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Conserved domains on  [gi|517341756|ref|WP_018517248|]
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MULTISPECIES: SDR family NAD(P)-dependent oxidoreductase [Rhizobium]

Protein Classification

SDR family NAD(P)-dependent oxidoreductase( domain architecture ID 11437015)

SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to Bacillus subtilis NADPH-dependent reductase BacG, which is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0070403|GO:0016491
SCOP:  4000029

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
7-255 6.63e-79

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: 238.15  E-value: 6.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpGRDLPDfLLTAESE-----RRALLLHADFSAVGGAAQFAEDA 81
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVIT-----DRDAEA-LEAAAAElraagGRALAVAADVTDEAAVEALVAAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGTMlGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIY 161
Cdd:COG1028   78 VAAFGRLDILVNNAGIT-PPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRG-SPGQAAY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER-YSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSG 240
Cdd:COG1028  156 AASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRAlLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASD-AAS 234
                        250
                 ....*....|....*
gi 517341756 241 YITGQVIEINGGQLI 255
Cdd:COG1028  235 YITGQVLAVDGGLTA 249
 
Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
7-255 6.63e-79

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: 238.15  E-value: 6.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpGRDLPDfLLTAESE-----RRALLLHADFSAVGGAAQFAEDA 81
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVIT-----DRDAEA-LEAAAAElraagGRALAVAADVTDEAAVEALVAAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGTMlGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIY 161
Cdd:COG1028   78 VAAFGRLDILVNNAGIT-PPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRG-SPGQAAY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER-YSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSG 240
Cdd:COG1028  156 AASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRAlLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASD-AAS 234
                        250
                 ....*....|....*
gi 517341756 241 YITGQVIEINGGQLI 255
Cdd:COG1028  235 YITGQVLAVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
12-250 3.76e-67

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: 207.52  E-value: 3.76e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVL-ADRNEEA-LAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMlGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALtGGSPGSSIYSASKAFVATY 171
Cdd:cd05233   79 VNNAGIA-RPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGL-RPLPGQAAYAASKAALEGL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517341756 172 SKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQVIEIN 250
Cdd:cd05233  157 TRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDE-ASYITGQVIPVD 234
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-252 7.78e-64

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 199.68  E-value: 7.78e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVH--TGRKPGRDLPDFLltAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAydINEEAAQELLEEI--KEEGGDAIAVKADVSSEEDVENLVEQIVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSsIYSAS 164
Cdd:PRK05565  81 FGKIDILVNNAGISNFG-LVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEV-LYSAS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRkSIPLQRLGTAEDCAPAYLFLAAPSlSGYITG 244
Cdd:PRK05565 159 KGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAE-EIPLGRLGKPEEIAKVVLFLASDD-ASYITG 236

                 ....*...
gi 517341756 245 QVIEINGG 252
Cdd:PRK05565 237 QIITVDGG 244
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
19-252 1.04e-53

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: 173.39  E-value: 1.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   19 RGIGLEVARQFLDCGAKVIVhTGRkpGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVLVNNAGTM 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVL-TDL--NEALAKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   99 LGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNTVSISALTGGsPGSSIYSASKAFVATYSKALAR 177
Cdd:pfam13561  83 PKLKgPFLDTSREDFDRALDVNLYSLFLLAKAALPLMK--EGGSIVNLSSIGAERVV-PNYNAYGAAKAALEALTRYLAV 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517341756  178 ELAPDGIRVNCVSPGTIETEFHERYSSREK-LEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGYITGQVIEINGG 252
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLAASGIPGFDElLAAAEARAPLGRLGTPEEVANAAAFLASD-LASYITGQVLYVDGG 234
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
10-252 5.07e-20

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 86.22  E-value: 5.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLH--------ADFSAVGGAAQFAEDA 81
Cdd:TIGR04504   2 RVALVTGAARGIGAATVRRLAADGWRVVAVDLCADDPAVGYPLATRAELDAVAAACpdqvlpviADVRDPAALAAAVALA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   82 LAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSI--SALTGGSPGSS 159
Cdd:TIGR04504  82 VERWGRLDAAVAAAGVIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARPDPRGGRFVAVasAAATRGLPHLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER----YSSREkLEQTRKSIPLQRLGTAEDCAPAYLFLAA 235
Cdd:TIGR04504 162 AYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAAtarlYGLTD-VEEFAGHQLLGRLLEPEEVAAAVAWLCS 240
                         250
                  ....*....|....*..
gi 517341756  236 PSlSGYITGQVIEINGG 252
Cdd:TIGR04504 241 PA-SSAVTGSVVHADGG 256
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
12-195 4.05e-11

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 60.19  E-value: 4.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756    12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLH---ADFSAVGGAAQFAEDALAFFDRV 88
Cdd:smart00822   3 YLITGGLGGLGRALARWLAERGARRLVLLSRSGPDAPGAAALLAELEAAGARVTvvaCDVADRDALAAVLAAIPAVEGPL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756    89 DVLVNNAGTmLGRFPAATLTDAEYEAVVRlnqtSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYSASKAFV 168
Cdd:smart00822  83 TGVIHAAGV-LDDGVLASLTPERFAAVLA----PKAAGAWNLHELTADLPLDFFVLFSSIAGVL-GSPGQANYAAANAFL 156
                          170       180
                   ....*....|....*....|....*..
gi 517341756   169 AtyskALARELAPDGIRVNCVSPGTIE 195
Cdd:smart00822 157 D----ALAEYRRARGLPALSIAWGAWA 179
 
Name Accession Description Interval E-value
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
7-255 6.63e-79

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: 238.15  E-value: 6.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpGRDLPDfLLTAESE-----RRALLLHADFSAVGGAAQFAEDA 81
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVIT-----DRDAEA-LEAAAAElraagGRALAVAADVTDEAAVEALVAAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGTMlGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIY 161
Cdd:COG1028   78 VAAFGRLDILVNNAGIT-PPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRG-SPGQAAY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER-YSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSG 240
Cdd:COG1028  156 AASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRAlLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASD-AAS 234
                        250
                 ....*....|....*
gi 517341756 241 YITGQVIEINGGQLI 255
Cdd:COG1028  235 YITGQVLAVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
12-250 3.76e-67

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: 207.52  E-value: 3.76e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVL-ADRNEEA-LAELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMlGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALtGGSPGSSIYSASKAFVATY 171
Cdd:cd05233   79 VNNAGIA-RPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGL-RPLPGQAAYAASKAALEGL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517341756 172 SKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQVIEIN 250
Cdd:cd05233  157 TRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDE-ASYITGQVIPVD 234
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-252 7.78e-64

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 199.68  E-value: 7.78e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVH--TGRKPGRDLPDFLltAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAydINEEAAQELLEEI--KEEGGDAIAVKADVSSEEDVENLVEQIVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSsIYSAS 164
Cdd:PRK05565  81 FGKIDILVNNAGISNFG-LVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEV-LYSAS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRkSIPLQRLGTAEDCAPAYLFLAAPSlSGYITG 244
Cdd:PRK05565 159 KGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAE-EIPLGRLGKPEEIAKVVLFLASDD-ASYITG 236

                 ....*...
gi 517341756 245 QVIEINGG 252
Cdd:PRK05565 237 QIITVDGG 244
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
7-252 1.79e-62

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 196.18  E-value: 1.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGR--KPGRDLPDFLltAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASseAGAEALVAEI--GALGGKALAVQGDVSDAESVERAVDEAKAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSAS 164
Cdd:PRK05557  81 FGGVDILVNNAGITRDN-LLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMG-NPGQANYAAS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHErYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGYITG 244
Cdd:PRK05557 159 KAGVIGFTKSLARELASRGITVNAVAPGFIETDMTD-ALPEDVKEAILAQIPLGRLGQPEEIASAVAFLASD-EAAYITG 236

                 ....*...
gi 517341756 245 QVIEINGG 252
Cdd:PRK05557 237 QTLHVNGG 244
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
6-254 3.53e-62

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 195.38  E-value: 3.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAGRGIGLEVARQFLDCGAKVIV-HTGRKPGRDLPDFLltAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIyDSNEEAAEALAAEL--RAAGGEARVLVFDVSDEAAVRALIEAAVEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSAS 164
Cdd:PRK05653  80 FGALDILVNNAG-ITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGN-PGQTNYSAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFhERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGYITG 244
Cdd:PRK05653 158 KAGVIGFTKALALELASRGITVNAVAPGFIDTDM-TEGLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASD-AASYITG 235
                        250
                 ....*....|
gi 517341756 245 QVIEINGGQL 254
Cdd:PRK05653 236 QVIPVNGGMY 245
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-252 1.55e-60

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 191.24  E-value: 1.55e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpGRDLPDFL--LTAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK12825   4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRS--DEEAAEELveAVEALGRRAQAVQADVTDKAALEAAVAAAVER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALtGGSPGSSIYSAS 164
Cdd:PRK12825  82 FGRIDILVNNAG-IFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGL-PGWPGRSNYAAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERySSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITG 244
Cdd:PRK12825 160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEA-TIEEAREAKDAETPLGRSGTPEDIARAVAFLCSDA-SDYITG 237

                 ....*...
gi 517341756 245 QVIEINGG 252
Cdd:PRK12825 238 QVIEVTGG 245
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
10-252 8.46e-60

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: 189.30  E-value: 8.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVH-TGRKPGRDLPDFLLTAESERRALLlhADFSAVGGAAQFAEDALAFFDRV 88
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTdRSEEAAAETVEEIKALGGNAAALE--ADVSDREAVEALVEKVEAEFGPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAG----TMLGRfpaatLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSAS 164
Cdd:cd05333   79 DILVNNAGitrdNLLMR-----MSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIG-NPGQANYAAS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYsSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGYITG 244
Cdd:cd05333  153 KAGVIGFTKSLAKELASRGITVNAVAPGFIDTDMTDAL-PEKVKEKILKQIPLGRLGTPEEVANAVAFLASD-DASYITG 230

                 ....*...
gi 517341756 245 QVIEINGG 252
Cdd:cd05333  231 QVLHVNGG 238
FabG-like PRK07231
SDR family oxidoreductase;
5-255 1.81e-59

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 188.50  E-value: 1.81e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   5 RLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPdfllTAE---SERRALLLHADFSAVGGAAQFAEDA 81
Cdd:PRK07231   1 MRLEGKVAIVTGASSGIGEGIARRFAAEGARVVV-TDRNEEAAER----VAAeilAGGRAIAVAADVSDEADVEAAVAAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIY 161
Cdd:PRK07231  76 LERFGSVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRP-RPGLGWY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY---SSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsL 238
Cdd:PRK07231 155 NASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFmgePTPENRAKFLATIPLGRLGTPEDIANAALFLASD-E 233
                        250
                 ....*....|....*..
gi 517341756 239 SGYITGQVIEINGGQLI 255
Cdd:PRK07231 234 ASWITGVTLVVDGGRCV 250
PRK12826 PRK12826
SDR family oxidoreductase;
5-254 5.27e-59

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 187.43  E-value: 5.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   5 RLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpGRDLPDFLLTAESE-RRALLLHADFSAVGGAAQFAEDALA 83
Cdd:PRK12826   2 RDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDIC--GDDAAATAELVEAAgGKARARQVDVRDRAALKAAVAAGVE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYSA 163
Cdd:PRK12826  80 DFGRLDILVANAG-IFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYPGLAHYAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYIT 243
Cdd:PRK12826 159 SKAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDE-ARYIT 237
                        250
                 ....*....|.
gi 517341756 244 GQVIEINGGQL 254
Cdd:PRK12826 238 GQTLPVDGGAT 248
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
8-235 2.76e-54

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: 174.99  E-value: 2.76e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdLPDflLTAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVL-AARRAER-LEA--LAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKAF 167
Cdd:COG4221   80 LDVLVNNAGVALLG-PLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRP-YPGGAVYAATKAA 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517341756 168 VATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLgTAEDCAPAYLFLAA 235
Cdd:COG4221  158 VRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPL-TPEDVAEAVLFALT 224
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-201 5.87e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 174.67  E-value: 5.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR--DLPDFLltAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVL-VARDAERleALAAEL--RAAGARVEVVALDVTDPDAVAALAEAVLAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSAS 164
Cdd:COG0300   80 FGPIDVLVNNAGVGGGG-PFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGL-PGMAAYAAS 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:COG0300  158 KAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTAR 194
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
19-252 1.04e-53

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: 173.39  E-value: 1.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   19 RGIGLEVARQFLDCGAKVIVhTGRkpGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVLVNNAGTM 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVL-TDL--NEALAKRVEELAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   99 LGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNTVSISALTGGsPGSSIYSASKAFVATYSKALAR 177
Cdd:pfam13561  83 PKLKgPFLDTSREDFDRALDVNLYSLFLLAKAALPLMK--EGGSIVNLSSIGAERVV-PNYNAYGAAKAALEALTRYLAV 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517341756  178 ELAPDGIRVNCVSPGTIETEFHERYSSREK-LEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGYITGQVIEINGG 252
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLAASGIPGFDElLAAAEARAPLGRLGTPEEVANAAAFLASD-LASYITGQVLYVDGG 234
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
10-197 1.24e-49

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 161.63  E-value: 1.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdlpdfLLTAESE-----RRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVL-VDRSEEK-----LEAVAKElgalgGKALFIQGDVTDRAQVKALVEQAVER 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   85 FDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSAS 164
Cdd:pfam00106  75 LGRLDILVNNAG-ITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPY-PGGSAYSAS 152
                         170       180       190
                  ....*....|....*....|....*....|...
gi 517341756  165 KAFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:pfam00106 153 KAAVIGFTRSLALELAPHGIRVNAVAPGGVDTD 185
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
8-253 1.92e-49

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: 162.83  E-value: 1.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVH--TGRKPGRDLPDFLLTAESerRALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05362    2 AGKVALVTGASRGIGRAIAKRLARDGASVVVNyaSSKAAAEEVVAEIEAAGG--KAIAVQADVSDPSQVARLFDAAEKAF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNqtsvvalTRALLPALKAA-----EGAAIVNTVSiSALTGGSPGSSI 160
Cdd:cd05362   80 GGVDILVNNAGVMLKK-PIAETSEEEFDRMFTVN-------TKGAFFVLQEAakrlrDGGRIINISS-SLTAAYTPNYGA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSG 240
Cdd:cd05362  151 YAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKMSPLGRLGEPEDIAPVVAFLASPD-GR 229
                        250
                 ....*....|...
gi 517341756 241 YITGQVIEINGGQ 253
Cdd:cd05362  230 WVNGQVIRANGGY 242
PRK12939 PRK12939
short chain dehydrogenase; Provisional
8-252 1.96e-48

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 160.52  E-value: 1.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRK-PGRDLPDFLLTAEseRRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK12939   6 AGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAaEARELAAALEAAG--GRAHAIAADLADPASVQRFFDAAAAALG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSASKA 166
Cdd:PRK12939  84 GLDGLVNNAGITNSK-SATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGA-PKLGAYVASKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGYITGQV 246
Cdd:PRK12939 162 AVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADERHAYYLKGRALERLQVPDDVAGAVLFLLSD-AARFVTGQL 240

                 ....*.
gi 517341756 247 IEINGG 252
Cdd:PRK12939 241 LPVNGG 246
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
8-255 2.67e-48

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: 159.86  E-value: 2.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIV-----HTGRKPGRDLPDflltaeserRALLLHADFSAVGGAAQFAEDAL 82
Cdd:cd05345    4 EGKVAIVTGAGSGFGEGIARRFAQEGARVVIadinaDGAERVAADIGE---------AAIAIQADVTKRADVEAMVEAAL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYS 162
Cdd:cd05345   75 SKFGRLDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLR-PRPGLTWYN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY---SSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLS 239
Cdd:cd05345  154 ASKGWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFmgeDTPENRAKFRATIPLGRLSTPDDIANAALYLASDEAS 233
                        250
                 ....*....|....*.
gi 517341756 240 gYITGQVIEINGGQLI 255
Cdd:cd05345  234 -FITGVALEVDGGRCI 248
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
9-252 3.78e-48

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: 159.75  E-value: 3.78e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpGRDLPDFLLTAE----SERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAIC-----ARNRENLERAASelraGGAGVLAVVADLTDPEDIDRLVEKAGDA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSAS 164
Cdd:cd05344   76 FGRVDILVNNAGGPPPG-PFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEP-EPNLVLSNVA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETE----FHERYSSREK------LEQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:cd05344  154 RAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTErvrrLLEARAEKEGisveeaEKEVASQIPLGRVGKPEELAALIAFLA 233
                        250
                 ....*....|....*...
gi 517341756 235 APsLSGYITGQVIEINGG 252
Cdd:cd05344  234 SE-KASYITGQAILVDGG 250
PRK12829 PRK12829
short chain dehydrogenase; Provisional
10-252 1.97e-47

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 158.30  E-value: 1.97e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGrDLpDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:PRK12829  12 LRVLVTGGASGIGRAIAEAFAEAGARVHV-CDVSEA-AL-AATAARLPGAKVTATVADVADPAQVERVFDTAVERFGGLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAE-GAAIVNTVSISALTGgSPGSSIYSASKAFV 168
Cdd:PRK12829  89 VLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhGGVIIALSSVAGRLG-YPGRTPYAASKWAV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 169 ATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTR----------KSIPLQRLGTAEDCAPAYLFLAAPsL 238
Cdd:PRK12829 168 VGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIgldemeqeylEKISLGRMVEPEDIAATALFLASP-A 246
                        250
                 ....*....|....
gi 517341756 239 SGYITGQVIEINGG 252
Cdd:PRK12829 247 ARYITGQAISVDGN 260
PRK06523 PRK06523
short chain dehydrogenase; Provisional
7-254 6.21e-47

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 156.60  E-value: 6.21e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPDflltaeserRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK06523   7 LAGKRALVTGGTKGIGAATVARLLEAGARVVT-TARSRPDDLPE---------GVEFVAADLTTAEGCAAVARAVLERLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAG---TMLGRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSI-YS 162
Cdd:PRK06523  77 GVDILVHVLGgssAPAGGF--AALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLP-LPESTTaYA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSR------EKLEQTRKS-------IPLQRLGTAEDCAPA 229
Cdd:PRK06523 154 AAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERlaeaagTDYEGAKQIimdslggIPLGRPAEPEEVAEL 233
                        250       260
                 ....*....|....*....|....*
gi 517341756 230 YLFLAAPSlSGYITGQVIEINGGQL 254
Cdd:PRK06523 234 IAFLASDR-AASITGTEYVIDGGTV 257
PRK09242 PRK09242
SDR family oxidoreductase;
9-255 6.82e-47

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 156.45  E-value: 6.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPG--RDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK09242   9 GQTALITGASKGIGLAIAREFLGLGADVLI-VARDADalAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDHWD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLgRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGsSIYSASKA 166
Cdd:PRK09242  88 GLHILVNNAGGNI-RKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSG-APYGMTKA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEFHERY-SSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQ 245
Cdd:PRK09242 166 ALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPlSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPA-ASYITGQ 244
                        250
                 ....*....|
gi 517341756 246 VIEINGGQLI 255
Cdd:PRK09242 245 CIAVDGGFLR 254
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
7-253 3.35e-46

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: 154.67  E-value: 3.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR-DLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAI-AGRKPEVlEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGtmlGRFPAAT--LTDAEYEAVVRLNQTSVVALTRALLPALKAAE-GAAIVNTVSISALTGgSPGSSIYS 162
Cdd:cd05369   80 GKIDILINNAA---GNFLAPAesLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKhGGSILNISATYAYTG-SPFQVHSA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFH-ERYSSREKLEQ-TRKSIPLQRLGTAEDCAPAYLFLAAPSLSg 240
Cdd:cd05369  156 AAKAGVDALTRSLAVEWGPYGIRVNAIAPGPIPTTEGmERLAPSGKSEKkMIERVPLGRLGTPEEIANLALFLLSDAAS- 234
                        250
                 ....*....|...
gi 517341756 241 YITGQVIEINGGQ 253
Cdd:cd05369  235 YINGTTLVVDGGQ 247
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
7-252 1.41e-45

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: 152.95  E-value: 1.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdLPD----FLLTAESERRALLLHADFSAVGGAAQFAEDAL 82
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLAL-TGRDAER-LEEtrqsCLQAGVSEKKILLVVADLTEEEGQDRIISTTL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVNNAGTMLgrfpAATLTD---AEYEAVVRLNQTSVVALTRALLPALKAAEGAaIVNTVSISALTGgSPGSS 159
Cdd:cd05364   79 AKFGRLDILVNNAGILA----KGGGEDqdiEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGE-IVNVSSVAGGRS-FPGVL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY-----SSREKLEQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:cd05364  153 YYCISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMgmpeeQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLA 232
                        250
                 ....*....|....*...
gi 517341756 235 ApSLSGYITGQVIEINGG 252
Cdd:cd05364  233 S-DASSFITGQLLPVDGG 249
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
9-253 2.00e-45

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 152.61  E-value: 2.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPD-FLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLNDGYRVIA-TYFSGNDCAKDwFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAG----TMLGRFPAATLTDaeyeaVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSiYSA 163
Cdd:PRK12824  81 VDILVNNAGitrdSVFKRMSHQEWND-----VINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTN-YSA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSrEKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYIT 243
Cdd:PRK12824 155 AKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVEQMGP-EVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEA-AGFIT 232
                        250
                 ....*....|
gi 517341756 244 GQVIEINGGQ 253
Cdd:PRK12824 233 GETISINGGL 242
PRK06500 PRK06500
SDR family oxidoreductase;
7-252 3.57e-45

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 152.03  E-value: 3.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgrdlpDFLLTAESE--RRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAI-TGRDP-----ASLEAARAElgESALVIRADAGDVAAQKALAQALAEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALkaAEGAAIVNTVSISALTGgSPGSSIYSAS 164
Cdd:PRK06500  78 FGRLDAVFINAGVAKFA-PLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL--ANPASIVLNGSINAHIG-MPNSSVYAAS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYS-SREKLEQTRKSI----PLQRLGTAEDCAPAYLFLAAPSlS 239
Cdd:PRK06500 154 KAALLSLAKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGlPEATLDAVAAQIqalvPLGRFGTPEEIAKAVLYLASDE-S 232
                        250
                 ....*....|...
gi 517341756 240 GYITGQVIEINGG 252
Cdd:PRK06500 233 AFIVGSEIIVDGG 245
PRK06701 PRK06701
short chain dehydrogenase; Provisional
8-252 5.05e-45

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 152.88  E-value: 5.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKV-IVHTGRKpgRDLPDFLLTAESE-RRALLLHADFSAvggaAQFAEDA---- 81
Cdd:PRK06701  45 KGKVALITGGDSGIGRAVAVLFAKEGADIaIVYLDEH--EDANETKQRVEKEgVKCLLIPGDVSD----EAFCKDAveet 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNTVSISALTGgSPGSSIY 161
Cdd:PRK06701 119 VRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLK--QGSAIINTGSITGYEG-NETLIDY 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGY 241
Cdd:PRK06701 196 SATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEKVSQFGSNTPMQRPGQPEELAPAYVFLASPD-SSY 274
                        250
                 ....*....|.
gi 517341756 242 ITGQVIEINGG 252
Cdd:PRK06701 275 ITGQMLHVNGG 285
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
10-254 3.14e-44

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: 149.43  E-value: 3.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESeRRALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:cd05347    6 KVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEG-VEATAFTCDVSDEEAIKAAVEAIEEDFGKID 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMLgRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSASKAFVA 169
Cdd:cd05347   85 ILVNNAGIIR-RHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGG-PPVPAYAASKGGVA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 170 TYSKALARELAPDGIRVNCVSPGTIETEFHER-YSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQVIE 248
Cdd:cd05347  163 GLTKALATEWARHGIQVNAIAPGYFATEMTEAvVADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDA-SDYVNGQIIF 241

                 ....*.
gi 517341756 249 INGGQL 254
Cdd:cd05347  242 VDGGWL 247
PRK07062 PRK07062
SDR family oxidoreductase;
1-252 1.46e-43

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 148.27  E-value: 1.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   1 MFHPRLfENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR--DLPDFLLTAESERRALLLHADFSAVGGAAQFA 78
Cdd:PRK07062   1 MMQIQL-EGRVAVVTGGSSGIGLATVELLLEAGASVAI-CGRDEERlaSAEARLREKFPGARLLAARCDVLDEADVAAFA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  79 EDALAFFDRVDVLVNNAGTmlGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPG 157
Cdd:PRK07062  79 AAVEARFGGVDMLVNNAGQ--GRVsTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQP-EPH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 158 SSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET-EFHERYSSREKLEQ----------TRKSIPLQRLGTAEDC 226
Cdd:PRK07062 156 MVATSAARAGLLNLVKSLATELAPKGVRVNSILLGLVESgQWRRRYEARADPGQsweawtaalaRKKGIPLGRLGRPDEA 235
                        250       260
                 ....*....|....*....|....*.
gi 517341756 227 APAYLFLAAPsLSGYITGQVIEINGG 252
Cdd:PRK07062 236 ARALFFLASP-LSSYTTGSHIDVSGG 260
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
8-255 3.91e-43

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: 147.44  E-value: 3.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESE-RRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:cd05355   25 KGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEEDDAEETKKLIEEEgRKCLLIPGDLGDESFCRDLVKEVVKEFG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNTVSISALTGgSPGSSIYSASKA 166
Cdd:cd05355  105 KLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLK--KGSSIINTTSVTAYKG-SPHLLDYAATKG 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQV 246
Cdd:cd05355  182 AIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQD-SSYVTGQV 260

                 ....*....
gi 517341756 247 IEINGGQLI 255
Cdd:cd05355  261 LHVNGGEII 269
PRK07856 PRK07856
SDR family oxidoreductase;
7-252 1.64e-42

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 145.08  E-value: 1.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgrdlPDFLLTAESERRAlllhADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVV-CGRRA----PETVDGRPAEFHA----ADVRDPDQVAALVDAIVERHG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTmlGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKA-AEGAAIVNTVSISAlTGGSPGSSIYSAS 164
Cdd:PRK07856  75 RLDVLVNNAGG--SPYaLAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSVSG-RRPSPGTAAYGAA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDgIRVNCVSPGTIETEF-HERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGYIT 243
Cdd:PRK07856 152 KAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQsELHYGDAEGIAAVAATVPLGRLATPADIAWACLFLASD-LASYVS 229

                 ....*....
gi 517341756 244 GQVIEINGG 252
Cdd:PRK07856 230 GANLEVHGG 238
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
10-252 3.05e-41

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: 141.85  E-value: 3.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDLPDFLLTAESERR---ALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:cd08942    7 KIVLVTGGSRGIGRMIAQGFLEAGARVII-----SARKAEACADAAEELSAygeCIAIPADLSSEEGIEALVARVAERSD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTM----LGRFPAATltdaeYEAVVRLNQTSVVALTRALLPALKAA----EGAAIVNTVSISALTGGSPGS 158
Cdd:cd08942   82 RLDVLVNNAGATwgapLEAFPESG-----WDKVMDINVKSVFFLTQALLPLLRAAataeNPARVINIGSIAGIVVSGLEN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 159 SIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSS-REKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPS 237
Cdd:cd08942  157 YSYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNdPAALEAEEKSIPLGRWGRPEDMAGLAIMLASRA 236
                        250
                 ....*....|....*
gi 517341756 238 lSGYITGQVIEINGG 252
Cdd:cd08942  237 -GAYLTGAVIPVDGG 250
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
8-252 1.62e-40

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: 139.89  E-value: 1.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVivHTGRKPGRDLPDFL----------------LTAESERRALLlhadfsav 71
Cdd:cd05329    5 EGKTALVTGGTKGIGYAIVEELAGLGAEV--YTCARNQKELDECLtewrekgfkvegsvcdVSSRSERQELM-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  72 ggaaQFAEDAlaFFDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAL 151
Cdd:cd05329   75 ----DTVASH--FGGKLNILVNNAGTNIRK-EAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 152 TGgSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER-YSSREKLEQTRKSIPLQRLGTAEDCAPAY 230
Cdd:cd05329  148 IA-VPSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPvIQQKENLDKVIERTPLKRFGEPEEVAALV 226
                        250       260
                 ....*....|....*....|..
gi 517341756 231 LFLAAPSLSgYITGQVIEINGG 252
Cdd:cd05329  227 AFLCMPAAS-YITGQIIAVDGG 247
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
10-255 2.00e-40

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 139.67  E-value: 2.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLpdflLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:PRK12936   7 RKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEA----LAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAG-TMLGRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKAFV 168
Cdd:PRK12936  83 ILVNNAGiTKDGLF--VRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTG-NPGQANYCASKAGM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 169 ATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKlEQTRKSIPLQRLGTAEDCAPAYLFLAApSLSGYITGQVIE 248
Cdd:PRK12936 160 IGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQK-EAIMGAIPMKRMGTGAEVASAVAYLAS-SEAAYVTGQTIH 237

