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Conserved domains on  [gi|19922066|ref|NP_610724|]
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uncharacterized protein Dmel_CG8888 [Drosophila melanogaster]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
96-380 1.65e-139

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd09805:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 281  Bit Score: 398.57  E-value: 1.65e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPieESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLphGA 175
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTK--NGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 176 EGLWSVVHCAHWIALGEL-EWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAA 254
Cdd:cd09805  77 KGLWGLVNNAGILGFGGDeELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 255 VDCFAACLRQEMRTRGVDVSVVAAGEFAPGNGWLNETELRdQAKQMWNQLSSEQKKTYGEDYYEAAMTSVEKY-SRQAAD 333
Cdd:cd09805 157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYcSRASPD 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 19922066 334 IQPTLRVLIDAVTRTFPMARYTPVTSSERLQIFlAEHLAPSLYESLY 380
Cdd:cd09805 236 LSPVIDSIEHALTSRHPRTRYYPGKDAKLLYIP-ASYLPTSLSDFLL 281
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
96-380 1.65e-139

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: 398.57  E-value: 1.65e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPieESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLphGA 175
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTK--NGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 176 EGLWSVVHCAHWIALGEL-EWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAA 254
Cdd:cd09805  77 KGLWGLVNNAGILGFGGDeELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 255 VDCFAACLRQEMRTRGVDVSVVAAGEFAPGNGWLNETELRdQAKQMWNQLSSEQKKTYGEDYYEAAMTSVEKY-SRQAAD 333
Cdd:cd09805 157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYcSRASPD 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 19922066 334 IQPTLRVLIDAVTRTFPMARYTPVTSSERLQIFlAEHLAPSLYESLY 380
Cdd:cd09805 236 LSPVIDSIEHALTSRHPRTRYYPGKDAKLLYIP-ASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
92-279 5.89e-22

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 93.78  E-value: 5.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  92 SASGKGVLITGCEAPLAWYLAKKLDDLGFTVYA-GFNTpiEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQH 170
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLvARDA--ERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 171 LPHgAEGLwsvVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQC 249
Cdd:COG0300  80 FGP-IDVL---VNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGMAAYA 155
                       170       180       190
                ....*....|....*....|....*....|
gi 19922066 250 ATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:COG0300 156 ASKAALEGFSESLRAELAPTGVRVTAVCPG 185
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
96-293 1.00e-19

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 86.13  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066    96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAgfnTPIEESDEAKILKEV--TSGRMKLLHLDVTSEKTILEAARYVSQHLPh 173
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVL---VDRSEEKLEAVAKELgaLGGKALFIQGDVTDRAQVKALVEQAVERLG- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   174 gaeGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQ 252
Cdd:pfam00106  77 ---RLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSAYSASK 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 19922066   253 AAVDCFAACLRQEMRTRGVDVSVVAAGEFAPGNGW-LNETEL 293
Cdd:pfam00106 154 AAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKeLREDEG 195
PRK06182 PRK06182
short chain dehydrogenase; Validated
96-279 3.64e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 75.00  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAGfntpieeSDEAKILKEVTSGRMKLLHLDVTSEKTILEAaryVSQHLphGA 175
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGA-------ARRVDKMEDLASLGVHPLSLDVTDEASIKAA---VDTII--AE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  176 EGLWSV-VHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAH-GRVVFLTSGLNRVPSPVRGIQCATQA 253
Cdd:PRK06182  72 EGRIDVlVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLGAWYHATKF 151
                        170       180
                 ....*....|....*....|....*.
gi 19922066  254 AVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK06182 152 ALEGFSDALRLEVAPFGIDVVVIEPG 177
 
Name Accession Description Interval E-value
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
96-380 1.65e-139

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: 398.57  E-value: 1.65e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPieESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLphGA 175
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTK--NGPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHV--GE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 176 EGLWSVVHCAHWIALGEL-EWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAA 254
Cdd:cd09805  77 KGLWGLVNNAGILGFGGDeELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 255 VDCFAACLRQEMRTRGVDVSVVAAGEFAPGNGWLNETELRdQAKQMWNQLSSEQKKTYGEDYYEAAMTSVEKY-SRQAAD 333
Cdd:cd09805 157 VEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEK-QAKKLWERLPPEVKKDYGEDYIDELKNKMLKYcSRASPD 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 19922066 334 IQPTLRVLIDAVTRTFPMARYTPVTSSERLQIFlAEHLAPSLYESLY 380
Cdd:cd09805 236 LSPVIDSIEHALTSRHPRTRYYPGKDAKLLYIP-ASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
98-354 1.77e-34

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: 127.73  E-value: 1.77e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  98 VLITGCEAPLAWYLAKKLDDLGFTVYAGFNTP--IEESDEAKilkevtSGRMKLLHLDVTSEKTILEAARYVSQHlpHGa 175
Cdd:cd05374   3 VLITGCSSGIGLALALALAAQGYRVIATARNPdkLESLGELL------NDNLEVLELDVTDEESIKAAVKEVIER--FG- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 176 eGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAA 254
Cdd:cd05374  74 -RIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPlMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 255 VDCFAACLRQEMRTRGVDVSVVAAGEFApgngwlneTELRDqakqmwNQLSSEQKKTYGEDYY---EAAMTSVEKYSRQA 331
Cdd:cd05374 153 LEALSESLRLELAPFGIKVTIIEPGPVR--------TGFAD------NAAGSALEDPEISPYAperKEIKENAAGVGSNP 218
                       250       260
                ....*....|....*....|...
gi 19922066 332 ADIQPTLRVLIDAVTRTFPMARY 354
Cdd:cd05374 219 GDPEKVADVIVKALTSESPPLRY 241
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
92-279 5.89e-22

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 93.78  E-value: 5.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  92 SASGKGVLITGCEAPLAWYLAKKLDDLGFTVYA-GFNTpiEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQH 170
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLvARDA--ERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 171 LPHgAEGLwsvVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQC 249
Cdd:COG0300  80 FGP-IDVL---VNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPlMRARGRGRIVNVSSVAGLRGLPGMAAYA 155
                       170       180       190
                ....*....|....*....|....*....|
gi 19922066 250 ATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:COG0300 156 ASKAALEGFSESLRAELAPTGVRVTAVCPG 185
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
92-346 2.53e-20

