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Conserved domains on  [gi|24640547|ref|NP_572466|]
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sniffer, isoform A [Drosophila melanogaster]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143154)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19011750|19011748|12604210|19027726|20423462
SCOP:  4000029

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 4-247 9.54e-96

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: 279.95  E-value: 9.54e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRnfDAYDKLVADIEGVTKDQGL 83
Cdd:cd05325   1 VLITGASRGIGLELVRQLLA--RGNNTVIATCRDPSAATELAALGASHSRLHILELDVT--DEIAESAEAVAERLGDAGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvgRAAIINMSSILGSIQGNTD 163
Cdd:cd05325  77 DVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGA-----------RAKIINISSRVGSIGDNTS 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSA----PLDVPTSTGQIVQTISKLGEKQNGGFVN 239
Cdd:cd05325 146 GGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAknkgPITPEESVAGLLKVIDNLNEEDSGKFLD 225


                ....*...
gi 24640547 240 YDGTPLAW 247
Cdd:cd05325 226 YDGTEIPW 233
 
Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 4-247 9.54e-96

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: 279.95  E-value: 9.54e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRnfDAYDKLVADIEGVTKDQGL 83
Cdd:cd05325   1 VLITGASRGIGLELVRQLLA--RGNNTVIATCRDPSAATELAALGASHSRLHILELDVT--DEIAESAEAVAERLGDAGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvgRAAIINMSSILGSIQGNTD 163
Cdd:cd05325  77 DVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGA-----------RAKIINISSRVGSIGDNTS 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSA----PLDVPTSTGQIVQTISKLGEKQNGGFVN 239
Cdd:cd05325 146 GGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAknkgPITPEESVAGLLKVIDNLNEEDSGKFLD 225


                ....*...
gi 24640547 240 YDGTPLAW 247
Cdd:cd05325 226 YDGTEIPW 233
PRK08177 PRK08177
SDR family oxidoreductase;
1-247 8.18e-51

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 165.20  E-value: 8.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAknhsNIHILEIDLRNFDAYDKLVADIEGVTKD 80
Cdd:PRK08177   1 KRTALIIGASRGLGLGLVDRLL---ERGWQVTATVRGPQQDTALQALP----GVHIEKLDMNDPASLDQLLQRLQGQRFD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 qglnVLFNNAGIA-PKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpmgvGRAAIINMSSILGSIQ 159
Cdd:PRK08177  74 ----LLFVNAGISgPAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRP------------GQGVLAFMSSQLGSVE 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  160 GNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISKLGEKQNGGFVN 239
Cdd:PRK08177 138 LPDGGEMPLYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMGGDNAPLDVETSVKGLVEQIEAASGKGGHRFID 217


                 ....*...
gi 24640547  240 YDGTPLAW 247
Cdd:PRK08177 218 YQGETLPW 225
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-212 1.33e-39

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 137.31  E-value: 1.33e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIEGvtKDQG 82
Cdd:COG0300   8 VLITGASSGIGRALARALA---ARGARVVLVARDAERLEALaAELRAAGARVEVVALDVTDPDAVAALAEAVLA--RFGP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 LNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIQGNt 162
Cdd:COG0300  83 IDVLVNNAGVGG-GGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRAR-----------GRGRIVNVSSVAGLRGLP- 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24640547 163 dgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:COG0300 150 --GMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGA 197
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 34-207 2.17e-26

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: 102.51  E-value: 2.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    34 TCRNREQAKELEDLAKNHSNiHILEIDLRNFDAYDKLVADIegVTKDQGLNVLFNNAGIAPK-SARITAVRSQELLDTLQ 112
Cdd:pfam13561  26 TDLNEALAKRVEELAEELGA-AVLPCDVTDEEQVEALVAAA--VEKFGRLDILVNNAGFAPKlKGPFLDTSREDFDRALD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   113 TNTVVPIMLAKACLPLLKKaakanesqpmgvgRAAIINMSSIlGSIQGNTDGGMYAyrTSKSALNAATKSLSVDLYPQRI 192
Cdd:pfam13561 103 VNLYSLFLLAKAALPLMKE-------------GGSIVNLSSI-GAERVVPNYNAYG--AAKAALEALTRYLAVELGPRGI 166

                         170
                  ....*....|....*
gi 24640547   193 MCVSLHPGWVKTDMG 207
Cdd:pfam13561 167 RVNAISPGPIKTLAA 181
 
Name Accession Description Interval E-value
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 4-247 9.54e-96

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: 279.95  E-value: 9.54e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRnfDAYDKLVADIEGVTKDQGL 83
Cdd:cd05325   1 VLITGASRGIGLELVRQLLA--RGNNTVIATCRDPSAATELAALGASHSRLHILELDVT--DEIAESAEAVAERLGDAGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvgRAAIINMSSILGSIQGNTD 163
Cdd:cd05325  77 DVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGA-----------RAKIINISSRVGSIGDNTS 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSA----PLDVPTSTGQIVQTISKLGEKQNGGFVN 239
Cdd:cd05325 146 GGWYSYRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPFAknkgPITPEESVAGLLKVIDNLNEEDSGKFLD 225


                ....*...
gi 24640547 240 YDGTPLAW 247
Cdd:cd05325 226 YDGTEIPW 233
PRK08177 PRK08177
SDR family oxidoreductase;
1-247 8.18e-51

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 165.20  E-value: 8.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAknhsNIHILEIDLRNFDAYDKLVADIEGVTKD 80
Cdd:PRK08177   1 KRTALIIGASRGLGLGLVDRLL---ERGWQVTATVRGPQQDTALQALP----GVHIEKLDMNDPASLDQLLQRLQGQRFD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 qglnVLFNNAGIA-PKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpmgvGRAAIINMSSILGSIQ 159
Cdd:PRK08177  74 ----LLFVNAGISgPAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRP------------GQGVLAFMSSQLGSVE 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  160 GNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISKLGEKQNGGFVN 239
Cdd:PRK08177 138 LPDGGEMPLYKASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDMGGDNAPLDVETSVKGLVEQIEAASGKGGHRFID 217


                 ....*...
gi 24640547  240 YDGTPLAW 247
Cdd:PRK08177 218 YQGETLPW 225
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 5-247 2.35e-47

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: 156.63  E-value: 2.35e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvTKDQGL 83
Cdd:cd05324   4 LVTGANRGIGFEIVRQLAK--SGPGTVILTARDVERGQAaVEKLRAEGLSVRFHQLDVTDDASIEAAADFVE--EKYGGL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSILGSIQgntd 163
Cdd:cd05324  80 DILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGR-----------IVNVSSGLGSLT---- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 164 ggmYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISKL-GEKQNGGFVnYDG 242
Cdd:cd05324 145 ---SAYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPKTPEEGAETPVYLALLPpDGEPTGKFF-SDK 220


                ....*
gi 24640547 243 TPLAW 247
Cdd:cd05324 221 KVVPW 225
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 4-212 2.82e-41

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: 141.27  E-value: 2.82e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGvtKDQGL 83
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGA---KVVLADRNEEALAELAAIEALGGNAVAVQADVSDEEDVEALVEEALE--EFGRL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSaRITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIQGntd 163
Cdd:cd05233  76 DILVNNAGIARPG-PLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQ-----------GGGRIVNISSVAGLRPL--- 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:cd05233 141 PGQAAYAASKAALEGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGP 189
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
4-212 1.33e-39

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 137.31  E-value: 1.33e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIEGvtKDQG 82
Cdd:COG0300   8 VLITGASSGIGRALARALA---ARGARVVLVARDAERLEALaAELRAAGARVEVVALDVTDPDAVAALAEAVLA--RFGP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 LNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIQGNt 162
Cdd:COG0300  83 IDVLVNNAGVGG-GGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRAR-----------GRGRIVNVSSVAGLRGLP- 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24640547 163 dgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:COG0300 150 --GMAAYAASKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGA 197
PRK06953 PRK06953
SDR family oxidoreductase;
1-247 9.59e-38

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 131.73  E-value: 9.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKnhsniHILEIDLRNFDAYDKLVADIEGvtkd 80
Cdd:PRK06953   1 MKTVLIVGASRGIGREFVRQYR---ADGWRVIATARDAAALAALQALGA-----EALALDVADPASVAGLAWKLDG---- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QGLNVLFNNAGI-APKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvGRAAIInmSSILGSIQ 159
Cdd:PRK06953  69 EALDAAVYVAGVyGPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAG----------GVLAVL--SSRMGSIG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  160 GNTDGGMYAYRTSKSALNAATKSLSVDlYPQRImCVSLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISKLGEKQNGGFVN 239
Cdd:PRK06953 137 DATGTTGWLYRASKAALNDALRAASLQ-ARHAT-CIALHPGWVRTDMGGAQAALDPAQSVAGMRRVIAQATRRDNGRFFQ 214


                 ....*...
gi 24640547  240 YDGTPLAW 247
Cdd:PRK06953 215 YDGVELSW 222
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 4-206 7.04e-36

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: 127.59  E-value: 7.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNlpqppQ--HLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIegVTKD 80
Cdd:COG1028   9 ALVTGGSSGIGRAIARALAA-----EgaRVVITDRDAEALEAAaAELRAAGGRALAVAADVTDEAAVEALVAAA--VAAF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  81 QGLNVLFNNAGIAPKsARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGsIQG 160
Cdd:COG1028  82 GRLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRER-----------GGGRIVNISSIAG-LRG 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 24640547 161 NtdGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:COG1028 149 S--PGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPM 192
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 2-212 6.46e-33

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 119.64  E-value: 6.46e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   2 NSILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREqakELEDLAKNH-SNIHILEIDLRNFDAYDKLVADIEGvtKD 80
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGY---RVIATARNPD---KLESLGELLnDNLEVLELDVTDEESIKAAVKEVIE--RF 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  81 QGLNVLFNNAGIAPKSArITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKanesqpmgvGRaaIINMSSILGSIqg 160
Cdd:cd05374  73 GRIDVLVNNAGYGLFGP-LEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGS---------GR--IVNVSSVAGLV-- 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24640547 161 nTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:cd05374 139 -PTPFLGPYCASKAALEALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAG 189
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 4-215 9.48e-29

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: 108.73  E-value: 9.48e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpqppQ---HLFTTCRNREqakELEDLAKNH-SNIHILEIDLRNFDAYDKLVADIegVTK 79
Cdd:COG4221   8 ALITGASSGIGAATARALA------AagaRVVLAARRAE---RLEALAAELgGRALAVPLDVTDEAAVEAAVAAA--VAE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  80 DQGLNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGsIQ 159
Cdd:COG4221  77 FGRLDVLVNNAGVAL-LGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRAR-----------GSGHIVNISSIAG-LR 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24640547 160 GNTDGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDV 215
Cdd:COG4221 144 PYPGGAVYA--ATKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDA 197
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 4-223 4.92e-27

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: 104.03  E-value: 4.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEdlAKNHSNIHILEIDLRNFDAYDKLVADIEGVTkdqgl 83
Cdd:cd05354   6 VLVTGANRGIGKAFVESLLA--HGAKKVYAAVRDPGSAAHLV--AKYGDKVVPLRLDVTDPESIKAAAAQAKDVD----- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 nVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIqgnTD 163
Cdd:cd05354  77 -VVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKAN-----------GGGAIVNLNSVASLK---NF 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMG-GSSAPLDVPTSTGQIV 223
Cdd:cd05354 142 PAMGTYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAaGAGGPKESPETVAEAV 202
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 34-207 2.17e-26

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: 102.51  E-value: 2.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    34 TCRNREQAKELEDLAKNHSNiHILEIDLRNFDAYDKLVADIegVTKDQGLNVLFNNAGIAPK-SARITAVRSQELLDTLQ 112
Cdd:pfam13561  26 TDLNEALAKRVEELAEELGA-AVLPCDVTDEEQVEALVAAA--VEKFGRLDILVNNAGFAPKlKGPFLDTSREDFDRALD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   113 TNTVVPIMLAKACLPLLKKaakanesqpmgvgRAAIINMSSIlGSIQGNTDGGMYAyrTSKSALNAATKSLSVDLYPQRI 192
Cdd:pfam13561 103 VNLYSLFLLAKAALPLMKE-------------GGSIVNLSSI-GAERVVPNYNAYG--AAKAALEALTRYLAVELGPRGI 166

                         170
                  ....*....|....*
gi 24640547   193 MCVSLHPGWVKTDMG 207
Cdd:pfam13561 167 RVNAISPGPIKTLAA 181
PRK08264 PRK08264
SDR family oxidoreductase;
4-226 2.40e-25

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 99.58  E-value: 2.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNreqakeLEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTkdqgl 83
Cdd:PRK08264   9 VLVTGANRGIGRAFVEQLLA--RGAAKVYAAARD------PESVTDLGPRVVPLQLDVTDPASVAAAAEAASDVT----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 nVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIqgnTD 163
Cdd:PRK08264  76 -ILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAAN-----------GGGAIVNVLSVLSWV---NF 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640547  164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMggsSAPLDVP-TSTGQIVQTI 226
Cdd:PRK08264 141 PNLGTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM---AAGLDAPkASPADVARQI 201
PRK12826 PRK12826
SDR family oxidoreductase;
5-208 2.93e-25

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 99.61  E-value: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADieGVTKDQGL 83
Cdd:PRK12826  10 LVTGAARGIGRAIAVRLAADGA---EVIVVDICGDDAAAtAELVEAAGGKARARQVDVRDRAALKAAVAA--GVEDFGRL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIAPKsARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSILGSIQGNtd 163
Cdd:PRK12826  85 DILVANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRA---------GGGR--IVLTSSVAGPRVGY-- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24640547  164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGG 208
Cdd:PRK12826 151 PGLAHYAASKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAG 195
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 4-212 1.75e-24

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 96.14  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547     4 ILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKELEDLAKNHS-NIHILEIDLRNFDAYDKLVADIegVTKDQG 82
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGA---KVVLVDRSEEKLEAVAKELGALGgKALFIQGDVTDRAQVKALVEQA--VERLGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    83 LNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSILGsIQGNT 162
Cdd:pfam00106  78 LDILVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGR-----------IVNISSVAG-LVPYP 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 24640547   163 DGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:pfam00106 145 GGSAYS--ASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELRE 192
PRK09009 PRK09009
SDR family oxidoreductase;
1-247 2.78e-23

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 93.97  E-value: 2.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNsILITGCNRGLGLGLVKALLNlPQPPQHLFTTCRNREQAKEledlaknHSNIHILEIDLRNFDAYDKLVADIEGvtkd 80
Cdd:PRK09009   1 MN-ILIVGGSGGIGKAMVKQLLE-RYPDATVHATYRHHKPDFQ-------HDNVQWHALDVTDEAEIKQLSEQFTQ---- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 qgLNVLFNNAGI------APKSArITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKAnesqpmgvgRAAIInmSSI 154
Cdd:PRK09009  68 --LDWLINCVGMlhtqdkGPEKS-LQALDADFFLQNITLNTLPSLLLAKHFTPKLKQSESA---------KFAVI--SAK 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  155 LGSIQGNTDGGMYAYRTSKSALNAATKSLSVDLypQRIM---CV-SLHPGWVKTDMggsSAPL--DVPT--------STG 220
Cdd:PRK09009 134 VGSISDNRLGGWYSYRASKAALNMFLKTLSIEW--QRSLkhgVVlALHPGTTDTAL---SKPFqqNVPKgklftpeyVAQ 208

                        250       260
                 ....*....|....*....|....*..
gi 24640547  221 QIVQTISKLGEKQNGGFVNYDGTPLAW 247
Cdd:PRK09009 209 CLLGIIANATPAQSGSFLAYDGETLPW 235
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 4-206 9.01e-23

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: 93.44  E-value: 9.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKE-LEDLAKN--HSNIHILEIDLRNFDAYDKLVADIegvtKD 80
Cdd:cd05327   4 VVITGANSGIGKETARELAKRGA---HVIIACRNEEKGEEaAAEIKKEtgNAKVEVIQLDLSSLASVRQFAEEF----LA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  81 QG--LNVLFNNAGIAPKSARITAvrsQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSIL--- 155
Cdd:cd05327  77 RFprLDILINNAGIMAPPRRLTK---DGFELQFAVNYLGHFLLTNLLLPVLKASAPSR-----------IVNVSSIAhra 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24640547 156 GSIQGNTD--------GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd05327 143 GPIDFNDLdlennkeySPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL 201
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 2-208 9.52e-23

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: 92.92  E-value: 9.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   2 NSILITGCNRGLGLGLVKALL---NlpqppqHLFTTCRNREQakeLEDLAKNHSNIHILEIDLRNFDAYDKLVADIegVT 78
Cdd:COG3967   6 NTILITGGTSGIGLALAKRLHargN------TVIITGRREEK---LEEAAAANPGLHTIVLDVADPASIAALAEQV--TA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  79 KDQGLNVLFNNAGIAPK-SARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesQPmgvgRAAIINMSSILgs 157
Cdd:COG3967  75 EFPDLNVLINNAGIMRAeDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKA-------QP----EAAIVNVSSGL-- 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24640547 158 iqGNTDGGMYA-YRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGG 208
Cdd:COG3967 142 --AFVPLAVTPtYSATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTG 191
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-206 1.40e-21

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 89.83  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIegVTK 79
Cdd:PRK05653   5 GKTALVTGASRGIGRAIALRLAADGA---KVVIYDSNEEAAEALaAELRAAGGEARVLVFDVSDEAAVRALIEAA--VEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   80 DQGLNVLFNNAGIAPKsARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSILGsIQ 159
Cdd:PRK05653  80 FGALDILVNNAGITRD-ALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKA---------RYGR--IVNISSVSG-VT 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640547  160 GNtdGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK05653 147 GN--PGQTNYSAAKAGVIGFTKALALELASRGITVNAVAPGFIDTDM 191
PRK07326 PRK07326
SDR family oxidoreductase;
5-223 4.45e-21