                 ....*..
gi 517341756 249 INGGQLI 255
Cdd:PRK12936 238 VNGGMAM 244
PRK06138 PRK06138
SDR family oxidoreductase;
10-255 3.68e-40

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 139.13  E-value: 3.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESerRALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGG--RAFARQGDVGSAEAVEALVDFVAARWGRLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSASKAFVA 169
Cdd:PRK06138  84 VLVNNAGFGCGG-TVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGG-RGRAAYVASKGAIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 170 TYSKALARELAPDGIRVNCVSPGTIET----EFHERYSSREKL-EQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITG 244
Cdd:PRK06138 162 SLTRAMALDHATDGIRVNAVAPGTIDTpyfrRIFARHADPEALrEALRARHPMNRFGTAEEVAQAALFLASDE-SSFATG 240
                        250
                 ....*....|.
gi 517341756 245 QVIEINGGQLI 255
Cdd:PRK06138 241 TTLVVDGGWLA 251
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-254 5.84e-40

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 138.76  E-value: 5.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIV--HTGRKPGRDLpdflltaeSERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVlyNSAENEAKEL--------REKGVFTIKCDVGNRDQVKKSKEVVEKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLgRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYSAS 164
Cdd:PRK06463  77 FGRVDVLVNNAGIMY-LMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGTTFYAIT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSRE---KLEQT-RKSIPLQRLGTAEDCAPAYLFLAApSLSG 240
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEeaeKLRELfRNKTVLKTTGKPEDIANIVLFLAS-DDAR 234
                        250
                 ....*....|....
gi 517341756 241 YITGQVIEINGGQL 254
Cdd:PRK06463 235 YITGQVIVADGGRI 248
PRK12827 PRK12827
short chain dehydrogenase; Provisional
10-252 6.82e-40

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 138.31  E-value: 6.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKP-GRDLPDFL--LTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK12827   7 RRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMrGRAEADAVaaGIEAAGGKALGLAFDVRDFAATRAALDAGVEEFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALL-PALKAAEGAAIVNTVSIsALTGGSPGSSIYSASK 165
Cdd:PRK12827  87 RLDILVNNAG-IATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRARRGGRIVNIASV-AGVRGNRGQVNYAASK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTrksIPLQRLGTAEDCAPAYLFLAAPSLSgYITGQ 245
Cdd:PRK12827 165 AGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEHLLNP---VPVQRLGEPDEVAALVAFLVSDAAS-YVTGQ 240

                 ....*..
gi 517341756 246 VIEINGG 252
Cdd:PRK12827 241 VIPVDGG 247
PRK09135 PRK09135
pteridine reductase; Provisional
12-252 1.78e-39

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 137.37  E-value: 1.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTgRKPGRDLPdfLLTAESERR----ALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIHY-HRSAAEAD--ALAAELNALrpgsAAALQADLLDPDALPELVAACVAAFGR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMLgRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGaAIVNTVSISAlTGGSPGSSIYSASKAF 167
Cdd:PRK09135  86 LDALVNNASSFY-PTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQRG-AIVNITDIHA-ERPLKGYPVYCAAKAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 168 VATYSKALARELAPDgIRVNCVSPGTIE-TEFHERYSSREKlEQTRKSIPLQRLGTAEDCAPAYLFLAAPslSGYITGQV 246
Cdd:PRK09135 163 LEMLTRSLALELAPE-VRVNAVAPGAILwPEDGNSFDEEAR-QAILARTPLKRIGTPEDIAEAVRFLLAD--ASFITGQI 238

                 ....*.
gi 517341756 247 IEINGG 252
Cdd:PRK09135 239 LAVDGG 244
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
7-252 1.78e-39

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 137.32  E-value: 1.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpGRDLpDFLltAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK08220   6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVI-------GFDQ-AFL--TQEDYPFATFVLDVSDAAAVAQVCQRLLAETG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTM-LGrfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTggsP--GSSIYSA 163
Cdd:PRK08220  76 PLDVLVNAAGILrMG--ATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHV---PriGMAAYGA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETE-----FHERYSSRE----KLEQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:PRK08220 151 SKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDmqrtlWVDEDGEQQviagFPEQFKLGIPLGKIARPQEIANAVLFLA 230
                        250
                 ....*....|....*...
gi 517341756 235 ApSLSGYITGQVIEINGG 252
Cdd:PRK08220 231 S-DLASHITLQDIVVDGG 247
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
12-252 2.96e-39

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: 136.45  E-value: 2.96e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpGRDLPdFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVI-------ALDLP-FVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLgrfPAAT--LTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAltgGSPGSSI--YSASKAF 167
Cdd:cd05331   73 VNCAGVLR---PGATdpLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAA---HVPRISMaaYGASKAA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 168 VATYSKALARELAPDGIRVNCVSPGTIETE-----FHERYSS----REKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsL 238
Cdd:cd05331  147 LASLSKCLGLELAPYGVRCNVVSPGSTDTAmqrtlWHDEDGAaqviAGVPEQFRLGIPLGKIAQPADIANAVLFLASD-Q 225
                        250
                 ....*....|....
gi 517341756 239 SGYITGQVIEINGG 252
Cdd:cd05331  226 AGHITMHDLVVDGG 239
PRK07774 PRK07774
SDR family oxidoreductase;
7-255 4.20e-39

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 136.41  E-value: 4.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIV-----HTGRKPGRDLpdflltAESERRALLLHADFSAVGGAAQFAEDA 81
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVadinaEGAERVAKQI------VADGGTAIAVQVDVSDPDSAKAMADAT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGTMLGR--FPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSisalTGGSPGSS 159
Cdd:PRK07774  78 VSAFGGIDYLVNNAAIYGGMklDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSS----TAAWLYSN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlS 239
Cdd:PRK07774 154 FYGLAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDE-A 232
                        250
                 ....*....|....*.
gi 517341756 240 GYITGQVIEINGGQLI 255
Cdd:PRK07774 233 SWITGQIFNVDGGQII 248
PRK07814 PRK07814
SDR family oxidoreductase;
13-252 6.22e-39

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 136.06  E-value: 6.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDLPDFLLTAE----SERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK07814  14 VVTGAGRGLGAAIALAFAEAGADVLI-----AARTESQLDEVAEqiraAGRRAHVVAADLAHPEATAGLAGQAVEAFGRL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGtmlGRFPAATL--TDAEYEAVVRLNQTSVVALTRALLP-ALKAAEGAAIVNTVSISALTGGsPGSSIYSASK 165
Cdd:PRK07814  89 DIVVNNVG---GTMPNPLLstSTKDLADAFTFNVATAHALTVAAVPlMLEHSGGGSVINISSTMGRLAG-RGFAAYGTAK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDgIRVNCVSPGTIETEFHERYSSREKLEQT-RKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITG 244
Cdd:PRK07814 165 AALAHYTRLAALDLCPR-IRVNAIAPGSILTSALEVVAANDELRAPmEKATPLRRLGDPEDIAAAAVYLASPA-GSYLTG 242

                 ....*...
gi 517341756 245 QVIEINGG 252
Cdd:PRK07814 243 KTLEVDGG 250
PRK06172 PRK06172
SDR family oxidoreductase;
7-252 2.36e-38

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 134.49  E-value: 2.36e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGR-KPGRDLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDaAGGEETVALIREAGGE--ALFVACDVTRDAEVKALVEQTIAAY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALtGGSPGSSIYSASK 165
Cdd:PRK06172  83 GRLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGL-GAAPKMSIYAASK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY--SSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYIT 243
Cdd:PRK06172 162 HAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAyeADPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDG-ASFTT 240

                 ....*....
gi 517341756 244 GQVIEINGG 252
Cdd:PRK06172 241 GHALMVDGG 249
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
12-252 2.94e-38

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: 134.02  E-value: 2.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAlTGGSPGSSIYSASKAFVATY 171
Cdd:cd05359   81 VSNAAAGAFR-PLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGS-IRALPNYLAVGTAKAALEAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 172 SKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQT-RKSIPLQRLGTAEDCAPAYLFLAAPsLSGYITGQVIEIN 250
Cdd:cd05359  159 VRYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAaAANTPAGRVGTPQDVADAVGFLCSD-AARMITGQTLVVD 237

                 ..
gi 517341756 251 GG 252
Cdd:cd05359  238 GG 239
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
12-252 5.77e-38

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: 133.28  E-value: 5.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIV-----HTGRKpgrdlpdflLTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:cd05341    8 AIVTGGARGLGLAHARLLVAEGAKVVLsdildEEGQA---------AAAELGDAARFFHLDVTDEDGWTAVVDTAREAFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYSASKA 166
Cdd:cd05341   79 RLDVLVNNAGILTGG-TVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLV-GDPALAAYNASKG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAP--DGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITG 244
Cdd:cd05341  157 AVRGLTKSAALECATqgYGIRVNSVHPGYIYTPMTDELLIAQGEMGNYPNTPMGRAGEPDEIAYAVVYLASDE-SSFVTG 235

                 ....*...
gi 517341756 245 QVIEINGG 252
Cdd:cd05341  236 SELVVDGG 243
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
5-252 6.62e-38

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 133.53  E-value: 6.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   5 RLF--ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgrdlpDFLLTAESE-----RRALLLHADFSAVGGAAQF 77
Cdd:PRK08213   6 ELFdlSGKTALVTGGSRGLGLQIAEALGEAGARVVL-SARKA-----EELEEAAAHlealgIDALWIAADVADEADIERL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  78 AEDALAFFDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLP-ALKAAEGAAIVNTVSISALTGGSP 156
Cdd:PRK08213  80 AEETLERFGHVDILVNNAGATWGA-PAEDHPVEAWDKVMNLNVRGLFLLSQAVAKrSMIPRGYGRIINVASVAGLGGNPP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 157 GS--SI-YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHErySSREKLEQTRKS-IPLQRLGTAEDCAPAYLF 232
Cdd:PRK08213 159 EVmdTIaYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTR--GTLERLGEDLLAhTPLGRLGDDEDLKGAALL 236
                        250       260
                 ....*....|....*....|
gi 517341756 233 LAAPSlSGYITGQVIEINGG 252
Cdd:PRK08213 237 LASDA-SKHITGQILAVDGG 255
PRK12937 PRK12937
short chain dehydrogenase; Provisional
9-252 8.47e-38

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 132.94  E-value: 8.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGrkpGRDLPDFLLTAESER---RALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVNYA---GSAAAADELVAEIEAaggRAIAVQADVADAAAVTRLFDAAETAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLgRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNtVSISALTGGSPGSSIYSASK 165
Cdd:PRK12937  82 GRIDVLVNNAGVMP-LGTIADFDLEDFDRTIATNLRGAFVVLREAARHLG--QGGRIIN-LSTSVIALPLPGYGPYAASK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQ 245
Cdd:PRK12937 158 AAVEGLVHVLANELRGRGITVNAVAPGPVATELFFNGKSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPD-GAWVNGQ 236

                 ....*..
gi 517341756 246 VIEINGG 252
Cdd:PRK12937 237 VLRVNGG 243
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-255 8.87e-38

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 132.39  E-value: 8.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpGRDLPDflltaeserrALLLHADFSA-VGGAAQFAEDALAFF 85
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAFLAQGAQVY-------GVDKQD----------KPDLSGNFHFlQLDLSDDLEPLFDWV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSiYSASK 165
Cdd:PRK06550  66 PSVDILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAA-YTASK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIET-----EFHERYSSREKLEQTrksiPLQRLGTAEDCAPAYLFLAAPSLSg 240
Cdd:PRK06550 145 HALAGFTKQLALDYAKDGIQVFGIAPGAVKTpmtaaDFEPGGLADWVARET----PIKRWAEPEEVAELTLFLASGKAD- 219
                        250
                 ....*....|....*
gi 517341756 241 YITGQVIEINGGQLI 255
Cdd:PRK06550 220 YMQGTIVPIDGGWTL 234
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
11-252 1.51e-37

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: 131.92  E-value: 1.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  11 NVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPG-RDLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGaEAVAAAIQQAGGQ--AIGLECNVTSEQDLEAVVKATVSQFGGIT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAG-TMLGRFPAAtLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKAFV 168
Cdd:cd05365   79 ILVNNAGgGGPKPFDMP-MTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENK-NVRIAAYGSSKAAV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 169 ATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQVIE 248
Cdd:cd05365  157 NHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPEIERAMLKHTPLGRLGEPEDIANAALFLCSPA-SAWVSGQVLT 235

                 ....
gi 517341756 249 INGG 252
Cdd:cd05365  236 VSGG 239
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
12-201 1.63e-37

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: 131.97  E-value: 1.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgRDLPDflLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd05374    3 VLITGCSSGIGLALALALAAQGYRVIA-TARNP-DKLES--LGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLgRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALtGGSPGSSIYSASKAFVATY 171
Cdd:cd05374   79 VNNAGYGL-FGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGL-VPTPFLGPYCASKAALEAL 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 517341756 172 SKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:cd05374  157 SESLRLELAPFGIKVTIIEPGPVRTGFADN 186
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
7-254 1.75e-37

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: 132.27  E-value: 1.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILAAGDA--AHVHTADLETYAGAQGVVRAAVERFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgspGSSIYSASKA 166
Cdd:cd08937   80 RVDVLINNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGI---YRIPYSAAKG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEFHER------YSSREK------LEQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:cd08937  157 GVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIprnaapMSEQEKvwyqriVDQTLDSSLMGRYGTIDEQVRAILFLA 236
                        250       260
                 ....*....|....*....|
gi 517341756 235 APSLSgYITGQVIEINGGQL 254
Cdd:cd08937  237 SDEAS-YITGTVLPVGGGDL 255
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
12-252 5.53e-37

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: 130.47  E-value: 5.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPdflLTAESE---RRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:cd05357    3 ALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQR---LKDELNalrNSAVLVQADLSDFAACADLVAAAFRAFGRC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTmlgrFPAATLTDAEYEAVVRLNQTSVVA---LTRALLPALKAAEGAAIVNtVSISALTGGSPGSSIYSASK 165
Cdd:cd05357   80 DVLVNNASA----FYPTPLGQGSEDAWAELFGINLKApylLIQAFARRLAGSRNGSIIN-IIDAMTDRPLTGYFAYCMSK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDgIRVNCVSPGTIetEFHERySSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAApslSGYITGQ 245
Cdd:cd05357  155 AALEGLTRSAALELAPN-IRVNGIAPGLI--LLPED-MDAEYRENALRKVPLKRRPSAEEIADAVIFLLD---SNYITGQ 227

                 ....*..
gi 517341756 246 VIEINGG 252
Cdd:cd05357  228 IIKVDGG 234
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
8-252 6.19e-37

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: 130.58  E-value: 6.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIV--HTGRKPGRDLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05358    2 KGKVALVTGASSGIGKAIAIRLATAGANVVVnyRSKEDAAEEVVEEIKAVGGK--AIAVQADVSKEEDVVALFQSAIKEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTR-ALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSAS 164
Cdd:cd05358   80 GTLDILVNNAG-LQGDASSHEMTLEDWNKVIDVNLTGQFLCAReAIKRFRKSKIKGKIINMSSVHEKIP-WPGHVNYAAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFH-ERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAApSLSGYIT 243
Cdd:cd05358  158 KGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINaEAWDDPEQRADLLSLIPMGRIGEPEEIAAAAAWLAS-DEASYVT 236

                 ....*....
gi 517341756 244 GQVIEINGG 252
Cdd:cd05358  237 GTTLFVDGG 245
PRK06128 PRK06128
SDR family oxidoreductase;
10-255 6.61e-37

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 131.91  E-value: 6.61e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESE-RRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK06128  56 RKALITGADSGIGRATAIAFAREGADIALNYLPEEEQDAAEVVQLIQAEgRKAVALPGDLKDEAFCRQLVERAVKELGGL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAaeGAAIVNTVSISALTGgSPGSSIYSASKAFV 168
Cdd:PRK06128 136 DILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPP--GASIINTGSIQSYQP-SPTLLDYASTKAAI 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 169 ATYSKALARELAPDGIRVNCVSPGTIETEFHERYSS-REKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQVI 247
Cdd:PRK06128 213 VAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQpPEKIPDFGSETPMKRPGQPVEMAPLYVLLASQE-SSYVTGEVF 291

                 ....*...
gi 517341756 248 EINGGQLI 255
Cdd:PRK06128 292 GVTGGLLL 299
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
11-235 7.93e-37

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: 130.48  E-value: 7.93e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  11 NVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR--DLPDfLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:cd05346    2 TVLITGASSGIGEATARRFAKAGAKLIL-TGRRAERlqELAD-ELGAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAlTGGSPGSSIYSASKAFV 168
Cdd:cd05346   80 DILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAG-RYPYAGGNVYCATKAAV 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 169 ATYSKALARELAPDGIRVNCVSPGTIETEFHE-RY-SSREKLEQTRKSI-PLqrlgTAEDCAPAYLFLAA 235
Cdd:cd05346  159 RQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLvRFhGDKEKADKVYEGVePL----TPEDIAETILWVAS 224
PRK07890 PRK07890
short chain dehydrogenase; Provisional
6-254 3.72e-36

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 128.92  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpGRDLPDFLLTAESE-----RRALLLHADFSAVGGAAQFAED 80
Cdd:PRK07890   2 LLKGKVVVVSGVGPGLGRTLAVRAARAGADVVL------AARTAERLDEVAAEiddlgRRALAVPTDITDEDQCANLVAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAaIVNTVSiSALTGGSPGSSI 160
Cdd:PRK07890  76 ALERFGRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGS-IVMINS-MVLRHSQPKYGA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPG-----TIETEFHERYSSR-----EKLEQTRKSIPLQRLGTAEDCAPAY 230
Cdd:PRK07890 154 YKMAKGALLAASQSLATELGPQGIRVNSVAPGyiwgdPLKGYFRHQAGKYgvtveQIYAETAANSDLKRLPTDDEVASAV 233
                        250       260
                 ....*....|....*....|....
gi 517341756 231 LFLAAPSLSGyITGQVIEINGGQL 254
Cdd:PRK07890 234 LFLASDLARA-ITGQTLDVNCGEY 256
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
13-252 7.70e-36

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 127.81  E-value: 7.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVH--TGRKPGRDLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAFFDRVDV 90
Cdd:PRK12935  10 IVTGGAKGIGKAITVALAQEGAKVVINynSSKEAAENLVNELGKEGHD--VYAVQADVSKVEDANRLVEEAVNHFGKVDI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  91 LVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSpGSSIYSASKAFVAT 170
Cdd:PRK12935  88 LVNNAGITRDR-TFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGF-GQTNYSAAKAGMLG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 171 YSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKlEQTRKSIPLQRLGTAEDCAPAYLFLAAPslSGYITGQVIEIN 250
Cdd:PRK12935 166 FTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEVR-QKIVAKIPKKRFGQADEIAKGVVYLCRD--GAYITGQQLNIN 242

                 ..
gi 517341756 251 GG 252
Cdd:PRK12935 243 GG 244
PRK07577 PRK07577
SDR family oxidoreductase;
8-252 9.05e-36

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 127.15  E-value: 9.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPDFLLT---AESERRALLLhadfsavggaAQFAEDAlaf 84
Cdd:PRK07577   2 SSRTVLVTGATKGIGLALSLRLANLGHQVIG-IARSAIDDFPGELFAcdlADIEQTAATL----------AQINEIH--- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 fdRVDVLVNNAGTM----LGRFPAATLTDaeyeaVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALtgGSPGSSI 160
Cdd:PRK07577  68 --PVDAIVNNVGIAlpqpLGKIDLAALQD-----VYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIF--GALDRTS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETE-FHERY---SSREKleQTRKSIPLQRLGTAEDCAPAYLFLAAP 236
Cdd:PRK07577 139 YSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETElFRQTRpvgSEEEK--RVLASIPMRRLGTPEEVAAAIAFLLSD 216
                        250
                 ....*....|....*.
gi 517341756 237 SlSGYITGQVIEINGG 252
Cdd:PRK07577 217 D-AGFITGQVLGVDGG 231
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
7-254 9.32e-36

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 127.75  E-value: 9.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKV-------IVHtgrkpgrDLPDFLLTAESErrALLLHADFSAVGGAAQFAE 79
Cdd:PRK12823   6 FAGKVVVVTGAAQGIGRGVALRAAAEGARVvlvdrseLVH-------EVAAELRAAGGE--ALALTADLETYAGAQAAMA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  80 DALAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISalTGG---SP 156
Cdd:PRK12823  77 AAVEAFGRIDVLINNVGGTIWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIA--TRGinrVP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 157 gssiYSASKAFVATYSKALARELAPDGIRVNCVSPGTIE-------------TEfHERYSSREKLEQTRKSIPLQRLGTA 223
Cdd:PRK12823 155 ----YSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEapprrvprnaapqSE-QEKAWYQQIVDQTLDSSLMKRYGTI 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 517341756 224 EDCAPAYLFLAAPSLSgYITGQVIEINGGQL 254
Cdd:PRK12823 230 DEQVAAILFLASDEAS-YITGTVLPVGGGDL 259
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
12-252 1.04e-35

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: 127.20  E-value: 1.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpGRDLPDFLLtAESER----RALLLHA-DFSAVggaaqfaEDALAFFD 86
Cdd:cd05368    5 ALITAAAQGIGRAIALAFAREGANVI-------ATDINEEKL-KELERgpgiTTRVLDVtDKEQV-------AALAKEEG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTM-LGRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYSASK 165
Cdd:cd05368   70 RIDVLFNCAGFVhHGSI--LDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFVYSTTK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIET-EFHERYSSREKLEQTRKS----IPLQRLGTAEDCAPAYLFLAAPSlSG 240
Cdd:cd05368  148 AAVIGLTKSVAADFAQQGIRCNAICPGTVDTpSLEERIQAQPDPEEALKAfaarQPLGRLATPEEVAALAVYLASDE-SA 226
                        250
                 ....*....|..
gi 517341756 241 YITGQVIEINGG 252
Cdd:cd05368  227 YVTGTAVVIDGG 238
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
10-198 1.30e-35

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: 126.58  E-value: 1.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLpdfllTAESERRALLLHADF-----SAVGGAAQFAEDALAF 84
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQ-----AAVEKLRAEGLSVRFhqldvTDDASIEAAADFVEEK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtvsISALTGgsPGSSIYSAS 164
Cdd:cd05324   76 YGGLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVN---VSSGLG--SLTSAYGVS 150
                        170       180       190
                 ....*....|....*....|....*....|....
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:cd05324  151 KAALNALTRILAKELKETGIKVNACCPGWVKTDM 184
PRK12828 PRK12828
short chain dehydrogenase; Provisional
8-254 1.94e-35

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 126.45  E-value: 1.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRkpGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK12828   6 QGKVVAITGGFGGLGRATAAWLAARGARVAL-IGR--GAAPLSQTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTmlgrFPAATL---TDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSAS 164
Cdd:PRK12828  83 LDALVNIAGA----FVWGTIadgDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAG-PGMGAYAAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETefheryssreklEQTRKSIPLQRLG---TAEDCAPAYLFLAAPSlSGY 241
Cdd:PRK12828 158 KAGVARLTEALAAELLDRGITVNAVLPSIIDT------------PPNRADMPDADFSrwvTPEQIAAVIAFLLSDE-AQA 224
                        250
                 ....*....|...
gi 517341756 242 ITGQVIEINGGQL 254
Cdd:PRK12828 225 ITGASIPVDGGVA 237
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
7-255 2.66e-35

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: 126.29  E-value: 2.66e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFS---AV-GGAAQFAEDal 82
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSsqeSVeKTFKQIQKD-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 afFDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPG-SSIY 161
Cdd:cd05352   84 --FGKIDILIANAG-ITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNRPQpQAAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFhERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGY 241
Cdd:cd05352  161 NASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL-TDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDA-SSY 238
                        250
                 ....*....|....
gi 517341756 242 ITGQVIEINGGQLI 255
Cdd:cd05352  239 TTGSDLIIDGGYTC 252
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
12-252 8.74e-35

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: 124.88  E-value: 8.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPdflLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd05349    3 VLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEA---VAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAgtmLGRFP--------AATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtVSISALTGGSPGSSIYSA 163
Cdd:cd05349   80 VNNA---LIDFPfdpdqrktFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVIN-IGTNLFQNPVVPYHDYTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYIT 243
Cdd:cd05349  156 AKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPW-ARAVT 234

                 ....*....
gi 517341756 244 GQVIEINGG 252
Cdd:cd05349  235 GQNLVVDGG 243
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
7-227 1.12e-34

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


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 125.01  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR--DLPDfLLTAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVL-SARREERleEVKS-ECLELGAPSPHVVPLDMSDLEDAEQVVEEALKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGT-MLGRFPAATLTDaeYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtvsISALTG--GSPGSSIY 161
Cdd:cd05332   79 FGGLDILINNAGIsMRSLFHDTSIDV--DRKIMEVNYFGPVALTKAALPHLIERSQGSIVV---VSSIAGkiGVPFRTAY 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERySSREKLEQTRKSIPLQRLG-TAEDCA 227
Cdd:cd05332  154 AASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMN-ALSGDGSMSAKMDDTTANGmSPEECA 219
PRK06841 PRK06841
short chain dehydrogenase; Provisional
7-256 1.67e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 124.39  E-value: 1.67e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAeserRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGG----NAKGLVCDVSDSQSVEAAVAAVISAFG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGT-MLGrfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSiSALTGGSPGSSIYSASK 165
Cdd:PRK06841  89 RIDILVNSAGVaLLA--PAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLAS-QAGVVALERHVAYCASK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAApSLSGYITGQ 245
Cdd:PRK06841 166 AGVVGMTKVLALEWGPYGITVNAISPTVVLTELGKKAWAGEKGERAKKLIPAGRFAYPEEIAAAALFLAS-DAAAMITGE 244
                        250
                 ....*....|.
gi 517341756 246 VIEINGGQLIC 256
Cdd:PRK06841 245 NLVIDGGYTIQ 255
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
12-245 4.49e-34

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: 123.49  E-value: 4.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpGRDLPDFLLTAESERRAL------LLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05327    4 VVITGANSGIGKETARELAKRGAHVIIA-----CRNEEKGEEAAAEIKKETgnakveVIQLDLSSLASVRQFAEEFLARF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLgrfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSP--------- 156
Cdd:cd05327   79 PRLDILINNAGIMA---PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDfndldlenn 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 157 ----GSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSrekLEQTRKSIPLQRLGTAEDCAPAYLF 232
Cdd:cd05327  156 keysPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGS---FFLLYKLLRPFLKKSPEQGAQTALY 232
                        250
                 ....*....|....
gi 517341756 233 LAA-PSLSGyITGQ 245
Cdd:cd05327  233 AATsPELEG-VSGK 245
PRK06484 PRK06484
short chain dehydrogenase; Validated
1-252 7.65e-34

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 127.66  E-value: 7.65e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   1 MFHPRLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESerraLLLHADFSAVGGAAQFAED 80
Cdd:PRK06484 261 APSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEH----LSVQADITDEAAVESAFAQ 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALkaAEGAAIVNTVSISALtGGSPGSSI 160
Cdd:PRK06484 337 IQARWGRLDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASL-LALPPRNA 413
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY--SSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSL 238
Cdd:PRK06484 414 YCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPAVLALkaSGRADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAA 493
                        250
                 ....*....|....
gi 517341756 239 SgYITGQVIEINGG 252
Cdd:PRK06484 494 S-YVNGATLTVDGG 506
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
8-255 7.75e-34

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 122.92  E-value: 7.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGrkpGRDLPDFLLTAESE-RRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK06935  14 DGKVAIVTGGNTGLGQGYAVALAKAGADIIITTH---GTNWDETRRLIEKEgRKVTFVQVDLTKPESAEKVVKEALEEFG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTmLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGS--PGssiYSAS 164
Cdd:PRK06935  91 KIDILVNNAGT-IRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLSFQGGKfvPA---YTAS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKL-EQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYIT 243
Cdd:PRK06935 167 KHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNRnDEILKRIPAGRWGEPDDLMGAAVFLASRA-SDYVN 245
                        250
                 ....*....|..
gi 517341756 244 GQVIEINGGQLI 255
Cdd:PRK06935 246 GHILAVDGGWLV 257
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
7-252 8.31e-34

