH-----TIVLDVADPASIAALAEQVTA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKV--LIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:COG3967  75 EFPDLNVLINNAGIMRAEDLLDEAEDLADAerEITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSA 154
                       170
                ....*....|....*...
gi 61556948 205 SKLALRGFFDVLRTELFD 222
Cdd:COG3967 155 TKAALHSYTQSLRHQLKD 172
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
45-259 2.46e-31

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 118.05  E-value: 2.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQE-LERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKT 123
Cdd:PRK12825   2 GSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEaAEELVEAVEALG----RRAQAVQADVTDKAALEAAVAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  124 VLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:PRK12825  78 AVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYA 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 61556948  204 ASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFtGDFTETRLPKIPL 259
Cdd:PRK12825 158 AAKAGLVGLTKALARELAEY-GITVNMVAPGDIDTDMKEATI-EEAREAKDAETPL 211
PRK09072 PRK09072
SDR family oxidoreductase;
47-222 1.32e-30

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 116.19  E-value: 1.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKekdilVLPLDLADTSSHDiATKTVLQ 126
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHR-----WVVADLTSEAGRE-AVLARAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK09072  77 EMGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASK 156
                        170
                 ....*....|....*.
gi 61556948  207 LALRGFFDVLRTELFD 222
Cdd:PRK09072 157 FALRGFSEALRRELAD 172
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
47-236 1.92e-30

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 115.75  E-value: 1.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAG----GKAIGVAMDVTDEEAINAGIDYAVE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK12429  78 TFGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAK 157
                        170       180       190
                 ....*....|....*....|....*....|
gi 61556948  207 LALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:PRK12429 158 HGLIGLTKVVALEGATH-GVTVNAICPGYV 186
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
52-246 3.15e-30

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: 114.73  E-value: 3.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  52 VWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGNlkeKDILVLPLDLADTSSHDIATKTVLQEFGRI 131
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAE-LLNPN---PSVEVEILDVTDEERNQLVIAELEAELGGL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 132 DILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALRG 211
Cdd:cd05350  77 DLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSS 156
                       170       180       190
                ....*....|....*....|....*....|....*
gi 61556948 212 FFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFT 246
Cdd:cd05350 157 LAESLRYDVKKR-GIRVTVINPGFIDTPLTANMFT 190
PRK12826 PRK12826
SDR family oxidoreductase;
45-262 8.66e-30

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 113.86  E-value: 8.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGNLKekdILVLPLDLADTSSHDIATKTV 124
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAEL-VEAAGGK---ARARQVDVRDRAALKAAVAAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVG-IVPRPLCSGYA 203
Cdd:PRK12826  78 VEDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGpRVGYPGLAHYA 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948  204 ASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPLFKM 262
Cdd:PRK12826 158 ASKAGLVGFTRALALELAAR-NITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAIPLGRL 215
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
50-287 1.08e-29

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: 113.55  E-value: 1.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARR-----GQELervkrrcleNGNLKEKDILVLPLDLADTSSHDIATKTV 124
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNenpgaAAEL---------QAINPKVKATFVQCDVTSWEQLAAAFKKA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 125 LQEFGRIDILVNNGGVA---HASLVENTNMDIFKVlIEVNYLGTVSLTKCVLPHMMERNQGK---IVVMKSLVGIVPRPL 198
Cdd:cd05323  72 IEKFGRVDILINNAGILdekSYLFAGKLPPPWEKT-IDVNLTGVINTTYLALHYMDKNKGGKggvIVNIGSVAGLYPAPQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 199 CSGYAASKLALRGFFDVLRTELFDYPGITLSMICPGPVHSNIFQNAftGDFTETRLPKIPLfkMETSRCVQLILVSLAND 278
Cdd:cd05323 151 FPVYSASKHGVVGFTRSLADLLEYKTGVRVNAICPGFTNTPLLPDL--VAKEAEMLPSAPT--QSPEVVAKAIVYLIEDD 226
                       250
                ....*....|.
gi 61556948 279 LED--IWIANQ 287
Cdd:cd05323 227 EKNgaIWIVDG 237
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
50-234 1.34e-29

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: 113.03  E-value: 1.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVkrrcLENGNLKEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAET----VEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:cd05333  77 PVDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGV 156
                       170       180
                ....*....|....*....|....*
gi 61556948 210 RGFFDVLRTELFDYpGITLSMICPG 234
Cdd:cd05333 157 IGFTKSLAKELASR-GITVNAVAPG 180
PRK05866 PRK05866
SDR family oxidoreductase;
47-233 3.97e-29

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 113.30  E-value: 3.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGG----DAMAVPCDLSDLDAVDALVADVEK 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGG-----VAHASL-----VENTnmdifkvlIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLvGIVPR 196
Cdd:PRK05866 114 RIGGVDILINNAGrsirrPLAESLdrwhdVERT--------MVLNYYAPLRLIRGLAPGMLERGDGHIINVATW-GVLSE 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 61556948  197 --PLCSGYAASKLALRGFFDVLRTEL---------FDYPGITLSMICP 233
Cdd:PRK05866 185 asPLFSVYNASKAALSAVSRVIETEWgdrgvhsttLYYPLVATPMIAP 232
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
46-220 7.25e-29

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: 110.86  E-value: 7.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRrclENGNLKEKDilvlpLDLADTSSHDIATKTVL 125
Cdd:cd05370   2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKK---ELPNIHTIV-----LDVGDAESVEALAEALL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 126 QEFGRIDILVNNGGVAHASLVENTNMDIFKVL--IEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:cd05370  74 SEYPNLDILINNAGIQRPIDLRDPASDLDKADteIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYC 153
                       170
                ....*....|....*..
gi 61556948 204 ASKLALRGFFDVLRTEL 220
Cdd:cd05370 154 ATKAALHSYTLALRHQL 170
FabG-like PRK07231
SDR family oxidoreductase;
47-259 8.09e-29

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 111.08  E-value: 8.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGnlkEKDILVlPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAE-ILAG---GRAIAV-AADVSDEADVEAAVAAALE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHA--SLVEnTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK07231  78 RFGSVDILVNNAGTTHRngPLLD-VDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948  205 SKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQnAFTGDFTETRLPK----IPL 259
Cdd:PRK07231 157 SKGAVITLTKALAAELGPD-KIRVNAVAPVVVETGLLE-AFMGEPTPENRAKflatIPL 213
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
47-236 8.95e-29

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 111.43  E-value: 8.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLsARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLIL-LDISPEIEKLADELCGRGH----RCTAVVADVRDPASVAAAIKRAKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVG-IVPRPLCSGYAAS 205
Cdd:PRK08226  79 KEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYALT 158
                        170       180       190
                 ....*....|....*....|....*....|.
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:PRK08226 159 KAAIVGLTKSLAVEYAQS-GIRVNAICPGYV 188
PRK07326 PRK07326
SDR family oxidoreductase;
45-239 3.33e-28

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 109.33  E-value: 3.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekdILVLPLDLADTSSHDIATKTV 124
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGN-----VLGLAADVRDEADVQRAVDAI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHmMERNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK07326  77 VAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPA-LKRGGGYIINISSLAGTNFFAGGAAYNA 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 61556948  205 SKLALRGFFDVLRTELFDYpGITLSMICPGPVHSN 239
Cdd:PRK07326 156 SKFGLVGFSEAAMLDLRQY-GIKVSTIMPGSVATH 189
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-242 1.75e-27

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 107.62  E-value: 1.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQE--LERVKRrclengnLKEKDILVLPL--DLADTSSHDIATK 122
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEaaQELLEE-------IKEEGGDAIAVkaDVSSEEDVENLVE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:PRK05565  76 QIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLY 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 61556948  203 AASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQ 242
Cdd:PRK05565 156 SASKGAVNAFTKALAKELAPS-GIRVNAVAPGAIDTEMWS 194
PRK08263 PRK08263
short chain dehydrogenase; Provisional
52-235 2.19e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 108.20  E-value: 2.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   52 VW-ITGASSGIGEELAFQLSKLGVCLVLSARRGQELErvkrrclengNLKEK---DILVLPLDLADTSSHDIATKTVLQE 127
Cdd:PRK08263   5 VWfITGASRGFGRAWTEAALERGDRVVATARDTATLA----------DLAEKygdRLLPLALDVTDRAAVFAAVETAVEH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  128 FGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:PRK08263  75 FGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKW 154
                        170       180
                 ....*....|....*....|....*...
gi 61556948  208 ALRGFFDVLRTELFDYpGITLSMICPGP 235
Cdd:PRK08263 155 ALEGMSEALAQEVAEF-GIKVTLVEPGG 181
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
50-243 8.71e-27

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: 105.99  E-value: 8.71e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlKEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd08940   3 KVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGLAAK--HGVKVLYHGADLSKPAAIEDMVAYAQRQFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:cd08940  81 GVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGV 160
                       170       180       190
                ....*....|....*....|....*....|....
gi 61556948 210 RGFFDVLRTELFDYpGITLSMICPGPVHSNIFQN 243
Cdd:cd08940 161 VGLTKVVALETAGT-GVTCNAICPGWVLTPLVEK 193
PRK05872 PRK05872
short chain dehydrogenase; Provisional
43-220 1.34e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 106.21  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   43 PEQALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLEngnlkEKDILVLPLDLADTSSHDIATK 122
Cdd:PRK05872   3 PMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGG-----DDRVLTVVADVTDLAAMQAAAE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERnQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:PRK05872  78 EAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIER-RGYVLQVSSLAAFAAAPGMAAY 156
                        170
                 ....*....|....*...
gi 61556948  203 AASKLALRGFFDVLRTEL 220
Cdd:PRK05872 157 CASKAGVEAFANALRLEV 174
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
47-269 1.40e-26

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: 105.29  E-value: 1.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05343   4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGY---PTLFPYQCDLSNEEQILSMFSAIRT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHAS-LVENTNMDIfKVLIEVNYLGTVSLTKCVLPHMMERN--QGKIVVMKSLVG--IVPRPLCSG 201
Cdd:cd05343  81 QHQGVDVCINNAGLARPEpLLSGKTEGW-KEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGhrVPPVSVFHF 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948 202 YAASKLALRGFFDVLRTEL-FDYPGITLSMICPGPVHSNIFQNAFTGDftetrlPKIPLFKMETSRCVQ 269
Cdd:cd05343 160 YAATKHAVTALTEGLRQELrEAKTHIRATSISPGLVETEFAFKLHDND------PEKAAATYESIPCLK 222
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
47-257 2.09e-26

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: 104.78  E-value: 2.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQE------------LERVKRRCLENGNlkekDILVLPLDLADT 114
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEgdngsakslpgtIEETAEEIEAAGG----QALPIVVDVRDE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 115 SSHDIATKTVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIV 194
Cdd:cd05338  77 DQVRALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLR 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61556948 195 PRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGP-VHSNIFQNAFTG-DFTETRLPKI 257
Cdd:cd05338 157 PARGDVAYAAGKAGMSRLTLGLAAELRRH-GIAVNSLWPSTaIETPAATELSGGsDPARARSPEI 220
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
50-234 2.10e-26

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: 105.44  E-value: 2.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGV-----CLVLSARRGQELERVkrrCleNGNLKekdilVLPLDLADTSSHDIATKTV 124
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFtvlagCLTKNGPGAKELRRV---C--SDRLR-----TLQLDVTKPEQIKRAAQWV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 125 LQEFGRIDI--LVNNGGV-AHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPhMMERNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:cd09805  71 KEHVGEKGLwgLVNNAGIlGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGA 149
                       170       180       190
                ....*....|....*....|....*....|...
gi 61556948 202 YAASKLALRGFFDVLRTELfDYPGITLSMICPG 234
Cdd:cd09805 150 YCASKAAVEAFSDSLRREL-QPWGVKVSIIEPG 181
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
49-236 2.33e-26

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: 104.66  E-value: 2.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKrrclENGNLKEKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAA----SELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:cd05344  77 GRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAG 156
                       170       180
                ....*....|....*....|....*...
gi 61556948 209 LRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:cd05344 157 LIGLVKTLSRELAPD-GVTVNSVLPGYI 183
PRK07832 PRK07832
SDR family oxidoreductase;
50-236 3.54e-26

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 104.74  E-value: 3.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRrclENGNLKEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVA---DARALGGTVPEHRALDISDYDAVAAFAADIHAAHG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:PRK07832  78 SMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRgGHLVNVSSAAGLVALPWHAAYSASKFG 157
                        170       180
                 ....*....|....*....|....*...
gi 61556948  209 LRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:PRK07832 158 LRGLSEVLRFDLARH-GIGVSVVVPGAV 184
PRK07454 PRK07454
SDR family oxidoreductase;
50-240 7.50e-26

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 103.12  E-value: 7.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTG----VKAAAYSIDLSNPEAIAPGIAELLEQFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:PRK07454  83 CPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAAL 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 61556948  210 RGFFDVLRTELFDYpGITLSMICPGPVHSNI 240
Cdd:PRK07454 163 AAFTKCLAEEERSH-GIRVCTITLGAVNTPL 192
PRK07890 PRK07890
short chain dehydrogenase; Provisional
47-234 7.51e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 103.50  E-value: 7.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLG----RRALAVPTDITDEDQCANLVALALE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNgGVAHASL--VENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNqGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK07890  79 RFGRVDALVNN-AFRVPSMkpLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAYKM 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 61556948  205 SKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK07890 157 AKGALLAASQSLATELGPQ-GIRVNSVAPG 185
PRK07825 PRK07825
short chain dehydrogenase; Provisional
47-236 1.58e-25

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 103.10  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLG--VCL-----VLSARRGQELERVkrrclengnlkekdiLVLPLDLADTSSHDI 119
Cdd:PRK07825   3 LRGKVVAITGGARGIGLATARALAALGarVAIgdldeALAKETAAELGLV---------------VGGPLDVTDPASFAA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  120 ATKTVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLC 199
Cdd:PRK07825  68 FLDAVEADLGPIDVLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGM 147
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 61556948  200 SGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:PRK07825 148 ATYCASKHAVVGFTDAARLELRGT-GVHVSVVLPSFV 183
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
47-212 2.35e-25

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: 101.69  E-value: 2.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRclengnLKEKDILVlPLDLADTSSHDIATKTVLQ 126
Cdd:cd05341   3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAE------LGDAARFF-HLDVTDEDGWTAVVDTARE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd05341  76 AFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASK 155

                ....*.
gi 61556948 207 LALRGF 212
Cdd:cd05341 156 GAVRGL 161
PRK06138 PRK06138
SDR family oxidoreductase;
47-246 4.48e-25

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 101.38  E-value: 4.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGG-----RAFARQGDVGSAEAVEALVDFVAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK06138  78 RWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASK 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 61556948  207 LALrgfFDVLRTELFDYP--GITLSMICPGPVHSNIFQNAFT 246
Cdd:PRK06138 158 GAI---ASLTRAMALDHAtdGIRVNAVAPGTIDTPYFRRIFA 196
PRK05855 PRK05855
SDR family oxidoreductase;
33-253 5.96e-25

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 105.06  E-value: 5.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   33 LLRAAWMGqcPEQALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLA 112
Cdd:PRK05855 301 LLRARVGR--PRGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAG----AVAHAYRVDVS 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  113 DTSS-HDIATkTVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSL 190
Cdd:PRK05855 375 DADAmEAFAE-WVRAEHGVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASA 453
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61556948  191 VGIVPRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNA-FTGDFTETR 253
Cdd:PRK05855 454 AAYAPSRSLPAYATSKAAVLMLSECLRAELAAA-GIGVTAICPGFVDTNIVATTrFAGADAEDE 516
PRK07775 PRK07775
SDR family oxidoreductase;
54-235 6.85e-25

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 101.37  E-value: 6.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEFGRIDI 133
Cdd:PRK07775  15 VAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGG----EAVAFPLDVTDPDSVKSFVAQAEEALGEIEV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  134 LVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALRGFF 213
Cdd:PRK07775  91 LVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMV 170
                        170       180
                 ....*....|....*....|..
gi 61556948  214 DVLRTELfDYPGITLSMICPGP 235
Cdd:PRK07775 171 TNLQMEL-EGTGVRASIVHPGP 191
PRK07774 PRK07774
SDR family oxidoreductase;
47-287 9.33e-25

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 100.20  E-value: 9.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLAD-TSSHDIATKTVl 125
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGG----TAIAVQVDVSDpDSAKAMADATV- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNN----GGVAHASLVeNTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPrplcSG 201
Cdd:PRK07774  79 SAFGGIDYLVNNaaiyGGMKLDLLI-TVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLY----SN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  202 -YAASKLALRGFFDVLRTELfDYPGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPLFKMETSR-----CvqLILVSL 275
Cdd:PRK07774 154 fYGLAKVGLNGLTQQLAREL-GGMNIRVNAIAPGPIDTEATRTVTPKEFVADMVKGIPLSRMGTPEdlvgmC--LFLLSD 230
                        250
                 ....*....|..
gi 61556948  276 ANDlediWIANQ 287
Cdd:PRK07774 231 EAS----WITGQ 238
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
47-234 1.23e-24

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 100.02  E-value: 1.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALG----IDALWIAADVADEADIERLAEETLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMM-ERNQGKIVVMKSLVGIV---PRPLCS-G 201
Cdd:PRK08213  86 RFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMiPRGYGRIINVASVAGLGgnpPEVMDTiA 165
                        170       180       190
                 ....*....|....*....|....*....|...
gi 61556948  202 YAASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK08213 166 YNTSKGAVINFTRALAAEWGPH-GIRVNAIAPG 197
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
47-234 1.49e-24

