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Conserved domains on  [gi|19549323|ref|NP_598767|]
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retinol dehydrogenase 5 isoform b [Mus musculus]

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 ...
 30-306 1.99e-137

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: 390.49  E-value: 1.99e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  30 FIFITGCDSGFGRLLALQLDQKGFQVLAGCLTP--SGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFG 107
Cdd:cd09805   2 AVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFS 186
Cdd:cd09805  82 LVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 187 DSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTL-KACWARLPPAIQAHYGEAFLDTylrvQRRIMNLI---CDPELT 262
Cdd:cd09805 162 DSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDE----LKNKMLKYcsrASPDLS 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 19549323 263 KVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:cd09805 238 PVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 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; ...
 30-306 1.99e-137

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: 390.49  E-value: 1.99e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  30 FIFITGCDSGFGRLLALQLDQKGFQVLAGCLTP--SGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFG 107
Cdd:cd09805   2 AVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFS 186
Cdd:cd09805  82 LVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 187 DSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTL-KACWARLPPAIQAHYGEAFLDTylrvQRRIMNLI---CDPELT 262
Cdd:cd09805 162 DSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDE----LKNKMLKYcsrASPDLS 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 19549323 263 KVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:cd09805 238 PVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
31-310 6.60e-45

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 153.49  E-value: 6.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ---MASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:COG0300   8 VLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG--PIDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:COG0300  86 LVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLmRARGRGRIVNVSSVAGLRGLPGmAAYAASKAALEGF 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVTNleslESTLKACWARLPPAiqahygeafldtylRVQRRIMNLIcdpeltkvt 265
Cdd:COG0300 165 SESLRAELAPTGVRVTAVCPGPVDTPFTA----RAGAPAGRPLLSPE--------------EVARAILRAL--------- 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 19549323 266 sclehaltaRHPRTRYSPGWDAKLLWLPASYLPaRVVDAVLTWIL 310
Cdd:COG0300 218 ---------ERGRAEVYVGWDARLLARLLRLLP-RLFDRLLRRAL 252
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 31-213 2.81e-39

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 136.97  E-value: 2.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323    31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL---QQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVakeLGALGGKALFIQGDVTDRAQVKALVEQAVERLG--RLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   108 LVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAF 185
Cdd:pfam00106  81 LVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAVIGF 159

                         170       180
                  ....*....|....*....|....*...
gi 19549323   186 SDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMT 187
PRK08017 PRK08017
SDR family oxidoreductase;
31-308 6.37e-39

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 137.91  E-value: 6.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPsgaEDLQQMASSRLHTTLLDITDPQNVQQVAKWVkTRVGETGLFGLVN 110
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYRVLAACRKP---DDVARMNSLGFTGILLDLDDPESVERAADEV-IALTDNRLYGLFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK08017  81 NAGF-GVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLpAMLPHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWSDA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  189 LRRDMAPFGVQVSIVEPGFFRT-------------PVTNleslestlkacwarlpPAIQAHYgeafldtylrvqrrimnl 255
Cdd:PRK08017 160 LRMELRHSGIKVSLIEPGPIRTrftdnvnqtqsdkPVEN----------------PGIAARF------------------ 205

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19549323  256 ICDPEltKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLTW 308
Cdd:PRK08017 206 TLGPE--AVVPKLRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
 
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; ...
 30-306 1.99e-137

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: 390.49  E-value: 1.99e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  30 FIFITGCDSGFGRLLALQLDQKGFQVLAGCLTP--SGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFG 107
Cdd:cd09805   2 AVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKngPGAKELRRVCSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLWG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFS 186
Cdd:cd09805  82 LVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPaGGAYCASKAAVEAFS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 187 DSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTL-KACWARLPPAIQAHYGEAFLDTylrvQRRIMNLI---CDPELT 262
Cdd:cd09805 162 DSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQaKKLWERLPPEVKKDYGEDYIDE----LKNKMLKYcsrASPDLS 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 19549323 263 KVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:cd09805 238 PVIDSIEHALTSRHPRTRYYPGKDAKLLYIPASYLPTSLSDFLL 281
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 30-288 4.62e-59

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: 189.75  E-value: 4.62e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  30 FIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFG--RIDVLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSD 187
Cdd:cd05374  80 NNAGY-GLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPtPFLGPYCASKAALEALSE 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 188 SLRRDMAPFGVQVSIVEPGFFRTPVTNlesleSTLKACWARLPPAIQAHYGEAFLDTYLRVqrriMNLICDPEltKVTSC 267
Cdd:cd05374 159 SLRLELAPFGIKVTIIEPGPVRTGFAD-----NAAGSALEDPEISPYAPERKEIKENAAGV----GSNPGDPE--KVADV 227

                       250       260
                ....*....|....*....|.
gi 19549323 268 LEHALTARHPRTRYSPGWDAK 288
Cdd:cd05374 228 IVKALTSESPPLRYFLGSDAL 248
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
31-310 6.60e-45

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 153.49  E-value: 6.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ---MASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:COG0300   8 VLITGASSGIGRALARALAARGARVVLVARDAERLEALAAelrAAGARVEVVALDVTDPDAVAALAEAVLARFG--PIDV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:COG0300  86 LVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLmRARGRGRIVNVSSVAGLRGLPGmAAYAASKAALEGF 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVTNleslESTLKACWARLPPAiqahygeafldtylRVQRRIMNLIcdpeltkvt 265
Cdd:COG0300 165 SESLRAELAPTGVRVTAVCPGPVDTPFTA----RAGAPAGRPLLSPE--------------EVARAILRAL--------- 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 19549323 266 sclehaltaRHPRTRYSPGWDAKLLWLPASYLPaRVVDAVLTWIL 310
Cdd:COG0300 218 ---------ERGRAEVYVGWDARLLARLLRLLP-RLFDRLLRRAL 252
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 31-211 9.51e-41

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: 142.24  E-value: 9.51e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVN 110
Cdd:COG4221   8 ALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFG--RLDVLVN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 111 NAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDS 188
Cdd:COG4221  86 NAGVA-LLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAmRARGSGHIVNISSIAGLRPyPGGAVYAATKAAVRGLSES 164

                       170       180
                ....*....|....*....|...
gi 19549323 189 LRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:COG4221 165 LRAELRPTGIRVTVIEPGAVDTE 187
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 31-213 2.81e-39

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 136.97  E-value: 2.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323    31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL---QQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVakeLGALGGKALFIQGDVTDRAQVKALVEQAVERLG--RLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   108 LVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAF 185
Cdd:pfam00106  81 LVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAGLVPyPGGSAYSASKAAVIGF 159

                         170       180
                  ....*....|....*....|....*...
gi 19549323   186 SDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMT 187
PRK08017 PRK08017
SDR family oxidoreductase;
31-308 6.37e-39

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 137.91  E-value: 6.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPsgaEDLQQMASSRLHTTLLDITDPQNVQQVAKWVkTRVGETGLFGLVN 110
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYRVLAACRKP---DDVARMNSLGFTGILLDLDDPESVERAADEV-IALTDNRLYGLFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK08017  81 NAGF-GVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLpAMLPHGEGRIVMTSSVMGLISTPGrGAYAASKYALEAWSDA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  189 LRRDMAPFGVQVSIVEPGFFRT-------------PVTNleslestlkacwarlpPAIQAHYgeafldtylrvqrrimnl 255
Cdd:PRK08017 160 LRMELRHSGIKVSLIEPGPIRTrftdnvnqtqsdkPVEN----------------PGIAARF------------------ 205

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19549323  256 ICDPEltKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLTW 308
Cdd:PRK08017 206 TLGPE--AVVPKLRHALESPKPKLRYPVTLVTHAVMVLKRLLPGRMMDKILRG 256
PRK06914 PRK06914
SDR family oxidoreductase;
32-300 1.13e-36

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 132.84  E-value: 1.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMA-----SSRLHTTLLDITDPQNVQQVAKWVKtRVGETGLf 106
Cdd:PRK06914   7 IVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQAtqlnlQQNIKVQQLDVTDQNSIHNFQLVLK-EIGRIDL- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 gLVNNAGVA--GIIGPTPwltQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFGL 182
Cdd:PRK06914  85 -LVNNAGYAngGFVEEIP---VEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGlSPYVSSKYAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN----LESLESTLKACWARLPPAIQAHYgEAFLDTYLRvQRRIMNLICd 258
Cdd:PRK06914 161 EGFSESLRLELKPFGIDVALIEPGSYNTNIWEvgkqLAENQSETTSPYKEYMKKIQKHI-NSGSDTFGN-PIDVANLIV- 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 19549323  259 peltkvtscleHALTARHPRTRYSPGWDAKLLWLPASYLPAR 300
Cdd:PRK06914 238 -----------EIAESKRPKLRYPIGKGVKLMILAKKILPWR 268
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 31-210 7.90e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 130.42  E-value: 7.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVN 110
Cdd:PRK06180   7 WLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDV--LVN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVA--GIIGPTPwltQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFGLEAFS 186
Cdd:PRK06180  85 NAGYGheGAIEESP---LAEMRRQFEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGiGYYCGSKFALEGIS 161

                        170       180
                 ....*....|....*....|....
gi 19549323  187 DSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06180 162 ESLAKEVAPFGIHVTAVEPGSFRT 185
PRK06182 PRK06182
short chain dehydrogenase; Validated
 31-306 7.98e-36

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 130.08  E-value: 7.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCltpSGAEDLQQMASSRLHTTLLDITDPQNVQQVakwVKTRVGETGLFG-LV 109
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYGAA---RRVDKMEDLASLGVHPLSLDVTDEASIKAA---VDTIIAEEGRIDvLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAAN-GGGYCVSKFGLEAFSD 187
Cdd:PRK06182  80 NNAGY-GSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGKIYTPlGAWYHATKFALEGFSD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  188 SLRRDMAPFGVQVSIVEPGFFRTPVTNL--ESLESTLkacwARLPPAIQAHYGEAFLDTYLRVQRrimnlICDPELtkVT 265
Cdd:PRK06182 159 ALRLEVAPFGIDVVVIEPGGIKTEWGDIaaDHLLKTS----GNGAYAEQAQAVAASMRSTYGSGR-----LSDPSV--IA 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 19549323  266 SCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:PRK06182 228 DAISKAVTARRPKTRYAVGFGAKPLIFLRRILPDRAFDRLI 268
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 31-211 3.46e-34

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: 124.70  E-value: 3.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASS--RLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALggNAVAVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 109 VNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFGLEAFS 186
Cdd:cd05233  79 VNNAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPlPGQAAYAASKAALEGLT 157

                       170       180
                ....*....|....*....|....*
gi 19549323 187 DSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05233 158 RSLALELAPYGIRVNAVAPGLVDTP 182
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 31-213 1.86e-32

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: 120.66  E-value: 1.86e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM---ASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:COG1028   9 ALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAElraAGGRALAVAADVTDEAAVEALVAAAVAAFG--RLDI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAF 185
Cdd:COG1028  87 LVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHmRERGGGRIVNISSIAGLRGsPGQAAYAASKAAVVGL 165

                       170       180
                ....*....|....*....|....*...
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:COG1028 166 TRSLALELAPRGIRVNAVAPGPIDTPMT 193
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 33-306 4.00e-32

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 120.39  E-value: 4.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMassrlhTTL-LDITDPQNVQQVAKWVKTRVGETGLfgLVNN 111
Cdd:PRK06179   9 VTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPIPGV------ELLeLDVTDDASVQAAVDEVIARAGRIDV--LVNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  112 AGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGG-YCVSKFGLEAFSDSL 189
Cdd:PRK06179  81 AGV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMAlYAASKHAVEGYSESL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  190 RRDMAPFGVQVSIVEPGFFRTpvtnleSLESTlkacwarlppAIQAhygEAFLDTYLRVQRRIMNLICD-----PELTKV 264
Cdd:PRK06179 160 DHEVRQFGIRVSLVEPAYTKT------NFDAN----------APEP---DSPLAEYDRERAVVSKAVAKavkkaDAPEVV 220

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 19549323  265 TSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVL 306
Cdd:PRK06179 221 ADTVVKAALGPWPKMRYTAGGQASLLSKLRRFMPAGAVDKSL 262
PRK05693 PRK05693
SDR family oxidoreductase;
31-206 3.53e-31

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 117.97  E-value: 3.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAgclTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVN 110
Cdd:PRK05693   4 VLITGCSSGIGRALADAFKAAGYEVWA---TARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHG--GLDVLIN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFSDSL 189
Cdd:PRK05693  79 NAGY-GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPfAGAYCASKAAVHALSDAL 157

                        170
                 ....*....|....*..
gi 19549323  190 RRDMAPFGVQVSIVEPG 206
Cdd:PRK05693 158 RLELAPFGVQVMEVQPG 174
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 31-210 1.09e-29

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: 112.77  E-value: 1.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQL-DQKGFQVLAGCLTPSGAEDLQQMAS--SRLHTTLLDITDPqnVQQVAKWVKTRVGETGLFG 107
Cdd:cd05325   1 VLITGASRGIGLELVRQLlARGNNTVIATCRDPSAATELAALGAshSRLHILELDVTDE--IAESAEAVAERLGDAGLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVT-LALLPLLQQARGRVVNITSVLGRIAANGGG----YCVSKFGL 182
Cdd:cd05325  79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTqAFLPLLLKGARAKIINISSRVGSIGDNTSGgwysYRASKAAL 158

                       170       180
                ....*....|....*....|....*...
gi 19549323 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05325 159 NMLTKSLAVELKRDGITVVSLHPGWVRT 186
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 31-213 4.49e-29

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: 111.57  E-value: 4.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM---ASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfg 107
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNvrkAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTI-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAgiIGPTPW-LTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGLEA 184
Cdd:cd05339  80 LINNAGVV--SGKKLLeLPDEEIEKTFEVNTLAHFWTTKAFLpDMLERNHGHIVTIASVAGLISPAGLAdYCASKAAAVG 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 19549323 185 FSDSLRRDMAPF---GVQVSIVEPGFFRTPVT 213
Cdd:cd05339 158 FHESLRLELKAYgkpGIKTTLVCPYFINTGMF 189
PRK05993 PRK05993
SDR family oxidoreductase;
31-308 7.60e-29

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 111.66  E-value: 7.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPsgaEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGeTGLFGLVN 110
Cdd:PRK05993   7 ILITGCSSGIGAYCARALQSDGWRVFATCRKE---EDVAALEAEGLEAFQLDYAEPESIAALVAQVLELSG-GRLDALFN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NaGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAAN-GGGYCVSKFGLEAFSDS 188
Cdd:PRK05993  83 N-GAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIpVMRKQGQGRIVQCSSILGLVPMKyRGAYNASKFAIEGLSLT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  189 LRRDMAPFGVQVSIVEPGFFRTPVTNlesleSTLKACWARLPPAIQAHYGEafldtYLRVQRRIMN------LICDPElt 262
Cdd:PRK05993 162 LRMELQGSGIHVSLIEPGPIETRFRA-----NALAAFKRWIDIENSVHRAA-----YQQQMARLEGggsksrFKLGPE-- 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 19549323  263 KVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLTW 308
Cdd:PRK05993 230 AVYAVLLHALTAPRPRPHYRVTTPAKQGALLKRLLPARWLYRLLRK 275
PRK09291 PRK09291
SDR family oxidoreductase;
31-210 4.95e-28

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 109.32  E-value: 4.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSR---LHTTLLDITDPQNVQQVAKW---Vktrvgetg 104
Cdd:PRK09291   5 ILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRglaLRVEKLDLTDAIDRAQAAEWdvdV-------- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  105 lfgLVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA-ANGGGYCVSKFGL 182
Cdd:PRK09291  77 ---LLNNAGI-GEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKmVARGKGKVVFTSSMAGLITgPFTGAYCASKHAL 152

                        170       180
                 ....*....|....*....|....*...
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK09291 153 EAIAEAMHAELKPFGIQVATVNPGPYLT 180
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 31-213 1.07e-27

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 107.97  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPS-GAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK05557   8 ALVTGASRGIGRAIAERLAAQGANVVINYASSEaGAEALVAEIGAlggKALAVQGDVSDAESVERAVDEAKAEFG--GVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRI-AANGGGYCVSKFGLEA 184
Cdd:PRK05557  86 ILVNNAGIT-RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMgNPGQANYAASKAGVIG 164

                        170       180
                 ....*....|....*....|....*....
gi 19549323  185 FSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK05557 165 FTKSLARELASRGITVNAVAPGFIETDMT 193
PRK06482 PRK06482
SDR family oxidoreductase;
32-210 7.84e-26

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 103.66  E-value: 7.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVakwVKTRVGETGLFG-LVN 110
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAV---VDRAFAALGRIDvVVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGG-YCVSKFGLEAFSDS 188
Cdd:PRK06482  83 NAGY-GLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGgGRIVQVSSEGGQIAYPGFSlYHATKWGIEGFVEA 161

                        170       180
                 ....*....|....*....|..
gi 19549323  189 LRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06482 162 VAQEVAPFGIEFTIVEPGPART 183
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 33-210 3.48e-25

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 101.51  E-value: 3.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRL-------HTTLLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:cd05332   8 ITGASSGIGEELAYHLARLGARLV---LSARREERLEEVKSECLelgapspHVVPLDMSDLEDAEQVVEEALKLFG--GL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 106 FGLVNNAGVAGiigPTPW--LTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFG 181
Cdd:cd05332  83 DILINNAGISM---RSLFhdTSIDVDRKIMEVNYFGPVALTKAALPHLIERSqGSIVVVSSIAGKIGVPFrTAYAASKHA 159

