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Conserved domains on  [gi|497642378|ref|WP_009956562|]
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MULTISPECIES: SDR family oxidoreductase [Mycobacterium]

Protein Classification

SDR family NAD(P)-dependent oxidoreductase( domain architecture ID 11416738)

SDR family NAD(P)-dependent oxidoreductase, a short-chain dehydrogenase (SDR) family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
11-271 2.41e-54

Short-chain dehydrogenase [General function prediction only];


:

Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 176.21  E-value: 2.41e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAa 90
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVS 169
Cdd:COG0300   83 IDVLVNNAGVGGGGPFEEL-DLEDLRRVFEVNVFGPVRLTRALLPLMR----ARGRGrIVNVSSVAGLRGLPGMAAYAAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISeqsselatklMRWTGLSAEKVARTCLDAHDRGELYCMPQ 249
Cdd:COG0300  158 KAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAP----------AGRPLLSPEEVARAILRALERGRAEVYVG 227
                        250       260
                 ....*....|....*....|..
gi 497642378 250 FDAKVGWNIKRLAPQAYTRTAG 271
Cdd:COG0300  228 WDARLLARLLRLLPRLFDRLLR 249
 
Name Accession Description Interval E-value
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
11-271 2.41e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 176.21  E-value: 2.41e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAa 90
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVS 169
Cdd:COG0300   83 IDVLVNNAGVGGGGPFEEL-DLEDLRRVFEVNVFGPVRLTRALLPLMR----ARGRGrIVNVSSVAGLRGLPGMAAYAAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISeqsselatklMRWTGLSAEKVARTCLDAHDRGELYCMPQ 249
Cdd:COG0300  158 KAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAP----------AGRPLLSPEEVARAILRALERGRAEVYVG 227
                        250       260
                 ....*....|....*....|..
gi 497642378 250 FDAKVGWNIKRLAPQAYTRTAG 271
Cdd:COG0300  228 WDARLLARLLRLLPRLFDRLLR 249
PRK05650 PRK05650
SDR family oxidoreductase;
16-266 9.01e-54

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 175.61  E-value: 9.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLVI 95
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKW-GGIDVIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 NNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVSKAGVLS 175
Cdd:PRK05650  83 NNAGVASGGFFEEL-SLEDWDWQIAINLMGVVKGCKAFLPLFK--RQKSGR-IVNIASMAGLMQGPAMSSYNVAKAGVVA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 176 LSETLAAELAGTPVRVTVLCPTFVKTNILESGR-ISEQSSELATKLMRWTGLSAEKVARTCLDAHDRGELYCMPQFDAKV 254
Cdd:PRK05650 159 LSETLLVELADDEIGVHVVCPSFFQTNLLDSFRgPNPAMKAQVGKLLEKSPITAADIADYIYQQVAKGEFLILPHEQGRR 238
                        250
                 ....*....|..
gi 497642378 255 GWNIKRLAPQAY 266
Cdd:PRK05650 239 AWQLKRQAPQAL 250
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
15-236 1.36e-42

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: 145.50  E-value: 1.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADaITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAaPTLV 94
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGR-LDIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:cd05233   79 VNNAGIARPGPLEEL-TDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGR---IVNISSVAGLRPLPGQAAYAASKAALE 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMRWTGLSAEKVARTCL 236
Cdd:cd05233  155 GLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVV 216
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
15-206 1.10e-32

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 118.48  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   95 iNNaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESraprG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:pfam00106  83 -NN-AGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSG----GrIVNISSVAGLVPYPGGSAYSASKAAV 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 497642378  174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMTKE 189
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
15-205 8.99e-08

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: 51.94  E-value: 8.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDI-----DQTAAQKTA---DAITEQ-GGKAIAIRCDVSRFDEVQALAEQSQA 85
Cdd:TIGR04504   4 ALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpAVGYPLATRaelDAVAAAcPDQVLPVIADVRDPAALAAAVALAVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   86 WFPAAPTLVinnagvGAGGAAIGDAPL-----DDWAWTLGINLWGPIHGCHVFTPILRDAEsrAPRG--IINVASAAAFG 158
Cdd:TIGR04504  84 RWGRLDAAV------AAAGVIAGGRPLwettdAELDLLLDVNLRGVWNLARAAVPAMLARP--DPRGgrFVAVASAAATR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 497642378  159 AAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:TIGR04504 156 GLPHLAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLA 202
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
16-88 6.52e-06

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: 45.55  E-value: 6.52e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642378    16 VVTGAGSGIGAAFAVELGRRGGA--VVCS--DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrlVLLSrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80
 
Name Accession Description Interval E-value
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
11-271 2.41e-54

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 176.21  E-value: 2.41e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAa 90
Cdd:COG0300    4 TGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVS 169
Cdd:COG0300   83 IDVLVNNAGVGGGGPFEEL-DLEDLRRVFEVNVFGPVRLTRALLPLMR----ARGRGrIVNVSSVAGLRGLPGMAAYAAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISeqsselatklMRWTGLSAEKVARTCLDAHDRGELYCMPQ 249
Cdd:COG0300  158 KAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAP----------AGRPLLSPEEVARAILRALERGRAEVYVG 227
                        250       260
                 ....*....|....*....|..
gi 497642378 250 FDAKVGWNIKRLAPQAYTRTAG 271
Cdd:COG0300  228 WDARLLARLLRLLPRLFDRLLR 249
PRK05650 PRK05650
SDR family oxidoreductase;
16-266 9.01e-54

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 175.61  E-value: 9.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLVI 95
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKW-GGIDVIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 NNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVSKAGVLS 175
Cdd:PRK05650  83 NNAGVASGGFFEEL-SLEDWDWQIAINLMGVVKGCKAFLPLFK--RQKSGR-IVNIASMAGLMQGPAMSSYNVAKAGVVA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 176 LSETLAAELAGTPVRVTVLCPTFVKTNILESGR-ISEQSSELATKLMRWTGLSAEKVARTCLDAHDRGELYCMPQFDAKV 254
Cdd:PRK05650 159 LSETLLVELADDEIGVHVVCPSFFQTNLLDSFRgPNPAMKAQVGKLLEKSPITAADIADYIYQQVAKGEFLILPHEQGRR 238
                        250
                 ....*....|..
gi 497642378 255 GWNIKRLAPQAY 266
Cdd:PRK05650 239 AWQLKRQAPQAL 250
PRK06194 PRK06194
hypothetical protein; Provisional
12-248 2.49e-50

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 167.11  E-value: 2.49e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPaAP 91
Cdd:PRK06194   6 GKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFG-AV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDApLDDWAWTLGINLWGPIHGCHVFTPIL--RDAESRAPRG-IINVASAAAFGAAPGMAAYNV 168
Cdd:PRK06194  85 HLLFNNAGVGAGGLVWENS-LADWEWVLGVNLWGVIHGVRAFTPLMlaAAEKDPAYEGhIVNTASMAGLLAPPAMGIYNV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 169 SKAGVLSLSETLAA--ELAGTPVRVTVLCPTFVKTNILESGR-------------ISEQSSELATKLMRWTG-LSAEKVA 232
Cdd:PRK06194 164 SKHAVVSLTETLYQdlSLVTDQVGASVLCPYFVPTGIWQSERnrpadlantapptRSQLIAQAMSQKAVGSGkVTAEEVA 243
                        250
                 ....*....|....*.
gi 497642378 233 RTCLDAHDRGELYCMP 248
Cdd:PRK06194 244 QLVFDAIRAGRFYIYS 259
PRK05855 PRK05855
SDR family oxidoreductase;
15-270 6.86e-46