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 88.14  E-value: 4.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIegVTKDQGLN 84
Cdd:PRK07326  10 LITGGSKGIGFAIAEALL---AEGYKVAITARDQKELEEAAAELNNKGNVLGLAADVRDEADVQRAVDAI--VAAFGGLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpmgvGRAAIINMSSILGSiqgNTDG 164
Cdd:PRK07326  85 VLIANAGVG-HFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKR------------GGGYIINISSLAGT---NFFA 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640547  165 GMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDV-----PTSTGQIV 223
Cdd:PRK07326 149 GGAAYNASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDawkiqPEDIAQLV 212
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 36-222 1.25e-20

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 87.20  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   36 RNREQAKELED-LAKNHSNIHILEIDLRNFDAYDKLVADIegVTKDQGLNVLFNNAGIApKSARITAVRSQELLDTLQTN 114
Cdd:PRK05565  38 INEEAAQELLEeIKEEGGDAIAVKADVSSEEDVENLVEQI--VEKFGKIDILVNNAGIS-NFGLVTDMTDEEWDRVIDVN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  115 TVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGsIQGNTDGGmyAYRTSKSALNAATKSLSVDLYPQRIMC 194
Cdd:PRK05565 115 LTGVMLLTRYALPYMIKR-----------KSGVIVNISSIWG-LIGASCEV--LYSASKGAVNAFTKALAKELAPSGIRV 180

                        170       180
                 ....*....|....*....|....*...
gi 24640547  195 VSLHPGWVKTDMGGSSAPLDVPTSTGQI 222
Cdd:PRK05565 181 NAVAPGAIDTEMWSSFSEEDKEGLAEEI 208
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 4-206 2.30e-20

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: 86.26  E-value: 2.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELedLAKNHsNIHILEIDLRNFDAYDKLVADIEgvTKDQGL 83
Cdd:cd08932   3 ALVTGASRGIGIEIARALA---RDGYRVSLGLRNPEDLAAL--SASGG-DVEAVPYDARDPEDARALVDALR--DRFGRI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSARITAvrSQELLD-TLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIqgnT 162
Cdd:cd08932  75 DVLVHNAGIGRPTTLREG--SDAELEaHFSINVIAPAELTRALLPALREA-----------GSGRVVFLNSLSGKR---V 138

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24640547 163 DGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd08932 139 LAGNAGYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPM 182
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
1-206 5.80e-18

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 80.11  E-value: 5.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALLnlpQPPQHLFttCRNREQAKELEDLAK-NHSNIHILEIDLRNFDAYDKLVADI-EGVT 78
Cdd:PRK06924   1 MRYVIITGTSQGLGEAIANQLL---EKGTHVI--SISRTENKELTKLAEqYNSNLTFHSLDLQDVHELETNFNEIlSSIQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   79 KDQGLNV-LFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKAclpLLKKAAKANesqpmgvGRAAIINMSSilGS 157
Cdd:PRK06924  76 EDNVSSIhLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTST---FMKHTKDWK-------VDKRVINISS--GA 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24640547  158 IQgNTDGGMYAYRTSKSALNAATKSLSVD----LYPQRImcVSLHPGWVKTDM 206
Cdd:PRK06924 144 AK-NPYFGWSAYCSSKAGLDMFTQTVATEqeeeEYPVKI--VAFSPGVMDTNM 193
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 4-240 1.05e-17

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: 79.25  E-value: 1.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLPQPPQhLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTKDqgL 83
Cdd:cd05367   2 IILTGASRGIGRALAEELLKRGSPSV-VVLLARSEEPLQELKEELRPGLRVTTVKADLSDAAGVEQLLEAIRKLDGE--R 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKanesqpmgVGRaaIINMSSiLGSIQGNTd 163
Cdd:cd05367  79 DLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGL--------KKT--VVNVSS-GAAVNPFK- 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 164 gGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSlhPGWVKTDMG-----GSSAPLDVPT-----STGQIV---QTISKL- 229
Cdd:cd05367 147 -GWGLYCSSKAARDMFFRVLAAEEPDVRVLSYA--PGVVDTDMQreireTSADPETRSRfrslkEKGELLdpeQSAEKLa 223

                       250
                ....*....|....*.
gi 24640547 230 -----GEKQNGGFVNY 240
Cdd:cd05367 224 nllekDKFESGAHVDY 239
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 4-210 1.86e-17

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: 79.24  E-value: 1.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLpqpPQHLFTTCRNREQ--AKELEDLakNHSNIHILEIDLRNFDAYDKLVADIEGVTKDQ 81
Cdd:cd09805   3 VLITGCDSGFGNLLAKKLDSL---GFTVLAGCLTKNGpgAKELRRV--CSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAGIapksarITAVRSQELLDT------LQTNTVVPIMLAKACLPLLKKAAkanesqpmgvGRaaIINMSSIL 155
Cdd:cd09805  78 GLWGLVNNAGI------LGFGGDEELLPMddyrkcMEVNLFGTVEVTKAFLPLLRRAK----------GR--VVNVSSMG 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24640547 156 GSIQGNTDGgmyAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSS 210
Cdd:cd09805 140 GRVPFPAGG---AYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNS 191
PRK08219 PRK08219
SDR family oxidoreductase;
1-206 3.58e-16

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 74.97  E-value: 3.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALlnlpQPPQHLFTTCRNREQAKELEDlakNHSNIHILEIDLRNFDAYDKLVADIEGVTkd 80
Cdd:PRK08219   3 RPTALITGASRGIGAAIAREL----APTHTLLLGGRPAERLDELAA---ELPGATPFPVDLTDPEAIAAAVEQLGRLD-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 qglnVLFNNAGIAPKsARITAVRSQELLDTLQTNTVVPIMLAKACLPLLkKAAKanesqpmgvGRAAIINMSSILgsiqg 160
Cdd:PRK08219  74 ----VLVHNAGVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPAL-RAAH---------GHVVFINSGAGL----- 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640547  161 NTDGGMYAYRTSKSALNAATKSLSVDlYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK08219 134 RANPGWGSYAASKFALRALADALREE-EPGNVRVTSVHPGRTDTDM 178
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 4-206 3.69e-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: 75.09  E-value: 3.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNlpqPPQHLFTTCRNREQAKELEDLAKNHS-NIHILEIDLRNFDAYDKLVADIEgvtKDQG 82
Cdd:cd05347   8 ALVTGASRGIGFGIASGLAE---AGANIVINSRNEEKAEEAQQLIEKEGvEATAFTCDVSDEEAIKAAVEAIE---EDFG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 -LNVLFNNAGIA--PKSARITAvrsQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILgSIQ 159
Cdd:cd05347  82 kIDILVNNAGIIrrHPAEEFPE---AEWRDVIDVNLNGVFFVSQAVARHMIKQ-----------GHGKIINICSLL-SEL 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24640547 160 GNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd05347 147 GGP--PVPAYAASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEM 191
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 3-212 4.13e-16

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: 74.85  E-value: 4.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   3 SILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNreqAKELEDLAKN-HSNIHILEIDLRNFDAYDKLVADIEgvTKDQ 81
Cdd:cd08929   2 AALVTGASRGIGEATARLLH---AEGYRVGICARD---EARLAAAAAQeLEGVLGLAGDVRDEADVRRAVDAME--EAFG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpmgvGRAAIINMSSILGSiqgN 161
Cdd:cd08929  74 GLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRR------------GGGTIVNVGSLAGK---N 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24640547 162 TDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:cd08929 139 AFKGGAAYNASKFGLLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGSPEG 189
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 4-206 6.21e-16

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 74.46  E-value: 6.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADiegvTKDQ- 81
Cdd:PRK05557   8 ALVTGASRGIGRAIAERLAA--QGANVVINYASSEAGAEALvAEIGALGGKALAVQGDVSDAESVERAVDE----AKAEf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 -GLNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSILGSIqG 160
Cdd:PRK05557  82 gGVDILVNNAGIT-RDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQ---------RSGR--IINISSVVGLM-G 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640547  161 NTDGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK05557 149 NPGQANYA--ASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM 192
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 4-205 7.45e-16

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: 74.24  E-value: 7.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELED-LAKNHSN-IHILEIDLRNFDAYDKLVADIEGVTKDq 81
Cdd:cd05346   3 VLITGASSGIGEATARRFA---KAGAKLILTGRRAERLQELADeLGAKFPVkVLPLQLDVSDRESIEAALENLPEEFRD- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 gLNVLFNNAGIAPKSARITAVRSQELLDTLQTN---------TVVPIMLAKaclpllkkaakanesqpmgvGRAAIINMS 152
Cdd:cd05346  79 -IDILVNNAGLALGLDPAQEADLEDWETMIDTNvkgllnvtrLILPIMIAR--------------------NQGHIINLG 137

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547 153 SILGSiqgntdgGMYA----YRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:cd05346 138 SIAGR-------YPYAggnvYCATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVETE 187
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-224 9.22e-16

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 74.13  E-value: 9.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALLNLPQppqHLFTTCR-NREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVT 78
Cdd:PRK12825   6 GRVALVTGAARGLGRAIALRLARAGA---DVVVHYRsDEEAAEELvEAVEALGRRAQAVQADVTDKAALEAAVA--AAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   79 KDQGLNVLFNNAGIAPKsARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSILGSI 158
Cdd:PRK12825  81 RFGRIDILVNNAGIFED-KPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQ---------RGGR--IVNISSVAGLP 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640547  159 qGNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP-----LDVPTSTGQIVQ 224
Cdd:PRK12825 149 -GWP--GRSNYAAAKAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEeareaKDAETPLGRSGT 216
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 4-206 9.40e-16

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: 73.74  E-value: 9.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKELEDLAKNH-SNIHILEIDLRNFDAYDKLVADIEgvTKDQG 82
Cdd:cd05333   3 ALVTGASRGIGRAIALRLAAEGA---KVAVTDRSEEAAAETVEEIKALgGNAAALEADVSDREAVEALVEKVE--AEFGP 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 LNVLFNNAGIApKSARITAVRSQELLDTLQTNTvvpimlaKACLPLLKKAAKANESQpmGVGRaaIINMSSILGSIqGNt 162
Cdd:cd05333  78 VDILVNNAGIT-RDNLLMRMSEEDWDAVINVNL-------TGVFNVTQAVIRAMIKR--RSGR--IINISSVVGLI-GN- 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24640547 163 dGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd05333 144 -PGQANYAASKAGVIGFTKSLAKELASRGITVNAVAPGFIDTDM 186
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 2-209 1.36e-15

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: 73.11  E-value: 1.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   2 NSILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQakeLEDLAKNHSNIHILEIDLRNFDAYDKLVadiEGVTKD- 80
Cdd:cd05370   6 NTVLITGGTSGIGLALARKFLEAGN---TVIITGRREER---LAEAKKELPNIHTIVLDVGDAESVEALA---EALLSEy 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  81 QGLNVLFNNAGIA-PKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKanesqpmgvgrAAIINMSSILGSIq 159
Cdd:cd05370  77 PNLDILINNAGIQrPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPE-----------ATIVNVSSGLAFV- 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24640547 160 gnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGS 209
Cdd:cd05370 145 --PMAANPVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEE 192
FabG-like PRK07231
SDR family oxidoreductase;
3-226 1.73e-15

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 73.33  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQG 82
Cdd:PRK07231   7 VAIVTGASSGIGEGIARRFA---AEGARVVVTDRNEEAAERVAAEILAGGRAIAVAADVSDEADVEAAVA--AALERFGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKAclpllkkAAKANesqpMGVGRAAIINMSSIlGSIQGNt 162
Cdd:PRK07231  82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQA-------AVPAM----RGEGGGAIVNVAST-AGLRPR- 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640547  163 dGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDVPTSTGQIVQTI 226
Cdd:PRK07231 149 -PGLGWYNASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTPENRAKFLATI 211
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-206 3.13e-15

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 72.30  E-value: 3.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLnlpqppqhlfttcrnrEQ-----AKELEDLAKNHSNIHILEIDLRnfDAYDKLVADIEGVt 78
Cdd:PRK06550   8 VLITGAASGIGLAQARAFL----------------AQgaqvyGVDKQDKPDLSGNFHFLQLDLS--DDLEPLFDWVPSV- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   79 kdqglNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSI 158
Cdd:PRK06550  69 -----DILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLER-----------KSGIIINMCSIASFV 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640547  159 QGntdGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK06550 133 AG---GGGAAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPM 177
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 3-210 3.84e-15

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: 72.44  E-value: 3.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   3 SILITGCNRGLGLGLvkALLnLPQPPQHLFTTCRNREQ----AKELEDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVT 78
Cdd:cd05364   5 VAIITGSSSGIGAGT--AIL-FARLGARLALTGRDAERleetRQSCLQAGVSEKKILLVVADLTEEEGQDRIIS--TTLA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  79 KDQGLNVLFNNAGIAPKSaRITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvgRAAIINMSSILGSI 158
Cdd:cd05364  80 KFGRLDILVNNAGILAKG-GGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT------------KGEIVNVSSVAGGR 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24640547 159 QgnTDGGMYaYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSS 210
Cdd:cd05364 147 S--FPGVLY-YCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRM 195
PRK09072 PRK09072
SDR family oxidoreductase;
3-206 5.56e-15

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 72.28  E-value: 5.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvtKDQG 82
Cdd:PRK09072   7 RVLLTGASGGIGQALAEALAAAGA---RLLLVGRNAEKLEALAARLPYPGRHRWVVADLTSEAGREAVLARAR---EMGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIqgnt 162
Cdd:PRK09072  81 INVLINNAGVN-HFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQ-----------PSAMVVNVGSTFGSI---- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640547  163 dG--GMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK09072 145 -GypGYASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 1-211 6.80e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 72.26  E-value: 6.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKNHSniHILEIDLRNFDAYDKLVADIEgvTKD 80
Cdd:PRK06180   4 MKTWLITGVSSGFGRALAQAAL---AAGHRVVGTVRSEAARADFEALHPDRA--LARLLDVTDFDAIDAVVADAE--ATF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QGLNVLFNNAGIAPKSA----RITAVRSQelldtLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILG 156
Cdd:PRK06180  77 GPIDVLVNNAGYGHEGAieesPLAEMRRQ-----FEVNVFGAVAMTKAVLPGMRAR-----------RRGHIVNITSMGG 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24640547  157 SIqgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSA 211
Cdd:PRK06180 141 LI---TMPGIGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRTDWAGRSM 192
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 4-206 8.97e-15

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: 71.35  E-value: 8.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNREQAKELEdlakNHSNIHILEIDLRNFDAYDKLVADIEGVtkdqgl 83
Cdd:cd05368   5 ALITAAAQGIGRAIALAF---AREGANVIATDINEEKLKELE----RGPGITTRVLDVTDKEQVAALAKEEGRI------ 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSILGSIQGntD 163
Cdd:cd05368  72 DVLFNCAGFVH-HGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGS-----------IINMSSVASSIKG--V 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd05368 138 PNRFVYSTTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPS 180
PRK06914 PRK06914
SDR family oxidoreductase;
5-205 1.03e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 71.59  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLglvKALLNLPQPPQHLFTTCRNREQAKELEDLAKNHS---NIHILEIDLRNFDAydklVADIEGVTKDQ 81
Cdd:PRK06914   7 IVTGASSGFGL---LTTLELAKKGYLVIATMRNPEKQENLLSQATQLNlqqNIKVQQLDVTDQNS----IHNFQLVLKEI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 G-LNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIqg 160
Cdd:PRK06914  80 GrIDLLVNNAGYA-NGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQ-----------KSGKIINISSISGRV-- 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640547  161 ntdG--GMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:PRK06914 146 ---GfpGLSPYVSSKYALEGFSESLRLELKPFGIDVALIEPGSYNTN 189
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 4-238 1.61e-14

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: 71.03  E-value: 1.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNlpQPPQHLFttCRNRE---QAKELEDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKD 80
Cdd:cd08933  12 VIVTGGSRGIGRGIVRAFVE--NGAKVVF--CARGEaagQALESELNRAGPGSCKFVPCDVTKEEDIKTLIS--VTVERF 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  81 QGLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvgRAAIINMSSILGSIqG 160
Cdd:cd08933  86 GRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKS------------QGNIINLSSLVGSI-G 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 161 NTDGGmyAYRTSKSALNAATKSLSVD--LYPQRIMCVSlhPGWVKTDM-GGSSAPLDVPTST---GQIVQTISKLGEKQN 234
Cdd:cd08933 153 QKQAA--PYVATKGAITAMTKALAVDesRYGVRVNCIS--PGNIWTPLwEELAAQTPDTLATikeGELAQLLGRMGTEAE 228


                ....
gi 24640547 235 GGFV 238
Cdd:cd08933 229 SGLA 232
PRK07069 PRK07069
short chain dehydrogenase; Validated
 58-206 5.73e-14

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 69.35  E-value: 5.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   58 EIDLRNFDAYDKLVAdiEGVTKDQGLNVLFNNAGIapksARITAVRS--QELLDTLQTNTVVPIML-AKACLPLLKkaak 134
Cdd:PRK07069  57 VQDVTDEAQWQALLA--QAADAMGGLSVLVNNAGV----GSFGAIEQieLDEWRRVMAINVESIFLgCKHALPYLR---- 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640547  135 anESQPmgvgrAAIINMSSILGSIQGNTdggMYAYRTSKSALNAATKSLSVDLYPQR--IMCVSLHPGWVKTDM 206
Cdd:PRK07069 127 --ASQP-----ASIVNISSVAAFKAEPD---YTAYNASKAAVASLTKSIALDCARRGldVRCNSIHPTFIRTGI 190
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 3-206 6.59e-14