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


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 122.95  E-value: 8.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERrALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGR-AIALAADVLDRASLERAREEIVAQFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGtmlGRFPAATLTDAEY----------------EAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISA 150
Cdd:cd08935   82 TVDILINGAG---GNHPDATTDPEHYepeteqnffdldeegwEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSMNA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 151 LTggsPGSSI--YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER--------YSSREK--LEQTrksiPLQ 218
Cdd:cd08935  159 FS---PLTKVpaYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKllinpdgsYTDRSNkiLGRT----PMG 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 517341756 219 RLGTAEDCAPAYLFLAAPSLSGYITGQVIEINGG 252
Cdd:cd08935  232 RFGKPEELLGALLFLASEKASSFVTGVVIPVDGG 265
PRK06124 PRK06124
SDR family oxidoreductase;
1-255 1.13e-33

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 122.13  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   1 MFHPRLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpGRDLPDfLLTAESERRALLLHAD---FSAVGGAAQF 77
Cdd:PRK06124   3 ILQRFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVN-----GRNAAT-LEAAVAALRAAGGAAEalaFDIADEEAVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  78 A--EDALAFFDRVDVLVNNAGTMlGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGS 155
Cdd:PRK06124  77 AafARIDAEHGRLDILVNNVGAR-DRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQV-AR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKL-EQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:PRK06124 155 AGDAVYPAAKQGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVgPWLAQRTPLGRWGRPEEIAGAAVFLA 234
                        250       260
                 ....*....|....*....|.
gi 517341756 235 APSLSgYITGQVIEINGGQLI 255
Cdd:PRK06124 235 SPAAS-YVNGHVLAVDGGYSV 254
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-255 1.44e-33

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 121.75  E-value: 1.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:PRK06077   9 VVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVADIL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGtmLGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNTVSISALTgGSPGSSIYSASKAFVAT 170
Cdd:PRK06077  89 VNNAG--LGLFsPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMR--EGGAIVNIASVAGIR-PAYGLSIYGAMKAAVIN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 171 YSKALARELAPDgIRVNCVSPGTIETEFHE---RYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAApslSGYITGQVI 247
Cdd:PRK06077 164 LTKYLALELAPK-IRVNAIAPGFVKTKLGEslfKVLGMSEKEFAEKFTLMGKILDPEEVAEFVAAILK---IESITGQVF 239

                 ....*...
gi 517341756 248 EINGGQLI 255
Cdd:PRK06077 240 VLDSGESL 247
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-252 1.63e-33

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 121.61  E-value: 1.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpgrdLPDflLTAESERRALllhADFSAVGGAAQF---------- 77
Cdd:PRK08217   4 KDKVIVITGGAQGLGRAMAEYLAQKGAKLA----------LID--LNQEKLEEAV---AECGALGTEVRGyaanvtdeed 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  78 ----AEDALAFFDRVDVLVNNAGT----MLGRFPAATLTD----AEYEAVVRLNQTSVVALTR-ALLPALKAAEGAAIVN 144
Cdd:PRK08217  69 veatFAQIAEDFGQLNGLINNAGIlrdgLLVKAKDGKVTSkmslEQFQSVIDVNLTGVFLCGReAAAKMIESGSKGVIIN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 145 TVSISalTGGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHE--RYSSREKLEqtrKSIPLQRLGT 222
Cdd:PRK08217 149 ISSIA--RAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAamKPEALERLE---KMIPVGRLGE 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 517341756 223 AEDCAPAYLFLAApslSGYITGQVIEINGG 252
Cdd:PRK08217 224 PEEIAHTVRFIIE---NDYVTGRVLEIDGG 250
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
7-252 5.20e-33

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 121.16  E-value: 5.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRK--PGRDLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAI-LDRNqeKAEAVVAEIKAAGGE--ALAVKADVLDKESLEQARQQILED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGtmlGRFPAATLTDAEY-----------------EAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVS 147
Cdd:PRK08277  85 FGPCDILINGAG---GNHPKATTDNEFHelieptktffdldeegfEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 148 ISALTggsPGSSI--YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER--------YSSREK--LEQTrksi 215
Cdd:PRK08277 162 MNAFT---PLTKVpaYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRAllfnedgsLTERANkiLAHT---- 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 517341756 216 PLQRLGTAEDCAPAYLFLAAPSLSGYITGQVIEINGG 252
Cdd:PRK08277 235 PMGRFGKPEELLGTLLWLADEKASSFVTGVVLPVDGG 271
PRK06198 PRK06198
short chain dehydrogenase; Provisional
4-247 6.87e-33

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 120.50  E-value: 6.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   4 PRLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGR--KPGRDLPDFLltAESERRALLLHADFSAVGGAAQFAEDA 81
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRnaEKGEAQAAEL--EALGAKAVFVQADLSDVEDCRRVVAAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNA-----GTMLGRFPAatLTDAEYEAVVR----LNQtSVVALTRAllpalKAAEGaAIVNTVSISALt 152
Cdd:PRK06198  79 DEAFGRLDALVNAAgltdrGTILDTSPE--LFDRHFAVNVRapffLMQ-EAIKLMRR-----RKAEG-TIVNIGSMSAH- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 153 GGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEfHERYSSREK-------LEQTRKSIPLQRLGTAED 225
Cdd:PRK06198 149 GGQPFLAAYCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATE-GEDRIQREFhgapddwLEKAAATQPFGRLLDPDE 227
                        250       260
                 ....*....|....*....|..
gi 517341756 226 CAPAYLFLAAPSlSGYITGQVI 247
Cdd:PRK06198 228 VARAVAFLLSDE-SGLMTGSVI 248
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
9-252 6.96e-33

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: 120.17  E-value: 6.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgRDLPDFLLTAESER-------RALLLHADFSAVGGAAQFAEDA 81
Cdd:cd05366    2 SKVAIITGAAQGIGRAIAERLAADGFNIVL-------ADLNLEEAAKSTIQeiseagyNAVAVGADVTDKDDVEALIDQA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPAL-KAAEGAAIVNTVSISALTGgSPGSSI 160
Cdd:cd05366   75 VEKFGSFDVMVNNAGIAPIT-PLLTITEEDLKKVYAVNVFGVLFGIQAAARQFkKLGHGGKIINASSIAGVQG-FPNLGA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSRE-----KLEQTRK-----SIPLQRLGTAEDCAPAY 230
Cdd:cd05366  153 YSASKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVgeiagKPEGEGFaefssSIPLGRLSEPEDVAGLV 232
                        250       260
                 ....*....|....*....|..
gi 517341756 231 LFLAAPSlSGYITGQVIEINGG 252
Cdd:cd05366  233 SFLASED-SDYITGQTILVDGG 253
PRK06484 PRK06484
short chain dehydrogenase; Validated
10-252 2.52e-32

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 123.42  E-value: 2.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpGRDLPDFLLTAESER---RALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVV-------VADRNVERARERADSlgpDHHALAMDVSDEAQIREGFEQLHREFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGtMLGRFPAATLtDAEYEAVVRL---NQTSVVALTRALLPALKAA-EGAAIVNTVSISALTGgSPGSSIYS 162
Cdd:PRK06484  79 RIDVLVNNAG-VTDPTMTATL-DTTLEEFARLqaiNLTGAYLVAREALRLMIEQgHGAAIVNVASGAGLVA-LPKRTAYS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQT--RKSIPLQRLGTAEDCAPAYLFLAAPSlSG 240
Cdd:PRK06484 156 ASKAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGKLDPSavRSRIPLGRLGRPEEIAEAVFFLASDQ-AS 234
                        250
                 ....*....|..
gi 517341756 241 YITGQVIEINGG 252
Cdd:PRK06484 235 YITGSTLVVDGG 246
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
13-252 1.41e-31

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: 116.79  E-value: 1.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIV-----HTGRKPGRDLPDflltaeseRRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:cd05326    8 IITGGASGIGEATARLFAKHGARVVIadiddDAGQAVAAELGD--------PDISFVHCDVTVEADVRAAVDTAVARFGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGtMLGRFPAATL--TDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSpGSSIYSASK 165
Cdd:cd05326   80 LDIMFNNAG-VLGAPCYSILetSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGL-GPHAYTASK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEF--HERYSSREKLEQT--RKSIPLQRLGTAEDCAPAYLFLAAPSlSGY 241
Cdd:cd05326  158 HAVLGLTRSAATELGEHGIRVNCVSPYGVATPLltAGFGVEDEAIEEAvrGAANLKGTALRPEDIAAAVLYLASDD-SRY 236
                        250
                 ....*....|.
gi 517341756 242 ITGQVIEINGG 252
Cdd:cd05326  237 VSGQNLVVDGG 247
PRK07060 PRK07060
short chain dehydrogenase; Provisional
7-252 1.43e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 116.35  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKViVHTGRKpGRDLPDflLTAESERRALLLHadfsaVGGAAQfAEDALAFFD 86
Cdd:PRK07060   7 FSGKSVLVTGASSGIGRACAVALAQRGARV-VAAARN-AAALDR--LAGETGCEPLRLD-----VGDDAA-IRAALAAAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAA-EGAAIVNTVSISALTGgSPGSSIYSASK 165
Cdd:PRK07060  77 AFDGLVNCAGIASLE-SALDMTAEGFDRVMAVNARGAALVARHVARAMIAAgRGGSIVNVSSQAALVG-LPDHLAYCASK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHER-YSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLSgYITG 244
Cdd:PRK07060 155 AALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEaWSDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAAS-MVSG 233

                 ....*...
gi 517341756 245 QVIEINGG 252
Cdd:PRK07060 234 VSLPVDGG 241
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
9-199 1.65e-31

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 116.41  E-value: 1.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdlpdfLLTAESERRAL-LLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:COG3967    5 GNTILITGGTSGIGLALAKRLHARGNTVII-TGRREEK-----LEEAAAANPGLhTIVLDVADPASIAALAEQVTAEFPD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMlgRF-----PAATLTDAEYEavVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYS 162
Cdd:COG3967   79 LNVLINNAGIM--RAedlldEAEDLADAERE--ITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFV-PLAVTPTYS 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFH 199
Cdd:COG3967  154 ATKAALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLT 190
PRK08628 PRK08628
SDR family oxidoreductase;
8-252 1.82e-31

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 116.60  E-value: 1.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGA-KVIVhtgrkpGRDLPDFLLTAESER---RALLLHADFSAVGGAAQFAEDALA 83
Cdd:PRK08628   6 KDKVVIVTGGASGIGAAISLRLAEEGAiPVIF------GRSAPDDEFAEELRAlqpRAEFVQVDLTDDAQCRDAVEQTVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAGTMLGrfpaATLtDAEYEAVVR---LNQTSVVALTRALLPALKAAEGAaIVNTVSISALTGGSpGSSI 160
Cdd:PRK08628  80 KFGRIDGLVNNAGVNDG----VGL-EAGREAFVAsleRNLIHYYVMAHYCLPHLKASRGA-IVNISSKTALTGQG-GTSG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSS-----REKLEQTRKSIPL-QRLGTAEDCAPAYLFLA 234
Cdd:PRK08628 153 YAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIAtfddpEAKLAAITAKIPLgHRMTTAEEIADTAVFLL 232
                        250
                 ....*....|....*...
gi 517341756 235 APsLSGYITGQVIEINGG 252
Cdd:PRK08628 233 SE-RSSHTTGQWLFVDGG 249
PRK06123 PRK06123
SDR family oxidoreductase;
12-253 2.60e-31

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 116.03  E-value: 2.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKpgRDLPDFLLTAESER--RALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLNYLRN--RDAAEAVVQAIRRQggEALAVAADVADEADVLRLFEAVDRELGRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGtMLGRfpAATLTDAEYEAVVRLNQTSVVALTRALLPALK------AAEGAAIVNTVSISALTGgSPGSSI-YS 162
Cdd:PRK06123  83 ALVNNAG-ILEA--QMRLEQMDAARLTRIFATNVVGSFLCAREAVKrmstrhGGRGGAIVNVSSMAARLG-SPGEYIdYA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLSgYI 242
Cdd:PRK06123 159 ASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDRVKAGIPMGRGGTAEEVARAILWLLSDEAS-YT 237
                        250
                 ....*....|.
gi 517341756 243 TGQVIEINGGQ 253
Cdd:PRK06123 238 TGTFIDVSGGR 248
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
8-252 3.23e-31

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: 115.89  E-value: 3.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMlGRFPAATLTDAEYE---AVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAL--------TGGSP 156
Cdd:cd08930   81 IDILINNAYPS-PKVWGSRFEEFPYEqwnEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGViapdfriyENTQM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 157 GSSI-YSASKAFVATYSKALARELAPDGIRVNCVSPGTI----ETEFHERYSSRekleqtrksIPLQRLGTAEDCAPAYL 231
Cdd:cd08930  160 YSPVeYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIlnnqPSEFLEKYTKK---------CPLKRMLNPEDLRGAII 230
                        250       260
                 ....*....|....*....|.
gi 517341756 232 FLAApSLSGYITGQVIEINGG 252
Cdd:cd08930  231 FLLS-DASSYVTGQNLVIDGG 250
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
9-252 3.52e-31

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: 115.37  E-value: 3.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKV-IVHTGRKPGRDLpdflltAESER-RALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVvFADIDEERGADF------AEAEGpNLFFVHGDVADETLVKFVVYAMLEKLG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRFPAATLTDaEYEAVVRLNQTSVVALTRALLPALKAAEGAaIVNTVSISALTGgSPGSSIYSASKA 166
Cdd:cd09761   75 RIDVLVNNAARGSKGILSSLLLE-EWDRILSVNLTGPYELSRYCRDELIKNKGR-IINIASTRAFQS-EPDSEAYAASKG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDgIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQV 246
Cdd:cd09761  152 GLVALTHALAMSLGPD-IRVNCISPGWINTTEQQEFTAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQD-AGFITGET 229

                 ....*.
gi 517341756 247 IEINGG 252
Cdd:cd09761  230 FIVDGG 235
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
8-252 5.28e-31

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 115.44  E-value: 5.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR------DLPDFLLTAESERRAlllHADFSAVggaaqfAEDA 81
Cdd:PRK06200   5 HGQVALITGGGSGIGRALVERFLAEGARVAV-LERSAEKlaslrqRFGDHVLVVEGDVTS---YADNQRA------VDQT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAG-----TMLGRFPAATLtDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVnTVSISAL-TGGs 155
Cdd:PRK06200  75 VDAFGKLDCFVGNAGiwdynTSLVDIPAETL-DTAFDEIFNVNVKGYLLGAKAALPALKASGGSMIF-TLSNSSFyPGG- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 pGSSIYSASKAFVATYSKALARELAPDgIRVNCVSPGTIETEFH---------ERYSSREKLEQTRKSI-PLQRLGTAED 225
Cdd:PRK06200 152 -GGPLYTASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLRgpaslgqgeTSISDSPGLADMIAAItPLQFAPQPED 229
                        250       260
                 ....*....|....*....|....*..
gi 517341756 226 CAPAYLFLAAPSLSGYITGQVIEINGG 252
Cdd:PRK06200 230 HTGPYVLLASRRNSRALTGVVINADGG 256
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
1-252 6.51e-31

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: 114.95  E-value: 6.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   1 MFHPRLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESerraLLLHADFSAVGGAA---QF 77
Cdd:cd08936    2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEG----LSVTGTVCHVGKAEdreRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  78 AEDALAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPG 157
Cdd:cd08936   78 VATAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHP-FPG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 158 SSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEF-HERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAP 236
Cdd:cd08936  157 LGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFsSALWMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSE 236
                        250
                 ....*....|....*.
gi 517341756 237 SLSgYITGQVIEINGG 252
Cdd:cd08936  237 DAS-YITGETVVVGGG 251
PRK08589 PRK08589
SDR family oxidoreductase;
5-252 9.34e-31

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 115.26  E-value: 9.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   5 RLfENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgRDLPDFL-LTAESER----RALLLHADFSAVGGAAQFAE 79
Cdd:PRK08589   3 RL-ENKVAVITGASTGIGQASAIALAQEGAYVLA-------VDIAEAVsETVDKIKsnggKAKAYHVDISDEQQVKDFAS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  80 DALAFFDRVDVLVNNAGT-----MLGRFPAATltdaeYEAVVRLNQTSVVALTRALLPaLKAAEGAAIVNTVSISALTGG 154
Cdd:PRK08589  75 EIKEQFGRVDVLFNNAGVdnaagRIHEYPVDV-----FDKIMAVDMRGTFLMTKMLLP-LMMEQGGSIINTSSFSGQAAD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 155 SPGSSiYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRK-------SIPLQRLGTAEDCA 227
Cdd:PRK08589 149 LYRSG-YNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKLTGTSEDEAGKTfrenqkwMTPLGRLGKPEEVA 227
                        250       260
                 ....*....|....*....|....*
gi 517341756 228 PAYLFLAAPSlSGYITGQVIEINGG 252
Cdd:PRK08589 228 KLVVFLASDD-SSFITGETIRIDGG 251
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
10-227 2.20e-30

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: 112.84  E-value: 2.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhtGRKPGRDLPDFLLtaeSERRALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSL--GLRNPEDLAALSA---SGGDVEAVPYDARDPEDARALVDALRDRFGRID 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMlGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAlTGGSPGSSIYSASKAFVA 169
Cdd:cd08932   76 VLVHNAGIG-RPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSG-KRVLAGNAGYSASKFALR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517341756 170 TYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREkleqtrkSIPLQRLGTAEDCA 227
Cdd:cd08932  154 ALAHALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVG-------AFPPEEMIQPKDIA 204
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
13-252 2.22e-30

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: 113.70  E-value: 2.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPD-FLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd08940    6 LVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVrAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGGVDIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAG----TMLGRFPAATltdaeYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYSASKAF 167
Cdd:cd08940   86 VNNAGiqhvAPIEDFPTEK-----WDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLV-ASANKSAYVAAKHG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 168 VATYSKALARELAPDGIRVNCVSPGTIETEFHERysSREKLEQTR-------------KSIPLQRLGTAEDCAPAYLFLA 234
Cdd:cd08940  160 VVGLTKVVALETAGTGVTCNAICPGWVLTPLVEK--QISALAQKNgvpqeqaarelllEKQPSKQFVTPEQLGDTAVFLA 237
                        250
                 ....*....|....*...
gi 517341756 235 APSLSGyITGQVIEINGG 252
Cdd:cd08940  238 SDAASQ-ITGTAVSVDGG 254
PRK07985 PRK07985
SDR family oxidoreductase;
7-253 2.47e-30

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 114.71  E-value: 2.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDF-LLTAESERRALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAQDVkKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKAL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAaeGAAIVNTVSISALTGgSPGSSIYSASK 165
Cdd:PRK07985 127 GGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPK--GASIITTSSIQAYQP-SPHLLDYAATK 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFH-ERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITG 244
Cdd:PRK07985 204 AAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQiSGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQE-SSYVTA 282

                 ....*....
gi 517341756 245 QVIEINGGQ 253
Cdd:PRK07985 283 EVHGVCGGE 291
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
8-252 2.52e-30

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 113.44  E-value: 2.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpGRDLPDFLLTAESER----RALLLHADFSAVGGAAQFAEDALA 83
Cdd:PRK12429   3 KGKVALVTGAASGIGLEIALALAKEGAKVVIA-----DLNDEAAAAAAEALQkaggKAIGVAMDVTDEEAINAGIDYAVE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAG----TMLGRFPAATltdaeYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSS 159
Cdd:PRK12429  78 TFGGVDILVNNAGiqhvAPIEDFPTEK-----WKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLV-GSAGKA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET-----EFHERYSSR-EKLEQTRKSI-----PLQRLGTAEDCAP 228
Cdd:PRK12429 152 AYVSAKHGLIGLTKVVALEGATHGVTVNAICPGYVDTplvrkQIPDLAKERgISEEEVLEDVllplvPQKRFTTVEEIAD 231
                        250       260
                 ....*....|....*....|....
gi 517341756 229 AYLFLAAPSLSGyITGQVIEINGG 252
Cdd:PRK12429 232 YALFLASFAAKG-VTGQAWVVDGG 254
PRK07035 PRK07035
SDR family oxidoreductase;
13-255 2.91e-30

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 113.19  E-value: 2.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVhTGRK--PGRDLPDFLLTAESERRALLLHadfsaVGGAAQFaeDAL-----AFF 85
Cdd:PRK07035  12 LVTGASRGIGEAIAKLLAQQGAHVIV-SSRKldGCQAVADAIVAAGGKAEALACH-----IGEMEQI--DALfahirERH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGT------MLGRFPAAtltdaeYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSS 159
Cdd:PRK07035  84 GRLDILVNNAAAnpyfghILDTDLGA------FQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPG-DFQG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREK-LEQTRKSIPLQRLGTAEDCAPAYLFLAApSL 238
Cdd:PRK07035 157 IYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAiLKQALAHIPLRRHAEPSEMAGAVLYLAS-DA 235
                        250
                 ....*....|....*..
gi 517341756 239 SGYITGQVIEINGGQLI 255
Cdd:PRK07035 236 SSYTTGECLNVDGGYLS 252
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
8-252 4.68e-30

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 112.97  E-value: 4.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLH-ADFSAVGGAAQFAEDAlafFD 86
Cdd:PRK08226   5 TGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCGRGHRCTAVVADvRDPASVAAAIKRAKEK---EG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTM-LGRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYSASK 165
Cdd:PRK08226  82 RIDILVNNAGVCrLGSF--LDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVADPGETAYALTK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREK-------LEQTRKSIPLQRLGTAEDCAPAYLFLAAPSl 238
Cdd:PRK08226 160 AAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSNpedpesvLTEMAKAIPLRRLADPLEVGELAAFLASDE- 238
                        250
                 ....*....|....
gi 517341756 239 SGYITGQVIEINGG 252
Cdd:PRK08226 239 SSYLTGTQNVIDGG 252
PRK07063 PRK07063
SDR family oxidoreductase;
4-252 5.23e-30

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 112.84  E-value: 5.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   4 PRLfENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgRDLPDFLLTAESER--------RALLLHADFSAVGGAA 75
Cdd:PRK07063   3 NRL-AGKVALVTGAAQGIGAAIARAFAREGAAVAL-------ADLDAALAERAAAAiardvagaRVLAVPADVTDAASVA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  76 QFAEDALAFFDRVDVLVNNAGTMLGRFPaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGS 155
Cdd:PRK07063  75 AAVAAAEEAFGPLDVLVNNAGINVFADP-LAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFK-II 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSR-----EKLEQTRKSIPLQRLGTAEDCAPAY 230
Cdd:PRK07063 153 PGCFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAqpdpaAARAETLALQPMKRIGRPEEVAMTA 232
                        250       260
                 ....*....|....*....|....*
gi 517341756 231 LFLA---APslsgYITGQVIEINGG 252
Cdd:PRK07063 233 VFLAsdeAP----FINATCITIDGG 253
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
7-252 5.65e-30

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: 112.20  E-value: 5.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLpdflLTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQA----VVAQIAGGALALRVDVTDEQQVAALFERAVEEFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAlTGGSPGSSIYSASKA 166
Cdd:cd08944   77 GLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAG-QSGDPGYGAYGASKA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREklEQTRKSIP--------LQRLGTAEDCAPAYLFLAAPSL 238
Cdd:cd08944  156 AIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGF--EGALGPGGfhllihqlQGRLGRPEDVAAAVVFLLSDDA 233
                        250
                 ....*....|....
gi 517341756 239 SgYITGQVIEINGG 252
Cdd:cd08944  234 S-FITGQVLCVDGG 246
PRK09072 PRK09072
SDR family oxidoreductase;
8-198 6.91e-30

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 112.73  E-value: 6.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtGRKPGRdlpdflLTAESER-----RALLLHADFSAVGGAAQFAEDAL 82
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLV-GRNAEK------LEALAARlpypgRHRWVVADLTSEAGREAVLARAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFfDRVDVLVNNAGTmlGRFpaATLTDAEYEAVVR---LNQTSVVALTRALLPALKAAEGAAIVNTVSisalTGGS---P 156
Cdd:PRK09072  77 EM-GGINVLINNAGV--NHF--ALLEDQDPEAIERllaLNLTAPMQLTRALLPLLRAQPSAMVVNVGS----TFGSigyP 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 517341756 157 GSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK09072 148 GYASYCASKFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
PRK07576 PRK07576
short chain dehydrogenase; Provisional
7-253 8.72e-30

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 112.36  E-value: 8.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPDFLLTAESERRALLLHAD---FSAVGGAAQFAEDALA 83
Cdd:PRK07576   7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAV-ASRSQEKVDAAVAQLQQAGPEGLGVSADvrdYAAVEAAFAQIADEFG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDrvdVLVNNAGtmlGRFPA--ATLTDAEYEAVVRLNQTSVVALTRALLPALKAAeGAAIVNtvsISALTGG--SPGSS 159
Cdd:PRK07576  86 PID---VLVSGAA---GNFPApaAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRP-GASIIQ---ISAPQAFvpMPMQA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIE-TEFHERYSSREKLEQT-RKSIPLQRLGTAEDCAPAYLFLAAPS 237
Cdd:PRK07576 156 HVCAAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAgTEGMARLAPSPELQAAvAQSVPLKRNGTKQDIANAALFLASDM 235
                        250
                 ....*....|....*.
gi 517341756 238 LSgYITGQVIEINGGQ 253
Cdd:PRK07576 236 AS-YITGVVLPVDGGW 250
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
1-252 1.26e-29

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 111.86  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   1 MFHPRLF--ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpgRDLPDFLLTAESER--RALLLHADFSAVGGAAQ 76
Cdd:PRK06113   1 MFNSDNLrlDGKCAIITGAGAGIGKEIAITFATAGASVVVSDIN---ADAANHVVDEIQQLggQAFACRCDITSEQELSA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  77 FAEDALAFFDRVDVLVNNAGtmlGRFPAA-TLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGS 155
Cdd:PRK06113  78 LADFALSKLGKVDILVNNAG---GGGPKPfDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSiYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAA 235
Cdd:PRK06113 155 NMTS-YASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCS 233
                        250
                 ....*....|....*..
gi 517341756 236 PSlSGYITGQVIEINGG 252
Cdd:PRK06113 234 PA-ASWVSGQILTVSGG 249
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
8-252 1.97e-29

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 111.36  E-value: 1.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIV--HTGRKPGRDLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:PRK08936   6 EGKVVVITGGSTGLGRAMAVRFGKEKAKVVInyRSDEEEANDVAEEIKKAGGE--AIAVKGDVTVESDVVNLIQTAVKEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTR-ALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSAS 164
Cdd:PRK08936  84 GTLDVMINNAG-IENAVPSHEMSLEDWNKVINTNLTGAFLGSReAIKYFVEHDIKGNIINMSSVHEQIPW-PLFVHYAAS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFH-ERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAApSLSGYIT 243
Cdd:PRK08936 162 KGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINaEKFADPKQRADVESMIPMGYIGKPEEIAAVAAWLAS-SEASYVT 240

                 ....*....
gi 517341756 244 GQVIEINGG 252
Cdd:PRK08936 241 GITLFADGG 249
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
5-253 2.00e-29

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 111.27  E-value: 2.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   5 RLfENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDlpdFLLTAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK07067   3 RL-QGKVALLTGAASGIGEAVAERYLAEGARVVI-ADIKPARA---RLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVER 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTmlgrFPAATLTD---AEYEAVVRLNQTSVVALTRALLPALKA-AEGAAIVNTVSiSALTGGSPGSSI 160
Cdd:PRK07067  78 FGGIDILFNNAAL----FDMAPILDisrDSYDRLFAVNVKGLFFLMQAVARHMVEqGRGGKIINMAS-QAGRRGEALVSH 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHE-------RYSSR---EKLEQTRKSIPLQRLGTAEDCAPAY 230
Cdd:PRK07067 153 YCATKAAVISYTQSAALALIRHGINVNAIAPGVVDTPMWDqvdalfaRYENRppgEKKRLVGEAVPLGRMGVPDDLTGMA 232
                        250       260
                 ....*....|....*....|...
gi 517341756 231 LFLAAPSlSGYITGQVIEINGGQ 253
Cdd:PRK07067 233 LFLASAD-ADYIVAQTYNVDGGN 254
PRK09730 PRK09730
SDR family oxidoreductase;
13-253 2.06e-29

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 111.10  E-value: 2.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAvggaaqfAEDALAFFDRVD--- 89
Cdd:PRK09730   5 LVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISD-------ENQVVAMFTAIDqhd 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 ----VLVNNAGTMlgrFPAATLTDAEYEAVVRLNQTSVVALTRALLPALK------AAEGAAIVNtVSISALTGGSPGSS 159
Cdd:PRK09730  78 eplaALVNNAGIL---FTQCTVENLTAERINRVLSTNVTGYFLCCREAVKrmalkhGGSGGAIVN-VSSAASRLGAPGEY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 160 I-YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSL 238
Cdd:PRK09730 154 VdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGRVDRVKSNIPMQRGGQPEEVAQAIVWLLSDKA 233
                        250
                 ....*....|....*
gi 517341756 239 SgYITGQVIEINGGQ 253
Cdd:PRK09730 234 S-YVTGSFIDLAGGK 247
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
7-220 2.36e-29