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 162.07  E-value: 6.86e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLV 94
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEH-GVPDIV 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDaesrapRG----IINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK05855 397 VNNAGIGMAGGFLDTSA-EDWDRVLDVNLWGVIHGCRLFGRQMVE------RGtgghIVNVASAAAYAPSRSLPAYATSK 469
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSE-------LATKLMRWTGLSAEKVARTCLDA--HDR 241
Cdd:PRK05855 470 AAVLMLSECLRAELAAAGIGVTAICPGFVDTNIVATTRFAGADAEdearrrgRADKLYQRRGYGPEKVAKAIVDAvkRNK 549
                        250       260
                 ....*....|....*....|....*....
gi 497642378 242 GELYCMPQfdAKVGWNIKRLAPQAYTRTA 270
Cdd:PRK05855 550 AVVPVTPE--AHAGYGVSRFAPWLLRSLA 576
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
1-236 8.36e-44

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: 149.17  E-value: 8.36e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   1 MFGLNkpkisrGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALA 80
Cdd:COG1028    1 MTRLK------GKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  81 EQSQAWFPaAPTLVINNaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAA 160
Cdd:COG1028   75 AAAVAAFG-RLDILVNN-AGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGR---IVNISSIAGLRGS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497642378 161 PGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATK---LMRWTglSAEKVARTCL 236
Cdd:COG1028  150 PGQAAYAASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAAripLGRLG--TPEEVAAAVL 226
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
10-241 2.11e-43

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: 147.64  E-value: 2.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  10 SRGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAWFpA 89
Cdd:COG4221    3 DKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEF-G 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVINNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNV 168
Cdd:COG4221   79 RLDVLVNNAGVALLGPLEEL-DPEDWDRMIDVNVKGVLYVTRAALPAMR----ARGSGhIVNISSIAGLRPYPGGAVYAA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATkLMRWTGLSAEKVARTCLDAHDR 241
Cdd:COG4221  154 TKAAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAV-YEGLEPLTPEDVAEAVLFALTQ 225
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
15-236 1.36e-42

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: 145.50  E-value: 1.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADaITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAaPTLV 94
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAA-IEALGGNAVAVQADVSDEEDVEALVEEALEEFGR-LDIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:cd05233   79 VNNAGIARPGPLEEL-TDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGR---IVNISSVAGLRPLPGQAAYAASKAALE 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMRWTGLSAEKVARTCL 236
Cdd:cd05233  155 GLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAIPLGRLGTPEEVAEAVV 216
FabG-like PRK07231
SDR family oxidoreductase;
12-206 2.54e-34

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 124.56  E-value: 2.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAItEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:PRK07231   5 GKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEI-LAGGRAIAVAADVSDEADVEAAVAAALERF-GSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK07231  83 DILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGA---IVNVASTAGLRPRPGLGWYNASKG 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:PRK07231 160 AVITLTKALAAELGPDKIRVNAVAPVVVETGLLEA 194
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
15-206 1.10e-32

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 118.48  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDILV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   95 iNNaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESraprG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:pfam00106  83 -NN-AGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSG----GrIVNISSVAGLVPYPGGSAYSASKAAV 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 497642378  174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:pfam00106 157 IGFTRSLALELAPHGIRVNAVAPGGVDTDMTKE 189
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
12-236 9.39e-32

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 117.57  E-value: 9.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:PRK05653   5 GKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAF-GAL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK05653  84 DILVNNAGITRDALLPRMSE-EDWDRVIDVNLTGTFNVVRAALPPMI--KARYGR-IVNISSVSGVTGNPGQTNYSAAKA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMRWTGlSAEKVARTCL 236
Cdd:PRK05653 160 GVIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEVKAEILKEIPLGRLG-QPEEVANAVA 223
PRK07832 PRK07832
SDR family oxidoreductase;
13-267 3.35e-31

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 117.07  E-value: 3.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  13 ASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRC-DVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIHAAHGSMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 tlVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdaeSRAPRG--IINVASAAAFGAAPGMAAYNVS 169
Cdd:PRK07832  81 --VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPM----VAAGRGghLVNVSSAAGLVALPWHAAYSAS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRI-----SEQSSELATKLMRWTGLSAEKVARTCLDAHDRGEL 244
Cdd:PRK07832 155 KFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPLVNTVEIagvdrEDPRVQKWVDRFRGHAVTPEKAAEKILAGVEKNRY 234
                        250       260
                 ....*....|....*....|...
gi 497642378 245 YCMPQFDAKVGWNIKRLAPQAYT 267
Cdd:PRK07832 235 LVYTSPDIRALYWFKRKAWWPYS 257
PRK05876 PRK05876
short chain dehydrogenase; Provisional
12-253 2.16e-30

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 115.05  E-value: 2.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSqAWFPAAP 91
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEA-FRLLGHV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPilRDAESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK05876  85 DVVFSNAGIVVGGPIVEMTH-DDWRWVIDVDLWGSIHTVEAFLP--RLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNIL-ESGRI-------SEQSSELATKLMRWTGLSAEKVARTCLDAHDRGE 243
Cdd:PRK05876 162 GVVGLAETLAREVTADGIGVSVLCPMVVETNLVaNSERIrgaacaqSSTTGSPGPLPLQDDNLGVDDIAQLTADAILANR 241
                        250
                 ....*....|
gi 497642378 244 LYCMPQFDAK 253
Cdd:PRK05876 242 LYVLPHAASR 251
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
12-206 3.11e-29

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: 111.04  E-value: 3.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:cd08944    3 GKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQI---AGGALALRVDVTDEQQVAALFERAVEEF-GGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaeSRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:cd08944   79 DLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMI---ARGGGSIVNLSSIAGQSGDPGYGAYGASKA 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:cd08944  156 AIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLA 190
PRK06181 PRK06181
SDR family oxidoreductase;
15-270 1.02e-27

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 107.37  E-value: 1.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:PRK06181   4 VIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDILV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 iNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdaesRAPRG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:PRK06181  84 -NNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHL-----KASRGqIVVVSSLAGLTGVPTRSGYAASKHAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILESGrISEQSSELATKLMRWTG-LSAEKVARTCLDAHDRGELYCMPQFDA 252
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATDIRKRA-LDGDGKPLGKSPMQESKiMSAEECAEAILPAIARRKRLLVMSLRG 236
                        250
                 ....*....|....*...
gi 497642378 253 KVGWNIKRLAPQAYTRTA 270
Cdd:PRK06181 237 RLGRWLKLIAPGLVDKIA 254
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
15-205 1.16e-27

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: 106.86  E-value: 1.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLV 94
Cdd:cd05333    3 ALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEF-GPVDIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAesRAPRgIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:cd05333   82 VNNAGITRDNLLMRMSE-EDWDAVINVNLTGVFNVTQAVIRAMIKR--RSGR-IINISSVVGLIGNPGQANYAASKAGVI 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:cd05333  158 GFTKSLAKELASRGITVNAVAPGFIDTDMTD 188
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
12-231 2.22e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 106.51  E-value: 2.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK12429   4 GKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK12429  84 ILV--NNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMK--AQGGGR-IINMASVHGLVGSAGKAAYVSAKH 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILEsGRISEQSSELatklmrwtGLSAEKV 231
Cdd:PRK12429 159 GLIGLTKVVALEGATHGVTVNAICPGYVDTPLVR-KQIPDLAKER--------GISEEEV 209
PRK07774 PRK07774
SDR family oxidoreductase;
15-210 5.42e-27