                       170       180
                ....*....|....*....|....*....
gi 19549323 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05332 160 LQGFFDSLRAELSEPNISVTVVCPGLIDT 188
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 31-281 3.92e-25

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: 101.38  E-value: 3.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQL---DQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL----LDITDPQNVQQVAKWVKTRVGET 103
Cdd:cd09806   3 VLITGCSSGIGLHLAVRLasdPSKRFKVYATMRDLKKKGRLWEAAGALAGGTLetlqLDVCDSKSVAAAVERVTERHVDV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 104 glfgLVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGR--IAANGGgYCVSKF 180
Cdd:cd09806  83 ----LVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLqgLPFNDV-YCASKF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 181 GLEAFSDSLRRDMAPFGVQVSIVEPGffrtPV-TNLES--LESTLKACWARLPPaIQAHYgeaFLDTYLRVQRRIM-NLI 256
Cdd:cd09806 157 ALEGLCESLAVQLLPFNVHLSLIECG----PVhTAFMEkvLGSPEEVLDRTADD-ITTFH---FFYQYLAHSKQVFrEAA 228

                       250       260
                ....*....|....*....|....*
gi 19549323 257 CDPEltKVTSCLEHALTARHPRTRY 281
Cdd:cd09806 229 QNPE--EVAEVFLTAIRAPKPPLRY 251
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 30-224 6.49e-25

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: 100.13  E-value: 6.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  30 FIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAeDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDL-AALSASGGDVEAVPYDARDPEDARALVDALRDRFG--RIDVLV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGvagIIGPTPWL--TQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:cd08932  79 HNAG---IGRPTTLRegSDAELEAHFSINVIAPAELTRALLpALREAGSGRVVFLNSLSGKRVLAGnAGYSASKFALRAL 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKA 224
Cdd:cd08932 156 AHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAFPP 194
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 32-229 6.72e-24

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: 97.61  E-value: 6.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  32 FITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMAS------SRLHTTLLDITDPQnvqQVAKWVKTRVGETG- 104
Cdd:cd08934   7 LVTGASSGIGEATARALAAEGAAV---AIAARRVDRLEALADeleaegGKALVLELDVTDEQ---QVDAAVERTVEALGr 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 105 LFGLVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAA-NGGGYCVSKFGL 182
Cdd:cd08934  81 LDILVNNAGI-MLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALpHHLLRNKGTIVNISSVAGRVAVrNSAVYNATKFGV 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 19549323 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARL 229
Cdd:cd08934 160 NAFSEGLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYEERI 206
PRK12826 PRK12826
SDR family oxidoreductase;
32-230 8.26e-24

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 97.68  E-value: 8.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAE---DLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:PRK12826  10 LVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAataELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFG--RLDIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGG--GYCVSKFGLEAF 185
Cdd:PRK12826  88 VANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPRVGYPGlaHYAASKAGLVGF 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARLP 230
Cdd:PRK12826 167 TRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAIP 211
PRK05650 PRK05650
SDR family oxidoreductase;
31-241 1.06e-23

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 97.80  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQM--ASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLaLADVNEEGGEETLKLLreAGGDGFYQRCDVRDYSQLTALAQACEEKWG--GIDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVA--GIIGPtpwLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLE 183
Cdd:PRK05650  81 IVNNAGVAsgGFFEE---LSLEDWDWQIAINLMGVVkGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAmSSYNVAKAGVV 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPGFFRtpvTNL-ESLESTLkacwarlpPAIQAHYGEAF 241
Cdd:PRK05650 158 ALSETLLVELADDEIGVHVVCPSFFQ---TNLlDSFRGPN--------PAMKAQVGKLL 205
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 32-210 2.88e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 96.65  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNV-QQVAKWVKtRVGEtgLFGLVN 110
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVfAAVETAVE-HFGR--LDIVVN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGvAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDS 188
Cdd:PRK08263  84 NAG-YGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGGISAfPMSGIYHASKWALEGMSEA 162

                        170       180
                 ....*....|....*....|..
gi 19549323  189 LRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK08263 163 LAQEVAEFGIKVTLVEPGGYST 184
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 37-230 5.74e-23

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: 94.80  E-value: 5.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323    37 DSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASsRLHTTLL--DITDPQNVQQVAKWVKTRVGetGLFGLVNNAGV 114
Cdd:pfam13561   5 ESGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAE-ELGAAVLpcDVTDEEQVEALVAAAVEKFG--RLDILVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   115 AG-IIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQaRGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDSLRRD 192
Cdd:pfam13561  82 APkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVvPNYNAYGAAKAALEALTRYLAVE 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19549323   193 MAPFGVQVSIVEPGFFRTP-VTNLESLESTLKACWARLP 230
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLaASGIPGFDELLAAAEARAP 199
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 30-206 1.97e-22

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 93.34  E-value: 1.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  30 FIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:cd08929   2 AALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFG--GLDALV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGVaGIIGPTPWLTQDDFQR-VLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGG-GYCVSKFGLEAFSD 187
Cdd:cd08929  80 NNAGV-GVMKPVEELTPEEWRLvLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGaAYNASKFGLLGLSE 158

                       170
                ....*....|....*....
gi 19549323 188 SLRRDMAPFGVQVSIVEPG 206
Cdd:cd08929 159 AAMLDLREANIRVVNVMPG 177
PRK07832 PRK07832
SDR family oxidoreductase;
29-214 2.39e-22

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 94.34  E-value: 2.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   29 AFIFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS--------RLHTTLlDITDPQNVQQVAKWVKTRV 100
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF---LTDRDADGLAQTVADaralggtvPEHRAL-DISDYDAVAAFAADIHAAH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  101 GETGLfgLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGV--TLALLPLLQQARGRVVNITSVLGRIAAN-GGGYCV 177
Cdd:PRK07832  77 GSMDV--VMNIAGIS-AWGTVDRLTHEQWRRMVDVNLMGPIHVieTFVPPMVAAGRGGHLVNVSSAAGLVALPwHAAYSA 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19549323  178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK07832 154 SKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 31-213 3.84e-22

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: 93.00  E-value: 3.84e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA---EDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd05333   3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAaetVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFG--PVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVagiigpT-----PWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGrIAANGG--GYCVSK 179
Cdd:cd05333  81 LVNNAGI------TrdnllMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVG-LIGNPGqaNYAASK 153

                       170       180       190
                ....*....|....*....|....*....|....
gi 19549323 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05333 154 AGVIGFTKSLAKELASRGITVNAVAPGFIDTDMT 187
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
31-213 8.32e-22

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 92.15  E-value: 8.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ---MASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK05653   8 ALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAelrAAGGEARVLVFDVSDEAAVRALIEAAVEAFG--ALDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGG-YCVSKFGLEAF 185
Cdd:PRK05653  86 LVNNAGITRD-ALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISSVSGVTGNPGQTnYSAAKAGVIGF 164

                        170       180
                 ....*....|....*....|....*...
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK05653 165 TKALALELASRGITVNAVAPGFIDTDMT 192
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 31-206 5.33e-21

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: 90.03  E-value: 5.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMAS-------SRLHTTLLDITDPQNVQQV-----AKWVKT 98
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLI---LTGRRAERLQELADelgakfpVKVLPLQLDVSDRESIEAAlenlpEEFRDI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  99 RVgetglfgLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYC 176
Cdd:cd05346  80 DI-------LVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILpIMIARNQGHIINLGSIAGRYPyAGGNVYC 152

                       170       180       190
                ....*....|....*....|....*....|
gi 19549323 177 VSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:cd05346 153 ATKAAVRQFSLNLRKDLIGTGIRVTNIEPG 182
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 27-305 8.82e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 90.00  E-value: 8.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   27 SDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDlQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLf 106
Cdd:PRK07825   4 RGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKE-TAAELGLVVGGPLDVTDPASFAAFLDAVEADLGPIDV- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 gLVNNAGVAGIigpTPWLTQDD--FQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGL 182
Cdd:PRK07825  82 -LVNNAGVMPV---GPFLDEPDavTRRILDVNVYGVIlGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMAtYCASKHAV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTpvtnleSLESTLKACWArLPPAIQAHYGEAFLDtylrvqrrimnlicdpelt 262
Cdd:PRK07825 158 VGFTDAARLELRGTGVHVSVVLPSFVNT------ELIAGTGGAKG-FKNVEPEDVAAAIVG------------------- 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 19549323  263 kvtsclehalTARHPRTRYS-PGWDAKLLWLpASYLPARVVDAV 305
Cdd:PRK07825 212 ----------TVAKPRPEVRvPRALGPLAQA-QRLLPRRVREAL 244
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 27-213 1.50e-20

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: 88.62  E-value: 1.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  27 SDAFIFITGCDSGFGR-LLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQ---QVAKWVKTrvge 102
Cdd:cd05354   2 KDKTVLVTGANRGIGKaFVESLLAHGAKKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKaaaAQAKDVDV---- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 103 tglfgLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYCVSKF 180
Cdd:cd05354  78 -----VINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFApVLKANGGGAIVNLNSVASLKNfPAMGTYSASKS 152

                       170       180       190
                ....*....|....*....|....*....|...
gi 19549323 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05354 153 AAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMA 185
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 31-211 1.52e-20

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: 88.46  E-value: 1.52e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPS----GAEDLQQMA---SSRLHTTLLDITDPQNVQQVakwVKTRVGET 103
Cdd:cd08939   4 VLITGGSSGIGKALAKELVKEGANVIIVARSESkleeAVEEIEAEAnasGQKVSYISADLSDYEEVEQA---FAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 104 GLFG-LVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKF 180
Cdd:cd08939  81 GPPDlVVNCAGIS-IPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGySAYCPSKF 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 19549323 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd08939 160 ALRGLAESLRQELKPYNIRVSVVYPPDTDTP 190
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 31-211 3.53e-20

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 87.62  E-value: 3.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCltPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGetG 104
Cdd:PRK12825   9 ALVTGAARGLGRAIALRLARAGADVVVHY--RSDEEAAEELVEAvealgrRAQAVQADVTDKAALEAAVAAAVERFG--R 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  105 LFGLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVlgriAANGG-----GYCVS 178
Cdd:PRK12825  85 IDILVNNAGIF-EDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSV----AGLPGwpgrsNYAAA 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19549323  179 KFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12825 160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTD 192
PRK06181 PRK06181
SDR family oxidoreductase;
31-210 4.53e-20

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 87.73  E-value: 4.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK06181   4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALvvpTDVSDAEACERLIEAAVARFG--GIDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVagiigpTPWLTQDD------FQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKF 180
Cdd:PRK06181  82 LVNNAGI------TMWSRFDEltdlsvFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTrSGYAASKH 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 19549323  181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06181 156 ALHGFFDSLRIELADDGVAVTVVCPGFVAT 185
PRK07326 PRK07326
SDR family oxidoreductase;
32-206 6.30e-20

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 86.60  E-value: 6.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASS--RLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:PRK07326  10 LITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNkgNVLGLAADVRDEADVQRAVDAIVAAFG--GLDVLI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDS 188
Cdd:PRK07326  88 ANAGV-GHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFfAGGAAYNASKFGLVGFSEA 166

                        170
                 ....*....|....*...
gi 19549323  189 LRRDMAPFGVQVSIVEPG 206
Cdd:PRK07326 167 AMLDLRQYGIKVSTIMPG 184
PRK08264 PRK08264
SDR family oxidoreductase;
28-213 7.96e-20

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 86.48  E-value: 7.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   28 DAFIFITGCDSGFGRLLALQLDQKG-FQVLAGCLTPSGAEDLQqmasSRLHTTLLDITDPQNVQQVAKwvktRVGETGLf 106
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDLG----PRVVPLQLDVTDPASVAAAAE----AASDVTI- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 gLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLA-LLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEA 184
Cdd:PRK08264  77 -LVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAfAPVLAANGGGAIVNVLSVLSWVNfPNLGTYSASKAAAWS 155

                        170       180
                 ....*....|....*....|....*....
gi 19549323  185 FSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK08264 156 LTQALRAELAPQGTRVLGVHPGPIDTDMA 184
PRK09072 PRK09072
SDR family oxidoreductase;
27-205 1.66e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 86.15  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   27 SDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ--MASSRLHTTLLDITDPQNVQQVAKWVKTRvgeTG 104
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAArlPYPGRHRWVVADLTSEAGREAVLARAREM---GG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  105 LFGLVNNAGVAGIIgptpWLTQ---DDFQRVLSVNTLGPIGVTLAL-LPLLQQARGRVVNITSVLGRIAANG-GGYCVSK 179
Cdd:PRK09072  81 INVLINNAGVNHFA----LLEDqdpEAIERLLALNLTAPMQLTRALlPLLRAQPSAMVVNVGSTFGSIGYPGyASYCASK 156

                        170       180
                 ....*....|....*....|....*.
gi 19549323  180 FGLEAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:PRK09072 157 FALRGFSEALRRELADTGVRVLYLAP 182
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 31-213 3.85e-19

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 85.02  E-value: 3.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ---MASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK12939  10 ALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAaleAAGGRAHAIAADLADPASVQRFFDAAAAALG--GLDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAGIIGPTPwLTQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNI-TSVLGRIAANGGGYCVSKFGLEAF 185
Cdd:PRK12939  88 LVNNAGITNSKSATE-LDIDTWDAVMNVNVRGTFLMLRAALPHlRDSGRGRIVNLaSDTALWGAPKLGAYVASKGAVIGM 166

                        170       180
                 ....*....|....*....|....*...
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK12939 167 TRSLARELGGRGITVNAIAPGLTATEAT 194
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 31-200 1.12e-18

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 83.29  E-value: 1.12e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGcltpsG--AEDLQQMASSR--LHTTLLDITDPQNVQQVAKWVKTRVGEtgLF 106
Cdd:COG3967   8 ILITGGTSGIGLALAKRLHARGNTVIIT-----GrrEEKLEEAAAANpgLHTIVLDVADPASIAALAEQVTAEFPD--LN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 107 GLVNNAGVAGII----GPTPWltqDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRI-AANGGGYCVSKF 180
Cdd:COG3967  81 VLINNAGIMRAEdlldEAEDL---ADAEREITTNLLGPIRLTAAFLPHlKAQPEAAIVNVSSGLAFVpLAVTPTYSATKA 157

                       170       180
                ....*....|....*....|
gi 19549323 181 GLEAFSDSLRRDMAPFGVQV 200
Cdd:COG3967 158 ALHSYTQSLRHQLKDTSVKV 177
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 31-211 3.57e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 82.07  E-value: 3.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSrlHTTLLDITDPQnvqqvakWVKTRVGETGLF-GLV 109
Cdd:PRK07060  12 VLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGC--EPLRLDVGDDA-------AIRAALAAAGAFdGLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQ--ARGRVVNITSvlgrIAANGG-----GYCVSKFGL 182
Cdd:PRK07060  83 NCAGIA-SLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAagRGGSIVNVSS----QAALVGlpdhlAYCASKAAL 157

                        170       180
                 ....*....|....*....|....*....
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07060 158 DAITRVLCVELGPHGIRVNSVNPTVTLTP 186
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 31-214 4.36e-18

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: 81.61  E-value: 4.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQV-LAG----CLTPSGAEDLQQMASSRLHTtlLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVaLAArrtdRLDELKAELLNPNPSVEVEI--LDVTDEERNQLVIAELEAELG--GL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 106 FGLVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGLE 183
Cdd:cd05350  77 DLVIINAGV-GKGTSLGDLSFKAFRETIDTNLLGAAaILEAALPQFRAKGRGHLVLISSVAAlRGLPGAAAYSASKAALS 155

                       170       180       190
                ....*....|....*....|....*....|.
gi 19549323 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:cd05350 156 SLAESLRYDVKKRGIRVTVINPGFIDTPLTA 186
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 21-309 5.18e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 83.05  E-value: 5.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   21 RQSLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVK 97
Cdd:PRK07109   1 MMLKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALavvADVADAEAVQAAADRAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   98 TRVGetGLFGLVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRI-----AAn 171
Cdd:PRK07109  81 EELG--PIDTWVNNAMV-TVFGPFEDVTPEEFRRVTEVTYLGVVhGTLAALRHMRPRDRGAIIQVGSALAYRsiplqSA- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  172 gggYCVSKFGLEAFSDSLR----RDMAPfgVQVSIVEPGFFRTPVTNleslestlkacWARlppaiqahygeafldTYLR 247
Cdd:PRK07109 157 ---YCAAKHAIRGFTDSLRcellHDGSP--VSVTMVQPPAVNTPQFD-----------WAR---------------SRLP 205

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19549323  248 VQRRIMNLICDPELtkVTSCLEHAltARHPRTRYSPGWDAKLLWLpASYLPARVVDAVLTWI 309
Cdd:PRK07109 206 VEPQPVPPIYQPEV--VADAILYA--AEHPRRELWVGGPAKAAIL-GNRLAPGLLDRYLART 262
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 31-211 8.09e-18

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: 80.89  E-value: 8.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMAS--SRLHTTLL----DITDPQNVQQVAKWVKTRVGETG 104
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAKVV---LAARSAEALHELARevRELGGEAIavvaDVADAAQVERAADTAVERFGRID 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 105 LFglVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGL 182
Cdd:cd05360  80 TW--VNNAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVyGTLAALPHLRRRGGGALINVGSLLGyRSAPLQAAYSASKHAV 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 19549323 183 EAFSDSLRRDMAPFG--VQVSIVEPGFFRTP 211
Cdd:cd05360 157 RGFTESLRAELAHDGapISVTLVQPTAMNTP 187
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 32-210 9.01e-18