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 69.32  E-value: 6.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREqakELEDLAKNH--SNIHILEIDLRNFDAYDKLVADIegVTKD 80
Cdd:PRK12829  13 RVLVTGGASGIGRAIAEAFA---EAGARVHVCDVSEA---ALAATAARLpgAKVTATVADVADPAQVERVFDTA--VERF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QGLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKkaakanESQPMGVgraaIINMSSILGsIQG 160
Cdd:PRK12829  85 GGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLK------ASGHGGV----IIALSSVAG-RLG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640547  161 ntdggmYAYRT----SKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK12829 154 ------YPGRTpyaaSKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPR 197
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 4-206 1.03e-13

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: 68.56  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQ----AKELEDLAknhsniHILEIDLRNFDAYDKLVADIEgvTK 79
Cdd:cd05341   8 AIVTGGARGLGLAHARLLV---AEGAKVVLSDILDEEgqaaAAELGDAA------RFFHLDVTDEDGWTAVVDTAR--EA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  80 DQGLNVLFNNAGIA-PKSarITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSI 158
Cdd:cd05341  77 FGRLDVLVNNAGILtGGT--VETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEA-----------GGGSIINMSSIEGLV 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24640547 159 qgnTDGGMYAYRTSKSALNAATKSLSVDLYPQ--RIMCVSLHPGWVKTDM 206
Cdd:cd05341 144 ---GDPALAAYNASKGAVRGLTKSAALECATQgyGIRVNSVHPGYIYTPM 190
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 4-204 3.77e-13

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: 67.10  E-value: 3.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLPQPPQHLFTTCRNREQAKELEDLAKNH--SNIHILEIDLRNfdayDKLVADIEGVTKDQ 81
Cdd:cd09806   3 VLITGCSSGIGLHLAVRLASDPSKRFKVYATMRDLKKKGRLWEAAGALagGTLETLQLDVCD----SKSVAAAVERVTER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAG---IAPksarITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpMGVGRaaIINMSSILGsI 158
Cdd:cd09806  79 HVDVLVCNAGvglLGP----LEALSEDAMASVFDVNVFGTVRMLQAFLPDMKR---------RGSGR--ILVTSSVGG-L 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 24640547 159 QGNTDGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:cd09806 143 QGLPFNDVYC--ASKFALEGLCESLAVQLLPFNVHLSLIECGPVHT 186
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 4-214 3.96e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 66.67  E-value: 3.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKAL-------LNLPQPPQhlfttcRNREQAKELEDLAKNH-SNIHILEIDLRNFDAYDKLVADie 75
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLaadgadvIVLDIHPM------RGRAEADAVAAGIEAAgGKALGLAFDVRDFAATRAALDA-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   76 GVTKDQGLNVLFNNAGIAPKSArITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKAnesqpmgvGRaaIINMSSIL 155
Cdd:PRK12827  81 GVEEFGRLDILVNNAGIATDAA-FAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRG--------GR--IVNIASVA 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24640547  156 GsIQGNtdGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLD 214
Cdd:PRK12827 150 G-VRGN--RGQVNYAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTE 205
PRK06124 PRK06124
SDR family oxidoreductase;
5-205 4.02e-13

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 67.05  E-value: 4.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKAllnLPQPPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVtkDQGL 83
Cdd:PRK06124  15 LVTGSARGLGFEIARA---LAGAGAHVLVNGRNAATLEAaVAALRAAGGAAEALAFDIADEEAVAAAFARIDAE--HGRL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGiapksAR----ITAVRSQELLDTLQTNTVVPIMLAkaclpllKKAAKANESQpmGVGRaaIINMSSILGSIq 159
Cdd:PRK06124  90 DILVNNVG-----ARdrrpLAELDDAAIRALLETDLVAPILLS-------RLAAQRMKRQ--GYGR--IIAITSIAGQV- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640547  160 gnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:PRK06124 153 --ARAGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATE 196
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 4-200 4.51e-13

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 66.74  E-value: 4.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIegVTKDQGL 83
Cdd:cd08942   9 VLVTGGSRGIGRMIAQGFL---EAGARVIISARKAEACADAAEELSAYGECIAIPADLSSEEGIEALVARV--AERSDRL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGiAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANESqpmgvgrAAIINmssiLGSIQGNTD 163
Cdd:cd08942  84 DVLVNNAG-ATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATAENP-------ARVIN----IGSIAGIVV 151

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24640547 164 GGM--YAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPG 200
Cdd:cd08942 152 SGLenYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 5-204 5.42e-13

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: 66.32  E-value: 5.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALLNLpqpPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTkDQGL 83
Cdd:cd05329  10 LVTGGTKGIGYAIVEELAGL---GAEVYTCARNQKELDEcLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHF-GGKL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIA-PKSAriTAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSILGSIQGNT 162
Cdd:cd05329  86 NILVNNAGTNiRKEA--KDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGN-----------IVFISSVAGVIAVPS 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24640547 163 dGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:cd05329 153 -GAPYG--ATKGALNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 5-201 7.10e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 66.19  E-value: 7.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpqPPQHLFTTCRNREQAKELEdlAKNHSNIHILEIDLRNFDAYDKLVADIegVTKDQGLN 84
Cdd:PRK08265  10 IVTGGATLIGAAVARALVA---AGARVAIVDIDADNGAAVA--ASLGERARFIATDITDDAAIERAVATV--VARFGRVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNA------GIApkSARitavrsQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpmgvGRAAIINMSSILGSI 158
Cdd:PRK08265  83 ILVNLActylddGLA--SSR------ADWLAALDVNLVSAAMLAQAAHPHLAR------------GGGAIVNFTSISAKF 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24640547  159 qGNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGW 201
Cdd:PRK08265 143 -AQT--GRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGW 182
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 4-228 7.20e-13

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 65.81  E-value: 7.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKN---HSNIHILEID--LRNFDAYDKLVADIEGvt 78
Cdd:cd05350   1 VLITGASSGIGRALAREFA---KAGYNVALAARRTDRLDELKAELLNpnpSVEVEILDVTdeERNQLVIAELEAELGG-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  79 kdqgLNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSI 158
Cdd:cd05350  76 ----LDLVIINAGVG-KGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAK-----------GRGHLVLISSVAALR 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640547 159 qgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP----LDVPTSTGQIVQTISK 228
Cdd:cd05350 140 ---GLPGAAAYSASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANMFTmpflMSVEQAAKRIYKAIKK 210
PRK08267 PRK08267
SDR family oxidoreductase;
1-206 9.07e-13

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 66.11  E-value: 9.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCnrGLGLGLVKALLnlpqppqhlF--------TTCRNREQAKELEdLAKNHSNIHILEIDLRNFDAYDKLVA 72
Cdd:PRK08267   1 MKSIFITGA--ASGIGRATALL---------FaaegwrvgAYDINEAGLAALA-AELGAGNAWTGALDVTDRAAWDAALA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   73 DIEGVTkDQGLNVLFNNAGIaPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKAnesqpmgvgraAIINMS 152
Cdd:PRK08267  69 DFAAAT-GGRLDVLFNNAGI-LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGA-----------RVINTS 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547  153 S---ILGSiqgntdGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK08267 136 SasaIYGQ------PGLAVYSATKFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAM 186
PRK06484 PRK06484
short chain dehydrogenase; Validated
 4-206 1.49e-12

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 66.41  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVkallnlpqppqHLFTTCRNREQA--KELEDLAKNHSNI----HILEIDLRNFDAYDKLVADIEgv 77
Cdd:PRK06484   8 VLVTGAAGGIGRAAC-----------QRFARAGDQVVVadRNVERARERADSLgpdhHALAMDVSDEAQIREGFEQLH-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   78 tKDQG-LNVLFNNAGIAPKSARITAVRSQELLDTLQT-NTVVPIMLAKACLPLLKKAAKAnesqpmgvgrAAIINMSSIL 155
Cdd:PRK06484  75 -REFGrIDVLVNNAGVTDPTMTATLDTTLEEFARLQAiNLTGAYLVAREALRLMIEQGHG----------AAIVNVASGA 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24640547  156 GsIQGNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK06484 144 G-LVALP--KRTAYSASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQM 191
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 5-206 2.96e-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: 2.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNR--EQAKELeDLAKNHSNIHILEIDLRNfdaYDKLVADIEGVTKDQG 82
Cdd:cd05323   4 IITGGASGIGLATAKLLL---KKGAKVAILDRNEnpGAAAEL-QAINPKVKATFVQCDVTS---WEQLAAAFKKAIEKFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 -LNVLFNNAGIA-PKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakaNESQPMGVgraaIINMSSIlgsiqg 160
Cdd:cd05323  77 rVDILINNAGILdEKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDK----NKGGKGGV----IVNIGSV------ 142

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24640547 161 ntdGGMY------AYRTSKSALNAATKSLSVDLYPQ---RIMCVslHPGWVKTDM 206
Cdd:cd05323 143 ---AGLYpapqfpVYSASKHGVVGFTRSLADLLEYKtgvRVNAI--CPGFTNTPL 192
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 3-206 3.11e-12

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: 64.32  E-value: 3.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   3 SILITGCNRGLGLGLVK---------ALLNLPqppqhlfttcrNREQAKELEDLAKNHS-NIHILEIDLRNFDAYDKLVA 72
Cdd:cd05366   4 VAIITGAAQGIGRAIAErlaadgfniVLADLN-----------LEEAAKSTIQEISEAGyNAVAVGADVTDKDDVEALID 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  73 diEGVTKDQGLNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmGVGRaaIINMS 152
Cdd:cd05366  73 --QAVEKFGSFDVMVNNAGIAP-ITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLG--------HGGK--IINAS 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24640547 153 SILGsIQGNTDGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd05366 140 SIAG-VQGFPNLGAYS--ASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEM 190
PRK06398 PRK06398
aldose dehydrogenase; Validated
 4-231 4.75e-12

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 64.08  E-value: 4.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLnlpqppqhlfttcrnREQA-------KELEDLAKNHsnihiLEIDLRNfdaYDKLVADIEG 76
Cdd:PRK06398   9 AIVTGGSQGIGKAVVNRLK---------------EEGSnvinfdiKEPSYNDVDY-----FKVDVSN---KEQVIKGIDY 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   77 VTKDQG-LNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpmgVGRAAIINMSSIL 155
Cdd:PRK06398  66 VISKYGrIDILVNNAGIE-SYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLK-----------QDKGVIINIASVQ 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547  156 GSI-QGNTDggmyAYRTSKSALNAATKSLSVDlYPQRIMCVSLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISKLGE 231
Cdd:PRK06398 134 SFAvTRNAA----AYVTSKHAVLGLTRSIAVD-YAPTIRCVAVCPGSIRTPLLEWAAELEVGKDPEHVERKIREWGE 205
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 3-212 6.24e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 63.28  E-value: 6.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLNLpqppqHLFTTCRNREQAKELEDLA-KNHSNIHILEIDLRNFDAYDKLVADIegVTKDQ 81
Cdd:PRK12828   9 VVAITGGFGGLGRATAAWLAAR-----GARVALIGRGAAPLSQTLPgVPADALRIGGIDLVDPQAARRAVDEV--NRQFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSILGSIQGn 161
Cdd:PRK12828  82 RLDALVNIAGAFV-WGTIADGDADTWDRMYGVNVKTTLNASKAALPALTAS---------GGGR--IVNIGAGAALKAG- 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24640547  162 tdGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:PRK12828 149 --PGMGAYAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMP 197
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 5-209 7.58e-12

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: 62.97  E-value: 7.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNREQAKELED-LAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQGL 83
Cdd:cd05365   3 IVTGGAAGIGKAIAGTL---AKAGASVVIADLKSEGAEAVAAaIQQAGGQAIGLECNVTSEQDLEAVVK--ATVSQFGGI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSiqgNTD 163
Cdd:cd05365  78 TILVNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKA-----------GGGAILNISSMSSE---NKN 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGS 209
Cdd:cd05365 144 VRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALAS 189
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 4-206 8.55e-12

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 63.07  E-value: 8.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALlnlpqpPQHLFTTCRNREQAKELEDLA----KNHSNIHILEIDLRNFDAYDKLVAdiEGVTK 79
Cdd:PRK12939  10 ALVTGAARGLGAAFAEAL------AEAGATVAFNDGLAAEARELAaaleAAGGRAHAIAADLADPASVQRFFD--AAAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   80 DQGLNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSilgSIQ 159
Cdd:PRK12939  82 LGGLDGLVNNAGITN-SKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDS-----------GRGRIVNLAS---DTA 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640547  160 GNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK12939 147 LWGAPKLGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 5-205 9.76e-12

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: 63.06  E-value: 9.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALLNLpqppQHLFTTC-RNREQ-AKELEDLAKNHSNIHILEIDLRNFDAYDKLVADieGVTKDQG 82
Cdd:cd05344   5 LVTAASSGIGLAIARALARE----GARVAICaRNRENlERAASELRAGGAGVLAVVADLTDPEDIDRLVEK--AGDAFGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 LNVLFNNAGIAPKSARITAVRSQeLLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSILGsIQGNT 162
Cdd:cd05344  79 VDILVNNAGGPPPGPFAELTDED-WLEAFDLKLLSVIRIVRAVLPGMKER---------GWGR--IVNISSLTV-KEPEP 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24640547 163 DggMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:cd05344 146 N--LVLSNVARAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
PRK09242 PRK09242
SDR family oxidoreductase;
5-223 1.01e-11

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 62.84  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNLpqpPQHLFTTCRNREQAKELED-LAKNHSN--IHILEIDLRNFDAYDKLVADIEgvTKDQ 81
Cdd:PRK09242  13 LITGASKGIGLAIAREFLGL---GADVLIVARDADALAQARDeLAEEFPEreVHGLAADVSDDEDRRAILDWVE--DHWD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAG--IAPKSARITAvrsQELLDTLQTNTVVPIMLAKACLPLLKKAAKanesqpmgvgrAAIINMSSILGsIQ 159
Cdd:PRK09242  88 GLHILVNNAGgnIRKAAIDYTE---DEWRGIFETNLFSAFELSRYAHPLLKQHAS-----------SAIVNIGSVSG-LT 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640547  160 GNTDGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMggSSAPLDVPTSTGQIV 223
Cdd:PRK09242 153 HVRSGAPYG--MTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPL--TSGPLSDPDYYEQVI 212
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 4-212 1.15e-11

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: 62.49  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNREQakeLEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVtkdqgl 83
Cdd:cd05351  10 ALVTGAGKGIGRATVKAL---AKAGARVVAVSRTQAD---LDSLVRECPGIEPVCVDLSDWDATEEALGSVGPV------ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIAPKSArITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpMGVGrAAIINMSSILGSIqgnTD 163
Cdd:cd05351  78 DLLVNNAAVAILQP-FLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIA---------RGVP-GSIVNVSSQASQR---AL 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMG--GSSAP 212
Cdd:cd05351 144 TNHTVYCSTKAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGrdNWSDP 194
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 4-189 1.72e-11

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: 61.91  E-value: 1.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLPQPpqhLFTTCRNREQ-AKELED-LAKNHSNIHILEIDLRNFDAYDKLVADIEGVTKdq 81
Cdd:cd05357   3 ALVTGAAKRIGRAIAEALAAEGYR---VVVHYNRSEAeAQRLKDeLNALRNSAVLVQADLSDFAACADLVAAAFRAFG-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAGIAPKSArITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSILGSiQGN 161
Cdd:cd05357  78 RCDVLVNNASAFYPTP-LGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGS-----------IINIIDAMTD-RPL 144

                       170       180
                ....*....|....*....|....*...
gi 24640547 162 TdgGMYAYRTSKSALNAATKSLSVDLYP 189
Cdd:cd05357 145 T--GYFAYCMSKAALEGLTRSAALELAP 170
PRK05693 PRK05693
SDR family oxidoreductase;
1-207 2.52e-11

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 62.12  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALLNlpqPPQHLFTTCRNREQAKELEDLAKNhsnihILEIDLRNFDAYDKLVADIEGVTkd 80
Cdd:PRK05693   1 MPVVLITGCSSGIGRALADAFKA---AGYEVWATARKAEDVEALAAAGFT-----AVQLDVNDGAALARLAEELEAEH-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QGLNVLFNNAGIAPK----SARITAVRSQelldtLQTNTVVPIMLAKACLPLLKKaakanesqpmgvGRAAIINMSSILG 156
Cdd:PRK05693  71 GGLDVLINNAGYGAMgpllDGGVEAMRRQ-----FETNVFAVVGVTRALFPLLRR------------SRGLVVNIGSVSG 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24640547  157 SIQGNTDGgmyAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMG 207
Cdd:PRK05693 134 VLVTPFAG---AYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQFA 181
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
5-239 3.42e-11

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 61.32  E-value: 3.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpqPPQHLFTTCR-NREQAKELEDL-AKNHSNIHILEIDLRNFDAYDKLVADIEgvTKDQG 82
Cdd:PRK12824   6 LVTGAKRGIGSAIARELLN---DGYRVIATYFsGNDCAKDWFEEyGFTEDQVRLKELDVTDTEECAEALAEIE--EEEGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIApKSARITAVRSQELLDTLQTNTvvpIMLAKACLPLLkkaakanesQPM---GVGRaaIINMSSILG--S 157
Cdd:PRK12824  81 VDILVNNAGIT-RDSVFKRMSHQEWNDVINTNL---NSVFNVTQPLF---------AAMceqGYGR--IINISSVNGlkG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  158 IQGNTdggmyAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGsSAPLDVPTStgqIVQTISK--LGEKQ-- 233
Cdd:PRK12824 146 QFGQT-----NYSAAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVE-QMGPEVLQS---IVNQIPMkrLGTPEei 216