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 105.21  E-value: 5.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:PRK07774   9 AIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGIDYLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 iNNAG--VGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDaesRAPRGIINvasAAAFGAAPGMAAYNVSKAG 172
Cdd:PRK07774  89 -NNAAiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAK---RGGGAIVN---QSSTAAWLYSNFYGLAKVG 161
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 497642378 173 VLSLSETLAAELAGTPVRVTVLCPTFVKTnilESGRIS 210
Cdd:PRK07774 162 LNGLTQQLARELGGMNIRVNAIAPGPIDT---EATRTV 196
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
11-231 7.22e-26

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 102.67  E-value: 7.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK13394   6 NGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINnaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPilrdAESRAPRG--IINVASAAAFGAAPGMAAYNV 168
Cdd:PRK13394  86 DILVSN--AGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALK----HMYKDDRGgvVIYMGSVHSHEASPLKSAYVT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESgRISEQSSELatklmrwtGLSAEKV 231
Cdd:PRK13394 160 AKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDK-QIPEQAKEL--------GISEEEV 213
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
12-206 2.07e-25

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 101.08  E-value: 2.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:PRK06113  11 GKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKL-GKV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNagVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK06113  90 DILVNN--AGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGV---ILTITSMAAENKNINMTSYASSKA 164
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:PRK06113 165 AASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKS 199
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
15-212 2.81e-24

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: 98.03  E-value: 2.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:cd05365    2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 iNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:cd05365   82 -NNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGA---ILNISSMSSENKNVRIAAYGSSKAAVN 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQ 212
Cdd:cd05365  158 HMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPEI 195
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
22-236 6.79e-24

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: 96.73  E-value: 6.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   22 SGIGAAFAVELGRRGGAVVCSDIDqTAAQKTADAITEQGGKAIaIRCDVSRFDEVQALAEQSQAWFPaapTL--VINNA- 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLN-EALAKRVEELAEELGAAV-LPCDVTDEEQVEALVAAAVEKFG---RLdiLVNNAg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   99 GVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESraprgIINVASAAAFGAAPGMAAYNVSKAGVLSLSE 178
Cdd:pfam13561  81 FAPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGS-----IVNLSSIGAERVVPNYNAYGAAKAALEALTR 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642378  179 TLAAELAGTPVRVTVLCPTFVKT----NILESGRISEQSSELAtkLMRWTGlSAEKVARTCL 236
Cdd:pfam13561 156 YLAVELGPRGIRVNAISPGPIKTlaasGIPGFDELLAAAEARA--PLGRLG-TPEEVANAAA 214
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
12-203 3.53e-23

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: 95.14  E-value: 3.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVC---SDIDqtAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:cd05358    3 GKVALVTGASSGIGKAIAIRLATAGANVVVnyrSKED--AAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDaeSRAPRGIINVASAAAFGAAPGMAAYNV 168
Cdd:cd05358   81 TLDILV--NNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRK--SKIKGKIINMSSVHEKIPWPGHVNYAA 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:cd05358  157 SKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPI 191
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
11-205 5.29e-23

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: 94.35  E-value: 5.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:cd05347    4 KGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVSK 170
Cdd:cd05347   84 DILV--NNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMI--KQGHGK-IINICSLLSELGGPPVPAYAASK 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:cd05347  159 GGVAGLTKALATEWARHGIQVNAIAPGYFATEMTE 193
PRK12826 PRK12826
SDR family oxidoreductase;
11-201 5.33e-23

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 94.60  E-value: 5.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQAL-AEQSQAWfpA 89
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAvAAGVEDF--G 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAA-AFGAAPGMAAYNV 168
Cdd:PRK12826  83 RLDILVANAGIFPLTPFAEMDD-EQWERVIDVNLTGTFLLTQAALPALI--RAGGGR-IVLTSSVAgPRVGYPGLAHYAA 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK12826 159 SKAGLVGFTRALALELAARNITVNSVHPGGVDT 191
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
12-206 1.10e-22

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: 93.61  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:cd05345    5 GKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADI---GEAAIAIQADVTKRADVEAMVEAALSKF-GRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdaESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:cd05345   81 DILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHM---EEQGGGVIINIASTAGLRPRPGLTWYNASKG 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:cd05345  158 WVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSM 192
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
15-236 1.20e-22

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 93.37  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCS-DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:PRK05565   8 AIVTGASGGIGRAIAELLAKEGAKVVIAyDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:PRK05565  88 V--NNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGV---IVNISSIWGLIGASCEVLYSASKGAV 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMRWTGlSAEKVARTCL 236
Cdd:PRK05565 163 NAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEEDKEGLAEEIPLGRLG-KPEEIAKVVL 224
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
15-233 1.33e-22

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: 93.52  E-value: 1.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAApTLV 94
Cdd:cd05323    3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRV-DIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDAPLD-DWAWTLGINLWGPIHGCHVFTPILRDAESRAPRGIINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:cd05323   82 INNAGILDEKSYLFAGKLPpPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASKHGV 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497642378 174 LSLSETLAAEL-AGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMrwtglSAEKVAR 233
Cdd:cd05323  162 VGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPTQ-----SPEVVAK 217
PRK06138 PRK06138
SDR family oxidoreductase;
12-204 1.64e-22

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 93.29  E-value: 1.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEqGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK06138   5 GRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA-GGRAFARQGDVGSAEAVEALVDFVAARWGRLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK06138  84 VLV-NNAGFGCGGTVVTTDE-ADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGS---IVNTASQLALAGGRGRAAYVASKG 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNIL 204
Cdd:PRK06138 159 AIASLTRAMALDHATDGIRVNAVAPGTIDTPYF 191
PRK06172 PRK06172
SDR family oxidoreductase;
12-205 7.63e-22

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 91.35  E-value: 7.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:PRK06172   7 GKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAY-GRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK06172  86 DYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGA---IVNTASVAGLGAAPKMSIYAASKH 162
                        170       180       190
                 ....*....|....*....|....*....|....
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:PRK06172 163 AVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFR 196
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
15-266 1.02e-21

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: 90.76  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLV 94
Cdd:cd05339    2 VLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEV-GDVTIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDaesrAPRG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:cd05339   81 INN-AGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLE----RNHGhIVTIASVAGLISPAGLADYCASKAAA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 174 LSLSETLAAEL--AGTP-VRVTVLCPTFVKTNILESGRIseqSSELATKLMRWTGLsAEKVARTCLdaHDRGELyCMPQF 250
Cdd:cd05339  156 VGFHESLRLELkaYGKPgIKTTLVCPYFINTGMFQGVKT---PRPLLAPILEPEYV-AEKIVRAIL--TNQQML-YLPFY 228
                        250
                 ....*....|....*.
gi 497642378 251 dAKVGWNIKRLAPQAY 266
Cdd:cd05339  229 -AYFLPILKRTLPTPV 243
PRK12829 PRK12829
short chain dehydrogenase; Provisional
12-201 1.02e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 91.27  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:PRK12829  11 GLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARL--PGAKVTATVADVADPAQVERVFDTAVERF-GGL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK12829  88 DVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLK--ASGHGGVIIALSSVAGRLGYPGRTPYAASKW 165
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK12829 166 AVVGLVKSLAIELGPLGIRVNAILPGIVRG 195
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
12-243 1.50e-21