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 99.96  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLengnlkekdilvlPLDLADTSSHDIATKTVLQ 126
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYPFATF-------------VLDVSDAAAVAQVCQRLLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK08220  73 ETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASK 152
                        170       180
                 ....*....|....*....|....*...
gi 61556948  207 LALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK08220 153 AALTSLAKCVGLELAPY-GVRCNVVSPG 179
PRK06841 PRK06841
short chain dehydrogenase; Provisional
47-258 2.16e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 99.35  E-value: 2.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLsARRGQELERVKRRcLENGNLKEkdilvLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVAL-LDRSEDVAEVAAQ-LLGGNAKG-----LVCDVSDSQSVEAAVAAVIS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK06841  86 AFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASK 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 61556948  207 LALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIP 258
Cdd:PRK06841 166 AGVVGMTKVLALEWGPY-GITVNAISPTVVLTELGKKAWAGEKGERAKKLIP 216
PRK09291 PRK09291
SDR family oxidoreductase;
50-235 2.59e-24

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 99.30  E-value: 2.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQEL----ERVKRRCLengnlkekDILVLPLDLadTSSHDIATKTVL 125
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVtalrAEAARRGL--------ALRVEKLDL--TDAIDRAQAAEW 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QefgrIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK09291  73 D----VDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCAS 148
                        170       180       190
                 ....*....|....*....|....*....|
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPGP 235
Cdd:PRK09291 149 KHALEAIAEAMHAELKPF-GIQVATVNPGP 177
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
47-236 4.57e-24

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 98.81  E-value: 4.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLsARRGQELERVKRRCLENGNLKekdILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK13394   5 LNGKTAVVTGAASGIGKEIALELARAGAAVAI-ADLNQDGANAVADEINKAGGK---AIGVAMDVTNEDAVNAGIDKVAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMM-ERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK13394  81 RFGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSAYVTA 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:PRK13394 161 KHGLLGLARVLAKEGAKH-NVRSHVVCPGFV 190
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
49-282 4.61e-24

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: 98.84  E-value: 4.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlKEKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKET--GNAKVEVIQLDLSSLASVRQFAEEFLARF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 GRIDILVNNGGVAHASlvENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPR-----PLCSG-- 201
Cdd:cd05327  79 PRLDILINNAGIMAPP--RRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPidfndLDLENnk 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 202 -------YAASKLALrgffdVLRT----ELFDYPGITLSMICPGPVHSNIFQNAFTGDFTETRLPkiPLFKMETSRCVQL 270
Cdd:cd05327 157 eyspykaYGQSKLAN-----ILFTrelaRRLEGTGVTVNALHPGVVRTELLRRNGSFFLLYKLLR--PFLKKSPEQGAQT 229
                       250
                ....*....|...
gi 61556948 271 IL-VSLANDLEDI 282
Cdd:cd05327 230 ALyAATSPELEGV 242
PRK12828 PRK12828
short chain dehydrogenase; Provisional
44-250 5.13e-24

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 97.94  E-value: 5.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   44 EQALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELER-VKRRCLENGNLKEkdilvlpLDLADTSSHDIATK 122
Cdd:PRK12828   2 EHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQtLPGVPADALRIGG-------IDLVDPQAARRAVD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:PRK12828  75 EVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAY 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 61556948  203 AASKLALRGFFDVLRTELFDYpGITLSMICPGPVHS-NIFQNAFTGDFT 250
Cdd:PRK12828 155 AAAKAGVARLTEALAAELLDR-GITVNAVLPSIIDTpPNRADMPDADFS 202
PRK12829 PRK12829
short chain dehydrogenase; Provisional
45-262 8.86e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 97.82  E-value: 8.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRclengnLKEKDILVLPLDLADTSSHDIATKTV 124
Cdd:PRK12829   7 KPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAAR------LPGAKVTATVADVADPAQVERVFDTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVA--HASLVENTNMDIFKVlIEVNYLGTVSLTKCVLPHMMERNQGK-IVVMKSLVGIVPRPLCSG 201
Cdd:PRK12829  81 VERFGGLDVLVNNAGIAgpTGGIDEITPEQWEQT-LAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTP 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61556948  202 YAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFT----------GDFTETRLPKIPLFKM 262
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPL-GIRVNAILPGIVRGPRMRRVIEaraqqlgiglDEMEQEYLEKISLGRM 229
PRK12937 PRK12937
short chain dehydrogenase; Provisional
46-251 1.01e-23

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 97.51  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLS-ARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTV 124
Cdd:PRK12937   2 TLSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGG----RAIAVQADVADAAAVTRLFDAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK12937  78 ETAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 61556948  205 SKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGDFTE 251
Cdd:PRK12937 156 SKAAVEGLVHVLANELRGR-GITVNAVAPGPVATELFFNGKSAEQID 201
PRK06482 PRK06482
SDR family oxidoreductase;
53-239 1.25e-23

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 97.88  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   53 W-ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENgnlkekdILVLPLDLADTSSHDIATKTVLQEFGRI 131
Cdd:PRK06482   5 WfITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDR-------LWVLQLDVTDSAAVRAVVDRAFAALGRI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  132 DILVNNGGVA---HASLVENTNMDifkVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:PRK06482  78 DVVVSNAGYGlfgAAEELSDAQIR---RQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWG 154
                        170       180       190
                 ....*....|....*....|....*....|.
gi 61556948  209 LRGFFDVLRTELFDYpGITLSMICPGPVHSN 239
Cdd:PRK06482 155 IEGFVEAVAQEVAPF-GIEFTIVEPGPARTN 184
PRK12939 PRK12939
short chain dehydrogenase; Provisional
47-244 1.27e-23

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 97.35  E-value: 1.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK12939   5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGG----RAHAIAADLADPASVQRFFDAAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK12939  81 ALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASK 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 61556948  207 LALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNA 244
Cdd:PRK12939 161 GAVIGMTRSLARELGGR-GITVNAIAPGLTATEATAYV 197
PRK05650 PRK05650
SDR family oxidoreductase;
52-234 1.36e-23

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 97.80  E-value: 1.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   52 VWITGASSGIGEELAFQLSKLG--VCLV-LSARRGQELERVKRrclENGNlkekDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGwrLALAdVNEEGGEETLKLLR---EAGG----DGFYQRCDVRDYSQLTALAQACEEKW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:PRK05650  76 GGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAG 155
                        170       180
                 ....*....|....*....|....*.
gi 61556948  209 LRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK05650 156 VVALSETLLVELADD-EIGVHVVCPS 180
PRK08017 PRK08017
SDR family oxidoreductase;
50-243 1.81e-23

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 97.08  E-value: 1.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENgnlkekdilvLPLDLADTSSHDIATKTVLQ-EF 128
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNSLGFTG----------ILLDLDDPESVERAADEVIAlTD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:PRK08017  73 NRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYA 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 61556948  209 LRGFFDVLRTELfDYPGITLSMICPGPVHSNIFQN 243
Cdd:PRK08017 153 LEAWSDALRMEL-RHSGIKVSLIEPGPIRTRFTDN 186
PRK07024 PRK07024
SDR family oxidoreductase;
52-234 4.41e-23

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 95.77  E-value: 4.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   52 VWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkekDILVLPLDLADTSSHDIATKTVLQEFGRI 131
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAA-----RVSVYAADVRDADALAAAAADFIAAHGLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  132 DILVNNGGVAHASLVENT-NMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALR 210
Cdd:PRK07024  80 DVVIANAGISVGTLTEEReDLAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAI 159
                        170       180
                 ....*....|....*....|....
gi 61556948  211 GFFDVLRTELFDyPGITLSMICPG 234
Cdd:PRK07024 160 KYLESLRVELRP-AGVRVVTIAPG 182
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
54-254 1.11e-22

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: 94.66  E-value: 1.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  54 ITGASSGIGEELAFQLSKLG-VCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQEFGRID 132
Cdd:cd05367   4 LTGASRGIGRALAEELLKRGsPSVVVLLARSEEPLQELKEELRPG----LRVTTVKADLSDAAGVEQLLEAIRKLDGERD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 133 ILVNNGGV-AHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERN-QGKIVVMKSLVGIVPRPLCSGYAASKLALR 210
Cdd:cd05367  80 LLINNAGSlGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSSKAARD 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 61556948 211 GFFDVLRTELfdyPGITLSMICPGPVHSNIFQNAFTGDFTETRL 254
Cdd:cd05367 160 MFFRVLAAEE---PDVRVLSYAPGVVDTDMQREIRETSADPETR 200
PRK08219 PRK08219
SDR family oxidoreductase;
50-236 1.65e-22

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 93.84  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKlGVCLVLSARRGqelERVKRRCLENGNLKekdilVLPLDLADTSshdiATKTVLQEFG 129
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP-THTLLLGGRPA---ERLDELAAELPGAT-----PFPVDLTDPE----AIAAAVEQLG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMErNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:PRK08219  71 RLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRA-AHGHVVFINSGAGLRANPGWGSYAASKFAL 149
                        170       180
                 ....*....|....*....|....*..
gi 61556948  210 RGFFDVLRTElfDYPGITLSMICPGPV 236
Cdd:PRK08219 150 RALADALREE--EPGNVRVTSVHPGRT 174
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
49-245 1.86e-22

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: 94.12  E-value: 1.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkEKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:cd05330   3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAP--DAEVLLIKADVSDEAQVEAYVDATVEQF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 GRIDILVNNGGV-AHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:cd05330  81 GRIDGFFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 61556948 208 ALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAF 245
Cdd:cd05330 161 GVVGLTRNSAVEYGQY-GIRINAIAPGAILTPMVEGSL 197
PRK08264 PRK08264
SDR family oxidoreductase;
47-283 5.86e-22

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 92.26  E-value: 5.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRgqELERVKRRclengnlkEKDILVLPLDLADTSSHDIATKTVlq 126
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAAKVYAAAR--DPESVTDL--------GPRVVPLQLDVTDPASVAAAAEAA-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 efGRIDILVNNGGVAH-ASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK08264  72 --SDVTILVNNAGIFRtGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSAS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPGPVhsnifqnaftgdftETRLPK-IPLFKMETSRCVQLILVSLANDLEDIW 283
Cdd:PRK08264 150 KAAAWSLTQALRAELAPQ-GTRVLGVHPGPI--------------DTDMAAgLDAPKASPADVARQILDALEAGDEEVL 213
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
49-283 6.27e-22

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: 92.47  E-value: 6.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRgqELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQef 128
Cdd:cd05354   3 DKTVLVTGANRGIGKAFVESLLAHGAKKVYAAVR--DPGSAAHLVAKYGD----KVVPLRLDVTDPESIKAAAAQAKD-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 grIDILVNNGGVAH-ASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:cd05354  75 --VDVVINNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSASKS 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61556948 208 ALRGFFDVLRTELFDYpGITLSMICPGPVhsnifqnaftgdftETRLP-KIPLFKMETSRCVQLILVSLANDLEDIW 283
Cdd:cd05354 153 AAYSLTQGLRAELAAQ-GTLVLSVHPGPI--------------DTRMAaGAGGPKESPETVAEAVLKALKAGEFHVF 214
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
47-234 9.19e-22

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: 92.17  E-value: 9.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkekdiLVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGA-------LALRVDVTDEQQVAALFERAVE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAH-ASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:cd08944  74 EFGGLDLLVNNAGAMHlTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGAS 153
                       170       180
                ....*....|....*....|....*....
gi 61556948 206 KLALRGFFDVLRTELfDYPGITLSMICPG 234
Cdd:cd08944 154 KAAIRNLTRTLAAEL-RHAGIRCNALAPG 181
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
52-279 1.07e-21

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: 91.76  E-value: 1.07e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  52 VWITGASSGIGEELAFQLSKLGVcLVLSARRGQELERVKRRCLEngnlkekdilVLPLDLADTSSHDIATKTVLQEFGRI 131
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGA-TVIALDLPFVLLLEYGDPLR----------LTPLDVADAAAVREVCSRLLAEHGPI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 132 DILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALRG 211
Cdd:cd05331  70 DALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALAS 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61556948 212 FFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGDFTETRLPK---------IPLFKMETSRCVQLILVSLANDL 279
Cdd:cd05331 150 LSKCLGLELAPY-GVRCNVVSPGSTDTAMQRTLWHDEDGAAQVIAgvpeqfrlgIPLGKIAQPADIANAVLFLASDQ 225
PRK12827 PRK12827
short chain dehydrogenase; Provisional
47-245 1.28e-21

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 91.70  E-value: 1.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLG---VCLVLSARRG-QELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATK 122
Cdd:PRK12827   4 LDSRRVLITGGSGGLGRAIAVRLAADGadvIVLDIHPMRGrAEADAVAAGIEAAGG----KALGLAFDVRDFAATRAALD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGRIDILVNNGGVA-HASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVGIVPRPLCS 200
Cdd:PRK12827  80 AGVEEFGRLDILVNNAGIAtDAAFAELSIEE-WDDVIDVNLDGFFNVTQAALPPMIRARRgGRIVNIASVAGVRGNRGQV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 61556948  201 GYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAF 245
Cdd:PRK12827 159 NYAASKAGLIGLTKTLANELAPR-GITVNAVAPGAINTPMADNAA 202
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
54-236 2.05e-21

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: 90.82  E-value: 2.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVkrrcLENGNLKEKDILVLPLDLADTSSHDIATKTVLQEFGRIDI 133
Cdd:cd05325   3 ITGASRGIGLELVRQLLARGNNTVIATCRDPSAATE----LAALGASHSRLHILELDVTDEIAESAEAVAERLGDAGLDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 134 LVNNGGVAHAS-LVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVG----IVPRPLcSGYAASKLA 208
Cdd:cd05325  79 LINNAGILHSYgPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGsigdNTSGGW-YSYRASKAA 157
                       170       180
                ....*....|....*....|....*...
gi 61556948 209 LRGFFDVLRTELFDyPGITLSMICPGPV 236
Cdd:cd05325 158 LNMLTKSLAVELKR-DGITVVSLHPGWV 184
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
56-236 2.62e-21

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: 90.57  E-value: 2.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948    56 GA--SSGIGEELAFQLSKLGVCLVLSARRGQELERVKRrclengNLKEKDILVLPLDLADTSSHDIATKTVLQEFGRIDI 133
Cdd:pfam13561   1 GAanESGIGWAIARALAEEGAEVVLTDLNEALAKRVEE------LAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   134 LVNNGGVAHASL--VENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGYAASKLALRG 211
Cdd:pfam13561  75 LVNNAGFAPKLKgpFLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEA 152
                         170       180
                  ....*....|....*....|....*
gi 61556948   212 FFDVLRTELFDYpGITLSMICPGPV 236
Cdd:pfam13561 153 LTRYLAVELGPR-GIRVNAISPGPI 176
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
50-236 2.75e-21

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: 90.26  E-value: 2.75e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENgnlkekdILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEG-------VLGLAGDVRDEADVRRAVDAMEEAFG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:cd08929  74 GLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGL 153
                       170       180
                ....*....|....*....|....*..
gi 61556948 210 RGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:cd08929 154 LGLSEAAMLDLREA-NIRVVNVMPGSV 179
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
47-241 4.90e-21

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: 90.03  E-value: 4.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLS-ARRGQELERVKRRCLENGNlkeKDILVLpldlADTSS-HDIAT--K 122
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEIEAAGG---KAIAVQ----ADVSDpSQVARlfD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 123 TVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:cd05362  74 AAEKAFGGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAY 151
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 61556948 203 AASKLALRGFFDVLRTELFDyPGITLSMICPGPVHSNIF 241
Cdd:cd05362 152 AGSKAAVEAFTRVLAKELGG-RGITVNAVAPGPVDTDMF 189
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
54-278 5.15e-21

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 89.97  E-value: 5.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKrrclenGNLKEKdILVLPLDLADTSSHDIATKTVLQEFGRIDI 133
Cdd:PRK12936  11 VTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALA------AELGER-VKIFPANLSDRDEVKALGQKAEADLEGVDI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  134 LVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALRGFF 213
Cdd:PRK12936  84 LVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFS 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948  214 DVLRTELFDYpGITLSMICPGPVHSnifqnAFTGDFT----ETRLPKIPLFKMETSRCVQLILVSLAND 278
Cdd:PRK12936 164 KSLAQEIATR-NVTVNCVAPGFIES-----AMTGKLNdkqkEAIMGAIPMKRMGTGAEVASAVAYLASS 226
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-236 8.04e-21

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 89.78  E-value: 8.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRG-QELERVKRRCLENGNlkeKDILVLpldlADTSSH----DIAT 121
Cdd:PRK06077   4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRaEEMNETLKMVKENGG---EGIGVL----ADVSTRegceTLAK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  122 KTvLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:PRK06077  77 AT-IDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSI 153
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 61556948  202 YAASKLALRGFFDVLRTELfdYPGITLSMICPGPV 236
Cdd:PRK06077 154 YGAMKAAVINLTKYLALEL--APKIRVNAIAPGFV 186
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
47-281 8.44e-21