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: 89.09  E-value: 2.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  92 SASGKGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPieesDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHL 171
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRA----ERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 172 PHgaegLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCA 250
Cdd:COG4221  78 GR----LDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPaMRARGSGHIVNISSIAGLRPYPGGAVYAA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 251 TQAAVDCFAACLRQEMRTRGVDVSVVaagefAPGNGwlnETElrdqakqMWNQLSSEQKKTYGEDYYEAAMTSVEkysrQ 330
Cdd:COG4221 154 TKAAVRGLSESLRAELRPTGIRVTVI-----EPGAV---DTE-------FLDSVFDGDAEAAAAVYEGLEPLTPE----D 214
                       250       260
                ....*....|....*....|..
gi 19922066 331 AADI------QPtLRVLIDAVT 346
Cdd:COG4221 215 VAEAvlfaltQP-AHVNVNELV 235
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
96-293 1.00e-19

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 86.13  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066    96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAgfnTPIEESDEAKILKEV--TSGRMKLLHLDVTSEKTILEAARYVSQHLPh 173
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVL---VDRSEEKLEAVAKELgaLGGKALFIQGDVTDRAQVKALVEQAVERLG- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   174 gaeGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQ 252
Cdd:pfam00106  77 ---RLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPaMIKGSGGRIVNISSVAGLVPYPGGSAYSASK 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 19922066   253 AAVDCFAACLRQEMRTRGVDVSVVAAGEFAPGNGW-LNETEL 293
Cdd:pfam00106 154 AAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKeLREDEG 195
PRK06182 PRK06182
short chain dehydrogenase; Validated
96-279 3.64e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 75.00  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAGfntpieeSDEAKILKEVTSGRMKLLHLDVTSEKTILEAaryVSQHLphGA 175
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGA-------ARRVDKMEDLASLGVHPLSLDVTDEASIKAA---VDTII--AE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  176 EGLWSV-VHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAH-GRVVFLTSGLNRVPSPVRGIQCATQA 253
Cdd:PRK06182  72 EGRIDVlVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPLGAWYHATKF 151
                        170       180
                 ....*....|....*....|....*.
gi 19922066  254 AVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK06182 152 ALEGFSDALRLEVAPFGIDVVVIEPG 177
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
98-279 1.98e-14

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: 71.93  E-value: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  98 VLITGC-----EAplawyLAKKLDDLGFTVY-AGFNtpiEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHL 171
Cdd:cd05233   1 ALVTGAssgigRA-----IARRLAREGAKVVlADRN---EEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 172 PHgaegLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCA 250
Cdd:cd05233  73 GR----LDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPhMKKQGGGRIVNISSVAGLRPLPGQAAYAA 148
                       170       180
                ....*....|....*....|....*....
gi 19922066 251 TQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:cd05233 149 SKAALEGLTRSLALELAPYGIRVNAVAPG 177
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
94-273 2.60e-14

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: 72.12  E-value: 2.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  94 SGKGVLITGCEAPLAWYLAKKLDDLGFTVY-AGfntpieeSDEAKiLKEVTSGR--MKLLHLDVTSEKTILEAARYVSQH 170
Cdd:COG3967   4 TGNTILITGGTSGIGLALAKRLHARGNTVIiTG-------RREEK-LEEAAAANpgLHTIVLDVADPASIAALAEQVTAE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 171 LPHgaegLWSVVHCA---HWIALGELEWiPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRG 246
Cdd:COG3967  76 FPD----LNVLINNAgimRAEDLLDEAE-DLADAEREITTNLLGPIRLTAAFLPhLKAQPEAAIVNVSSGLAFVPLAVTP 150
                       170       180
                ....*....|....*....|....*..
gi 19922066 247 IQCATQAAVDCFAACLRQEMRTRGVDV 273
Cdd:COG3967 151 TYSATKAALHSYTQSLRHQLKDTSVKV 177
PRK06914 PRK06914
SDR family oxidoreductase;
94-379 5.60e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 71.59  E-value: 5.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITgceapLAwyLAKKlddlGFTVYAGFNTPieesDEAKILKEVT-----SGRMKLLHLDVTSEKTILEAARYVS 168
Cdd:PRK06914  13 SGFGLLTT-----LE--LAKK----GYLVIATMRNP----EKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  169 QHLPhgaegLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAH-GRVVFLTSGLNRVPSPVRGI 247
Cdd:PRK06914  78 EIGR-----IDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGLSP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  248 QCATQAAVDCFAACLRQEMRTRGVDVSVVAAGEFapgngwlnETELRDQAKQMWNQLSSEQKKTYgeDYYEAAMTSVEKY 327
Cdd:PRK06914 153 YVSSKYALEGFSESLRLELKPFGIDVALIEPGSY--------NTNIWEVGKQLAENQSETTSPYK--EYMKKIQKHINSG 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19922066  328 SRQAADIQPTLRVLIDAVTRTFPMARYtPVTSSERLQIFLAEHLAPSLYESL 379
Cdd:PRK06914 223 SDTFGNPIDVANLIVEIAESKRPKLRY-PIGKGVKLMILAKKILPWRLWEYL 273
PRK05993 PRK05993
SDR family oxidoreductase;
96-367 8.09e-14

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 71.21  E-value: 8.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAgfnTPIEESDeakiLKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLPHGA 175
Cdd:PRK05993   5 RSILITGCSSGIGAYCARALQSDGWRVFA---TCRKEED----VAALEAEGLEAFQLDYAEPESIAALVAQVLELSGGRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  176 EGLWSvvHCAHWIAlGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVR-RAHGRVVFLTSGLNRVPSPVRGIQCATQAA 254
Cdd:PRK05993  78 DALFN--NGAYGQP-GAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRkQGQGRIVQCSSILGLVPMKYRGAYNASKFA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  255 VDCFAACLRQEMRTRGVDVSVVAAGEFapgngwlnETELRDQAKQMWNQLSSEQKKTYGEDyYEAAMTSVEKYSRQAADI 334
Cdd:PRK05993 155 IEGLSLTLRMELQGSGIHVSLIEPGPI--------ETRFRANALAAFKRWIDIENSVHRAA-YQQQMARLEGGGSKSRFK 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 19922066  335 QP---TLRVLIDAVTRTFPMARYtPVTSSERLQIFL 367
Cdd:PRK05993 226 LGpeaVYAVLLHALTAPRPRPHY-RVTTPAKQGALL 260
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
94-279 1.13e-13