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: 90.39  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIT----EQGGKAIAIRCDVSRFDEVQALAEQSQAWF 87
Cdd:cd08939    1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEaeanASGQKVSYISADLSDYEEVEQAFAQAVEKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  88 pAAPTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVftpILRDAESRAPRGIINVASAAAFGAAPGMAAYN 167
Cdd:cd08939   81 -GPPDLVVNCAGISIPGLFEDLTA-EEFERGMDVNYFGSLNVAHA---VLPLMKEQRPGHIVFVSSQAALVGIYGYSAYC 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497642378 168 VSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILEsgrISEQSSELATKLMRWTG--LSAEKVARTCLDAHDRGE 243
Cdd:cd08939  156 PSKFALRGLAESLRQELKPYNIRVSVVYPPDTDTPGFE---EENKTKPEETKAIEGSSgpITPEEAARIIVKGLDRGY 230
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
12-221 2.96e-21

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 89.87  E-value: 2.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVV---CSDIDqtAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:PRK05557   5 GKVALVTGASRGIGRAIAERLAAQGANVVinyASSEA--GAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNV 168
Cdd:PRK05557  83 GVDILV-NNAGITRDNLLMRMKE-EDWDRVIDTNLTGVFNLTKAVARPMM--KQRSGR-IINISSVVGLMGNPGQANYAA 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESgrISEQSSELATKLM 221
Cdd:PRK05557 158 SKAGVIGFTKSLARELASRGITVNAVAPGFIETDMTDA--LPEDVKEAILAQI 208
PRK07069 PRK07069
short chain dehydrogenase; Validated
15-222 3.35e-21

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 89.77  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGK--AIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDInDAAGLDAFAAEINAAHGEgvAFAAVQDVTDEAQWQALLAQAADAMGGLS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAesrAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK07069  82 VLV--NNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRAS---QPASIVNISSVAAFKAEPDYTAYNASKA 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497642378 172 GVLSLSETLAAELA--GTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMR 222
Cdd:PRK07069 157 AVASLTKSIALDCArrGLDVRCNSIHPTFIRTGIVDPIFQRLGEEEATRKLAR 209
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
16-208 1.48e-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: 1.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLVi 95
Cdd:cd05360    4 VITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTWV- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 nNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaeSRAPRGIINVASAAAFGAAPGMAAYNVSKAGVLS 175
Cdd:cd05360   83 -NNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLR---RRGGGALINVGSLLGYRSAPLQAAYSASKHAVRG 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 176 LSETLAAELA--GTPVRVTVLCPTFVKTNILESGR 208
Cdd:cd05360  159 FTESLRAELAhdGAPISVTLVQPTAMNTPFFGHAR 193
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
12-218 1.49e-20

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: 87.72  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCS-DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAA 90
Cdd:cd05362    3 GKVALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAF-GG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHgchvftpILRDAESRAPRG--IINVASAAAFGAAPGMAAYNV 168
Cdd:cd05362   82 VDILVNNAGVMLKKPIAETSE-EEFDRMFTVNTKGAFF-------VLQEAAKRLRDGgrIINISSSLTAAYTPNYGAYAG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELAT 218
Cdd:cd05362  154 SKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAK 203
PRK07063 PRK07063
SDR family oxidoreductase;
11-207 1.59e-20

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 88.18  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITE--QGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:PRK07063   6 AGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARdvAGARVLAVPADVTDAASVAAAVAAAEEAFG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLViNNagvgaGGAAIGDAPL----DDWAWTLGINLWGPIHGCHVFTP--ILRDAESraprgIINVASAAAFGAAPG 162
Cdd:PRK07063  86 PLDVLV-NN-----AGINVFADPLamtdEDWRRCFAVDLDGAWNGCRAVLPgmVERGRGS-----IVNIASTHAFKIIPG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 497642378 163 MAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESG 207
Cdd:PRK07063 155 CFPYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDW 199
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
15-201 2.40e-20

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: 86.91  E-value: 2.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRG-GAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:cd05324    3 ALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 ViNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDaeSRAPRgIINVASAAAFGAAPgmaaYNVSKAGV 173
Cdd:cd05324   83 V-NNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKK--SPAGR-IVNVSSGLGSLTSA----YGVSKAAL 154
                        170       180
                 ....*....|....*....|....*...
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:cd05324  155 NALTRILAKELKETGIKVNACCPGWVKT 182
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
15-233 2.81e-20

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: 87.29  E-value: 2.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQktaDAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLV 94
Cdd:cd05374    3 VLITGCSSGIGLALALALAAQGYRVIATARNPDKLE---SLGELLNDNLEVLELDVTDEESIKAAVKEVIERF-GRIDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:cd05374   79 VNNAGYGLFGPLEET-SIEEVRELFEVNVFGPLRVTRAFLPLMR----KQGSGrIVNVSSVAGLVPTPFLGPYCASKAAL 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSE-------LATKLMRW------TGLSAEKVAR 233
Cdd:cd05374  154 EALSESLRLELAPFGIKVTIIEPGPVRTGFADNAAGSALEDPeispyapERKEIKENaagvgsNPGDPEKVAD 226
PRK06841 PRK06841
short chain dehydrogenase; Provisional
12-201 4.10e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 87.02  E-value: 4.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTAdaiTEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK06841  15 GKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAA---QLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRID 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK06841  92 ILV--NSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGK---IVNLASQAGVVALERHVAYCASKA 166
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK06841 167 GVVGMTKVLALEWGPYGITVNAISPTVVLT 196
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
15-202 6.19e-20

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: 86.74  E-value: 6.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLV 94
Cdd:cd08935    8 AVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQF-GTVDIL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 IN-----------NAGVGAGGAAIGDAPLDDWAW--TLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAP 161
Cdd:cd08935   87 INgaggnhpdattDPEHYEPETEQNFFDLDEEGWefVFDLNLNGSFLPSQVFGKDMLEQKGGS---IINISSMNAFSPLT 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 497642378 162 GMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTN 202
Cdd:cd08935  164 KVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
12-201 1.01e-19

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: 85.79  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDapLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:cd05344   81 ILVNNAGGPPPGPFAELT--DEDWLEAFDLKLLSVIRIVRAVLPGMK--ERGWGR-IVNISSLTVKEPEPNLVLSNVARA 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:cd05344  156 GLIGLVKTLSRELAPDGVTVNSVLPGYIDT 185
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-206 1.20e-19

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 85.31  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVC-SDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAA 90
Cdd:PRK12825   6 GRVALVTGAARGLGRAIALRLARAGADVVVhYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERF-GR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAesRAPRgIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK12825  85 IDILVNNAGIFEDKPLADMSD-DEWDEVIDVNLSGVFHLLRAVVPPMRKQ--RGGR-IVNISSVAGLPGWPGRSNYAAAK 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:PRK12825 161 AGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEA 196
PRK08264 PRK08264
SDR family oxidoreductase;
12-253 1.59e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 84.94  E-value: 1.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVcsdidqTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAwfpaaP 91
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGAAKV------YAAARDPESVTDLGPRVVPLQLDVTDPASVAAAAEAASD-----V 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdaESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK08264  75 TILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVL---AANGGGAIVNVLSVLSWVNFPNLGTYSASKA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNiLESGRISEQSselatklmrwtglSAEKVARTCLDAHDRGELYCMPQFD 251
Cdd:PRK08264 152 AAWSLTQALRAELAPQGTRVLGVHPGPIDTD-MAAGLDAPKA-------------SPADVARQILDALEAGDEEVLPDEM 217