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 110.09  E-value: 2.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdlpdfLLTAESERRALL-LHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVII-TGRREER-----LAEAKKELPNIHtIVLDVGDAESVEALAEALLSEY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLG---RFPAATLTDAEYEavVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYS 162
Cdd:cd05370   77 PNLDILINNAGIQRPidlRDPASDLDKADTE--IDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFV-PMAANPVYC 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHErySSREKLEQTRKSIPLQRL 220
Cdd:cd05370  154 ATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHE--ERRNPDGGTPRKMPLDEF 209
PRK08265 PRK08265
short chain dehydrogenase; Provisional
8-252 3.33e-29

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 110.87  E-value: 3.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKV-IVHTGRKPGRDLpdfllTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK08265   5 AGKVAIVTGGATLIGAAVARALVAAGARVaIVDIDADNGAAV-----AASLGERARFIATDITDDAAIERAVATVVARFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRFPAATltDAEYEAVVRLNQTSVVALTRALLPALKAAeGAAIVNTVSISAlTGGSPGSSIYSASKA 166
Cdd:PRK08265  80 RVDILVNLACTYLDDGLASS--RADWLAALDVNLVSAAMLAQAAHPHLARG-GGAIVNFTSISA-KFAQTGRWLYPASKA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEFHERYS--SREKLEQTRKSI-PLQRLGTAEDCAPAYLFLAAPSLSgYIT 243
Cdd:PRK08265 156 AIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDELSggDRAKADRVAAPFhLLGRVGDPEEVAQVVAFLCSDAAS-FVT 234

                 ....*....
gi 517341756 244 GQVIEINGG 252
Cdd:PRK08265 235 GADYAVDGG 243
PRK05867 PRK05867
SDR family oxidoreductase;
10-252 3.41e-29

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 110.51  E-value: 3.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDLPDFLLTAESER----RALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:PRK05867  10 KRALITGASTGIGKRVALAYVEAGAQVAI-----AARHLDALEKLADEIGtsggKVVPVCCDVSQHQQVTSMLDQVTAEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPAL-KAAEGAAIVNTVSISALTGGSPGS-SIYSA 163
Cdd:PRK05867  85 GGIDIAVCNAG-IITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMvKQGQGGVIINTASMSGHIINVPQQvSHYCA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRksIPLQRLGTAEDCAPAYLFLAAPSlSGYIT 243
Cdd:PRK05867 164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQPLWEPK--IPLGRLGRPEELAGLYLYLASEA-SSYMT 240

                 ....*....
gi 517341756 244 GQVIEINGG 252
Cdd:PRK05867 241 GSDIVIDGG 249
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
13-252 3.77e-29

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 110.59  E-value: 3.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIV-----HTGRKPGRDLpdflltAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK08643   6 LVTGAGQGIGFAIAKRLVEDGFKVAIvdyneETAQAAADKL------SKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGtmLG-RFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKA-AEGAAIVNTVSiSALTGGSPGSSIYSASK 165
Cdd:PRK08643  80 LNVVVNNAG--VApTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKlGHGGKIINATS-QAGVVGNPELAVYSSTK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHE---RYSSREK-------LEQTRKSIPLQRLGTAEDCAPAYLFLAA 235
Cdd:PRK08643 157 FAVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFdiaHQVGENAgkpdewgMEQFAKDITLGRLSEPEDVANCVSFLAG 236
                        250
                 ....*....|....*..
gi 517341756 236 PSlSGYITGQVIEINGG 252
Cdd:PRK08643 237 PD-SDYITGQTIIVDGG 252
PRK07074 PRK07074
SDR family oxidoreductase;
9-252 4.52e-29

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 110.24  E-value: 4.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK07074   2 KRTALVTGAAGGIGQALARRFLAAGDRVLA---LDIDAAALAAFADALGDARFVPVACDLTDAASLAAALANAAAERGPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMLGRFPAATlTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTG-GSPGssiYSASKAF 167
Cdd:PRK07074  79 DVLVANAGAARAASLHDT-TPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGMAAlGHPA---YSAAKAG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 168 VATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSR--EKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGYITGQ 245
Cdd:PRK07074 155 LIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAAnpQVFEELKKWYPLQDFATPDDVANAVLFLASP-AARAITGV 233

                 ....*..
gi 517341756 246 VIEINGG 252
Cdd:PRK07074 234 CLPVDGG 240
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
8-252 5.89e-29

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: 110.13  E-value: 5.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgrdlpdflLTAESERRALLLHA---DFSAVGGAAQFAED---- 80
Cdd:cd05348    3 KGEVALITGGGSGLGRALVERFVAEGAKVAV--------------LDRSAEKVAELRADfgdAVVGVEGDVRSLADnera 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ---ALAFFDRVDVLVNNAG-----TMLGRFPAATLTDAeYEAVVRLNQTSVVALTRALLPALKAAEGAAIVnTVSISALT 152
Cdd:cd05348   69 varCVERFGKLDCFIGNAGiwdysTSLVDIPEEKLDEA-FDELFHINVKGYILGAKAALPALYATEGSVIF-TVSNAGFY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 153 GGSpGSSIYSASKAFVATYSKALARELAPDgIRVNCVSPGTIET--------EFHERYSSREKLEQTRKSI-PLQRLGTA 223
Cdd:cd05348  147 PGG-GGPLYTASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTdlrgpaslGQGETSISTPPLDDMLKSIlPLGFAPEP 224
                        250       260
                 ....*....|....*....|....*....
gi 517341756 224 EDCAPAYLFLAAPSLSGYITGQVIEINGG 252
Cdd:cd05348  225 EDYTGAYVFLASRGDNRPATGTVINYDGG 253
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
6-252 1.04e-28

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 108.95  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAGRGIGLEVARQFLDCGAKVIV------HTGRKPGRDLPDflLTAESERR----ALllhADFSAVGGAA 75
Cdd:cd05353    2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdRKGSGKSSSAAD--KVVDEIKAaggkAV---ANYDSVEDGE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  76 QFAEDALAFFDRVDVLVNNAGTMLGR-FpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgG 154
Cdd:cd05353   77 KIVKTAIDAFGRVDILVNNAGILRDRsF--AKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLY-G 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 155 SPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSP--GTIETEFHERYSSREKLEqtrksiplqrlgtAEDCAPAYLF 232
Cdd:cd05353  154 NFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPaaGSRMTETVMPEDLFDALK-------------PEYVAPLVLY 220
                        250       260
                 ....*....|....*....|
gi 517341756 233 LAAPSLSgyITGQVIEINGG 252
Cdd:cd05353  221 LCHESCE--VTGGLFEVGAG 238
PRK07326 PRK07326
SDR family oxidoreductase;
7-198 1.25e-28

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 108.56  E-value: 1.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK07326   4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAI-TARDQKE-LEEAAAELNNKGNVLGLAADVRDEADVQRAVDAIVAAFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGtmLGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIvntvSISALTGGSP--GSSIYSA 163
Cdd:PRK07326  82 GLDVLIANAG--VGHFaPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYII----NISSLAGTNFfaGGAAYNA 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK07326 156 SKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHF 190
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
13-255 2.00e-28

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 108.51  E-value: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPDFLLTAESE-RRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAI-NDRPDDEELAATQQELRALgVEVIFFPADVADLSAHEAMLDAAQAAWGRIDCL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAG-TMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEG------AAIVNTVSISAlTGGSPGSSIYSAS 164
Cdd:PRK12745  85 VNNAGvGVKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNA-IMVSPNRGEYCIS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEF----HERYSSREKLEQTrksiPLQRLGTAEDCAPAYLFLAAPSLsG 240
Cdd:PRK12745 164 KAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMtapvTAKYDALIAKGLV----PMPRWGEPEDVARAVAALASGDL-P 238
                        250
                 ....*....|....*
gi 517341756 241 YITGQVIEINGGQLI 255
Cdd:PRK12745 239 YSTGQAIHVDGGLSI 253
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
8-253 3.35e-28

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 108.17  E-value: 3.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKViVHTGRKPGRDLPDFLLtaeserralLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK06171   8 QGKIIIVTGGSSGIGLAIVKELLANGANV-VNADIHGGDGQHENYQ---------FVPTDVSSAEEVNHTVAEIIEKFGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMLGRF--------PAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSS 159
Cdd:PRK06171  78 IDGLVNNAGINIPRLlvdekdpaGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEG-SEGQS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIE-----TEFHER---YSSREKLEQTR------KSIPLQRLGTAED 225
Cdd:PRK06171 157 CYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEatglrTPEYEEalaYTRGITVEQLRagytktSTIPLGRSGKLSE 236
                        250       260
                 ....*....|....*....|....*...
gi 517341756 226 CAPAYLFLAAPSlSGYITGQVIEINGGQ 253
Cdd:PRK06171 237 VADLVCYLLSDR-ASYITGVTTNIAGGK 263
PRK12743 PRK12743
SDR family oxidoreductase;
9-255 3.85e-28

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 107.81  E-value: 3.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIG----LEVARQFLDCGakVIVHTGRKPGRDlpdfllTAESER----RALLLHADFSAVGGAAQFAED 80
Cdd:PRK12743   2 AQVAIVTASDSGIGkacaLLLAQQGFDIG--ITWHSDEEGAKE------TAEEVRshgvRAEIRQLDLSDLPEGAQALDK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGTMLGrfpaATLTDAEYEAVVRLNQTSV----VALTRALLPALKAAEGAAIVNTVSISALTGgSP 156
Cdd:PRK12743  74 LIQRLGRIDVLVNNAGAMTK----APFLDMDFDEWRKIFTVDVdgafLCSQIAARHMVKQGQGGRIINITSVHEHTP-LP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 157 GSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKlEQTRKSIPLQRLGTAEDCAPAYLFLAAP 236
Cdd:PRK12743 149 GASAYTAAKHALGGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVK-PDSRPGIPLGRPGDTHEIASLVAWLCSE 227
                        250
                 ....*....|....*....
gi 517341756 237 SlSGYITGQVIEINGGQLI 255
Cdd:PRK12743 228 G-ASYTTGQSLIVDGGFML 245
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
13-232 4.41e-28

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: 107.24  E-value: 4.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPG-RDLPDfLLTAESERrALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd08934    7 LVTGASSGIGEATARALAAEGAAVAIAARRVDRlEALAD-ELEAEGGK-ALVLELDVTDEQQVDAAVERTVEALGRLDIL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTML-GrfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAlTGGSPGSSIYSASKAFVAT 170
Cdd:cd08934   85 VNNAGIMLlG--PVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAG-RVAVRNSAVYNATKFGVNA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517341756 171 YSKALARELAPDGIRVNCVSPGTIETEF--HERYSSREKL--EQTRKSIPLQrlgtAEDCAPAYLF 232
Cdd:cd08934  162 FSEGLRQEVTERGVRVVVIEPGTVDTELrdHITHTITKEAyeERISTIRKLQ----AEDIAAAVRY 223
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
6-245 7.28e-28

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: 106.51  E-value: 7.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtGRKPG--RDLPDFLlTAESERRALLLHADFSAVGG--AAQFAEDA 81
Cdd:cd05340    1 LLNDRIILVTGASDGIGREAALTYARYGATVILL-GRNEEklRQVADHI-NEEGGRQPQWFILDLLTCTSenCQQLAQRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSiY 161
Cdd:cd05340   79 AVNYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGA-Y 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETefherySSREKLEQTRKSiplQRLGTAEDCAPAYLFLAAPSLSGy 241
Cdd:cd05340  158 AVSKFATEGL*QVLADEYQQRNLRVNCINPGGTRT------AMRASAFPTEDP---QKLKTPADIMPLYLWLMGDDSRR- 227

                 ....
gi 517341756 242 ITGQ 245
Cdd:cd05340  228 KTGM 231
PRK08264 PRK08264
SDR family oxidoreductase;
7-197 8.03e-28

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 106.51  E-value: 8.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRdlpdfllTAESERRALLLHADFS---AVGGAAQFAEDala 83
Cdd:PRK08264   4 IKGKVVLVTGANRGIGRAFVEQLLARGAAKVYAAARDPES-------VTDLGPRVVPLQLDVTdpaSVAAAAEAASD--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 ffdrVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSA 163
Cdd:PRK08264  74 ----VTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNF-PNLGTYSA 148
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 517341756 164 SKAfvATYS--KALARELAPDGIRVNCVSPGTIETE 197
Cdd:PRK08264 149 SKA--AAWSltQALRAELAPQGTRVLGVHPGPIDTD 182
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
12-252 1.13e-27

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 106.42  E-value: 1.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpGRDLpdflltaeserRALLLHADFSAVGGAAQFAEDALAFFDRV-DV 90
Cdd:cd05328    2 IVITGAASGIGAATAELLEDAGHTVI-------GIDL-----------READVIADLSTPEGRAAAIADVLARCSGVlDG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  91 LVNNAGTmlgrfPAATLTDAeyeaVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAL------------------- 151
Cdd:cd05328   64 LVNCAGV-----GGTTVAGL----VLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdklelakalaagtea 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 152 -------TGGSPGSSIYSASKAFVATYSKALARE-LAPDGIRVNCVSPGTIETEFHERYSSREKL-EQTRKSI-PLQRLG 221
Cdd:cd05328  135 ravalaeHAGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPRGgESVDAFVtPMGRRA 214
                        250       260       270
                 ....*....|....*....|....*....|.
gi 517341756 222 TAEDCAPAYLFLAAPSLSgYITGQVIEINGG 252
Cdd:cd05328  215 EPDEIAPVIAFLASDAAS-WINGANLFVDGG 244
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
6-253 1.16e-27

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 106.34  E-value: 1.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKpgRDLPDFLLtAESE---RRALLLHADFSAVGGAAQFAEDAL 82
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARS--RKAAEETA-EEIEalgRKALAVKANVGDVEKIKEMFAQID 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVntvSISALtgGS----PGS 158
Cdd:PRK08063  78 EEFGRLDVFVNNAASGVLR-PAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKII---SLSSL--GSirylENY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 159 SIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREK-LEQTRKSIPLQRLGTAEDCAPAYLFLAAPS 237
Cdd:PRK08063 152 TTVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREElLEDARAKTPAGRMVEPEDVANAVLFLCSPE 231
                        250
                 ....*....|....*.
gi 517341756 238 lSGYITGQVIEINGGQ 253
Cdd:PRK08063 232 -ADMIRGQTIIVDGGR 246
PRK06181 PRK06181
SDR family oxidoreductase;
9-235 1.47e-27

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 106.22  E-value: 1.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKvIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQ-LVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAG-TMLGRFpaATLTDAE-YEAVVRLNQTSVVALTRALLPALKAAEGAAIVntvsISALTG--GSPGSSIYSAS 164
Cdd:PRK06181  80 DILVNNAGiTMWSRF--DELTDLSvFERVMRVNYLGAVYCTHAALPHLKASRGQIVV----VSSLAGltGVPTRSGYAAS 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKlEQTRKSiPLQ--RLGTAEDCAPAYLFLAA 235
Cdd:PRK06181 154 KHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALDGDG-KPLGKS-PMQesKIMSAEECAEAILPAIA 224
PRK07478 PRK07478
short chain dehydrogenase; Provisional
6-256 1.74e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 106.17  E-value: 1.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLpdflLTAESER---RALLLHADFSAVGGAAQFAEDAL 82
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQ----LVAEIRAeggEAVALAGDVRDEAYAKALVALAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYS 162
Cdd:PRK07478  79 ERFGGLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFPGMAAYA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETEF-HERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLSgY 241
Cdd:PRK07478 159 ASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMgRAMGDTPEALAFVAGLHALKRMAQPEEIAQAALFLASDAAS-F 237
                        250
                 ....*....|....*
gi 517341756 242 ITGQVIEINGGQLIC 256
Cdd:PRK07478 238 VTGTALLVDGGVSIT 252
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-255 1.99e-27

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 109.16  E-value: 1.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpGRDLP---DFLLTAESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK08261 209 AGKVALVTGAARGIGAAIAEVLARDGAHVV-------CLDVPaagEALAAVANRVGGTALALDITAPDAPARIAEHLAER 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGT----MLGRfpaatLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALtGGSPGSSI 160
Cdd:PRK08261 282 HGGLDIVVHNAGItrdkTLAN-----MDEARWDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSISGI-AGNRGQTN 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETE------FHERyssreklEQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:PRK08261 356 YAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQmtaaipFATR-------EAGRRMNSLQQGGLPVDVAETIAWLA 428
                        250       260
                 ....*....|....*....|.
gi 517341756 235 APSlSGYITGQVIEINGGQLI 255
Cdd:PRK08261 429 SPA-SGGVTGNVVRVCGQSLL 448
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
7-252 2.18e-27

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: 106.08  E-value: 2.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIV-HTGRKPGRDLpDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd08933    7 YADKVVIVTGGSRGIGRGIVRAFVENGAKVVFcARGEAAGQAL-ESELNRAGPGSCKFVPCDVTKEEDIKTLISVTVERF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGaaivNTVSISALTG--GSPGSSIYSA 163
Cdd:cd08933   86 GRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQG----NIINLSSLVGsiGQKQAAPYVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSreKLEQTRKSI-------PLQRLGTAEDCAPAYLFLAAP 236
Cdd:cd08933  162 TKGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAA--QTPDTLATIkegelaqLLGRMGTEAESGLAALFLAAE 239
                        250
                 ....*....|....*.
gi 517341756 237 slSGYITGQVIEINGG 252
Cdd:cd08933  240 --ATFCTGIDLLLSGG 253
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
1-252 2.34e-27

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 110.32  E-value: 2.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   1 MFHPRLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgRDL-PDFLLTAESE----RRALLLHADF---SAVg 72
Cdd:PRK08324 414 MPKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVL-------ADLdEEAAEAAAAElggpDRALGVACDVtdeAAV- 485
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  73 gAAQFAEDALAFfDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAE-GAAIVNTVSISAL 151
Cdd:PRK08324 486 -QAAFEEAALAF-GGVDIVVSNAGIAISG-PIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAV 562
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 152 TGGsPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTI-------ETEFHERYS-----SREKLEQT-RKSIPLQ 218
Cdd:PRK08324 563 NPG-PNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAVvrgsgiwTGEWIEARAaayglSEEELEEFyRARNLLK 641
                        250       260       270
                 ....*....|....*....|....*....|....
gi 517341756 219 RLGTAEDCAPAYLFLAAPsLSGYITGQVIEINGG 252
Cdd:PRK08324 642 REVTPEDVAEAVVFLASG-LLSKTTGAIITVDGG 674
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
12-197 2.66e-27

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: 105.07  E-value: 2.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPG--RDLPDFlltAESERRALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSaaTELAAL---GASHSRLHILELDVTDEIAESAEAVAERLGDAGLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTV----SISALTGGspGSSIYSASK 165
Cdd:cd05325   78 VLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISsrvgSIGDNTSG--GWYSYRASK 155
                        170       180       190
                 ....*....|....*....|....*....|..
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:cd05325  156 AALNMLTKSLAVELKRDGITVVSLHPGWVRTD 187
PRK06947 PRK06947
SDR family oxidoreductase;
12-253 4.14e-27

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 104.89  E-value: 4.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpgrDLPDFLLTAESER----RALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK06947   5 VLITGASRGIGRATAVLAAARGWSVGINYAR----DAAAAEETADAVRaaggRACVVAGDVANEADVIAMFDAVQSAFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMLgrfPAATLTDAEYEAVVRLNQTSVVAltrALLPALKAAE---------GAAIVNTVSISALTGgSPGS 158
Cdd:PRK06947  81 LDALVNNAGIVA---PSMPLADMDAARLRRMFDTNVLG---AYLCAREAARrlstdrggrGGAIVNVSSIASRLG-SPNE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 159 SI-YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPS 237
Cdd:PRK06947 154 YVdYAGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAARLGAQTPLGRAGEADEVAETIVWLLSDA 233
                        250
                 ....*....|....*.
gi 517341756 238 LSgYITGQVIEINGGQ 253
Cdd:PRK06947 234 AS-YVTGALLDVGGGR 248
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
8-252 8.05e-27

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: 104.54  E-value: 8.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDLPDFLLTAESERRALL----LHADFSAVGGAAQFAEDALA 83
Cdd:cd08945    2 DSEVALVTGATSGIGLAIARRLGKEGLRVFV-----CARGEEGLATTVKELREAGVeadgRTCDVRSVPEIEALVAAAVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAGTmLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPA--LKAAEGAAIVNTVSisalTGGSPG---S 158
Cdd:cd08945   77 RYGPIDVLVNNAGR-SGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIAS----TGGKQGvvhA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 159 SIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY----------SSREKLEQTRKSIPLQRLGTAEDCAP 228
Cdd:cd08945  152 APYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVrehyadiwevSTEEAFDRITARVPLGRYVTPEEVAG 231
                        250       260
                 ....*....|....*....|....
gi 517341756 229 AYLFLAAPSlSGYITGQVIEINGG 252
Cdd:cd08945  232 MVAYLIGDG-AAAVTAQALNVCGG 254
PRK08267 PRK08267
SDR family oxidoreductase;
10-227 1.32e-26

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 103.86  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGA-AQFAEdalAFFDRV 88
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAWTGALDVTDRAAWDAAlADFAA---ATGGRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTML-GRFpaatlTDAEYEAVVRL---NQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSAS 164
Cdd:PRK08267  79 DVLFNNAGILRgGPF-----EDIPLEAHDRVidiNVKGVLNGAHAALPYLKATPGARVINTSSASAIYG-QPGLAVYSAT 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRksiplqRLG---TAEDCA 227
Cdd:PRK08267 153 KFAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTK------RLGvrlTPEDVA 212
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
10-255 1.47e-26

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: 103.15  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAI-LDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMLG-RFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAA---EGAAIVNTVSISALTgGSPGSSIYSASK 165
Cdd:cd05323   80 ILINNAGILDEkSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAGLY-PAPQFPVYSASK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPD-GIRVNCVSPGTIETEF-HERYSSREKLEQtrkSIPLQrlgTAEDCAPAYLFLAAPSLSgyiT 243
Cdd:cd05323  159 HGVVGFTRSLADLLEYKtGVRVNAICPGFTNTPLlPDLVAKEAEMLP---SAPTQ---SPEVVAKAIVYLIEDDEK---N 229
                        250
                 ....*....|..
gi 517341756 244 GQVIEINGGQLI 255
Cdd:cd05323  230 GAIWIVDGGKLI 241
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
7-253 1.86e-26

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 103.37  E-value: 1.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAK-VIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKlSLVDLNEEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSpGSSIYSASK 165
Cdd:cd05330   81 GRIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVG-NQSGYAAAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY-------SSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSl 238
Cdd:cd05330  160 HGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSlkqlgpeNPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDD- 238
                        250
                 ....*....|....*
gi 517341756 239 SGYITGQVIEINGGQ 253
Cdd:cd05330  239 AGYVNAAVVPIDGGQ 253
PRK07677 PRK07677
short chain dehydrogenase; Provisional
9-253 2.07e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 103.22  E-value: 2.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdlpdfLLTAESE-----RRALLLHADFSAVGGAAQFAEDALA 83
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVI-TGRTKEK-----LEEAKLEieqfpGQVLTVQMDVRNPEDVQKMVEQIDE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAGtmlGRF--PAATLTDAEYEAVVR--LNQTSVValTRALLPA-LKAAEGAAIVNTVSISALTGGsPGS 158
Cdd:PRK07677  75 KFGRIDALINNAA---GNFicPAEDLSVNGWNSVIDivLNGTFYC--SQAVGKYwIEKGIKGNIINMVATYAWDAG-PGV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 159 sIYSAS-KAFVATYSKALARELAPD-GIRVNCVSPGTIE-TEFHER-YSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:PRK07677 149 -IHSAAaKAGVLAMTRTLAVEWGRKyGIRVNAIAPGPIErTGGADKlWESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLL 227
                        250
                 ....*....|....*....
gi 517341756 235 APSLSgYITGQVIEINGGQ 253
Cdd:PRK07677 228 SDEAA-YINGTCITMDGGQ 245
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
7-256 8.61e-26

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: 101.39  E-value: 8.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTgRKPGrDLPDFLLTAESERRALLLHADFSAVggaaqfaEDALAFFD 86
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVS-RTQA-DLDSLVRECPGIEPVCVDLSDWDAT-------EEALGSVG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAE-GAAIVNtVSISALTGGSPGSSIYSASK 165
Cdd:cd05351   76 PVDLLVNNAAVAILQ-PFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVN-VSSQASQRALTNHTVYCSTK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEF-HERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAApSLSGYITG 244
Cdd:cd05351  154 AALDMLTKVMALELGPHKIRVNSVNPTVVMTDMgRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLS-DKSSMTTG 232
                        250
                 ....*....|..
gi 517341756 245 QVIEINGGQLIC 256
Cdd:cd05351  233 STLPVDGGFLAS 244
PRK06114 PRK06114
SDR family oxidoreductase;
4-252 1.67e-25

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 100.63  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   4 PRLF--ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDA 81
Cdd:PRK06114   1 PQLFdlDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVART 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAFFDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISA-LTGGSPGSSI 160
Cdd:PRK06114  81 EAELGALTLAVNAAG-IANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGiIVNRGLLQAH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERyssREKLEQTR---KSIPLQRLGTAEDCAPAYLFLAAPS 237
Cdd:PRK06114 160 YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTR---PEMVHQTKlfeEQTPMQRMAKVDEMVGPAVFLLSDA 236
                        250
                 ....*....|....*
gi 517341756 238 LSgYITGQVIEINGG 252
Cdd:PRK06114 237 AS-FCTGVDLLVDGG 250
PRK06057 PRK06057
short chain dehydrogenase; Provisional
4-252 3.67e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 99.80  E-value: 3.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   4 PRLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgRDL-PDFLLTAESERRALLLHADFSAVGGAAQFAEDAL 82
Cdd:PRK06057   2 SQRLAGRVAVITGGGSGIGLATARRLAAEGATVVV-------GDIdPEAGKAAADEVGGLFVPTDVTDEDAVNALFDTAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVNNAGTMLGRFPAATLTDAE-YEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIY 161
Cdd:PRK06057  75 ETYGSVDIAFNNAGISPPEDDSILNTGLDaWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQISY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRK--SIPLQRLGTAEDCAPAYLFLAAPSLS 239
Cdd:PRK06057 155 TASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDPERAARRlvHVPMGRFAEPEEIAAAVAFLASDDAS 234
                        250
                 ....*....|...
gi 517341756 240 gYITGQVIEINGG 252
Cdd:PRK06057 235 -FITASTFLVDGG 246
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
7-197 5.25e-25

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: 99.02  E-value: 5.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDlpdFLLTAESERRALLLHADFSAVGGAAQFAEDAlaffD 86
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVYAAVRDPGSA---AHLVAKYGDKVVPLRLDVTDPESIKAAAAQA----K 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAG--TMLGRFPAATLTDAEYEAVVrlNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSAS 164
Cdd:cd05354   74 DVDVVINNAGvlKPATLLEEGALEALKQEMDV--NVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKN-FPAMGTYSAS 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:cd05354  151 KSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTR 183
PRK07831 PRK07831
SDR family oxidoreductase;
6-249 6.76e-25

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 99.34  E-value: 6.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGA-GRGIGLEVARQFLDCGAKVIV---HTGR-KPGRDLpdflLTAES-ERRALLLHADFSAVGGAAQFAE 79
Cdd:PRK07831  14 LLAGKVVLVTAAaGTGIGSATARRALEEGARVVIsdiHERRlGETADE----LAAELgLGRVEAVVCDVTSEAQVDALID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  80 DALAFFDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAE-GAAIVNTVSISALTGgSPGS 158
Cdd:PRK07831  90 AAVERLGRLDVLVNNAG-LGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGhGGVIVNNASVLGWRA-QHGQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 159 SIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAApSL 238
Cdd:PRK07831 168 AHYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVTSAELLDELAAREAFGRAAEPWEVANVIAFLAS-DY 246
                        250
                 ....*....|.
gi 517341756 239 SGYITGQVIEI 249
Cdd:PRK07831 247 SSYLTGEVVSV 257
PRK06398 PRK06398
aldose dehydrogenase; Validated
7-255 8.89e-25