                        250
                 ....*....|....*.
gi 24640547  234 ----------NGGFVN 239
Cdd:PRK12824 217 aaavaflvseAAGFIT 232
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 4-206 8.09e-11

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: 60.33  E-value: 8.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVK---------ALLNLpqppqhlfttcrNREQAKELEDLA-KNHSNIHILEIDLRNFDAYDKLVAD 73
Cdd:cd05339   2 VLITGGGSGIGRLLALefakrgakvVILDI------------NEKGAEETANNVrKAGGKVHYYKCDVSKREEVYEAAKK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  74 IEgvtKDQG-LNVLFNNAGIAPKSaRITAVRSQELLDTLQTNTVVPIMLAKACLPLLkkaakanesqpMGVGRAAIINMS 152
Cdd:cd05339  70 IK---KEVGdVTILINNAGVVSGK-KLLELPDEEIEKTFEVNTLAHFWTTKAFLPDM-----------LERNHGHIVTIA 134

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547 153 SILGSIqgnTDGGMYAYRTSKSALNAATKSLSVDLYPQ---RIMCVSLHPGWVKTDM 206
Cdd:cd05339 135 SVAGLI---SPAGLADYCASKAAAVGFHESLRLELKAYgkpGIKTTLVCPYFINTGM 188
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-210 1.20e-10

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 59.80  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLNLPQPPQHLFTtcRNREQAKELEDlaknhSNIHILEIDLRNFDAYDKLVADIEGVTKDqgL 83
Cdd:PRK06463  10 ALITGGTRGIGRAIAEAFLREGAKVAVLYN--SAENEAKELRE-----KGVFTIKCDVGNRDQVKKSKEVVEKEFGR--V 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIapksariTAVRSQELLDTLQTNTVVPIMLAKAC------LPLLKKAAkanesqpmgvgRAAIINMSSILGS 157
Cdd:PRK06463  81 DVLVNNAGI-------MYLMPFEEFDEEKYNKMIKINLNGAIyttyefLPLLKLSK-----------NGAIVNIASNAGI 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24640547  158 iqGNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM--GGSS 210
Cdd:PRK06463 143 --GTAAEGTTFYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMtlSGKS 195
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-206 1.31e-10

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 59.59  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKAL--------LNLPQPPQHLFTTCRnreqakELEDLAknhSNIHILEIDLRNFDAYDKLVADIEG 76
Cdd:PRK12745   6 LVTGGRRGIGLGIARALaaagfdlaINDRPDDEELAATQQ------ELRALG---VEVIFFPADVADLSAHEAMLDAAQA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   77 VTKdqGLNVLFNNAGIAPKsaritaVRSqELLDT--------LQTNTVVPIML----AKACLpllkkAAKANESQPMGvg 144
Cdd:PRK12745  77 AWG--RIDCLVNNAGVGVK------VRG-DLLDLtpesfdrvLAINLRGPFFLtqavAKRML-----AQPEPEELPHR-- 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24640547  145 raAIINMSSIlGSIQGNTDGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK12745 141 --SIVFVSSV-NAIMVSPNRGEYC--ISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM 197
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 36-230 1.80e-10

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 59.15  E-value: 1.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  36 RNREQ----AKELEDlaKNHSNIHILEIDLRN-FDAYDKLVADIEGVtkDQGlnVLFNNAGIAPK-SARITAVRSQELLD 109
Cdd:cd05356  33 RTQEKldavAKEIEE--KYGVETKTIAADFSAgDDIYERIEKELEGL--DIG--ILVNNVGISHSiPEYFLETPEDELQD 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 110 TLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIQGntdgGMYA-YRTSKSALNAATKSLSVDLY 188
Cdd:cd05356 107 IINVNVMATLKMTRLILPGMVKR-----------KKGAIVNISSFAGLIPT----PLLAtYSASKAFLDFFSRALYEEYK 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24640547 189 PQRIMCVSLHPGWVKTDM-GGSSAPLDVPTSTGQIVQTISKLG 230
Cdd:cd05356 172 SQGIDVQSLLPYLVATKMsKIRKSSLFVPSPEQFVRSALNTLG 214
PRK08251 PRK08251
SDR family oxidoreductase;
3-220 1.99e-10

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 59.18  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKELED-LAKNHSNIHIL--EIDLRNFDAYDKLVADIegvtK 79
Cdd:PRK08251   4 KILITGASSGLGAGMAREFAAKGR---DLALCARRTDRLEELKAeLLARYPGIKVAvaALDVNDHDQVFEVFAEF----R 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   80 DQ--GLNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGs 157
Cdd:PRK08251  77 DElgGLDRVIVNAGIG-KGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQ-----------GSGHLVLISSVSA- 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24640547  158 IQGnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM--GGSSAPLDVPTSTG 220
Cdd:PRK08251 144 VRG-LPGVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMnaKAKSTPFMVDTETG 207
PRK08017 PRK08017
SDR family oxidoreductase;
3-204 2.06e-10

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 59.33  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLglvKALLNLPQPPQHLFTTCRNReqakelEDLAK-NHSNIHILEIDLRNFDAYDKLVADIEGVTkDQ 81
Cdd:PRK08017   4 SVLITGCSSGIGL---EAALELKRRGYRVLAACRKP------DDVARmNSLGFTGILLDLDDPESVERAADEVIALT-DN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIAPKSARITAVRsQELLDTLQTNTVVPIMLAKACLPLLkkaakanesQPMGVGRaaIINMSSILGSIqgn 161
Cdd:PRK08017  74 RLYGLFNNAGFGVYGPLSTISR-QQMEQQFSTNFFGTHQLTMLLLPAM---------LPHGEGR--IVMTSSVMGLI--- 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640547  162 TDGGMYAYRTSKSALNAATKSLSVDLYPQRIMcVSL-HPGWVKT 204
Cdd:PRK08017 139 STPGRGAYAASKYALEAWSDALRMELRHSGIK-VSLiEPGPIRT 181
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 71-206 3.52e-10

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: 58.44  E-value: 3.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  71 VADIEGVTK--------DQGLNVLFNNAGIAPKSArITAVrSQELLD-TLQTNTvvpimlaKACLPLLKKAAKAnesqpM 141
Cdd:cd05362  62 VSDPSQVARlfdaaekaFGGVDILVNNAGVMLKKP-IAET-SEEEFDrMFTVNT-------KGAFFVLQEAAKR-----L 127

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24640547 142 GVGrAAIINMSSILGSIqgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd05362 128 RDG-GRIINISSSLTAA---YTPNYGAYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 82-201 3.96e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 58.51  E-value: 3.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvgrAAIINMSSILGsIQGN 161
Cdd:PRK06701 124 RLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQG-------------SAIINTGSITG-YEGN 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 24640547  162 TDggMYAYRTSKSALNAATKSLSVDLYPQ--RIMCVSLHPGW 201
Cdd:PRK06701 190 ET--LIDYSATKGAIHAFTRSLAQSLVQKgiRVNAVAPGPIW 229
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 82-214 8.43e-10

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: 57.69  E-value: 8.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvgrAAIINMSSILGsIQGN 161
Cdd:cd05355 105 KLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKG-------------SSIINTTSVTA-YKGS 170

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 24640547 162 tdGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLD 214
Cdd:cd05355 171 --PHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEE 221
PRK06482 PRK06482
SDR family oxidoreductase;
5-227 8.64e-10

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 57.43  E-value: 8.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRnREQAkeLEDLAKNHSN-IHILEIDLRNFDAYDKLVADIEGVTKDqgL 83
Cdd:PRK06482   6 FITGASSGFGRGMTERLL---ARGDRVAATVR-RPDA--LDDLKARYGDrLWVLQLDVTDSAAVRAVVDRAFAALGR--I 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIAPKSAritavrSQELLDT-----LQTNTVVPIMLAKACLPLLKKaakanesqpMGVGRaaIINMSSILGSI 158
Cdd:PRK06482  78 DVVVSNAGYGLFGA------AEELSDAqirrqIDTNLIGSIQVIRAALPHLRR---------QGGGR--IVQVSSEGGQI 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640547  159 qgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGS---SAPLDV--PTSTGQIVQTIS 227
Cdd:PRK06482 141 ---AYPGFSLYHATKWGIEGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGldrGAPLDAydDTPVGDLRRALA 211
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 4-206 9.26e-10

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: 57.34  E-value: 9.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKEL-EDLAKNH-SNIHILEIDLRNFDAYDKLVADIEgvtKDQ 81
Cdd:cd05352  11 AIVTGGSRGIGLAIARALA---EAGADVAIIYNSAPRAEEKaEELAKKYgVKTKAYKCDVSSQESVEKTFKQIQ---KDF 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 G-LNVLFNNAGIapksariTAVRSQELLDTLQTNTVVPIML------AKACLPLLKKAakanesqpmgvGRAAIINMSSI 154
Cdd:cd05352  85 GkIDILIANAGI-------TVHKPALDYTYEQWNKVIDVNLngvfncAQAAAKIFKKQ-----------GKGSLIITASM 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24640547 155 LGSIqGNTDGGMYAYRTSKSALNAATKSLSVDL--YPQRIMCVSlhPGWVKTDM 206
Cdd:cd05352 147 SGTI-VNRPQPQAAYNASKAAVIHLAKSLAVEWakYFIRVNSIS--PGYIDTDL 197
PRK07577 PRK07577
SDR family oxidoreductase;
1-206 1.21e-09

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 56.66  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNS--ILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREqakelEDLAKnhsniHILEIDLRNFDAYDKLVADIEGvt 78
Cdd:PRK07577   1 MSSrtVLVTGATKGIGLALSLRLANLGH---QVIGIARSAI-----DDFPG-----ELFACDLADIEQTAATLAQINE-- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   79 kDQGLNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSIlgSI 158
Cdd:PRK07577  66 -IHPVDAIVNNVGIA-LPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLR---------EQGR--IVNICSR--AI 130

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640547  159 QGNTDggMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK07577 131 FGALD--RTSYSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETEL 176
PRK08628 PRK08628
SDR family oxidoreductase;
4-189 1.23e-09

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 56.89  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLNLPQPPQHLfttCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIegVTKDQGL 83
Cdd:PRK08628  10 VIVTGGASGIGAAISLRLAEEGAIPVIF---GRSAPDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQT--VAKFGRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIApKSARITAVRsQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvgRAAIINMSS---ILGsiQG 160
Cdd:PRK08628  85 DGLVNNAGVN-DGVGLEAGR-EAFVASLERNLIHYYVMAHYCLPHLKAS------------RGAIVNISSktaLTG--QG 148

                        170       180
                 ....*....|....*....|....*....
gi 24640547  161 NTDGgmyaYRTSKSALNAATKSLSVDLYP 189
Cdd:PRK08628 149 GTSG----YAAAKGAQLALTREWAVALAK 173
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 5-205 1.56e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 56.84  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNLPQppqHLFTTCRNReqakeLEDLAknhSNIHILEIDLRNFDAYDKL---VADIEGvtkdq 81
Cdd:PRK06523  13 LVTGGTKGIGAATVARLLEAGA---RVVTTARSR-----PDDLP---EGVEFVAADLTTAEGCAAVaraVLERLG----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAG--IAPKSArITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIQ 159
Cdd:PRK06523  77 GVDILVHVLGgsSAPAGG-FAALTDEEWQDELNLNLLAAVRLDRALLPGMIAR-----------GSGVIIHVTSIQRRLP 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640547  160 gnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:PRK06523 145 --LPESTTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 4-195 2.77e-09

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: 55.72  E-value: 2.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRN----REQAKELEDLAKNHSN-IHILEIDLRNFDAYDKLVADIegVT 78
Cdd:cd08939   4 VLITGGSSGIGKALAKELV---KEGANVIIVARSesklEEAVEEIEAEANASGQkVSYISADLSDYEEVEQAFAQA--VE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  79 KDQGLNVLFNNAGIA-PKsaRITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSILGS 157
Cdd:cd08939  79 KGGPPDLVVNCAGISiPG--LFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGH-----------IVFVSSQAAL 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24640547 158 IqgntdgGMY---AYRTSKSALNAATKSLSVDL--YPQRIMCV 195
Cdd:cd08939 146 V------GIYgysAYCPSKFALRGLAESLRQELkpYNIRVSVV 182
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 82-212 3.95e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 55.32  E-value: 3.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSiqgn 161
Cdd:PRK07478  83 GLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLAR-----------GGGSLIFTSTFVGH---- 147

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24640547  162 TDG--GMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:PRK07478 148 TAGfpGMAAYAASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGD 200
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 82-202 4.61e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 55.35  E-value: 4.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvgRAAIINMSSilgSIQGN 161
Cdd:PRK07890  82 RVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES------------GGSIVMINS---MVLRH 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 24640547  162 TDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWV 202
Cdd:PRK07890 147 SQPKYGAYKMAKGALLAASQSLATELGPQGIRVNSVAPGYI 187
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 3-206 4.62e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 55.11  E-value: 4.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNreqAKELEDLAkNHSNIHILEIDLRNfDAYDKLVADIEGVtkdqg 82
Cdd:PRK07060  11 SVLVTGASSGIGRACAVALA---QRGARVVAAARN---AAALDRLA-GETGCEPLRLDVGD-DAAIRAALAAAGA----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIAPKSARITAvrSQELLD-TLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvGRAAIINMSSIlGSIQGN 161
Cdd:PRK07060  78 FDGLVNCAGIASLESALDM--TAEGFDrVMAVNARGAALVARHVARAMIAAG----------RGGSIVNVSSQ-AALVGL 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24640547  162 TDggMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK07060 145 PD--HLAYCASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPM 187
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 5-211 5.45e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 55.43  E-value: 5.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQakeLEDLAKNH-SNIHILEIDLRNFDAYDKLVAdiEGVTKDQGL 83
Cdd:PRK08263   7 FITGASRGFGRAWTEAAL---ERGDRVVATARDTAT---LADLAEKYgDRLLPLALDVTDRAAVFAAVE--TAVEHFGRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesQPMGvgraAIINMSSIlGSIQGNTD 163
Cdd:PRK08263  79 DIVVNNAGYG-LFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLRE-------QRSG----HIIQISSI-GGISAFPM 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640547  164 GGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSA 211
Cdd:PRK08263 146 SGIYH--ASKWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAGTSA 191
PRK05650 PRK05650
SDR family oxidoreductase;
2-232 6.38e-09

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 55.05  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    2 NSILITGCNRGLGLGLVK---------ALLNLPQPpqhlfttcRNREQAKELEDLAknhSNIHILEIDLRNFDAYDKLVA 72
Cdd:PRK05650   1 NRVMITGAASGLGRAIALrwaregwrlALADVNEE--------GGEETLKLLREAG---GDGFYQRCDVRDYSQLTALAQ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   73 DIEgvTKDQGLNVLFNNAGIApkSARITAVRSQELLD-TLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINM 151
Cdd:PRK05650  70 ACE--EKWGGIDVIVNNAGVA--SGGFFEELSLEDWDwQIAINLMGVVKGCKAFLPLFKRQ---------KSGR--IVNI 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  152 SSILGSIQGNtdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMgGSSAPLDVPTSTgqivQTISKLGE 231
Cdd:PRK05650 135 ASMAGLMQGP---AMSSYNVAKAGVVALSETLLVELADDEIGVHVVCPSFFQTNL-LDSFRGPNPAMK----AQVGKLLE 206


                 .
gi 24640547  232 K 232
Cdd:PRK05650 207 K 207
PRK07814 PRK07814
SDR family oxidoreductase;
5-204 7.66e-09

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 54.78  E-value: 7.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQGL 83
Cdd:PRK07814  14 VVTGAGRGLGAAIALAF---AEAGADVLIAARTESQLDEVaEQIRAAGRRAHVVAADLAHPEATAGLAG--QAVEAFGRL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIAPKSARITAvRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvGRAAIINMSSILGSIQGNtd 163
Cdd:PRK07814  89 DIVVNNVGGTMPNPLLST-STKDLADAFTFNVATAHALTVAAVPLMLEHS----------GGGSVINISSTMGRLAGR-- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 24640547  164 gGMYAYRTSKSALNAATKSLSVDLYPqRIMCVSLHPGWVKT 204
Cdd:PRK07814 156 -GFAAYGTAKAALAHYTRLAALDLCP-RIRVNAIAPGSILT 194
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-205 8.68e-09

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 54.53  E-value: 8.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKAL---------LNLPQPPqhlfttcrnrEQAKELEDLAKNhsnIHILEIDLRNFDAYDKLVAdiE 75
Cdd:PRK12481  12 IITGCNTGLGQGMAIGLakagadivgVGVAEAP----------ETQAQVEALGRK---FHFITADLIQQKDIDSIVS--Q 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   76 GVTKDQGLNVLFNNAGIapksaritaVRSQELLDTLQTN--TVVPIMlAKACLPLLKKAAKANESQPMGvgrAAIINMSS 153
Cdd:PRK12481  77 AVEVMGHIDILINNAGI---------IRRQDLLEFGNKDwdDVININ-QKTVFFLSQAVAKQFVKQGNG---GKIINIAS 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24640547  154 ILgSIQGNTDggMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:PRK12481 144 ML-SFQGGIR--VPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMATD 192
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 36-232 1.07e-08

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: 53.99  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  36 RNREQAKELEdLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTkDQGLNVLFNNAGIApKSARITAVRSQELLDTLQTNT 115
Cdd:cd08931  32 IDEDGLAALA-AELGAENVVAGALDVTDRAAWAAALADFAAAT-GGRLDALFNNAGVG-RGGPFEDVPLAAHDRMVDINV 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 116 VVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSILGsIQGNTDggMYAYRTSKSALNAATKSLSVDLYPQRIMCV 195
Cdd:cd08931 109 KGVLNGAYAALPYLKATPGAR-----------VINTASSSA-IYGQPD--LAVYSATKFAVRGLTEALDVEWARHGIRVA 174