                 ..
gi 497642378 252 AK 253
Cdd:PRK08264 218 AR 219
PRK06484 PRK06484
short chain dehydrogenase; Validated
11-204 1.61e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 87.98  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSL---GPDHHALAMDVSDEAQIREGFEQLHREFGRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdAESRAPRGIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK06484  81 DVLVNNAGVTDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLM--IEQGHGAAIVNVASGAGLVALPKRTAYSASK 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNIL 204
Cdd:PRK06484 159 AAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMV 192
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
15-206 2.19e-19

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: 84.71  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVC---SDIDqtAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd05359    1 ALVTGGSRGIGKAIALRLAERGADVVInyrKSKD--AAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDA-ESRaprgIINVASAAAFGAAPGMAAYNVSK 170
Cdd:cd05359   79 VLV-SNAAAGAFRPLSELTP-AHWDAKMNTNLKALVHCAQQAAKLMRERgGGR----IVAISSLGSIRALPNYLAVGTAK 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:cd05359  153 AALEALVRYLAVELGPRGIRVNAVSPGVIDTDALAH 188
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
12-204 2.26e-19

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 84.67  E-value: 2.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCS-DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK12935   6 GKVAIVTGGAKGIGKAITVALAQEGAKVVINyNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK12935  86 DILV--NNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGR---IISISSIIGQAGGFGQTNYSAAK 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNIL 204
Cdd:PRK12935 161 AGMLGFTKSLALELAKTNVTVNAICPGFIDTEMV 194
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
12-220 2.60e-19

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: 84.28  E-value: 2.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQktadAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd05370    5 GNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLA----EAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaeSRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:cd05370   81 ILINNAGIQRPIDLRDPASDLDKADTEIDTNLIGPIRLIKAFLPHLK---KQPEATIVNVSSGLAFVPMAANPVYCATKA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKL 220
Cdd:cd05370  158 ALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKMPL 206
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
14-223 2.95e-19

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 84.74  E-value: 2.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  14 SAVVTGAGSGIGAAFAVELGRRGGAVVCSDID-QTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPT 92
Cdd:cd05366    4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNlEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSFDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAESRAPrgIINVASAAAFGAAPGMAAYNVSKAG 172
Cdd:cd05366   84 MV-NNAGIAPITPLLTITE-EDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGK--IINASSIAGVQGFPNLGAYSASKFA 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497642378 173 VLSLSETLAAELAGTPVRVTVLCPTFVKTNILEsgRISEQSSELATKLMRW 223
Cdd:cd05366  160 VRGLTQTAAQELAPKGITVNAYAPGIVKTEMWD--YIDEEVGEIAGKPEGE 208
PRK12939 PRK12939
short chain dehydrogenase; Provisional
12-212 3.89e-19

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 84.25  E-value: 3.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK12939  87 GLV--NNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGR---IVNLASDTALWGAPKLGAYVASKG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQ 212
Cdd:PRK12939 162 AVIGMTRSLARELGGRGITVNAIAPGLTATEATAYVPADER 202
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
15-223 4.32e-19

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 84.01  E-value: 4.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLV 94
Cdd:PRK08643   5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTF-GDLNVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdAESRAPRgIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:PRK08643  84 VNNAGVAPTTPIETITE-EQFDKVYNINVGGVIWGIQAAQEAFK-KLGHGGK-IINATSQAGVVGNPELAVYSSTKFAVR 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILESgrISEQSSELATKLMRW 223
Cdd:PRK08643 161 GLTQTAARDLASEGITVNAYAPGIVKTPMMFD--IAHQVGENAGKPDEW 207
PRK07825 PRK07825
short chain dehydrogenase; Provisional
11-201 4.37e-19

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 84.22  E-value: 4.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqgGKAIAIRCDVSRFDEVQA-LAEQSQAWFPA 89
Cdd:PRK07825   4 RGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL----GLVVGGPLDVTDPASFAAfLDAVEADLGPI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 apTLVINNAGVGAGGaaigdaPLDDWA-----WTLGINLWGPIHGCHVFTPILRdaesraPRG---IINVASAAAFGAAP 161
Cdd:PRK07825  80 --DVLVNNAGVMPVG------PFLDEPdavtrRILDVNVYGVILGSKLAAPRMV------PRGrghVVNVASLAGKIPVP 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497642378 162 GMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK07825 146 GMATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNT 185
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
12-233 6.36e-19

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: 83.36  E-value: 6.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd08934    3 GKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaeSRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:cd08934   83 ILV--NNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHL---LRNKGTIVNISSVAGRVAVRNSAVYNATKF 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNIleSGRISEQSSELATK--LMRWTGLSAEKVAR 233
Cdd:cd08934  158 GVNAFSEGLRQEVTERGVRVVVIEPGTVDTEL--RDHITHTITKEAYEerISTIRKLQAEDIAA 219
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
11-205 6.49e-19

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: 83.65  E-value: 6.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTA--DAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:cd08940    1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVraGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDaesrapRG---IINVASAAAFGAAPGMAA 165
Cdd:cd08940   81 GVDILV--NNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKK------QGwgrIINIASVHGLVASANKSA 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497642378 166 YNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:cd08940  153 YVAAKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVE 192
PRK07454 PRK07454
SDR family oxidoreductase;
7-236 7.65e-19

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 83.08  E-value: 7.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   7 PKISRGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAW 86
Cdd:PRK07454   1 MSLNSMPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  87 FpAAPTLVINNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRDAESraprG-IINVASAAAFGAAPGMAA 165
Cdd:PRK07454  81 F-GCPDVLINNAGMAYTGPLLEM-PLSDWQWVIQLNLTSVFQCCSAVLPGMRARGG----GlIINVSSIAARNAFPQWGA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497642378 166 YNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRIseQSSelatkLMRWTGLSAEKVARTCL 236
Cdd:PRK07454 155 YCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPLWDTETV--QAD-----FDRSAMLSPEQVAQTIL 218
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
11-203 7.76e-19

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 83.62  E-value: 7.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPA 89
Cdd:PRK08936   6 EGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGChvftpilRDA-----ESRAPRGIINVASAAAFGAAPGMA 164
Cdd:PRK08936  86 LDVMI--NNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGS-------REAikyfvEHDIKGNIINMSSVHEQIPWPLFV 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:PRK08936 157 HYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPI 195
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
12-213 9.81e-19

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: 82.89  E-value: 9.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIaiRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd05326    4 GKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFV--HCDVTVEADVRAAVDTAVARFGRLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPihgchvFTPILRDAESRAPRG---IINVASAAAFGAAPGMAAYNV 168
Cdd:cd05326   82 IMFNNAGVLGAPCYSILETSLEEFERVLDVNVYGA------FLGTKHAARVMIPAKkgsIVSVASVAGVVGGLGPHAYTA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQS 213
Cdd:cd05326  156 SKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDE 200
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
11-264 1.17e-18