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 99.14  E-value: 8.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFlltaeserrallLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDY------------FKVDVSNKEQVIKGIDYVISKYG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGtmLGRFPAATLTDA-EYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAlTGGSPGSSIYSASK 165
Cdd:PRK06398  72 RIDILVNNAG--IESYGAIHAVEEdEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQS-FAVTRNAAAYVTSK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPdGIRVNCVSPGTIETEF----------HERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAA 235
Cdd:PRK06398 149 HAVLGLTRSIAVDYAP-TIRCVAVCPGSIRTPLlewaaelevgKDPEHVERKIREWGEMHPMKRVGKPEEVAYVVAFLAS 227
                        250       260
                 ....*....|....*....|
gi 517341756 236 pSLSGYITGQVIEINGGQLI 255
Cdd:PRK06398 228 -DLASFITGECVTVDGGLRA 246
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
7-252 9.48e-25

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 98.84  E-value: 9.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKV-IVHTGRKPGRdlpdfLLTAESERRALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVaIADINLEAAR-----ATAAEIGPAACAISLDVTDQASIDRCVAALVDRW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKA-AEGAAIVNTVSiSALTGGSPGSSIYSAS 164
Cdd:cd05363   76 GSIDILVNNAALFDLA-PIVDITRESYDRLFAINVSGTLFMMQAVARAMIAqGRGGKIINMAS-QAGRRGEALVGVYCAT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHE-------RYSSR---EKLEQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:cd05363  154 KAAVISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDgvdakfaRYENRprgEKKRLVGEAVPFGRMGRAEDLTGMAIFLA 233
                        250
                 ....*....|....*...
gi 517341756 235 APSlSGYITGQVIEINGG 252
Cdd:cd05363  234 STD-ADYIVAQTYNVDGG 250
PRK07791 PRK07791
short chain dehydrogenase; Provisional
6-252 1.57e-24

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 98.98  E-value: 1.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVH----------TGRKPGRDLPDFLLTAESErrALLLHADFSAVGGAA 75
Cdd:PRK07791   3 LLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNdigvgldgsaSGGSAAQAVVDEIVAAGGE--AVANGDDIADWDGAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  76 QFAEDALAFFDRVDVLVNNAGTMLGRFpAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAE------GAAIVNTVSIS 149
Cdd:PRK07791  81 NLVDAAVETFGGLDVLVNNAGILRDRM-IANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAESkagravDARIINTSSGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 150 ALTgGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPgtietefherySSREKLEQTRKSIPLQRLGTA------ 223
Cdd:PRK07791 160 GLQ-GSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP-----------AARTRMTETVFAEMMAKPEEGefdama 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 517341756 224 -EDCAPAYLFLAAPSlSGYITGQVIEINGG 252
Cdd:PRK07791 228 pENVSPLVVWLGSAE-SRDVTGKVFEVEGG 256
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
10-227 1.72e-24

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: 97.71  E-value: 1.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdlpdfLLTAESERRALLLH---------ADFSAVGGAAQFAED 80
Cdd:cd08939    2 KHVLITGGSSGIGKALAKELVKEGANVII-VARSESK-----LEEAVEEIEAEANAsgqkvsyisADLSDYEEVEQAFAQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGTML-GRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSS 159
Cdd:cd08939   76 AVEKGGPPDLVVNCAGISIpGLF--EDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVG-IYGYS 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERySSREKLEQTRKSIPLQRLGTAEDCA 227
Cdd:cd08939  153 AYCPSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFEE-ENKTKPEETKAIEGSSGPITPEEAA 219
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-252 1.80e-24

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 98.22  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGR--GIGLEVARQFLDCGAKVIVHTGRKPGRDLP-------DFLLTAESERRALLLH---ADFSAVGGAAQF 77
Cdd:PRK12748   6 KIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPwgmhdkePVLLKEEIESYGVRCEhmeIDLSQPYAPNRV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  78 AEDALAFFDRVDVLVNNAG----TMLGRFPAATLtDAEYEAVVRlnqtSVVALTRALLPALKAAEGAAIVNTVSISALtG 153
Cdd:PRK12748  86 FYAVSERLGDPSILINNAAysthTRLEELTAEQL-DKHYAVNVR----ATMLLSSAFAKQYDGKAGGRIINLTSGQSL-G 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 154 GSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEfherYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFL 233
Cdd:PRK12748 160 PMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTG----WITEELKHHLVPKFPQGRVGEPVDAARLIAFL 235
                        250
                 ....*....|....*....
gi 517341756 234 AAPSlSGYITGQVIEINGG 252
Cdd:PRK12748 236 VSEE-AKWITGQVIHSEGG 253
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
13-254 3.29e-24

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 97.28  E-value: 3.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKvIVHTGRKPGRDLPDflLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVLV 92
Cdd:PRK12481  12 IITGCNTGLGQGMAIGLAKAGAD-IVGVGVAEAPETQA--QVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDILI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  93 NNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPAL-KAAEGAAIVNTVSISALTGGSPGSSiYSASKAFVATY 171
Cdd:PRK12481  89 NNAG-IIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFvKQGNGGKIINIASMLSFQGGIRVPS-YTASKSAVMGL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 172 SKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQT-RKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQVIEIN 250
Cdd:PRK12481 167 TRALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAiLERIPASRWGTPDDLAGPAIFLSSSA-SDYVTGYTLAVD 245

                 ....
gi 517341756 251 GGQL 254
Cdd:PRK12481 246 GGWL 249
PRK05650 PRK05650
SDR family oxidoreductase;
11-196 3.32e-24

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 97.80  E-value: 3.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  11 NVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTaESERRALLLHADFSAVGGAAQFAEDALAFFDRVDV 90
Cdd:PRK05650   2 RVMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLR-EAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  91 LVNNAGTML-GRFPAATLTDAEYeaVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSASKAFVA 169
Cdd:PRK05650  81 IVNNAGVASgGFFEELSLEDWDW--QIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQG-PAMSSYNVAKAGVV 157
                        170       180
                 ....*....|....*....|....*..
gi 517341756 170 TYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK05650 158 ALSETLLVELADDEIGVHVVCPSFFQT 184
PRK08219 PRK08219
SDR family oxidoreductase;
8-197 3.55e-24

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 96.54  E-value: 3.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDcGAKVIVHtGRKPGRdLPDFlltAESERRALLLHADFSAVGGAAqfaeDALAFFDR 87
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAP-THTLLLG-GRPAER-LDEL---AAELPGATPFPVDLTDPEAIA----AAVEQLGR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIvnTVSISALTGGSPGSSIYSASKAF 167
Cdd:PRK08219  72 LDVLVHNAGVADLG-PVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVV--FINSGAGLRANPGWGSYAASKFA 148
                        170       180       190
                 ....*....|....*....|....*....|
gi 517341756 168 VATYSKALaRELAPDGIRVNCVSPGTIETE 197
Cdd:PRK08219 149 LRALADAL-REEEPGNVRVTSVHPGRTDTD 177
PRK07825 PRK07825
short chain dehydrogenase; Provisional
10-197 5.45e-24

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 96.93  E-value: 5.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpgrDLPDFLL--TAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALGARVAIG-------DLDEALAkeTAAELGLVVGGPLDVTDPASFAAFLDAVEADLGP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTM-LGRFpaatltDAEYEAVVRL----NQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYS 162
Cdd:PRK07825  79 IDVLVNNAGVMpVGPF------LDEPDAVTRRildvNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKI-PVPGMATYC 151
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:PRK07825 152 ASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTE 186
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
13-254 6.87e-24

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 96.48  E-value: 6.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPdfLLTAESeRRALLLHADFSAVGGAAQFAEDALAFFDRVDVLV 92
Cdd:PRK08993  14 VVTGCDTGLGQGMALGLAEAGCDIVGINIVEPTETIE--QVTALG-RRFLSLTADLRKIDGIPALLERAVAEFGHIDILV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  93 NNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPA-LKAAEGAAIVNTVSISALTGGSPGSSiYSASKAFVATY 171
Cdd:PRK08993  91 NNAG-LIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHfIAQGNGGKIINIASMLSFQGGIRVPS-YTASKSGVMGV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 172 SKALARELAPDGIRVNCVSPGTIETEFHERYSSRE-KLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQVIEIN 250
Cdd:PRK08993 169 TRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEqRSAEILDRIPAGRWGLPSDLMGPVVFLASSA-SDYINGYTIAVD 247

                 ....
gi 517341756 251 GGQL 254
Cdd:PRK08993 248 GGWL 251
PRK06125 PRK06125
short chain dehydrogenase; Provisional
7-252 9.63e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 96.27  E-value: 9.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDlPDFLLTAESERRALL-----LHA-DFSAVGGAAQFAED 80
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHL-----VARD-ADALEALAADLRAAHgvdvaVHAlDLSSPEAREQLAAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 AlaffDRVDVLVNNAGTMlgrfPAATL---TDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISaltGGSPG 157
Cdd:PRK06125  79 A----GDIDILVNNAGAI----PGGGLddvDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAA---GENPD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 158 SSiY---SASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHE---------RYSSREKLEQTRKSIPLQRLGTAED 225
Cdd:PRK06125 148 AD-YicgSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLtllkgraraELGDESRWQELLAGLPLGRPATPEE 226
                        250       260
                 ....*....|....*....|....*..
gi 517341756 226 CAPAYLFLAAPSlSGYITGQVIEINGG 252
Cdd:PRK06125 227 VADLVAFLASPR-SGYTSGTVVTVDGG 252
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-252 1.27e-23

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 95.54  E-value: 1.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLpdfLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAE---ALADELGDRAIALQADVTDREQVQAMFATATEHFGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 -VDVLVNNAgtmLGRF--------PAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTvsisaltggspGS 158
Cdd:PRK08642  81 pITTVVNNA---LADFsfdgdarkKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINI-----------GT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 159 SI----------YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAP 228
Cdd:PRK08642 147 NLfqnpvvpyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDEVFDLIAATTPLRKVTTPQEFAD 226
                        250       260
                 ....*....|....*....|....
gi 517341756 229 AYLFLAAPSLSGyITGQVIEINGG 252
Cdd:PRK08642 227 AVLFFASPWARA-VTGQNLVVDGG 249
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
12-198 1.57e-23

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: 94.88  E-value: 1.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdlPDFLLTAESERrALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd08929    3 ALVTGASRGIGEATARLLHAEGYRVGI-CARDEAR--LAAAAAQELEG-VLGLAGDVRDEADVRRAVDAMEEAFGGLDAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtvsISALTGGSP--GSSIYSASKAFVA 169
Cdd:cd08929   79 VNNAGVGVMK-PVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVN---VGSLAGKNAfkGGAAYNASKFGLL 154
                        170       180
                 ....*....|....*....|....*....
gi 517341756 170 TYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:cd08929  155 GLSEAAMLDLREANIRVVNVMPGSVDTGF 183
PRK07069 PRK07069
short chain dehydrogenase; Validated
14-252 1.87e-23

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 95.16  E-value: 1.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  14 VTGAGRGIGLEVARQFLDCGAKVIVH--TGRKPGRDLPDFLLTAESERRALLLHADFSAVG---GAAQFAEDALAffdRV 88
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTdiNDAAGLDAFAAEINAAHGEGVAFAAVQDVTDEAqwqALLAQAADAMG---GL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKAFV 168
Cdd:PRK07069  81 SVLVNNAG-VGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKA-EPDYTAYNASKAAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 169 ATYSKALARELAPDGIRVNC--VSPGTIET----EFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYI 242
Cdd:PRK07069 159 ASLTKSIALDCARRGLDVRCnsIHPTFIRTgivdPIFQRLGEEEATRKLARGVPLGRLGEPDDVAHAVLYLASDE-SRFV 237
                        250
                 ....*....|
gi 517341756 243 TGQVIEINGG 252
Cdd:PRK07069 238 TGAELVIDGG 247
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
10-252 2.33e-23

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 95.08  E-value: 2.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTG-RKPGRDlpDFLltaeSERRALLLhaDFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAGCGpNSPRRV--KWL----EDQKALGF--DFIASEGNVGDWDSTKAAFDKV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 -------DVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtvsISALTG--GSPGSS 159
Cdd:PRK12938  76 kaevgeiDVLVNNAG-ITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIIN---ISSVNGqkGQFGQT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFhERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlS 239
Cdd:PRK12938 152 NYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDM-VKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEE-S 229
                        250
                 ....*....|...
gi 517341756 240 GYITGQVIEINGG 252
Cdd:PRK12938 230 GFSTGADFSLNGG 242
PRK12744 PRK12744
SDR family oxidoreductase;
8-252 3.01e-23

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 94.81  E-value: 3.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVI-VHTGRKPGRDLPDFLLTA--ESERRALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK12744   7 KGKVVLIAGGAKNLGGLIARDLAAQGAKAVaIHYNSAASKADAEETVAAvkAAGAKAVAFQADLTTAAAVEKLFDDAKAA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLgRFPAATLTDAEYEAVVRLN-QTSVVALTRAllpALKAAEGAAIVnTVSISALTGGSPGSSIYSA 163
Cdd:PRK12744  87 FGRPDIAINTVGKVL-KKPIVEISEAEYDEMFAVNsKSAFFFIKEA---GRHLNDNGKIV-TLVTSLLGAFTPFYSAYAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPL-----QRLGTAEDCAPAYLFLAapSL 238
Cdd:PRK12744 162 SKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFFYPQEGAEAVAYHKTAAALspfskTGLTDIEDIVPFIRFLV--TD 239
                        250
                 ....*....|....
gi 517341756 239 SGYITGQVIEINGG 252
Cdd:PRK12744 240 GWWITGQTILINGG 253
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
9-197 3.69e-23

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 93.99  E-value: 3.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFldcgAKVIVHTGRKpGRDLPDFLLTAESER----RALLLHADFSAVGGAAQFAEDALAF 84
Cdd:PRK07666   7 GKNALITGAGRGIGRAVAIAL----AKEGVNVGLL-ARTEENLKAVAEEVEaygvKVVIATADVSDYEEVTAAIEQLKNE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTmlGRFPAAT-LTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtVSISALTGGSPGSSIYSA 163
Cdd:PRK07666  82 LGSIDILINNAGI--SKFGKFLeLDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIIN-ISSTAGQKGAAVTSAYSA 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:PRK07666 159 SKFGVLGLTESLMQEVRKHNIRVTALTPSTVATD 192
PRK09134 PRK09134
SDR family oxidoreductase;
10-253 6.96e-23

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 93.84  E-value: 6.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpGRDLPDFLLT--AESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVAVHYNR--SRDEAEALAAeiRALGRRAVALQADLADEAEVRALVARASAALGP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAgtmlGRFPAATLTDAEYEAVVRLNQTSVVA---LTRALLPALKAAEGAAIVNTVS--ISALTggsPGSSIYS 162
Cdd:PRK09134  88 ITLLVNNA----SLFEYDSAASFTRASWDRHMATNLRApfvLAQAFARALPADARGLVVNMIDqrVWNLN---PDFLSYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELAPDgIRVNCVSPG-TIETEfherYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLA-APSlsg 240
Cdd:PRK09134 161 LSKAALWTATRTLAQALAPR-IRVNAIGPGpTLPSG----RQSPEDFARQHAATPLGRGSTPEEIAAAVRYLLdAPS--- 232
                        250
                 ....*....|...
gi 517341756 241 yITGQVIEINGGQ 253
Cdd:PRK09134 233 -VTGQMIAVDGGQ 244
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
75-252 2.17e-22

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 92.25  E-value: 2.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  75 AQFAEDALAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSiSALTGG 154
Cdd:cd05361   60 EELVDAVLQAGGAIDVLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITS-AVPKKP 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 155 SPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYS----SREKLEQTRKSIPLQRLGTAEDCAPAY 230
Cdd:cd05361  139 LAYNSLYGPARAAAVALAESLAKELSRDNILVYAIGPNFFNSPTYFPTSdwenNPELRERVKRDVPLGRLGRPDEMGALV 218
                        170       180
                 ....*....|....*....|..
gi 517341756 231 LFLAAPSlSGYITGQVIEINGG 252
Cdd:cd05361  219 AFLASRR-ADPITGQFFAFAGG 239
PRK06180 PRK06180
short chain dehydrogenase; Provisional
8-198 2.59e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 92.67  E-value: 2.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgRDLPDFLLTAESERRALLLH-ADFSAVGGAAQFAEDAlafFD 86
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAGHRVVG-TVRSE-AARADFEALHPDRALARLLDvTDFDAIDAVVADAEAT---FG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGtmLGRFpaATLTDAEYEAVVRLNQTSV---VALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSA 163
Cdd:PRK06180  78 PIDVLVNNAG--YGHE--GAIEESPLAEMRRQFEVNVfgaVAMTKAVLPGMRARRRGHIVNITSMGGLIT-MPGIGYYCG 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK06180 153 SKFALEGISESLAKEVAPFGIHVTAVEPGSFRTDW 187
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
13-252 2.82e-22

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: 92.14  E-value: 2.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVLV 92
Cdd:cd05337    5 IVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCLV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  93 NNAG-TMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGA------AIVNTVSISALTGgSPGSSIYSASK 165
Cdd:cd05337   85 NNAGiAVRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRfdgphrSIIFVTSINAYLV-SPNRGEYCISK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEF----HERYSsrEKLEQTRksIPLQRLGTAEDCAPAYLFLAAPSLSgY 241
Cdd:cd05337  164 AGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMtapvKEKYD--ELIAAGL--VPIRRWGQPEDIAKAVRTLASGLLP-Y 238
                        250
                 ....*....|.
gi 517341756 242 ITGQVIEINGG 252
Cdd:cd05337  239 STGQPINIDGG 249
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
10-196 3.37e-22

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: 91.36  E-value: 3.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGrdLPDFLLTAESERraLLLHA----DFSAVGGA-AQFAEDALAf 84
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDG--LAALAAELGAEN--VVAGAldvtDRAAWAAAlADFAAATGG- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 fdRVDVLVNNAGtmLGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSA 163
Cdd:cd08931   76 --RLDALFNNAG--VGRGgPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYG-QPDLAVYSA 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:cd08931  151 TKFAVRGLTEALDVEWARHGIRVADVWPWFVDT 183
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
8-252 4.02e-22

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: 91.58  E-value: 4.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKV-IVHTGRKPGrdlpdfLLTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVvILDLPNSPG------ETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGT-----MLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAA------IVNTVSISALTGgS 155
Cdd:cd05371   75 RLDIVVNCAGIavaakTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPDQggergvIINTASVAAFEG-Q 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAA 235
Cdd:cd05371  154 IGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKVRDFLAKQVPFPSRLGDPAEYAHLVQHIIE 233
                        250
                 ....*....|....*..
gi 517341756 236 PSlsgYITGQVIEINGG 252
Cdd:cd05371  234 NP---YLNGEVIRLDGA 247
PRK06179 PRK06179
short chain dehydrogenase; Provisional
8-198 7.49e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 91.12  E-value: 7.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKViVHTGRKPGRdlpdflltAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK06179   3 NSKVALVTGASSGIGRATAEKLARAGYRV-FGTSRNPAR--------AAPIPGVELLELDVTDDASVQAAVDEVIARAGR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAG-TMLGrfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKA 166
Cdd:PRK06179  74 IDVLVNNAGvGLAG--AAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLP-APYMALYAASKH 150
                        170       180       190
                 ....*....|....*....|....*....|..
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK06179 151 AVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
12-234 7.70e-22

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 90.97  E-value: 7.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR------DLPDFLLTAESERRalllhaDFSAVggaAQFAEDALAFF 85
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIA-TGRRQERlqelkdELGDNLYIAQLDVR------NRAAI---EEMLASLPAEW 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtvsISALTGGSP--GSSIYSA 163
Cdd:PRK10538  73 RNIDVLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIIN---IGSTAGSWPyaGGNVYGA 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIE-TEF-HERYS-SREKLEQT-RKSIPLqrlgTAEDCAPAYLFLA 234
Cdd:PRK10538 150 TKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGgTEFsNVRFKgDDGKAEKTyQNTVAL----TPEDVSEAVWWVA 220
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
12-217 7.78e-22

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: 90.74  E-value: 7.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpgrdlPDFL--LTAESER----RALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05356    4 AVVTGATDGIGKAYAEELAKRGFNVILISRT------QEKLdaVAKEIEEkygvETKTIAADFSAGDDIYERIEKELEGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DrVDVLVNNAG---TMLGRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYS 162
Cdd:cd05356   78 D-IGILVNNVGishSIPEYF--LETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIP-TPLLATYS 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIETefheryssreKLEQTRKSIPL 217
Cdd:cd05356  154 ASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVAT----------KMSKIRKSSLF 198
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
12-252 1.16e-21

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 90.53  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDlpDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:cd08943    4 ALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAE--KVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAE-GAAIVNTVSISALTGGsPGSSIYSASKAFVAT 170
Cdd:cd08943   82 VSNAGIATSS-PIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPG-PNAAAYSAAKAAEAH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 171 YSKALARELAPDGIRVNCVSPGTI-------ETEFHERYSSREKL--EQTRKSIPLQRLGTAEDCAPAYLFLAAPsLSGY 241
Cdd:cd08943  160 LARCLALEGGEDGIRVNTVNPDAVfrgskiwEGVWRAARAKAYGLleEEYRTRNLLKREVLPEDVAEAVVAMASE-DFGK 238
                        250
                 ....*....|.
gi 517341756 242 ITGQVIEINGG 252
Cdd:cd08943  239 TTGAIVTVDGG 249
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
3-248 2.26e-21

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 89.55  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   3 HPRLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHtGR--KPGRDLPDFLLTAESERRAL----LLHADFSAVggaAQ 76
Cdd:PRK08945   6 KPDLLKDRIILVTGAGDGIGREAALTYARHGATVILL-GRteEKLEAVYDEIEAAGGPQPAIipldLLTATPQNY---QQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  77 FAEDALAFFDRVDVLVNNAGtMLG-RFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSiSALTGGS 155
Cdd:PRK08945  82 LADTIEEQFGRLDGVLHNAG-LLGeLGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSS-SVGRQGR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFheryssREKLEQTRKSiplQRLGTAEDCAPAYLFLAA 235
Cdd:PRK08945 160 ANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM------RASAFPGEDP---QKLKTPEDIMPLYLYLMG 230
                        250
                 ....*....|...
gi 517341756 236 PSLSGyITGQVIE 248
Cdd:PRK08945 231 DDSRR-KNGQSFD 242
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
6-252 2.75e-21

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 89.31  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAG--RGIGLEVARQFLDCGAKVIV-HTGRKPGRDLPDFlltAESERRALLLHADFSAVGGAAQFAEDAL 82
Cdd:COG0623    2 LLKGKRGLITGVAndRSIAWGIAKALHEEGAELAFtYQGEALKKRVEPL---AEELGSALVLPCDVTDDEQIDALFDEIK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVN-----NAGTMLGRFpaatlTDAEYEAVVRLNQTSV---VALTRALLPALKaaEGAAIVntvsisALTgg 154
Cdd:COG0623   79 EKWGKLDFLVHsiafaPKEELGGRF-----LDTSREGFLLAMDISAyslVALAKAAEPLMN--EGGSIV------TLT-- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 155 spgssIYSASKAF-------VAtysKA--------LARELAPDGIRVNCVSPGTIETefheRYSS-----REKLEQTRKS 214
Cdd:COG0623  144 -----YLGAERVVpnynvmgVA---KAaleasvryLAADLGPKGIRVNAISAGPIKT----LAASgipgfDKLLDYAEER 211
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 517341756 215 IPLQRLGTAEDCAPAYLFLAAPsLSGYITGQVIEINGG 252
Cdd:COG0623  212 APLGRNVTIEEVGNAAAFLLSD-LASGITGEIIYVDGG 248
PRK07454 PRK07454
SDR family oxidoreductase;
10-197 3.36e-21

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 88.86  E-value: 3.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR--DLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGWDLAL-VARSQDAleALAAELRSTGVK--AAAYSIDLSNPEAIAPGIAELLEQFGC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAlTGGSPGSSIYSASKAF 167
Cdd:PRK07454  84 PDVLINNAG-MAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAA-RNAFPQWGAYCVSKAA 161
                        170       180       190
                 ....*....|....*....|....*....|
gi 517341756 168 VATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:PRK07454 162 LAAFTKCLAEEERSHGIRVCTITLGAVNTP 191
PRK05875 PRK05875
short chain dehydrogenase; Provisional
7-255 6.73e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 88.71  E-value: 6.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdLPDFL--LTAESERRALLLH-ADFSAVGGAAQFAEDALA 83
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMI-VGRNPDK-LAAAAeeIEALKGAGAVRYEpADVTDEDQVARAVDAATA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISAlTGGSPGSSIYSA 163
Cdd:PRK05875  83 WHGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAA-SNTHRWFGAYGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY-SSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYI 242
Cdd:PRK05875 162 TKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPItESPELSADYRACTPLPRVGEVEDVANLAMFLLSDA-ASWI 240
                        250
                 ....*....|...
gi 517341756 243 TGQVIEINGGQLI 255
Cdd:PRK05875 241 TGQVINVDGGHML 253
PRK12746 PRK12746
SDR family oxidoreductase;
13-252 9.68e-21

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 88.17  E-value: 9.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFF------D 86
Cdd:PRK12746  10 LVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELqirvgtS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAaEGAAIvnTVSISALTGGSPGSSIYSASKA 166
Cdd:PRK12746  90 EIDILVNNAG-IGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRA-EGRVI--NISSAEVRLGFTGSIAYGLSKG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQ-TRKSIPLQRLGTAEDCAPAYLFLAApSLSGYITGQ 245
Cdd:PRK12746 166 ALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNfATNSSVFGRIGQVEDIADAVAFLAS-SDSRWVTGQ 244

                 ....*..
gi 517341756 246 VIEINGG 252
Cdd:PRK12746 245 IIDVSGG 251
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
12-205 1.04e-20

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 87.44  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDlpdfLLTAESER---RALLLHAD---FSAVGGAAQFAEDAlafF 85
Cdd:cd05360    3 VVITGASSGIGRATALAFAERGAKVVLAARSAEALH----ELAREVRElggEAIAVVADvadAAQVERAADTAVER---F 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGT-MLGRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYSAS 164
Cdd:cd05360   76 GRIDTWVNNAGVaVFGRF--EDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYR-SAPLQAAYSAS 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 517341756 165 KAFVATYSKALARELAPDG--IRVNCVSPGTIETEFHERYSSR 205
Cdd:cd05360  153 KHAVRGFTESLRAELAHDGapISVTLVQPTAMNTPFFGHARSY 195
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
8-255 1.20e-20

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 87.89  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAEserralllhaDFSAVGGA-----AQFAEDAL 82
Cdd:PRK08085   8 AGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQE----------GIKAHAAPfnvthKQEVEAAI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDR----VDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSI-SALtgGSPG 157
Cdd:PRK08085  78 EHIEKdigpIDVLINNAG-IQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMqSEL--GRDT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 158 SSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKL-EQTRKSIPLQRLGTAEDCAPAYLFLAAP 236
Cdd:PRK08085 155 ITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAFtAWLCKRTPAARWGDPQELIGAAVFLSSK 234
                        250
                 ....*....|....*....
gi 517341756 237 SlSGYITGQVIEINGGQLI 255
Cdd:PRK08085 235 A-SDFVNGHLLFVDGGMLV 252
PRK08263 PRK08263
short chain dehydrogenase; Provisional
14-213 2.94e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 87.02  E-value: 2.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  14 VTGAGRGIGLEVARQFLDCGAKViVHTGRKPGRdLPDflLTAESERRALLLH-------ADFSAVggaaqfaEDALAFFD 86
Cdd:PRK08263   8 ITGASRGFGRAWTEAALERGDRV-VATARDTAT-LAD--LAEKYGDRLLPLAldvtdraAVFAAV-------ETAVEHFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTML-GrfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSASK 165
Cdd:PRK08263  77 RLDIVVNNAGYGLfG--MIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAF-PMSGIYHASK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFH----------ERYSS-REKLEQTRK 213
Cdd:PRK08263 154 WALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWAgtsakratplDAYDTlREELAEQWS 212
PRK06914 PRK06914
SDR family oxidoreductase;
13-196 3.41e-20

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 87.00  E-value: 3.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPdflLTAESERRALLLH--------ADFSAVggaaQFAEDALAF 84
Cdd:PRK06914   7 IVTGASSGFGLLTTLELAKKGYLVIA-TMRNPEKQEN---LLSQATQLNLQQNikvqqldvTDQNSI----HNFQLVLKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRFpAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSAS 164
Cdd:PRK06914  79 IGRIDLLVNNAGYANGGF-VEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVG-FPGLSPYVSS 156
                        170       180       190
                 ....*....|....*....|....*....|..
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK06914 157 KYALEGFSESLRLELKPFGIDVALIEPGSYNT 188
PRK05872 PRK05872
short chain dehydrogenase; Provisional
1-197 3.69e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 87.33  E-value: 3.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   1 MFHPRLfENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdLPDFLLTAESERRALLLHADFSAVGGAAQFAED 80
Cdd:PRK05872   2 PPMTSL-AGKVVVVTGAARGIGAELARRLHARGAKLAL-VDLEEAE-LAALAAELGGDDRVLTVVADVTDLAAMQAAAEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVntVSISALTGGSPGSSI 160
Cdd:PRK05872  79 AVERFGGIDVVVANAGIASGG-SVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQ--VSSLAAFAAAPGMAA 155
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:PRK05872 156 YCASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTD 192
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
10-252 5.07e-20

SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are putative oxidoreductases belonging to the larger SDR family. All members occur in genomes that encode a cassette for the biosynthesis of mycofactocin, a proposed electron carrier of a novel redox pool. Characterized members of this family are described as NDMA-dependent, meaning that a blue aniline dye serving as an artificial electron acceptor is required for members of this family to cycle in vitro, since the bound NAD residue is not exchangeable. This family resembles TIGR03971 most closely in the N-terminal region, consistent with the published hypothesis of NAD interaction with mycofactocin. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 86.22  E-value: 5.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLH--------ADFSAVGGAAQFAEDA 81
Cdd:TIGR04504   2 RVALVTGAARGIGAATVRRLAADGWRVVAVDLCADDPAVGYPLATRAELDAVAAACpdqvlpviADVRDPAALAAAVALA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   82 LAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSI--SALTGGSPGSS 159
Cdd:TIGR04504  82 VERWGRLDAAVAAAGVIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARPDPRGGRFVAVasAAATRGLPHLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER----YSSREkLEQTRKSIPLQRLGTAEDCAPAYLFLAA 235
Cdd:TIGR04504 162 AYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLAAtarlYGLTD-VEEFAGHQLLGRLLEPEEVAAAVAWLCS 240
                         250
                  ....*....|....*..
gi 517341756  236 PSlSGYITGQVIEINGG 252
Cdd:TIGR04504 241 PA-SSAVTGSVVHADGG 256
PRK12747 PRK12747
short chain dehydrogenase; Provisional
6-252 1.03e-19

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 85.13  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAaqfaEDALAFF 85
Cdd:PRK12747   1 MLKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGV----EALYSSL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 D----------RVDVLVNNAGTMLGRFPAATlTDAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNtVSISALTGGS 155
Cdd:PRK12747  77 DnelqnrtgstKFDILINNAGIGPGAFIEET-TEQFFDRMVSVNAKAPFFIIQQALSRLR--DNSRIIN-ISSAATRISL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSI-PLQRLGTAEDCAPAYLFLA 234
Cdd:PRK12747 153 PDFIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTIsAFNRLGEVEDIADTAAFLA 232
                        250
                 ....*....|....*...
gi 517341756 235 APSlSGYITGQVIEINGG 252
Cdd:PRK12747 233 SPD-SRWVTGQLIDVSGG 249
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
12-220 1.13e-19

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: 85.03  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTgrkPGRDLPDFLLTAESERRALLLH---ADFSAVGGAAQFAEDALAFFDRV 88
Cdd:cd05367    2 IILTGASRGIGRALAEELLKRGSPSVVVL---LARSEEPLQELKEELRPGLRVTtvkADLSDAAGVEQLLEAIRKLDGER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGtMLGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGA-AIVNTVSISALTgGSPGSSIYSASKA 166
Cdd:cd05367   79 DLLINNAG-SLGPVsKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKkTVVNVSSGAAVN-PFKGWGLYCSSKA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517341756 167 FVATYSKALARELapDGIRVNCVSPGTIETEFHeryssREKLEQTRKSIPLQRL 220
Cdd:cd05367  157 ARDMFFRVLAAEE--PDVRVLSYAPGVVDTDMQ-----REIRETSADPETRSRF 203
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-252 1.20e-19

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 85.22  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   3 HPRLfENRNVVVTGAGR--GIGLEVARQFLDCGAKVIVHTGRKPGRDLP-------DFLLTAESERRALLLHA---DFSA 70
Cdd:PRK12859   1 MNQL-KNKVAVVTGVSRldGIGAAICKELAEAGADIFFTYWTAYDKEMPwgvdqdeQIQLQEELLKNGVKVSSmelDLTQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  71 VGGAAQFAEDALAFFDRVDVLVNNAgTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISA 150
Cdd:PRK12859  80 NDAPKELLNKVTEQLGYPHILVNNA-AYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTSGQF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 151 LtGGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEfherYSSREKLEQTRKSIPLQRLGTAEDCAPAY 230
Cdd:PRK12859 159 Q-GPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTG----WMTEEIKQGLLPMFPFGRIGEPKDAARLI 233
                        250       260
                 ....*....|....*....|..
gi 517341756 231 LFLAAPSlSGYITGQVIEINGG 252
Cdd:PRK12859 234 KFLASEE-AEWITGQIIHSEGG 254
PRK05693 PRK05693
SDR family oxidoreductase;
11-198 2.16e-19

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 84.84  E-value: 2.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  11 NVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgrdlpdflltaesERRALLLHADFSAV-------GGAAQFAEDALA 83
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWA-TARKA-------------EDVEALAAAGFTAVqldvndgAALARLAEELEA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAG--TMlgrfpaATLTDAEYEAVVRLNQT---SVVALTRALLPALKAAEGAaIVNTVSISALTGgSPGS 158
Cdd:PRK05693  69 EHGGLDVLINNAGygAM------GPLLDGGVEAMRRQFETnvfAVVGVTRALFPLLRRSRGL-VVNIGSVSGVLV-TPFA 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 517341756 159 SIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK05693 141 GAYCASKAAVHALSDALRLELAPFGVQVMEVQPGAIASQF 180
PRK05717 PRK05717
SDR family oxidoreductase;
10-252 6.31e-19

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 83.01  E-value: 6.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIV-HTGRKPGRDLPDFLltaesERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLaDLDRERGSKVAKAL-----GENAWFIAMDVADEAQVAAGVAEVLGQFGRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMLGR-FPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGaAIVNTVSISAlTGGSPGSSIYSASKAF 167
Cdd:PRK05717  86 DALVCNAAIADPHnTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNG-AIVNLASTRA-RQSEPDTEAYAASKGG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 168 VATYSKALARELAPDgIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYITGQVI 247
Cdd:PRK05717 164 LLALTHALAISLGPE-IRVNAVSPGWIDARDPSQRRAEPLSEADHAQHPAGRVGTVEDVAAMVAWLLSRQ-AGFVTGQEF 241

                 ....*
gi 517341756 248 EINGG 252
Cdd:PRK05717 242 VVDGG 246
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
8-254 7.88e-19

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 83.19  E-value: 7.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpgrdlPDFLLTAESERRALLLHA-----DFSAVGGAAQFAEDAL 82
Cdd:PRK07097   9 KGKIALITGASYGIGFAIAKAYAKAGATIVFNDIN------QELVDKGLAAYRELGIEAhgyvcDVTDEDGVQAMVSQIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSI-SALtgGSPGSSIY 161
Cdd:PRK07097  83 KEVGVIDILVNNAG-IIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMmSEL--GRETVSAY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 162 SASKAFVATYSKALARELAPDGIRVNCVSPGTIETE----FHERYS--SREKLEQ---TRKsiPLQRLGTAEDCAPAYLF 232
Cdd:PRK07097 160 AAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPqtapLRELQAdgSRHPFDQfiiAKT--PAARWGDPEDLAGPAVF 237
                        250       260
                 ....*....|....*....|..
gi 517341756 233 LAAPSlSGYITGQVIEINGGQL 254
Cdd:PRK07097 238 LASDA-SNFVNGHILYVDGGIL 258
PLN02253 PLN02253
xanthoxin dehydrogenase
4-252 1.15e-18

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 82.95  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   4 PRLfENRNVVVTGAGRGIGLEVARQFLDCGAKV-IVHTGRKPGRDLPDFLltaESERRALLLHADFSAVGGAAQFAEDAL 82
Cdd:PLN02253  14 QRL-LGKVALVTGGATGIGESIVRLFHKHGAKVcIVDLQDDLGQNVCDSL---GGEPNVCFFHCDVTVEDDVSRAVDFTV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVNNAGtmlgrFPAATLTD------AEYEAVVRLNQTSVVA----LTRALLPALKAAegaaIVNTVSISALT 152
Cdd:PLN02253  90 DKFGTLDIMVNNAG-----LTGPPCPDirnvelSEFEKVFDVNVKGVFLgmkhAARIMIPLKKGS----IVSLCSVASAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 153 GGSpGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQ---------TRKSIPLQRLG-T 222
Cdd:PLN02253 161 GGL-GPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPEDERTEdalagfrafAGKNANLKGVElT 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 517341756 223 AEDCAPAYLFLAAPSlSGYITGQVIEINGG 252
Cdd:PLN02253 240 VDDVANAVLFLASDE-ARYISGLNLMIDGG 268
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
12-198 1.19e-18

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: 82.29  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpgrDLPDFLLTAESE------RRALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVIL-------DINEKGAEETANnvrkagGKVHYYKCDVSKREEVYEAAKKIKKEV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLGRFPAAtLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYSASK 165
Cdd:cd05339   75 GDVTILINNAGVVSGKKLLE-LPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLI-SPAGLADYCASK 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 517341756 166 AFVATYSKALARELAP---DGIRVNCVSPGTIETEF 198
Cdd:cd05339  153 AAAVGFHESLRLELKAygkPGIKTTLVCPYFINTGM 188
PRK06482 PRK06482
SDR family oxidoreductase;
14-198 1.26e-18

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 82.86  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  14 VTGAGRGIGLEVARQFLDCGAKViVHTGRKPG--RDLPDflLTAESERRALLLHADFSAVGGAAQfaeDALAFFDRVDVL 91
Cdd:PRK06482   7 ITGASSGFGRGMTERLLARGDRV-AATVRRPDalDDLKA--RYGDRLWVLQLDVTDSAAVRAVVD---RAFAALGRIDVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGtmLGRFPAA-TLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtVSISALTGGSPGSSIYSASKAFVAT 170
Cdd:PRK06482  81 VSNAG--YGLFGAAeELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQ-VSSEGGQIAYPGFSLYHATKWGIEG 157
                        170       180
                 ....*....|....*....|....*...
gi 517341756 171 YSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK06482 158 FVEAVAQEVAPFGIEFTIVEPGPARTNF 185
PRK05855 PRK05855
SDR family oxidoreductase;
4-196 1.57e-18

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 84.26  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   4 PRLFENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDLPDFLLTAEsERRALLLHA-----DFSAVGGAAQFA 78
Cdd:PRK05855 310 RGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVA-----SDIDEAAAERTAE-LIRAAGAVAhayrvDVSDADAMEAFA 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  79 EDALAFFDRVDVLVNNAGT-MLGRFPAAtlTDAEYEAVVRLNQTSVVALTRALLPALKA-AEGAAIVNTVSISALTgGSP 156
Cdd:PRK05855 384 EWVRAEHGVPDIVVNNAGIgMAGGFLDT--SAEDWDRVLDVNLWGVIHGCRLFGRQMVErGTGGHIVNVASAAAYA-PSR 460
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 517341756 157 GSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK05855 461 SLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDT 500
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
13-252 1.68e-18

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 82.25  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERrALLLHADFSAVGGAAQFAEDALAFFDRVDVLV 92
Cdd:PRK13394  11 VVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGK-AIGVAMDVTNEDAVNAGIDKVAERFGSVDILV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  93 NNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPAL-KAAEGAAIVNTVSISALTGgSPGSSIYSASKAFVATY 171
Cdd:PRK13394  90 SNAGIQIVN-PIENYSFADWKKMQAIHVDGAFLTTKAALKHMyKDDRGGVVIYMGSVHSHEA-SPLKSAYVTAKHGLLGL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 172 SKALARELAPDGIRVNCVSPGTIETEFHER----YSSREKL--EQTRKSIPLQR-----LGTAEDCAPAYLFLAAPsLSG 240
Cdd:PRK13394 168 ARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqipeQAKELGIseEEVVKKVMLGKtvdgvFTTVEDVAQTVLFLSSF-PSA 246
                        250
                 ....*....|..
gi 517341756 241 YITGQVIEINGG 252
Cdd:PRK13394 247 ALTGQSFVVSHG 258
PRK07041 PRK07041
SDR family oxidoreductase;
13-255 1.99e-18

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 81.24  E-value: 1.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdlpdflltAESERRALLLHADFSAVGGAAQFAEDALAFFDRVD--- 89
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTI-ASRSRDR--------LAAAARALGGGAPVRTAALDITDEAAVDAFFAEAGpfd 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 -VLVNNAGTMLGRFPAATLTDAEyeavvrlnqtsvVALTRALLPALKAAEGAAIVNTVSISALTG-----GSPGSSIYSA 163
Cdd:PRK07041  72 hVVITAADTPGGPVRALPLAAAQ------------AAMDSKFWGAYRVARAARIAPGGSLTFVSGfaavrPSASGVLQGA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPdgIRVNCVSPGTIETEFHERYSSREK---LEQTRKSIPLQRLGTAEDCAPAYLFLAApslSG 240
Cdd:PRK07041 140 INAALEALARGLALELAP--VRVNTVSPGLVDTPLWSKLAGDAReamFAAAAERLPARRVGQPEDVANAILFLAA---NG 214
                        250
                 ....*....|....*
gi 517341756 241 YITGQVIEINGGQLI 255
Cdd:PRK07041 215 FTTGSTVLVDGGHAI 229
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
12-240 2.81e-18

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 79.87  E-value: 2.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGA-KVIVHtgrkpgrdlpdflltaeserralllhadfsavggaaqfaedalaffDRVDV 90
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSpKVLVV----------------------------------------------SRRDV 34
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  91 LVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKAFVAT 170
Cdd:cd02266   35 VVHNAAILDDG-RLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFG-APGLGGYAASKAALDG 112
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517341756 171 YSKALARELAPDGIRVNCVSPGTIETEFHERY--SSREKLEQTRksiPLQRLGTAEDCAPAYLFLAAPSLSG 240
Cdd:cd02266  113 LAQQWASEGWGNGLPATAVACGTWAGSGMAKGpvAPEEILGNRR---HGVRTMPPEEVARALLNALDRPKAG 181
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-252 3.32e-18

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 80.96  E-value: 3.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTgRKPGRdLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINS-RNENK-LKRMKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVnnagTMLGRFPAATLTD-AEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNTVSISALTGGSPGSSIYSASK 165
Cdd:PRK05786  81 AIDGLV----VTVGGYVEDTVEEfSGLEEMLTNHIKIPLYAVNASLRFLK--EGSSIVLVSSMSGIYKASPDQLSYAVAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFheryssreklEQTRKSIPLQRLGTA----EDCAPAYLFLAAPSlSGY 241
Cdd:PRK05786 155 AGLAKAVEILASELLGRGIRVNGIAPTTISGDF----------EPERNWKKLRKLGDDmappEDFAKVIIWLLTDE-ADW 223
                        250
                 ....*....|.
gi 517341756 242 ITGQVIEINGG 252
Cdd:PRK05786 224 VDGVVIPVDGG 234
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
12-201 4.56e-18

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


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 80.45  E-value: 4.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRK--PGRDLPDFLLT-AESERRALLLHADFSAVggAAQFAEdALAFFDRV 88
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVAL-AARRtdRLDELKAELLNpNPSVEVEILDVTDEERN--QLVIAE-LEAELGGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKAFV 168
Cdd:cd05350   77 DLVIINAGVGKGT-SLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRG-LPGAAAYSASKAAL 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 517341756 169 ATYSKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:cd05350  155 SSLAESLRYDVKKRGIRVTVINPGFIDTPLTAN 187
PRK07201 PRK07201
SDR family oxidoreductase;
8-184 5.98e-18

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 82.69  E-value: 5.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKpGRDLPDflLTAESERRALLLHA---DFSAVGGAAQFAEDALAF 84
Cdd:PRK07201 370 VGKVVLITGASSGIGRATAIKVAEAGATVFL-VARN-GEALDE--LVAEIRAKGGTAHAytcDLTDSAAVDHTVKDILAE 445
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLGRFPAATlTDA--EYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYS 162
Cdd:PRK07201 446 HGHVDYLVNNAGRSIRRSVENS-TDRfhDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNA-PRFSAYV 523
                        170       180
                 ....*....|....*....|..
gi 517341756 163 ASKAFVATYSKALARELAPDGI 184
Cdd:PRK07201 524 ASKAALDAFSDVAASETLSDGI 545
PRK08339 PRK08339
short chain dehydrogenase; Provisional
15-254 8.33e-18

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 80.28  E-value: 8.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  15 TGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVLVNN 94
Cdd:PRK08339  14 TASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADLTKREDLERTVKELKNIGEPDIFFFST 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  95 AGTMLGRFPAATLTDaeYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSIsALTGGSPGSSIYSASKAFVATYSKA 174
Cdd:PRK08339  94 GGPKPGYFMEMSMED--WEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSV-AIKEPIPNIALSNVVRISMAGLVRT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 175 LARELAPDGIRVNCVSPGTIETEF----------HERYSSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAApSLSGYITG 244
Cdd:PRK08339 171 LAKELGPKGITVNGIMPGIIRTDRviqlaqdrakREGKSVEEALQEYAKPIPLGRLGEPEEIGYLVAFLAS-DLGSYING 249
                        250
                 ....*....|
gi 517341756 245 QVIEINGGQL 254
Cdd:PRK08339 250 AMIPVDGGRL 259
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
10-245 1.72e-17

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 79.43  E-value: 1.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTgrkpgRDLPDFLLTAESERRALL------LHADFSAVGGAAQFAEDALA 83
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMAC-----RDMAKCEEAAAEIRRDTLnhevivRHLDLASLKSIRAFAAEFLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAGTMlgRFPAATLTDAeYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSP------- 156
Cdd:cd09807   77 EEDRLDVLINNAGVM--RCPYSKTEDG-FEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINfddlnse 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 157 ----GSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRL-GTAEDCAPAYL 231
Cdd:cd09807  154 ksynTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTGIHHLFLSTLLNPLFWPFvKTPREGAQTSI 233
                        250
                 ....*....|....*
gi 517341756 232 FLA-APSLSGyITGQ 245
Cdd:cd09807  234 YLAlAEELEG-VSGK 247
PRK12742 PRK12742
SDR family oxidoreductase;
7-252 2.11e-17

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 78.65  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVI-VHTGRKPGRDLpdflLTAESERRALLLH-ADFSAVggaaqfaEDALAF 84
Cdd:PRK12742   4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVRfTYAGSKDAAER----LAQETGATAVQTDsADRDAV-------IDVVRK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMLgrFPAATLTDAEyeAVVRLNQTSVVALTRALLPAL-KAAEGAAIVNTVSISALTGGSPGSSIYSA 163
Cdd:PRK12742  73 SGALDILVVNAGIAV--FGDALELDAD--DIDRLFKINIHAPYHASVEAArQMPEGGRIIIIGSVNGDRMPVAGMAAYAA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHErySSREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYIT 243
Cdd:PRK12742 149 SKSALQGMARGLARDFGPRGITINVVQPGPIDTDANP--ANGPMKDMMHSFMAIKRHGRPEEVAGMVAWLAGPE-ASFVT 225

                 ....*....
gi 517341756 244 GQVIEINGG 252
Cdd:PRK12742 226 GAMHTIDGA 234
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
13-252 2.42e-17

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 79.20  E-value: 2.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPG--RDLPDfLLTAESERRALLLHADFSAVGGAAQFAED----ALAFFD 86
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAaaSTLAA-ELNARRPNSAVTCQADLSNSATLFSRCEAiidaCFRAFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   87 RVDVLVNNAGTMlgrFPAATLTDAEYE----------AVVRLNQTSVVA---LTRALLPALKAAEGAAIVNTVSISALTG 153
Cdd:TIGR02685  84 RCDVLVNNASAF---YPTPLLRGDAGEgvgdkkslevQVAELFGSNAIApyfLIKAFAQRQAGTRAEQRSTNLSIVNLCD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  154 GS-----PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLeqtRKSIPL-QRLGTAEDCA 227
Cdd:TIGR02685 161 AMtdqplLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPDAMPFEVQEDY---RRKVPLgQREASAEQIA 237
                         250       260
                  ....*....|....*....|....*
gi 517341756  228 PAYLFLAAPSlSGYITGQVIEINGG 252
Cdd:TIGR02685 238 DVVIFLVSPK-AKYITGTCIKVDGG 261
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
8-253 4.60e-17

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 78.15  E-value: 4.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVH--TGRKPGRdLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFF 85
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVAdiNSEKAAN-VAQEINAEYGEGMAYGFGADATSEQSVLALSRGVDEIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRVDVLVNNAGTMLgrfpAATLTDAEYEAVVRLNQtsvVALTRALLPALKAA--------EGaaivNTVSISALTG--GS 155
Cdd:PRK12384  80 GRVDLLVYNAGIAK----AAFITDFQLGDFDRSLQ---VNLVGYFLCAREFSrlmirdgiQG----RIIQINSKSGkvGS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETE-----FHERYSSR-----EKLEQTR-KSIPLQRLGTAE 224
Cdd:PRK12384 149 KHNSGYSAAKFGGVGLTQSLALDLAEYGITVHSLMLGNLLKSpmfqsLLPQYAKKlgikpDEVEQYYiDKVPLKRGCDYQ 228
                        250       260
                 ....*....|....*....|....*....
gi 517341756 225 DCAPAYLFLAAPSLSgYITGQVIEINGGQ 253
Cdd:PRK12384 229 DVLNMLLFYASPKAS-YCTGQSINVTGGQ 256
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
9-236 7.78e-17

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: 77.17  E-value: 7.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgrdlpdfllTAESERRALLLHADFSAVGGAAQFA--------ED 80
Cdd:cd05343    6 GRVALVTGASVGIGAAVARALVQHGMKVVG---------------CARRVDKIEALAAECQSAGYPTLFPyqcdlsneEQ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDR-------VDVLVNNAGtmLGRfpAATLTDAEYEAVVRLNQTSVVALTRALLPALK--AAEGAAIVNTVSISAL 151
Cdd:cd05343   71 ILSMFSAirtqhqgVDVCINNAG--LAR--PEPLLSGKTEGWKEMFDVNVLALSICTREAYQsmKERNVDDGHIININSM 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 152 TGGS----PGSSIYSASKAFVATYSKALAREL--APDGIRVNCVSPGTIETEFHERYSSR--EKLEQTRKSIP-LQrlgt 222
Cdd:cd05343  147 SGHRvppvSVFHFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNdpEKAAATYESIPcLK---- 222
                        250
                 ....*....|....*
gi 517341756 223 AEDCAPAYLF-LAAP 236
Cdd:cd05343  223 PEDVANAVLYvLSTP 237
PRK07109 PRK07109
short chain dehydrogenase; Provisional
8-198 8.64e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 78.42  E-value: 8.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDlpdfLLTAESER---RALLLHAD---FSAVGGAAQFAEDA 81
Cdd:PRK07109   7 GRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLE----ALAAEIRAaggEALAVVADvadAEAVQAAADRAEEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAffdRVDVLVNNAG-TMLGRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtVSiSALT-GGSPGSS 159
Cdd:PRK07109  83 LG---PIDTWVNNAMvTVFGPF--EDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQ-VG-SALAyRSIPLQS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 517341756 160 IYSASKAFVATYSKALARELAPDG--IRVNCVSPGTIETEF 198
Cdd:PRK07109 156 AYCAAKHAIRGFTDSLRCELLHDGspVSVTMVQPPAVNTPQ 196
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
10-252 1.42e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 76.73  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHtgrkpGRDlPDFLLTAESERRALLLHADFSA----VGGAAQFAEDAL-AF 84
Cdd:PRK07523  11 RRALVTGSSQGIGYALAEGLAQAGAEVILN-----GRD-PAKLAAAAESLKGQGLSAHALAfdvtDHDAVRAAIDAFeAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGtMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSI-SALtgGSPGSSIYSA 163
Cdd:PRK07523  85 IGPIDILVNNAG-MQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVqSAL--ARPGIAPYTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQ-TRKSIPLQRLGTAEDCAPAYLFLAAPSlSGYI 242
Cdd:PRK07523 162 TKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVADPEFSAwLEKRTPAGRWGKVEELVGACVFLASDA-SSFV 240
                        250
                 ....*....|
gi 517341756 243 TGQVIEINGG 252
Cdd:PRK07523 241 NGHVLYVDGG 250
PRK07023 PRK07023
SDR family oxidoreductase;
13-227 1.54e-16

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 76.21  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVI-VHTGRKPGrdlpdflLTAESERRALLLHADFSAVGGAAQF-AEDALAFF----D 86
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAVLgVARSRHPS-------LAAAAGERLAEVELDLSDAAAAAAWlAGDLLAAFvdgaS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVdVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNtVSISALTGGSPGSSIYSASKA 166
Cdd:PRK07023  78 RV-LLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILH-ISSGAARNAYAGWSVYCATKA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517341756 167 FVATYSKALARElAPDGIRVNCVSPGTIETEFH--------ERYSSREKLEQTRKSiplQRLGTAEDCA 227
Cdd:PRK07023 156 ALDHHARAVALD-ANRALRIVSLAPGVVDTGMQatiratdeERFPMRERFRELKAS---GALSTPEDAA 220
PRK05866 PRK05866
SDR family oxidoreductase;
12-186 1.59e-16

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 77.09  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKpgrDLPDFLLTAESER--RALLLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:PRK05866  43 ILLTGASSGIGEAAAEQFARRGATVVAVARRE---DLLDAVADRITRAggDAMAVPCDLSDLDAVDALVADVEKRIGGVD 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMLGRfPAATLTDA--EYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYSASKAF 167
Cdd:PRK05866 120 ILINNAGRSIRR-PLAESLDRwhDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASPLFSVYNASKAA 198
                        170
                 ....*....|....*....
gi 517341756 168 VATYSKALARELAPDGIRV 186
Cdd:PRK05866 199 LSAVSRVIETEWGDRGVHS 217
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
25-252 1.60e-16

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 76.19  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  25 VARQFLDCGAKVIVHTGRKPGRDLPDFLltaeserralllHADfsaVGGAAQFAEDALAFFDRVDVLVNNAGtMLGRFPA 104
Cdd:PRK12428   1 TARLLRFLGARVIGVDRREPGMTLDGFI------------QAD---LGDPASIDAAVAALPGRIDALFNIAG-VPGTAPV 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 105 atltdaeyEAVVRLNQTSVVALTRALLPALkaAEGAAIVNTVSISA--------LTGGSPGSSIYSASKAFVATYSKALA 176
Cdd:PRK12428  65 --------ELVARVNFLGLRHLTEALLPRM--APGGAIVNVASLAGaewpqrleLHKALAATASFDEGAAWLAAHPVALA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 177 R-------------------ELAPDGIRVNCVSPGTIET----EFHERYSSrEKLEQTRKsiPLQRLGTAEDCAPAYLFL 233
Cdd:PRK12428 135 TgyqlskealilwtmrqaqpWFGARGIRVNCVAPGPVFTpilgDFRSMLGQ-ERVDSDAK--RMGRPATADEQAAVLVFL 211
                        250
                 ....*....|....*....
gi 517341756 234 AAPSlSGYITGQVIEINGG 252
Cdd:PRK12428 212 CSDA-ARWINGVNLPVDGG 229
PRK07024 PRK07024
SDR family oxidoreductase;
12-196 2.91e-16

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 75.74  E-value: 2.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKpGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGL-VARR-TDALQAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPDVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLGrfpaaTLT----DAE-YEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKA 166
Cdd:PRK07024  83 IANAGISVG-----TLTeereDLAvFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRG-LPGAGAYSASKA 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK07024 157 AAIKYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK09186 PRK09186
flagellin modification protein A; Provisional
8-252 8.05e-16

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 74.64  E-value: 8.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPG-RDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK09186   3 KGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEAlNELLESLGKEFKSKKLSLVELDITDQESLEEFLSKSAEKYG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAgtmlgrFP-----AATLTDAEYEAV---VRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALT------ 152
Cdd:PRK09186  83 KIDGAVNCA------YPrnkdyGKKFFDVSLDDFnenLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVapkfei 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 153 --GGSPGSSI-YSASKAFVATYSKALARELAPDGIRVNCVSPGTI----ETEFHERYssrekleqtRKSIPLQRLGTAED 225
Cdd:PRK09186 157 yeGTSMTSPVeYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIldnqPEAFLNAY---------KKCCNGKGMLDPDD 227
                        250       260
                 ....*....|....*....|....*..
gi 517341756 226 CAPAYLFLAApSLSGYITGQVIEINGG 252
Cdd:PRK09186 228 ICGTLVFLLS-DQSKYITGQNIIVDDG 253
PRK06949 PRK06949
SDR family oxidoreductase;
7-252 9.06e-16