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: 70.20  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  94 SGKGVLITGC-----EAplawyLAKKLDDLGFTVYAgfnTPIEESDEAKILKEVTS--GRMKLLHLDVTSEKTILEAARY 166
Cdd:COG1028   5 KGKVALVTGGssgigRA-----IARALAAEGARVVI---TDRDAEALEAAAAELRAagGRALAVAADVTDEAAVEALVAA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 167 VSQHLPhgaeGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVR 245
Cdd:COG1028  77 AVAAFG----RLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPhMRERGGGRIVNISSIAGLRGSPGQ 152
                       170       180       190
                ....*....|....*....|....*....|....
gi 19922066 246 GIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:COG1028 153 AAYAASKAAVVGLTRSLALELAPRGIRVNAVAPG 186
PRK09291 PRK09291
SDR family oxidoreductase;
95-291 1.45e-13

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 70.03  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   95 GKGVLITGCEAPLAWYLAKKLDDLGFTVYAGfntpieesdeAKILKEVTSGR---------MKLLHLDVTSEKTILEAAR 165
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAG----------VQIAPQVTALRaeaarrglaLRVEKLDLTDAIDRAQAAE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  166 YVSQHLPHGA---EGlwsvvhcahwialGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTS--GLNR 239
Cdd:PRK09291  72 WDVDVLLNNAgigEA-------------GAVVDIPVELVRELFETNVFGPLELTQGFVRkMVARGKGKVVFTSSmaGLIT 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19922066  240 VPSpvRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAGEFAPGngwLNET 291
Cdd:PRK09291 139 GPF--TGAYCASKHALEAIAEAMHAELKPFGIQVATVNPGPYLTG---FNDT 185
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
96-279 1.66e-13

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: 69.31  E-value: 1.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPiEESDEAKILKevtsGRMKLLHLDVTSEktilEAARYVSQHLPHGA 175
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNP-EDLAALSASG----GDVEAVPYDARDP----EDARALVDALRDRF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 176 EGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAA 254
Cdd:cd08932  72 GRIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPaLREAGSGRVVFLNSLSGKRVLAGNAGYSASKFA 151
                       170       180
                ....*....|....*....|....*
gi 19922066 255 VDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:cd08932 152 LRALAHALRQEGWDHGVRVSAVCPG 176
PRK05693 PRK05693
SDR family oxidoreductase;
98-282 1.86e-13

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 69.82  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   98 VLITGCEAPLAWYLAKKLDDLGFTVYAgfnTPIEESDeakiLKEVTSGRMKLLHLDVTSEktilEAARYVSQHLPHGAEG 177
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA---TARKAED----VEALAAAGFTAVQLDVNDG----AALARLAEELEAEHGG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  178 LWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDC 257
Cdd:PRK05693  73 LDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHA 152
                        170       180
                 ....*....|....*....|....*
gi 19922066  258 FAACLRQEMRTRGVDVSVVAAGEFA 282
Cdd:PRK05693 153 LSDALRLELAPFGVQVMEVQPGAIA 177
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
140-337 2.08e-13

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: 69.49  E-value: 2.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 140 KEVTS--GRMKLLHLDVTSEKTILEAARYVSQHLPHgaegLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQ 217
Cdd:cd08934  45 DELEAegGKALVLELDVTDEQQVDAAVERTVEALGR----LDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTH 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 218 IFLPLVR-RAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAGefapgngwLNETELRDQ 296
Cdd:cd08934 121 AALPHHLlRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEGLRQEVTERGVRVVVIEPG--------TVDTELRDH 192
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 19922066 297 -----AKQMWNQLSSEQKKTYGEDYYEAAMTSVEKYSRQAAD---IQPT 337
Cdd:cd08934 193 ithtiTKEAYEERISTIRKLQAEDIAAAVRYAVTAPHHVTVNeilIRPT 241
PRK08219 PRK08219
SDR family oxidoreductase;
180-279 3.39e-12

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 65.34  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  180 SVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFA 259
Cdd:PRK08219  74 VLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALA 153
                         90       100
                 ....*....|....*....|
gi 19922066  260 ACLRQEMRTRgVDVSVVAAG 279
Cdd:PRK08219 154 DALREEEPGN-VRVTSVHPG 172
PRK08017 PRK08017
SDR family oxidoreductase;
96-279 9.83e-12

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 64.72  E-value: 9.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   96 KGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPieeSDEAkilkevtsgRMKLL-----HLDVTSEKTILEAARYVSQh 170
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKP---DDVA---------RMNSLgftgiLLDLDDPESVERAADEVIA- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  171 LPHGAegLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVrRAHG--RVVFLTSGLNRVPSPVRGIQ 248
Cdd:PRK08017  70 LTDNR--LYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAM-LPHGegRIVMTSSVMGLISTPGRGAY 146
                        170       180       190
                 ....*....|....*....|....*....|.
gi 19922066  249 CATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK08017 147 AASKYALEAWSDALRMELRHSGIKVSLIEPG 177
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
139-276 4.06e-11

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: 62.60  E-value: 4.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 139 LKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLphgaEGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQI 218
Cdd:cd05332  47 CLELGAPSPHVVPLDMSDLEDAEQVVEEALKLF----GGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKA 122
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19922066 219 FLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVV 276
Cdd:cd05332 123 ALPhLIERSQGSIVVVSSIAGKIGVPFRTAYAASKHALQGFFDSLRAELSEPNISVTVV 181
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
181-284 4.52e-11

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: 62.27  E-value: 4.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 181 VVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVR-RAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFA 259
Cdd:cd08939  86 VVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKeQRPGHIVFVSSQAALVGIYGYSAYCPSKFALRGLA 165
                        90       100
                ....*....|....*....|....*.
gi 19922066 260 ACLRQEMRTRGVDVSVVAAGEFA-PG 284
Cdd:cd08939 166 ESLRQELKPYNIRVSVVYPPDTDtPG 191
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
96-279 5.26e-11

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 62.48  E-value: 5.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  96 KGVLITGCEAPLAWYLAKKL---DDLGFTVYAGFNTPIEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLP 172
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLasdPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTERHV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 173 hgaeglwSVVHCAHWIAL-GELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTS--GLNRVpsPVRGIQ 248
Cdd:cd09806  81 -------DVLVCNAGVGLlGPLEALSEDAMASVFDVNVFGTVRMLQAFLPdMKRRGSGRILVTSSvgGLQGL--PFNDVY 151
                       170       180       190
                ....*....|....*....|....*....|.
gi 19922066 249 CATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:cd09806 152 CASKFALEGLCESLAVQLLPFNVHLSLIECG 182
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
94-273 1.49e-10