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: 83.02  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGK-AIAIRCDVSRFDEVQALAEQSQAWFPA 89
Cdd:cd05332    2 QGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPsPHVVPLDMSDLEDAEQVVEEALKLFGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVINnaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESraprG-IINVASAAAFGAAPGMAAYNV 168
Cdd:cd05332   82 LDILINN--AGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQ----GsIVVVSSIAGKIGVPFRTAYAA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI-----LESGRISEQSSELATKlmrwtGLSAEKVARTCLDAHDRG- 242
Cdd:cd05332  156 SKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIamnalSGDGSMSAKMDDTTAN-----GMSPEECALEILKAIALRk 230
                        250       260
                 ....*....|....*....|...
gi 497642378 243 -ELYcMPQFDAKVGWNIKRLAPQ 264
Cdd:cd05332  231 rEVF-YARQVPLLAVYLRQLFPG 252
PRK06114 PRK06114
SDR family oxidoreductase;
11-201 2.03e-18

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 82.14  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPA 89
Cdd:PRK06114   7 DGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLrTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELGA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGpihgchVFTPILRDAESRAPRG---IINVASAAAFGA--APGMA 164
Cdd:PRK06114  87 LTLAV--NAAGIANANPAEEMEEEQWQTVMDINLTG------VFLSCQAEARAMLENGggsIVNIASMSGIIVnrGLLQA 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK06114 159 HYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
PRK07035 PRK07035
SDR family oxidoreductase;
12-201 2.36e-18

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 81.99  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK07035   8 GKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK07035  88 ILV-NNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGS---IVNVASVNGVSPGDFQGIYSITKA 163
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK07035 164 AVISMTKAFAKECAPFGIRVNALLPGLTDT 193
PRK06139 PRK06139
SDR family oxidoreductase;
10-201 2.67e-18

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 83.23  E-value: 2.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  10 SRGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAwFPA 89
Cdd:PRK06139   5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAAS-FGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVINNaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAEsrapRGI-INVASAAAFGAAPGMAAYNV 168
Cdd:PRK06139  84 RIDVWVNN-VGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQG----HGIfINMISLGGFAAQPYAAAYSA 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 497642378 169 SKAGVLSLSETLAAELAGTP-VRVTVLCPTFVKT 201
Cdd:PRK06139 159 SKFGLRGFSEALRGELADHPdIHVCDVYPAFMDT 192
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
6-236 2.93e-18

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 84.51  E-value: 2.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   6 KPKISRGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQgGKAIAIRCDVSRFDEVQALAEQsqa 85
Cdd:PRK08324 416 KPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGP-DRALGVACDVTDEAAVQAAFEE--- 491
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  86 wfpAAPT-----LVINNaGVGAGGAAIGDAPLDDWAWTLGINLWGpihgchVFTpILRDAES---RAPRG--IINVASAA 155
Cdd:PRK08324 492 ---AALAfggvdIVVSN-AGIAISGPIEETSDEDWRRSFDVNATG------HFL-VAREAVRimkAQGLGgsIVFIASKN 560
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 156 AFGAAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPT--FVKTNILESGRISEQSselATKLMRWTGLSAEKVAR 233
Cdd:PRK08324 561 AVNPGPNFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDavVRGSGIWTGEWIEARA---AAYGLSEEELEEFYRAR 637

                 ...
gi 497642378 234 TCL 236
Cdd:PRK08324 638 NLL 640
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
12-203 5.48e-18

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: 80.84  E-value: 5.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGG-KAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:cd05352    8 GKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGvKTKAYKCDVSSQESVEKTFKQIQKDFGKI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGdaPLDDWAWTLGINLWGPIHGCHVFTPILRD-------AESRAPRGIINVASAAAFgaapgm 163
Cdd:cd05352   88 DILIANAGITVHKPALDY--TYEQWNKVIDVNLNGVFNCAQAAAKIFKKqgkgsliITASMSGTIVNRPQPQAA------ 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497642378 164 aaYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:cd05352  160 --YNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL 197
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
12-222 5.62e-18

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: 80.89  E-value: 5.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd05341    5 GKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAEL---GDAARFFHLDVTDEDGWTAVVDTAREAFGRLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAEsrapRG-IINVASAAAFGAAPGMAAYNVSK 170
Cdd:cd05341   82 VLV--NNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAG----GGsIINMSSIEGLVGDPALAAYNASK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497642378 171 AGVLSLSETLAAELA--GTPVRVTVLCPTFVKTNILESGRISEQSSEL--ATKLMR 222
Cdd:cd05341  156 GAVRGLTKSAALECAtqGYGIRVNSVHPGYIYTPMTDELLIAQGEMGNypNTPMGR 211
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
15-201 9.52e-18

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: 80.19  E-value: 9.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAitEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLV 94
Cdd:cd05349    3 VLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAA--EAGERAIAIQADVRDRDQVQAMIEEAKNHF-GPVDTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDAPLDDWAW-----TLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVS 169
Cdd:cd05349   80 VNNALIDFPFDPDQRKTFDTIDWedyqqQLEGAVKGALNLLQAVLPDFK--ERGSGR-VINIGTNLFQNPVVPYHDYTTA 156
                        170       180       190
                 ....*....|....*....|....*....|..
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:cd05349  157 KAALLGFTRNMAKELGPYGITVNMVSGGLLKV 188
PRK05867 PRK05867
SDR family oxidoreductase;
11-205 1.58e-17

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 79.69  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK05867   8 HGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINnaGVGAGGAAIGDAPLDDWAWTLGINLWGpihgchVFTPILRDAESRAPRG--------------IINVasaaa 156
Cdd:PRK05867  88 DIAVCN--AGIITVTPMLDMPLEEFQRLQNTNVTG------VFLTAQAAAKAMVKQGqggviintasmsghIINV----- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 497642378 157 fgaAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:PRK05867 155 ---PQQVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVE 200
PRK12937 PRK12937
short chain dehydrogenase; Provisional
15-221 1.81e-17

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 79.40  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:PRK12937   8 AIVTGASRGIGAAIARRLAADGFAVAVNYAgSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRIDVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VinNAGVGAGGAAIGDAPLDDWAWTLGINLWGpihgchVFTpILRDAESRAPRG--IINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK12937  88 V--NNAGVMPLGTIADFDLEDFDRTIATNLRG------AFV-VLREAARHLGQGgrIINLSTSVIALPLPGYGPYAASKA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELAtKLM 221
Cdd:PRK12937 159 AVEGLVHVLANELRGRGITVNAVAPGPVATELFFNGKSAEQIDQLA-GLA 207
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
15-206 2.09e-17

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: 78.94  E-value: 2.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAqktaDAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLv 94
Cdd:cd08932    3 ALVTGASRGIGIEIARALARDGYRVSLGLRNPEDL----AALSASGGDVEAVPYDARDPEDARALVDALRDRFGRIDVL- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:cd08932   78 VHNAGIGRPTTLREGSD-AELEAHFSINVIAPAELTRALLPALR----EAGSGrVVFLNSLSGKRVLAGNAGYSASKFAL 152
                        170       180       190
                 ....*....|....*....|....*....|...
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:cd08932  153 RALAHALRQEGWDHGVRVSAVCPGFVDTPMAQG 185
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
11-205 4.11e-17