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24640547 196 SLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISKLGEK 232
Cdd:cd08931 175 DVWPWFVDTPILTKGETGAAPKKGLGRVLPVSDVAKV 211
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 5-212 1.53e-08

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: 53.62  E-value: 1.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALlnlPQPPQHLFTT-CRNREQAKELEDLAKNHSnihileidlRNFDAYDKLVADIEGVTK--DQ 81
Cdd:cd05337   5 IVTGASRGIGRAIATEL---AARGFDIAINdLPDDDQATEVVAEVLAAG---------RRAIYFQADIGELSDHEAllDQ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 ------GLNVLFNNAGIAPKSARITAVRSQELLDTL-QTNTVVPIMLAKAclpllkkAAKANESQPMGVGRA--AIINMS 152
Cdd:cd05337  73 awedfgRLDCLVNNAGIAVRPRGDLLDLTEDSFDRLiAINLRGPFFLTQA-------VARRMVEQPDRFDGPhrSIIFVT 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 153 SIlGSIQGNTDGGMYAyrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:cd05337 146 SI-NAYLVSPNRGEYC--ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKE 202
PRK05993 PRK05993
SDR family oxidoreductase;
3-204 1.62e-08

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 53.88  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKAllnLPQPPQHLFTTCRNREQAKELEDlaknhSNIHILEIDLRNFDAYDKLVADIEGVTKDQg 82
Cdd:PRK05993   6 SILITGCSSGIGAYCARA---LQSDGWRVFATCRKEEDVAALEA-----EGLEAFQLDYAEPESIAALVAQVLELSGGR- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIAPKSA----RITAVRSQelldtLQTN---------TVVPIMLAKaclpllkkaakanesqpmGVGRaaII 149
Cdd:PRK05993  77 LDALFNNGAYGQPGAvedlPTEALRAQ-----FEANffgwhdltrRVIPVMRKQ------------------GQGR--IV 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24640547  150 NMSSILGSIQGNTDGgmyAYRTSKSALNAATKSLSVDLYPQRIMcVSL-HPGWVKT 204
Cdd:PRK05993 132 QCSSILGLVPMKYRG---AYNASKFAIEGLSLTLRMELQGSGIH-VSLiEPGPIET 183
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 39-207 1.73e-08

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 53.64  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   39 EQAKELEDLAKNHSNIHILEIDLRNFDAYDKLvadIEGVTKDQGL-NVLFNNAGIApKSARITAVRSQELLDTLQTNTVV 117
Cdd:PRK12859  55 EQIQLQEELLKNGVKVSSMELDLTQNDAPKEL---LNKVTEQLGYpHILVNNAAYS-TNNDFSNLTAEELDKHYMVNVRA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  118 PIMLAKACLPLLKKaakanesqPMGvGRaaIINMSSilGSIQGNTDGGMyAYRTSKSALNAATKSLSVDLYPQRIMCVSL 197
Cdd:PRK12859 131 TTLLSSQFARGFDK--------KSG-GR--IINMTS--GQFQGPMVGEL-AYAATKGAIDALTSSLAAEVAHLGITVNAI 196

                        170
                 ....*....|
gi 24640547  198 HPGwvKTDMG 207
Cdd:PRK12859 197 NPG--PTDTG 204
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 82-206 1.80e-08

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: 53.65  E-value: 1.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIqgn 161
Cdd:cd08944  77 GLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIAR-----------GGGSIVNLSSIAGQS--- 142

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 24640547 162 TDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd08944 143 GDPGYGAYGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPL 187
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 4-94 1.86e-08

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 53.93  E-value: 1.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLPQPPQ--HLFTTCRNREQAKE-LEDLAKNHSN----IHILEIDLRNFDAYDKLVADIEg 76
Cdd:cd08941   4 VLVTGANSGLGLAICERLLAEDDENPelTLILACRNLQRAEAaCRALLASHPDarvvFDYVLVDLSNMVSVFAAAKELK- 82

                        90
                ....*....|....*...
gi 24640547  77 vTKDQGLNVLFNNAGIAP 94
Cdd:cd08941  83 -KRYPRLDYLYLNAGIMP 99
PRK12746 PRK12746
SDR family oxidoreductase;
5-206 2.00e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 53.50  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTK---- 79
Cdd:PRK12746  10 LVTGASRGIGRAIAMRLAN--DGALVAIHYGRNKQAADEtIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELQirvg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   80 DQGLNVLFNNAGIAPKSArITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKanesqpmgvgraaIINMSSILGSIq 159
Cdd:PRK12746  88 TSEIDILVNNAGIGTQGT-IENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEGR-------------VINISSAEVRL- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640547  160 GNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK12746 153 GFT--GSIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 5-206 2.00e-08

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: 53.60  E-value: 2.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKAL--------LNLPQPPqhlfttcrNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEg 76
Cdd:cd08940   6 LVTGSTSGIGLGIARALaaaganivLNGFGDA--------AEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQ- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  77 vtkDQ--GLNVLFNNAGiapksarITAVRSQELLDTLQTNTVVPIMLA------KACLPLLKKaakanesqpMGVGRaaI 148
Cdd:cd08940  77 ---RQfgGVDILVNNAG-------IQHVAPIEDFPTEKWDAIIALNLSavfhttRLALPHMKK---------QGWGR--I 135

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640547 149 INMSSILGSIqgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd08940 136 INIASVHGLV---ASANKSAYVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPL 190
PRK07023 PRK07023
SDR family oxidoreductase;
5-206 2.85e-08

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 52.71  E-value: 2.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAkeledLAKNH-SNIHILEIDLRNF---------DAYDKLVADI 74
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLL---QPGIAVLGVARSRHPS-----LAAAAgERLAEVELDLSDAaaaaawlagDLLAAFVDGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   75 EGVTkdqglnvLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKAclpLLKKAAKANESQpmgvgraaIINMSSi 154
Cdd:PRK07023  77 SRVL-------LINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAA---LAQAASDAAERR--------ILHISS- 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24640547  155 lGSIQgNTDGGMYAYRTSKSALNAATKSLSVDlYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK07023 138 -GAAR-NAYAGWSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDTGM 186
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 3-212 3.93e-08

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 52.60  E-value: 3.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   3 SILITGCNRGLGLGlvkALLNLPQPPQHLFTTCRNREQAKELE-DLAKNHSN----IHILeiDLRNFDAYDKLVADIEgv 77
Cdd:cd09808   3 SFLITGANSGIGKA---AALAIAKRGGTVHMVCRNQTRAEEARkEIETESGNqnifLHIV--DMSDPKQVWEFVEEFK-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  78 TKDQGLNVLFNNAGIAPKSARITavrSQELLDTLQTNTVVPIMLAKACLPLLKKAakaNESQPMGVGRAAIINMSSILGS 157
Cdd:cd09808  76 EEGKKLHVLINNAGCMVNKRELT---EDGLEKNFATNTLGTYILTTHLIPVLEKE---EDPRVITVSSGGMLVQKLNTNN 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640547 158 IQ---GNTDGGMyAYRTSKSALNAATKSLSvDLYPQrIMCVSLHPGWVKTDMGGSSAP 212
Cdd:cd09808 150 LQserTAFDGTM-VYAQNKRQQVIMTEQWA-KKHPE-IHFSVMHPGWADTPAVRNSMP 204
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 5-234 5.64e-08

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 52.00  E-value: 5.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlPQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDA----YDKLVADIEGVTKD 80
Cdd:PRK12747   8 LVTGASRGIGRAIAKRLAN-DGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGvealYSSLDNELQNRTGS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QGLNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKanesqpmgvgraaIINMSSILGSIqg 160
Cdd:PRK12747  87 TKFDILINNAGIGP-GAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSR-------------IINISSAATRI-- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24640547  161 nTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISKLGEKQN 234
Cdd:PRK12747 151 -SLPDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAFNRLGEVED 223
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 4-204 6.28e-08

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: 51.81  E-value: 6.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLvkALLNLPQPPQHLFTTCrNREQAKELEDLAKNHsnIHILEIDLRNFDAYDKLVADIEGvtKDQGL 83
Cdd:cd09761   4 AIVTGGGHGIGKQI--CLDFLEAGDKVVFADI-DEERGADFAEAEGPN--LFFVHGDVADETLVKFVVYAMLE--KLGRI 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIApkSARITAVRSQELLD-TLQTNTVVPIMLAKACLPLLKKaakanesqpmgvGRAAIINMSSILgSIQGNT 162
Cdd:cd09761  77 DVLVNNAARG--SKGILSSLLLEEWDrILSVNLTGPYELSRYCRDELIK------------NKGRIINIASTR-AFQSEP 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24640547 163 DGgmYAYRTSKSALNAATKSLSVDLYPQrIMCVSLHPGWVKT 204
Cdd:cd09761 142 DS--EAYAASKGGLVALTHALAMSLGPD-IRVNCISPGWINT 180
PRK06484 PRK06484
short chain dehydrogenase; Validated
 83-204 6.66e-08

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 52.54  E-value: 6.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvgraAIINMSSILGSIqgnT 162
Cdd:PRK06484 344 LDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGG-------------VIVNLGSIASLL---A 407

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 24640547  163 DGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK06484 408 LPPRNAYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 45-204 7.07e-08

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 52.00  E-value: 7.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   45 EDLAKNHSNIHILEIDLRNFDAYDKLVadiEGVTKDQG-LNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAK 123
Cdd:PRK12748  60 EEIESYGVRCEHMEIDLSQPYAPNRVF---YAVSERLGdPSILINNAAYS-THTRLEELTAEQLDKHYAVNVRATMLLSS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  124 AclpllkkAAKANESQPMGvgraAIINMSSilGSIQGNTDGGMyAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVK 203
Cdd:PRK12748 136 A-------FAKQYDGKAGG----RIINLTS--GQSLGPMPDEL-AYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTD 201


                 .
gi 24640547  204 T 204
Cdd:PRK12748 202 T 202
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 4-245 7.62e-08

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 51.94  E-value: 7.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLNLPQPPQHLfttcrnreqakeleDLAKN---HSNIHILEIDLRNFDAYDKLVADIegVTKD 80
Cdd:PRK06171  12 IIVTGGSSGIGLAIVKELLANGANVVNA--------------DIHGGdgqHENYQFVPTDVSSAEEVNHTVAEI--IEKF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QGLNVLFNNAGI----------APKSA---------RITAVRSQELLdtLQTNTVVPIMLakaclpllkkaakaneSQPM 141
Cdd:PRK06171  76 GRIDGLVNNAGIniprllvdekDPAGKyelneaafdKMFNINQKGVF--LMSQAVARQMV----------------KQHD 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  142 GVgraaIINMSSILGSiQGNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWV-KTDMGGSSAPLDVPTSTG 220
Cdd:PRK06171 138 GV----IVNMSSEAGL-EGSE--GQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILeATGLRTPEYEEALAYTRG 210

                        250       260
                 ....*....|....*....|....*
gi 24640547  221 QIVqtisklgEKQNGGFVNYDGTPL 245
Cdd:PRK06171 211 ITV-------EQLRAGYTKTSTIPL 228
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 5-220 9.51e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 51.60  E-value: 9.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvtKDQG-L 83
Cdd:PRK07097  14 LITGASYGIGFAIAKAYAK--AGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIE---KEVGvI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLP-LLKKaakanesqpmgvGRAAIINMSSILGSIQGNT 162
Cdd:PRK07097  89 DILVNNAGII-KRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPsMIKK------------GHGKIINICSMMSELGRET 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640547  163 DGgmyAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDmggSSAPLDVPTSTG 220
Cdd:PRK07097 156 VS---AYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATP---QTAPLRELQADG 207
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
5-228 1.17e-07

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 51.34  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNLPQPPQHLFTTCRNREQAKELedLAKNHSNIHILeIDLRNFDAYDKLVADIEgvTKDQGLN 84
Cdd:PRK08226  10 LITGALQGIGEGIARVFARHGANLILLDISPEIEKLADEL--CGRGHRCTAVV-ADVRDPASVAAAIKRAK--EKEGRID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNAGIApksaRITAVR--SQELLD-TLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIQGn 161
Cdd:PRK08226  85 ILVNNAGVC----RLGSFLdmSDEDRDfHIDINIKGVWNVTKAVLPEMIAR-----------KDGRIVMMSSVTGDMVA- 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547  162 tDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISK 228
Cdd:PRK08226 149 -DPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSNPEDPESVLTEMAK 214
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 1-214 1.28e-07

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 50.95  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   1 MNSILITGCNRGLGLGLVKALLNlpqPPQHLFTTCRNREQA---KELEDLAKnhsniHILEIDLRNFDAYDKLVADIEGV 77
Cdd:cd08951   7 MKRIFITGSSDGLGLAAARTLLH---QGHEVVLHARSQKRAadaKAACPGAA-----GVLIGDLSSLAETRKLADQVNAI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  78 TKdqgLNVLFNNAGIApkSARITAVRSQELLDTLQTNTVVPIMLAkaCLPLLKKAAKANESQPMGVGRAAiinMSSILGS 157
Cdd:cd08951  79 GR---FDAVIHNAGIL--SGPNRKTPDTGIPAMVAVNVLAPYVLT--ALIRRPKRLIYLSSGMHRGGNAS---LDDIDWF 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547 158 IQGNTDGGMYayrtSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLD 214
Cdd:cd08951 149 NRGENDSPAY----SDSKLHVLTLAAAVARRWKDVSSNAVHPGWVPTKMGGAGAPDD 201
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 4-216 1.43e-07

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: 50.65  E-value: 1.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGlglVKALLNLPQPPQHLFTTCRNREQAKELED--LAKNHSNIHILEIDLRNFDA--YDKLVADIEGVTK 79
Cdd:cd05340   7 ILVTGASDGIG---REAALTYARYGATVILLGRNEEKLRQVADhiNEEGGRQPQWFILDLLTCTSenCQQLAQRIAVNYP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  80 DqgLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKanesqpmgvgrAAIINMSSILGSiQ 159
Cdd:cd05340  84 R--LDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDA-----------GSLVFTSSSVGR-Q 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640547 160 GNTDGGmyAYRTSKSALNAATKSLSvDLYPQRIMCV-SLHPGWVKTDMGGSSAPLDVP 216
Cdd:cd05340 150 GRANWG--AYAVSKFATEGL*QVLA-DEYQQRNLRVnCINPGGTRTAMRASAFPTEDP 204
PRK09291 PRK09291
SDR family oxidoreductase;
1-200 1.45e-07

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 50.77  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGlvkALLNLPQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRnfDAYDKLVA---DIEg 76
Cdd:PRK09291   2 SKTILITGAGSGFGRE---VALRLARKGHNVIAGVQIAPQVTALrAEAARRGLALRVEKLDLT--DAIDRAQAaewDVD- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   77 vtkdqglnVLFNNAGI--APKSARITAVRSQELLDtlqTNTVVPIMLAKACLPllKKAAKanesqpmgvGRAAIINMSSI 154
Cdd:PRK09291  76 --------VLLNNAGIgeAGAVVDIPVELVRELFE---TNVFGPLELTQGFVR--KMVAR---------GKGKVVFTSSM 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640547  155 LGSIqgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPG 200
Cdd:PRK09291 134 AGLI---TGPFTGAYCASKHALEAIAEAMHAELKPFGIQVATVNPG 176
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 40-229 1.48e-07

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: 50.61  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  40 QAKELEDLAK----NHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQGLNVLFNNAGIAPKSArITAVRSQELLDTLQTNT 115
Cdd:cd08934  36 RVDRLEALADeleaEGGKALVLELDVTDEQQVDAAVE--RTVEALGRLDILVNNAGIMLLGP-VEDADTTDWTRMIDTNL 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 116 VVPIMLAKACLPLLKkaakanesqPMGVGRaaIINMSSILGSIQGNTDGGmyaYRTSKSALNAATKSLSVDLYPQRIMCV 195
Cdd:cd08934 113 LGLMYTTHAALPHHL---------LRNKGT--IVNISSVAGRVAVRNSAV---YNATKFGVNAFSEGLRQEVTERGVRVV 178

                       170       180       190
                ....*....|....*....|....*....|....
gi 24640547 196 SLHPGWVKTDMGGSSAPLDVPTSTGQIVQTISKL 229
Cdd:cd08934 179 VIEPGTVDTELRDHITHTITKEAYEERISTIRKL 212
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 2-227 1.55e-07

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 50.72  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    2 NSILITGCNRGLGLGLVKALLN-------LPqppqhlfttcRNREQAKELEDLAKNHsnIHILEIDLRNFDAYDKLVAdi 74
Cdd:PRK06200   7 QVALITGGGSGIGRALVERFLAegarvavLE----------RSAEKLASLRQRFGDH--VLVVEGDVTSYADNQRAVD-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   75 EGVTKDQGLNVLFNNAGIAPKSARITAVrSQELLDTL-----QTNTVVPIMLAKACLPLLKKAakanesqpmgvgRAAII 149
Cdd:PRK06200  73 QTVDAFGKLDCFVGNAGIWDYNTSLVDI-PAETLDTAfdeifNVNVKGYLLGAKAALPALKAS------------GGSMI 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24640547  150 NMSSILGSIQGntdGGMYAYRTSKSALNAATKSLSVDLYPQ-RIMCVSlhPGWVKTDMGGssapldvPTSTGQIVQTIS 227
Cdd:PRK06200 140 FTLSNSSFYPG---GGGPLYTASKHAVVGLVRQLAYELAPKiRVNGVA--PGGTVTDLRG-------PASLGQGETSIS 206
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-212 1.55e-07