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: 80.36  E-value: 9.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  32 FITGCDSGFGRLLALQLDQKGF-QVLAGCLTP-SGAEDLQQMASSRLHTTL--LDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd05324   4 LVTGANRGIGFEIVRQLAKSGPgTVILTARDVeRGQAAVEKLRAEGLSVRFhqLDVTDDASIEAAADFVEEKYG--GLDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAAnggGYCVSKFGLEAFS 186
Cdd:cd05324  82 LVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLpLLKKSPAGRIVNVSSGLGSLTS---AYGVSKAALNALT 158

                       170       180
                ....*....|....*....|....
gi 19549323 187 DSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05324 159 RILAKELKETGIKVNACCPGWVKT 182
PRK06484 PRK06484
short chain dehydrogenase; Validated
 33-214 1.00e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 83.36  E-value: 1.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNNA 112
Cdd:PRK06484 274 ITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDV--LVNNA 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  113 GVAGIIGPTPWLTQDDFQRVLSVNTLGPIgVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDSLRR 191
Cdd:PRK06484 352 GIAEVFKPSLEQSAEDFTRVYDVNLSGAF-ACARAAARLMSQGGVIVNLGSIASLLALPPrNAYCASKAAVTMLSRSLAC 430

                        170       180
                 ....*....|....*....|...
gi 19549323  192 DMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK06484 431 EWAPAGIRVNTVAPGYIETPAVL 453
PRK12743 PRK12743
SDR family oxidoreductase;
33-216 2.57e-17

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 80.08  E-value: 2.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVlaGCLTPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK12743   7 VTASDSGIGKACALLLAQQGFDI--GITWHSDEEGAKETAEevrshgVRAEIRQLDLSDLPEGAQALDKLIQRLG--RID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGvAGIIGPTPWLTQDDFQRVLSVNTLGPI--GVTLALLPLLQQARGRVVNITSV---LGRIAAngGGYCVSKFG 181
Cdd:PRK12743  83 VLVNNAG-AMTKAPFLDMDFDEWRKIFTVDVDGAFlcSQIAARHMVKQGQGGRIINITSVhehTPLPGA--SAYTAAKHA 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19549323  182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLE 216
Cdd:PRK12743 160 LGGLTKAMALELVEHGILVNAVAPGAIATPMNGMD 194
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 27-214 3.95e-17

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 79.38  E-value: 3.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  27 SDAFIFITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASSRLHTTLL---------DITDPQNVQQVakwVK 97
Cdd:cd05364   2 SGKVAIITGSSSGIGAGTAILFARLGARL---ALTGRDAERLEETRQSCLQAGVSekkillvvaDLTEEEGQDRI---IS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  98 TRVGETG-LFGLVNNAGVAGIIGPTPwLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGG-GY 175
Cdd:cd05364  76 TTLAKFGrLDILVNNAGILAKGGGED-QDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVlYY 154

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19549323 176 CVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:cd05364 155 CISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR 193
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
33-211 4.72e-17

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 79.04  E-value: 4.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA----EDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgL 108
Cdd:PRK12824   7 VTGAKRGIGSAIARELLNDGYRVIATYFSGNDCakdwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVDI--L 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVA--GIIGPtpwLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGG-GYCVSKFGLEA 184
Cdd:PRK12824  85 VNNAGITrdSVFKR---MSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGyGRIINISSVNGLKGQFGQtNYSAAKAGMIG 161

                        170       180
                 ....*....|....*....|....*..
gi 19549323  185 FSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12824 162 FTKALASEGARYGITVNCIAPGYIATP 188
PRK06484 PRK06484
short chain dehydrogenase; Validated
 31-216 6.56e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 81.05  E-value: 6.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVN 110
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDV--LVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NagvAGIIGPTPWLTQD----DFQRVLSVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANG-GGYCVSKFGLE 183
Cdd:PRK06484  86 N---AGVTDPTMTATLDttleEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKrTAYSASKAAVI 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPGFFRTP-VTNLE 216
Cdd:PRK06484 163 SLTRSLACEWAAKGIRVNAVLPGYVRTQmVAELE 196
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 33-213 1.04e-16

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 78.17  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:cd05347  10 VTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKegvEATAFTCDVSDEEAIKAAVEAIEEDFGKIDI--LV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGvagIIGPTPWL--TQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSV---LGRIaaNGGGYCVSKFGLE 183
Cdd:cd05347  88 NNAG---IIRRHPAEefPEAEWRDVIDVNLNGVFFVSQAVARHmIKQGHGKIINICSLlseLGGP--PVPAYAASKGGVA 162

                       170       180       190
                ....*....|....*....|....*....|
gi 19549323 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05347 163 GLTKALATEWARHGIQVNAIAPGYFATEMT 192
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 31-232 1.29e-16

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 77.49  E-value: 1.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ-QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtGLFGLV 109
Cdd:cd08931   3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAaELGAENVVAGALDVTDRAAWAAALADFAAATGG-RLDALF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-----RIAAngggYCVSKFGLE 183
Cdd:cd08931  82 NNAGV-GRGGPFEDVPLAAHDRMVDINVKGVLnGAYAALPYLKATPGARVINTASSSAiygqpDLAV----YSATKFAVR 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 19549323 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARLPPA 232
Cdd:cd08931 157 GLTEALDVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKGLGRVLPV 205
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 31-211 1.65e-16

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 77.51  E-value: 1.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLtpsgAEDLQQMASSRLHTTLLDITDPQNV-QQVAKWVKtrvgETGLFG-L 108
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDL----PFVLLLEYGDPLRLTPLDVADAAAVrEVCSRLLA----EHGPIDaL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 109 VNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITS-VLGRIAANGGGYCVSKFGLEAFS 186
Cdd:cd05331  73 VNCAGVL-RPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASnAAHVPRISMAAYGASKAALASLS 151

                       170       180
                ....*....|....*....|....*
gi 19549323 187 DSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05331 152 KCLGLELAPYGVRCNVVSPGSTDTA 176
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 25-211 2.80e-16

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 77.02  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   25 PASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ-QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGet 103
Cdd:PRK12829   8 PLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAaRLPGAKVTATVADVADPAQVERVFDTAVERFG-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  104 GLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVV-NITSVLGRIAANGG-GYCVSKF 180
Cdd:PRK12829  86 GLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFyFARAAVPLLKASGHGGVIiALSSVAGRLGYPGRtPYAASKW 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19549323  181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12829 166 AVVGLVKSLAIELGPLGIRVNAILPGIVRGP 196
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 33-231 3.00e-16

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 77.03  E-value: 3.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:cd05366   7 ITGAAQGIGRAIAERLAADGFNIvLADLNLEEAAKSTIQEISEagyNAVAVGADVTDKDDVEALIDQAVEKFG--SFDVM 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 109 VNNAGVAGIigpTPWL--TQDDFQRVLSVNTLGPI-GVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFGLE 183
Cdd:cd05366  85 VNNAGIAPI---TPLLtiTEEDLKKVYAVNVFGVLfGIQAAARQFKKLGHgGKIINASSIAGVQGfPNLGAYSASKFAVR 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19549323 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTP---------VTNLESLESTLKACWARLPP 231
Cdd:cd05366 162 GLTQTAAQELAPKGITVNAYAPGIVKTEmwdyideevGEIAGKPEGEGFAEFSSSIP 218
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 30-194 4.54e-16

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: 76.17  E-value: 4.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  30 FIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSgAEDLQQMAS-----SRLHTTLLDITDPQNVQQVAKWVKTRVGEtg 104
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPSVVVLLARS-EEPLQELKEelrpgLRVTTVKADLSDAAGVEQLLEAIRKLDGE-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 105 LFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLAL--LPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFG 181
Cdd:cd05367  78 RDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLlrAFKKRGLKKTVVNVSSGAAVNPFKGwGLYCSSKAA 157

                       170
                ....*....|...
gi 19549323 182 LeafsDSLRRDMA 194
Cdd:cd05367 158 R----DMFFRVLA 166
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 31-265 1.09e-15

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 75.72  E-value: 1.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED-----LQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgL 105
Cdd:cd05327   4 VVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEaaaeiKKETGNAKVEVIQLDLSSLASVRQFAEEFLARFPR--L 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 106 FGLVNNAGVAGiigPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA---------ANGGG- 174
Cdd:cd05327  82 DILINNAGIMA---PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASApSRIVNVSSIAHRAGpidfndldlENNKEy 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 175 -----YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLkacWARLPPAIqahygeafLDTYLRVQ 249
Cdd:cd05327 159 spykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFFLL---YKLLRPFL--------KKSPEQGA 227

                       250
                ....*....|....*.
gi 19549323 250 RRIMNLICDPELTKVT 265
Cdd:cd05327 228 QTALYAATSPELEGVS 243
PRK07454 PRK07454
SDR family oxidoreductase;
32-235 1.58e-15

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 74.61  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK07454  10 LITGASSGIGKATALAFAKAGWDLA---LVARSQDALEALAAelrstgVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 fgLVNNAGVA--GIIGPTPWltqDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFG 181
Cdd:PRK07454  87 --LINNAGMAytGPLLEMPL---SDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAfPQWGAYCVSKAA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19549323  182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACwARLPPAIQA 235
Cdd:PRK07454 162 LAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTETVQADFDRS-AMLSPEQVA 214
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 32-252 2.40e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 75.01  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMA-----SSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK05872  13 VVTGAARGIGAELARRLHARGAKLA---LVDLEEAELAALAaelggDDRVLTVVADVTDLAAMQAAAEEAVERFG--GID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGVAGiigPTPWLTQD--DFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSvLGRIAANGGG--YCVSKFGL 182
Cdd:PRK05872  88 VVVANAGIAS---GGSVAQVDpdAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSS-LAAFAAAPGMaaYCASKAGV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT-----NLESLESTLkacwARLPPAIQAHY-----GEAFLDTYLRVQRRI 252
Cdd:PRK05872 164 EAFANALRLEVAHHGVTVGSAYLSWIDTDLVrdadaDLPAFRELR----ARLPWPLRRTTsvekcAAAFVDGIERRARRV 239
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 33-205 2.75e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 74.31  E-value: 2.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNNA 112
Cdd:PRK06841  20 VTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDI--LVNSA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  113 GVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQA-RGRVVNITSVLGRIAANGG-GYCVSKFGLEAFSDSLR 190
Cdd:PRK06841  98 GVA-LLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAgGGKIVNLASQAGVVALERHvAYCASKAGVVGMTKVLA 176

                        170
                 ....*....|....*
gi 19549323  191 RDMAPFGVQVSIVEP 205
Cdd:PRK06841 177 LEWGPYGITVNAISP 191
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 32-211 3.22e-15

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 73.76  E-value: 3.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQqmassrLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNn 111
Cdd:PRK08220  12 WVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYP------FATFVLDVSDAAAVAQVCQRLLAETGPLDV--LVN- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  112 agVAGII--GPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVlgriAANG-----GGYCVSKFGLE 183
Cdd:PRK08220  83 --AAGILrmGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRsGAIVTVGSN----AAHVprigmAAYGASKAALT 156

                        170       180
                 ....*....|....*....|....*...
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK08220 157 SLAKCVGLELAPYGVRCNVVSPGSTDTD 184
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 33-213 4.58e-15

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 73.57  E-value: 4.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:cd05341  10 VTGGARGLGLAHARLLVAEGAKVV---LSDILDEEGQAAAAElgdAARFFHLDVTDEDGWTAVVDTAREAFG--RLDVLV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGVAgIIGPTPWLTQDDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRI-AANGGGYCVSKFGLEAFSD 187
Cdd:cd05341  85 NNAGIL-TGGTVETTTLEEWRRLLDINLTGVfLGTRAVIPPMKEAGGGSIINMSSIEGLVgDPALAAYNASKGAVRGLTK 163

                       170       180
                ....*....|....*....|....*...
gi 19549323 188 SLRRDMAP--FGVQVSIVEPGFFRTPVT 213
Cdd:cd05341 164 SAALECATqgYGIRVNSVHPGYIYTPMT 191
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 28-212 4.75e-15

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 73.71  E-value: 4.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  28 DAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED-----LQQMASSRLHTTLLDITDpqnVQQVAKWVKTRVGE 102
Cdd:cd05330   3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAakaalLEIAPDAEVLLIKADVSD---EAQVEAYVDATVEQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 103 TG-LFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSK 179
Cdd:cd05330  80 FGrIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVfYGLEKVLKVMREQGSGMIVNTASVGGiRGVGNQSGYAAAK 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 19549323 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:cd05330 160 HGVVGLTRNSAVEYGQYGIRINAIAPGAILTPM 192
PRK08219 PRK08219
SDR family oxidoreductase;
33-211 8.11e-15

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 72.27  E-value: 8.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLdQKGFQVLAGCLTPSGAEDLQQmASSRLHTTLLDITDPQNVQqvakWVKTRVGEtgLFGLVNNA 112
Cdd:PRK08219   8 ITGASRGIGAAIAREL-APTHTLLLGGRPAERLDELAA-ELPGATPFPVDLTDPEAIA----AAVEQLGR--LDVLVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  113 GVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDSLRR 191
Cdd:PRK08219  80 GVA-DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRAnPGWGSYAASKFALRALADALRE 158

                        170       180
                 ....*....|....*....|
gi 19549323  192 DMAPfGVQVSIVEPGFFRTP 211
Cdd:PRK08219 159 EEPG-NVRVTSVHPGRTDTD 177
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 31-211 9.60e-15

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 72.52  E-value: 9.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:PRK12828  10 VAITGGFGGLGRATAAWLAARGARVaLIGRGAAPLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG--RLDALV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVagiigpTPW-----LTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGL 182
Cdd:PRK12828  88 NIAGA------FVWgtiadGDADTWDRMYGVNVKTTLnASKAALPALTASGGGRIVNIGAGAALKAGPGmGAYAAAKAGV 161

                        170       180
                 ....*....|....*....|....*....
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12828 162 ARLTEALAAELLDRGITVNAVLPSIIDTP 190
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 32-206 1.13e-14

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 72.47  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPS-GAEDLQ---QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK12937   9 IVTGASRGIGAAIARRLAADGFAVAVNYAGSAaAADELVaeiEAAGGRAIAVQADVADAAAVTRLFDAAETAFG--RIDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIgVTLALLPLLQQARGRVVNI-TSVLGRIAANGGGYCVSKFGLEAFS 186
Cdd:PRK12937  87 LVNNAGVMPL-GTIADFDLEDFDRTIATNLRGAF-VVLREAARHLGQGGRIINLsTSVIALPLPGYGPYAASKAAVEGLV 164

                        170       180
                 ....*....|....*....|
gi 19549323  187 DSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12937 165 HVLANELRGRGITVNAVAPG 184
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 33-223 1.64e-14

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 72.03  E-value: 1.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLT-PSGAEDLQQMASSRLHTTLL---DITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:cd05358   8 VTGASSGIGKAIAIRLATAGANVVVNYRSkEDAAEEVVEEIKAVGGKAIAvqaDVSKEEDVVALFQSAIKEFG--TLDIL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 109 VNNAGVAGIIgPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:cd05358  86 VNNAGLQGDA-SSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGhVNYAASKGGVKMM 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPGFFRTPVT-----NLESLESTLK 223
Cdd:cd05358 165 TKTLAQEYAPKGIRVNAIAPGAINTPINaeawdDPEQRADLLS 207
PRK05855 PRK05855
SDR family oxidoreductase;
25-214 2.25e-14

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 73.48  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   25 PASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAE---DLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVG 101
Cdd:PRK05855 312 PFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAErtaELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHG 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  102 ETGLfgLVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPI-------------GVTlallpllqqarGRVVNITSVlgri 168
Cdd:PRK05855 392 VPDI--VVNNAGI-GMAGGFLDTSAEDWDRVLDVNLWGVIhgcrlfgrqmverGTG-----------GHIVNVASA---- 453

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19549323  169 AANG-----GGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK05855 454 AAYApsrslPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVA 504
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 31-206 2.29e-14

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: 71.18  E-value: 2.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSrLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFGLVN 110
Cdd:cd05370   8 VLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSEYPN--LDILIN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 111 NAGVA---GIIGPTPWLtqDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAF 185
Cdd:cd05370  85 NAGIQrpiDLRDPASDL--DKADTEIDTNLIGPIRLIKAFLpHLKKQPEATIVNVSSGLAFVPmAANPVYCATKAALHSY 162

                       170       180
                ....*....|....*....|..
gi 19549323 186 SDSLRRDMAPFGVQV-SIVEPG 206
Cdd:cd05370 163 TLALRHQLKDTGVEVvEIVPPA 184
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 32-211 2.96e-14

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: 71.15  E-value: 2.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQmASSRLHTTLL-------DITDPQNVQQVAKWVKTRVGetG 104
Cdd:cd05344   5 LVTAASSGIGLAIARALAREGARVA---ICARNRENLER-AASELRAGGAgvlavvaDLTDPEDIDRLVEKAGDAFG--R 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 105 LFGLVNNAGvAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGR------IAANgggycV 177
Cdd:cd05344  79 VDILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKepepnlVLSN-----V 152

                       170       180       190
                ....*....|....*....|....*....|....
gi 19549323 178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05344 153 ARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 31-211 3.48e-14

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 70.90  E-value: 3.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCL-TPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVakwVKTRVGET 103
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLAADGADVIVLDIhPMRGRAEADAVAAgieaagGKALGLAFDVRDFAATRAA---LDAGVEEF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  104 G-LFGLVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANGG-GYCVSK 179
Cdd:PRK12827  86 GrLDILVNNAGIATD-AAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQvNYAASK 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19549323  180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12827 165 AGLIGLTKTLANELAPRGITVNAVAPGAINTP 196
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 27-207 5.52e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 70.37  E-value: 5.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   27 SDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVKTRVGet 103
Cdd:PRK07890   4 KGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALavpTDITDEDQCANLVALALERFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  104 GLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITS-VLGRIAANGGGYCVSKFGL 182
Cdd:PRK07890  82 RVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSmVLRHSQPKYGAYKMAKGAL 161