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: 89.75  E-value: 8.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEKDILvlpldlADTSSHDIATK---T 123
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQ------ADVSKEEDVVAlfqS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 124 VLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERN-QGKIVVMKSLVGIVPRPLCSGY 202
Cdd:cd05358  75 AIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKiKGKIINMSSVHEKIPWPGHVNY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 203 AASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIfqNAFTGDFTETR---LPKIPLFKMETSRCVQLILVSLANDL 279
Cdd:cd05358 155 AASKGGVKMMTKTLAQEYAPK-GIRVNAIAPGAINTPI--NAEAWDDPEQRadlLSLIPMGRIGEPEEIAAAAAWLASDE 231

                ..
gi 61556948 280 ED 281
Cdd:cd05358 232 AS 233
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
50-234 2.87e-20

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 87.90  E-value: 2.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELerVKRRCLENGNLKEKdILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDC--AKDWFEEYGFTEDQ-VRLKELDVTDTEECAEALAEIEEEEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVG---IVPRPlcsGYAASK 206
Cdd:PRK12824  80 PVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGlkgQFGQT---NYSAAK 156
                        170       180
                 ....*....|....*....|....*...
gi 61556948  207 LALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK12824 157 AGMIGFTKALASEGARY-GITVNCIAPG 183
PRK05693 PRK05693
SDR family oxidoreductase;
50-244 3.14e-20

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 88.31  E-value: 3.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELErvkrrclengNLKEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVE----------ALAAAGFTAVQLDVNDGAALARLAEELEAEHG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPhMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:PRK05693  72 GLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFP-LLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 61556948  210 RGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNA 244
Cdd:PRK05693 151 HALSDALRLELAPF-GVQVMEVQPGAIASQFASNA 184
PRK06172 PRK06172
SDR family oxidoreductase;
47-248 3.35e-20

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 87.88  E-value: 3.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLadtsSHDIATKTVLQ 126
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGG----EALFVACDV----TRDAEVKALVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 E----FGRIDILVNNGGV--AHASLVENTnMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCS 200
Cdd:PRK06172  77 QtiaaYGRLDYAFNNAGIeiEQGRLAEGS-EAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 61556948  201 GYAASKLALRGffdVLRTELFDYP--GITLSMICPGPVHSNIFQNAFTGD 248
Cdd:PRK06172 156 IYAASKHAVIG---LTKSAAIEYAkkGIRVNAVCPAVIDTDMFRRAYEAD 202
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
47-206 3.62e-20

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: 87.83  E-value: 3.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkekdiLVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05345   3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAA-------IAIQADVTKRADVEAMVEAALS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAH----ASLVENTNMD-IFKVLIEVNYLGtvslTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:cd05345  76 KFGRLDILVNNAGITHrnkpMLEVDEEEFDrVFAVNVKSIYLS----AQALVPHMEEQGGGVIINIASTAGLRPRPGLTW 151

                ....*
gi 61556948 202 YAASK 206
Cdd:cd05345 152 YNASK 156
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
47-262 4.46e-20

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: 87.64  E-value: 4.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRgqeLERVKRRCLENGNLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRK---PEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMER-NQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:cd05369  78 EFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAkHGGSILNISATYAYTGSPFQVHSAAA 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948 206 KLALRGFFDVLRTELFDYpGITLSMICPGPV-HSNIFQNAF-TGDFTETRLPKIPLFKM 262
Cdd:cd05369 158 KAGVDALTRSLAVEWGPY-GIRVNAIAPGPIpTTEGMERLApSGKSEKKMIERVPLGRL 215
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
46-247 4.50e-20

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 87.62  E-value: 4.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEkdiLVLPLDLADTSSH---DIAtK 122
Cdd:PRK08945   9 LLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQP---AIIPLDLLTATPQnyqQLA-D 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGRIDILVNNGGVAHA-SLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:PRK08945  85 TIEEQFGRLDGVLHNAGLLGElGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGA 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 61556948  202 YAASKLALRGFFDVLRTELfDYPGITLSMICPGPVHSNIFQNAFTG 247
Cdd:PRK08945 165 YAVSKFATEGMMQVLADEY-QGTNLRVNCINPGGTRTAMRASAFPG 209
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
43-209 5.12e-20

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 90.68  E-value: 5.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   43 PEQALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkekDILVLPLDLADTSSHDIATK 122
Cdd:PRK08324 416 KPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-----RALGVACDVTDEAAVQAAFE 490
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGK---IVVMKSLVGIVPRPLC 199
Cdd:PRK08324 491 EAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIM--KAQGLggsIVFIASKNAVNPGPNF 568
                        170
                 ....*....|
gi 61556948  200 SGYAASKLAL 209
Cdd:PRK08324 569 GAYGAAKAAE 578
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
47-236 8.22e-20

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 87.00  E-value: 8.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARrgqELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADI---KPARARLAALEIGP----AAIAVSLDVTRQDSIDRIVAAAVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAH-ASLVENTNmDIFKVLIEVNYLGTVSLTKCVLPHMMERNQG-KIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK07067  77 RFGGIDILFNNAALFDmAPILDISR-DSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRRGEALVSHYCA 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 61556948  205 SKLALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:PRK07067 156 TKAAVISYTQSAALALIRH-GINVNAIAPGVV 186
PRK08251 PRK08251
SDR family oxidoreductase;
50-244 1.25e-19

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 86.14  E-value: 1.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLE-NGNLKekdILVLPLDLADtssHDiATKTVL--- 125
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLArYPGIK---VAVAALDVND---HD-QVFEVFaef 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 -QEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGI--VPRPLcSGY 202
Cdd:PRK08251  76 rDELGGLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVrgLPGVK-AAY 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 61556948  203 AASKLALRGFFDVLRTELFDYPgITLSMICPGPVHSNIFQNA 244
Cdd:PRK08251 155 AASKAGVASLGEGLRAELAKTP-IKVSTIEPGYIRSEMNAKA 195
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
51-248 1.49e-19

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 85.96  E-value: 1.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   51 VVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENgnlkekdILVLPLDLADTSSHDIATKTVLQEFGR 130
Cdd:PRK10538   2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDN-------LYIAQLDVRNRAAIEEMLASLPAEWRN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  131 IDILVNNGGVAHA-SLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:PRK10538  75 IDVLVNNAGLALGlEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFV 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 61556948  210 RGFFDVLRTELFDyPGITLSMICPGPVHSNIFQNA-FTGD 248
Cdd:PRK10538 155 RQFSLNLRTDLHG-TAVRVTDIEPGLVGGTEFSNVrFKGD 193
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
48-252 1.56e-19

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: 86.43  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  48 ADKVVWITGASSGIGEELAFQLSKLGVCLVLSAR---RGQELERVKRRCLENGnlkekdILVLPLDLadTSSHDIAT--- 121
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARgeaAGQALESELNRAGPGS------CKFVPCDV--TKEEDIKTlis 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 122 KTVlQEFGRIDILVNNGGVaHA--SLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERnQGKIVVMKSLVGIVPRPLC 199
Cdd:cd08933  80 VTV-ERFGRIDCLVNNAGW-HPphQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKS-QGNIINLSSLVGSIGQKQA 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 61556948 200 SGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQN--AFTGDFTET 252
Cdd:cd08933 157 APYVATKGAITAMTKALAVDESRY-GVRVNCISPGNIWTPLWEElaAQTPDTLAT 210
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
50-238 1.89e-19

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: 85.89  E-value: 1.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELerVKRRCLEngnLKEKD--ILVLPLDLADTSSHDIATKTVLQE 127
Cdd:cd05366   3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEA--AKSTIQE---ISEAGynAVAVGADVTDKDDVEALIDQAVEK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 128 FGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERN-QGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd05366  78 FGSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASK 157
                       170       180       190
                ....*....|....*....|....*....|..
gi 61556948 207 LALRGFFDVLRTELFDYpGITLSMICPGPVHS 238
Cdd:cd05366 158 FAVRGLTQTAAQELAPK-GITVNAYAPGIVKT 188
PRK06124 PRK06124
SDR family oxidoreductase;
46-234 2.29e-19

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 85.92  E-value: 2.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEkdilVLPLDLADTSSHDIATKTVL 125
Cdd:PRK06124   8 SLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAE----ALAFDIADEEAVAAAFARID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK06124  84 AEHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAA 163
                        170       180
                 ....*....|....*....|....*....
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK06124 164 KQGLTGLMRALAAEFGPH-GITSNAIAPG 191
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
51-259 2.54e-19

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: 85.31  E-value: 2.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  51 VVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEFGR 130
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGG----QAIGLECNVTSEQDLEAVVKATVSQFGG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 131 IDILVNN--GGVAHASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:cd05365  77 ITILVNNagGGGPKPFDMPMTEED-FEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAA 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 61556948 209 LRgffDVLRTELFDY--PGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPL 259
Cdd:cd05365 156 VN---HMTRNLAFDLgpKGIRVNAVAPGAVKTDALASVLTPEIERAMLKHTPL 205
PRK07478 PRK07478
short chain dehydrogenase; Provisional
47-220 2.59e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 85.37  E-value: 2.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELER-VKRRCLENGnlkekDILVLPLDLADTSSHDIATKTVL 125
Cdd:PRK07478   4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQlVAEIRAEGG-----EAVALAGDVRDEAYAKALVALAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGGV--AHASLVENTNMDIFKVLievnylgTVSLT------KCVLPHMMERNQGKIVVMKSLVG-IVPR 196
Cdd:PRK07478  79 ERFGGLDIAFNNAGTlgEMGPVAEMSLEGWRETL-------ATNLTsaflgaKHQIPAMLARGGGSLIFTSTFVGhTAGF 151
                        170       180
                 ....*....|....*....|....
gi 61556948  197 PLCSGYAASKLALRGFFDVLRTEL 220
Cdd:PRK07478 152 PGMAAYAASKAGLIGLTQVLAAEY 175
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
47-258 2.65e-19

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 85.44  E-value: 2.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQE-LERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVL 125
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEaAENLVNELGKEGH----DVYAVQADVSKVEDANRLVEEAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK12935  80 NHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAA 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 61556948  206 KLALRGFFDVLRTELFDyPGITLSMICPGPVHSNIFQnAFTGDFTETRLPKIP 258
Cdd:PRK12935 160 KAGMLGFTKSLALELAK-TNVTVNAICPGFIDTEMVA-EVPEEVRQKIVAKIP 210
PRK06484 PRK06484
short chain dehydrogenase; Validated
50-242 4.10e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 87.60  E-value: 4.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQelervkrRCLENGNLKEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVE-------RARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVA--HASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGK-IVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK06484  79 RIDVLVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASK 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 61556948  207 LALRGFFDVLRTELfDYPGITLSMICPGPVHSNIFQ 242
Cdd:PRK06484 159 AAVISLTRSLACEW-AAKGIRVNAVLPGYVRTQMVA 193
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
50-238 4.91e-19

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: 84.90  E-value: 4.91e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd08945   4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAG----VEADGRTCDVRSVPEIEALVAAAVARYG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNN----GGVAHASLVENTNMDIfkvlIEVNYLGTVSLTKCVLPH--MMERNQGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:cd08945  80 PIDVLVNNagrsGGGATAELADELWLDV----VETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYS 155
                       170       180       190
                ....*....|....*....|....*....|....*
gi 61556948 204 ASKLALRGFFDVLRTELFDyPGITLSMICPGPVHS 238
Cdd:cd08945 156 ASKHGVVGFTKALGLELAR-TGITVNAVCPGFVET 189
PRK07060 PRK07060
short chain dehydrogenase; Provisional
50-229 7.39e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 84.00  E-value: 7.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKrrclengnlKEKDILVLPLDLADTSSHDIAtktvLQEFG 129
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLA---------GETGCEPLRLDVGDDAAIRAA----LAAAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:PRK07060  77 AFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRgGSIVNVSSQAALVGLPDHLAYCASKAA 156
                        170       180
                 ....*....|....*....|....*....
gi 61556948  209 LRGFFDVLRTELFDY--------PGITLS 229
Cdd:PRK07060 157 LDAITRVLCVELGPHgirvnsvnPTVTLT 185
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
47-236 7.56e-19

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: 84.65  E-value: 7.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLS--------ARRGQEL-ERVKRRCLengnlkekdilVLPLDLADTSSH 117
Cdd:cd05355  24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylpeeeddAEETKKLiEEEGRKCL-----------LIPGDLGDESFC 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 118 DIATKTVLQEFGRIDILVNNGGVAHASlveNTNMDIFKVLIE----VNYLGTVSLTKCVLPHMMErnQGKIVVMKSLVGI 193
Cdd:cd05355  93 RDLVKEVVKEFGKLDILVNNAAYQHPQ---ESIEDITTEQLEktfrTNIFSMFYLTKAALPHLKK--GSSIINTTSVTAY 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 61556948 194 VPRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:cd05355 168 KGSPHLLDYAATKGAIVAFTRGLSLQLAEK-GIRVNAVAPGPI 209
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
54-255 9.52e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 84.05  E-value: 9.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGNLKEKdilVLPLDLADTSSHDIATKTVLQEFGRIDI 133
Cdd:PRK07523  15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAES-LKGQGLSAH---ALAFDVTDHDAVRAAIDAFEAEIGPIDI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  134 LVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALRGFF 213
Cdd:PRK07523  91 LVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAVGNLT 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 61556948  214 DVLRTELFDYpGITLSMICPG----PVHSNIFQNAFTGDFTETRLP 255
Cdd:PRK07523 171 KGMATDWAKH-GLQCNAIAPGyfdtPLNAALVADPEFSAWLEKRTP 215
PRK06398 PRK06398
aldose dehydrogenase; Validated
47-236 1.01e-18

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 84.11  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVlsarrgqelervkrrcleNGNLKEKDILVLPLDLADTSSHDIATKTV-- 124
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVI------------------NFDIKEPSYNDVDYFKVDVSNKEQVIKGIdy 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 -LQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:PRK06398  66 vISKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYV 145
                        170       180       190
                 ....*....|....*....|....*....|....
gi 61556948  204 ASKLALRGffdVLRTELFDY-PGITLSMICPGPV 236
Cdd:PRK06398 146 TSKHAVLG---LTRSIAVDYaPTIRCVAVCPGSI 176
PRK07814 PRK07814
SDR family oxidoreductase;
47-236 1.88e-18

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 83.29  E-value: 1.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADT-SSHDIATKTVl 125
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAG----RRAHVVAADLAHPeATAGLAGQAV- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNN-GGVAHASLVENTNMDIfKVLIEVNYLGTVSLTKCVLPHMMERN-QGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:PRK07814  83 EAFGRLDIVVNNvGGTMPNPLLSTSTKDL-ADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYG 161
                        170       180       190
                 ....*....|....*....|....*....|...
gi 61556948  204 ASKLALRGFFDVLRTELfdYPGITLSMICPGPV 236
Cdd:PRK07814 162 TAKAALAHYTRLAALDL--CPRIRVNAIAPGSI 192
PRK08703 PRK08703
SDR family oxidoreductase;
46-238 2.02e-18

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 82.67  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEKDIlvlPLDLADTSSHDIA--TKT 123
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAI---RFDLMSAEEKEFEqfAAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  124 VLQEF-GRIDILVNNGGVAHA-SLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:PRK08703  80 IAEATqGKLDGIVHCAGYFYAlSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGG 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 61556948  202 YAASKLALRGFFDVLRTELFDYPGITLSMICPGPVHS 238
Cdd:PRK08703 160 FGASKAALNYLCKVAADEWERFGNLRANVLVPGPINS 196
PRK07063 PRK07063
SDR family oxidoreductase;
47-234 2.25e-18

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 83.18  E-value: 2.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVA--GARVLAVPADVTDAASVAAAVAAAEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGV-AHASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK07063  83 AFGPLDVLVNNAGInVFADPLAMTDED-WRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVA 161
                        170       180
                 ....*....|....*....|....*....
gi 61556948  206 KLALRGFFDVLRTElFDYPGITLSMICPG 234
Cdd:PRK07063 162 KHGLLGLTRALGIE-YAARNVRVNAIAPG 189
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
47-248 2.89e-18

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: 82.24  E-value: 2.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEkdiLVLPLDLADTSSHD---IATKt 123
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQP---QWFILDLLTCTSENcqqLAQR- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 124 VLQEFGRIDILVNNGGVAHASL-VENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:cd05340  78 IAVNYPRLDGVLHNAGLLGDVCpLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 61556948 203 AASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTGD 248
Cdd:cd05340 158 AVSKFATEGL*QVLADEYQQR-NLRVNCINPGGTRTAMRASAFPTE 202
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
47-210 3.09e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 82.80  E-value: 3.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERvkrrCLENgnLKEKDILVLPL--DLADTSSHDIATKTV 124
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDK----GLAA--YRELGIEAHGYvcDVTDEDGVQAMVSQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK07097  82 EKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAA 161