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 50.73  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVkalLNLPQPPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvtKDQG 82
Cdd:PRK08217   8 IVITGGAQGLGRAMA---EYLAQKGAKLALIDLNQEKLEEaVAECGALGTEVRGYAANVTDEEDVEATFAQIA---EDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 -LNVLFNNAGIAPKSARITA----VRSQELLDtlQTNTVVPIMLAKACLPLLKKAAKANESQPMGVgraaIINMSSIlgS 157
Cdd:PRK08217  82 qLNGLINNAGILRDGLLVKAkdgkVTSKMSLE--QFQSVIDVNLTGVFLCGREAAAKMIESGSKGV----IINISSI--A 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24640547  158 IQGNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAP 212
Cdd:PRK08217 154 RAGNM--GQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKP 206
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-206 2.28e-07

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 50.07  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTKdqGL 83
Cdd:PRK07666  11 LITGAGRGIGRAVAIAL---AKEGVNVGLLARTEENLKAVaEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELG--SI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSILGSiqgNTD 163
Cdd:PRK07666  86 DILINNAGIS-KFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGD-----------IINISSTAGQ---KGA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24640547  164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK07666 151 AVTSAYSASKFGVLGLTESLMQEVRKHNIRVTALTPSTVATDM 193
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-205 2.51e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 50.39  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    2 NSILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELED-LAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKD 80
Cdd:PRK06198   7 KVALVTGGTQGLGAAIARAFAE--RGAAGLVICGRNAEKGEAQAAeLEALGAKAVFVQADLSDVEDCRRVVA--AADEAF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QGLNVLFNNAGIapkSARITAV-RSQELLDTL-QTNTVVPIMLAKACLPLLKKaakanESQPmgvgrAAIINMSSIlgsi 158
Cdd:PRK06198  83 GRLDALVNAAGL---TDRGTILdTSPELFDRHfAVNVRAPFFLMQEAIKLMRR-----RKAE-----GTIVNIGSM---- 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640547  159 qgNTDGG---MYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:PRK06198 146 --SAHGGqpfLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-204 2.52e-07

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 50.12  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALlnlPQPPQHLFTTC--RNREQAKEL-EDLAKNhsnIHILEIDLRNFDAYDKLVAdiEGVTKDQ 81
Cdd:PRK06935  19 IVTGGNTGLGQGYAVAL---AKAGADIIITThgTNWDETRRLiEKEGRK---VTFVQVDLTKPESAEKVVK--EALEEFG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIapksaritaVRSQELLDTLQT--NTVVPIMLaKACLPLLKKAAKANESQpmgvGRAAIINMSSILgSIQ 159
Cdd:PRK06935  91 KIDILVNNAGT---------IRRAPLLEYKDEdwNAVMDINL-NSVYHLSQAVAKVMAKQ----GSGKIINIASML-SFQ 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640547  160 GntdgGMY--AYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK06935 156 G----GKFvpAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 5-205 2.78e-07

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: 50.20  E-value: 2.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEI--DLRNFDAYDKLVADIEgvTKDQG 82
Cdd:cd05343  10 LVTGASVGIGAAVARALV---QHGMKVVGCARRVDKIEALAAECQSAGYPTLFPYqcDLSNEEQILSMFSAIR--TQHQG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 LNVLFNNAGIAPKSARITAVRS--QELLDtlqtntvVPIMLAKACLPLLKKAAKAnesqpMGVGRAAIINMSSILGS--I 158
Cdd:cd05343  85 VDVCINNAGLARPEPLLSGKTEgwKEMFD-------VNVLALSICTREAYQSMKE-----RNVDDGHIININSMSGHrvP 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 24640547 159 QGNTdggMYAYRTSKSALNAATKSLSVDLYPQR--IMCVSLHPGWVKTD 205
Cdd:cd05343 153 PVSV---FHFYAATKHAVTALTEGLRQELREAKthIRATSISPGLVETE 198
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 5-206 3.96e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 49.56  E-value: 3.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQGL 83
Cdd:PRK08213  16 LVTGGSRGLGLQIAEAL---GEAGARVVLSARKAEELEEaAAHLEALGIDALWIAADVADEADIERLAE--ETLERFGHV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGI---APkSARITAVRSQELLDTLQTNTVvpimlakaclpLLKKAAKANESQPMGVGRaaIINMSSILGsIQG 160
Cdd:PRK08213  91 DILVNNAGAtwgAP-AEDHPVEAWDKVMNLNVRGLF-----------LLSQAVAKRSMIPRGYGR--IINVASVAG-LGG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640547  161 NTDGGM--YAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK08213 156 NPPEVMdtIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKM 203
PRK05717 PRK05717
SDR family oxidoreductase;
5-204 4.53e-07

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 49.50  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEDLAknhSNIHILEIDLRNFDAYDKLVADIEGvtKDQGLN 84
Cdd:PRK05717  14 LVTGAARGIGLGIAAWLIA--EGWQVVLADLDRERGSKVAKALG---ENAWFIAMDVADEAQVAAGVAEVLG--QFGRLD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNAGIA-PKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKkaakanesqpmgVGRAAIINMSSILGSiQGNTD 163
Cdd:PRK05717  87 ALVCNAAIAdPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLR------------AHNGAIVNLASTRAR-QSEPD 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24640547  164 GGMYAyrTSKSALNAATKSLSVDLYPQ-RIMCVSlhPGWVKT 204
Cdd:PRK05717 154 TEAYA--ASKGGLLALTHALAISLGPEiRVNAVS--PGWIDA 191
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 77-205 4.76e-07

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 49.46  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   77 VTKDQGLNVLFNNAGIA-PKSARITAvrsQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSIL 155
Cdd:PRK06113  83 LSKLGKVDILVNNAGGGgPKPFDMPM---ADFRRAYELNVFSFFHLSQLVAPEMEKN-----------GGGVILTITSMA 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640547  156 GSiqgNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:PRK06113 149 AE---NKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 4-207 5.09e-07

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 49.12  E-value: 5.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLPQppqHLFTTCRNREQAKE-LEDLAKNHSN-IHILEIDLRNFDAYDKLVADIegVTKDQ 81
Cdd:cd05369   6 AFITGGGTGIGKAIAKAFAELGA---SVAIAGRKPEVLEAaAEEISSATGGrAHPIQCDVRDPEAVEAAVDET--LKEFG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAG---IAPkSARITAvrsqelldtlqtN---TVVPIML------AKACLPLLKKaakanesqpmGVGRAAII 149
Cdd:cd05369  81 KIDILINNAAgnfLAP-AESLSP------------NgfkTVIDIDLngtfntTKAVGKRLIE----------AKHGGSIL 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547 150 NMSSIlgsiqgntdggmYAYRTS---------KSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMG 207
Cdd:cd05369 138 NISAT------------YAYTGSpfqvhsaaaKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEG 192
PRK05867 PRK05867
SDR family oxidoreductase;
5-206 6.98e-07

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 48.88  E-value: 6.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELED-LAKNHSNIHILEIDLRNFDA----YDKLVADIEGVtk 79
Cdd:PRK05867  13 LITGASTGIGKRVALAYV---EAGAQVAIAARHLDALEKLADeIGTSGGKVVPVCCDVSQHQQvtsmLDQVTAELGGI-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   80 dqglNVLFNNAGIAPKSARITaVRSQELLDTLQTNTVVPIMLAKAclpllkkAAKANESQPMGvgrAAIINMSSILGSIQ 159
Cdd:PRK05867  88 ----DIAVCNAGIITVTPMLD-MPLEEFQRLQNTNVTGVFLTAQA-------AAKAMVKQGQG---GVIINTASMSGHII 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640547  160 gNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK05867 153 -NVPQQVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 2-230 7.05e-07

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: 48.89  E-value: 7.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   2 NSILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKNhsNIHILEIDLRNFDAYDKLVAdiEGVTKDQ 81
Cdd:cd05348   5 EVALITGGGSGLGRALVERFV---AEGAKVAVLDRSAEKVAELRADFGD--AVVGVEGDVRSLADNERAVA--RCVERFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAGIAPKSARITAVrSQELLDTL-----QTNTVVPIMLAKACLPLLKKaakanesqpmgvGRAAIINMSSILG 156
Cdd:cd05348  78 KLDCFIGNAGIWDYSTSLVDI-PEEKLDEAfdelfHINVKGYILGAKAALPALYA------------TEGSVIFTVSNAG 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24640547 157 SIQGntdGGMYAYRTSKSALNAATKSLSVDLYPQ-RIMCVSlhPGWVKTDMGGssapldvPTSTGQIVQTISKLG 230
Cdd:cd05348 145 FYPG---GGGPLYTASKHAVVGLVKQLAYELAPHiRVNGVA--PGGMVTDLRG-------PASLGQGETSISTPP 207
PRK06947 PRK06947
SDR family oxidoreductase;
1-226 7.24e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 48.65  E-value: 7.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGlvKALLNLPQPPQHLFTTCRNREQAKELEDLAKNHSNiHILEI--DLRNfDAydKLVADIEGVT 78
Cdd:PRK06947   2 RKVVLITGASRGIGRA--TAVLAAARGWSVGINYARDAAAAEETADAVRAAGG-RACVVagDVAN-EA--DVIAMFDAVQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   79 KDQG-LNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAkaclpllKKAAKANESQPMGVGrAAIINMSSI--- 154
Cdd:PRK06947  76 SAFGrLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCA-------REAARRLSTDRGGRG-GAIVNVSSIasr 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  155 LGSIQGNTDggmyaYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMG------------GSSAPLDVPTSTGQI 222
Cdd:PRK06947 148 LGSPNEYVD-----YAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHasggqpgraarlGAQTPLGRAGEADEV 222


                 ....
gi 24640547  223 VQTI 226
Cdd:PRK06947 223 AETI 226
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
5-205 8.62e-07

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 48.56  E-value: 8.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGlglvKAL-LNLPQPPQHLFTT-CRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTKdq 81
Cdd:PRK08063   8 LVTGSSRGIG----KAIaLRLAEEGYDIAVNyARSRKAAEETaEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGiapkSARITAVRSQELLD---TLQTNtvvpimlAKACLPLLKKAAKANESqpmgVGRAAIINMSSiLGSI 158
Cdd:PRK08063  82 RLDVFVNNAA----SGVLRPAMELEESHwdwTMNIN-------AKALLFCAQEAAKLMEK----VGGGKIISLSS-LGSI 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640547  159 QGNTDggmYAY-RTSKSALNAATKSLSVDLYPQRIM--CVSlhPGWVKTD 205
Cdd:PRK08063 146 RYLEN---YTTvGVSKAALEALTRYLAVELAPKGIAvnAVS--GGAVDTD 190
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 5-199 9.32e-07

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: 48.54  E-value: 9.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELedLAKNHSNIHILEIDLRNFDAYDKLVADieGVTKDQGLN 84
Cdd:cd05345   9 IVTGAGSGFGEGIARRFA---QEGARVVIADINADGAERV--AADIGEAAIAIQADVTKRADVEAMVEA--ALSKFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  85 VLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGsiqGNTDG 164
Cdd:cd05345  82 ILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQ-----------GGGVIINIASTAG---LRPRP 147

                       170       180       190
                ....*....|....*....|....*....|....*
gi 24640547 165 GMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHP 199
Cdd:cd05345 148 GLTWYNASKGWVVTATKAMAVELAPRNIRVNCLCP 182
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-203 1.06e-06

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: 48.48  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALL-----------NLPqppqhlfttcRNREQAKELEDLAKNHsnIHILEIDLRNFDAYDKLVA 72
Cdd:cd08930   5 ILITGAAGLIGKAFCKALLsagarliladiNAP----------ALEQLKEELTNLYKNR--VIALELDITSKESIKELIE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  73 DIEGVTKDqgLNVLFNNAGIAPK--SARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIIN 150
Cdd:cd08930  73 SYLEKFGR--IDILINNAYPSPKvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQ-----------GKGSIIN 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 151 MSSILGSIQGN----TDGGMYA---YRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVK 203
Cdd:cd08930 140 IASIYGVIAPDfriyENTQMYSpveYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL 199
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
4-204 1.10e-06

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 48.43  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITG--CNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEDLAKNHSNIhILEIDLRNFDAYDKLVADIeGVTKDq 81
Cdd:PRK08690   9 ILITGmiSERSIAYGIAKACRE--QGAELAFTYVVDKLEERVRKMAAELDSEL-VFRCDVASDDEINQVFADL-GKHWD- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIAPKSARitavrSQELLDTLQTNTV-VPIMLAKACLPLLKKAAKanesqPMGVGRAAIINMSSILGSIQG 160
Cdd:PRK08690  84 GLDGLVHSIGFAPKEAL-----SGDFLDSISREAFnTAHEISAYSLPALAKAAR-----PMMRGRNSAIVALSYLGAVRA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640547  161 ----NTDGgmyayrTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK08690 154 ipnyNVMG------MAKASLEAGIRFTAACLGKEGIRCNGISAGPIKT 195
PRK06181 PRK06181
SDR family oxidoreductase;
4-216 1.37e-06

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 48.05  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGlglvKAL-LNLPQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIegVTKDQ 81
Cdd:PRK06181   4 VIITGASEGIG----RALaVRLARAGAQLVLAARNETRLASLaQELADHGGEALVVPTDVSDAEACERLIEAA--VARFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIApKSARITAVRSQELLDTL-QTNTVVPIMLAKACLPLLKKAakanesqpmgvgRAAIINMSSILGSIQG 160
Cdd:PRK06181  78 GIDILVNNAGIT-MWSRFDELTDLSVFERVmRVNYLGAVYCTHAALPHLKAS------------RGQIVVVSSLAGLTGV 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640547  161 NTDGGmyaYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD-----MGGSSAPLDVP 216
Cdd:PRK06181 145 PTRSG---YAASKHALHGFFDSLRIELADDGVAVTVVCPGFVATDirkraLDGDGKPLGKS 202
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 5-206 1.38e-06

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 47.81  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvTKDQGL 83
Cdd:PRK12937   9 IVTGASRGIGAAIARRLAA--DGFAVAVNYAGSAAAADELvAEIEAAGGRAIAVQADVADAAAVTRLFDAAE--TAFGRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIAPKSAriTAVRSQELLD-TLQTNTvvpimlaKACLPLLKKAAkanesQPMGVGrAAIINMSSilgSIQGNT 162
Cdd:PRK12937  85 DVLVNNAGVMPLGT--IADFDLEDFDrTIATNL-------RGAFVVLREAA-----RHLGQG-GRIINLST---SVIALP 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640547  163 DGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK12937 147 LPGYGPYAASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 4-212 1.40e-06

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: 47.84  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELedLAKNHSNIHILEIDLRNFDAYDKLvadIEGVTKDQG- 82
Cdd:cd05349   3 VLVTGASRGLGAAIARSFAR--EGARVVVNYYRSTESAEAV--AAEAGERAIAIQADVRDRDQVQAM---IEEAKNHFGp 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 LNVLFNNAgIAPKS----ARITA--VRSQELLDTLQTNTVVPIMLAKACLPLLKKaakanesqpMGVGRaaIINMSSilg 156
Cdd:cd05349  76 VDTIVNNA-LIDFPfdpdQRKTFdtIDWEDYQQQLEGAVKGALNLLQAVLPDFKE---------RGSGR--VINIGT--- 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24640547 157 SIQGNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIM--CVSlhPGWVK-TDMGGSSAP 212
Cdd:cd05349 141 NLFQNPVVPYHDYTTAKAALLGFTRNMAKELGPYGITvnMVS--GGLLKvTDASAATPK 197
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 4-207 1.43e-06

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: 48.23  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGlglVKALLNLPQPPQHLFTTCRNREQ----AKELEDLAKNHsNIHILEIDLRNFDAYDKLVADIegVTK 79
Cdd:cd09807   4 VIITGANTGIG---KETARELARRGARVIMACRDMAKceeaAAEIRRDTLNH-EVIVRHLDLASLKSIRAFAAEF--LAE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  80 DQGLNVLFNNAGI--APKSARITAVRSQelldtLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgraaIINMSSIL-- 155
Cdd:cd09807  78 EDRLDVLINNAGVmrCPYSKTEDGFEMQ-----FGVNHLGHFLLTNLLLDLLKKSAPSR-----------IVNVSSLAhk 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640547 156 -GSIqgNTD--------GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMG 207
Cdd:cd09807 142 aGKI--NFDdlnseksyNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELG 200
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 60-215 1.77e-06

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: 47.84  E-value: 1.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  60 DLRNFDAYDKLVAdiEGVTKDQGLNVLFNNAGI-APKSARITAVRSQELLDTLQTNTVVPIMLAKaclpllkKAAKANES 138
Cdd:cd05326  59 DVTVEADVRAAVD--TAVARFGRLDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVYGAFLGTK-------HAARVMIP 129

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24640547 139 QpmgvGRAAIINMSSILGSIQGntdGGMYAYRTSKSALNAATKSLSVDLYPQ--RIMCVSlhPGWVKTDMGGSSAPLDV 215
Cdd:cd05326 130 A----KKGSIVSVASVAGVVGG---LGPHAYTASKHAVLGLTRSAATELGEHgiRVNCVS--PYGVATPLLTAGFGVED 199
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 3-166 2.25e-06

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 47.51  E-value: 2.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   3 SILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvTKDQ 81
Cdd:cd09810   3 TVVITGASSGLGLAAAKALAR--RGEWHVVMACRDFLKAEQaAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFR--RTGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqpmgvgrAAIInmssILGSIQGN 161
Cdd:cd09810  79 PLDALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENAS---------PRIV----IVGSITHN 145