                        170       180
                 ....*....|....*....|....*
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGF 207
Cdd:PRK07890 162 LAASQSLATELGPQGIRVNSVAPGY 186
FabG-like PRK07231
SDR family oxidoreductase;
33-211 6.07e-14

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 70.24  E-value: 6.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMAS-----SRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK07231  10 VTGASSGIGEGIARRFAAEGARV---VVTDRNEEAAERVAAeilagGRAIAVAADVSDEADVEAAVAAALERFG--SVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLG-RIAANGGGYCVSKFGLEAF 185
Cdd:PRK07231  85 LVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGlRPRPGLGWYNASKGAVITL 164

                        170       180
                 ....*....|....*....|....*.
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07231 165 TKALAAELGPDKIRVNAVAPVVVETG 190
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 31-206 1.77e-13

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 69.02  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQV-----AKWVKTRVgetgl 105
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMlaslpAEWRNIDV----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 fgLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGLE 183
Cdd:PRK10538  78 --LVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLpGMVERNHGHIINIGSTAGSWPYAGGNvYGATKAFVR 155

                        170       180
                 ....*....|....*....|...
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEPG 178
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 33-213 1.88e-13

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 69.03  E-value: 1.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL----LDITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:cd05337   6 VTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAiyfqADIGELSDHEALLDQAWEDFG--RLDCL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 109 VNNAGVAGII-GPTPWLTQDDFQRVLSVNTLGPIGVTLALL-------PLLQQARGRVVNITSV-LGRIAANGGGYCVSK 179
Cdd:cd05337  84 VNNAGIAVRPrGDLLDLTEDSFDRLIAINLRGPFFLTQAVArrmveqpDRFDGPHRSIIFVTSInAYLVSPNRGEYCISK 163

                       170       180       190
                ....*....|....*....|....*....|....
gi 19549323 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05337 164 AGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMT 197
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 22-205 2.06e-13

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 68.56  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   22 QSLPASDAFIfiTGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKW 95
Cdd:PRK07666   3 QSLQGKNALI--TGAGRGIGRAVAIALAKEGVNV---GLLARTEENLKAVAEEveaygvKVVIATADVSDYEEVTAAIEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   96 VKTRVGETGLfgLVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLG-RIAANGG 173
Cdd:PRK07666  78 LKNELGSIDI--LINNAGISKF-GKFLELDPAEWEKIIQVNLMGVYYATRAVLpSMIERQSGDIINISSTAGqKGAAVTS 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19549323  174 GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:PRK07666 155 AYSASKFGVLGLTESLMQEVRKHNIRVTALTP 186
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-210 2.85e-13

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 68.33  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASSRLHTTLL---DITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:PRK05565  10 VTGASGGIGRAIAELLAKEGAKVvIAYDINEEAAQELLEEIKEEGGDAIAvkaDVSSEEDVENLVEQIVEKFG--KIDIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRI-AANGGGYCVSKFGLEAFS 186
Cdd:PRK05565  88 VNNAGI-SNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKsGVIVNISSIWGLIgASCEVLYSASKGAVNAFT 166

                        170       180
                 ....*....|....*....|....
gi 19549323  187 DSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK05565 167 KALAKELAPSGIRVNAVAPGAIDT 190
PRK07024 PRK07024
SDR family oxidoreductase;
31-213 2.95e-13

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 68.42  E-value: 2.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS-----RLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLG---LVARRTDALQAFAARlpkaaRVSVYAADVRDADALAAAAADFIAAHGLPDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 fgLVNNAGVA-GIigptpwLTQ-----DDFQRVLSVNTLGPIGV-TLALLPLLQQARGRVVNITSVLG-RIAANGGGYCV 177
Cdd:PRK07024  82 --VIANAGISvGT------LTEeredlAVFREVMDTNYFGMVATfQPFIAPMRAARRGTLVGIASVAGvRGLPGAGAYSA 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19549323  178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK07024 154 SKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMT 189
PRK08267 PRK08267
SDR family oxidoreductase;
31-313 3.26e-13

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 68.43  E-value: 3.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL-QQMASSRLHTTLLDITDPQNVQQ-VAKWVKTRVGetGLFGL 108
Cdd:PRK08267   4 IFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALaAELGAGNAWTGALDVTDRAAWDAaLADFAAATGG--RLDVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-----RIAAngggYCVSKFGL 182
Cdd:PRK08267  82 FNNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLnGAHAALPYLKATPGARVINTSSASAiygqpGLAV----YSATKFAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLE---STLKACWARLPPAIQAhygeafldtylrvqrrimnlicdp 259
Cdd:PRK08267 157 RGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEvdaGSTKRLGVRLTPEDVA------------------------ 212

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19549323  260 eltkvtsclEHALTARHPRTR--YSPGWDAKLLWLPASYLPARVVDAVLTWiLPRP 313
Cdd:PRK08267 213 ---------EAVWAAVQHPTRlhWPVGKQAKLLAFLARLSPGFVRRLINKS-LARP 258
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 28-211 3.55e-13

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 68.08  E-value: 3.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  28 DAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQmASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFG 107
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAK-LGDNCRFVPVDVTSEKDVKAALALAKAKFGR--LDI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVA------GIIGPTPwLTQDDFQRVLSVNTLGPIGVTLALLPLLQQA-------RGRVVNITSVlgriAANGG- 173
Cdd:cd05371  79 VVNCAGIAvaaktyNKKGQQP-HSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqggeRGVIINTASV----AAFEGq 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19549323 174 ----GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05371 154 igqaAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTP 195
PRK07023 PRK07023
SDR family oxidoreductase;
33-206 4.09e-13

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 67.73  E-value: 4.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLagCLTPSGAEDLQQMASSRLHTTLLDITDPQnvqQVAKWVKTRVGETGLFG----- 107
Cdd:PRK07023   6 VTGHSRGLGAALAEQLLQPGIAVL--GVARSRHPSLAAAAGERLAEVELDLSDAA---AAAAWLAGDLLAAFVDGasrvl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLA-LLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:PRK07023  81 LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAAlAQAASDAAERRILHISSGAARNAYAGwSVYCATKAALDHH 160

                        170       180
                 ....*....|....*....|.
gi 19549323  186 SDSLRRDmAPFGVQVSIVEPG 206
Cdd:PRK07023 161 ARAVALD-ANRALRIVSLAPG 180
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
32-210 4.79e-13

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 67.73  E-value: 4.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGC--LTPSGAEDLQQMAS--SRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfg 107
Cdd:PRK12938   7 YVTGGMGGIGTSICQRLHKDGFKVVAGCgpNSPRRVKWLEDQKAlgFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAGIIGPTPwLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:PRK12938  85 LVNNAGITRDVVFRK-MTREDWTAVIDTNLTSLFNVTKQVIDGMVERGwGRIINISSVNGQKGQFGqTNYSTAKAGIHGF 163

                        170       180
                 ....*....|....*....|....*
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK12938 164 TMSLAQEVATKGVTVNTVSPGYIGT 188
PRK06101 PRK06101
SDR family oxidoreductase;
31-219 7.86e-13

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 66.82  E-value: 7.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQmASSRLHTTLLDITDPQNVQQVAKWVKTrVGETGLFglvn 110
Cdd:PRK06101   4 VLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHT-QSANIFTLAFDVTDHPGTKAALSQLPF-IPELWIF---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVAGIIgptpwltqDD-------FQRVLSVNTLGPIGVTLALLPLLQqaRG-RVVNITSVLGRIA-ANGGGYCVSKFG 181
Cdd:PRK06101  78 NAGDCEYM--------DDgkvdatlMARVFNVNVLGVANCIEGIQPHLS--CGhRVVIVGSIASELAlPRAEAYGASKAA 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19549323  182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLE 219
Cdd:PRK06101 148 VAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTFA 185
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 33-211 1.13e-12

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: 66.53  E-value: 1.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPS-GAEDLQ---QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:cd05362   8 VTGASRGIGRAIAKRLARDGASVVVNYASSKaAAEEVVaeiEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG--GVDIL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 109 VNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQArGRVVNITSVLGRIAA-NGGGYCVSKFGLEAFSD 187
Cdd:cd05362  86 VNNAGV-MLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTpNYGAYAGSKAAVEAFTR 163

                       170       180
                ....*....|....*....|....
gi 19549323 188 SLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05362 164 VLAKELGGRGITVNAVAPGPVDTD 187
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
30-210 1.16e-12

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 66.63  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   30 FIFITGCDSGFGRLLALQLDQKGFQVLagCLTPSGAEDLQQMAS---SRLHTTLLDITDPQNVQQVAKWVKTRVGETGLF 106
Cdd:PRK06924   3 YVIITGTSQGLGEAIANQLLEKGTHVI--SISRTENKELTKLAEqynSNLTFHSLDLQDVHELETNFNEILSSIQEDNVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 G--LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARG--RVVNITSVLGRIAANG-GGYCVSKFG 181
Cdd:PRK06924  81 SihLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVdkRVINISSGAAKNPYFGwSAYCSSKAG 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19549323  182 LEAFSDS--LRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06924 161 LDMFTQTvaTEQEEEEYPVKIVAFSPGVMDT 191
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 32-214 2.02e-12

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 65.71  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASS---RLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGL 108
Cdd:PRK12936  10 LVTGASGGIGEEIARLLHAQGAIV---GLHGTRVEKLEALAAElgeRVKIFPANLSDRDEVKALGQKAEADLE--GVDIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGrIAANGG--GYCVSKFGLEAF 185
Cdd:PRK12936  85 VNNAGITKD-GLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRyGRIINITSVVG-VTGNPGqaNYCASKAGMIGF 162

                        170       180
                 ....*....|....*....|....*....
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK12936 163 SKSLAQEIATRNVTVNCVAPGFIESAMTG 191
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
32-211 2.11e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 65.90  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFG-LVN 110
Cdd:PRK08643   6 LVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNvVVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVAGIIgPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARG-RVVNITSVLGRIA-ANGGGYCVSKFGLEAFSD 187
Cdd:PRK08643  86 NAGVAPTT-PIETITEEQFDKVYNINVGGVIwGIQAAQEAFKKLGHGgKIINATSQAGVVGnPELAVYSSTKFAVRGLTQ 164

                        170       180
                 ....*....|....*....|....
gi 19549323  188 SLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK08643 165 TAARDLASEGITVNAYAPGIVKTP 188
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 31-205 2.18e-12

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 65.57  E-value: 2.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPsgaEDLQQMASSRLH--TTLLDITDpqnvqqvakWVKTR--VGETGLF 106
Cdd:cd05351  10 ALVTGAGKGIGRATVKALAKAGARVVAVSRTQ---ADLDSLVRECPGiePVCVDLSD---------WDATEeaLGSVGPV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 107 -GLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPL--LQQARGRVVNITSVLGRIA-ANGGGYCVSKFGL 182
Cdd:cd05351  78 dLLVNNAAVA-ILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGmiARGVPGSIVNVSSQASQRAlTNHTVYCSTKAAL 156

                       170       180
                ....*....|....*....|...
gi 19549323 183 EAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:cd05351 157 DMLTKVMALELGPHKIRVNSVNP 179
PRK06124 PRK06124
SDR family oxidoreductase;
33-228 3.21e-12

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 65.50  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK06124  16 VTGSARGLGFEIARALAGAGAHVL---VNGRNAATLEAAVAAlraaggAAEALAFDIADEEAVAAAFARIDAEHG--RLD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGvAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIA-ANGGGYCVSKFGLEA 184
Cdd:PRK06124  91 ILVNNVG-ARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGyGRIIAITSIAGQVArAGDAVYPAAKQGLTG 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19549323  185 FSDSLRRDMAPFGVQVSIVEPGFFRTPvTNLESLESTLKACWAR 228
Cdd:PRK06124 170 LMRALAAEFGPHGITSNAIAPGYFATE-TNAAMAADPAVGPWLA 212
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 32-212 7.06e-12

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 64.48  E-value: 7.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  32 FITGCDSGFGRLLALQLDQKGFQVLaGCltPSGAEDLQ------QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:cd08945   7 LVTGATSGIGLAIARRLGKEGLRVF-VC--ARGEEGLAttvkelREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 106 fgLVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPL---LQQARGRVVNITSVLGRIAA-NGGGYCVSKFG 181
Cdd:cd08945  84 --LVNNAGRSGG-GATAELADELWLDVVETNLTGVFRVTKEVLKAggmLERGTGRIINIASTGGKQGVvHAAPYSASKHG 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 19549323 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:cd08945 161 VVGFTKALGLELARTGITVNAVCPGFVETPM 191
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 33-212 7.32e-12

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 64.53  E-value: 7.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA----EDLQQMASSRLHTTLlDITDPQNVQQVAKWVKTRVGETGLfgL 108
Cdd:PRK13394  12 VTGAASGIGKEIALELARAGAAVAIADLNQDGAnavaDEINKAGGKAIGVAM-DVTNEDAVNAGIDKVAERFGSVDI--L 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIAANG-GGYCVSKFGLEAF 185
Cdd:PRK13394  89 VSNAGIQ-IVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLkSAYVTAKHGLLGL 167

                        170       180
                 ....*....|....*....|....*..
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK13394 168 ARVLAKEGAKHNVRSHVVCPGFVRTPL 194
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
32-220 7.39e-12

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 64.44  E-value: 7.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTT--LLDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:PRK08226  10 LITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRCTavVADVRDPASVAAAIKRAKEKEGRIDI--LV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRIAANGG--GYCVSKFGLEAFS 186
Cdd:PRK08226  88 NNAGVC-RLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLpEMIARKDGRIVMMSSVTGDMVADPGetAYALTKAAIVGLT 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19549323  187 DSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLES 220
Cdd:PRK08226 167 KSLAVEYAQSGIRVNAICPGYVRTPMAESIARQS 200
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 28-211 7.80e-12

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: 64.13  E-value: 7.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  28 DAFIFITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASSRLHTTLLDITD-----PQNVQQVAKWVKTRVG 101
Cdd:cd05340   4 DRIILVTGASDGIGREAALTYARYGATViLLGRNEEKLRQVADHINEEGGRQPQWFILDlltctSENCQQLAQRIAVNYP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 102 EtgLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRI-AANGGGYCVSK 179
Cdd:cd05340  84 R--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQgRANWGAYAVSK 161

                       170       180       190
                ....*....|....*....|....*....|..
gi 19549323 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05340 162 FATEGL*QVLADEYQQRNLRVNCINPGGTRTA 193
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 33-230 8.12e-12

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: 64.24  E-value: 8.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLT--PSGAEDLQQMASS---RLHTTllDITDPQnvQQVAKWVKTRVGETGLFG 107
Cdd:cd05323   5 ITGGASGIGLATAKLLLKKGAKVAILDRNenPGAAAELQAINPKvkaTFVQC--DVTSWE--QLAAAFKKAIEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGvagiIGPTPWLTQD-----DFQRVLSVNTLGPI-GVTLALLPLLQQAR---GRVVNITSVLGRIAANGGG-YCV 177
Cdd:cd05323  81 LINNAG----ILDEKSYLFAgklppPWEKTIDVNLTGVInTTYLALHYMDKNKGgkgGVIVNIGSVAGLYPAPQFPvYSA 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 19549323 178 SKFGLEAFSDSLRRDM-APFGVQVSIVEPGFFRTPVtnLESLESTLKACWARLP 230
Cdd:cd05323 157 SKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPL--LPDLVAKEAEMLPSAP 208
PRK06194 PRK06194
hypothetical protein; Provisional
 33-210 1.36e-11

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 63.88  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQ-VLAgcltpsgaeDLQQMASSRLHTTL-----------LDITDPQNVQQVAKWVKTRV 100
Cdd:PRK06194  11 ITGAASGFGLAFARIGAALGMKlVLA---------DVQQDALDRAVAELraqgaevlgvrTDVSDAAQVEALADAALERF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  101 GETGLfgLVNNAGVAGiiGPTPWL-TQDDFQRVLSVNTLGPI-GVTL------ALLPLLQQARGRVVNITSVLGRIAA-N 171
Cdd:PRK06194  82 GAVHL--LFNNAGVGA--GGLVWEnSLADWEWVLGVNLWGVIhGVRAftplmlAAAEKDPAYEGHIVNTASMAGLLAPpA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19549323  172 GGGYCVSKFGLEAFSDSLRRDMAPFGVQV--SIVEPGFFRT 210
Cdd:PRK06194 158 MGIYNVSKHAVVSLTETLYQDLSLVTDQVgaSVLCPYFVPT 198
PRK08589 PRK08589
SDR family oxidoreductase;
33-212 1.64e-11

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 63.64  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM--ASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVN 110
Cdd:PRK08589  11 ITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIksNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDV--LFN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGV---AGIIGPTPwltQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFS 186
Cdd:PRK08589  89 NAGVdnaAGRIHEYP---VDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAAdLYRSGYNAAKGAVINFT 165

                        170       180
                 ....*....|....*....|....*.
gi 19549323  187 DSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK08589 166 KSIAIEYGRDGIRANAIAPGTIETPL 191
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 31-213 1.73e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 63.23  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAE----DLQQMAsSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLf 106
Cdd:PRK08085  12 ILITGSAQGIGFLLATGLAEYGAEIIINDITAERAElavaKLRQEG-IKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDV- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 gLVNNAGVAGiIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQ-ARGRVVNITSV---LGRIAANggGYCVSKFGL 182
Cdd:PRK08085  90 -LINNAGIQR-RHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKrQAGKIINICSMqseLGRDTIT--PYAASKGAV 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK08085 166 KMLTRGMCVELARHNIQVNGIAPGYFKTEMT 196
PRK06949 PRK06949
SDR family oxidoreductase;
32-210 2.17e-11