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: 60.78  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  94 SGKGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPiEESDEAKilKEVtsGRMKLLHLDVTSektileaaryvsqhlPH 173
Cdd:cd05370   4 TGNTVLITGGTSGIGLALARKFLEAGNTVIITGRRE-ERLAEAK--KEL--PNIHTIVLDVGD---------------AE 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 174 GAEGLWSVVHCAH--------------WIALGELEWIPFAVLRKsLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLN 238
Cdd:cd05370  64 SVEALAEALLSEYpnldilinnagiqrPIDLRDPASDLDKADTE-IDTNLIGPIRLIKAFLPhLKKQPEATIVNVSSGLA 142
                       170       180       190
                ....*....|....*....|....*....|....*
gi 19922066 239 RVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDV 273
Cdd:cd05370 143 FVPMAANPVYCATKAALHSYTLALRHQLKDTGVEV 177
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
108-276 4.92e-10

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: 59.15  E-value: 4.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 108 AWYLAKKlddlGFTVYAGFNTPIEESDEAKILKEVTSGRMKLLHLDVTSEKTILEaaryvsqHLPHGAEGLwSV------ 181
Cdd:cd05356  18 AEELAKR----GFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSAGDDIYE-------RIEKELEGL-DIgilvnn 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 182 VHCAHWIALGELEwIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAA 260
Cdd:cd05356  86 VGISHSIPEYFLE-TPEDELQDIINVNVMATLKMTRLILPgMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFSR 164
                       170
                ....*....|....*.
gi 19922066 261 CLRQEMRTRGVDVSVV 276
Cdd:cd05356 165 ALYEEYKSQGIDVQSL 180
PRK06180 PRK06180
short chain dehydrogenase; Provisional
92-281 9.70e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 58.77  E-value: 9.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   92 SASGKGVLITGCEAPLAWYLAKKLDDLGFTVYAgfnTPIEESDeAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHl 171
Cdd:PRK06180   1 MSSMKTWLITGVSSGFGRALAQAALAAGHRVVG---TVRSEAA-RADFEALHPDRALARLLDVTDFDAIDAVVADAEAT- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  172 pHGAegLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVR-RAHGRVVFLTS--GLnrVPSPVRGIQ 248
Cdd:PRK06180  76 -FGP--IDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRaRRRGHIVNITSmgGL--ITMPGIGYY 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 19922066  249 CATQAAVDCFAACLRQEMRTRGVDVSVVAAGEF 281
Cdd:PRK06180 151 CGSKFALEGISESLAKEVAPFGIHVTAVEPGSF 183
PRK06179 PRK06179
short chain dehydrogenase; Provisional
94-276 1.04e-09

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 58.76  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNtpieesdeaKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHlph 173
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSR---------NPARAAPIPGVELLELDVTDDASVQAAVDEVIAR--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  174 gaEGLWSV-VHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAH-GRVVFLTSGLNRVPSPVRGIQCAT 251
Cdd:PRK06179  71 --AGRIDVlVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMALYAAS 148
                        170       180
                 ....*....|....*....|....*
gi 19922066  252 QAAVDCFAACLRQEMRTRGVDVSVV 276
Cdd:PRK06179 149 KHAVEGYSESLDHEVRQFGIRVSLV 173
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
98-284 5.13e-09

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: 56.15  E-value: 5.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  98 VLITGCEAPLAWYLAKKL-DDLGFTVYAGFNTPIEESDEAKILKevTSGRMKLLHLDVTSEKTilEAARYVSQHLphGAE 176
Cdd:cd05325   1 VLITGASRGIGLELVRQLlARGNNTVIATCRDPSAATELAALGA--SHSRLHILELDVTDEIA--ESAEAVAERL--GDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 177 GLWSVVHCA---HwiALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRA-HGRVVFLTSGL----NRVPSPVRGiQ 248
Cdd:cd05325  75 GLDVLINNAgilH--SYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGaRAKIINISSRVgsigDNTSGGWYS-Y 151
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19922066 249 CATQAAVDCFAACLRQEMRTRGvdVSVVAageFAPG 284
Cdd:cd05325 152 RASKAALNMLTKSLAVELKRDG--ITVVS---LHPG 182
PRK07890 PRK07890
short chain dehydrogenase; Provisional
181-323 1.48e-08

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 54.96  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  181 VVHCAHWI-ALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFA 259
Cdd:PRK07890  86 LVNNAFRVpSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYGAYKMAKGALLAAS 165
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922066  260 ACLRQEMRTRGVDVSVVaagefAPGNGWlnetelRDQAKQMWNQLSSEQKKTYGEDYYEAAMTS 323
Cdd:PRK07890 166 QSLATELGPQGIRVNSV-----APGYIW------GDPLKGYFRHQAGKYGVTVEQIYAETAANS 218
PRK07775 PRK07775
SDR family oxidoreductase;
98-303 4.52e-08

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 53.99  E-value: 4.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   98 VLITGCEAPLAWYLAKKLDDLGFTVYAGFNTpIEESDEakILKEVTS--GRMKLLHLDVTSEKTILEA-ARYVSQHLPhg 174
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARR-VEKCEE--LVDKIRAdgGEAVAFPLDVTDPDSVKSFvAQAEEALGE-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  175 aegLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQA 253
Cdd:PRK07775  88 ---IEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPgMIERRRGDLIFVGSDVALRQRPHMGAYGAAKA 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19922066  254 AVDCFAACLRQEMRTRGVDVSVVAAGEFAPGNGWLNETE-----LRDQAKqmWNQ 303
Cdd:PRK07775 165 GLEAMVTNLQMELEGTGVRASIVHPGPTLTGMGWSLPAEvigpmLEDWAK--WGQ 217
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
136-288 6.84e-08