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: 78.64  E-value: 4.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:cd05329    5 EGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGGK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSK 170
Cdd:cd05329   85 LNILVNNAGTNIRKEAKDYTE-EDYSLIMSTNFEAAYHLSRLAHPLLKASGNGN---IVFISSVAGVIAVPSGAPYGATK 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:cd05329  161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVE 195
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
17-202 1.02e-16

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: 77.51  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  17 VTGAGSGIGAAFAVELGRRGGAV-VCSdidqtAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLVI 95
Cdd:COG3967   10 ITGGTSGIGLALAKRLHARGNTViITG-----RREEKLEEAAAANPGLHTIVLDVADPASIAALAEQVTAEFPDLNVLIN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 NNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:COG3967   85 NAGIMRAEDLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLK----AQPEAaIVNVSSGLAFVPLAVTPTYSATKAALH 160
                        170       180
                 ....*....|....*....|....*...
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTN 202
Cdd:COG3967  161 SYTQSLRHQLKDTSVKVIELAPPAVDTD 188
PRK08589 PRK08589
SDR family oxidoreductase;
15-205 1.17e-16

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 77.51  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQtAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLv 94
Cdd:PRK08589   9 AVITGASTGIGQASAIALAQEGAYVLAVDIAE-AVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDVL- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESraprGIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:PRK08589  87 FNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGG----SIINTSSFSGQAADLYRSGYNAAKGAVI 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:PRK08589 163 NFTKSIAIEYGRDGIRANAIAPGTIETPLVD 193
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-216 2.08e-16

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 76.75  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVcsdIDQTAAQKTADAITEQGGkaIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK06463   6 KGKVALITGGTRGIGRAIAEAFLREGAKVA---VLYNSAENEAKELREKGV--FTIKCDVGNRDQVKKSKEVVEKEFGRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLViNNAGVGAGGaaigdaPLDDW-----AWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAA 165
Cdd:PRK06463  81 DVLV-NNAGIMYLM------PFEEFdeekyNKMIKINLNGAIYTTYEFLPLLKLSKNGA---IVNIASNAGIGTAAEGTT 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497642378 166 -YNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSEL 216
Cdd:PRK06463 151 fYAITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEAEKL 202
PRK07326 PRK07326
SDR family oxidoreductase;
11-202 2.66e-16

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 76.20  E-value: 2.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAItEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAA 90
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAEL-NNKGNVLGLAADVRDEADVQRAVDAIVAAF-GG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAESRaprgIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK07326  83 LDVLIANAGVGHFAPVEELTP-EEWRLVIDTNLTGAFYTIKAAVPALKRGGGY----IINISSLAGTNFFAGGAAYNASK 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTN 202
Cdd:PRK07326 158 FGLVGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
PRK06484 PRK06484
short chain dehydrogenase; Validated
7-213 3.04e-16

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 78.35  E-value: 3.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   7 PKISRGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAW 86
Cdd:PRK06484 264 PLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEAL---GDEHLSVQADITDEAAVESAFAQIQAR 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  87 FpAAPTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHgchvftpILRDAESRAPRG--IINVASAAAFGAAPGMA 164
Cdd:PRK06484 341 W-GRLDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFA-------CARAAARLMSQGgvIVNLGSIASLLALPPRN 412
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT----NILESGRISEQS 213
Cdd:PRK06484 413 AYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETpavlALKASGRADFDS 465
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
11-196 1.03e-15

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: 74.74  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCS-------------DIDQTAAQkTADAITEQGGKAIAIRCDVSRFDEVQ 77
Cdd:cd05338    2 SGKVAFVTGASRGIGRAIALRLAKAGATVVVAaktasegdngsakSLPGTIEE-TAEEIEAAGGQALPIVVDVRDEDQVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  78 ALAEQSQAWFPAAPTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAA 156
Cdd:cd05338   81 ALVEATVDQFGRLDILV--NNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMV----KAGQGhILNISPPLS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497642378 157 FGAAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCP 196
Cdd:cd05338  155 LRPARGDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWP 194
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
15-237 1.06e-15

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 74.69  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGG--KAIAIRCDVSRFDEVQALAEQSQAWFPAAPT 92
Cdd:PRK12384   5 AVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGegMAYGFGADATSEQSVLALSRGVDEIFGRVDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LVINnaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPIL-RDAESraprG-IINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK12384  85 LVYN--AGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMiRDGIQ----GrIIQINSKSGKVGSKHNSGYSAAK 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPtfvkTNILESGRISEQSSELATKLmrwtGLSAEKVARTCLD 237
Cdd:PRK12384 159 FGGVGLTQSLALDLAEYGITVHSLML----GNLLKSPMFQSLLPQYAKKL----GIKPDEVEQYYID 217
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
15-223 1.08e-15

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: 74.81  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:cd05337    4 AIVTGASRGIGRAIATELAARGFDIAINDLpDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPIL---RDAESRAPRGIINVASAAAFGAAPGMAAYNVSK 170
Cdd:cd05337   84 VNNAGIAVRPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMveqPDRFDGPHRSIIFVTSINAYLVSPNRGEYCISK 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESG--RISEQSSELATKLMRW 223
Cdd:cd05337  164 AGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVkeKYDELIAAGLVPIRRW 218
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
15-184 1.13e-15

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 74.74  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCS-DIDQTAAQKTADaitEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:PRK08642   8 VLVTGGSRGLGAAIARAFAREGARVVVNyHQSEDAAEALAD---ELGDRAIALQADVTDREQVQAMFATATEHFGKPITT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIGDAPLDDWAWT-LGINLWGPIHGC-HVFTPILRDAESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK08642  85 VVNNALADFSFDGDARKKADDITWEdFQQQLEGSVKGAlNTIQAALPGMREQGFGRIINIGTNLFQNPVVPYHDYTTAKA 164
                        170
                 ....*....|...
gi 497642378 172 GVLSLSETLAAEL 184
Cdd:PRK08642 165 ALLGLTRNLAAEL 177
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
15-201 1.73e-15

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: 73.90  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLV 94
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAEL-GGLDLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRDaesRAPRGIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:cd05350   80 IINAGVGKGTSLGDL-SFKAFRETIDTNLLGAAAILEAALPQFRA---KGRGHLVLISSVAALRGLPGAAAYSASKAALS 155
                        170       180
                 ....*....|....*....|....*..
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:cd05350  156 SLAESLRYDVKKRGIRVTVINPGFIDT 182
PRK06057 PRK06057
short chain dehydrogenase; Provisional
12-205 2.23e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 74.00  E-value: 2.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADaitEQGGkaIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK06057   7 GRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAAD---EVGG--LFVPTDVTDEDAVNALFDTAAETYGSVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVAS-AAAFGAAPGMAAYNVS 169
Cdd:PRK06057  82 IAFNNAGISPPEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMV----RQGKGsIINTASfVAVMGSATSQISYTAS 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:PRK06057 158 KGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQ 193
PRK07062 PRK07062
SDR family oxidoreductase;
12-230 2.81e-15