                 ....*.
gi 61556948  205 SKLALR 210
Cdd:PRK07097 162 AKGGLK 167
PRK06057 PRK06057
short chain dehydrogenase; Provisional
45-259 3.86e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 82.47  E-value: 3.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLG---VCLVLSARRGQELErvkrrclengnlKEKDILVLPLDLADTSSHDIAT 121
Cdd:PRK06057   3 QRLAGRVAVITGGGSGIGLATARRLAAEGatvVVGDIDPEAGKAAA------------DEVGGLFVPTDVTDEDAVNALF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  122 KTVLQEFGRIDILVNNGGVAHA--SLVENTNMDIFKVLIEVNyLGTVSL-TKCVLPHMMERNQGKIVVMKSLVGIVprpl 198
Cdd:PRK06057  71 DTAAETYGSVDIAFNNAGISPPedDSILNTGLDAWQRVQDVN-LTSVYLcCKAALPHMVRQGKGSIINTASFVAVM---- 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948  199 csGYAASKL---ALRGFFDVLRTEL---FDYPGITLSMICPGPVHSNIFQNAFTGD--FTETRLPKIPL 259
Cdd:PRK06057 146 --GSATSQIsytASKGGVLAMSRELgvqFARQGIRVNALCPGPVNTPLLQELFAKDpeRAARRLVHVPM 212
PRK06125 PRK06125
short chain dehydrogenase; Provisional
47-236 4.19e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 82.40  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLkekDILVLPLDLADTSSHDiatkTVLQ 126
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGV---DVAVHALDLSSPEARE----QLAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPlcsGY---A 203
Cdd:PRK06125  78 EAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDA---DYicgS 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 61556948  204 ASKLALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:PRK06125 155 AGNAALMAFTRALGGKSLDD-GVRVVGVNPGPV 186
PRK08589 PRK08589
SDR family oxidoreductase;
47-236 6.46e-18

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 82.13  E-value: 6.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVcLVLSARRGQELERVKRRCLENGNLKEKDILvlplDLADTSSHDIATKTVLQ 126
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGA-YVLAVDIAEAVSETVDKIKSNGGKAKAYHV----DISDEQQVKDFASEIKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAH-ASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMErNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK08589  79 QFGRVDVLFNNAGVDNaAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQAADLYRSGYNAA 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 61556948  206 KLALRGFfdvLRTELFDY--PGITLSMICPGPV 236
Cdd:PRK08589 158 KGAVINF---TKSIAIEYgrDGIRANAIAPGTI 187
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
47-234 7.30e-18

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: 81.42  E-value: 7.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGNLkekdILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEI-LAAGDA----AHVHTADLETYAGAQGVVRAAVE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNN-GGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLV--GIVPRPlcsgYA 203
Cdd:cd08937  77 RFGRVDVLINNvGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIYRIP----YS 152
                       170       180       190
                ....*....|....*....|....*....|.
gi 61556948 204 ASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:cd08937 153 AAKGGVNALTASLAFEHARD-GIRVNAVAPG 182
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
49-234 7.57e-18

(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: 81.21  E-value: 7.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQelervkrRCLENGNLKEKDILVLPLD------LADtsSHDIAT- 121
Cdd:cd05353   5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGD-------RKGSGKSSSAADKVVDEIKaaggkaVAN--YDSVEDg 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 122 ----KTVLQEFGRIDILVNNGGVAH-ASLVENTNMDIFKVlIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPR 196
Cdd:cd05353  76 ekivKTAIDAFGRVDILVNNAGILRdRSFAKMSEEDWDLV-MRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYGN 154
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 61556948 197 PLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:cd05353 155 FGQANYSAAKLGLLGLSNTLAIEGAKY-NITCNTIAPA 191
PRK06949 PRK06949
SDR family oxidoreductase;
47-240 1.42e-17

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 80.96  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGG----AAHVVSLDVTDYQSIKAAVAHAET 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERN--------QGKIVVMKSLVGIVPRPL 198
Cdd:PRK06949  83 EAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARAkgagntkpGGRIINIASVAGLRVLPQ 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 61556948  199 CSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNI 240
Cdd:PRK06949 163 IGLYCMSKAAVVHMTRAMALEWGRH-GINVNAICPGYIDTEI 203
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
47-234 2.01e-17

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 80.55  E-value: 2.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARrGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTH-GTNWDETRRLIEKEG----RKVTFVQVDLTKPESAEKVVKEALE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAH-ASLVENTNMDIFKVlIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK06935  88 EFGKIDILVNNAGTIRrAPLLEYKDEDWNAV-MDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKFVPAYTAS 166
                        170       180
                 ....*....|....*....|....*....
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK06935 167 KHGVAGLTKAFANELAAY-NIQVNAIAPG 194
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
50-278 2.51e-17

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: 79.82  E-value: 2.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLV---LSARRGQELERVKRrclengnlkekdILVLPLDLADtsshDIATKTVLQ 126
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREGANVIatdINEEKLKELERGPG------------ITTRVLDVTD----KEQVAALAK 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGG-VAHASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVG-IVPRPLCSGYAA 204
Cdd:cd05368  67 EEGRIDVLFNCAGfVHHGSILDCEDDD-WDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYST 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948 205 SKLALRGFFDVLRTElFDYPGITLSMICPGPVHSNIFQN--AFTGDFTETR---LPKIPLFKMETSRCVQLILVSLAND 278
Cdd:cd05368 146 TKAAVIGLTKSVAAD-FAQQGIRCNAICPGTVDTPSLEEriQAQPDPEEALkafAARQPLGRLATPEEVAALAVYLASD 223
PRK12743 PRK12743
SDR family oxidoreductase;
48-234 2.52e-17

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 80.08  E-value: 2.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   48 ADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQE-LERVKRRCLENGNLKEkdilVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEgAKETAEEVRSHGVRAE----IRQLDLSDLPEGAQALDKLIQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK12743  77 RLGRIDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQgGRIINITSVHEHTPLPGASAYTAA 156
                        170       180
                 ....*....|....*....|....*....
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK12743 157 KHALGGLTKAMALELVEH-GILVNAVAPG 184
PRK07577 PRK07577
SDR family oxidoreductase;
49-278 2.63e-17

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 79.39  E-value: 2.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQElervkrrclengNLKEKDILVlplDLADTSSHDIATKTVLQEF 128
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQVIGIARSAID------------DFPGELFAC---DLADIEQTAATLAQINEIH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GrIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLvGIVPRPLCSGYAASKLA 208
Cdd:PRK07577  68 P-VDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSR-AIFGALDRTSYSAAKSA 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61556948  209 LRGffdVLRT---ELFDYpGITLSMICPGPVHSNIFQNAF-TGDFTETR-LPKIPLFKMETSRCVQLILVSLAND 278
Cdd:PRK07577 146 LVG---CTRTwalELAEY-GITVNAVAPGPIETELFRQTRpVGSEEEKRvLASIPMRRLGTPEEVAAAIAFLLSD 216
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
47-262 2.71e-17

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: 79.68  E-value: 2.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEKDILVlplDLADTSSHDIATKTVLQ 126
Cdd:cd05352   6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKC---DVSSQESVEKTFKQIQK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVG-IVPRPL-CSGYAA 204
Cdd:cd05352  83 DFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGtIVNRPQpQAAYNA 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 61556948 205 SKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTgDFTETRLPKIPLFKM 262
Cdd:cd05352 163 SKAAVIHLAKSLAVEWAKY-FIRVNSISPGYIDTDLTDFVDK-ELRKKWESYIPLKRI 218
PRK06500 PRK06500
SDR family oxidoreductase;
47-242 1.41e-16

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 77.69  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRrclENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARA---ELGE----SALVIRADAGDVAAQKALAQALAE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK06500  77 AFGRLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL--ANPASIVLNGSINAHIGMPNSSVYAASK 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 61556948  207 LALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQ 242
Cdd:PRK06500 155 AALLSLAKTLSGELLPR-GIRVNAVSPGPVQTPLYG 189
PRK08628 PRK08628
SDR family oxidoreductase;
47-209 1.74e-16

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 77.69  E-value: 1.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRrclengnLKEK--DILVLPLDLADTSSHDIATKTV 124
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEE-------LRALqpRAEFVQVDLTDDAQCRDAVEQT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVAHASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMErNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK08628  78 VAKFGRIDGLVNNAGVNDGVGLEAGREA-FVASLERNLIHYYVMAHYCLPHLKA-SRGAIVNISSKTALTGQGGTSGYAA 155

                 ....*...
gi 61556948  205 SK---LAL 209
Cdd:PRK08628 156 AKgaqLAL 163
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
49-246 2.25e-16

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: 77.37  E-value: 2.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARrgqELERVKRRCLENGNLKEKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:cd08930   2 DKIILITGAAGLIGKAFCKALLSAGARLILADI---NAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 GRIDILVNNGGV---AHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIV---------PR 196
Cdd:cd08930  79 GRIDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIapdfriyenTQ 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 61556948 197 PLCS-GYAASKLALRGFFDVLRTELFDYpGITLSMICPGPV---HSNIFQNAFT 246
Cdd:cd08930 159 MYSPvEYSVIKAGIIHLTKYLAKYYADT-GIRVNAISPGGIlnnQPSEFLEKYT 211
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
43-220 2.32e-16

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: 77.13  E-value: 2.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  43 PEQALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRClengnlkeKDILVLPLDLADTSshdiATK 122
Cdd:cd05351   1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREC--------PGIEPVCVDLSDWD----ATE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 123 TVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERN-QGKIVVMKSLVGIVPRPLCSG 201
Cdd:cd05351  69 EALGSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTV 148
                       170
                ....*....|....*....
gi 61556948 202 YAASKLALRGFFDVLRTEL 220
Cdd:cd05351 149 YCSTKAALDMLTKVMALEL 167
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
45-239 3.35e-16

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: 76.81  E-value: 3.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELER-----------VKRRCLENGNLKEKDILVlpldlad 113
Cdd:cd08936   6 DPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRavatlqgeglsVTGTVCHVGKAEDRERLV------- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 114 tsshdiatKTVLQEFGRIDILVNNGGVA--HASLVENTNmDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLV 191
Cdd:cd08936  79 --------ATAVNLHGGVDILVSNAAVNpfFGNILDSTE-EVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVA 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 61556948 192 GIVPRPLCSGYAASKLALRGFFDVLRTELfDYPGITLSMICPGPVHSN 239
Cdd:cd08936 150 AFHPFPGLGPYNVSKTALLGLTKNLAPEL-APRNIRVNCLAPGLIKTS 196
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
49-234 4.31e-16

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 76.61  E-value: 4.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCleNGNLKEKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEI--NAEYGEGMAYGFGADATSEQSVLALSRGVDEIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERN-QGKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:PRK12384  80 GRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKF 159
                        170       180
                 ....*....|....*....|....*..
gi 61556948  208 ALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK12384 160 GGVGLTQSLALDLAEY-GITVHSLMLG 185
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
54-256 4.94e-16

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: 75.25  E-value: 4.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRrclengnlkEKDILVLPLDLAdtssHDIATKTVLQEFGRIDI 133
Cdd:cd11730   3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAA---------EVGALARPADVA----AELEVWALAQELGPLDL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 134 LVNNGGVAHAS-LVENTNMDIFKVLiEVNYLGTVSLTKCVLPHMMErnQGKIVVMKSLVGIVPRPLCSGYAASKLALRGF 212
Cdd:cd11730  70 LVYAAGAILGKpLARTKPAAWRRIL-DANLTGAALVLKHALALLAA--GARLVFLGAYPELVMLPGLSAYAAAKAALEAY 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 61556948 213 FDVLRTELfdyPGITLSMICPGPVHSNIFQNAFtgdftetRLPK 256
Cdd:cd11730 147 VEVARKEV---RGLRLTLVRPPAVDTGLWAPPG-------RLPK 180
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
47-234 6.48e-16

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 76.48  E-value: 6.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGG----EALAVKADVLDKESLEQARQQILE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHA---------SLVENT----NMDI--FKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLV 191
Cdd:PRK08277  84 DFGPCDILINGAGGNHPkattdnefhELIEPTktffDLDEegFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMN 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 61556948  192 GivPRPLCS--GYAASKLALRGFFDVLRTElFDYPGITLSMICPG 234
Cdd:PRK08277 164 A--FTPLTKvpAYSAAKAAISNFTQWLAVH-FAKVGIRVNAIAPG 205
PRK06701 PRK06701
short chain dehydrogenase; Provisional
47-236 8.88e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 76.23  E-value: 8.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAfqlsklgvclVLSARRG-----------QELERVKRRCLENGnlkeKDILVLPLDLADTS 115
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVA----------VLFAKEGadiaivyldehEDANETKQRVEKEG----VKCLLIPGDVSDEA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  116 -SHDIATKTVlQEFGRIDILVNNGGVA-HASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGI 193
Cdd:PRK06701 110 fCKDAVEETV-RELGRLDILVNNAAFQyPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL--KQGSAIINTGSITGY 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 61556948  194 VPRPLCSGYAASKLALRGFFDVLRTELFDyPGITLSMICPGPV 236
Cdd:PRK06701 187 EGNETLIDYSATKGAIHAFTRSLAQSLVQ-KGIRVNAVAPGPI 228
PRK06114 PRK06114
SDR family oxidoreductase;
47-234 1.72e-15

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 74.82  E-value: 1.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRG--------QELERVKRRCLengnlkekdilVLPLDLADTSSHD 118
Cdd:PRK06114   6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTddglaetaEHIEAAGRRAI-----------QIAADVTSKADLR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  119 IATKTVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVG-IVPRP 197
Cdd:PRK06114  75 AAVARTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGiIVNRG 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 61556948  198 LC-SGYAASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK06114 155 LLqAHYNASKAGVIHLSKSLAMEWVGR-GIRVNSISPG 191
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
54-236 2.04e-15

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: 74.31  E-value: 2.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQEL-ERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQEFGRID 132
Cdd:cd05359   3 VTGGSRGIGKAIALRLAERGADVVINYRKSKDAaAEVAAEIEELG----GKAVVVRADVSQPQDVEEMFAAVKERFGRLD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 133 ILVNNGGV-AHASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPlcsGYAA---SKLA 208
Cdd:cd05359  79 VLVSNAAAgAFRPLSELTPAH-WDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALP---NYLAvgtAKAA 154
                       170       180
                ....*....|....*....|....*...
gi 61556948 209 LRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:cd05359 155 LEALVRYLAVELGPR-GIRVNAVSPGVI 181
PRK07074 PRK07074
SDR family oxidoreductase;
48-236 2.31e-15

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 74.42  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   48 ADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRclengnLKEKDILVLPLDLADTSSHDIATKTVLQE 127
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADA------LGDARFVPVACDLTDAASLAAALANAAAE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  128 FGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGI--VPRPlcsGYAAS 205
Cdd:PRK07074  75 RGPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMaaLGHP---AYSAA 151
                        170       180       190
                 ....*....|....*....|....*....|.
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:PRK07074 152 KAGLIHYTKLLAVEYGRF-GIRANAVAPGTV 181
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
45-236 2.50e-15

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 73.84  E-value: 2.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGeelafqLSKLGVCLVLSAR-RGQELErvkrrclENGNLkEKDILVLPLDLADtsshdiATKT 123
Cdd:PRK06550   1 QEFMTKTVLITGAASGIG------LAQARAFLAQGAQvYGVDKQ-------DKPDL-SGNFHFLQLDLSD------DLEP 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  124 VLQEFGRIDILVNNGGV--AHASLVENTNMDIFKVLiEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:PRK06550  61 LFDWVPSVDILCNTAGIldDYKPLLDTSLEEWQHIF-DTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAA 139
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 61556948  202 YAASKLALRGFFDVLRtelFDYP--GITLSMICPGPV 236
Cdd:PRK06550 140 YTASKHALAGFTKQLA---LDYAkdGIQVFGIAPGAV 173
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
47-244 2.54e-15

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 74.38  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQE-LERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVL 125
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEeANDVAEEIKKAGG----EAIAVKGDVTVESDVVNLIQTAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK08936  81 KEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIkGNIINMSSVHEQIPWPLFVHYAA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 61556948  205 SKLALRGFFDVLRTElFDYPGITLSMICPGPVHSNIfqNA 244
Cdd:PRK08936 161 SKGGVKLMTETLAME-YAPKGIRVNNIGPGAINTPI--NA 197
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
47-245 2.72e-15

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: 74.03  E-value: 2.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLG--VCLV-LSARRGQELERvkrrclengNLKEKDILVLPLDLADTSSHDIATKT 123
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGarVVIAdIDDDAGQAVAA---------ELGDPDISFVHCDVTVEADVRAAVDT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 124 VLQEFGRIDILVNNGGV--AHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:cd05326  73 AVARFGRLDIMFNNAGVlgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHA 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 61556948 202 YAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAF 245
Cdd:cd05326 153 YTASKHAVLGLTRSAATELGEH-GIRVNCVSPYGVATPLLTAGF 195
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
50-282 3.88e-15

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: 74.04  E-value: 3.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSAR---RGQELERVKRRCLENGnlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd09807   2 KTVIITGANTGIGKETARELARRGARVIMACRdmaKCEEAAAEIRRDTLNH-----EVIVRHLDLASLKSIRAFAAEFLA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHA--SLVEntnmDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLV---GIVP------ 195
Cdd:cd09807  77 EEDRLDVLINNAGVMRCpySKTE----DGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAhkaGKINfddlns 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 196 -RPLCSG--YAASKLAlrgffDVLRT-EL---FDYPGITLSMICPGPVHSNIFQN-AFTGDFTETRLPKI--PLFKMETS 265
Cdd:cd09807 153 eKSYNTGfaYCQSKLA-----NVLFTrELarrLQGTGVTVNALHPGVVRTELGRHtGIHHLFLSTLLNPLfwPFVKTPRE 227
                       250
                ....*....|....*..
gi 61556948 266 RCVQLILVSLANDLEDI 282
Cdd:cd09807 228 GAQTSIYLALAEELEGV 244
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
47-209 4.12e-15

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: 73.64  E-value: 4.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELErvkrRCLENGNLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05329   4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELD----ECLTEWREKGFKVEGSVCDVSSRSERQELMDTVAS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EF-GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:cd05329  80 HFgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGAT 159