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 62.86  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK06949  13 LVTGASSGLGARFAQVLAQAGAKVV---LASRRVERLKELRAEieaeggAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 fgLVNNAGVAG---IIGPTPwltqDDFQRVLSVNTLGPIGVTL---------ALLPLLQQARGRVVNITSVLG-RIAANG 172
Cdd:PRK06949  90 --LVNNSGVSTtqkLVDVTP----ADFDFVFDTNTRGAFFVAQevakrmiarAKGAGNTKPGGRIINIASVAGlRVLPQI 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19549323  173 GGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06949 164 GLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDT 201
PRK07069 PRK07069
short chain dehydrogenase; Validated
 32-212 2.25e-11

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 62.81  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRL---HTTLLDITDPQNVQQVAKWvKTRVGET----- 103
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVF---LTDINDAAGLDAFAAEInaaHGEGVAFAAVQDVTDEAQW-QALLAQAadamg 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  104 GLFGLVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFG 181
Cdd:PRK07069  79 GLSVLVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFlGCKHALPYLRASQPASIVNISSVAAFKAePDYTAYNASKAA 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19549323  182 LEAFSDSLRRDMAPFGVQV--SIVEPGFFRTPV 212
Cdd:PRK07069 158 VASLTKSIALDCARRGLDVrcNSIHPTFIRTGI 190
PRK07774 PRK07774
SDR family oxidoreductase;
33-230 2.87e-11

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 62.45  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:PRK07774  11 VTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIavqVDVSDPDSAKAMADATVSAFG--GIDYLV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVAGIIGPTPWLTQ--DDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAanGGGYCVSKFGLEAFS 186
Cdd:PRK07774  89 NNAAIYGGMKLDLLITVpwDYYKKFMSVNLDGALVCTRAVYKHMAKRGgGAIVNQSSTAAWLY--SNFYGLAKVGLNGLT 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19549323  187 DSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARLP 230
Cdd:PRK07774 167 QQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEFVADMVKGIP 210
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 32-213 2.92e-11

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 62.67  E-value: 2.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPS-GAEDLQQMASS---RLHTTLLDITD----PQNVQQVAKWvktrvget 103
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAINDRPDDeELAATQQELRAlgvEVIFFPADVADlsahEAMLDAAQAA-------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  104 glFG----LVNNAGVAGII-GPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGR-------VVNITSVLGRIAA- 170
Cdd:PRK12745  78 --WGridcLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPeelphrsIVFVSSVNAIMVSp 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19549323  171 NGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK12745 156 NRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMT 198
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 32-211 3.66e-11

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 62.21  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRLHTTL------LDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:PRK12429   8 LVTGAASGIGLEIALALAKEGAKVV---IADLNDEAAAAAAEALQKAGGkaigvaMDVTDEEAINAGIDYAVETFG--GV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 FGLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFGLE 183
Cdd:PRK12429  83 DILVNNAGIQ-HVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGkAAYVSAKHGLI 161

                        170       180
                 ....*....|....*....|....*...
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK12429 162 GLTKVVALEGATHGVTVNAICPGYVDTP 189
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 33-224 5.47e-11

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 61.89  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQmASSRLH----TTLL---DITDPQNVQQVAKWVKTRVGETGL 105
Cdd:PRK08213  17 VTGGSRGLGLQIAEALGEAGARVV---LSARKAEELEE-AAAHLEalgiDALWiaaDVADEADIERLAEETLERFGHVDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 fgLVNNAGVA-GiiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRiaanGG--------- 173
Cdd:PRK08213  93 --LVNNAGATwG--APAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRgyGRIINVASVAGL----GGnppevmdti 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19549323  174 GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN--LESLESTLKA 224
Cdd:PRK08213 165 AYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRgtLERLGEDLLA 217
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 31-213 6.45e-11

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 61.13  E-value: 6.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAgcltpsgaEDLQQ--MASSRLHTTLLDITDPqnVQQVAKWVKTrvgetgLFGL 108
Cdd:PRK06550   8 VLITGAASGIGLAQARAFLAQGAQVYG--------VDKQDkpDLSGNFHFLQLDLSDD--LEPLFDWVPS------VDIL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLAL-LPLLQQARGRVVNITSVLGRIAANGG-GYCVSKFGLEAFS 186
Cdd:PRK06550  72 CNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYlPQMLERKSGIIINMCSIASFVAGGGGaAYTASKHALAGFT 151

                        170       180
                 ....*....|....*....|....*..
gi 19549323  187 DSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK06550 152 KQLALDYAKDGIQVFGIAPGAVKTPMT 178
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 33-211 6.60e-11

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 61.69  E-value: 6.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQ-VLAGCLTPSGAEDLQQMASSRLHTTLL----DITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd08940   7 VTGSTSGIGLGIARALAAAGANiVLNGFGDAAEIEAVRAGLAAKHGVKVLyhgaDLSKPAAIEDMVAYAQRQFG--GVDI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAF 185
Cdd:cd08940  85 LVNNAGIQHV-APIEDFPTEKWDAIIALNLSAVfHTTRLALPHMKKQGWGRIINIASVHGLVAsANKSAYVAAKHGVVGL 163

                       170       180
                ....*....|....*....|....*.
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd08940 164 TKVVALETAGTGVTCNAICPGWVLTP 189
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 28-224 1.35e-10

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 60.74  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   28 DAFIFITGCDSGFGRLLALQLDQKGFQvLAgcLTPSGAEDLQQ------MASSRLHTTLLDITDPQNVQQVAKWVKTRVG 101
Cdd:PRK08217   5 DKVIVITGGAQGLGRAMAEYLAQKGAK-LA--LIDLNQEKLEEavaecgALGTEVRGYAANVTDEEDVEATFAQIAEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  102 etGLFGLVNNAGVA----------GIIGPTPWLTQddFQRVLSVNTLGPI--GVTLALLPLLQQARGRVVNITSVlGRiA 169
Cdd:PRK08217  82 --QLNGLINNAGILrdgllvkakdGKVTSKMSLEQ--FQSVIDVNLTGVFlcGREAAAKMIESGSKGVIINISSI-AR-A 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  170 ANGG--GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT---NLESLESTLKA 224
Cdd:PRK08217 156 GNMGqtNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTaamKPEALERLEKM 215
PRK07201 PRK07201
SDR family oxidoreductase;
31-187 1.52e-10

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 61.89  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGETG 104
Cdd:PRK07201 374 VLITGASSGIGRATAIKVAEAGATVF---LVARNGEALDELVAEirakggTAHAYTCDLTDSAAVDHTVKDILAEHGHVD 450

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  105 LfgLVNNAGVAgiIGPTPWLTQD---DFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITS--VLG---RIAAngggY 175
Cdd:PRK07201 451 Y--LVNNAGRS--IRRSVENSTDrfhDYERTMAVNYFGAVRLILGLLPHMRERRfGHVVNVSSigVQTnapRFSA----Y 522

                        170
                 ....*....|..
gi 19549323  176 CVSKFGLEAFSD 187
Cdd:PRK07201 523 VASKAALDAFSD 534
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 77-213 2.12e-10

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 60.08  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   77 HTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNNAGvagIIGPTPWL--TQDDFQRVLSVNTLGPIGVTLALLPLLQQA 154
Cdd:PRK07097  62 HGYVCDVTDEDGVQAMVSQIEKEVGVIDI--LVNNAG---IIKRIPMLemSAEDFRQVIDIDLNAPFIVSKAVIPSMIKK 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19549323  155 R-GRVVNI---TSVLGRiaANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK07097 137 GhGKIINIcsmMSELGR--ETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPQT 197
PRK06114 PRK06114
SDR family oxidoreductase;
21-211 2.74e-10

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 59.80  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   21 RQSLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSG--AEDLQQMASSRLHTTLL--DITDPQNVQQVAKWV 96
Cdd:PRK06114   1 PQLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDglAETAEHIEAAGRRAIQIaaDVTSKADLRAAVART 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   97 KTRVGETGLfgLVNNAGVAGIIgPTPWLTQDDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANG--- 172
Cdd:PRK06114  81 EAELGALTL--AVNAAGIANAN-PAEEMEEEQWQTVMDINLTGVfLSCQAEARAMLENGGGSIVNIASMSGIIVNRGllq 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19549323  173 GGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK06114 158 AHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATP 196
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 108-211 3.83e-10

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 58.30  E-value: 3.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRI-AANGGGYCVSKFGLEAF 185
Cdd:cd02266  35 VVHNAAI-LDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFgAPGLGGYAASKAALDGL 113

                        90       100
                ....*....|....*....|....*.
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd02266 114 AQQWASEGWGNGLPATAVACGTWAGS 139
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 33-213 5.28e-10

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: 58.66  E-value: 5.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQnvqQVAKWVKTRVGETG-LFGLVNN 111
Cdd:cd08944   8 VTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQ---QVAALFERAVEEFGgLDLLVNN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 112 AGVAGIIGPTPWLTQDDFQRVLSVNTLGPIgVTLALLPLLQQAR--GRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDS 188
Cdd:cd08944  85 AGAMHLTPAIIDTDLAVWDQTMAINLRGTF-LCCRHAAPRMIARggGSIVNLSSIAGQSGDPGyGAYGASKAAIRNLTRT 163

                       170       180
                ....*....|....*....|....*
gi 19549323 189 LRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd08944 164 LAAELRHAGIRCNALAPGLIDTPLL 188
PRK06947 PRK06947
SDR family oxidoreductase;
31-212 8.58e-10

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 58.28  E-value: 8.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ----QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK06947   5 VLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETadavRAAGGRACVVAGDVANEADVIAMFDAVQSAFG--RLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR----GRVVNITSVLGRIAANGG--GYCVSKF 180
Cdd:PRK06947  83 ALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRLGSPNEyvDYAGSKG 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19549323  181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK06947 163 AVDTLTLGLAKELGPHGVRVNAVRPGLIETEI 194
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 32-210 9.91e-10

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: 58.13  E-value: 9.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  32 FITGCDSGFGRLLALQLDQKGFQVLAGCLTPS--GAEDLQQMASSRLHTTLL--DITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd05359   2 LVTGGSRGIGKAIALRLAERGADVVINYRKSKdaAAEVAAEIEELGGKAVVVraDVSQPQDVEEMFAAVKERFG--RLDV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGvAGIIGPTPWLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVL-GRIAANGGGYCVSKFGLEAF 185
Cdd:cd05359  80 LVSNAA-AGAFRPLSELTPAHWDAKMNTNLKALVhCAQQAAKLMRERGGGRIVAISSLGsIRALPNYLAVGTAKAALEAL 158

                       170       180
                ....*....|....*....|....*
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05359 159 VRYLAVELGPRGIRVNAVSPGVIDT 183
PRK09730 PRK09730
SDR family oxidoreductase;
33-210 1.05e-09

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 57.94  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA--EDLQQMASSRLHTTLL--DITDPQNVQQVAKWVKtRVGETgLFGL 108
Cdd:PRK09730   6 VTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAaqEVVNLITQAGGKAFVLqaDISDENQVVAMFTAID-QHDEP-LAAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR----GRVVNITSVLGRIAANGG--GYCVSKFGL 182
Cdd:PRK09730  84 VNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHggsgGAIVNVSSAASRLGAPGEyvDYAASKGAI 163

                        170       180
                 ....*....|....*....|....*...
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK09730 164 DTLTTGLSLEVAAQGIRVNCVRPGFIYT 191
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 21-213 1.22e-09

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 57.84  E-value: 1.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  21 RQSLPASDAFIfiTGCDSGFGRLLALQLDQKGFQVLAgCLTPSGAED--LQQMASSRLHTTLL--DITDPQNVQQVAKWV 96
Cdd:cd05329   1 RWNLEGKTALV--TGGTKGIGYAIVEELAGLGAEVYT-CARNQKELDecLTEWREKGFKVEGSvcDVSSRSERQELMDTV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  97 KTRVGETgLFGLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLAL-LPLLQQARGRVVNITSVLGRIAANGGG- 174
Cdd:cd05329  78 ASHFGGK-LNILVNNAGTN-IRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAhPLLKASGNGNIVFISSVAGVIAVPSGAp 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19549323 175 YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:cd05329 156 YGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLV 194
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 33-210 1.38e-09

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 57.71  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGC-LTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFG-LVN 110
Cdd:PRK12935  11 VTGGAKGIGKAITVALAQEGAKVVINYnSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDiLVN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVAGIIGPTPwLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK12935  91 NAGITRDRTFKK-LNREDWERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGqTNYSAAKAGMLGFTKS 169

                        170       180
                 ....*....|....*....|..
gi 19549323  189 LRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK12935 170 LALELAKTNVTVNAICPGFIDT 191
PRK06172 PRK06172
SDR family oxidoreductase;
33-210 1.48e-09

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 57.45  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED---LQQMASSRLHTTLLDITDPQNVQQ-VAKWVKTrvgetglFGL 108
Cdd:PRK06172  12 VTGGAAGIGRATALAFAREGAKVVVADRDAAGGEEtvaLIREAGGEALFVACDVTRDAEVKAlVEQTIAA-------YGR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 V----NNAGVAGIIGPTPWLTQDDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGL 182
Cdd:PRK06172  85 LdyafNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVwLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKmSIYAASKHAV 164

                        170       180
                 ....*....|....*....|....*...
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06172 165 IGLTKSAAIEYAKKGIRVNAVCPAVIDT 192
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 33-211 1.51e-09

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 57.63  E-value: 1.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVNNA 112
Cdd:cd05363   8 ITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWG--SIDILVNNA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 113 GVAGiIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQA--RGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDSL 189
Cdd:cd05363  86 ALFD-LAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgrGGKIINMASQAGRRGeALVGVYCATKAAVISLTQSA 164

                       170       180
                ....*....|....*....|..
gi 19549323 190 RRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05363 165 GLNLIRHGINVNAIAPGVVDGE 186
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-213 1.74e-09

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 58.31  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLagCL-TPSGAEDLQQMASsRLH-TTL-LDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:PRK08261 215 VTGAARGIGAAIAEVLARDGAHVV--CLdVPAAGEALAAVAN-RVGgTALaLDITAPDAPARIAEHLAERHG--GLDIVV 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGV------AGiigptpwLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGrIAANGG--GYCVSKF 180
Cdd:PRK08261 290 HNAGItrdktlAN-------MDEARWDSVLAVNLLAPLRITEALLAAGALGDgGRIVGVSSISG-IAGNRGqtNYAASKA 361

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19549323  181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK08261 362 GVIGLVQALAPLLAERGITINAVAPGFIETQMT 394
PRK07074 PRK07074
SDR family oxidoreductase;
33-211 1.77e-09

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 57.47  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL-QQMASSRLHTTLLDITDPQNVQQVakwVKTRVGETGLFG-LVN 110
Cdd:PRK07074   7 VTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFaDALGDARFVPVACDLTDAASLAAA---LANAAAERGPVDvLVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVAGIIG--PTpwlTQDDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANGGGYCVSKFGLEAFSD 187
Cdd:PRK07074  84 NAGAARAASlhDT---TPASWRADNALNLEAAyLCVEAVLEGMLKRSRGAVVNIGSVNGMAALGHPAYSAAKAGLIHYTK 160

                        170       180
                 ....*....|....*....|....
gi 19549323  188 SLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07074 161 LLAVEYGRFGIRANAVAPGTVKTQ 184
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
33-211 2.05e-09

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 57.34  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVNNA 112
Cdd:PRK07067  11 LTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFG--GIDILFNNA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  113 GVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDSL 189
Cdd:PRK07067  89 ALFDM-APILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGrgGKIINMASQAGRRGeALVSHYCATKAAVISYTQSA 167

                        170       180
                 ....*....|....*....|..
gi 19549323  190 RRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK07067 168 ALALIRHGINVNAIAPGVVDTP 189
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 31-260 2.96e-09

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 56.71  E-value: 2.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQqmASSRLHTTLLDITDPQNVQQVAKwvktRVGETGLfgLVN 110
Cdd:cd05368   5 ALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELE--RGPGITTRVLDVTDKEQVAALAK----EEGRIDV--LFN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 111 NAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAA--NGGGYCVSKFGLEAFSD 187
Cdd:cd05368  77 CAGFVHH-GSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKdGSIINMSSVASSIKGvpNRFVYSTTKAAVIGLTK 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19549323 188 SLRRDMAPFGVQVSIVEPGFFRTPvtnleSLESTLKAcwarlppaiQAHYGEAFLDTylrVQRRIMNLICDPE 260
Cdd:cd05368 156 SVAADFAQQGIRCNAICPGTVDTP-----SLEERIQA---------QPDPEEALKAF---AARQPLGRLATPE 211
PRK12746 PRK12746
SDR family oxidoreductase;
32-212 3.46e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 56.58  E-value: 3.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLA--GCLTPSGAEDLQQMASSRLHTTLL--DITDPQNVQQVAKWVKT----RVGET 103
Cdd:PRK12746  10 LVTGASRGIGRAIAMRLANDGALVAIhyGRNKQAADETIREIESNGGKAFLIeaDLNSIDGVKKLVEQLKNelqiRVGTS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  104 GLFGLVNNAGVaGIIGPTPWLTQDDFQRVLSVNTLGPIGVTlALLPLLQQARGRVVNITSVLGRIAANGG-GYCVSKFGL 182
Cdd:PRK12746  90 EIDILVNNAGI-GTQGTIENTTEEIFDEIMAVNIKAPFFLI-QQTLPLLRAEGRVINISSAEVRLGFTGSiAYGLSKGAL 167