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 74.41  E-value: 9.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIvhtgrkpgrdlpdflLTAESERRALLLHADFSAVGGAAQFAE------- 79
Cdd:PRK06949   7 LEGKVALVTGASSGLGARFAQVLAQAGAKVV---------------LASRRVERLKELRAEIEAEGGAAHVVSldvtdyq 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  80 ---DALAFFDR----VDVLVNNAG-TMLGRFpaATLTDAEYEAVVRLNQTSV--VA-------LTRALlPALKAAEGAAI 142
Cdd:PRK06949  72 sikAAVAHAETeagtIDILVNNSGvSTTQKL--VDVTPADFDFVFDTNTRGAffVAqevakrmIARAK-GAGNTKPGGRI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 143 VNTVSISALTGgSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSIPLQRLGT 222
Cdd:PRK06949 149 INIASVAGLRV-LPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQGQKLVSMLPRKRVGK 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 517341756 223 AEDCAPAYLFLAAPSlSGYITGQVIEINGG 252
Cdd:PRK06949 228 PEDLDGLLLLLAADE-SQFINGAIISADDG 256
PRK08416 PRK08416
enoyl-ACP reductase;
7-252 1.67e-15

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 73.65  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVI------VHTGRKPGRDLPD-FLLTAESERRALLLHADFSAVggAAQFAE 79
Cdd:PRK08416   6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIAftynsnVEEANKIAEDLEQkYGIKAKAYPLNILEPETYKEL--FKKIDE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  80 DalafFDRVDVLVNNAgTMLGRFPAATltdaeYEAVVRLN--------QTSVVALTRALLPALKAAE---GAAIVntvSI 148
Cdd:PRK08416  84 D----FDRVDFFISNA-IISGRAVVGG-----YTKFMRLKpkglnniyTATVNAFVVGAQEAAKRMEkvgGGSII---SL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 149 SAlTGG---SPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKL-EQTRKSIPLQRLGTAE 224
Cdd:PRK08416 151 SS-TGNlvyIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNYEEVkAKTEELSPLNRMGQPE 229
                        250       260
                 ....*....|....*....|....*...
gi 517341756 225 DCAPAYLFLAAPSLSgYITGQVIEINGG 252
Cdd:PRK08416 230 DLAGACLFLCSEKAS-WLTGQTIVVDGG 256
PRK08017 PRK08017
SDR family oxidoreductase;
10-223 2.05e-15

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 73.58  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTgRKPGrdlpDFLLTAESERRALLLHADFSAvgGAAQFAEDALAFFD-RV 88
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAAC-RKPD----DVARMNSLGFTGILLDLDDPE--SVERAADEVIALTDnRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGtmLGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASKAF 167
Cdd:PRK08017  76 YGLFNNAG--FGVYgPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLIS-TPGRGAYAASKYA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517341756 168 VATYSKALARELAPDGIRVNCVSPGTIETEFheryssREKLEQTRKSIPLQRLGTA 223
Cdd:PRK08017 153 LEAWSDALRMELRHSGIKVSLIEPGPIRTRF------TDNVNQTQSDKPVENPGIA 202
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
13-252 2.08e-15

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 73.38  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAG--RGIGLEVARQFLDCGAKVIVhTGRkpGRDLPDFL--LTAESERRALLLHADfsavggaAQFAEDALAFFDRV 88
Cdd:cd05372    5 LITGIAndRSIAWGIAKALHEAGAELAF-TYQ--PEALRKRVekLAERLGESALVLPCD-------VSNDEEIKELFAEV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 -------DVLVNNAG-----TMLGRFPAATLtdAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVnTVSISALTGGSP 156
Cdd:cd05372   75 kkdwgklDGLVHSIAfapkvQLKGPFLDTSR--KGFLKALDISAYSLVSLAKAALPIMN--PGGSIV-TLSYLGSERVVP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 157 GSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREK-LEQTRKSIPLQRLGTAEDCAPAYLFLAA 235
Cdd:cd05372  150 GYNVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLAASGITGFDKmLEYSEQRAPLGRNVTAEEVGNTAAFLLS 229
                        250
                 ....*....|....*..
gi 517341756 236 PSLSGyITGQVIEINGG 252
Cdd:cd05372  230 DLSSG-ITGEIIYVDGG 245
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
12-247 2.49e-15

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 72.23  E-value: 2.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDLPDFL--LTAESERRALllhadFSAVGgaaqfaedalaffdRVD 89
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVIT-----AGRSSGDYQvdITDEASIKAL-----FEKVG--------------HFD 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTmlGRF-PAATLTDAEYEAVVRLNQTSVVALTRALLPALkaAEGAAIVntvsisaLTGGS------PGSSIYS 162
Cdd:cd11731   57 AIVSTAGD--AEFaPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSIT-------LTSGIlaqrpiPGGAAAA 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELaPDGIRVNCVSPGTIETefherysSREKLEQtrkSIPLQRLGTAEDCAPAYLFlaapSLSGYI 242
Cdd:cd11731  126 TVNGALEGFVRAAAIEL-PRGIRINAVSPGVVEE-------SLEAYGD---FFPGFEPVPAEDVAKAYVR----SVEGAF 190

                 ....*
gi 517341756 243 TGQVI 247
Cdd:cd11731  191 TGQVL 195
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
12-210 3.52e-15

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: 73.08  E-value: 3.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVI--VHTGRKPGRDLpdfLLTAESER-RALLLH-ADFSAVGGAAQFAEDALAffDR 87
Cdd:cd09805    3 VLITGCDSGFGNLLAKKLDSLGFTVLagCLTKNGPGAKE---LRRVCSDRlRTLQLDvTKPEQIKRAAQWVKEHVG--EK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 -VDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAaIVNtvsISALTGG--SPGSSIYSAS 164
Cdd:cd09805   78 gLWGLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGR-VVN---VSSMGGRvpFPAGGAYCAS 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQ 210
Cdd:cd09805  154 KAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAK 199
PRK09291 PRK09291
SDR family oxidoreductase;
12-201 5.14e-15

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 72.34  E-value: 5.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVI--VHTGRKPgrdlpdFLLTAESERRALLLHA---DFSAVGGAAQFAEdalafFD 86
Cdd:PRK09291   5 ILITGAGSGFGREVALRLARKGHNVIagVQIAPQV------TALRAEAARRGLALRVeklDLTDAIDRAQAAE-----WD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 rVDVLVNNAGTMlgrfPAATLTDAEYEAVVRLNQTSV---VALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSA 163
Cdd:PRK09291  74 -VDVLLNNAGIG----EAGAVVDIPVELVRELFETNVfgpLELTQGFVRKMVARGKGKVVFTSSMAGLITG-PFTGAYCA 147
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:PRK09291 148 SKHALEAIAEAMHAELKPFGIQVATVNPGPYLTGFNDT 185
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
12-233 8.12e-15

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


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 71.64  E-value: 8.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGrdlpdflltaesERRALLLHADFSAVGGAAQFAEDA------LAFF 85
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVAL-AARREA------------KLEALLVDIIRDAGGSAKAVPTDArdedevIALF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  86 DRV-------DVLVNNAGTMLgRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGS 158
Cdd:cd05373   69 DLIeeeigplEVLVYNAGANV-WFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRG-RAGF 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517341756 159 SIYSASKAFVATYSKALARELAPDGIRV-NCVSPGTIETEF-HERYSSREKLEQTRKSIPlqrlgtAEDCAPAYLFL 233
Cdd:cd05373  147 AAFAGAKFALRALAQSMARELGPKGIHVaHVIIDGGIDTDFiRERFPKRDERKEEDGILD------PDAIAEAYWQL 217
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
12-197 1.29e-14

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 71.27  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIV---HTGRKPGRDLPDFLLTAESERR--------ALLLHADFSAVGGAAQFAED 80
Cdd:cd05338    6 AFVTGASRGIGRAIALRLAKAGATVVVaakTASEGDNGSAKSLPGTIEETAEeieaaggqALPIVVDVRDEDQVRALVEA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGTMLGRFPAATLTDaEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALtGGSPGSSI 160
Cdd:cd05338   86 TVDQFGRLDILVNNAGAIWLSLVEDTPAK-RFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSL-RPARGDVA 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 517341756 161 YSASKAFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:cd05338  164 YAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIET 200
PRK06182 PRK06182
short chain dehydrogenase; Validated
12-198 2.06e-14

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 70.76  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGR--DLPDFLLTAeserrallLHADFSAVGGAAQFAEDALAFFDRVD 89
Cdd:PRK06182   6 ALVTGASSGIGKATARRLAAQGYTVYG-AARRVDKmeDLASLGVHP--------LSLDVTDEASIKAAVDTIIAEEGRID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTML-GRFPAATLTDAEYEAVVrlNQTSVVALTRALLPALKAAEGAAIVNTVSIsaltGG---SPGSSIYSASK 165
Cdd:PRK06182  77 VLVNNAGYGSyGAIEDVPIDEARRQFEV--NLFGAARLTQLVLPHMRAQRSGRIINISSM----GGkiyTPLGAWYHATK 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK06182 151 FALEGFSDALRLEVAPFGIDVVVIEPGGIKTEW 183
PRK06194 PRK06194
hypothetical protein; Provisional
7-219 2.71e-14

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 70.81  E-value: 2.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgRD-LPDFLLTAESERRA-----LLLHADFSAVGGAAQFAED 80
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKLVL-------ADvQQDALDRAVAELRAqgaevLGVRTDVSDAAQVEALADA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGTMLGRFPAATlTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAA------IVNTVSISALTgG 154
Cdd:PRK06194  77 ALERFGAVHLLFNNAGVGAGGLVWEN-SLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEKDpayeghIVNTASMAGLL-A 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517341756 155 SPGSSIYSASKAFVATYSKALARELAPDGIRVNC--VSPGTIETEFHErySSREKLEQTRKSIPLQR 219
Cdd:PRK06194 155 PPAMGIYNVSKHAVVSLTETLYQDLSLVTDQVGAsvLCPYFVPTGIWQ--SERNRPADLANTAPPTR 219
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
10-196 5.17e-14

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 68.89  E-value: 5.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkpgrdlPDFLLTAESERRALLLHADfSAVGGAAQFAEDALAFFDRVD 89
Cdd:cd05334    2 RVVLVYGGRGALGSAVVQAFKSRGWWVAS----------IDLAENEEADASIIVLDSD-SFTEQAKQVVASVARLSGKVD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKaaEGAAIVNTVSISALtGGSPGSSIYSASKAFVA 169
Cdd:cd05334   71 ALICVAGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLL--SGGLLVLTGAKAAL-EPTPGMIGYGAAKAAVH 147
                        170       180
                 ....*....|....*....|....*....
gi 517341756 170 TYSKALAREL--APDGIRVNCVSPGTIET 196
Cdd:cd05334  148 QLTQSLAAENsgLPAGSTANAILPVTLDT 176
PRK06196 PRK06196
oxidoreductase; Provisional
13-196 8.52e-14

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 69.71  E-value: 8.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDlPDfllTAESERRAL----LLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK06196  30 IVTGGYSGLGLETTRALAQAGAHVIV-----PARR-PD---VAREALAGIdgveVVMLDLADLESVRAFAERFLDSGRRI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMlgrfpAATLTDAE--YEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSIsaltgGSPGSSI------ 160
Cdd:PRK06196 101 DILINNAGVM-----ACPETRVGdgWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSA-----GHRRSPIrwddph 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 517341756 161 ----------YSASKAFVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK06196 171 ftrgydkwlaYGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILT 216
PRK05876 PRK05876
short chain dehydrogenase; Provisional
7-198 1.06e-13

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 68.83  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESeRRALLLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK05876   4 FPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEG-FDVHGVMCDVRHREEVTHLADEAFRLLG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPA-LKAAEGAAIVNTVSISALTGGSpGSSIYSASK 165
Cdd:PRK05876  83 HVDVVFSNAGIVVGG-PIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRlLEQGTGGHVVFTASFAGLVPNA-GLGAYGVAK 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK05876 161 YGVVGLAETLAREVTADGIGVSVLCPMVVETNL 193
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
10-249 1.20e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 68.56  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPDFlltAESERRALLLHA-DFSAVGGAAQFAEDAL--AFFD 86
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVIS-ISRTENKELTKL---AEQYNSNLTFHSlDLQDVHELETNFNEILssIQED 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVD--VLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYSAS 164
Cdd:PRK06924  78 NVSsiHLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDWKVDKRVINISSGAAKNPYFGWSAYCSS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALA--RELAPDGIRVNCVSPGTIETEFHE--RYSSREKLEQTRKSIPLQRLGTaedcapaylfLAAPSlsg 240
Cdd:PRK06924 158 KAGLDMFTQTVAteQEEEEYPVKIVAFSPGVMDTNMQAqiRSSSKEDFTNLDRFITLKEEGK----------LLSPE--- 224

                 ....*....
gi 517341756 241 YITGQVIEI 249
Cdd:PRK06924 225 YVAKALRNL 233
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
12-253 7.37e-13

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 66.11  E-value: 7.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgRDLPDFLltaeSERRALLLHADFSAVGGAAQFAEDALAFFDRVDVL 91
Cdd:PRK06483   5 ILITGAGQRIGLALAWHLLAQGQPVIV-SYRTH-YPAIDGL----RQAGAQCIQADFSTNAGIMAFIDELKQHTDGLRAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLGRFPAATLTDaeyeAVVRLNQTSVVA---LTRALLPALKAAEGAAiVNTVSISALTG--GSPGSSIYSASKA 166
Cdd:PRK06483  79 IHNASDWLAEKPGAPLAD----VLARMMQIHVNApylLNLALEDLLRGHGHAA-SDIIHITDYVVekGSDKHIAYAASKA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDgIRVNCVSPGTIetEFHERYSSREKLEQTRKSIplqrLGTAEDCAPAYLFLAAPSLSGYITGQV 246
Cdd:PRK06483 154 ALDNMTLSFAAKLAPE-VKVNSIAPALI--LFNEGDDAAYRQKALAKSL----LKIEPGEEEIIDLVDYLLTSCYVTGRS 226

                 ....*..
gi 517341756 247 IEINGGQ 253
Cdd:PRK06483 227 LPVDGGR 233
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
8-255 1.72e-12

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


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 65.18  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADF---SAVGGAAQFAEDAlaf 84
Cdd:cd05322    1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADAtneQSVIALSKGVDEI--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNAGTMlgrfPAATLTDAEYEAVVRLNQtsvVALTRALLPALKAA----EGAAIVNTVSISALTG--GSPGS 158
Cdd:cd05322   78 FKRVDLLVYSAGIA----KSAKITDFELGDFDRSLQ---VNLVGYFLCAREFSklmiRDGIQGRIIQINSKSGkvGSKHN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 159 SIYSASKAFVATYSKALARELAPDGIRVNCVSPGT-IETEFHE----RYSSR-----EKLEQT-RKSIPLQRLGTAEDCA 227
Cdd:cd05322  151 SGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLGNlLKSPMFQsllpQYAKKlgikeSEVEQYyIDKVPLKRGCDYQDVL 230
                        250       260
                 ....*....|....*....|....*...
gi 517341756 228 PAYLFLAAPSLSgYITGQVIEINGGQLI 255
Cdd:cd05322  231 NMLLFYASPKAS-YCTGQSINITGGQVM 257
PRK07832 PRK07832
SDR family oxidoreductase;
10-196 5.32e-12

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 63.91  E-value: 5.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDLPDFLLTAE---------SERRALLLhADFSAVggaAQFAED 80
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFL-----TDRDADGLAQTVAdaralggtvPEHRALDI-SDYDAV---AAFAAD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGTMLGRFPAAtLTDAEYEAVVRLNQTSVVALTRALLPAL-KAAEGAAIVNtVSISALTGGSPGSS 159
Cdd:PRK07832  72 IHAAHGSMDVVMNIAGISAWGTVDR-LTHEQWRRMVDVNLMGPIHVIETFVPPMvAAGRGGHLVN-VSSAAGLVALPWHA 149
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK07832 150 AYSASKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKT 186
PRK08703 PRK08703
SDR family oxidoreductase;
4-249 1.23e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 62.64  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   4 PRLFENRNVVVTGAGRGIGLEVARQFLDCGAKV----------------IVHTGRKPGRDLPDFLLTAESERRALLlhad 67
Cdd:PRK08703   1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVilvarhqkklekvydaIVEAGHPEPFAIRFDLMSAEEKEFEQF---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  68 fsavggAAQFAEdalAFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVS 147
Cdd:PRK08703  77 ------AATIAE---ATQGKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 148 ISALTgGSPGSSIYSASKAFVATYSKALARELAPDG-IRVNCVSPGTIETEFHERYSSREKlEQTRKSIplqrlgtaEDC 226
Cdd:PRK08703 148 SHGET-PKAYWGGFGASKAALNYLCKVAADEWERFGnLRANVLVPGPINSPQRIKSHPGEA-KSERKSY--------GDV 217
                        250       260
                 ....*....|....*....|...
gi 517341756 227 APAYLFLAAPSLSGYiTGQVIEI 249
Cdd:PRK08703 218 LPAFVWWASAESKGR-SGEIVYL 239
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
13-197 2.22e-11

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 62.24  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   13 VVTGAGRGIGLEVARQFLDC---GAKVIVHTGRKPG--RDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAF--- 84
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKClksPGSVLVLSARNDEalRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLKALRELprp 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   85 --FDRVdVLVNNAGTM--LGRFpAATLTDAEY-EAVVRLNQTSVVALTRALLPALKAAEGA--AIVNTVSISALTGgSPG 157
Cdd:TIGR01500  84 kgLQRL-LLINNAGTLgdVSKG-FVDLSDSTQvQNYWALNLTSMLCLTSSVLKAFKDSPGLnrTVVNISSLCAIQP-FKG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 517341756  158 SSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:TIGR01500 161 WALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTD 200
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
12-196 3.40e-11

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: 61.74  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHtGRKPGRdLPDflLTAESERRALLLHADFSAVGGAAQFAEDALAfFDRVDVL 91
Cdd:cd08951   10 IFITGSSDGLGLAAARTLLHQGHEVVLH-ARSQKR-AAD--AKAACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLGRFPAATLTDAeyEAVVRLNQTSVVALTRALLPALKAA--------EGAAIVNtvSISALTGGSPGSSIYSA 163
Cdd:cd08951   85 IHNAGILSGPNRKTPDTGI--PAMVAVNVLAPYVLTALIRRPKRLIylssgmhrGGNASLD--DIDWFNRGENDSPAYSD 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 517341756 164 SKAFVATYSKALARelAPDGIRVNCVSPGTIET 196
Cdd:cd08951  161 SKLHVLTLAAAVAR--RWKDVSSNAVHPGWVPT 191
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
12-195 4.05e-11

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


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 60.19  E-value: 4.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756    12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLH---ADFSAVGGAAQFAEDALAFFDRV 88
Cdd:smart00822   3 YLITGGLGGLGRALARWLAERGARRLVLLSRSGPDAPGAAALLAELEAAGARVTvvaCDVADRDALAAVLAAIPAVEGPL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756    89 DVLVNNAGTmLGRFPAATLTDAEYEAVVRlnqtSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYSASKAFV 168
Cdd:smart00822  83 TGVIHAAGV-LDDGVLASLTPERFAAVLA----PKAAGAWNLHELTADLPLDFFVLFSSIAGVL-GSPGQANYAAANAFL 156
                          170       180
                   ....*....|....*....|....*..
gi 517341756   169 AtyskALARELAPDGIRVNCVSPGTIE 195
Cdd:smart00822 157 D----ALAEYRRARGLPALSIAWGAWA 179
PRK08278 PRK08278
SDR family oxidoreductase;
7-196 4.27e-11

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 61.46  E-value: 4.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   7 FENRNVVVTGAGRGIGLEVARQFLDCGAKvIVHTGR--KPGRDLPDFLLTAESERR-----ALLLHADFSAVGGAAQFAE 79
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGAN-IVIAAKtaEPHPKLPGTIHTAAEEIEaaggqALPLVGDVRDEDQVAAAVA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  80 DALAFFDRVDVLVNNAGtmlgrfpAATLTDAE------YEAVVRLNQTSVVALTRALLPALKAAEGAAIVnTVS--ISAL 151
Cdd:PRK08278  83 KAVERFGGIDICVNNAS-------AINLTGTEdtpmkrFDLMQQINVRGTFLVSQACLPHLKKSENPHIL-TLSppLNLD 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 517341756 152 TGGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGT-IET 196
Cdd:PRK08278 155 PKWFAPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPRTtIAT 200
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
8-253 4.94e-11

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 61.72  E-value: 4.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIG----LEVARQfldcGAKVIV--HTGRKPGRDLPDFLLTAESerRALLLHADFSAVGGAAQFAEDA 81
Cdd:PRK07792  11 SGKVAVVTGAAAGLGraeaLGLARL----GATVVVndVASALDASDVLDEIRAAGA--KAVAVAGDISQRATADELVATA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  82 LAfFDRVDVLVNNAGTMLGRFpAATLTDAEYEAVVRLNQTSVVALTRALLP----ALKAAEGAA---IVNTVSISALTgG 154
Cdd:PRK07792  85 VG-LGGLDIVVNNAGITRDRM-LFNMSDEEWDAVIAVHLRGHFLLTRNAAAywraKAKAAGGPVygrIVNTSSEAGLV-G 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 155 SPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSSREKLEQTRKSiPLqrlgTAEDCAPAYLFLA 234
Cdd:PRK07792 162 PVGQANYGAAKAGITALTLSAARALGRYGVRANAICPRARTAMTADVFGDAPDVEAGGID-PL----SPEHVVPLVQFLA 236
                        250
                 ....*....|....*....
gi 517341756 235 APSLSGyITGQVIEINGGQ 253
Cdd:PRK07792 237 SPAAAE-VNGQVFIVYGPM 254
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
87-201 5.47e-11

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 60.94  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGT-MLGrfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSSIYSASK 165
Cdd:cd09806   79 HVDVLVCNAGVgLLG--PLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQG-LPFNDVYCASK 155
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 517341756 166 AFVATYSKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:cd09806  156 FALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEK 191
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
9-197 6.49e-11

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 61.63  E-value: 6.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLtAESERRALLLHADFSAVGGAAQFAE--DALAFFD 86
Cdd:cd05274  150 DGTYLITGGLGGLGLLVARWLAARGARHLVLLSRRGPAPRAAARA-ALLRAGGARVSVVRCDVTDPAALAAllAELAAGG 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTmlGRF-PAATLTDAEYEAVVRlnqtSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSASK 165
Cdd:cd05274  229 PLAGVIHAAGV--LRDaLLAELTPAAFAAVLA----AKVAGALNLHELTPDLPLDFFVLFSSVAALLGG-AGQAAYAAAN 301
                        170       180       190
                 ....*....|....*....|....*....|..
gi 517341756 166 AFVAtyskALARELAPDGIRVNCVSPGTIETE 197
Cdd:cd05274  302 AFLD----ALAAQRRRRGLPATSVQWGAWAGG 329
PLN02780 PLN02780
ketoreductase/ oxidoreductase
16-197 9.43e-11

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 61.04  E-value: 9.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  16 GAGRGIGLEVARQFLDcgakvIVHTGRKPGR--DLPDFLLTAESERRALLLHADFSA-VGGAAQFAEDALAFFDrVDVLV 92
Cdd:PLN02780  64 GIGKGFAFQLARKGLN-----LVLVARNPDKlkDVSDSIQSKYSKTQIKTVVVDFSGdIDEGVKRIKETIEGLD-VGVLI 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  93 NNAGTmlgRFPAATL---TDAEY-EAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGS-PGSSIYSASKAF 167
Cdd:PLN02780 138 NNVGV---SYPYARFfheVDEELlKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSdPLYAVYAATKAY 214
                        170       180       190
                 ....*....|....*....|....*....|
gi 517341756 168 VATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:PLN02780 215 IDQFSRCLYVEYKKSGIDVQCQVPLYVATK 244
PRK06197 PRK06197
short chain dehydrogenase; Provisional
10-147 1.94e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 60.04  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHTgRKP--GRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALAAKGAHVVLAV-RNLdkGKAAAARITAATPGADVTLQELDLTSLASVRAAADALRAAYPR 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMLGrfPAATLTDAeYEAVVRLNQTSVVALTRALLPALKAAEGAAIVnTVS 147
Cdd:PRK06197  96 IDLLINNAGVMYT--PKQTTADG-FELQFGTNHLGHFALTGLLLDRLLPVPGSRVV-TVS 151
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
13-177 2.51e-10

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 60.07  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRAL-----LLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:cd08953  209 LVTGGAGGIGRALARALARRYGARLVLLGRSPLPPEEEWKAQTLAALEALgarvlYISADVTDAAAVRRLLEKVRERYGA 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMLGRFPaATLTDAEYEAVvrlnQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGsPGSSIYSASKAF 167
Cdd:cd08953  289 IDGVIHAAGVLRDALL-AQKTAEDFEAV----LAPKVDGLLNLAQALADEPLDFFVLFSSVSAFFGG-AGQADYAAANAF 362
                        170
                 ....*....|
gi 517341756 168 VATYSKALAR 177
Cdd:cd08953  363 LDAFAAYLRQ 372
PRK05993 PRK05993
SDR family oxidoreductase;
8-198 7.66e-10

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 57.73  E-value: 7.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgRDLPDflLTAESeRRALLLhaDFSAVGGAAQFAEDALAFFD- 86
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFA-TCRKE-EDVAA--LEAEG-LEAFQL--DYAEPESIAALVAQVLELSGg 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNagtmlGRF--PAAtLTDAEYEAVVRLNQTSVVA---LTRALLPALKAAEGAAIVNTVSISALTG----GSpg 157
Cdd:PRK05993  76 RLDALFNN-----GAYgqPGA-VEDLPTEALRAQFEANFFGwhdLTRRVIPVMRKQGQGRIVQCSSILGLVPmkyrGA-- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 517341756 158 ssiYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:PRK05993 148 ---YNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRF 185
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
6-252 8.06e-10

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 57.82  E-value: 8.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTGAG--RGIGLEVARQFLDCGAKVI-VHTGRKPGRDLPDFLLTAESERRALL---LHADFSAVGGAAQFAE 79
Cdd:PRK08594   4 SLEGKTYVVMGVAnkRSIAWGIARSLHNAGAKLVfTYAGERLEKEVRELADTLEGQESLLLpcdVTSDEEITACFETIKE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  80 DA---------LAFFDRVDvlvnnagtMLGRFpaATLTDAEYEAVVRLNQTSVVALTRALLPALkaAEGAAIVNTVSIsa 150
Cdd:PRK08594  84 EVgvihgvahcIAFANKED--------LRGEF--LETSRDGFLLAQNISAYSLTAVAREAKKLM--TEGGSIVTLTYL-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 151 ltGGS---PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETefherYSSR------EKLEQTRKSIPLQRLG 221
Cdd:PRK08594 150 --GGErvvQNYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRT-----LSAKgvggfnSILKEIEERAPLRRTT 222
                        250       260       270
                 ....*....|....*....|....*....|.
gi 517341756 222 TAEDCAPAYLFLAApSLSGYITGQVIEINGG 252
Cdd:PRK08594 223 TQEEVGDTAAFLFS-DLSRGVTGENIHVDSG 252
PRK07806 PRK07806
SDR family oxidoreductase;
9-143 9.55e-10

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 57.42  E-value: 9.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGL 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517341756  89 DVLVNNA-GTMlgrfpaatLTDAEYEAVVRLNQTSVVALTRALLPALkaAEGAAIV 143
Cdd:PRK07806  86 DALVLNAsGGM--------ESGMDEDYAMRLNRDAQRNLARAALPLM--PAGSRVV 131
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
12-247 1.42e-09

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: 57.07  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPDfllTAESER----RALLL---HADFSAVggAAQFAEDALAF 84
Cdd:cd09763    6 ALVTGASRGIGRGIALQLGEAGATVYI-TGRTILPQLPG---TAEEIEarggKCIPVrcdHSDDDEV--EALFERVAREQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  85 FDRVDVLVNNA-----GTMLGRFPA-----ATLTDAEYEAVVRLNQTSVVALTRALLPALKaaegAAIVNTVSISALTG- 153
Cdd:cd09763   80 QGRLDILVNNAyaavqLILVGVAKPfweepPTIWDDINNVGLRAHYACSVYAAPLMVKAGK----GLIVIISSTGGLEYl 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 154 -GSPgssiYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERY-SSREKLEQTRKSIPLQRLGTAEDCAPAYL 231
Cdd:cd09763  156 fNVA----YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMpEDDEGSWHAKERDAFLNGETTEYSGRCVV 231
                        250
                 ....*....|....*.
gi 517341756 232 FLAAPSLSGYITGQVI 247
Cdd:cd09763  232 ALAADPDLMELSGRVL 247
PRK05854 PRK05854
SDR family oxidoreductase;
10-196 1.95e-09