                ....
gi 61556948 206 KLAL 209
Cdd:cd05329 160 KGAL 163
PRK06194 PRK06194
hypothetical protein; Provisional
47-242 4.16e-15

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 74.28  E-value: 4.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQG----AEVLGVRTDVSDAAQVEALADAALE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLV-ENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERN------QGKIVVMKSLVGIVPRPLC 199
Cdd:PRK06194  80 RFGAVHLLFNNAGVGAGGLVwENSLAD-WEWVLGVNLWGVIHGVRAFTPLMLAAAekdpayEGHIVNTASMAGLLAPPAM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 61556948  200 SGYAASKLALRGFFDVLRTELFDYPG-ITLSMICPGPVHSNIFQ 242
Cdd:PRK06194 159 GIYNVSKHAVVSLTETLYQDLSLVTDqVGASVLCPYFVPTGIWQ 202
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
50-247 5.51e-15

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: 72.87  E-value: 5.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGNLkekdiLVLPLDLADTSSHDIAtktvLQEF- 128
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAE-LGAENV-----VAGALDVTDRAAWAAA----LADFa 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 ----GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:cd08931  71 aatgGRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSA 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 61556948 205 SKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAFTG 247
Cdd:cd08931 151 TKFAVRGLTEALDVEWARH-GIRVADVWPWFVDTPILTKGETG 192
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
47-287 5.86e-15

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 73.34  E-value: 5.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVkrrcLENGNLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHV----VDEIQQLGGQAFACRCDITSEQELSALADFALS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVEnTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK06113  85 KLGKVDILVNNAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  207 LALRgffDVLRTELFDY--PGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPLFKMETSRCV---QLILVSLANdled 281
Cdd:PRK06113 164 AAAS---HLVRNMAFDLgeKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIanaALFLCSPAA---- 236

                 ....*.
gi 61556948  282 IWIANQ 287
Cdd:PRK06113 237 SWVSGQ 242
PLN02780 PLN02780
ketoreductase/ oxidoreductase
54-219 7.60e-15

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 73.75  E-value: 7.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLEN-GNLKEKDILVlplDLADTSSHDIATKTVLQEFGRID 132
Cdd:PLN02780  58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKySKTQIKTVVV---DFSGDIDEGVKRIKETIEGLDVG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  133 ILVNNGGVAH--ASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIV--PRPLCSGYAASKLA 208
Cdd:PLN02780 135 VLINNVGVSYpyARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVipSDPLYAVYAATKAY 214
                        170
                 ....*....|.
gi 61556948  209 LRGFFDVLRTE 219
Cdd:PLN02780 215 IDQFSRCLYVE 225
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
51-220 7.71e-15

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 72.80  E-value: 7.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  51 VVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVkrrCLENGNLKEKDILVLPLDLADTSSHDIATKTVLQEFGR 130
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAL---LVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 131 IDILVNN-GGVAHASLVENTNmDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLAL 209
Cdd:cd05373  78 LEVLVYNaGANVWFPILETTP-RVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFAL 156
                       170
                ....*....|.
gi 61556948 210 RGFFDVLRTEL 220
Cdd:cd05373 157 RALAQSMAREL 167
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
50-236 1.37e-14

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 72.45  E-value: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGG----KAIAVKADVSDRDQVFAAVRQVVDTFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:PRK08643  79 DLNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHgGKIINATSQAGVVGNPELAVYSSTKFA 158
                        170       180
                 ....*....|....*....|....*...
gi 61556948  209 LRGFFDVLRTELFDyPGITLSMICPGPV 236
Cdd:PRK08643 159 VRGLTQTAARDLAS-EGITVNAYAPGIV 185
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-240 1.48e-14

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 72.12  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQElervkrrclENGNLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---------EAKELREKGVFTIKCDVGNRDQVKKSKEVVEK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGI-VPRPLCSGYAAS 205
Cdd:PRK06463  76 EFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAIT 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 61556948  206 KLALRGFFDVLRTELFDYpGITLSMICPGPVHSNI 240
Cdd:PRK06463 156 KAGIIILTRRLAFELGKY-GIRVNAVAPGWVETDM 189
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
52-262 1.62e-14

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: 70.62  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  52 VWITGASSGIGEELAFQLSKLGVCLVLsarrgqelervkrrclengnlkekdiLVLpldladtsshdiatktvlqefgRI 131
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGSPKVL--------------------------VVS----------------------RR 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 132 DILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALRG 211
Cdd:cd02266  33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDG 112
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 61556948 212 FFDVLRTELFDYpGITLSMICPGPVHsnifqnaftGDFTEtRLPKIPLFKM 262
Cdd:cd02266 113 LAQQWASEGWGN-GLPATAVACGTWA---------GSGMA-KGPVAPEEIL 152
PRK06198 PRK06198
short chain dehydrogenase; Provisional
47-211 2.05e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 71.96  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGV-CLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVL 125
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAELEALG----AKAVFVQADLSDVEDCRRVVAAAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGGV-AHASLVEnTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERN-QGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:PRK06198  80 EAFGRLDALVNAAGLtDRGTILD-TSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMSAHGGQPFLAAYC 158

                 ....*...
gi 61556948  204 ASKLALRG 211
Cdd:PRK06198 159 ASKGALAT 166
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
47-212 5.72e-14

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 70.81  E-value: 5.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSArrgqelervkrrcLENGNLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNAD-------------IHGGDGQHENYQFVPTDVSSAEEVNHTVAEIIE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHAS-LVENTNMD--------IFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRP 197
Cdd:PRK06171  74 KFGRIDGLVNNAGINIPRlLVDEKDPAgkyelneaAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGSE 153
                        170
                 ....*....|....*
gi 61556948  198 LCSGYAASKLALRGF 212
Cdd:PRK06171 154 GQSCYAATKAALNSF 168
PRK08265 PRK08265
short chain dehydrogenase; Provisional
45-210 5.88e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 70.42  E-value: 5.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLEngnlkekDILVLPLDLADTSSHDIATKTV 124
Cdd:PRK08265   2 IGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGE-------RARFIATDITDDAAIERAVATV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGgvahASLVEN----TNMDIFKVLiEVNYLGTVSLTKCVLPHmMERNQGKIVVMKSL---VGIVPRP 197
Cdd:PRK08265  75 VARFGRVDILVNLA----CTYLDDglasSRADWLAAL-DVNLVSAAMLAQAAHPH-LARGGGAIVNFTSIsakFAQTGRW 148
                        170
                 ....*....|...
gi 61556948  198 LcsgYAASKLALR 210
Cdd:PRK08265 149 L---YPASKAAIR 158
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
49-234 1.16e-13

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: 69.62  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLG--VCLV-LSARRGQELERVKRRClengnlkekdILVlPLDLADTSSHDIATKTVL 125
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGakVVILdLPNSPGETVAKLGDNC----------RFV-PVDVTSEKDVKAALALAK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 126 QEFGRIDILVNNGGVAHASLVENTN------MDIFKVLIEVNYLGTVSLTKCVLPHMM--ERNQGK----IVVMKSLVGI 193
Cdd:cd05371  71 AKFGRLDIVVNCAGIAVAAKTYNKKgqqphsLELFQRVINVNLIGTFNVIRLAAGAMGknEPDQGGergvIINTASVAAF 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 61556948 194 VPRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:cd05371 151 EGQIGQAAYSASKGGIVGMTLPIARDLAPQ-GIRVVTIAPG 190
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
45-234 1.18e-13

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: 69.79  E-value: 1.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTV 124
Cdd:cd08935   1 FSLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALG----GRAIALAADVLDRASLERAREEI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 125 LQEFGRIDILVNNGGVAH-------ASLVENTNMDIFKVLIE-------VNYLGTVSLTKCVLPHMMERNQGKIVVMKSL 190
Cdd:cd08935  77 VAQFGTVDILINGAGGNHpdattdpEHYEPETEQNFFDLDEEgwefvfdLNLNGSFLPSQVFGKDMLEQKGGSIINISSM 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 61556948 191 VGIVPRPLCSGYAASKLALRGFFDVLRTElFDYPGITLSMICPG 234
Cdd:cd08935 157 NAFSPLTKVPAYSAAKAAVSNFTQWLAVE-FATTGVRVNAIAPG 199
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
47-278 1.29e-13

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 69.27  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVL-----SARRGQELERVKRRCLengnlkekDILVLPLDLADTSSHDIAT 121
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnSPRRVKWLEDQKALGF--------DFIASEGNVGDWDSTKAAF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  122 KTVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:PRK12938  73 DKVKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTN 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61556948  202 YAASKLALRGFFDVLRTELFDyPGITLSMICPGPVHSNIFQnAFTGDFTETRLPKIPLFKMETSRCVQLILVSLAND 278
Cdd:PRK12938 153 YSTAKAGIHGFTMSLAQEVAT-KGVTVNTVSPGYIGTDMVK-AIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASE 227
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-209 1.51e-13

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 69.22  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRG-QELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDdEELAATQQELRALG----VEVIFFPADVADLSAHEAMLDAAQAAW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVA---HASLVENTNmDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ------GKIVVMKSLVGIVPRPLC 199
Cdd:PRK12745  79 GRIDCLVNNAGVGvkvRGDLLDLTP-ESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNR 157
                        170
                 ....*....|
gi 61556948  200 SGYAASKLAL 209
Cdd:PRK12745 158 GEYCISKAGL 167
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
50-234 2.48e-13

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: 68.64  E-value: 2.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQE-LERVKRrclengNLKEKDILVlPLDLADTSSHDIATKTVLQEF 128
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTEsAEAVAA------EAGERAIAI-QADVRDRDQVQAMIEEAKNHF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 129 GRIDILVNN--GGVAHASLVENTNMDI----FKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:cd05349  74 GPVDTIVNNalIDFPFDPDQRKTFDTIdwedYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDY 153
                       170       180       190
                ....*....|....*....|....*....|..
gi 61556948 203 AASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:cd05349 154 TTAKAALLGFTRNMAKELGPY-GITVNMVSGG 184
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
47-236 2.84e-13

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: 68.41  E-value: 2.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRgqeLERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADIN---LEAARATAAEIG----PAACAISLDVTDQASIDRCVAALVD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:cd05363  74 RWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRgGKIINMASQAGRRGEALVGVYCAT 153
                       170       180       190
                ....*....|....*....|....*....|.
gi 61556948 206 KLALRGFFDVLRTELFDYpGITLSMICPGPV 236
Cdd:cd05363 154 KAAVISLTQSAGLNLIRH-GINVNAIAPGVV 183
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
50-234 5.02e-13

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: 67.73  E-value: 5.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948    50 KVVWITGASSGIGEELAFQLSKLGVCLVLSAR------------RGQELERVKRRClengnlkEKDILVLPLDLADTSSH 117
Cdd:TIGR04504   2 RVALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpavgyplaTRAELDAVAAAC-------PDQVLPVIADVRDPAAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   118 DIATKTVLQEFGRIDILVNNGGV--AHASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERNQ---GKIVVMKSLVG 192
Cdd:TIGR04504  75 AAAVALAVERWGRLDAAVAAAGViaGGRPLWETTDAE-LDLLLDVNLRGVWNLARAAVPAMLARPDprgGRFVAVASAAA 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 61556948   193 IVPRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:TIGR04504 154 TRGLPHLAAYCAAKHAVVGLVRGLAADLGGT-GVTANAVSPG 194
PRK07035 PRK07035
SDR family oxidoreductase;
47-209 6.16e-13

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 67.35  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEkdilVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAE----ALACHIGEMEQIDALFAHIRE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGV----AHaslVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:PRK07035  82 RHGRLDILVNNAAAnpyfGH---ILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIY 158

                 ....*..
gi 61556948  203 AASKLAL 209
Cdd:PRK07035 159 SITKAAV 165
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
51-245 8.38e-13

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: 67.13  E-value: 8.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  51 VVWITGASSGIGEELAfqlsklgvclVLSARRGQELERVkrrclengNLKEKDILVlplDLADTSSHDIATKTVL-QEFG 129
Cdd:cd05328   1 TIVITGAASGIGAATA----------ELLEDAGHTVIGI--------DLREADVIA---DLSTPEGRAAAIADVLaRCSG 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVAHASLVENTnmdifkvlIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPR------------- 196
Cdd:cd05328  60 VLDGLVNCAGVGGTTVAGLV--------LKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAqdklelakalaag 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61556948 197 --------------PLCSGYAASKLAL-RGFFDVLRTELFDYpGITLSMICPGPVHSNIFQNAF 245
Cdd:cd05328 132 tearavalaehagqPGYLAYAGSKEALtVWTRRRAATWLYGA-GVRVNTVAPGPVETPILQAFL 194
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
54-240 9.28e-13

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: 67.10  E-value: 9.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  54 ITGASSGIGEELAFQLSKLGVCLVLSARRG--------QELERVKRRCLengnlkekdilVLPLDLADTSSHDIATKTVL 125
Cdd:cd05337   6 VTGASRGIGRAIATELAARGFDIAINDLPDddqatevvAEVLAAGRRAI-----------YFQADIGELSDHEALLDQAW 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 126 QEFGRIDILVNNGGVA---HASLVENTNmDIFKVLIEVNYLGTVSLTKCVL------PHMMERNQGKIVVMKSLVGIVPR 196
Cdd:cd05337  75 EDFGRLDCLVNNAGIAvrpRGDLLDLTE-DSFDRLIAINLRGPFFLTQAVArrmveqPDRFDGPHRSIIFVTSINAYLVS 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 61556948 197 PLCSGYAASKLALRGFFDVLRTELFDyPGITLSMICPGPVHSNI 240
Cdd:cd05337 154 PNRGEYCISKAGLSMATRLLAYRLAD-EGIAVHEIRPGLIHTDM 196
PRK08278 PRK08278
SDR family oxidoreductase;
47-207 1.09e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 67.24  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQ-------ELERVKRRCLENGNlkekDILVLPLDLADTSSHDI 119
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEphpklpgTIHTAAEEIEAAGG----QALPLVGDVRDEDQVAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  120 ATKTVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLC 199
Cdd:PRK08278  80 AVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSPPLNLDPKWFA 159
                        170
                 ....*....|
gi 61556948  200 --SGYAASKL 207
Cdd:PRK08278 160 phTAYTMAKY 169
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
47-239 1.34e-12

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 66.67  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLS-ARRG-------QELERVKRRClengnlkekdiLVLPLDLADTSSHD 118
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRkaaeetaEEIEALGRKA-----------LAVKANVGDVEKIK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  119 IATKTVLQEFGRIDILVNNGgvahASLVENTNMDI----FKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIV 194
Cdd:PRK08063  71 EMFAQIDEEFGRLDVFVNNA----ASGVLRPAMELeeshWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIR 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 61556948  195 PRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSN 239
Cdd:PRK08063 147 YLENYTTVGVSKAALEALTRYLAVELAPK-GIAVNAVSGGAVDTD 190
PRK06484 PRK06484
short chain dehydrogenase; Validated
45-234 1.40e-12

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 67.95  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKrrclenGNLKEKDiLVLPLDLADTSSHDIATKTV 124
Cdd:PRK06484 265 LAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLA------EALGDEH-LSVQADITDEAAVESAFAQI 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVAH--ASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGY 202
Cdd:PRK06484 338 QARWGRLDVLVNNAGIAEvfKPSLEQSAED-FTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAY 414
                        170       180       190
                 ....*....|....*....|....*....|..
gi 61556948  203 AASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK06484 415 CASKAAVTMLSRSLACEWAPA-GIRVNTVAPG 445
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
47-187 1.53e-12

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: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRG--------------QELERVKRRCLEngnlkekdilvLPLDLA 112
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAephpklpgtiytaaEEIEAAGGKALP-----------CIVDIR 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61556948 113 DTSSHDIATKTVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVM 187
Cdd:cd09762  70 DEDQVRAAVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNL 144
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
50-209 1.71e-12

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: 66.26  E-value: 1.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVkRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKV-AEAAQGGP----RALGVQCDVTSEAQVQSAFEQAVLEFG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGK---IVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd08943  77 GLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIM--KSQGIggnIVFNASKNAVAPGPNAAAYSAAK 154

                ...
gi 61556948 207 LAL 209
Cdd:cd08943 155 AAE 157
PRK07677 PRK07677
short chain dehydrogenase; Provisional
50-236 1.90e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 66.24  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENgnlkEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQF----PGQVLTVQMDVRNPEDVQKMVEQIDEKFG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSL------VGIVPRplcsgy 202
Cdd:PRK07677  78 RIDALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIkGNIINMVATyawdagPGVIHS------ 151
                        170       180       190
                 ....*....|....*....|....*....|....
gi 61556948  203 AASKLALRGFFDVLRTELFDYPGITLSMICPGPV 236
Cdd:PRK07677 152 AAAKAGVLAMTRTLAVEWGRKYGIRVNAIAPGPI 185
PRK06523 PRK06523
short chain dehydrogenase; Provisional
47-236 1.96e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 66.08  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRgqelervkrrclENGNLKEkDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06523   7 LAGKRALVTGGTKGIGAATVARLLEAGARVVTTARS------------RPDDLPE-GVEFVAADLTTAEGCAAVARAVLE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLventnmDIFKVLIE--------VNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPL 198
Cdd:PRK06523  74 RLGGVDILVHVLGGSSAPA------GGFAALTDeewqdelnLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPE 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 61556948  199 CS-GYAASKLALRGFFDVLRTELfdYP-GITLSMICPGPV 236
Cdd:PRK06523 148 STtAYAAAKAALSTYSKSLSKEV--APkGVRVNTVSPGWI 185
PRK09242 PRK09242
SDR family oxidoreductase;
47-209 2.66e-12