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: 52.62  E-value: 6.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 136 AKILKEVTSGRMklLHLDVTSEKTILEAARYVSQHlpHGaeGLWSVVHCAHWIALGELEWIPF-AVLRKSLDLNLLGSAR 214
Cdd:cd05324  43 EKLRAEGLSVRF--HQLDVTDDASIEAAADFVEEK--YG--GLDILVNNAGIAFKGFDDSTPTrEQARETMKTNFFGTVD 116
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19922066 215 LTQIFLPLVRRA-HGRVVFLTSGLNRVPSPVRgiqcATQAAVDCFAACLRQEMRTRGVDVSVVAAG----EFAPGNGWL 288
Cdd:cd05324 117 VTQALLPLLKKSpAGRIVNVSSGLGSLTSAYG----VSKAALNALTRILAKELKETGIKVNACCPGwvktDMGGGKAPK 191
PRK12826 PRK12826
SDR family oxidoreductase;
94-279 1.01e-07

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 52.61  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITGCEAPLAWYLAKKLDDLGFTVYAgfnTPIEESDEAKILKEVTS--GRMKLLHLDVTSEKTILEAARYVSQHl 171
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIV---VDICGDDAAATAELVEAagGKARARQVDVRDRAALKAAVAAGVED- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  172 pHGaeGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTS--GLnRVPSPVRGIQ 248
Cdd:PRK12826  81 -FG--RLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPaLIRAGGGRIVLTSSvaGP-RVGYPGLAHY 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 19922066  249 CATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK12826 157 AASKAGLVGFTRALALELAARNITVNSVHPG 187
PRK05872 PRK05872
short chain dehydrogenase; Provisional
95-275 1.20e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 52.66  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   95 GKGVLITGCEAPLAWYLAKKLDDLGFTVYAgfnTPIEEsDEAKILKEVTSGRMKLLHL--DVTSEKTILEAARYVSQHLp 172
Cdd:PRK05872   9 GKVVVVTGAARGIGAELARRLHARGAKLAL---VDLEE-AELAALAAELGGDDRVLTVvaDVTDLAAMQAAAEEAVERF- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  173 hgaeGLWSVVHCAHWIALGElewiPFAV-----LRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGI 247
Cdd:PRK05872  84 ----GGIDVVVANAGIASGG----SVAQvdpdaFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMAA 155
                        170       180
                 ....*....|....*....|....*...
gi 19922066  248 QCATQAAVDCFAACLRQEMRTRGVDVSV 275
Cdd:PRK05872 156 YCASKAGVEAFANALRLEVAHHGVTVGS 183
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
205-279 1.51e-07

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 51.84  E-value: 1.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922066  205 LDLNLLGSARLT-QIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK12936 108 LEVNLTATFRLTrELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPG 183
PRK07825 PRK07825
short chain dehydrogenase; Provisional
94-276 2.03e-07

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 51.87  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITGCEAPLAWYLAKKLDDLGFTVYAGfntpieESDEAkiLKEVTSGRMKLLH---LDVTSE---KTILEAARyv 167
Cdd:PRK07825   4 RGKVVAITGGARGIGLATARALAALGARVAIG------DLDEA--LAKETAAELGLVVggpLDVTDPasfAAFLDAVE-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  168 sqhlphGAEGLWSV-VHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVR 245
Cdd:PRK07825  74 ------ADLGPIDVlVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPrMVPRGRGHVVNVASLAGKIPVPGM 147
                        170       180       190
                 ....*....|....*....|....*....|.
gi 19922066  246 GIQCATQAAVDCFAACLRQEMRTRGVDVSVV 276
Cdd:PRK07825 148 ATYCASKHAVVGFTDAARLELRGTGVHVSVV 178
PRK05650 PRK05650
SDR family oxidoreductase;
98-281 8.60e-07

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 50.04  E-value: 8.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   98 VLITGCEAPLAWYLAKKLDDLGFTVYAGfntPIEESDEAKILKEVTS--GRMKLLHLDVTSEKTILEAARYVSQHLphga 175
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALA---DVNEEGGEETLKLLREagGDGFYQRCDVRDYSQLTALAQACEEKW---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  176 EGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRA-HGRVVFLTSGLNRVPSPVRGIQCATQAA 254
Cdd:PRK05650  76 GGIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQkSGRIVNIASMAGLMQGPAMSSYNVAKAG 155
                        170       180
                 ....*....|....*....|....*..
gi 19922066  255 VDCFAACLRQEMRTRGVDVSVVAAGEF 281
Cdd:PRK05650 156 VVALSETLLVELADDEIGVHVVCPSFF 182
PRK06181 PRK06181
SDR family oxidoreductase;
186-279 1.32e-06

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 49.21  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  186 HWIALGELEWIpfAVLRKSLDLNLLGSARLTQIFLPLVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQE 265
Cdd:PRK06181  90 MWSRFDELTDL--SVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALHGFFDSLRIE 167
                         90
                 ....*....|....
gi 19922066  266 MRTRGVDVSVVAAG 279
Cdd:PRK06181 168 LADDGVAVTVVCPG 181
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
108-279 1.64e-06

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: 48.58  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   108 AWYLAKKLDDLGFTVYAgfnTPIEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLPhgaeGLWSVVHCA-- 185
Cdd:pfam13561   9 GWAIARALAEEGAEVVL---TDLNEALAKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEKFG----RLDILVNNAgf 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   186 ---HWIALGELEWipfAVLRKSLDLNLLGSARLTQIFLPLvRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACL 262
Cdd:pfam13561  82 apkLKGPFLDTSR---EDFDRALDVNLYSLFLLAKAALPL-MKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYL 157
                         170
                  ....*....|....*..
gi 19922066   263 RQEMRTRGVDVSVVAAG 279
Cdd:pfam13561 158 AVELGPRGIRVNAISPG 174
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
98-279 2.56e-06

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: 48.12  E-value: 2.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  98 VLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPIEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHLPHgaeg 177
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGR---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 178 LWSVVHCAHWIA---LGELEWipfAVLRKSLDLNLLGSARLTQIFLPLVRRA-HGRVVFLTSGLNRVPSPVRGIQCATQA 253
Cdd:cd05359  77 LDVLVSNAAAGAfrpLSELTP---AHWDAKMNTNLKALVHCAQQAAKLMRERgGGRIVAISSLGSIRALPNYLAVGTAKA 153
                       170       180
                ....*....|....*....|....*.
gi 19922066 254 AVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:cd05359 154 ALEALVRYLAVELGPRGIRVNAVSPG 179
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
206-279 3.96e-06

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: 47.65  E-value: 3.96e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19922066 206 DLNLLGSARLTQIFLPLVRRAhGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:cd05362 110 TVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPG 182
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
98-276 4.69e-06