                        170       180       190
                 ....*....|....*....|....*....|
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK12746 168 NTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 28-212 3.61e-09

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 56.39  E-value: 3.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  28 DAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQ-MASSRLHTTLL---DITDPQNVQQVAKWVKTRVGEt 103
Cdd:cd08933   9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESeLNRAGPGSCKFvpcDVTKEEDIKTLISVTVERFGR- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 104 gLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGL 182
Cdd:cd08933  88 -IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGqKQAAPYVATKGAI 166

                       170       180       190
                ....*....|....*....|....*....|
gi 19549323 183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:cd08933 167 TAMTKALAVDESRYGVRVNCISPGNIWTPL 196
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
22-205 3.61e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 57.55  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   22 QSLPASDAF-------------------------IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRL 76
Cdd:PRK08324 391 EPLSEQEAFdieywsleqaklqrmpkpkplagkvALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD 470

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   77 H--TTLLDITDPQNVQQVAKWVKTRVGetGLFGLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLG--------------- 139
Cdd:PRK08324 471 RalGVACDVTDEAAVQAAFEEAALAFG--GVDIVVSNAGIA-ISGPIEETSDEDWRRSFDVNATGhflvareavrimkaq 547

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19549323  140 PIGvtlallpllqqarGRVVNITSVLGRIA-ANGGGYCVSKfgleAFSDSLRR----DMAPFGVQVSIVEP 205
Cdd:PRK08324 548 GLG-------------GSIVFIASKNAVNPgPNFGAYGAAK----AAELHLVRqlalELGPDGIRVNGVNP 601
PRK06139 PRK06139
SDR family oxidoreductase;
25-211 5.30e-09

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 56.65  E-value: 5.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   25 PASDAFIFITGCDSGFGRLLALQLDQKGFQ-VLAGcltpSGAEDLQQMASS--RLHTTLL----DITDPQNVQQVAKWVK 97
Cdd:PRK06139   4 PLHGAVVVITGASSGIGQATAEAFARRGARlVLAA----RDEEALQAVAEEcrALGAEVLvvptDVTDADQVKALATQAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   98 TRVGETGLFglVNNAGVaGIIG---PTPWltqDDFQRVLSVNTLG---------PIGVTLAllpllqqaRGRVVNITSVL 165
Cdd:PRK06139  80 SFGGRIDVW--VNNVGV-GAVGrfeETPI---EAHEQVIQTNLIGymrdahaalPIFKKQG--------HGIFINMISLG 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 19549323  166 GRIAAN-GGGYCVSKFGLEAFSDSLRRDMAPF-GVQVSIVEPGFFRTP 211
Cdd:PRK06139 146 GFAAQPyAAAYSASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDTP 193
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 31-210 5.65e-09

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 55.93  E-value: 5.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCL-TPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:cd05349   3 VLVTGASRGLGAAIARSFAREGARVVVNYYrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT--IV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGVAGIIGPTPWLTQD-----DFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSvlgRIAANG----GGYCVSK 179
Cdd:cd05349  81 NNALIDFPFDPDQRKTFDtidweDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGT---NLFQNPvvpyHDYTTAK 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 19549323 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05349 158 AALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 33-206 5.73e-09

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 55.81  E-value: 5.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDL-----QQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfg 107
Cdd:PRK12384   7 VIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVaqeinAEYGEGMAYGFGADATSEQSVLALSRGVDEIFGRVDL-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPI--GVTLALLPLLQQARGRVVNITSVLGRIAA-NGGGYCVSKFGLEA 184
Cdd:PRK12384  85 LVYNAGIA-KAAFITDFQLGDFDRSLQVNLVGYFlcAREFSRLMIRDGIQGRIIQINSKSGKVGSkHNSGYSAAKFGGVG 163

                        170       180
                 ....*....|....*....|..
gi 19549323  185 FSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12384 164 LTQSLALDLAEYGITVHSLMLG 185
PRK07814 PRK07814
SDR family oxidoreductase;
33-206 6.83e-09

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 55.56  E-value: 6.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSG----AEDLQQmASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgL 108
Cdd:PRK07814  15 VTGAGRGLGAAIALAFAEAGADVLIAARTESQldevAEQIRA-AGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDI--V 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  109 VNNAGVAGiigPTPWL--TQDDFQRVLSVNTLGPIGVTLALL--PLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLE 183
Cdd:PRK07814  92 VNNVGGTM---PNPLLstSTKDLADAFTFNVATAHALTVAAVplMLEHSGGGSVINISSTMGRLAGRGfAAYGTAKAALA 168

                        170       180
                 ....*....|....*....|...
gi 19549323  184 AFSDSLRRDMAPfGVQVSIVEPG 206
Cdd:PRK07814 169 HYTRLAALDLCP-RIRVNAIAPG 190
PRK05867 PRK05867
SDR family oxidoreductase;
32-210 7.11e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 55.43  E-value: 7.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASS------RLHTTLLDITDPQnvqQVAKWVKTRVGETGl 105
Cdd:PRK05867  13 LITGASTGIGKRVALAYVEAGAQV---AIAARHLDALEKLADEigtsggKVVPVCCDVSQHQ---QVTSMLDQVTAELG- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 fGLVNNAGVAGIIGPTPWLTQ--DDFQRVLSVNTLGpIGVTLALLPLLQQARGR---VVNITSVLGRI---AANGGGYCV 177
Cdd:PRK05867  86 -GIDIAVCNAGIITVTPMLDMplEEFQRLQNTNVTG-VFLTAQAAAKAMVKQGQggvIINTASMSGHIinvPQQVSHYCA 163

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19549323  178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK05867 164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILT 196
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 33-212 8.22e-09

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 55.15  E-value: 8.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKG-FQVLAGCLTPSGAE---DLQQMASSRLHTtllDITDPQNVQQVAKWVKTRVGEtgLFGL 108
Cdd:cd05326   9 ITGGASGIGEATARLFAKHGaRVVIADIDDDAGQAvaaELGDPDISFVHC---DVTVEADVRAAVDTAVARFGR--LDIM 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 109 VNNAGVAGiiGPTPWL---TQDDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAanGGG---YCVSKFG 181
Cdd:cd05326  84 FNNAGVLG--APCYSIletSLEEFERVLDVNVYGAfLGTKHAARVMIPAKKGSIVSVASVAGVVG--GLGphaYTASKHA 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 19549323 182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:cd05326 160 VLGLTRSAATELGEHGIRVNCVSPYGVATPL 190
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 33-205 9.27e-09

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 55.09  E-value: 9.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVakwVKTRVGETG-LFGLVNN 111
Cdd:cd05345  10 VTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAM---VEAALSKFGrLDILVNN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 112 AGVAGIIGPTPWLTQDDFQRVLSVNTLGpIGVTLALLPLLQQARGRVVNITsvlgrIAANGGG--------YCVSKFGLE 183
Cdd:cd05345  87 AGITHRNKPMLEVDEEEFDRVFAVNVKS-IYLSAQALVPHMEEQGGGVIIN-----IASTAGLrprpgltwYNASKGWVV 160

                       170       180
                ....*....|....*....|..
gi 19549323 184 AFSDSLRRDMAPFGVQVSIVEP 205
Cdd:cd05345 161 TATKAMAVELAPRNIRVNCLCP 182
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 31-210 1.06e-08

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 55.17  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED-----LQQMASSRLHTTLLDITDPQNVQQVAKWVKTRvgETGL 105
Cdd:cd09807   4 VIITGANTGIGKETARELARRGARVIMACRDMAKCEEaaaeiRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAE--EDRL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 106 FGLVNNAGVagIIGPTpWLTQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVL---GRIAAN---------- 171
Cdd:cd09807  82 DVLINNAGV--MRCPY-SKTEDGFEMQFGVNHLGHFLLTNLLLdLLKKSAPSRIVNVSSLAhkaGKINFDdlnseksynt 158

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19549323 172 GGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd09807 159 GFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK07063 PRK07063
SDR family oxidoreductase;
31-213 1.55e-08

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 54.67  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVL-----AGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGL 105
Cdd:PRK07063  10 ALVTGAAQGIGAAIARAFAREGAAVAladldAALAERAAAAIARDVAGARVLAVPADVTDAASVAAAVAAAEEAFG--PL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 FGLVNNAGVAGIIGPTPwLTQDDFQRVLSVNTLGPI-GVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGLE 183
Cdd:PRK07063  88 DVLVNNAGINVFADPLA-MTDEDWRRCFAVDLDGAWnGCRAVLPGMVERGRGSIVNIASTHAfKIIPGCFPYPVAKHGLL 166

                        170       180       190
                 ....*....|....*....|....*....|
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK07063 167 GLTRALGIEYAARNVRVNAIAPGYIETQLT 196
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 31-210 1.88e-08

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 54.11  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDIT------DPQNVQQVAKWVKTRVGEtg 104
Cdd:PRK08945  15 ILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPldlltaTPQNYQQLADTIEEQFGR-- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  105 LFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIA-ANGGGYCVSKFGL 182
Cdd:PRK08945  93 LDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLlLKSPAASLVFTSSSVGRQGrANWGAYAVSKFAT 172

                        170       180
                 ....*....|....*....|....*...
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK08945 173 EGMMQVLADEYQGTNLRVNCINPGGTRT 200
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 27-216 2.15e-08

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 54.25  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   27 SDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDlqqmasSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLF 106
Cdd:PRK06171   8 QGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGQH------ENYQFVPTDVSSAEEVNHTVAEIIEKFGR--ID 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGVAG---IIGPTP-----WLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGG-YC 176
Cdd:PRK06171  80 GLVNNAGINIprlLVDEKDpagkyELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHdGVIVNMSSEAGLEGSEGQScYA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19549323  177 VSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFR-TPVTNLE 216
Cdd:PRK06171 160 ATKAALNSFTRSWAKELGKHNIRVVGVAPGILEaTGLRTPE 200
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 27-213 2.26e-08

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 54.02  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   27 SDAFIFITGCDSGFGRLLALQLDQKGFQVLAgcLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLf 106
Cdd:PRK06463   6 KGKVALITGGTRGIGRAIAEAFLREGAKVAV--LYNSAENEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGRVDV- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 gLVNNAGVAGIIgptPWLTQDD--FQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSV--LGRIAANGGGYCVSKFG 181
Cdd:PRK06463  83 -LVNNAGIMYLM---PFEEFDEekYNKMIKINLNGAIYTTYEFLPLLKLSKnGAIVNIASNagIGTAAEGTTFYAITKAG 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19549323  182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK06463 159 IIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
PRK06953 PRK06953
SDR family oxidoreductase;
31-210 2.83e-08

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 53.54  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASsrlHTTLLDITDPQNVQQVAkWVKTrvGETGLFGLVn 110
Cdd:PRK06953   4 VLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA---EALALDVADPASVAGLA-WKLD--GEALDAAVY- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 nagVAGIIGP----TPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGG----YCVSKFGL 182
Cdd:PRK06953  77 ---VAGVYGPrtegVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGDATGTtgwlYRASKAAL 153

                        170       180
                 ....*....|....*....|....*...
gi 19549323  183 EAFSDSLRRDmAPFGVQVSIvEPGFFRT 210
Cdd:PRK06953 154 NDALRAASLQ-ARHATCIAL-HPGWVRT 179
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 33-210 4.93e-08

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 52.96  E-value: 4.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAE---DLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLV 109
Cdd:cd05365   4 VTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEavaAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFG--GITILV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAA-NGGGYCVSKFGLEAFSD 187
Cdd:cd05365  82 NNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSENKNvRIAAYGSSKAAVNHMTR 161

                       170       180
                ....*....|....*....|...
gi 19549323 188 SLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05365 162 NLAFDLGPKGIRVNAVAPGAVKT 184
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 28-210 8.39e-08

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 52.54  E-value: 8.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   28 DAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ---QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETG 104
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVdeiQQLGGQAFACRCDITSEQELSALADFALSKLGKVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  105 LfgLVNNAGVAgiiGPTPW-LTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVV-NITSVLGR-IAANGGGYCVSKFG 181
Cdd:PRK06113  91 I--LVNNAGGG---GPKPFdMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVIlTITSMAAEnKNINMTSYASSKAA 165

                        170       180
                 ....*....|....*....|....*....
gi 19549323  182 LEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK06113 166 ASHLVRNMAFDLGEKNIRVNGIAPGAILT 194
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 33-212 8.47e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 52.46  E-value: 8.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPS---GAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:PRK07523  15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAklaAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDI--LV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLL-QQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSD 187
Cdd:PRK07523  93 NNAGMQ-FRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMiARGAGKIINIASVQSALARPGiAPYTATKGAVGNLTK 171

                        170       180
                 ....*....|....*....|....*
gi 19549323  188 SLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK07523 172 GMATDWAKHGLQCNAIAPGYFDTPL 196
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 25-210 1.08e-07

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 52.11  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  25 PASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKwvktRVGETG 104
Cdd:cd08951   4 PPPMKRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLAD----QVNAIG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 105 LF-GLVNNAGVagIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLqqargRVVNITSVL--------------GRIA 169
Cdd:cd08951  80 RFdAVIHNAGI--LSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRRPK-----RLIYLSSGMhrggnaslddidwfNRGE 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19549323 170 ANGGGYCVSKFGLEAFSDSLRRdmAPFGVQVSIVEPGFFRT 210
Cdd:cd08951 153 NDSPAYSDSKLHVLTLAAAVAR--RWKDVSSNAVHPGWVPT 191
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
33-213 1.12e-07

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 52.04  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAE-----DLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfg 107
Cdd:PRK06935  20 VTGGNTGLGQGYAVALAKAGADII---ITTHGTNwdetrRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDI-- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGvagIIGPTPWL--TQDDFQRVLSVNtLGPIGVTLALLPLLQQAR--GRVVNITSVLgriAANGG----GYCVSK 179
Cdd:PRK06935  95 LVNNAG---TIRRAPLLeyKDEDWNAVMDIN-LNSVYHLSQAVAKVMAKQgsGKIINIASML---SFQGGkfvpAYTASK 167

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19549323  180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT 213
Cdd:PRK06935 168 HGVAGLTKAFANELAAYNIQVNAIAPGYIKTANT 201
PRK08628 PRK08628
SDR family oxidoreductase;
28-230 1.32e-07

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 51.88  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   28 DAFIFITGCDSGFGRLLALQLDQKG-FQVLAGCLTPSG--AEDLQQmASSRLHTTLLDITDPQnvqQVAKWVKTRVGETG 104
Cdd:PRK08628   7 DKVVIVTGGASGIGAAISLRLAEEGaIPVIFGRSAPDDefAEELRA-LQPRAEFVQVDLTDDA---QCRDAVEQTVAKFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  105 -LFGLVNNAGVAGIIGptpwL--TQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGrIAANGG--GYCVSK 179
Cdd:PRK08628  83 rIDGLVNNAGVNDGVG----LeaGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTA-LTGQGGtsGYAAAK 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19549323  180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP-----VTNLESLESTLKACWARLP 230
Cdd:PRK08628 158 GAQLALTREWAVALAKDGVRVNAVIPAEVMTPlyenwIATFDDPEAKLAAITAKIP 213
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 33-218 1.81e-07

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 51.31  E-value: 1.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLL----DITDPQNVQQVAKWVKTRVGETGLfgL 108
Cdd:cd05322   7 VIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYgfgaDATNEQSVIALSKGVDEIFKRVDL--L 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 109 VNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPI--GVTLALLPLLQQARGRVVNITSVLGRIAA-NGGGYCVSKFGLEAF 185
Cdd:cd05322  85 VYSAGIA-KSAKITDFELGDFDRSLQVNLVGYFlcAREFSKLMIRDGIQGRIIQINSKSGKVGSkHNSGYSAAKFGGVGL 163

                       170       180       190
                ....*....|....*....|....*....|....
gi 19549323 186 SDSLRRDMAPFGVQVSIVEPG-FFRTPVtnLESL 218
Cdd:cd05322 164 TQSLALDLAEHGITVNSLMLGnLLKSPM--FQSL 195
PRK08177 PRK08177
SDR family oxidoreductase;
31-210 4.17e-07

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 50.03  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTtlLDITDPQNVQQVAkwvkTRVGETGLFGLVN 110
Cdd:PRK08177   4 ALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEK--LDMNDPASLDQLL----QRLQGQRFDLLFV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVAgiiGPTPW----LTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGG----YCVSKFGL 182
Cdd:PRK08177  78 NAGIS---GPAHQsaadATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGemplYKASKAAL 154

                        170       180
                 ....*....|....*....|....*...
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK08177 155 NSMTRSFVAELGEPTLTVLSMHPGWVKT 182
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 64-231 4.20e-07

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 50.41  E-value: 4.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  64 GAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFGLVNNAGVA---GIIGptpwLTQDDFQRVLSVNTLGP 140
Cdd:cd05352  48 KAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGK--IDILIANAGITvhkPALD----YTYEQWNKVIDVNLNGV 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 141 IGV-TLALLPLLQQARGRVVNITSVLGRIA---ANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLE 216
Cdd:cd05352 122 FNCaQAAAKIFKKQGKGSLIITASMSGTIVnrpQPQAAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFV 201

                       170
                ....*....|....*
gi 19549323 217 SLEstLKACWARLPP 231
Cdd:cd05352 202 DKE--LRKKWESYIP 214
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 31-207 4.58e-07