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 65.92  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLEngNLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAE--EFPEREVHGLAADVSDDEDRRAILDWVED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK09242  85 HWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTK 164

                 ...
gi 61556948  207 LAL 209
Cdd:PRK09242 165 AAL 167
PRK07062 PRK07062
SDR family oxidoreductase;
47-238 4.82e-12

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 65.06  E-value: 4.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENgnLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREK--FPGARLLAARCDVLDEADVAAFAAAVEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK07062  84 RFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAAR 163
                        170       180       190
                 ....*....|....*....|....*....|..
gi 61556948  207 LALRGFFDVLRTELFDYpGITLSMICPGPVHS 238
Cdd:PRK07062 164 AGLLNLVKSLATELAPK-GVRVNSILLGLVES 194
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
47-238 5.06e-12

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: 64.81  E-value: 5.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkekDILVLPLDLadtsSHDIATKTVLQ 126
Cdd:cd08942   4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG-----ECIAIPADL----SSEEGIEALVA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFG----RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPhMMER-----NQGKIVVMKSLVGIVPRP 197
Cdd:cd08942  75 RVAersdRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLP-LLRAaataeNPARVINIGSIAGIVVSG 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 61556948 198 LCS-GYAASKLALRGFFDVLRTELFDyPGITLSMICPGPVHS 238
Cdd:cd08942 154 LENySYGASKAAVHQLTRKLAKELAG-EHITVNAIAPGRFPS 194
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
50-236 6.45e-12

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: 64.22  E-value: 6.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRG--------QELERVKRRCLengnlkekdilVLPLDLADTSSHDIAT 121
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSeaeaqrlkDELNALRNSAV-----------LVQADLSDFAACADLV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 122 KTVLQEFGRIDILVNNGGVAHA-SLVENTN---MDIFKVLIEVNYLgtvsLTKCVLPHMMERNQGKIVVMksLVGIVPRP 197
Cdd:cd05357  70 AAAFRAFGRCDVLVNNASAFYPtPLGQGSEdawAELFGINLKAPYL----LIQAFARRLAGSRNGSIINI--IDAMTDRP 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 61556948 198 LC--SGYAASKLALRGFFDVLRTELfdYPGITLSMICPGPV 236
Cdd:cd05357 144 LTgyFAYCMSKAALEGLTRSAALEL--APNIRVNGIAPGLI 182
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
48-206 7.09e-12

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 64.58  E-value: 7.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   48 ADKVVWITGASSGIGEELAFQLSKLGVCLVLsARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQE 127
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVL-VDRSELVHEVAAELRAAGG----EALALTADLETYAGAQAAMAAAVEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  128 FGRIDILVNN-GGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLV--GI--VPrplcsgY 202
Cdd:PRK12823  82 FGRIDVLINNvGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIAtrGInrVP------Y 155

                 ....
gi 61556948  203 AASK 206
Cdd:PRK12823 156 SAAK 159
PRK08267 PRK08267
SDR family oxidoreductase;
50-212 9.03e-12

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 64.19  E-value: 9.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRcLENGNLkekdiLVLPLDLADTSSHDIAtktvLQEF- 128
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAE-LGAGNA-----WTGALDVTDRAAWDAA----LADFa 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 ----GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK08267  72 aatgGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSA 151

                 ....*...
gi 61556948  205 SKLALRGF 212
Cdd:PRK08267 152 TKFAVRGL 159
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
46-234 1.01e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 64.00  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTVL 125
Cdd:PRK08085   6 SLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEG----IKAHAAPFNVTHKQEVEAAIEHIE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGGVA--HAsLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:PRK08085  82 KDIGPIDVLINNAGIQrrHP-FTEFPEQE-WNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYA 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 61556948  204 ASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK08085 160 ASKGAVKMLTRGMCVELARH-NIQVNGIAPG 189
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
43-266 1.03e-11

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 65.24  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   43 PEQALADKVVWITGASSGIGEELAFQLSKLG---VCL-VLSArrGQELERVKRRCleNGNlkekdilVLPLDL-ADTSSH 117
Cdd:PRK08261 204 WDRPLAGKVALVTGAARGIGAAIAEVLARDGahvVCLdVPAA--GEALAAVANRV--GGT-------ALALDItAPDAPA 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  118 DIATKtVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRP 197
Cdd:PRK08261 273 RIAEH-LAERHGGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGIAGNR 351
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  198 LCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGpvhsnifqnaftgdFTETRL-PKIPLFKMETSR 266
Cdd:PRK08261 352 GQTNYAASKAGVIGLVQALAPLLAER-GITINAVAPG--------------FIETQMtAAIPFATREAGR 406
PRK05876 PRK05876
short chain dehydrogenase; Provisional
54-244 1.08e-11

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 64.21  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERvkrrCLENGNLKEKDILVLPLDLADTSSHDIATKTVLQEFGRIDI 133
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQ----AVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  134 LVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVGIVPRPLCSGYAASKLALRGF 212
Cdd:PRK05876  87 VFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTgGHVVFTASFAGLVPNAGLGAYGVAKYGVVGL 166
                        170       180       190
                 ....*....|....*....|....*....|..
gi 61556948  213 FDVLRTELFDyPGITLSMICPGPVHSNIFQNA 244
Cdd:PRK05876 167 AETLAREVTA-DGIGVSVLCPMVVETNLVANS 197
PRK07831 PRK07831
SDR family oxidoreductase;
42-206 1.41e-11

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 63.51  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   42 CPEQALADKVVWITGAS-SGIGEELAFQLSKLGVCLVLS---ARR-GQELERVKrrclenGNLKEKDILVLPLDLADTSS 116
Cdd:PRK07831  10 PGHGLLAGKVVLVTAAAgTGIGSATARRALEEGARVVISdihERRlGETADELA------AELGLGRVEAVVCDVTSEAQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  117 HDIATKTVLQEFGRIDILVNNGGVA-HASLVENTNMDIFKVLiEVNYLGTVSLTKCVLPHMMERNQGKIVV-MKSLVGIV 194
Cdd:PRK07831  84 VDALIDAAVERLGRLDVLVNNAGLGgQTPVVDMTDDEWSRVL-DVTLTGTFRATRAALRYMRARGHGGVIVnNASVLGWR 162
                        170
                 ....*....|..
gi 61556948  195 PRPLCSGYAASK 206
Cdd:PRK07831 163 AQHGQAHYAAAK 174
PLN02253 PLN02253
xanthoxin dehydrogenase
43-240 2.33e-11

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 63.30  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   43 PEQALADKVVWITGASSGIGEELAFQLSKLG--VCLV-LSARRGQELervkRRCLENgnlkEKDILVLPLDLadTSSHDI 119
Cdd:PLN02253  12 PSQRLLGKVALVTGGATGIGESIVRLFHKHGakVCIVdLQDDLGQNV----CDSLGG----EPNVCFFHCDV--TVEDDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  120 --ATKTVLQEFGRIDILVNNGGVAHA--SLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVP 195
Cdd:PLN02253  82 srAVDFTVDKFGTLDIMVNNAGLTGPpcPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 61556948  196 RPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNI 240
Cdd:PLN02253 162 GLGPHAYTGSKHAVLGLTRSVAAELGKH-GIRVNCVSPYAVPTAL 205
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-237 2.73e-11

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 62.67  E-value: 2.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGT----EVRGYAANVTDEEDVEATFAQIAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGG---------VAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMME-RNQGKIVVMKSL-----V 191
Cdd:PRK08217  79 DFGQLNGLINNAGilrdgllvkAKDGKVTSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIEsGSKGVIINISSIaragnM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 61556948  192 GIvprplcSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVH 237
Cdd:PRK08217 159 GQ------TNYSASKAGVAAMTVTWAKELARY-GIRVAAIAPGVIE 197
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
50-281 6.03e-11

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: 61.44  E-value: 6.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLG--VCLV-LSARRGQELERVKRrclengnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEAGdkVVFAdIDEERGADFAEAEG----------PNLFFVHGDVADETLVKFVVYAMLE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMeRNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd09761  72 KLGRIDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELI-KNKGRIINIASTRAFQSEPDSEAYAASK 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61556948 207 LALRGFFDVLRTELfdYPGITLSMICPGPVHSNIFQNAFTGDFTETRLPKIPLFKMETSRCVQLILVSLANDLED 281
Cdd:cd09761 151 GGLVALTHALAMSL--GPDIRVNCISPGWINTTEQQEFTAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAG 223
PRK07856 PRK07856
SDR family oxidoreductase;
47-237 1.16e-10

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 60.72  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRgqELERVKRRCLEngnlkekdilVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR--APETVDGRPAE----------FHAADVRDPDQVAALVDAIVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVM-KSLVGIVPRPLCSGYAAS 205
Cdd:PRK07856  72 RHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGGGSIVNiGSVSGRRPSPGTAAYGAA 151
                        170       180       190
                 ....*....|....*....|....*....|..
gi 61556948  206 KLALRGFFDVLRTELfdYPGITLSMICPGPVH 237
Cdd:PRK07856 152 KAGLLNLTRSLAVEW--APKVRVNAVVVGLVR 181
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
47-234 1.25e-10

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 60.74  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEEL--AF--QLSKLGVcLVLSARRGQELervkRRCLEngnlkeKDILVLPLDLADTSSHDIATK 122
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALveRFlaEGARVAV-LERSAEKLASL----RQRFG------DHVLVVEGDVTSYADNQRAVD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGRIDILVNNGGV--AHASLVENTNMDI---FKVLIEVNYLGTVSLTKCVLPHMMERNqGKIVVMKSLVGIVPR- 196
Cdd:PRK06200  73 QTVDAFGKLDCFVGNAGIwdYNTSLVDIPAETLdtaFDEIFNVNVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPGg 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 61556948  197 --PLcsgYAASKLALRGFFDVLRTELfdYPGITLSMICPG 234
Cdd:PRK06200 152 ggPL---YTASKHAVVGLVRQLAYEL--APKIRVNGVAPG 186
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
50-242 1.42e-10

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: 60.56  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRclENGNLKEKDiLVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd05322   3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADE--INAEYGEKA-YGFGADATNEQSVIALSKGVDEIFK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERN-QGKIVVMKSLVGIVPRPLCSGYAASKLA 208
Cdd:cd05322  80 RVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 61556948 209 LRGFFDVLRTELFDYpGITLSMICPGP-VHSNIFQ 242
Cdd:cd05322 160 GVGLTQSLALDLAEH-GITVNSLMLGNlLKSPMFQ 193
PRK09135 PRK09135
pteridine reductase; Provisional
48-259 1.46e-10

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 60.71  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   48 ADKVVWITGASSGIGEELAFQLSKLGVCLVLSARR-GQELERvkrRCLENGNLKEKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADA---LAAELNALRPGSAAALQADLLDPDALPELVAACVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHmMERNQGKIVvmkSLVGI-VPRPLC--SGYA 203
Cdd:PRK09135  82 AFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQ-LRKQRGAIV---NITDIhAERPLKgyPVYC 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948  204 ASKLALRGFFDVLRTELfdYPGITLSMICPGPvhsNIF---QNAFTGDFTETRLPKIPL 259
Cdd:PRK09135 158 AAKAALEMLTRSLALEL--APEVRVNAVAPGA---ILWpedGNSFDEEARQAILARTPL 211
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
47-234 1.59e-10

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: 60.44  E-value: 1.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVC---LVLSARRGQELERvkrrclENGNlkekDILVLPLDLADTSSHDIATKT 123
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKvavLDRSAEKVAELRA------DFGD----AVVGVEGDVRSLADNERAVAR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 124 VLQEFGRIDILVNNGGV--AHASLVENTNMDI---FKVLIEVNYLGTVSLTKCVLPHMMERNqGKIVVMKSLVGIVPRPL 198
Cdd:cd05348  72 CVERFGKLDCFIGNAGIwdYSTSLVDIPEEKLdeaFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPGGG 150
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 61556948 199 CSGYAASKLALRGFFDVLRTELfdYPGITLSMICPG 234
Cdd:cd05348 151 GPLYTASKHAVVGLVKQLAYEL--APHIRVNGVAPG 184
PRK06197 PRK06197
short chain dehydrogenase; Provisional
50-190 2.51e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 60.42  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARR----GQELERVKRrclengNLKEKDILVLPLDLADTSSHDIATKTVL 125
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNldkgKAAAARITA------ATPGADVTLQELDLTSLASVRAAADALR 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61556948  126 QEFGRIDILVNNGGVAHASlvENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSL 190
Cdd:PRK06197  91 AAYPRIDLLINNAGVMYTP--KQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSG 153
PRK05717 PRK05717
SDR family oxidoreductase;
50-234 6.25e-10

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 58.75  E-value: 6.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkekdiLVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENA-------WFIAMDVADEAQVAAGVAEVLGQFG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGVA--HASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNqGKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:PRK05717  84 RLDALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPDTEAYAASKG 162
                        170       180
                 ....*....|....*....|....*..
gi 61556948  208 ALRGFFDVLRTELfdYPGITLSMICPG 234
Cdd:PRK05717 163 GLLALTHALAISL--GPEIRVNAVSPG 187
PRK12746 PRK12746
SDR family oxidoreductase;
47-253 9.12e-10

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 58.12  E-value: 9.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLS-ARRGQELERVKRRCLENGN---LKEKDILVLP--LDLADTSSHDIA 120
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIESNGGkafLIEADLNSIDgvKKLVEQLKNELQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  121 TKTVLQEfgrIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPhmMERNQGKIVVMKSLVGIVPRPLCS 200
Cdd:PRK12746  84 IRVGTSE---IDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLP--LLRAEGRVINISSAEVRLGFTGSI 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 61556948  201 GYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIfqNAFTGDFTETR 253
Cdd:PRK12746 159 AYGLSKGALNTMTLPLAKHLGER-GITVNTIMPGYTKTDI--NAKLLDDPEIR 208
PRK07985 PRK07985
SDR family oxidoreductase;
47-264 1.06e-09

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 58.47  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLS--ARRGQELERVKRRCLENGnlkeKDILVLPLDLADTSSHDIATKTV 124
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISylPVEEEDAQDVKKIIEECG----RKAVLLPGDLSDEKFARSLVHEA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILVNNGGVAHA-SLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:PRK07985 123 HKALGGLDIMALVAGKQVAiPDIADLTSEQFQKTFAINVFALFWLTQEAIPLL--PKGASIITTSSIQAYQPSPHLLDYA 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61556948  204 ASKLALRGFFDVLRTELFDyPGITLSMICPGPVHSNIfqnAFTGDFTETrlpKIPLFKMET 264
Cdd:PRK07985 201 ATKAAILNYSRGLAKQVAE-KGIRVNIVAPGPIWTAL---QISGGQTQD---KIPQFGQQT 254
PRK06128 PRK06128
SDR family oxidoreductase;
47-236 1.53e-09

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 57.95  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARrgQELERVKRRCLENGNLKEKDILVLPLDLADTS-SHDIATKTVl 125
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYL--PEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAfCRQLVERAV- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 QEFGRIDILVNNGG--VAHASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:PRK06128 130 KELGGLDILVNIAGkqTAVKDIADITTEQ-FDATFKTNVYAMFWLCKAAIPHL--PPGASIINTGSIQSYQPSPTLLDYA 206
                        170       180       190
                 ....*....|....*....|....*....|...
gi 61556948  204 ASKLALRGFFDVLRTELFDyPGITLSMICPGPV 236
Cdd:PRK06128 207 STKAAIVAFTKALAKQVAE-KGIRVNAVAPGPV 238
PRK05867 PRK05867
SDR family oxidoreductase;
47-262 3.89e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 56.58  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGG----KVVPVCCDVSQHQQVTSMLDQVTA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-GKIVVMKSLVG-IVPRP-LCSGYA 203
Cdd:PRK05867  83 ELGGIDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQgGVIINTASMSGhIINVPqQVSHYC 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 61556948  204 ASKLALRGFFDVLRTELFDYPgITLSMICPGPVHSNIFQNafTGDFTETRLPKIPLFKM 262
Cdd:PRK05867 163 ASKAAVIHLTKAMAVELAPHK-IRVNSVSPGYILTELVEP--YTEYQPLWEPKIPLGRL 218
PRK12742 PRK12742
SDR family oxidoreductase;
46-240 7.39e-09

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 55.53  E-value: 7.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   46 ALADKVVWITGASSGIGEELAFQLSKLGVCLVLS-ARRGQELERVKRrclENGNlkekdilvlPLDLADTSSHDIATKTV 124
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTyAGSKDAAERLAQ---ETGA---------TAVQTDSADRDAVIDVV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 lQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVN----YLGTVSLTKcvlpHMmeRNQGKIVVMKSLVG-IVPRPLC 199
Cdd:PRK12742  71 -RKSGALDILVVNAGIAVFGDALELDADDIDRLFKINihapYHASVEAAR----QM--PEGGRIIIIGSVNGdRMPVAGM 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 61556948  200 SGYAASKLALRGFFDVLRTElFDYPGITLSMICPGPVHSNI 240
Cdd:PRK12742 144 AAYAASKSALQGMARGLARD-FGPRGITINVVQPGPIDTDA 183
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
54-219 8.41e-09