                ....*..
gi 24640547 162 TD--GGM 166
Cdd:cd09810 146 PNtlAGN 152
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
37-206 2.67e-06

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 47.03  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   37 NREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQGLNVLFNNAGIAPKSaritavrsqeLLDTL---Q 112
Cdd:PRK08643  35 NEETAQAAaDKLSKDGGKAIAVKADVSDRDQVFAAVR--QVVDTFGDLNVVVNNAGVAPTT----------PIETIteeQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  113 TNTVVPIMLaKACLPLLKKAAKANESQPMGvGRaaIINMSSILGSIqGNTdgGMYAYRTSKSALNAATKSLSVDLYPQRI 192
Cdd:PRK08643 103 FDKVYNINV-GGVIWGIQAAQEAFKKLGHG-GK--IINATSQAGVV-GNP--ELAVYSSTKFAVRGLTQTAARDLASEGI 175

                        170
                 ....*....|....
gi 24640547  193 MCVSLHPGWVKTDM 206
Cdd:PRK08643 176 TVNAYAPGIVKTPM 189
PRK07454 PRK07454
SDR family oxidoreductase;
1-204 3.11e-06

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 46.88  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIegvtK 79
Cdd:PRK07454   6 MPRALITGASSGIGKATALAF---AKAGWDLALVARSQDALEALaAELRSTGVKAAAYSIDLSNPEAIAPGIAEL----L 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   80 DQGL--NVLFNNAGIApksaRITAVRSQELLD---TLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSI 154
Cdd:PRK07454  79 EQFGcpDVLINNAGMA----YTGPLLEMPLSDwqwVIQLNLTSVFQCCSAVLPGMRAR-----------GGGLIINVSSI 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640547  155 LGSiqgNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK07454 144 AAR---NAFPQWGAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNT 190
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 5-209 3.19e-06

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: 47.15  E-value: 3.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALLNLPQPpqhLFTTCRNREQ-AKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIegVTKDQGL 83
Cdd:cd08945   7 LVTGATSGIGLAIARRLGKEGLR---VFVCARGEEGlATTVKELREAGVEADGRTCDVRSVPEIEALVAAA--VARYGPI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGiAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLpllkkaaKANESQPMGVGRaaIINMSSilgsiQGNTD 163
Cdd:cd08945  82 DVLVNNAG-RSGGGATAELADELWLDVVETNLTGVFRVTKEVL-------KAGGMLERGTGR--IINIAS-----TGGKQ 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24640547 164 GGMYA--YRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGS 209
Cdd:cd08945 147 GVVHAapYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAAS 194
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 3-231 3.32e-06

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: 46.90  E-value: 3.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   3 SILITGCNRGLGLGLVKALLnlpqppqhlfttcrnREQAK---------ELEDLAKNHSNIHILEIDLRNFDAYDKLVAD 73
Cdd:cd05371   4 VAVVTGGASGLGLATVERLL---------------AQGAKvvildlpnsPGETVAKLGDNCRFVPVDVTSEKDVKAALAL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  74 IegVTKDQGLNVLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAkACLPLLKKAAKA-NESQPMGVG-RAAIINM 151
Cdd:cd05371  69 A--KAKFGRLDIVVNCAGIAV-AAKTYNKKGQQPHSLELFQRVINVNLI-GTFNVIRLAAGAmGKNEPDQGGeRGVIINT 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547 152 SSILGsiqgnTDG--GMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMgGSSAPLDVPTSTGQIVQTISKL 229
Cdd:cd05371 145 ASVAA-----FEGqiGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPL-LAGLPEKVRDFLAKQVPFPSRL 218


                ..
gi 24640547 230 GE 231
Cdd:cd05371 219 GD 220
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 5-228 5.58e-06

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 46.15  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQGL 83
Cdd:PRK12935  10 IVTGGAKGIGKAITVALAQ--EGAKVVINYNSSKEAAENLvNELGKEGHDVYAVQADVSKVEDANRLVE--EAVNHFGKV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIapksariTAVRSQELLDTLQTNTVVPIMLAK------ACLPLLKKAAKanesqpmgvGRaaIINMSSILGS 157
Cdd:PRK12935  86 DILVNNAGI-------TRDRTFKKLNREDWERVIDVNLSSvfnttsAVLPYITEAEE---------GR--IISISSIIGQ 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640547  158 IQGNtdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMgGSSAPLDVptsTGQIVQTISK 228
Cdd:PRK12935 148 AGGF---GQTNYSAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEM-VAEVPEEV---RQKIVAKIPK 211
PRK05866 PRK05866
SDR family oxidoreductase;
55-206 5.63e-06

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 46.27  E-value: 5.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   55 HILEIDLRNFDAYDKLVADIEGvtKDQGLNVLFNNAGiapKSARITAVRSqelLD-------TLQTNTVVPIMLAKACLP 127
Cdd:PRK05866  92 MAVPCDLSDLDAVDALVADVEK--RIGGVDILINNAG---RSIRRPLAES---LDrwhdverTMVLNYYAPLRLIRGLAP 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  128 LLKKAakanesqpmgvGRAAIINMSSilgsiQGNTDGGM---YAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK05866 164 GMLER-----------GDGHIINVAT-----WGVLSEASplfSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVAT 227


                 ..
gi 24640547  205 DM 206
Cdd:PRK05866 228 PM 229
PRK06128 PRK06128
SDR family oxidoreductase;
82-216 6.03e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 46.39  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLkkaakanesqPMGvgrAAIINMssilGSIQG- 160
Cdd:PRK06128 134 GLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL----------PPG---ASIINT----GSIQSy 196

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24640547  161 NTDGGMYAYRTSKSALNAATKSLSVDLYPQ--RIMCVSLHPGWVKTDMGGSSAPLDVP 216
Cdd:PRK06128 197 QPSPTLLDYASTKAAIVAFTKALAKQVAEKgiRVNAVAPGPVWTPLQPSGGQPPEKIP 254
PRK09730 PRK09730
SDR family oxidoreductase;
1-214 6.45e-06

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 46.00  E-value: 6.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    1 MNSILITGCNRGLGLGlvKALLNLPQPPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvTK 79
Cdd:PRK09730   1 MAIALVTGGSRGIGRA--TALLLAQEGYTVAVNYQQNLHAAQEvVNLITQAGGKAFVLQADISDENQVVAMFTAID--QH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   80 DQGLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVvpimlakACLPLLKKAAKANESQPMGVGrAAIINMSSI---LG 156
Cdd:PRK09730  77 DEPLAALVNNAGILFTQCTVENLTAERINRVLSTNVT-------GYFLCCREAVKRMALKHGGSG-GAIVNVSSAasrLG 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640547  157 SiqgntDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM---GGSSAPLD 214
Cdd:PRK09730 149 A-----PGEYVDYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMhasGGEPGRVD 204
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 4-216 6.83e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 46.05  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELedlaknhSNIHILEIDLRNFDAYDKLVADIegVTKDQGL 83
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLA---RAGYRVFGTSRNPARAAPI-------PGVELLELDVTDDASVQAAVDEV--IARAGRI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGI----APKSARITavRSQELLDTlqtNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSILGSIQ 159
Cdd:PRK06179  75 DVLVNNAGVglagAAEESSIA--QAQALFDT---NVFGILRMTRAVLPHMRAQ---------GSGR--IINISSVLGFLP 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547  160 GNTdggMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPLDVP 216
Cdd:PRK06179 139 APY---MALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPDSP 192
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 5-204 7.68e-06

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 45.65  E-value: 7.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQGLN 84
Cdd:PRK12429   8 LVTGAASGIGLEIALALAK--EGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGID--YAVETFGGVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNAGIapksariTAVRSQELLDTLQTNTVVPIML------AKACLPLLKKAakanesqpmGVGRaaIINMSSILGSI 158
Cdd:PRK12429  84 ILVNNAGI-------QHVAPIEDFPTEKWKKMIAIMLdgafltTKAALPIMKAQ---------GGGR--IINMASVHGLV 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24640547  159 qgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK12429 146 ---GSAGKAAYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-206 1.24e-05

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 45.13  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVkalLNLPQPPQHLFTTCRNRE--QAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTKDQg 82
Cdd:cd09763   7 LVTGASRGIGRGIA---LQLGEAGATVYITGRTILpqLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQGR- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  83 LNVLFNNA-----GIAPKSARITAVRSQELLDTLQTntvVPIMLAKAC----LPLLKKAakanesqpmgvGRAAIINMSS 153
Cdd:cd09763  83 LDILVNNAyaavqLILVGVAKPFWEEPPTIWDDINN---VGLRAHYACsvyaAPLMVKA-----------GKGLIVIISS 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24640547 154 iLGSIQGntdggMY--AYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd09763 149 -TGGLEY-----LFnvAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTEL 197
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 4-206 1.60e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 44.74  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNREQAKE-LEDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvtKDQG 82
Cdd:PRK08085  12 ILITGSAQGIGFLLATGL---AEYGAEIIINDITAERAELaVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIE---KDIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 -LNVLFNNAGIAPKSArITAVRSQELLDTLQTNTVVPIMLAKAclpLLKKAAKANesqpmgvgRAAIINMSSILGSIQGN 161
Cdd:PRK08085  86 pIDVLINNAGIQRRHP-FTEFPEQEWNDVIAVNQTAVFLVSQA---VARYMVKRQ--------AGKIINICSMQSELGRD 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24640547  162 TdggMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK08085 154 T---ITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEM 195
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 4-210 2.34e-05

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: 44.38  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKnhsnihILEIDLRNFDAYDKLVADIEgvTKDQGL 83
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLL---QAGATVIALDLPFVLLLEYGDPLR------LTPLDVADAAAVREVCSRLL--AEHGPI 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSilgSIQGNTD 163
Cdd:cd05331  70 DALVNCAGVL-RPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDR-----------RTGAIVTVAS---NAAHVPR 134

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24640547 164 GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSS 210
Cdd:cd05331 135 ISMAAYGASKAALASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTL 181
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
3-206 2.58e-05

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 44.25  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLnlpqppqhlfttcrnREQAK-ELEDLAKNHSNIHILEI---------DLRNFDAYDKLVA 72
Cdd:PRK07067   8 VALLTGAASGIGEAVAERYL---------------AEGARvVIADIKPARARLAALEIgpaaiavslDVTRQDSIDRIVA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   73 diEGVTKDQGLNVLFNNAGI---APksarITAVrSQELLDTLQTNTVvpimlaKACLPLLKKAAKANESQPMGvgrAAII 149
Cdd:PRK07067  73 --AAVERFGGIDILFNNAALfdmAP----ILDI-SRDSYDRLFAVNV------KGLFFLMQAVARHMVEQGRG---GKII 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24640547  150 NMSSILGSiQGntDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK07067 137 NMASQAGR-RG--EALVSHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPM 190
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 4-202 4.22e-05

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 43.59  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKNhsNIHILEIDLRNFDAYDKLVADIEGVTKDqgL 83
Cdd:PRK10538   3 VLVTGATAGFGECITRRFI---QQGHKVIATGRRQERLQELKDELGD--NLYIAQLDVRNRAAIEEMLASLPAEWRN--I 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   84 NVLFNNAGIA--PKSARITAVRSQELLdtLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGS---I 158
Cdd:PRK10538  76 DVLVNNAGLAlgLEPAHKASVEDWETM--IDTNNKGLVYMTRAVLPGMVER-----------NHGHIINIGSTAGSwpyA 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24640547  159 QGNTDGGMYAYrTSKSALNaatksLSVDLYPQRIMCVSLHPGWV 202
Cdd:PRK10538 143 GGNVYGATKAF-VRQFSLN-----LRTDLHGTAVRVTDIEPGLV 180
PRK06172 PRK06172
SDR family oxidoreductase;
83-206 5.72e-05

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 43.20  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIAPKSARItAVRSQELLDTLQTNTVVPIMLA-KACLPLLKKAakanesqpmgvGRAAIINMSSILGSIQGN 161
Cdd:PRK06172  85 LDYAFNNAGIEIEQGRL-AEGSEAEFDAIMGVNVKGVWLCmKYQIPLMLAQ-----------GGGAIVNTASVAGLGAAP 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 24640547  162 tdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK06172 153 ---KMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDM 194
PRK07035 PRK07035
SDR family oxidoreductase;
5-204 5.86e-05

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 43.08  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKAllnLPQPPQHLFTTCRNRE--QAKELEDLAKNHS----NIHILEIdlrnfdayDKLVADIEGVT 78
Cdd:PRK07035  12 LVTGASRGIGEAIAKL---LAQQGAHVIVSSRKLDgcQAVADAIVAAGGKaealACHIGEM--------EQIDALFAHIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   79 KDQG-LNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGS 157
Cdd:PRK07035  81 ERHGrLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQ-----------GGGSIVNVASVNGV 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24640547  158 IQGNTDGgmyAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK07035 150 SPGDFQG---IYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDT 193
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-205 6.32e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 42.94  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLG----LGLVKA-----LLNLPQPpqhlfttcrnREQAKELEDLAKNHSNIhilEIDLRNFDAYDKLVAdiE 75
Cdd:PRK08993  14 VVTGCDTGLGqgmaLGLAEAgcdivGINIVEP----------TETIEQVTALGRRFLSL---TADLRKIDGIPALLE--R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   76 GVTKDQGLNVLFNNAGIAPKSARITaVRSQELLDTLQTNTVVPIMLAKAclpllkkAAKANESQPMGvgrAAIINMSSIL 155
Cdd:PRK08993  79 AVAEFGHIDILVNNAGLIRREDAIE-FSEKDWDDVMNLNIKSVFFMSQA-------AAKHFIAQGNG---GKIINIASML 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640547  156 gSIQGNTDggMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:PRK08993 148 -SFQGGIR--VPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN 194
PRK08703 PRK08703
SDR family oxidoreductase;
4-205 6.48e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 43.00  E-value: 6.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALlnlpqpPQHLFTTCRNREQAKELED-----LAKNHSNIHILEIDLRNF--DAYDKLVADIEG 76
Cdd:PRK08703   9 ILVTGASQGLGEQVAKAY------AAAGATVILVARHQKKLEKvydaiVEAGHPEPFAIRFDLMSAeeKEFEQFAATIAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   77 VTKDQgLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAKANesqPMGVGRAAIINMSSILG 156
Cdd:PRK08703  83 ATQGK-LDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDAS---VIFVGESHGETPKAYWG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24640547  157 siqgntdggmyAYRTSKSALNAATK----------SLSVDLY-------PQRImcvSLHPGWVKTD 205
Cdd:PRK08703 159 -----------GFGASKAALNYLCKvaadewerfgNLRANVLvpgpinsPQRI---KSHPGEAKSE 210
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
4-154 6.71e-05

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 43.04  E-value: 6.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLpqpPQHLFTTCRNREQAKELEDLAknhsNIHILEIDLRNFDAYDKLVADIEGVtkdqgl 83
Cdd:COG0451   2 ILVTGGAGFIGSHLARRLLAR---GHEVVGLDRSPPGAANLAALP----GVEFVRGDLRDPEALAAALAGVDAV------ 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640547  84 nvlFNNAGIApksaritAVRSQELLDTLQTNTVVPIMLAKAClpllkKAAkanesqpmGVGRaaIINMSSI 154
Cdd:COG0451  69 ---VHLAAPA-------GVGEEDPDETLEVNVEGTLNLLEAA-----RAA--------GVKR--FVYASSS 114
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 5-205 6.72e-05

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: 43.14  E-value: 6.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKAL--------LNLPQPPqhlfttcrnrEQAKELEDLAKNHSNIHIL-EIDLRNFDAYDKLVAdiE 75
Cdd:cd05358   7 LVTGASSGIGKAIAIRLataganvvVNYRSKE----------DAAEEVVEEIKAVGGKAIAvQADVSKEEDVVALFQ--S 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  76 GVTKDQGLNVLFNNAGIAPKSA--RITAVRSQELLDTlqtNTVVPIMLAKACLPLLKKaakaneSQPMGVgraaIINMSS 153
Cdd:cd05358  75 AIKEFGTLDILVNNAGLQGDASshEMTLEDWNKVIDV---NLTGQFLCAREAIKRFRK------SKIKGK----IINMSS 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24640547 154 ILGSIQGntdGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:cd05358 142 VHEKIPW---PGHVNYAASKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTP 190
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 5-204 7.07e-05

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 42.91  E-value: 7.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALlnlPQPPQHLFTTCRNRE------QAKELEDLAKNHSNIHILEIDLRnfdayDKLVAdiEGVT 78
Cdd:cd08936  14 LVTASTDGIGLAIARRL---AQDGAHVVVSSRKQQnvdravATLQGEGLSVTGTVCHVGKAEDR-----ERLVA--TAVN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  79 KDQGLNVLFNNAGIAPKSARITAVrSQELLD-TLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGS 157
Cdd:cd08936  84 LHGGVDILVSNAAVNPFFGNILDS-TEEVWDkILDVNVKATALMTKAVVPEMEKR-----------GGGSVVIVSSVAAF 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24640547 158 iqgNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:cd08936 152 ---HPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT 195
PRK06123 PRK06123
SDR family oxidoreductase;
2-209 1.11e-04