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


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 49.97  E-value: 4.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED--LQQMASSRLHTTLL--DITDPQNVQQVAKWVKTRVGETGLf 106
Cdd:cd05357   3 ALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQrlKDELNALRNSAVLVqaDLSDFAACADLVAAAFRAFGRCDV- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 107 gLVNNAGV--AGIIGPTPWltqDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNIT-SVLGRIAANGGGYCVSKFGL 182
Cdd:cd05357  82 -LVNNASAfyPTPLGQGSE---DAWAELFGINLKAPYLLIQAFArRLAGSRNGSIINIIdAMTDRPLTGYFAYCMSKAAL 157

                       170       180
                ....*....|....*....|....*
gi 19549323 183 EAFSDSLRRDMAPFgVQVSIVEPGF 207
Cdd:cd05357 158 EGLTRSAALELAPN-IRVNGIAPGL 181
PRK07577 PRK07577
SDR family oxidoreductase;
26-206 5.53e-07

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 49.73  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   26 ASDAFIFITGCDSGFGRLLALQLDQKGFQVLAgcLTPSGAEDLqqmaSSRLHTTllDITDPqnvQQVAKWVKTRVGETGL 105
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIG--IARSAIDDF----PGELFAC--DLADI---EQTAATLAQINEIHPV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 FGLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGRIAANGGGYCVSKFGLEA 184
Cdd:PRK07577  70 DAIVNNVGIA-LPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICSRAIFGALDRTSYSAAKSALVG 148

                        170       180
                 ....*....|....*....|..
gi 19549323  185 FSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK07577 149 CTRTWALELAEYGITVNAVAPG 170
PRK06138 PRK06138
SDR family oxidoreductase;
33-211 6.45e-07

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 49.76  E-value: 6.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM--ASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVN 110
Cdd:PRK06138  10 VTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAiaAGGRAFARQGDVGSAEAVEALVDFVAARWG--RLDVLVN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NAGVaGIIGPTPWLTQDDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDS 188
Cdd:PRK06138  88 NAGF-GCGGTVVTTDEADWDAVMRVNVGGVfLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGrAAYVASKGAIASLTRA 166

                        170       180
                 ....*....|....*....|...
gi 19549323  189 LRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK06138 167 MALDHATDGIRVNAVAPGTIDTP 189
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 27-206 9.07e-07

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 49.25  E-value: 9.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  27 SDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED----LQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGE 102
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQlkeeLTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 103 TGlfGLVNNAGVAGIIGPTPW--LTQDDFQRVLSVNTLGPIGVTLALLPL-LQQARGRVVNITSVLGRIAAN-----GGG 174
Cdd:cd08930  81 ID--ILINNAYPSPKVWGSRFeeFPYEQWNEVLNVNLGGAFLCSQAFIKLfKKQGKGSIINIASIYGVIAPDfriyeNTQ 158

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19549323 175 ------YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:cd08930 159 myspveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 33-214 1.01e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 49.16  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK07478  11 ITGASSGIGRAAAKLFAREGAKVV---VGARRQAELDQLVAEiraeggEAVALAGDVRDEAYAKALVALAVERFG--GLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGVAGIIGPTPWLTQDDFQRVLSVN-TLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGG--GYCVSKFGLE 183
Cdd:PRK07478  86 IAFNNAGTLGEMGPVAEMSLEGWRETLATNlTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFPGmaAYAASKAGLI 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN 214
Cdd:PRK07478 166 GLTQVLAAEYGAQGIRVNALLPGGTDTPMGR 196
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 33-210 1.55e-06

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: 48.37  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVlagCLTPSGAEDLQQMASS-------RLHTTLLDITD-PQNVQQVAKWVKTRvgETG 104
Cdd:cd05356   6 VTGATDGIGKAYAEELAKRGFNV---ILISRTQEKLDAVAKEieekygvETKTIAADFSAgDDIYERIEKELEGL--DIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 105 LfgLVNNAGVAGIIgPTPWL--TQDDFQRVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLGRI-AANGGGYCVSKF 180
Cdd:cd05356  81 I--LVNNVGISHSI-PEYFLetPEDELQDIINVNVMATLKMTRLILpGMVKRKKGAIVNISSFAGLIpTPLLATYSASKA 157

                       170       180       190
                ....*....|....*....|....*....|
gi 19549323 181 GLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:cd05356 158 FLDFFSRALYEEYKSQGIDVQSLLPYLVAT 187
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 33-210 1.57e-06

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 48.34  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVNNA 112
Cdd:cd09761   6 VTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLG--RIDVLVNNA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 113 GVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGLEAFSDSLRR 191
Cdd:cd09761  84 ARGSK-GILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAfQSEPDSEAYAASKGGLVALTHALAM 162

                       170
                ....*....|....*....
gi 19549323 192 DMAPFgVQVSIVEPGFFRT 210
Cdd:cd09761 163 SLGPD-IRVNCISPGWINT 180
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 33-210 2.00e-06

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 48.16  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLL--DITDPQNVQQVAKWVKTRVGetGLFGLVN 110
Cdd:cd08943   6 VTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRALGVqcDVTSEAQVQSAFEQAVLEFG--GLDIVVS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 111 NAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR--GRVVNITSVLGrIAA--NGGGYCVSKfgleAFS 186
Cdd:cd08943  84 NAGIA-TSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNA-VAPgpNAAAYSAAK----AAE 157

                       170       180
                ....*....|....*....|....*....
gi 19549323 187 DSLRR----DMAPFGVQVSIVEP-GFFRT 210
Cdd:cd08943 158 AHLARclalEGGEDGIRVNTVNPdAVFRG 186
PRK06128 PRK06128
SDR family oxidoreductase;
33-212 2.35e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 48.32  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLtPSGAEDLQQM-----ASSRLHTTLL-DITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK06128  60 ITGADSGIGRATAIAFAREGADIALNYL-PEEEQDAAEVvqliqAEGRKAVALPgDLKDEAFCRQLVERAVKELG--GLD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLG------------PIGVTlallpllqqargrVVNITSVLG-RIAANGG 173
Cdd:PRK06128 137 ILVNIAGKQTAVKDIADITTEQFDATFKTNVYAmfwlckaaiphlPPGAS-------------IINTGSIQSyQPSPTLL 203

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19549323  174 GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK06128 204 DYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 32-210 2.40e-06

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 48.15  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLA--GCLTPSGAEDLQQMASS-----RLHTTLLDITDPQNV-QQVAKWVKTRVGET 103
Cdd:PRK12747   8 LVTGASRGIGRAIAKRLANDGALVAIhyGNRKEEAEETVYEIQSNggsafSIGANLESLHGVEALySSLDNELQNRTGST 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  104 GLFGLVNNAGvagiIGPTPWL---TQDDFQRVLSVNTLGPIGVTlALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSK 179
Cdd:PRK12747  88 KFDILINNAG----IGPGAFIeetTEQFFDRMVSVNAKAPFFII-QQALSRLRDNSRIINISSAATRISlPDFIAYSMTK 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19549323  180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK12747 163 GAINTMTFTLAKQLGARGITVNAILPGFIKT 193
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 33-210 2.56e-06

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 47.89  E-value: 2.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLaGC-----LTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd05343  11 VTGASVGIGAAVARALVQHGMKVV-GCarrvdKIEALAAECQSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQ--GVDV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAgiiGPTPWLT--QDDFQRVLSVNTLGPIGVTLALLPLLQ---QARGRVVNITSVLGRIAANG---GGYCVSK 179
Cdd:cd05343  88 CINNAGLA---RPEPLLSgkTEGWKEMFDVNVLALSICTREAYQSMKernVDDGHIININSMSGHRVPPVsvfHFYAATK 164

                       170       180       190
                ....*....|....*....|....*....|...
gi 19549323 180 FGLEAFSDSLRRDM--APFGVQVSIVEPGFFRT 210
Cdd:cd05343 165 HAVTALTEGLRQELreAKTHIRATSISPGLVET 197
PRK09135 PRK09135
pteridine reductase; Provisional
 25-206 2.58e-06

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 48.00  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   25 PASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTpSGAEdLQQMA----SSRLHTTLL---DITDPQNVQQVAKWVK 97
Cdd:PRK09135   3 TDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHR-SAAE-ADALAaelnALRPGSAAAlqaDLLDPDALPELVAACV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   98 TRVGetGLFGLVNNAGVagiIGPTPW--LTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLG-RIAANGGG 174
Cdd:PRK09135  81 AAFG--RLDALVNNASS---FYPTPLgsITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRGAIVNITDIHAeRPLKGYPV 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19549323  175 YCVSKFGLEAFSDSLRRDMAPfGVQVSIVEPG 206
Cdd:PRK09135 156 YCAAKAALEMLTRSLALELAP-EVRVNAVAPG 186
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 33-218 4.19e-06

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 47.26  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEdlQQMASSR-----LHTTLLDITDPQNVQQVAKWVKTRVGETGLfg 107
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLR--QAVNHLRaegfdVHGVMCDVRHREEVTHLADEAFRLLGHVDV-- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLA--LLPLLQQARGRVVNITSVLGRIAANG-GGYCVSKFGLEA 184
Cdd:PRK05876  87 VFSNAGIV-VGGPIVEMTHDDWRWVIDVDLWGSIHTVEAflPRLLEQGTGGHVVFTASFAGLVPNAGlGAYGVAKYGVVG 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19549323  185 FSDSLRRDMAPFGVQVSIVEPGFFRTP-VTNLESL 218
Cdd:PRK05876 166 LAETLAREVTADGIGVSVLCPMVVETNlVANSERI 200
PRK05717 PRK05717
SDR family oxidoreductase;
33-207 4.61e-06

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 47.19  E-value: 4.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETG-LFGLVNN 111
Cdd:PRK05717  15 VTGAARGIGLGIAAWLIAEGWQVV---LADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGrLDALVCN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  112 AGVAGIIGPT-PWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIA-ANGGGYCVSKFGLEAFSDSL 189
Cdd:PRK05717  92 AAIADPHNTTlESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSePDTEAYAASKGGLLALTHAL 171

                        170
                 ....*....|....*...
gi 19549323  190 RRDMAPfGVQVSIVEPGF 207
Cdd:PRK05717 172 AISLGP-EIRVNAVSPGW 188
PRK07102 PRK07102
SDR family oxidoreductase;
131-213 5.70e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 46.84  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  131 RVLSVNTLGPIGV-TLALLPLLQQARGRVVNITSVLG-RIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFF 208
Cdd:PRK07102 102 REFRTNFEGPIALlTLLANRFEARGSGTIVGISSVAGdRGRASNYVYGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFV 181


                 ....*
gi 19549323  209 RTPVT 213
Cdd:PRK07102 182 RTPMT 186
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
33-230 7.64e-06

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 46.44  E-value: 7.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLA-GCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNN 111
Cdd:PRK12481  13 ITGCNTGLGQGMAIGLAKAGADIVGvGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDI--LINN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  112 agvAGIIGPTPWL--TQDDFQRVLSVN--TLGPIGVTLALLPLLQQARGRVVNITSVLgriAANGG----GYCVSKFGLE 183
Cdd:PRK12481  91 ---AGIIRRQDLLefGNKDWDDVININqkTVFFLSQAVAKQFVKQGNGGKIINIASML---SFQGGirvpSYTASKSAVM 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN-LESLESTLKACWARLP 230
Cdd:PRK12481 165 GLTRALATELSQYNINVNAIAPGYMATDNTAaLRADTARNEAILERIP 212
PRK05866 PRK05866
SDR family oxidoreductase;
21-211 7.98e-06

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 46.66  E-value: 7.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   21 RQSLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAgclTPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVAK 94
Cdd:PRK05866  33 RQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVA---VARREDLLDAVADritragGDAMAVPCDLSDLDAVDALVA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   95 WVKTRVGetGLFGLVNNAGVAgIIGPTP-----WltqDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITS--VLG 166
Cdd:PRK05866 110 DVEKRIG--GVDILINNAGRS-IRRPLAesldrW---HDVERTMVLNYYAPLRLIRGLAPGMLERGdGHIINVATwgVLS 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19549323  167 RIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK05866 184 EASPLFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATP 228
PRK07831 PRK07831
SDR family oxidoreductase;
75-219 9.45e-06

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 46.18  E-value: 9.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   75 RLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVT--LALLPLLQ 152
Cdd:PRK07831  70 RVEAVVCDVTSEAQVDALIDAAVERLG--RLDVLVNNAGLGGQ-TPVVDMTDDEWSRVLDVTLTGTFRATraALRYMRAR 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19549323  153 QARGRVVNITSVLG-RIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP----VTNLESLE 219
Cdd:PRK07831 147 GHGGVIVNNASVLGwRAQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPflakVTSAELLD 218
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
33-230 1.04e-05

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 45.87  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGA-----EDLQQMASsRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:PRK08063   9 VTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAaeetaEEIEALGR-KALAVKANVGDVEKIKEMFAQIDEEFG--RLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGvAGIIGPTPWLTQDDFQRVLSVNTLG-PIGVTLALLPLLQQARGRVVNITSvLG--RIAANGGGYCVSKFGLEA 184
Cdd:PRK08063  86 FVNNAA-SGVLRPAMELEESHWDWTMNINAKAlLFCAQEAAKLMEKVGGGKIISLSS-LGsiRYLENYTTVGVSKAALEA 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 19549323  185 FSDSLRRDMAPFGVQVSIVEPGFFRT-PVTNLESLESTLKACWARLP 230
Cdd:PRK08063 164 LTRYLAVELAPKGIAVNAVSGGAVDTdALKHFPNREELLEDARAKTP 210
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 33-212 1.22e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 45.77  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLFGLVNNA 112
Cdd:PRK08265  11 VTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFG--RVDILVNLA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  113 ------GVAGiigptpwlTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGLEAF 185
Cdd:PRK08265  89 ctylddGLAS--------SRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWlYPASKAAIRQL 160

                        170       180
                 ....*....|....*....|....*..
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK08265 161 TRSMAMDLAPDGIRVNSVSPGWTWSRV 187
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 31-206 1.37e-05

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 46.05  E-value: 1.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAED-----LQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVgeTGL 105
Cdd:cd09809   4 IIITGANSGIGFETARSFALHGAHVILACRNMSRASAavsriLEEWHKARVEAMTLDLASLRSVQRFAEAFKAKN--SPL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 106 FGLVNNAGVAGIigptPW-LTQDDFQRVLSVNTLGPIGVTLA-LLPLLQQARGRVVNITSVLGRIA----ANGG------ 173
Cdd:cd09809  82 HVLVCNAAVFAL----PWtLTEDGLETTFQVNHLGHFYLVQLlEDVLRRSAPARVIVVSSESHRFTdlpdSCGNldfsll 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19549323 174 -----------GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:cd09809 158 sppkkkywsmlAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
PRK08251 PRK08251
SDR family oxidoreductase;
31-242 1.48e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 45.70  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQvLAGC------LTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGetG 104
Cdd:PRK08251   5 ILITGASSGLGAGMAREFAAKGRD-LALCarrtdrLEELKAELLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELG--G 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  105 LFGLVNNAGvagiIGPTPWLTQDDFQ---RVLSVNTLGPIG-VTLALLPLLQQARGRVVNITSVL------GRIAAnggg 174
Cdd:PRK08251  82 LDRVIVNAG----IGKGARLGTGKFWankATAETNFVAALAqCEAAMEIFREQGSGHLVLISSVSavrglpGVKAA---- 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19549323  175 YCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVT----NLESLESTLKACWArLPPAIQAHYGEAFL 242
Cdd:PRK08251 154 YAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNakakSTPFMVDTETGVKA-LVKAIEKEPGRAAV 224
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 33-211 1.63e-05

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


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 45.53  E-value: 1.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVlagcltpsGAEDLQQmasSRLHTTLLDITD--------PQNVQQVAKWVKTRVGETG 104
Cdd:cd08935  10 ITGGTGVLGGAMARALAQAGAKV--------AALGRNQ---EKGDKVAKEITAlggraialAADVLDRASLERAREEIVA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 105 LFG----LVNNAGV---AGIIGPTPW----------LTQDDFQRVLSVNTLG---PIGVtlALLPLLQQARGRVVNITSV 164
Cdd:cd08935  79 QFGtvdiLINGAGGnhpDATTDPEHYepeteqnffdLDEEGWEFVFDLNLNGsflPSQV--FGKDMLEQKGGSIINISSM 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 19549323 165 -----LGRIAAngggYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd08935 157 nafspLTKVPA----YSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 33-139 2.14e-05

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 45.28  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQ-----QMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFG 107
Cdd:cd09808   6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARkeietESGNQNIFLHIVDMSDPKQVWEFVEEFKEEGKK--LHV 83

                        90       100       110
                ....*....|....*....|....*....|..
gi 19549323 108 LVNNAGVagiIGPTPWLTQDDFQRVLSVNTLG 139
Cdd:cd09808  84 LINNAGC---MVNKRELTEDGLEKNFATNTLG 112
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
33-230 4.61e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 44.09  E-value: 4.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLaGCLTPSGAEDLQQMASsrLHTTLLDIT-DPQNVQQVAKWVKTRVGETGLFG-LVN 110
Cdd:PRK08993  15 VTGCDTGLGQGMALGLAEAGCDIV-GINIVEPTETIEQVTA--LGRRFLSLTaDLRKIDGIPALLERAVAEFGHIDiLVN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  111 NagvAGIIGPTPWL--TQDDFQRVLSVN--TLGPIGVTLALLPLLQQARGRVVNITSVLgriAANGG----GYCVSKFGL 182
Cdd:PRK08993  92 N---AGLIRREDAIefSEKDWDDVMNLNikSVFFMSQAAAKHFIAQGNGGKIINIASML---SFQGGirvpSYTASKSGV 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTN-LESLESTLKACWARLP 230
Cdd:PRK08993 166 MGVTRLMANEWAKHNINVNAIAPGYMATNNTQqLRADEQRSAEILDRIP 214
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 31-210 5.84e-05