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: 47.62  E-value: 4.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  98 VLITGCEAPLAWYLAKKLDDLGFT-VYAGFNTP--IEESDEAKIlkevTSGRMKLLHLDVTSEKTILEAARYVSQhlPHG 174
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKvVILDINEKgaEETANNVRK----AGGKVHYYKCDVSKREEVYEAAKKIKK--EVG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 175 AEGLwsVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQA 253
Cdd:cd05339  76 DVTI--LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTIASVAGLISPAGLADYCASKA 153
                       170       180
                ....*....|....*....|....*.
gi 19922066 254 AVDCFAACLRQEMRT---RGVDVSVV 276
Cdd:cd05339 154 AAVGFHESLRLELKAygkPGIKTTLV 179
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
201-284 6.71e-06

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: 46.90  E-value: 6.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 201 LRKSLDLNLLGSARLTQIFLPLV--RRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEmrtrGVDVSVVAa 278
Cdd:cd05367 102 LQKYFDLNLTSPVCLTSTLLRAFkkRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDMFFRVLAAE----EPDVRVLS- 176

                ....*.
gi 19922066 279 geFAPG 284
Cdd:cd05367 177 --YAPG 180
PRK12937 PRK12937
short chain dehydrogenase; Provisional
94-279 8.91e-06

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 46.66  E-value: 8.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITGCEAPLAWYLAKKLDDLGFTV---YAGFNTPIEESDEAKilkEVTSGRMKLLHLDVTSEKTI---LEAARyv 167
Cdd:PRK12937   4 SNKVAIVTGASRGIGAAIARRLAADGFAVavnYAGSAAAADELVAEI---EAAGGRAIAVQADVADAAAVtrlFDAAE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  168 sqhlphGAEGLWSV-VHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAhGRVVFLTSGLNRVPSPVRG 246
Cdd:PRK12937  79 ------TAFGRIDVlVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQG-GRIINLSTSVIALPLPGYG 151
                        170       180       190
                 ....*....|....*....|....*....|...
gi 19922066  247 IQCATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK12937 152 PYAASKAAVEGLVHVLANELRGRGITVNAVAPG 184
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
205-279 9.47e-06

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: 46.50  E-value: 9.47e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922066 205 LDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:cd05346 107 IDTNVKGLLNVTRLILPiMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPG 182
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
94-282 9.50e-06

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: 46.63  E-value: 9.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  94 SGKGVLITGCEAPLAWYLAKKLDDLGFT-VYAGFNTPieesDEAKILKEVTSGRMKLLHLDVTSEKTILEAAryvsqhlp 172
Cdd:cd05354   2 KDKTVLVTGANRGIGKAFVESLLAHGAKkVYAAVRDP----GSAAHLVAKYGDKVVPLRLDVTDPESIKAAA-------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 173 HGAEGLWSVVHCAHWI-ALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAH-GRVVFLTSGLNRVPSPVRGIQCA 250
Cdd:cd05354  70 AQAKDVDVVINNAGVLkPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGgGAIVNLNSVASLKNFPAMGTYSA 149
                       170       180       190
                ....*....|....*....|....*....|..
gi 19922066 251 TQAAVDCFAACLRQEMRTRGVDVSVVAAGEFA 282
Cdd:cd05354 150 SKSAAYSLTQGLRAELAAQGTLVLSVHPGPID 181
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
202-282 1.70e-05

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: 45.73  E-value: 1.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 202 RKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAGE 280
Cdd:cd05344 103 LEAFDLKLLSVIRIVRAVLPgMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGY 182

                ..
gi 19922066 281 FA 282
Cdd:cd05344 183 ID 184
PRK07577 PRK07577
SDR family oxidoreductase;
93-293 1.71e-05

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 45.49  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   93 ASGKGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPIEEsdeakilkevTSGrmKLLHLDVTSEKTILEAARYVSQHLP 172
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIARSAIDD----------FPG--ELFACDLADIEQTAATLAQINEIHP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  173 HGAeglwsVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTS-----GLNRVPspvrg 246
Cdd:PRK07577  69 VDA-----IVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEgMKLREQGRIVNICSraifgALDRTS----- 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 19922066  247 iqcaTQAAVDCFAACLRQ---EMRTRGVDVSVVAAGEFapgngwlnETEL 293
Cdd:PRK07577 139 ----YSAAKSALVGCTRTwalELAEYGITVNAVAPGPI--------ETEL 176
PRK06523 PRK06523
short chain dehydrogenase; Provisional
189-279 2.72e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 45.28  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  189 ALGELEWIpfavlrKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQ-CATQAAVDCFAACLRQEM 266
Cdd:PRK06523  97 ALTDEEWQ------DELNLNLLAAVRLDRALLPgMIARGSGVIIHVTSIQRRLPLPESTTAyAAAKAALSTYSKSLSKEV 170
                         90
                 ....*....|...
gi 19922066  267 RTRGVDVSVVAAG 279
Cdd:PRK06523 171 APKGVRVNTVSPG 183
PRK08264 PRK08264
SDR family oxidoreductase;
95-279 3.44e-05

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 44.88  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   95 GKGVLITGCEAPLAWYLAKKLDDLG-FTVYAGFNTPieESDEAKILKEVTsgrmklLHLDVTSEKTILEAARYVS--QHL 171
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDP--ESVTDLGPRVVP------LQLDVTDPASVAAAAEAASdvTIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  172 PHGAeglwSVVHCAHWIALGelewiPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCA 250
Cdd:PRK08264  78 VNNA----GIFRTGSLLLEG-----DEDALRAEMETNYFGPLAMARAFAPvLAANGGGAIVNVLSVLSWVNFPNLGTYSA 148
                        170       180
                 ....*....|....*....|....*....
gi 19922066  251 TQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK08264 149 SKAAAWSLTQALRAELAPQGTRVLGVHPG 177
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
94-279 4.22e-05

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 44.41  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTPIEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHlpH 173
Cdd:PRK05557   4 EGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAE--F 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  174 GaeGLWSVVHCAHWIALGEL------EWipFAVlrksLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRG 246
Cdd:PRK05557  82 G--GVDILVNNAGITRDNLLmrmkeeDW--DRV----IDTNLTGVFNLTKAVARpMMKQRSGRIINISSVVGLMGNPGQA 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 19922066  247 IQCATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK05557 154 NYAASKAGVIGFTKSLARELASRGITVNAVAPG 186
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
153-287 1.19e-04