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 42.46  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    2 NSILITGCNRGLGLGLvkALLNLPQPPQHLFTTCRNREQAKELEDLAKNHSNIHI-------LEID-LRNFDAYDKLVAD 73
Cdd:PRK06123   3 KVMIITGASRGIGAAT--ALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALavaadvaDEADvLRLFEAVDRELGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   74 iegvtkdqgLNVLFNNAGIAPKSARITAVRSQELLDTLQTNTVVPIMLAKaclpllkKAAKANESQPMGVGrAAIINMSS 153
Cdd:PRK06123  81 ---------LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAR-------EAVKRMSTRHGGRG-GAIVNVSS 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24640547  154 I---LGSIQGNTDggmyaYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGS 209
Cdd:PRK06123 144 MaarLGSPGEYID-----YAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHAS 197
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 3-206 1.18e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 42.48  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQ----AKELEDLAKNHSnIHILEIDLRNFDAYDKLVADIEGVT 78
Cdd:PRK05875   9 TYLVTGGGSGIGKGVAAGLV---AAGAAVMIVGRNPDKlaaaAEEIEALKGAGA-VRYEPADVTDEDQVARAVDAATAWH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   79 KdqGLNVLFNNAGIAPKSARITAVRSQELLDTLQTNtVVPIMLakaclpLLKKAAKAnesqPMGVGRAAIINMSSILGSi 158
Cdd:PRK05875  85 G--RLHGVVHCAGGSETIGPITQIDSDAWRRTVDLN-VNGTMY------VLKHAARE----LVRGGGGSFVGISSIAAS- 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640547  159 qgNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK05875 151 --NTHRWFGAYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDL 196
PRK12742 PRK12742
SDR family oxidoreductase;
3-213 1.27e-04

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 42.05  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLNlpQPPQHLFTTCRNREQAKELEdlAKNHSNIhiLEIDLRNFDAYdklvadIEGVTKDQG 82
Cdd:PRK12742   8 KVLVLGGSRGIGAAIVRRFVT--DGANVRFTYAGSKDAAERLA--QETGATA--VQTDSADRDAV------IDVVRKSGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIAPKSARITaVRSQELLDTLQTNTVVPimlakaclplLKKAAKANESQPMGvGRAAIInmssilGSIQGNT 162
Cdd:PRK12742  76 LDILVVNAGIAVFGDALE-LDADDIDRLFKINIHAP----------YHASVEAARQMPEG-GRIIII------GSVNGDR 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24640547  163 D--GGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGGSSAPL 213
Cdd:PRK12742 138 MpvAGMAAYAASKSALQGMARGLARDFGPRGITINVVQPGPIDTDANPANGPM 190
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 4-204 2.14e-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: 41.36  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKALLNLpqpPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVAdiEGVTKDQGL 83
Cdd:cd08937   7 VVVTGAAQGIGRGVAERLAGE---GARVLLVDRSELVHEVLAEILAAGDAAHVHTADLETYAGAQGVVR--AAVERFGRV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  84 NVLFNNAG---IAP-----KSARITAVRSQELLDTLQT-NTVVPIMLAKaclpllkkaakanesqpmgvGRAAIINMSSI 154
Cdd:cd08937  82 DVLINNVGgtiWAKpyehyEEEQIEAEIRRSLFPTLWCcRAVLPHMLER--------------------QQGVIVNVSSI 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24640547 155 lgsiqgNTDGGMYA-YRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:cd08937 142 ------ATRGIYRIpYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEA 186
PRK12743 PRK12743
SDR family oxidoreductase;
38-208 2.34e-04

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 41.17  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   38 REQAKELEDLAKNHSNIHIleiDLRNF----DAYDKLVADIegvtkdQGLNVLFNNAGIAPKSARITavrsqelLDTLQT 113
Cdd:PRK12743  41 KETAEEVRSHGVRAEIRQL---DLSDLpegaQALDKLIQRL------GRIDVLVNNAGAMTKAPFLD-------MDFDEW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  114 NTVVPIMLAKACLpLLKKAAKANESQPMGvGRaaIINMSSILGSIQGNTDGgmyAYRTSKSALNAATKSLSVDLYPQRIM 193
Cdd:PRK12743 105 RKIFTVDVDGAFL-CSQIAARHMVKQGQG-GR--IINITSVHEHTPLPGAS---AYTAAKHALGGLTKAMALELVEHGIL 177

                        170
                 ....*....|....*
gi 24640547  194 CVSLHPGWVKTDMGG 208
Cdd:PRK12743 178 VNAVAPGAIATPMNG 192
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 82-209 2.52e-04

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 41.24  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   82 GLNVLFNNAGIAPKSARITAvrSQELLDT-LQTNtvvpIMLAKACLPLLKKAAKANesqpmgvgrAAIINMSSILGSIQG 160
Cdd:PRK06077  84 VADILVNNAGLGLFSPFLNV--DDKLIDKhISTD----FKSVIYCSQELAKEMREG---------GAIVNIASVAGIRPA 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 24640547  161 NtdgGMYAYRTSKSALNAATKSLSVDLYPqRIMCVSLHPGWVKTDMGGS 209
Cdd:PRK06077 149 Y---GLSIYGAMKAAVINLTKYLALELAP-KIRVNAIAPGFVKTKLGES 193
PRK06138 PRK06138
SDR family oxidoreductase;
5-206 2.88e-04

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 40.91  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCnrGLGLGLVKALLnLPQPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGvtKDQGLN 84
Cdd:PRK06138   9 IVTGA--GSGIGRATAKL-FAREGARVVVADRDAEAAERVAAAIAAGGRAFARQGDVGSAEAVEALVDFVAA--RWGRLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNAGIAPKSARITAvrSQELLDTLQTNTVVPIML-AKACLPLLKKAakanesqpmgvGRAAIINMSSILG--SIQGN 161
Cdd:PRK06138  84 VLVNNAGFGCGGTVVTT--DEADWDAVMRVNVGGVFLwAKYAIPIMQRQ-----------GGGSIVNTASQLAlaGGRGR 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 24640547  162 TdggmyAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK06138 151 A-----AYVASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 5-204 8.21e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 39.75  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALlnlpqpPQHLFTTCRN-REQAK---ELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGvtkD 80
Cdd:PRK07523  14 LVTGSSQGIGYALAEGL------AQAGAEVILNgRDPAKlaaAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEA---E 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QG-LNVLFNNAGIAPKSA--RITAVRSQELldtLQTNTVVPIMLAKAClpllkkaakaneSQPM-GVGRAAIINMSSILG 156
Cdd:PRK07523  85 IGpIDILVNNAGMQFRTPleDFPADAFERL---LRTNISSVFYVGQAV------------ARHMiARGAGKIINIASVQS 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640547  157 SIqgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK07523 150 AL---ARPGIAPYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 5-206 8.34e-04

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: 39.64  E-value: 8.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGlglvKAL-LNLPQPPQHLFTTCR-NREQAKEL-EDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvTKDQ 81
Cdd:cd05359   2 LVTGGSRGIG----KAIaLRLAERGADVVINYRkSKDAAAEVaAEIEELGGKAVVVRADVSQPQDVEEMFAAVK--ERFG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  82 GLNVLFNNAGIAPKS--ARITAVrsqELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmGVGRaaIINMSSiLGSIQ 159
Cdd:cd05359  76 RLDVLVSNAAAGAFRplSELTPA---HWDAKMNTNLKALVHCAQQAAKLMRER---------GGGR--IVAISS-LGSIR 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24640547 160 GNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:cd05359 141 ALP--NYLAVGTAKAALEALVRYLAVELGPRGIRVNAVSPGVIDTDA 185
PRK07024 PRK07024
SDR family oxidoreductase;
4-206 8.56e-04

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 39.53  E-value: 8.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREqakELEDLAKNHSN---IHILEIDLRNFDAYDKLVADIEGvtkD 80
Cdd:PRK07024   5 VFITGASSGIGQALAREYA---RQGATLGLVARRTD---ALQAFAARLPKaarVSVYAADVRDADALAAAAADFIA---A 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   81 QGL-NVLFNNAGIApksaRITAVRSQELLDTLQ----TNTvvpIMLAKACLPLLkkaakanesQPM-GVGRAAIINMSSI 154
Cdd:PRK07024  76 HGLpDVVIANAGIS----VGTLTEEREDLAVFRevmdTNY---FGMVATFQPFI---------APMrAARRGTLVGIASV 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24640547  155 LGsIQGNTDGGmyAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK07024 140 AG-VRGLPGAG--AYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPM 188
PRK06500 PRK06500
SDR family oxidoreductase;
5-208 9.37e-04

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 39.55  E-value: 9.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpqPPQHLFTTCRNREQAKEledlAKNH--SNIHILEIDLRNFDAYDKLVADIegvtKDQG 82
Cdd:PRK06500  10 LITGGTSGIGLETARQFLA---EGARVAITGRDPASLEA----ARAElgESALVIRADAGDVAAQKALAQAL----AEAF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 --LNVLFNNAGIApKSARITAVrSQELLD-TLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvgrAAIINmssilGSIq 159
Cdd:PRK06500  79 grLDAVFINAGVA-KFAPLEDW-DEAMFDrSFNTNVKGPYFLIQALLPLLANPA------------SIVLN-----GSI- 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 24640547  160 gNTDGGM---YAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGG 208
Cdd:PRK06500 139 -NAHIGMpnsSVYAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYG 189
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 5-207 9.79e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 39.64  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKELEDLAKNHSNIHILeiDLRNFDAYDKLVADIEGVTkdQGLN 84
Cdd:PRK06841  19 VVTGGASGIGHAIAELFA---AKGARVALLDRSEDVAEVAAQLLGGNAKGLVC--DVSDSQSVEAAVAAVISAF--GRID 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNAGIAPkSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAakanesqpmgvGRAAIINMSSILGSIQGNtdg 164
Cdd:PRK06841  92 ILVNSAGVAL-LAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAA-----------GGGKIVNLASQAGVVALE--- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 24640547  165 GMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMG 207
Cdd:PRK06841 157 RHVAYCASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELG 199
PRK05854 PRK05854
SDR family oxidoreductase;
5-176 9.79e-04

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 39.66  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKAL------LNLPqppqhlfttCRNR---EQAKELEDLAKNHSNIHILEIDLRNFDAY----DKLV 71
Cdd:PRK05854  18 VVTGASDGLGLGLARRLaaagaeVILP---------VRNRakgEAAVAAIRTAVPDAKLSLRALDLSSLASVaalgEQLR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   72 ADiegvtkDQGLNVLFNNAGIAPKSARITAVRSQELldTLQTNTVVPIMLAKACLPLLKkaakanesqpmgVGRAAIINM 151
Cdd:PRK05854  89 AE------GRPIHLLINNAGVMTPPERQTTADGFEL--QFGTNHLGHFALTAHLLPLLR------------AGRARVTSQ 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24640547  152 SSIL---GSIqgNTD--------GGMYAYRTSKSAL 176
Cdd:PRK05854 149 SSIAarrGAI--NWDdlnwersyAGMRAYSQSKIAV 182
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 4-200 1.60e-03

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: 39.12  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   4 ILITGCNRGLGLGLVKAllnLPQPPQHLFTTCRNREQAKE-----LEDLAKnhSNIHILEIDLRNFDAYDKLVADIEgvT 78
Cdd:cd09809   4 IIITGANSGIGFETARS---FALHGAHVILACRNMSRASAavsriLEEWHK--ARVEAMTLDLASLRSVQRFAEAFK--A 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  79 KDQGLNVLFNNAGIAPKSARITavrSQELLDTLQTNTVVPIMLAKACLPLLKKAAKA------NESQPMGVGRAAIINMS 152
Cdd:cd09809  77 KNSPLHVLVCNAAVFALPWTLT---EDGLETTFQVNHLGHFYLVQLLEDVLRRSAPArvivvsSESHRFTDLPDSCGNLD 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24640547 153 SILGSIQGNTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPG 200
Cdd:cd09809 154 FSLLSPPKKKYWSMLAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 5-206 2.05e-03

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 38.33  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpqppQHLFTTcrnreqAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEGVTKdqGLN 84
Cdd:PRK08220  12 WVTGAAQGIGYAVALAFVE-----AGAKVI------GFDQAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETG--PLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvgRAAIINMSSilgsiqgNTDG 164
Cdd:PRK08220  79 VLVNAAGIL-RMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQR-----------SGAIVTVGS-------NAAH 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24640547  165 ----GMYAYRTSKSALNAATKSLSVDLYPQRIMC--VSlhPGWVKTDM 206
Cdd:PRK08220 140 vpriGMAAYGASKAALTSLAKCVGLELAPYGVRCnvVS--PGSTDTDM 185
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 68-208 2.42e-03

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 38.36  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   68 DKLVADIEGVtkdqglNVLFNNAGIApKSARITAVRSQELLDTLQTNTVVPIMLAKAClpllkkaakaneSQPMGVGR-A 146
Cdd:PRK12936  72 QKAEADLEGV------DILVNNAGIT-KDGLFVRMSDEDWDSVLEVNLTATFRLTREL------------THPMMRRRyG 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24640547  147 AIINMSSILGsIQGNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDMGG 208
Cdd:PRK12936 133 RIINITSVVG-VTGNP--GQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTG 191
PRK08589 PRK08589
SDR family oxidoreductase;
5-204 2.64e-03

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 38.22  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVKALLNlpqPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRNFDAYDKLVADIEgvTKDQGLN 84
Cdd:PRK08589  10 VITGASTGIGQASAIALAQ---EGAYVLAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIK--EQFGRVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   85 VLFNNAGIAPKSARITAVrSQELLDT----------LQTNTVVPIMLAKAclpllkkaakanesqpmgvgrAAIINMSSI 154
Cdd:PRK08589  85 VLFNNAGVDNAAGRIHEY-PVDVFDKimavdmrgtfLMTKMLLPLMMEQG---------------------GSIINTSSF 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 24640547  155 LGSIqgnTDGGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKT 204
Cdd:PRK08589 143 SGQA---ADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 4-205 2.74e-03

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 38.20  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    4 ILITGCNRGLGLGLVKALLNlpqPPQHLFTTCRNREQAKELEDLAKNHSNIHILEIDLRN--------------FDAYDK 69
Cdd:PRK05786   8 VAIIGVSEGLGYAVAYFALK---EGAQVCINSRNENKLKRMKKTLSKYGNIHYVVGDVSStesarnviekaakvLNAIDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   70 LVADIEGVTKDqglnvlfnnagiapksariTAVRSQELLDTLQTNTVVPIMLAKACLPLLKKAAkanesqpmgvgraAII 149
Cdd:PRK05786  85 LVVTVGGYVED-------------------TVEEFSGLEEMLTNHIKIPLYAVNASLRFLKEGS-------------SIV 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24640547  150 NMSSIlgsiqgntdGGMY-------AYRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTD 205
Cdd:PRK05786 133 LVSSM---------SGIYkaspdqlSYAVAKAGLAKAVEILASELLGRGIRVNGIAPTTISGD 186
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 3-94 2.76e-03

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 38.10  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    3 SILITGCNRGLGLGLVKALLnlpQPPQHLFTTCRNREQAKEL-EDLAKNHS-NIHILEIDLRNFDAYDKLVADIEGVtkd 80
Cdd:PRK06125   9 RVLITGASKGIGAAAAEAFA---AEGCHLHLVARDADALEALaADLRAAHGvDVAVHALDLSSPEAREQLAAEAGDI--- 82

                         90
                 ....*....|....
gi 24640547   81 qglNVLFNNAGIAP 94
Cdd:PRK06125  83 ---DILVNNAGAIP 93
PRK06114 PRK06114
SDR family oxidoreductase;
83-206 5.58e-03

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 37.07  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   83 LNVLFNNAGIApksariTAVRSQELLDTlQTNTVVPIMLAKACLPLLKKAAKANESqpmgvGRAAIINMSSILGSIqgnT 162
Cdd:PRK06114  87 LTLAVNAAGIA------NANPAEEMEEE-QWQTVMDINLTGVFLSCQAEARAMLEN-----GGGSIVNIASMSGII---V 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 24640547  163 DGGMYA--YRTSKSALNAATKSLSVDLYPQRIMCVSLHPGWVKTDM 206
Cdd:PRK06114 152 NRGLLQahYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPM 197
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 5-220 5.58e-03

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 37.73  E-value: 5.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547   5 LITGCNRGLGLGLVKALLN-------------LPQPPQHlfttcrNREQAKELEDLAKnhsNIHILEIDLRNFDAYDKLV 71
Cdd:cd08953 209 LVTGGAGGIGRALARALARrygarlvllgrspLPPEEEW------KAQTLAALEALGA---RVLYISADVTDAAAVRRLL 279

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547  72 ADIEgvTKDQGLNVLFNNAGIaPKSARITAVRSQELLDTLQTNTVVPIMLAKAC--LPLlkkaakanesqpmgvgrAAII 149
Cdd:cd08953 280 EKVR--ERYGAIDGVIHAAGV-LRDALLAQKTAEDFEAVLAPKVDGLLNLAQALadEPL-----------------DFFV 339

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24640547 150 NMSSILGSIqGNTdgGMYAYRTSKSALNAATKSLSVDLYPQRIMCVSLhPGWVKTDMGGSSAPLDVPTSTG 220
Cdd:cd08953 340 LFSSVSAFF-GGA--GQADYAAANAFLDAFAAYLRQRGPQGRVLSINW-PAWREGGMAADLGARELLARAG 406
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 5-149 5.64e-03

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 37.54  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24640547    5 LITGCNRGLGLGLVkalLNLPQPPQHLFTTCRNREQAKELED-LAKNHSNIHILEIDLRNFDAYDKLVADIEGVTKDQGL 83
Cdd:PLN02780  57 LVTGPTDGIGKGFA---FQLARKGLNLVLVARNPDKLKDVSDsIQSKYSKTQIKTVVVDFSGDIDEGVKRIKETIEGLDV 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24640547   84 NVLFNNAGIAPKSARITAVRSQELLDTL----------QTNTVVPIMLAKaclpllKKAAKANesqpMGVGRAAII 149
Cdd:PLN02780 134 GVLINNVGVSYPYARFFHEVDEELLKNLikvnvegttkVTQAVLPGMLKR------KKGAIIN----IGSGAAIVI 199
 
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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