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 43.92  E-value: 5.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLAGCL-TPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETgLFGLV 109
Cdd:PRK08642   8 VLVTGGSRGLGAAIARAFAREGARVVVNYHqSEDAAEALADELGDRAIALQADVTDREQVQAMFATATEHFGKP-ITTVV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVAGIIGPT-----PWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNI-TSVLGRIAANGGGYCVSKFGL 182
Cdd:PRK08642  87 NNALADFSFDGDarkkaDDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIgTNLFQNPVVPYHDYTTAKAAL 166

                        170       180
                 ....*....|....*....|....*...
gi 19549323  183 EAFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK08642 167 LGLTRNLAAELGPYGITVNMVSGGLLRT 194
PRK07775 PRK07775
SDR family oxidoreductase;
33-247 7.80e-05

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 43.59  E-value: 7.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTL---LDITDPQNVQQVAKWVKTRVGETGLfgLV 109
Cdd:PRK07775  15 VAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVafpLDVTDPDSVKSFVAQAEEALGEIEV--LV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  110 NNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGV-TLALLPLLQQARGRVVNITS-VLGRIAANGGGYCVSKFGLEAFSD 187
Cdd:PRK07775  93 SGAGDT-YFGKLHEISTEQFESQVQIHLVGANRLaTAVLPGMIERRRGDLIFVGSdVALRQRPHMGAYGAAKAGLEAMVT 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19549323  188 SLRRDMAPFGVQVSIVEPGFFRTPV---TNLESLESTLKAcWARlppaiqahYGEAFLDTYLR 247
Cdd:PRK07775 172 NLQMELEGTGVRASIVHPGPTLTGMgwsLPAEVIGPMLED-WAK--------WGQARHDYFLR 225
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 23-225 1.23e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 42.87  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   23 SLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTP----SGAEDLQQMA-SSRLHTTLLDITDPQnvqQVAKWVK 97
Cdd:PRK05875   2 QLSFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPdklaAAAEEIEALKgAGAVRYEPADVTDED---QVARAVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   98 TRVGETG-LFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTL-ALLPLLQQARGRVVNITSvlgrIAANG--- 172
Cdd:PRK05875  79 AATAWHGrLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKhAARELVRGGGGSFVGISS----IAASNthr 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19549323  173 --GGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRT----PVTNLESLESTLKAC 225
Cdd:PRK05875 155 wfGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTdlvaPITESPELSADYRAC 213
PRK07985 PRK07985
SDR family oxidoreductase;
19-212 1.24e-04

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 43.06  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   19 RDRQSLpasdafifITGCDSGFGRLLALQLDQKGFQVLAGCLtPSGAEDLQQMAS----SRLHTTLL--DITDPQNVQQV 92
Cdd:PRK07985  48 KDRKAL--------VTGGDSGIGRAAAIAYAREGADVAISYL-PVEEEDAQDVKKiieeCGRKAVLLpgDLSDEKFARSL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   93 AKWVKTRVGETGLFGLVnnAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQArGRVVNITSVLG-RIAAN 171
Cdd:PRK07985 119 VHEAHKALGGLDIMALV--AGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKG-ASIITTSSIQAyQPSPH 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19549323  172 GGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:PRK07985 196 LLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 33-211 1.33e-04

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 42.66  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCL--TPSGAEDLQQMASSRLHTTLL---DITDPQNVQQVAKWVKTRVGetGLFG 107
Cdd:cd05355  31 ITGGDSGIGRAVAIAFAREGADVAINYLpeEEDDAEETKKLIEEEGRKCLLipgDLGDESFCRDLVKEVVKEFG--KLDI 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 108 LVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQArGRVVNITSVLGRiaaNGGG----YCVSKFGLE 183
Cdd:cd05355 109 LVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-SSIINTTSVTAY---KGSPhlldYAATKGAIV 184

                       170       180
                ....*....|....*....|....*...
gi 19549323 184 AFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:cd05355 185 AFTRGLSLQLAEKGIRVNAVAPGPIWTP 212
PRK12742 PRK12742
SDR family oxidoreductase;
108-206 1.63e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 42.44  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 LVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQArGRVVNITSVLG-RIAANGG-GYCVSKFGLEAF 185
Cdd:PRK12742  79 LVVNAGIA-VFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEG-GRIIIIGSVNGdRMPVAGMaAYAASKSALQGM 156

                         90       100
                 ....*....|....*....|.
gi 19549323  186 SDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12742 157 ARGLARDFGPRGITINVVQPG 177
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 31-206 1.77e-04

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 42.34  E-value: 1.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGEtgLFGLVN 110
Cdd:cd05348   7 ALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK--LDCFIG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 111 NAGV----AGIIGpTPWLTQDD-FQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGrIAANGGG--YCVSKFGLE 183
Cdd:cd05348  85 NAGIwdysTSLVD-IPEEKLDEaFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAG-FYPGGGGplYTASKHAVV 162

                       170       180
                ....*....|....*....|...
gi 19549323 184 AFSDSLRRDMAPFgVQVSIVEPG 206
Cdd:cd05348 163 GLVKQLAYELAPH-IRVNGVAPG 184
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 75-206 1.80e-04

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 42.47  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   75 RLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNNAGVAgIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQA 154
Cdd:PRK12859  69 KVSSMELDLTQNDAPKELLNKVTEQLGYPHI--LVNNAAYS-TNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKK 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19549323  155 RG-RVVNITS------VLGRIAangggYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12859 146 SGgRIINMTSgqfqgpMVGELA-----YAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
PLN02253 PLN02253
xanthoxin dehydrogenase
 33-205 1.88e-04

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 42.50  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVlagCLTpsgaeDLQQMASSRLHTTL----------LDITDPQNVQQVAKWVKTRVGE 102
Cdd:PLN02253  23 VTGGATGIGESIVRLFHKHGAKV---CIV-----DLQDDLGQNVCDSLggepnvcffhCDVTVEDDVSRAVDFTVDKFGT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  103 TGLfgLVNNAGVAGiiGPTPWLTQ---DDFQRVLSVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAANG-GGYCV 177
Cdd:PLN02253  95 LDI--MVNNAGLTG--PPCPDIRNvelSEFEKVFDVNVKGVfLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGpHAYTG 170

                        170       180
                 ....*....|....*....|....*...
gi 19549323  178 SKFGLEAFSDSLRRDMAPFGVQVSIVEP 205
Cdd:PLN02253 171 SKHAVLGLTRSVAAELGKHGIRVNCVSP 198
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 32-211 2.08e-04

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: 41.74  E-value: 2.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASSRlhTTLLDITDPQNVQQvakwVKTRVGETGLFGLVNN 111
Cdd:cd11730   2 LILGATGGIGRALARALAGRGWRLL---LSGRDAGALAGLAAEV--GALARPADVAAELE----VWALAQELGPLDLLVY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 112 AgvAGIIGPTPWL--TQDDFQRVLSVNTLGPIGVTLALLPLLQQArGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDS 188
Cdd:cd11730  73 A--AGAILGKPLArtKPAAWRRILDANLTGAALVLKHALALLAAG-ARLVFLGAYPELVMLPGlSAYAAAKAALEAYVEV 149

                       170       180
                ....*....|....*....|...
gi 19549323 189 LRRDMApfGVQVSIVEPGFFRTP 211
Cdd:cd11730 150 ARKEVR--GLRLTLVRPPAVDTG 170
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 25-212 2.24e-04

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 42.13  E-value: 2.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  25 PASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQM--ASSRLHTTLLDITDPQNVQQVAKWVKTRVGE 102
Cdd:cd08937   1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEIlaAGDAAHVHTADLETYAGAQGVVRAAVERFGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 103 TGLfgLVNNAGvaGIIGPTPWLTQDDFQRVLSVN-TLGPIGVTLALLPLLQQAR--GRVVNITSVLGRiAANGGGYCVSK 179
Cdd:cd08937  81 VDV--LINNVG--GTIWAKPYEHYEEEQIEAEIRrSLFPTLWCCRAVLPHMLERqqGVIVNVSSIATR-GIYRIPYSAAK 155

                       170       180       190
                ....*....|....*....|....*....|...
gi 19549323 180 FGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPV 212
Cdd:cd08937 156 GGVNALTASLAFEHARDGIRVNAVAPGGTEAPP 188
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
31-208 2.42e-04

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 42.27  E-value: 2.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCdSGF-GRLLALQLDQKGFQVLAGCLTPSGAEDLQQMAssRLHTTLLDITDPQNVQQVAKWVKTrvgetglfgLV 109
Cdd:COG0451   2 ILVTGG-AGFiGSHLARRLLARGHEVVGLDRSPPGAANLAALP--GVEFVRGDLRDPEALAAALAGVDA---------VV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 110 NNAGVAGIigptpwlTQDDFQRVLSVNTLGPI---------GVtlallpllqqarGRVVNI--TSVLGR---------IA 169
Cdd:COG0451  70 HLAAPAGV-------GEEDPDETLEVNVEGTLnlleaaraaGV------------KRFVYAssSSVYGDgegpidedtPL 130

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19549323 170 ANGGGYCVSKFGLEAFSDSLRRDmapFGVQVSIVEPGFF 208
Cdd:COG0451 131 RPVSPYGASKLAAELLARAYARR---YGLPVTILRPGNV 166
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 32-242 2.57e-04

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 41.61  E-value: 2.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  32 FITGCDSGFGRLLALQLDQKGFQVL-----AGCLTPSGAEDLQQMAssrlHTTLLDI-----------TDPQNVQQVAKW 95
Cdd:cd05338   7 FVTGASRGIGRAIALRLAKAGATVVvaaktASEGDNGSAKSLPGTI----EETAEEIeaaggqalpivVDVRDEDQVRAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  96 VKTRVGETG-LFGLVNNAGVA--GIIGPTPWLTQDDFQRvlsVNTLGP-IGVTLALLPLLQQARGRVVNITSVLGRIAAN 171
Cdd:cd05338  83 VEATVDQFGrLDILVNNAGAIwlSLVEDTPAKRFDLMQR---VNLRGTyLLSQAALPHMVKAGQGHILNISPPLSLRPAR 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19549323 172 GG-GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPgffRTPVTNLESLESTLKACWARL-PPAIQAHYGEAFL 242
Cdd:cd05338 160 GDvAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWP---STAIETPAATELSGGSDPARArSPEILSDAVLAIL 229
PRK07035 PRK07035
SDR family oxidoreductase;
32-210 5.64e-04

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 40.77  E-value: 5.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   32 FITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMASS------RLHTTLLDITDPQNVQQVAKWVKTRVGEtgL 105
Cdd:PRK07035  12 LVTGASRGIGEAIAKLLAQQGAHVI---VSSRKLDGCQAVADAivaaggKAEALACHIGEMEQIDALFAHIRERHGR--L 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  106 FGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGV-TLALLPLLQQARGRVVNITSVLGRIAANGGG-YCVSKFGLE 183
Cdd:PRK07035  87 DILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMsVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGiYSITKAAVI 166

                        170       180
                 ....*....|....*....|....*..
gi 19549323  184 AFSDSLRRDMAPFGVQVSIVEPGFFRT 210
Cdd:PRK07035 167 SMTKAFAKECAPFGIRVNALLPGLTDT 193
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 31-213 8.33e-04

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 40.17  E-value: 8.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  31 IFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEdlqqmassrlhttlLDITDPQNVQQVAKWVKTRVGEtGLFGLVN 110
Cdd:cd05328   2 IVITGAASGIGAATAELLEDAGHTVIGIDLREADVI--------------ADLSTPEGRAAAIADVLARCSG-VLDGLVN 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 111 NAGVAgiiGPTPwltQDDfqrVLSVNTLGPIGVTLALL-PLLQQARGRVVNITSVLG----------------------- 166
Cdd:cd05328  67 CAGVG---GTTV---AGL---VLKVNYFGLRALMEALLpRLRKGHGPAAVVVSSIAGagwaqdklelakalaagtearav 137

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19549323 167 RIAANGG-----GYCVSKfglEAFSDSLRRdMAP-----FGVQVSIVEPGFFRTPVT 213
Cdd:cd05328 138 ALAEHAGqpgylAYAGSK---EALTVWTRR-RAAtwlygAGVRVNTVAPGPVETPIL 190
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 33-211 9.61e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 40.40  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGCLTPSG-AEDLQQMASSRLHTTLL---DITDPQNVQQ-VAKWVKTrvgetglFG 107
Cdd:PRK06701  51 ITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEdANETKQRVEKEGVKCLLipgDVSDEAFCKDaVEETVRE-------LG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  108 ----LVNNAG----VAGIigptPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQArGRVVNITSVLGrIAANGG--GYCV 177
Cdd:PRK06701 124 rldiLVNNAAfqypQQSL----EDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-SAIINTGSITG-YEGNETliDYSA 197

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19549323  178 SKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTP 211
Cdd:PRK06701 198 TKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTP 231
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 33-206 1.01e-03

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 40.00  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  33 ITGCDSGFGRLLALQLDQKGFQVLAGCLtpsGAEDLQQMASSRLHTTLLD---------ITDPQNVQQVAKWVKTRVGEt 103
Cdd:cd05353  10 VTGAGGGLGRAYALAFAERGAKVVVNDL---GGDRKGSGKSSSAADKVVDeikaaggkaVANYDSVEDGEKIVKTAIDA- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323 104 glFG----LVNNAGV------AGIigptpwlTQDDFQRVLSVNTLGPIGVTLALLPLLQQAR-GRVVNITSVLGrIAANG 172
Cdd:cd05353  86 --FGrvdiLVNNAGIlrdrsfAKM-------SEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAG-LYGNF 155

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19549323 173 G--GYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:cd05353 156 GqaNYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 75-206 2.43e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 38.90  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   75 RLHTTLLDITDPQNVQQVAKWVKTRVGETGLfgLVNNAGVAGIiGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQA 154
Cdd:PRK12748  68 RCEHMEIDLSQPYAPNRVFYAVSERLGDPSI--LINNAAYSTH-TRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGK 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19549323  155 R-GRVVNITS------VLGRIAangggYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPG 206
Cdd:PRK12748 145 AgGRIINLTSgqslgpMPDELA-----YAATKGAIEAFTKSLAPELAEKGITVNAVNPG 198
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 33-210 2.89e-03

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 38.55  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQVLAGclTPSGAEDLQQM------ASSRLHTTLLDITDPQNVQQVAKWVKTRVGetGLF 106
Cdd:PRK06077  11 VTGSGRGIGRAIAVRLAKEGSLVVVN--AKKRAEEMNETlkmvkeNGGEGIGVLADVSTREGCETLAKATIDRYG--VAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323  107 GLVNNAGVaGIIgpTPWLTQDD--FQRVLSVNTLGPIGVTLALLPLLQQArGRVVNITSVLGRIAANG-GGYCVSKFGLE 183
Cdd:PRK06077  87 ILVNNAGL-GLF--SPFLNVDDklIDKHISTDFKSVIYCSQELAKEMREG-GAIVNIASVAGIRPAYGlSIYGAMKAAVI 162

                        170       180
                 ....*....|....*....|....*..
gi 19549323  184 AFSDSLRRDMAPfGVQVSIVEPGFFRT 210
Cdd:PRK06077 163 NLTKYLALELAP-KIRVNAIAPGFVKT 188
PRK07856 PRK07856
SDR family oxidoreductase;
82-210 4.71e-03

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 37.99  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   82 DITDPQnvqQVAKWVKTRVGETG-LFGLVNNAGVAgiigptPWLTQDD-----FQRVLSVNTLGPIGVTLA--LLPLLQQ 153
Cdd:PRK07856  55 DVRDPD---QVAALVDAIVERHGrLDVLVNNAGGS------PYALAAEasprfHEKIVELNLLAPLLVAQAanAVMQQQP 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19549323  154 ARGRVVNITSVLGRIAANG-GGYCVSKFGLEAFSDSLRRDMAPfGVQVSIVEPGFFRT 210
Cdd:PRK07856 126 GGGSIVNIGSVSGRRPSPGtAAYGAAKAGLLNLTRSLAVEWAP-KVRVNAVVVGLVRT 182
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 31-116 6.13e-03

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 37.74  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   31 IFITGCDSGFGRLLALQLDQKGFQVLagcLTPSGAEDLQQMAS------SRLHTTLLDITDPQNVQQVAKWVKTRVGEtg 104
Cdd:PRK07677   4 VIITGGSSGMGKAMAKRFAEEGANVV---ITGRTKEKLEEAKLeieqfpGQVLTVQMDVRNPEDVQKMVEQIDEKFGR-- 78

                         90
                 ....*....|..
gi 19549323  105 LFGLVNNAgvAG 116
Cdd:PRK07677  79 IDALINNA--AG 88
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 33-170 7.16e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 37.70  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19549323   33 ITGCDSGFGRLLALQLDQKGFQV-LAGCLTPSGAEDLQQMASSRLHTTL----LDITDPQNVQQVAKWVKTRVGETGLfg 107
Cdd:PRK06197  21 VTGANTGLGYETAAALAAKGAHVvLAVRNLDKGKAAAARITAATPGADVtlqeLDLTSLASVRAAADALRAAYPRIDL-- 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19549323  108 LVNNAGVagiIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARG-RVVNITSVLGRIAA 170
Cdd:PRK06197  99 LINNAGV---MYTPKQTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGsRVVTVSSGGHRIRA 159
 
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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