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: 43.14  E-value: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 153 DVTSEKTILEAARYVSQHLphGAEGLWsvVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVV 231
Cdd:cd05360  57 DVADAAQVERAADTAVERF--GRIDTW--VNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPhLRRRGGGALI 132
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19922066 232 FLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAGEFA---PGNGW 287
Cdd:cd05360 133 NVGSLLGYRSAPLQAAYSASKHAVRGFTESLRAELAHDGAPISVTLVQPTAmntPFFGH 191
PRK09072 PRK09072
SDR family oxidoreductase;
94-277 1.37e-04

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 43.01  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITGCEAPLAWYLAKKLDDLGFTVYA-GFNtpiEESDEAKILKEVTSGRMKLLHLDVTSEktileAARYVSQHLP 172
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLvGRN---AEKLEALAARLPYPGRHRWVVADLTSE-----AGREAVLARA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  173 HGAEGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRA-HGRVVFLTSGLNRVPSPVRGIQCAT 251
Cdd:PRK09072  76 REMGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQpSAMVVNVGSTFGSIGYPGYASYCAS 155
                        170       180
                 ....*....|....*....|....*.
gi 19922066  252 QAAVDCFAACLRQEMRTRGVDVSVVA 277
Cdd:PRK09072 156 KFALRGFSEALRRELADTGVRVLYLA 181
PRK06484 PRK06484
short chain dehydrogenase; Validated
92-279 1.45e-04

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 43.68  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   92 SASGKGVLITGCEAPLAWYLAKKLDDLGFTVYagfntpIEESD--EAKILKEVTSGRMKLLHLDVTSEKTILEAAryvsq 169
Cdd:PRK06484 266 AESPRVVAITGGARGIGRAVADRFAAAGDRLL------IIDRDaeGAKKLAEALGDEHLSVQADITDEAAVESAF----- 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  170 hlpHGAEGLWSVVHC------AHWIALGELEWIPfAVLRKSLDLNLLGSARLTQIFLPLVRRAhGRVVFLTSGLNRVPSP 243
Cdd:PRK06484 335 ---AQIQARWGRLDVlvnnagIAEVFKPSLEQSA-EDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALP 409
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19922066  244 VRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK06484 410 PRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPG 445
PRK06482 PRK06482
SDR family oxidoreductase;
99-284 1.48e-04

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 43.18  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   99 LITGCEAPLAWYLAKKLDDLGFTVYAGFNTPIEESDeakiLKEVTSGRMKLLHLDVTSEktilEAARYVSQHLPHGAEGL 178
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDD----LKARYGDRLWVLQLDVTDS----AAVRAVVDRAFAALGRI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  179 WSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRR-AHGRVVFLTSGLNRVPSPVRGIQCATQAAVDC 257
Cdd:PRK06482  78 DVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRqGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEG 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 19922066  258 FAACLRQEMRTRGVDVSVVAAG----EFAPG 284
Cdd:PRK06482 158 FVEAVAQEVAPFGIEFTIVEPGpartNFGAG 188
PLN02780 PLN02780
ketoreductase/ oxidoreductase
200-273 1.73e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 43.32  E-value: 1.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922066  200 VLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRV-PS-PVRGIQCATQAAVDCFAACLRQEMRTRGVDV 273
Cdd:PLN02780 157 LLKNLIKVNVEGTTKVTQAVLPgMLKRKKGAIINIGSGAAIViPSdPLYAVYAATKAYIDQFSRCLYVEYKKSGIDV 233
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
199-300 1.98e-04

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 42.47  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  199 AVLRKSLDLNLLGSARLTQIFLPLVRRAHG-RVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVA 277
Cdd:PRK12859 118 EELDKHYMVNVRATTLLSSQFARGFDKKSGgRIINMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAIN 197
                         90       100
                 ....*....|....*....|....
gi 19922066  278 AGefaPGN-GWLNEtELRDQAKQM 300
Cdd:PRK12859 198 PG---PTDtGWMTE-EIKQGLLPM 217
PRK12828 PRK12828
short chain dehydrogenase; Provisional
95-276 4.95e-04

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 41.32  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   95 GKGVLITGCEAPLAWYLAKKLDDLGFTVYAgfnTPIEESDEAKILKEVTSGRMKLLHLDVTSEKTILEA-ARYVSQHlph 173
Cdd:PRK12828   7 GKVVAITGGFGGLGRATAAWLAARGARVAL---IGRGAAPLSQTLPGVPADALRIGGIDLVDPQAARRAvDEVNRQF--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  174 gaEGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSGLNRVPSPVRGIQCATQ 252
Cdd:PRK12828  81 --GRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPaLTASGGGRIVNIGAGAALKAGPGMGAYAAAK 158
                        170       180
                 ....*....|....*....|....
gi 19922066  253 AAVDCFAACLRQEMRTRGVDVSVV 276
Cdd:PRK12828 159 AGVARLTEALAAELLDRGITVNAV 182
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
96-279 8.41e-04

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: 40.75  E-value: 8.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  96 KGVLITGCEAPLAWYLAKKLDDLGFTVY-AGFNtpiEESDEAKILKE-VTSGRMKLLHLDVTSEKTILEAARYVSQHLPH 173
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAiLDRN---ENPGAAAELQAiNPKVKATFVQCDVTSWEQLAAAFKKAIEKFGR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 174 gaegLWSVVHCA------HWIALGELEwipfAVLRKSLDLNLLGSARLTQIFLPLVRRAH----GRVVFLTS--GLNrvP 241
Cdd:cd05323  78 ----VDILINNAgildekSYLFAGKLP----PPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSvaGLY--P 147
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19922066 242 SPVRGIQCATQAAVDCFAACLRQEMRTR-GVDVSVVAAG 279
Cdd:cd05323 148 APQFPVYSASKHGVVGFTRSLADLLEYKtGVRVNAICPG 186
PRK07024 PRK07024
SDR family oxidoreductase;
199-279 8.72e-04

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 40.68  E-value: 8.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  199 AVLRKSLDLNLLGSARLTQIFL-PLVRRAHGRVVFLTS-----GLnrvpsPVRGIQCATQAAVDCFAACLRQEMRTRGVD 272
Cdd:PRK07024 101 AVFREVMDTNYFGMVATFQPFIaPMRAARRGTLVGIASvagvrGL-----PGAGAYSASKAAAIKYLESLRVELRPAGVR 175