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: 55.30  E-value: 8.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948    54 ITGASSGIGEELAFQLSKL----GVCLVLSARRGQELERVKRRCLENGNlkEKDILVLPLDLADTSSHDIATKTVLQ--- 126
Cdd:TIGR01500   5 VTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERS--GLRVVRVSLDLGAEAGLEQLLKALRElpr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   127 --EFGRIDILVNNGGVAHASLVENTNMDiFKVLIEVNYLGTVSL--TKCVLPHMMERNQG---KIVVMKSLVGIVPRPLC 199
Cdd:TIGR01500  83 pkGLQRLLLINNAGTLGDVSKGFVDLSD-STQVQNYWALNLTSMlcLTSSVLKAFKDSPGlnrTVVNISSLCAIQPFKGW 161
                         170       180
                  ....*....|....*....|
gi 61556948   200 SGYAASKLALRGFFDVLRTE 219
Cdd:TIGR01500 162 ALYCAGKAARDMLFQVLALE 181
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
47-234 1.15e-08

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 54.91  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRG-----QELERVKRRclengnlkekdILVLPLDLADTSSHDIAT 121
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEapetqAQVEALGRK-----------FHFITADLIQQKDIDSIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  122 KTVLQEFGRIDILVNNGGVA-HASLVENTNMDIFKVlIEVNYLGTVSLTKCVLPHMMER-NQGKIVVMKSLV----GI-V 194
Cdd:PRK12481  75 SQAVEVMGHIDILINNAGIIrRQDLLEFGNKDWDDV-ININQKTVFFLSQAVAKQFVKQgNGGKIINIASMLsfqgGIrV 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 61556948  195 PrplcsGYAASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK12481 154 P-----SYTASKSAVMGLTRALATELSQY-NINVNAIAPG 187
PRK06123 PRK06123
SDR family oxidoreductase;
48-240 1.45e-08

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 54.78  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   48 ADKVVWITGASSGIGEELAFQLSKLGVCLVLS-ARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLNyLRNRDAAEAVVQAIRRQGG----EALAVAADVADEADVLRLFEAVDR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASL-VENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGK---IVVMKSLVGIVPRPlcsG- 201
Cdd:PRK06123  77 ELGRLDALVNNAGILEAQMrLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRggaIVNVSSMAARLGSP---Ge 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 61556948  202 ---YAASKLALRGFFDVLRTELFDyPGITLSMICPGPVHSNI 240
Cdd:PRK06123 154 yidYAASKGAIDTMTIGLAKEVAA-EGIRVNAVRPGVIYTEI 194
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
47-310 1.84e-08

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: 54.37  E-value: 1.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQ-ELERVKRRCLENGNlkeKDILVlpldLADtSSHDIATKTVL 125
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGG---KCIPV----RCD-HSDDDEVEALF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 126 QEF-----GRIDILVNNGGVAHASLVENTNM-----------DIFKVLIEVNYLGTVSLTkcvlPHMMERNQGKIVVMKS 189
Cdd:cd09763  73 ERVareqqGRLDILVNNAYAAVQLILVGVAKpfweepptiwdDINNVGLRAHYACSVYAA----PLMVKAGKGLIVIISS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 190 LVGI-----VPrplcsgYAASKLAL-RGFFDvLRTELFDYpGITLSMICPGPVHSNIFQNAFTGD--FTETRLPKIplFK 261
Cdd:cd09763 149 TGGLeylfnVA------YGVGKAAIdRMAAD-MAHELKPH-GVAVVSLWPGFVRTELVLEMPEDDegSWHAKERDA--FL 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 61556948 262 M-ETSRCVQLILVSLANDlEDIWIANQPVLLRAYVWQYVPFRDwiLQGRY 310
Cdd:cd09763 219 NgETTEYSGRCVVALAAD-PDLMELSGRVLITGELAREYGFTD--VDGRQ 265
PRK06953 PRK06953
SDR family oxidoreductase;
50-236 2.00e-08

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 53.92  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLEngnlkekdilVLPLDLADTSShdIATKTVLQEFG 129
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGAE----------ALALDVADPAS--VAGLAWKLDGE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVNNGGV--AHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPhMMERNQGKIVVMKSLVGIVPRPLCSG---YAA 204
Cdd:PRK06953  70 ALDAAVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLP-LVEAAGGVLAVLSSRMGSIGDATGTTgwlYRA 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 61556948  205 SKLALRgffDVLRTELFDYPGITLSMICPGPV 236
Cdd:PRK06953 149 SKAALN---DALRAASLQARHATCIALHPGWV 177
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
50-260 2.78e-08

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: 54.32  E-value: 2.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQL-----SKLGVCLVLSARRGQELERVKRRCLENGNLKEKDILVLPLDLADTSSHDIATKTV 124
Cdd:cd08941   2 KVVLVTGANSGLGLAICERLlaeddENPELTLILACRNLQRAEAACRALLASHPDARVVFDYVLVDLSNMVSVFAAAKEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 125 LQEFGRIDILVNNGGV------------------------------AHASLVENTNM---DIFKVLIEVNYLGTVSLTKC 171
Cdd:cd08941  82 KKRYPRLDYLYLNAGImpnpgidwigaikevltnplfavtnptykiQAEGLLSQGDKateDGLGEVFQTNVFGHYYLIRE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 172 VLPHMMERNQ-GKIVVMKSLVGIV-------------PRPlcsgYAASKLALrgffDVLRTEL---FDYPGITLSMICPG 234
Cdd:cd08941 162 LEPLLCRSDGgSQIIWTSSLNASPkyfslediqhlkgPAP----YSSSKYLV----DLLSLALnrkFNKLGVYSYVVHPG 233
                       250       260
                ....*....|....*....|....*.
gi 61556948 235 PVHSNIFQnAFTGDFTETRlpKIPLF 260
Cdd:cd08941 234 ICTTNLTY-GILPPFTWTL--ALPLF 256
PRK07102 PRK07102
SDR family oxidoreductase;
50-236 2.95e-08

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 53.77  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkEKDILVLPLDLADTSSHDiATKTVLQEfg 129
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARG---AVAVSTHELDILDTASHA-AFLDSLPA-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  130 RIDILVnnggVAHASLVE----NTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAAS 205
Cdd:PRK07102  76 LPDIVL----IAVGTLGDqaacEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSA 151
                        170       180       190
                 ....*....|....*....|....*....|.
gi 61556948  206 KLALRGFFDVLRTELFDyPGITLSMICPGPV 236
Cdd:PRK07102 152 KAALTAFLSGLRNRLFK-SGVHVLTVKPGFV 181
PRK08339 PRK08339
short chain dehydrogenase; Provisional
47-239 3.57e-08

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 53.71  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNLKEKDIlvlpldLADTSSHDIATKTV-- 124
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYI------VADLTKREDLERTVke 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 LQEFGRIDILV-NNGGVAHASLVENTnMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYA 203
Cdd:PRK08339  80 LKNIGEPDIFFfSTGGPKPGYFMEMS-MEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSN 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 61556948  204 ASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSN 239
Cdd:PRK08339 159 VVRISMAGLVRTLAKELGPK-GITVNGIMPGIIRTD 193
PRK05854 PRK05854
SDR family oxidoreductase;
47-174 3.81e-08

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 53.92  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSAR---RGQE-LERVKRRclengnLKEKDILVLPLDLADTSSHDIATK 122
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRnraKGEAaVAAIRTA------VPDAKLSLRALDLSSLASVAALGE 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 61556948  123 TVLQEfGR-IDILVNNGGVAHASLVENTnMDIFKVLIEVNYLGTVSLTKCVLP 174
Cdd:PRK05854  86 QLRAE-GRpIHLLINNAGVMTPPERQTT-ADGFELQFGTNHLGHFALTAHLLP 136
PRK07069 PRK07069
short chain dehydrogenase; Validated
54-210 3.81e-08

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 53.56  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   54 ITGASSGIGEELAFQLSKLGVCLVLS-ARRGQELERVKRRCleNGNLKEKDILVLPLDLADTSSHDIATKTVLQEFGRID 132
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTdINDAAGLDAFAAEI--NAAHGEGVAFAAVQDVTDEAQWQALLAQAADAMGGLS 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61556948  133 ILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPLCSGYAASKLALR 210
Cdd:PRK07069  82 VLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVA 159
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
50-258 3.88e-08

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 53.54  E-value: 3.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGAS--SGIGEELAFQLSKLGVCLVLS-----------ARRGQELERVKRRCLENGNLKEKdilvLPLDLADTSS 116
Cdd:PRK12748   6 KIALVTGASrlNGIGAAVCRRLAAKGIDIFFTywspydktmpwGMHDKEPVLLKEEIESYGVRCEH----MEIDLSQPYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  117 HDIATKTVLQEFGRIDILVNNGGVA-HASLVENT--NMDIFKVlieVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGI 193
Cdd:PRK12748  82 PNRVFYAVSERLGDPSILINNAAYStHTRLEELTaeQLDKHYA---VNVRATMLLSSAFAKQYDGKAGGRIINLTSGQSL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61556948  194 VPRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIfqnaFTGDFTETRLPKIP 258
Cdd:PRK12748 159 GPMPDELAYAATKGAIEAFTKSLAPELAEK-GITVNAVNPGPTDTGW----ITEELKHHLVPKFP 218
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
56-247 5.20e-08

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: 52.20  E-value: 5.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  56 GASSGIGEELAFQLSKLGvCLVLSARRGQElervkrrclengnlkekDILVlplDLADTSShdiaTKTVLQEFGRIDILV 135
Cdd:cd11731   5 GATGTIGLAVAQLLSAHG-HEVITAGRSSG-----------------DYQV---DITDEAS----IKALFEKVGHFDAIV 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 136 NNGGVAH-ASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGYAASKLALRGFFD 214
Cdd:cd11731  60 STAGDAEfAPLAELTDAD-FQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVR 136
                       170       180       190
                ....*....|....*....|....*....|....*
gi 61556948 215 VLRTELFDypGITLSMICPGPVHSNI--FQNAFTG 247
Cdd:cd11731 137 AAAIELPR--GIRINAVSPGVVEESLeaYGDFFPG 169
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
47-239 5.20e-08

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 52.95  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGvCLVLSARRGQELERVKRRCLENgnlkeKDILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAG-CDIVGINIVEPTETIEQVTALG-----RRFLSLTADLRKIDGIPALLERAVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMER-NQGKIVVMKSLV----GI-VPrplcs 200
Cdd:PRK08993  82 EFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLsfqgGIrVP----- 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 61556948  201 GYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSN 239
Cdd:PRK08993 157 SYTASKSGVMGVTRLMANEWAKH-NINVNAIAPGYMATN 194
PRK12747 PRK12747
short chain dehydrogenase; Provisional
47-240 7.21e-08

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 52.77  E-value: 7.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLS-ARRGQELERVKRRCLENG--------NLKEkdiLVLPLDLADTSSH 117
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHyGNRKEEAEETVYEIQSNGgsafsigaNLES---LHGVEALYSSLDN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  118 DIATKTVLQEFgriDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRP 197
Cdd:PRK12747  79 ELQNRTGSTKF---DILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLP 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 61556948  198 LCSGYAASKLALRGFFDVLRTELfDYPGITLSMICPGPVHSNI 240
Cdd:PRK12747 154 DFIAYSMTKGAINTMTFTLAKQL-GARGITVNAILPGFIKTDM 195
PRK06196 PRK06196
oxidoreductase; Provisional
47-190 7.32e-08

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 53.15  E-value: 7.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRrclengNLKEKDilVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALA------GIDGVE--VVMLDLADLESVRAFAERFLD 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61556948  127 EFGRIDILVNNGGVahASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSL 190
Cdd:PRK06196  96 SGRRIDILINNAGV--MACPETRVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSA 157
PRK06947 PRK06947
SDR family oxidoreductase;
50-164 1.58e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 51.73  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARR--------GQELERV-KRRCLENGNL-KEKDILVLpldladtssHDI 119
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINYARdaaaaeetADAVRAAgGRACVVAGDVaNEADVIAM---------FDA 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 61556948  120 ATktvlQEFGRIDILVNNGG-VAHASLVENTNMDIFKVLIEVNYLG 164
Cdd:PRK06947  74 VQ----SAFGRLDALVNNAGiVAPSMPLADMDAARLRRMFDTNVLG 115
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
50-240 1.74e-07

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 51.61  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVcLVLSARRGQELERVKRRCLENGNLKEkdilvLPLDLADTSSHDIATKTVL---- 125
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGT-HVISISRTENKELTKLAEQYNSNLTF-----HSLDLQDVHELETNFNEILssiq 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  126 -QEFGRIdILVNNGG-VAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVV-MKSLVGIVPRPLCSGY 202
Cdd:PRK06924  76 eDNVSSI-HLINNAGmVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVDKRVInISSGAAKNPYFGWSAY 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 61556948  203 AASKLALRGFFDVLRTELFD--YPGITLSmICPGPVHSNI 240
Cdd:PRK06924 155 CSSKAGLDMFTQTVATEQEEeeYPVKIVA-FSPGVMDTNM 193
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
54-247 2.66e-07

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: 51.06  E-value: 2.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  54 ITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCL-ENGNlkeKDILVLPLDLADTSSHDIATKTVLQEFGRID 132
Cdd:cd09808   6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIEtESGN---QNIFLHIVDMSDPKQVWEFVEEFKEEGKKLH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 133 ILVNNGG--VAHASLVEntnmDIFKVLIEVNYLGTVSLTKCVLPhMMERNQGKIVVMKSLVGIVPRPLCSGYAASKlalR 210
Cdd:cd09808  83 VLINNAGcmVNKRELTE----DGLEKNFATNTLGTYILTTHLIP-VLEKEEDPRVITVSSGGMLVQKLNTNNLQSE---R 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 61556948 211 GFFD------------VLRTELF--DYPGITLSMICPGPVHSNIFQNAFTG 247
Cdd:cd09808 155 TAFDgtmvyaqnkrqqVIMTEQWakKHPEIHFSVMHPGWADTPAVRNSMPD 205
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
50-212 3.44e-07

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: 50.98  E-value: 3.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELAFQLSKLGVCLVLSARRgqELERVKRRCLENGnLKEKDILVLPLDLADTSSHDIATKTVLQEFG 129
Cdd:cd09810   2 GTVVITGASSGLGLAAAKALARRGEWHVVMACR--DFLKAEQAAQEVG-MPKDSYSVLHCDLASLDSVRQFVDNFRRTGR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 130 RIDILVNNGGVAHASLVENT-NMDIFKVLIEVNYLGTVSLTKCVLPHM--MERNQGKIVVMKSLVG--------IVPRPL 198
Cdd:cd09810  79 PLDALVCNAAVYLPTAKEPRfTADGFELTVGVNHLGHFLLTNLLLEDLqrSENASPRIVIVGSITHnpntlagnVPPRAT 158
                       170
                ....*....|....
gi 61556948 199 CSgyaasklALRGF 212
Cdd:cd09810 159 LG-------DLEGL 165
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-234 4.73e-07

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 50.09  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVL----SARRGQELERvkrrclengNLKEKDIlVLPLDLADTSSHDIATK 122
Cdd:PRK08642   3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVnyhqSEDAAEALAD---------ELGDRAI-ALQADVTDREQVQAMFA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  123 TVLQEFGR-IDILVNNG-------GVAHASLVENTNMDiFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIV-VMKSLVG- 192
Cdd:PRK08642  73 TATEHFGKpITTVVNNAladfsfdGDARKKADDITWED-FQQQLEGSVKGALNTIQAALPGMREQGFGRIInIGTNLFQn 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 61556948  193 -IVPRplcSGYAASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK08642 152 pVVPY---HDYTTAKAALLGLTRNLAAELGPY-GITVNMVSGG 190
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-287 4.91e-07

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 50.17  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGAS--SGIGEELAFQLSKLGVCLVL------------------SARRGQELERVKRRClenGNLKekdilv 106
Cdd:PRK12859   4 LKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFtywtaydkempwgvdqdeQIQLQEELLKNGVKV---SSME------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  107 lpLDLADTSSHDIATKTVLQEFGRIDILVNNGgvAHAslvenTNMDiFKVLIE--------VNYLGTVSLTkCVLPHMME 178
Cdd:PRK12859  75 --LDLTQNDAPKELLNKVTEQLGYPHILVNNA--AYS-----TNND-FSNLTAeeldkhymVNVRATTLLS-SQFARGFD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  179 RNQG-KIVVMKSLVGIVPRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSnifqNAFTGDFTETRLPKI 257
Cdd:PRK12859 144 KKSGgRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHL-GITVNAINPGPTDT----GWMTEEIKQGLLPMF 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 61556948  258 PLFKMETSRCVQLILVSLANDlEDIWIANQ 287
Cdd:PRK12859 219 PFGRIGEPKDAARLIKFLASE-EAEWITGQ 247
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-233 1.37e-06