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 57.00  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVI--VHTGRKpGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDR 87
Cdd:PRK05854  15 KRAVVTGASDGLGLGLARRLAAAGAEVIlpVRNRAK-GEAAVAAIRTAVPDAKLSLRALDLSSLASVAALGEQLRAEGRP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  88 VDVLVNNAGTMlgRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAeGAAIVNTVSISALTG-----------GSP 156
Cdd:PRK05854  94 IHLLINNAGVM--TPPERQTTADGFELQFGTNHLGHFALTAHLLPLLRAG-RARVTSQSSIAARRGainwddlnwerSYA 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 517341756 157 GSSIYSASKAFVATYSKALAR--ELAPDGIRVNCVSPGTIET 196
Cdd:PRK05854 171 GMRAYSQSKIAVGLFALELDRrsRAAGWGITSNLAHPGVAPT 212
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
165-252 1.99e-09

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 56.49  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 165 KAFVATYSKALARELAPDGIRVNCVSPGTIETefheRYSS-----REKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLS 239
Cdd:PRK07533 166 KAALESSVRYLAAELGPKGIRVHAISPGPLKT----RAASgiddfDALLEDAAERAPLRRLVDIDDVGAVAAFLASDAAR 241
                         90
                 ....*....|...
gi 517341756 240 GyITGQVIEINGG 252
Cdd:PRK07533 242 R-LTGNTLYIDGG 253
PRK06139 PRK06139
SDR family oxidoreductase;
8-196 2.49e-09

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 56.65  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIGLEVARQFLDCGAKVIVhtgrkPGRDLPDFLLTAESER----RALLLHADFSAVGGAAQFAEDALA 83
Cdd:PRK06139   6 HGAVVVITGASSGIGQATAEAFARRGARLVL-----AARDEEALQAVAEECRalgaEVLVVPTDVTDADQVKALATQAAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAGT-MLGRFPAATLtdAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYS 162
Cdd:PRK06139  81 FGGRIDVWVNNVGVgAVGRFEETPI--EAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFA-AQPYAAAYS 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 517341756 163 ASKAFVATYSKALARELAPD-GIRVNCVSPGTIET 196
Cdd:PRK06139 158 ASKFGLRGFSEALRGELADHpDIHVCDVYPAFMDT 192
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
11-157 1.04e-08

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: 54.83  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  11 NVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPGRdlpdflltAESERRAL--------LLHADFSAVGGAAQFAEDAL 82
Cdd:cd09810    3 TVVITGASSGLGLAAAKALARRGEWHVVMACRDFLK--------AEQAAQEVgmpkdsysVLHCDLASLDSVRQFVDNFR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  83 AFFDRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAA--IVNTVSISALT---GGSPG 157
Cdd:cd09810   75 RTGRPLDALVCNAAVYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLQRSENASprIVIVGSITHNPntlAGNVP 154
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
12-198 1.15e-08

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 55.31  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTgrkpgRDLPDFLLTAESERRALLLHA--DFSAVGGAAQFAEDALAFFDRVD 89
Cdd:COG3347  428 ALVTGGAGGIGRATAARLAAEGAAVVVAD-----LDGEAAEAAAAELGGGYGADAvdATDVDVTAEAAVAAAFGFAGLDI 502
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  90 VLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYSASKAFVA 169
Cdd:COG3347  503 GGSDIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVSKNAAAAAYGAAAAATAKA 582
                        170       180       190
                 ....*....|....*....|....*....|..
gi 517341756 170 ---TYSKALARELAPDGIRVNCVSPGTIETEF 198
Cdd:COG3347  583 aaqHLLRALAAEGGANGINANRVNPDAVLDGS 614
PRK08340 PRK08340
SDR family oxidoreductase;
11-251 1.42e-08

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 54.04  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  11 NVVVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpgrdlPDFLLTAESERRAL----LLHADFSAVGGAAQFAEDALAFFD 86
Cdd:PRK08340   2 NVLVTASSRGIGFNVARELLKKGARVVISSRN------EENLEKALKELKEYgevyAVKADLSDKDDLKNLVKEAWELLG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMlgRFPAATLTDAEYEAVVRLNQTSVVA---LTRALLPA-LKAAEGAAIVNTVSISALTGGSPgSSIYS 162
Cdd:PRK08340  76 GIDALVWNAGNV--RCEPCMLHEAGYSDWLEAALLHLVApgyLTTLLIQAwLEKKMKGVLVYLSSVSVKEPMPP-LVLAD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 163 ASKAFVATYSKALARELAPDGIRVNCVSPGTIET---------------EFHERYSSREKLEQTrksiPLQRLGTAEDCA 227
Cdd:PRK08340 153 VTRAGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTpgarenlariaeergVSFEETWEREVLERT----PLKRTGRWEELG 228
                        250       260
                 ....*....|....*....|....
gi 517341756 228 PAYLFLAAPSlSGYITGQVIEING 251
Cdd:PRK08340 229 SLIAFLLSEN-AEYMLGSTIVFDG 251
PRK08177 PRK08177
SDR family oxidoreductase;
10-197 2.06e-08

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 53.11  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRDLPdflLTAESERRALLLHA-DFSAVGGAAQfaedALAfFDRV 88
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTA-TVRGPQQDTA---LQALPGVHIEKLDMnDPASLDQLLQ----RLQ-GQRF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMlGrfPAA-TLTDAEYEAVVRLNQTSVVA---LTRALLPALKAAEGA-AIVNTVSISALTGGSPGSSIYSA 163
Cdd:PRK08177  73 DLLFVNAGIS-G--PAHqSAADATAAEIGQLFLTNAIApirLARRLLGQVRPGQGVlAFMSSQLGSVELPDGGEMPLYKA 149
                        170       180       190
                 ....*....|....*....|....*....|....
gi 517341756 164 SKAFVATYSKALARELAPDGIRVNCVSPGTIETE 197
Cdd:PRK08177 150 SKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTD 183
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
10-202 3.91e-08

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: 52.98  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVHT-GRKPGRDLPDFLLTAESERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:cd09809    2 KVIIITGANSGIGFETARSFALHGAHVILACrNMSRASAAVSRILEEWHKARVEAMTLDLASLRSVQRFAEAFKAKNSPL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMLGRFpaaTLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSIS-------------ALTGGS 155
Cdd:cd09809   82 HVLVCNAAVFALPW---TLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSEShrftdlpdscgnlDFSLLS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517341756 156 PGSSIYSASKAFVAT------YSKALARELAPDGIRVNCVSPGT-IETEFHERY 202
Cdd:cd09809  159 PPKKKYWSMLAYNRAklcnilFSNELHRRLSPRGITSNSLHPGNmMYSSIHRNW 212
KR_fFAS_like_SDR_c_like cd08928
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c) ...
12-196 4.06e-08

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c)-like SDRs; KR domain of FAS, including the fungal-type multidomain FAS alpha chain, and the single domain daunorubicin C-13 ketoreductase. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD(P)-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Single domain 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: 187633 [Multi-domain]  Cd Length: 248  Bit Score: 52.68  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRG-IGLEVARQFLDCGAKVIVHTgRKPGRDLPDFL--LTAESERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:cd08928    1 VLITGAGDGsIGAEVLQGLLNGGAKVYVTT-SRFSRQVTKYYqdIYAACGAAGSVLIVVPFNQGSKQDVEALAIGIYDTV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVnNAGTMLGRFPAATLTDAEYEAVVRLNQTS---VVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSS------ 159
Cdd:cd08928   80 NGLG-WDLDLYGPFAAIPETGIEIPAIDSKSEVAhriMLTNLLRPKGLVKIQKQLRGQETRPAQVILPFSPNHGtfgddg 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:cd08928  159 AYSESKLHLETLFNRWASESWGNDLTVCGAHIGWTRG 195
PRK06101 PRK06101
SDR family oxidoreductase;
9-201 4.94e-08

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 52.18  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   9 NRNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKpgRDLPDFLLTAESERRALLLhaDFSAVGGAAQfAEDALAFFDrv 88
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQVIA-CGRN--QSVLDELHTQSANIFTLAF--DVTDHPGTKA-ALSQLPFIP-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMlgRFPAATLTDAEYEA-VVRLNQTSVVALTRALLPALKAAEGAAIVNTV-SISALtggsPGSSIYSASKA 166
Cdd:PRK06101  73 ELWIFNAGDC--EYMDDGKVDATLMArVFNVNVLGVANCIEGIQPHLSCGHRVVIVGSIaSELAL----PRAEAYGASKA 146
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:PRK06101 147 AVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDK 181
PRK08251 PRK08251
SDR family oxidoreductase;
10-201 5.73e-08

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 52.25  E-value: 5.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFldcGAKvivhtgrkpGRDLP------DFL------LTAESERRALLLHA----DFSAVGG 73
Cdd:PRK08251   3 QKILITGASSGLGAGMAREF---AAK---------GRDLAlcarrtDRLeelkaeLLARYPGIKVAVAAldvnDHDQVFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  74 AAQFAEDALAFFDRVDVlvnNAGTMLGRFPAATLTDAEyEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTG 153
Cdd:PRK08251  71 VFAEFRDELGGLDRVIV---NAGIGKGARLGTGKFWAN-KATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRG 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 517341756 154 GSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:PRK08251 147 LPGVKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAK 194
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
10-213 5.97e-08

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 52.06  E-value: 5.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAK-VIVHTGRKPGRDLPDFLLTAESERRALLLHA--------DFSAVGGAaqfAED 80
Cdd:cd09762    4 KTLFITGASRGIGKAIALKAARDGANvVIAAKTAEPHPKLPGTIYTAAEEIEAAGGKAlpcivdirDEDQVRAA---VEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAFFDRVDVLVNNAGtmlgrfpAATLTDAE------YEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTvsisaltgg 154
Cdd:cd09762   81 AVEKFGGIDILVNNAS-------AISLTGTLdtpmkrYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNL--------- 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 155 SPGSSI----------YSASKAFVATYSKALARELAPDGIRVNCVSPGT-IETEFHERYSSREKLEQTRK 213
Cdd:cd09762  145 SPPLNLnpkwfknhtaYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPRTaIATAAMNMLGGVDVAACCRK 214
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
6-196 6.94e-08

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 51.87  E-value: 6.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   6 LFENRNVVVTG--AGRGIGLEVARQFLDCGAKVIVhTGRkpGRDLPdflLTAESERR----ALLLHADFSAVGGAAQFAE 79
Cdd:PRK07889   4 LLEGKRILVTGviTDSSIAFHVARVAQEQGAEVVL-TGF--GRALR---LTERIAKRlpepAPVLELDVTNEEHLASLAD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  80 DALAFFDRVDVLVNNAG-----TMLGRFpaatlTDAEYEAV---VRLNQTSVVALTRALLPALkaAEGAAIVntvsisAL 151
Cdd:PRK07889  78 RVREHVDGLDGVVHSIGfapqsALGGNF-----LDAPWEDVataLHVSAYSLKSLAKALLPLM--NEGGSIV------GL 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 517341756 152 T-GGSPGSSIYS---ASKAFVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK07889 145 DfDATVAWPAYDwmgVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRT 193
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
122-252 1.15e-07

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 51.28  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 122 SVVALTRALLPALKaaEGAAIVntvSISALTGGS--PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET--- 196
Cdd:PRK08415 121 SLIELTRALLPLLN--DGASVL---TLSYLGGVKyvPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKTlaa 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 197 ----EFheryssREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLSGyITGQVIEINGG 252
Cdd:PRK08415 196 sgigDF------RMILKWNEINAPLKKNVSIEEVGNSGMYLLSDLSSG-VTGEIHYVDAG 248
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
12-198 2.99e-07

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 49.44  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFldcgaKVIVHTGRKPGRDLPDFLLTAEsERRALLLHADFSAVGGAAQFAEDALAffdrVDVL 91
Cdd:cd11730    1 ALILGATGGIGRALARAL-----AGRGWRLLLSGRDAGALAGLAA-EVGALARPADVAAELEVWALAQELGP----LDLL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  92 VNNAGTMLGRfPAATLTDAEYEAVVRLNQTSV-VALTRALlpALKAAEGAAIVNTVSISALTggSPGSSIYSASKAFVAT 170
Cdd:cd11730   71 VYAAGAILGK-PLARTKPAAWRRILDANLTGAaLVLKHAL--ALLAAGARLVFLGAYPELVM--LPGLSAYAAAKAALEA 145
                        170       180
                 ....*....|....*....|....*...
gi 517341756 171 YSKALARELapDGIRVNCVSPGTIETEF 198
Cdd:cd11730  146 YVEVARKEV--RGLRLTLVRPPAVDTGL 171
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
10-210 4.47e-07

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 49.52  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIG----LEVARQfldcGAKV-IVHTGRKPGRDLPDFLLTaESERRALLLH-ADFSAVGGAAQFAEDALA 83
Cdd:cd09808    2 RSFLITGANSGIGkaaaLAIAKR----GGTVhMVCRNQTRAEEARKEIET-ESGNQNIFLHiVDMSDPKQVWEFVEEFKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  84 FFDRVDVLVNNAGTMLGRfpaATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGGSPGSSIYSA 163
Cdd:cd09808   77 EGKKLHVLINNAGCMVNK---RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLVQKLNTNNLQSE 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517341756 164 SKAFVATYSKA--------LARELAPD--GIRVNCVSPGTIET--------EFHERYSSREKLEQ 210
Cdd:cd09808  154 RTAFDGTMVYAqnkrqqviMTEQWAKKhpEIHFSVMHPGWADTpavrnsmpDFHARFKDRLRSEE 218
PRK07102 PRK07102
SDR family oxidoreductase;
11-196 5.05e-07

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 49.15  E-value: 5.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  11 NVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPGRdLPDFL--LTAESERRALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:PRK07102   3 KILIIGATSDIARACARRYAAAGARLYL-AARDVER-LERLAddLRARGAVAVSTHELDILDTASHAAFLDSLPALPDIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVnnaGTmLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVntvSISALTG--GSPGSSIYSASKA 166
Cdd:PRK07102  81 LIAV---GT-LGDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGSGTIV---GISSVAGdrGRASNYVYGSAKA 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 517341756 167 FVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK07102 154 ALTAFLSGLRNRLFKSGVHVLTVKPGFVRT 183
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
122-255 5.96e-07

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 49.33  E-value: 5.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 122 SVVALTRALLPALKaaEGAAIVNTVSISALTGgSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETefheR 201
Cdd:PRK07370 125 SLAPLCKAAKPLMS--EGGSIVTLTYLGGVRA-IPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRT----L 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 517341756 202 YSSR-----EKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLSGyITGQVIEINGGQLI 255
Cdd:PRK07370 198 ASSAvggilDMIHHVEEKAPLRRTVTQTEVGNTAAFLLSDLASG-ITGQTIYVDAGYCI 255
PRK06953 PRK06953
SDR family oxidoreductase;
10-197 6.87e-07

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 48.91  E-value: 6.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  10 RNVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgrdlpdfllTAESERRALLLHADFSAVGGAAQFAedALAFF---D 86
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIA-TARDA---------AALAALQALGAEALALDVADPASVA--GLAWKldgE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTMLGRFPAA-TLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTG-GSPGSSIYSAS 164
Cdd:PRK06953  70 ALDAAVYVAGVYGPRTEGVePITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSSRMGSIGDaTGTTGWLYRAS 149
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 517341756 165 KAFVatysKALARELAPDGIRVNCVS--PGTIETE 197
Cdd:PRK06953 150 KAAL----NDALRAASLQARHATCIAlhPGWVRTD 180
PRK07984 PRK07984
enoyl-ACP reductase FabI;
156-252 8.68e-07

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 48.74  E-value: 8.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSS-REKLEQTRKSIPLQRLGTAEDCAPAYLFLA 234
Cdd:PRK07984 154 PNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDfRKMLAHCEAVTPIRRTVTIEDVGNSAAFLC 233
                         90
                 ....*....|....*...
gi 517341756 235 ApSLSGYITGQVIEINGG 252
Cdd:PRK07984 234 S-DLSAGISGEVVHVDGG 250
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
11-194 1.28e-06

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 48.44  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  11 NVVVTGAGRGIGLEVARQFLDCGAKVIVhTGRKPgrdlpdflltaeSERRALLLHADFSAVGGAAQFAEDALAFFDRVDV 90
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARGHEVVG-LDRSP------------PGAANLAALPGVEFVRGDLRDPEALAAALAGVDA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  91 LVNNAGtmlgrfpAATLTDAEYEAVVRLNqtsvVALTRALLPALKAAEGAAIVNTVSISALtGGSPG----------SSI 160
Cdd:COG0451   68 VVHLAA-------PAGVGEEDPDETLEVN----VEGTLNLLEAARAAGVKRFVYASSSSVY-GDGEGpidedtplrpVSP 135
                        170       180       190
                 ....*....|....*....|....*....|....
gi 517341756 161 YSASKAFVATYSKALARElapDGIRVNCVSPGTI 194
Cdd:COG0451  136 YGASKLAAELLARAYARR---YGLPVTILRPGNV 166
PRK07578 PRK07578
short chain dehydrogenase; Provisional
87-249 1.01e-05

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 45.19  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  87 RVDVLVNNAGTmlGRF-PAATLTDAEYEAVVR---LNQtsvVALTRALLPALkaAEGAAIvntvsisALTGGS------P 156
Cdd:PRK07578  55 KVDAVVSAAGK--VHFaPLAEMTDEDFNVGLQsklMGQ---VNLVLIGQHYL--NDGGSF-------TLTSGIlsdepiP 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 157 GSSIYSASKAFVATYSKALARELaPDGIRVNCVSPGTIEtefhERYSSREKLEQTRKSIPlqrlgtAEDCAPAYLflaaP 236
Cdd:PRK07578 121 GGASAATVNGALEGFVKAAALEL-PRGIRINVVSPTVLT----ESLEKYGPFFPGFEPVP------AARVALAYV----R 185
                        170
                 ....*....|...
gi 517341756 237 SLSGYITGQVIEI 249
Cdd:PRK07578 186 SVEGAQTGEVYKV 198
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
64-252 2.64e-05

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 44.23  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  64 LHADFSAVGGAAQFAEDALAFFDRvdvlvnnaGTMLGRFPAATLTDaeYEAVVRLNQTSVVALTRALLPALKaaEGAAIV 143
Cdd:PRK06603  76 LFDDIKEKWGSFDFLLHGMAFADK--------NELKGRYVDTSLEN--FHNSLHISCYSLLELSRSAEALMH--DGGSIV 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 144 nTVSISALTGGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYSS-REKLEQTRKSIPLQRLGT 222
Cdd:PRK06603 144 -TLTYYGAEKVIPNYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIGDfSTMLKSHAATAPLKRNTT 222
                        170       180       190
                 ....*....|....*....|....*....|
gi 517341756 223 AEDCAPAYLFLAApSLSGYITGQVIEINGG 252
Cdd:PRK06603 223 QEDVGGAAVYLFS-ELSKGVTGEIHYVDCG 251
KR_fFAS_SDR_c_like cd08950
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ...
7-42 3.00e-05

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like SDRs; KR domain of fungal-type fatty acid synthase (FAS), type I. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member, is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the Classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187653 [Multi-domain]  Cd Length: 259  Bit Score: 44.10  E-value: 3.00e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 517341756   7 FENRNVVVTGAGRG-IGLEVARQFLDCGAKVIVHTGR 42
Cdd:cd08950    5 FAGKVALVTGAGPGsIGAEVVAGLLAGGATVIVTTSR 41
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
122-252 3.54e-05

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 43.94  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 122 SVVALTRALLPALKaaEGAAIVnTVSISALTGGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET----- 196
Cdd:PRK06079 121 SLIAVAKYARPLLN--PGASIV-TLTYFGSERAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTlavtg 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 517341756 197 -EFHeryssREKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLSGyITGQVIEINGG 252
Cdd:PRK06079 198 iKGH-----KDLLKESDSRTVDGVGVTIEEVGNTAAFLLSDLSTG-VTGDIIYVDKG 248
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
122-252 9.43e-05

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 42.65  E-value: 9.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 122 SVVALTRALLPALKAAEGAAIvnTVSISALTGGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:PRK08690 123 SLPALAKAARPMMRGRNSAIV--ALSYLGAVRAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASG 200
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517341756 202 YSSREK-LEQTRKSIPLQRLGTAEDCAPAYLFLAApSLSGYITGQVIEINGG 252
Cdd:PRK08690 201 IADFGKlLGHVAAHNPLRRNVTIEEVGNTAAFLLS-DLSSGITGEITYVDGG 251
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
12-189 2.04e-04

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 41.01  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   12 VVVTGAGRGIGLEVARQFLDCGAKVIVHTGRKPG-RDLPDFLLTAESER--RALLLHADFSAVGGAAQFAEDALAFFDRV 88
Cdd:pfam08659   3 YLITGGLGGLGRELARWLAERGARHLVLLSRSAApRPDAQALIAELEARgvEVVVVACDVSDPDAVAALLAEIKAEGPPI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   89 DVLVNNAGTmLGRFPAATLTDAEYEAVVRlnqtSVVALTRALLPALKAAEGAAIVNTVSISALTgGSPGSSIYSASKAFV 168
Cdd:pfam08659  83 RGVIHAAGV-LRDALLENMTDEDWRRVLA----PKVTGTWNLHEATPDEPLDFFVLFSSIAGLL-GSPGQANYAAANAFL 156
                         170       180
                  ....*....|....*....|.
gi 517341756  169 atysKALARELAPDGIRVNCV 189
Cdd:pfam08659 157 ----DALAEYRRSQGLPATSI 173
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
156-252 5.25e-04

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 40.50  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET-------EFheRYSsrekLEQTRKSIPLQRLGTAEDCAP 228
Cdd:PRK08159 157 PHYNVMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTlaasgigDF--RYI----LKWNEYNAPLRRTVTIEEVGD 230
                         90       100
                 ....*....|....*....|....
gi 517341756 229 AYLFLAApSLSGYITGQVIEINGG 252
Cdd:PRK08159 231 SALYLLS-DLSRGVTGEVHHVDSG 253
PLN00015 PLN00015
protochlorophyllide reductase
13-138 5.74e-04

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 40.46  E-value: 5.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  13 VVTGAGRGIGLEVARQFLDCGAKVIVHTGRkpgrdlpDFLLTAESERRA-------LLLHADFSAVGGAAQFAEDALAFF 85
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKWHVVMACR-------DFLKAERAAKSAgmpkdsyTVMHLDLASLDSVRQFVDNFRRSG 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517341756  86 DRVDVLVNNAGTMLGRFPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAE 138
Cdd:PLN00015  74 RPLDVLVCNAAVYLPTAKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLKKSD 126
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
147-252 6.72e-04

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 40.11  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 147 SISALT-GGS----PGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHERYS-SREKLEQTRKSIPLQRL 220
Cdd:PRK06505 140 SMLTLTyGGStrvmPNYNVMGVAKAALEASVRYLAADYGPQGIRVNAISAGPVRTLAGAGIGdARAIFSYQQRNSPLRRT 219
                         90       100       110
                 ....*....|....*....|....*....|..
gi 517341756 221 GTAEDCAPAYLFLAApSLSGYITGQVIEINGG 252
Cdd:PRK06505 220 VTIDEVGGSALYLLS-DLSSGVTGEIHFVDSG 250
PRK07775 PRK07775
SDR family oxidoreductase;
3-196 6.81e-04

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 40.12  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   3 HPrlfENRNVVVTGAGRGIGLEVARQFLDCGAKVIVHTGR-KPGRDLPDFLLTAESERRALLLH-ADFSAVGGAAQFAED 80
Cdd:PRK07775   7 HP---DRRPALVAGASSGIGAATAIELAAAGFPVALGARRvEKCEELVDKIRADGGEAVAFPLDvTDPDSVKSFVAQAEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  81 ALAffdRVDVLVNNAGTML-GRfpAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAEGAAIVNTVSISALTGgSPGSS 159
Cdd:PRK07775  84 ALG---EIEVLVSGAGDTYfGK--LHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQ-RPHMG 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 517341756 160 IYSASKAFVATYSKALARELAPDGIRVNCVSPGTIET 196
Cdd:PRK07775 158 AYGAAKAGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
PRK06940 PRK06940
short chain dehydrogenase; Provisional
183-252 1.06e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 39.62  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517341756 183 GIRVNCVSPGTIETEFHERYSSREKLEQTRKSI---PLQRLGTAEDCAPAYLFLAAPSlSGYITGQVIEINGG 252
Cdd:PRK06940 191 GARINSISPGIISTPLAQDELNGPRGDGYRNMFaksPAGRPGTPDEIAALAEFLMGPR-GSFITGSDFLVDGG 262
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
12-194 1.08e-03

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 38.92  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIV---HTGRKPGRDLPdflltaeserRALLLHADFSAvggaaqfAEDALAFFDRV 88
Cdd:cd05226    1 ILILGATGFIGRALARELLEQGHEVTLlvrNTKRLSKEDQE----------PVAVVEGDLRD-------LDSLSDAVQGV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  89 DVLVNNAGTMLgrfpaatltdaeyeaVVRLNQTSVVALTRALLPALKAAeGAAIVNTVSISALTGGSPGSSIYSASKAFV 168
Cdd:cd05226   64 DVVIHLAGAPR---------------DTRDFCEVDVEGTRNVLEAAKEA-GVKHFIFISSLGAYGDLHEETEPSPSSPYL 127
                        170       180
                 ....*....|....*....|....*.
gi 517341756 169 ATYSKAlARELAPDGIRVNCVSPGTI 194
Cdd:cd05226  128 AVKAKT-EAVLREASLPYTIVRPGVI 152
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
8-97 1.21e-03

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 39.64  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756   8 ENRNVVVTGAGRGIG---LEVARQFldcGAKVIVHTgrkpgrdlpdfllTAESERRALLLHADFSAVGGAaqFAEDALAF 84
Cdd:PRK13771 162 KGETVLVTGAGGGVGihaIQVAKAL---GAKVIAVT-------------SSESKAKIVSKYADYVIVGSK--FSEEVKKI 223
                         90
                 ....*....|...
gi 517341756  85 FDrVDVLVNNAGT 97
Cdd:PRK13771 224 GG-ADIVIETVGT 235
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
78-252 1.51e-03

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 38.99  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  78 AEDALAFFDRVDVLVNN--AGTMLGRfPAATLTDAEYEAVVRLNQTSVVALTRALLPALKAAeGAAIVNTVSISALTGGS 155
Cdd:PLN02730 111 AESVKADFGSIDILVHSlaNGPEVTK-PLLETSRKGYLAAISASSYSFVSLLQHFGPIMNPG-GASISLTYIASERIIPG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 156 PGSSIYSAsKAFVATYSKALARELAPD-GIRVNCVSPGTIETEFHERYSSREKL-EQTRKSIPLQRLGTAEDCAPAYLFL 233
Cdd:PLN02730 189 YGGGMSSA-KAALESDTRVLAFEAGRKyKIRVNTISAGPLGSRAAKAIGFIDDMiEYSYANAPLQKELTADEVGNAAAFL 267
                        170
                 ....*....|....*....
gi 517341756 234 AAPsLSGYITGQVIEINGG 252
Cdd:PLN02730 268 ASP-LASAITGATIYVDNG 285
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
122-252 2.95e-03

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 38.26  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756 122 SVVALTRALLPALKAAegaAIVNTVSISALTGGSPGSSIYSASKAFVATYSKALARELAPDGIRVNCVSPGTIETEFHER 201
Cdd:PRK06997 123 SFPALAKAALPMLSDD---ASLLTLSYLGAERVVPNYNTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLAASG 199
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517341756 202 YSS-REKLEQTRKSIPLQRLGTAEDCAPAYLFLAAPSLSGyITGQVIEINGG 252
Cdd:PRK06997 200 IKDfGKILDFVESNAPLRRNVTIEEVGNVAAFLLSDLASG-VTGEITHVDSG 250
PRK06720 PRK06720
hypothetical protein; Provisional
12-96 3.41e-03

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 37.26  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517341756  12 VVVTGAGRGIGLEVARQFLDCGAKVIV-HTGRKPGRDLPDFLLTAESErrALLLHADFSAVGGAAQFAEDALAFFDRVDV 90
Cdd:PRK06720  19 AIVTGGGIGIGRNTALLLAKQGAKVIVtDIDQESGQATVEEITNLGGE--ALFVSYDMEKQGDWQRVISITLNAFSRIDM 96

                 ....*.
gi 517341756  91 LVNNAG 96
Cdd:PRK06720  97 LFQNAG 102
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
7-38 5.50e-03

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 35.53  E-value: 5.50e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 517341756    7 FENRNVVVTGAGRgIGLEVARQFLDCGAKVIV 38
Cdd:pfam13241   5 LRGKRVLVVGGGE-VAARKARKLLEAGAKVTV 35
 
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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