                 ....*..
gi 19922066  273 VSVVAAG 279
Cdd:PRK07024 176 VVTIAPG 182
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
112-279 1.48e-03

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: 39.84  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 112 AKKLDDLGFTVyAGFNTPIEESDEAKILKEVTSGRMKLLHLDVTSEKTILEAARYVSQHlpHGA-EGLwsvVHCA----- 185
Cdd:cd05333  17 ALRLAAEGAKV-AVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAE--FGPvDIL---VNNAgitrd 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 186 -HWIALGELEWipfavlRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTSglnrvpspVRGIQ--------CATQAAV 255
Cdd:cd05333  91 nLLMRMSEEDW------DAVINVNLTGVFNVTQAVIRaMIKRRSGRIINISS--------VVGLIgnpgqanyAASKAGV 156
                       170       180
                ....*....|....*....|....
gi 19922066 256 DCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:cd05333 157 IGFTKSLAKELASRGITVNAVAPG 180
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
98-308 1.77e-03

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: 39.62  E-value: 1.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  98 VLITGCEAPLAWYLAKKLDDLGFTVY-AGFNTPIEESDEAKILKEvtSGRMKLLHLDVTSEKTILEAARyvsqHLPHGAE 176
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVAlAARRTDRLDELKAELLNP--NPSVEVEILDVTDEERNQLVIA----ELEAELG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 177 GLWSVVHCAHwIALGE-LEWIPFAVLRKSLDLNLLGSARLTQIFLP-LVRRAHGRVVFLTS--GLNRVP-SPVRGiqcAT 251
Cdd:cd05350  75 GLDLVIINAG-VGKGTsLGDLSFKAFRETIDTNLLGAAAILEAALPqFRAKGRGHLVLISSvaALRGLPgAAAYS---AS 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19922066 252 QAAVDCFAACLRQEMRTRGVDVSVVAAGeFApgngwlnETELRDQAKQMWNQLSSEQ 308
Cdd:cd05350 151 KAALSSLAESLRYDVKKRGIRVTVINPG-FI-------DTPLTANMFTMPFLMSVEQ 199
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
162-279 1.89e-03

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: 39.48  E-value: 1.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 162 EAARYVSQHLPHGAEGLWSVVHCAHWIA-LGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRAH-GRVVFLTSGLNR 239
Cdd:cd05340  69 ENCQQLAQRIAVNYPRLDGVLHNAGLLGdVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGR 148
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19922066 240 VPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:cd05340 149 QGRANWGAYAVSKFATEGL*QVLADEYQQRNLRVNCINPG 188
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
201-284 1.99e-03

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 39.67  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  201 LRKSLDLNLLGSARLTQIFLPLVRRAHG--RVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAa 278
Cdd:PRK06924 105 LITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGWSAYCSSKAGLDMFTQTVATEQEEEEYPVKIVA- 183

                 ....*.
gi 19922066  279 geFAPG 284
Cdd:PRK06924 184 --FSPG 187
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
199-284 2.64e-03

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: 38.66  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 199 AVLRKSLDLNLLGSARLTQIFLPLVRrAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEmrTRGVDVSVVAA 278
Cdd:cd11730  88 AAWRRILDANLTGAALVLKHALALLA-AGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKE--VRGLRLTLVRP 164

                ....*.
gi 19922066 279 GEFAPG 284
Cdd:cd11730 165 PAVDTG 170
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
180-303 2.95e-03

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: 39.01  E-value: 2.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066 180 SVVHCAHWIalgelEWIPFAVLRKSLDLNLLGSARLTQIFLPLVR-RAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCF 258
Cdd:cd08944  86 GAMHLTPAI-----IDTDLAVWDQTMAINLRGTFLCCRHAAPRMIaRGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNL 160
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19922066 259 AACLRQEMRTRGVDVSVVAAGefapgngwLNETELRDQAKQMWNQ 303
Cdd:cd08944 161 TRTLAAELRHAGIRCNALAPG--------LIDTPLLLAKLAGFEG 197
PRK12939 PRK12939
short chain dehydrogenase; Provisional
94-279 3.47e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 38.80  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITGCEAPLAWYLAKKLDDLGFTV-YAGFNTPIEESDEAKILKEvtSGRMKLLHLDVTSEKTIleaARYVSQHLp 172
Cdd:PRK12939   6 AGKRALVTGAARGLGAAFAEALAEAGATVaFNDGLAAEARELAAALEAA--GGRAHAIAADLADPASV---QRFFDAAA- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  173 HGAEGLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRR-AHGRVVFLTSGLNRVPSPVRGIQCAT 251
Cdd:PRK12939  80 AALGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDsGRGRIVNLASDTALWGAPKLGAYVAS 159
                        170       180
                 ....*....|....*....|....*...
gi 19922066  252 QAAVDCFAACLRQEMRTRGVDVSVVAAG 279
Cdd:PRK12939 160 KGAVIGMTRSLARELGGRGITVNAIAPG 187
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
225-294 3.90e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 38.52  E-value: 3.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19922066  225 RAHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRTRGVDVSVVAAGefaPGN-GWLNEtELR 294
Cdd:PRK12748 144 KAGGRIINLTSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPG---PTDtGWITE-ELK 210
PRK07023 PRK07023
SDR family oxidoreductase;
191-279 4.29e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 38.46  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066  191 GELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRR-AHGRVVFLTSGLNRVPSPVRGIQCATQAAVDCFAACLRQEMRtR 269
Cdd:PRK07023  92 GPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaAERRILHISSGAARNAYAGWSVYCATKAALDHHARAVALDAN-R 170
                         90
                 ....*....|
gi 19922066  270 GVDVSVVAAG 279
Cdd:PRK07023 171 ALRIVSLAPG 180
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
94-235 4.44e-03

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 38.61  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922066   94 SGKGVLITGCEAPLAWYLAKKLDDLGFTVYAGFNTpieESDEAKILKEVTSGRMKLlhlDVTSEKTILEAARYVSQHLPH 173
Cdd:PRK06463   6 KGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNS---AENEAKELREKGVFTIKC---DVGNRDQVKKSKEVVEKEFGR 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922066  174 gaegLWSVVHCAHWIALGELEWIPFAVLRKSLDLNLLGSARLTQIFLPLVRRA-HGRVVFLTS 235
Cdd:PRK06463  80 ----VDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSkNGAIVNIAS 138
 
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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