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 49.01  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLS--ARRGQELERVKrrclENGNLKEKDILVLPlDLADTSSHDIATKTV 124
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVNdvASALDASDVLD----EIRAAGAKAVAVAG-DISQRATADELVATA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  125 lQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQ-------GKIVVMKS---LVGIV 194
Cdd:PRK07792  85 -VGLGGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRAKAKaaggpvyGRIVNTSSeagLVGPV 163
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 61556948  195 PRPlcsGYAASKLALRGFFDVLRTELFDYpGITLSMICP 233
Cdd:PRK07792 164 GQA---NYGAAKAGITALTLSAARALGRY-GVRANAICP 198
PRK08177 PRK08177
SDR family oxidoreductase;
50-236 1.45e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 48.49  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSklgvclvlsaRRGQELERVKRRCLENGNLKEKDIL-VLPLDLADTSSHDiATKTVLQEf 128
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLL----------ERGWQVTATVRGPQQDTALQALPGVhIEKLDMNDPASLD-QLLQRLQG- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGV---AHASLVENTNMDIFKvLIEVNYLGTVSLTKCVLPHmMERNQGKIVVMKSLVGIVPRPLCSG---Y 202
Cdd:PRK08177  70 QRFDLLFVNAGIsgpAHQSAADATAAEIGQ-LFLTNAIAPIRLARRLLGQ-VRPGQGVLAFMSSQLGSVELPDGGEmplY 147
                        170       180       190
                 ....*....|....*....|....*....|....
gi 61556948  203 AASKLALRGFFDVLRTELFDYPGITLSMiCPGPV 236
Cdd:PRK08177 148 KASKAALNSMTRSFVAELGEPTLTVLSM-HPGWV 180
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
49-148 1.87e-06

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: 48.92  E-value: 1.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVC-LVLSARRGQELERVKR-RCLENGNLkekDILVLPLDLADTSshdiATKTVLQ 126
Cdd:cd05274 150 DGTYLITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARaALLRAGGA---RVSVVRCDVTDPA----ALAALLA 222
                        90       100
                ....*....|....*....|....*
gi 61556948 127 EFGR---IDILVNNGGVAHASLVEN 148
Cdd:cd05274 223 ELAAggpLAGVIHAAGVLRDALLAE 247
PRK07791 PRK07791
short chain dehydrogenase; Provisional
39-233 2.34e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 48.13  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   39 MGQCpeqalADKVVWITGASSGIGEE--LAFQ-------LSKLGVCLVLSARRGQELERVKRRCLENGNLkekdilvlpl 109
Cdd:PRK07791   1 MGLL-----DGRVVIVTGAGGGIGRAhaLAFAaegarvvVNDIGVGLDGSASGGSAAQAVVDEIVAAGGE---------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  110 dlADTSSHDIAT--------KTVLQEFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVsltkCVLPHMME--R 179
Cdd:PRK07791  66 --AVANGDDIADwdgaanlvDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHF----ATLRHAAAywR 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61556948  180 NQGK--------IVVMKSLVGIVPRPLCSGYAASKLALRGFFDVLRTELFDYpGITLSMICP 233
Cdd:PRK07791 140 AESKagravdarIINTSSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRY-GVTVNAIAP 200
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
48-212 2.55e-06

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 48.52  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  48 ADKVVWITGASSGIGEELAFQLSKLGVC-LVLSARRGQELERVK-----RRCLENGnlkeKDILVLPLDLADTSSHDIAT 121
Cdd:cd08953 204 PGGVYLVTGGAGGIGRALARALARRYGArLVLLGRSPLPPEEEWkaqtlAALEALG----ARVLYISADVTDAAAVRRLL 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 122 KTVLQEFGRIDILVNNGGV-AHASLVENTNMDIFKVLiEVNYLGTVSLTKCVlphmMERNQGKIVVMKSLVGIVPRPLCS 200
Cdd:cd08953 280 EKVRERYGAIDGVIHAAGVlRDALLAQKTAEDFEAVL-APKVDGLLNLAQAL----ADEPLDFFVLFSSVSAFFGGAGQA 354
                       170
                ....*....|..
gi 61556948 201 GYAASKLALRGF 212
Cdd:cd08953 355 DYAAANAFLDAF 366
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
43-209 4.00e-06

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 48.37  E-value: 4.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  43 PEQALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVkrrcleNGNLKEKDILVLPLDLADTSSHDIATK 122
Cdd:COG3347 419 KPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAA------AAELGGGYGADAVDATDVDVTAEAAVA 492
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 123 TVLQ----EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPL 198
Cdd:COG3347 493 AAFGfaglDIGGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVSKNAAAAAY 572
                       170
                ....*....|.
gi 61556948 199 cSGYAASKLAL 209
Cdd:COG3347 573 -GAAAAATAKA 582
PRK06101 PRK06101
SDR family oxidoreductase;
51-297 1.84e-05

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 45.25  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   51 VVWITGASSGIGEELAFQLSKLGVcLVLSARRGQELervkrrcLENGNLKEKDILVLPLDLADTSShdiaTKTVLQEFGR 130
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGW-QVIACGRNQSV-------LDELHTQSANIFTLAFDVTDHPG----TKAALSQLPF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  131 I-DILVNNGGvaHASLVENTNMD--IFKVLIEVNYLGTVSLTKCVLPHmMERNQgKIVVMKSLVGIVPRPLCSGYAASKL 207
Cdd:PRK06101  71 IpELWIFNAG--DCEYMDDGKVDatLMARVFNVNVLGVANCIEGIQPH-LSCGH-RVVIVGSIASELALPRAEAYGASKA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  208 ALRGFFDVLRTELfDYPGITLSMICPGpvhsnifqnaftgdFTETRLPKIPLFKM----ETSRCVQLILVSLANDLEDIW 283
Cdd:PRK06101 147 AVAYFARTLQLDL-RPKGIEVVTVFPG--------------FVATPLTDKNTFAMpmiiTVEQASQEIRAQLARGKSHIY 211
                        250       260
                 ....*....|....*....|
gi 61556948  284 I-ANQPVLLR-----AYVWQ 297
Cdd:PRK06101 212 FpARFTWLIRllgllPYAWQ 231
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
50-204 2.05e-05

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: 44.40  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948     50 KVVWITGASSGIGEELAFQLSKLGVC-LVLSARRGQELERVKRRCLENGNLKEkDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARrLVLLSRSGPDAPGAAALLAELEAAGA-RVTVVACDVADRDALAAVLAAIPAVE 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61556948    129 GRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERnqgkIVVMKSLVGIVPRPLCSGYAA 204
Cdd:smart00822  80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLPLDF----FVLFSSIAGVLGSPGQANYAA 151
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
120-241 2.20e-05

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 44.87  E-value: 2.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 120 ATKTVLQEFGRIDILVNNGGVAHA-SLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKSLVGIVPRPL 198
Cdd:cd05361  62 LVDAVLQAGGAIDVLVSNDYIPRPmNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAY 141
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 61556948 199 CSGYAASKLALRGFFDVLRTELFDYpGITLSMICPGPVHSNIF 241
Cdd:cd05361 142 NSLYGPARAAAVALAESLAKELSRD-NILVYAIGPNFFNSPTY 183
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-234 2.31e-05

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 44.75  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekdILVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGN-----IHYVVGDVSSTESARNVIEKAAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENtnmdiFKVLIEV--NYLGT-VSLTKCVLPHMMErnqGKIVVMKSLVGIV----PRPLc 199
Cdd:PRK05786  78 VLNAIDGLVVTVGGYVEDTVEE-----FSGLEEMltNHIKIpLYAVNASLRFLKE---GSSIVLVSSMSGIykasPDQL- 148
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 61556948  200 sGYAASKLALRGFFDVLRTELFDYpGITLSMICPG 234
Cdd:PRK05786 149 -SYAVAKAGLAKAVEILASELLGR-GIRVNGIAPT 181
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
50-234 3.09e-05

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: 44.24  E-value: 3.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  50 KVVWITGASSGIGEELA--FQLSKLGVCLVLSArrgqelervkrrclENGNLKEkDILVLPLDLADTSShDIATKTVLQE 127
Cdd:cd05334   2 RVVLVYGGRGALGSAVVqaFKSRGWWVASIDLA--------------ENEEADA-SIIVLDSDSFTEQA-KQVVASVARL 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948 128 FGRIDILVN-NGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMmeRNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:cd05334  66 SGKVDALICvAGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHL--LSGGLLVLTGAKAALEPTPGMIGYGAAK 143
                       170       180
                ....*....|....*....|....*....
gi 61556948 207 LALRGFFDVLRTELFDYP-GITLSMICPG 234
Cdd:cd05334 144 AAVHQLTQSLAAENSGLPaGSTANAILPV 172
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
110-192 3.76e-05

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 44.22  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  110 DLADTSSHDIAtktVLQEFGRIDILVNNGGV---AHASLVentnmdifkvlIEVNYLGTVSLTKCVLPHMmeRNQGKIVV 186
Cdd:PRK12428  31 DLGDPASIDAA---VAALPGRIDALFNIAGVpgtAPVELV-----------ARVNFLGLRHLTEALLPRM--APGGAIVN 94

                 ....*.
gi 61556948  187 MKSLVG 192
Cdd:PRK12428  95 VASLAG 100
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
52-178 4.16e-05

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 44.60  E-value: 4.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  52 VWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLEngnlKEKDILVLPLDLADTSShdiaTKTVLQEFGR- 130
Cdd:COG5748   9 VIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQELGI----PPDSYTIIHIDLASLES----VRRFVADFRAl 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 61556948 131 ---IDILVNNGGVAHASLVE-NTNMDIFKVLIEVNYLGTVSLTKCVLPHMME 178
Cdd:COG5748  81 grpLDALVCNAAVYYPLLKEpLRSPDGYELSVATNHLGHFLLCNLLLEDLKK 132
PRK07806 PRK07806
SDR family oxidoreductase;
45-263 4.58e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 43.94  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   45 QALADKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQE-LERVKRRCLENGNlkeKDILVlPLDLADTSSHDIATKT 123
Cdd:PRK07806   2 GDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPrANKVVAEIEAAGG---RASAV-GADLTDEESVAALMDT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  124 VLQEFGRIDILV-NNGGVAHASLVENTNMdifkvliEVNYLGTVSLTKCVLPHMMErnQGKIVVMKS----LVGIVPR-P 197
Cdd:PRK07806  78 AREEFGGLDALVlNASGGMESGMDEDYAM-------RLNRDAQRNLARAALPLMPA--GSRVVFVTShqahFIPTVKTmP 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61556948  198 LCSGYAASKlalRGFFDVLRTEL--FDYPGITL-----SMIcPGPVHSNIFQNAFTGDFTETRLPKIPLFKME 263
Cdd:PRK07806 149 EYEPVARSK---RAGEDALRALRpeLAEKGIGFvvvsgDMI-EGTVTATLLNRLNPGAIEARREAAGKLYTVS 217
PRK05599 PRK05599
SDR family oxidoreductase;
52-235 6.14e-05

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 43.72  E-value: 6.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   52 VWITGASSGIGEELAFQLSKlGVCLVLSARRGQELERVKRRCLENGnlkEKDILVLPLDLADTSSHDIATKTVLQEFGRI 131
Cdd:PRK05599   3 ILILGGTSDIAGEIATLLCH-GEDVVLAARRPEAAQGLASDLRQRG---ATSVHVLSFDAQDLDTHRELVKQTQELAGEI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  132 DILVNNGGV----AHASLVENTNMDIfkvlIEVNYLGTVS-LTkcVLPHMMERN--QGKIVVMKSLVGIVPRPLCSGYAA 204
Cdd:PRK05599  79 SLAVVAFGIlgdqERAETDEAHAVEI----ATVDYTAQVSmLT--VLADELRAQtaPAAIVAFSSIAGWRARRANYVYGS 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 61556948  205 SKLALRGFFDVLRTELFdypGITLSMICPGP 235
Cdd:PRK05599 153 TKAGLDAFCQGLADSLH---GSHVRLIIARP 180
PRK07576 PRK07576
short chain dehydrogenase; Provisional
47-236 6.44e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 43.79  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   47 LADKVVWITGASSGIGEELAFQLSKLGvCLVLSARRGQELERVKRRCLENGNLKEkdiLVLPLDLADTSSHDIATKTVLQ 126
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAG-ANVAVASRSQEKVDAAVAQLQQAGPEG---LGVSADVRDYAAVEAAFAQIAD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  127 EFGRIDILVNNGGVAHASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHmMERNQGKIVVMKSLVGIVPRPLCSGYAASK 206
Cdd:PRK07576  83 EFGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPL-LRRPGASIIQISAPQAFVPMPMQAHVCAAK 161
                        170       180       190
                 ....*....|....*....|....*....|
gi 61556948  207 LALRGFFDVLRTElFDYPGITLSMICPGPV 236
Cdd:PRK07576 162 AGVDMLTRTLALE-WGPEGIRVNSIVPGPI 190
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
49-189 7.42e-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: 43.74  E-value: 7.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  49 DKVVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkEKDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWH--KARVEAMTLDLASLRSVQRFAEAFKAKN 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61556948 129 GRIDILVNNGGVahASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGKIVVMKS 189
Cdd:cd09809  79 SPLHVLVCNAAV--FALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSS 137
PRK09730 PRK09730
SDR family oxidoreductase;
50-240 1.64e-04

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 42.53  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   50 KVVWITGASSGIGEELAFQLSKLGVCLVLS-ARRGQELERVKRRCLENGNlkekDILVLPLDLADTSSHDIATKTVLQEF 128
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNyQQNLHAAQEVVNLITQAGG----KAFVLQADISDENQVVAMFTAIDQHD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  129 GRIDILVNNGGVA-HASLVENTNMDIFKVLIEVNYLGTVSLTKCVLPHMMERNQGK---IVVMKSLVGIVPRPlcsG--- 201
Cdd:PRK09730  78 EPLAALVNNAGILfTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASRLGAP---Geyv 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 61556948  202 -YAASKlalrGFFDVLRTEL---FDYPGITLSMICPGPVHSNI 240
Cdd:PRK09730 155 dYAASK----GAIDTLTTGLsleVAAQGIRVNCVRPGFIYTEM 193
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
52-174 3.37e-04

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: 41.71  E-value: 3.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948  52 VWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekdilVLPLDLADTS-SHDIATKtvLQEFGR 130
Cdd:cd08951  10 IFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAG-------VLIGDLSSLAeTRKLADQ--VNAIGR 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 61556948 131 IDILVNNGGVAHASLVENTNMDIFKVLiEVNYLGTVSLTKCVLP 174
Cdd:cd08951  81 FDAVIHNAGILSGPNRKTPDTGIPAMV-AVNVLAPYVLTALIRR 123
PRK08862 PRK08862
SDR family oxidoreductase;
51-154 2.24e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 38.94  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   51 VVWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGNlkekdiLVLPLDLADTSSHDIAT--KTVLQEF 128
Cdd:PRK08862   7 IILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTD------NVYSFQLKDFSQESIRHlfDAIEQQF 80
                         90       100
                 ....*....|....*....|....*...
gi 61556948  129 GR-IDILVNN-GGVAHASLVENTNMDIF 154
Cdd:PRK08862  81 NRaPDVLVNNwTSSPLPSLFDEQPSESF 108
PRK08340 PRK08340
SDR family oxidoreductase;
52-197 3.18e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 38.63  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   52 VWITGASSGIGEELAFQLSKLGVCLVLSARRGQELERVKRRCLENGnlkekDILVLPLDLADTSSHDIATKTVLQEFGRI 131
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-----EVYAVKADLSDKDDLKNLVKEAWELLGGI 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61556948  132 DILVNNGGVAHAS---LVENTNMDifkvLIEVNYLGTVS---LTKCVLPHMMERN-QGKIVVMKSLVGIVPRP 197
Cdd:PRK08340  78 DALVWNAGNVRCEpcmLHEAGYSD----WLEAALLHLVApgyLTTLLIQAWLEKKmKGVLVYLSSVSVKEPMP 146
PLN00015 PLN00015
protochlorophyllide reductase
54-164 6.42e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 37.76  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   54 ITGASSGIGEELAFQLSKLGVCLVLSARRgqELERVKRRCLENGnLKEKDILVLPLDLADTSShdiaTKTVLQEFGR--- 130
Cdd:PLN00015   2 ITGASSGLGLATAKALAETGKWHVVMACR--DFLKAERAAKSAG-MPKDSYTVMHLDLASLDS----VRQFVDNFRRsgr 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 61556948  131 -IDILVNNGGVAHASLVENT-NMDIFKVLIEVNYLG 164
Cdd:PLN00015  75 pLDVLVCNAAVYLPTAKEPTfTADGFELSVGTNHLG 110
PRK07023 PRK07023
SDR family oxidoreductase;
54-142 6.65e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 37.30  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   54 ITGASSGIGEELAFQLSKLGVCLV-LSARRGQELERVKRRCLENGNlkekdilvlpLDLADTSS-HDIATKTVLQEFGR- 130
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVLgVARSRHPSLAAAAGERLAEVE----------LDLSDAAAaAAWLAGDLLAAFVDg 75
                         90
                 ....*....|....
gi 61556948  131 --IDILVNNGGVAH 142
Cdd:PRK07023  76 asRVLLINNAGTVE 89
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
51-204 7.24e-03

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 36.77  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948    51 VVWITGASSGIGEELAFQLSKLGV-CLVLSARRGQELERVKRRCLEngnLKEK--DILVLPLDLADTSSHDIATKTVLQE 127
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGArHLVLLSRSAAPRPDAQALIAE---LEARgvEVVVVACDVSDPDAVAALLAEIKAE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556948   128 FGRIdilvnnGGVAHA------SLVENTNMDIFKVLIEVNYLGTVSLTKCVLPhmmeRNQGKIVVMKSLVGIVPRPLCSG 201
Cdd:pfam08659  79 GPPI------RGVIHAagvlrdALLENMTDEDWRRVLAPKVTGTWNLHEATPD----EPLDFFVLFSSIAGLLGSPGQAN 148

                  ...
gi 61556948   202 YAA 204
Cdd:pfam08659 149 YAA 151
 
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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