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 73.54  E-value: 2.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAfAVELGRRGGAVV--CS-DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:PRK07062   8 GRVAVVTGGSSGIGLA-TVELLLEAGASVaiCGrDEERLASAEARLREKFPGARLLAARCDVLDEADVAAFAAAVEARFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNV 168
Cdd:PRK07062  87 GVDMLV--NNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAAS---IVCVNSLLALQPEPHMVATSA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRV-TVLcptfvkTNILESG---RISEQSSELATKLMRWTGLSAEK 230
Cdd:PRK07062 162 ARAGLLNLVKSLATELAPKGVRVnSIL------LGLVESGqwrRRYEARADPGQSWEAWTAALARK 221
PRK08267 PRK08267
SDR family oxidoreductase;
17-269 2.92e-15

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 73.43  E-value: 2.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  17 VTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITeqGGKAIAIRCDVSRFDEVQ-ALAEQSQAwfpAAPTL-- 93
Cdd:PRK08267   6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELG--AGNAWTGALDVTDRAAWDaALADFAAA---TGGRLdv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRDA-ESRaprgIINVASAAAFGAAPGMAAYNVSKAG 172
Cdd:PRK08267  81 LFNNAGILRGGPFEDI-PLEAHDRVIDINVKGVLNGAHAALPYLKATpGAR----VINTSSASAIYGQPGLAVYSATKFA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 173 VLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGriseqSSELATKLMRWTG--LSAEKVARTCLDA-HDRGELYCMPQ 249
Cdd:PRK08267 156 VRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGT-----SNEVDAGSTKRLGvrLTPEDVAEAVWAAvQHPTRLHWPVG 230
                        250       260
                 ....*....|....*....|
gi 497642378 250 FDAKVGWNIKRLAPQAYTRT 269
Cdd:PRK08267 231 KQAKLLAFLARLSPGFVRRL 250
PRK05866 PRK05866
SDR family oxidoreductase;
11-201 2.95e-15

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 74.01  E-value: 2.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK05866  39 TGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGV 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHgchvftPILRDAESRAPRG---IINVAS-AAAFGAAPGMAAY 166
Cdd:PRK05866 119 DILINNAGRSIRRPLAESLDRWHDVERTMVLNYYAPLR------LIRGLAPGMLERGdghIINVATwGVLSEASPLFSVY 192
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 167 NVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK05866 193 NASKAALSAVSRVIETEWGDRGVHSTTLYYPLVAT 227
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
15-202 4.17e-15

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 73.40  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWF------- 87
Cdd:PRK08277  13 AVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFgpcdili 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  88 -------PAApTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAA 160
Cdd:PRK08277  93 ngaggnhPKA-TTDNEFHELIEPTKTFFDLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGN---IINISSMNAFTPL 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 497642378 161 PGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTN 202
Cdd:PRK08277 169 TKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
12-204 6.20e-15

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: 72.86  E-value: 6.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQK-TADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:cd09763    3 GKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPgTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDA------PLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRGIINVASAAAFGAAPGMA 164
Cdd:cd09763   83 LDILVNNAYAAVQLILVGVAkpfweePPTIWDDINNVGLRAHYACSVYAAPLMV----KAGKGLIVIISSTGGLEYLFNV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNIL 204
Cdd:cd09763  159 AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELV 198
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-203 7.28e-15

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 72.03  E-value: 7.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK07666   6 QGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLvINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHgchVFTPILRDAESRAPRGIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK07666  86 DIL-INNAGISKFGKFLELDP-AEWEKIIQVNLMGVYY---ATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASK 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:PRK07666 161 FGVLGLTESLMQEVRKHNIRVTALTPSTVATDM 193
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
12-236 8.78e-15

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: 72.04  E-value: 8.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAiTEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd08943    1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEA-AQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINnaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG--IINVASAAAFGAAPGMAAYNVS 169
Cdd:cd08943   80 IVVSN--AGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMK----SQGIGgnIVFNASKNAVAPGPNAAAYSAA 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPtfvkTNILESGRISEQSSELATKLMRwtGLSAEK-VARTCL 236
Cdd:cd08943  154 KAAEAHLARCLALEGGEDGIRVNTVNP----DAVFRGSKIWEGVWRAARAKAY--GLLEEEyRTRNLL 215
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
13-196 8.96e-15

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: 71.92  E-value: 8.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  13 ASAVVTGAGSGIGAAFAVELGRRGGAVVCS-DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHyNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAesrAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:cd05357   81 VLV--NNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGS---RNGSIINIIDAMTDRPLTGYFAYCMSKA 155
                        170       180
                 ....*....|....*....|....*.
gi 497642378 172 GVLSLSETLAAELAgtP-VRVTVLCP 196
Cdd:cd05357  156 ALEGLTRSAALELA--PnIRVNGIAP 179
PRK07109 PRK07109
short chain dehydrogenase; Provisional
15-201 9.39e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 73.03  E-value: 9.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:PRK07109  11 VVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGPIDTWV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 inNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:PRK07109  91 --NNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMR----PRDRGaIIQVGSALAYRSIPLQSAYCAAKHAI 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 174 LSLSETLAAEL--AGTPVRVTVLCPTFVKT 201
Cdd:PRK07109 165 RGFTDSLRCELlhDGSPVSVTMVQPPAVNT 194
PRK06500 PRK06500
SDR family oxidoreductase;
12-201 1.99e-14

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 71.14  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKtadAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK06500   6 GKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEA---ARAELGESALVIRADAGDVAAQKALAQALAEAFGRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINnagvgagGAAIGDAPLDDW---AW--TLGINLWGPIHGCHVFTPILRDAESRAPRGIINVASAAAFGAApgmaaY 166
Cdd:PRK06500  83 AVFIN-------AGVAKFAPLEDWdeaMFdrSFNTNVKGPYFLIQALLPLLANPASIVLNGSINAHIGMPNSSV-----Y 150
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 167 NVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK06500 151 AASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQT 185
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
14-238 5.56e-14

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: 69.46  E-value: 5.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  14 SAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADaitEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:cd08929    2 AALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAA---QELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINnaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesraPRG---IINVASAAAFGAAPGMAAYNVSK 170
Cdd:cd08929   79 VNN--AGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALL------RRGggtIVNVGSLAGKNAFKGGAAYNASK 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNIleSGRISEQSselatklmrWTgLSAEKVARTCLDA 238
Cdd:cd08929  151 FGLLGLSEAAMLDLREANIRVVNVMPGSVDTGF--AGSPEGQA---------WK-LAPEDVAQAVLFA 206
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
11-253 5.80e-14

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: 69.36  E-value: 5.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVV---CSDIDQTAaqktaDAITEQGGKAIAIRCDVSRFDEVQALAEQSQAwf 87
Cdd:cd05354    2 KDKTVLVTGANRGIGKAFVESLLAHGAKKVyaaVRDPGSAA-----HLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  88 paaPTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAY 166
Cdd:cd05354   75 ---VDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLK----ANGGGaIVNLNSVASLKNFPAMGTY 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 167 NVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELatklmrwtglsaekVARTCLDAHDRGELYC 246
Cdd:cd05354  148 SASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPKESPET--------------VAEAVLKALKAGEFHV 213

                 ....*..
gi 497642378 247 MPQFDAK 253
Cdd:cd05354  214 FPDEMAK 220
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
12-206 9.14e-14

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 69.24  E-value: 9.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTAdaitEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd05371    2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA----KLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLV----INNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILR--DAESRAPRG-IINVASAAAFGAAPGMA 164
Cdd:cd05371   78 IVVncagIAVAAKTYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGknEPDQGGERGvIINTASVAAFEGQIGQA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:cd05371  158 AYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAG 199
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
15-201 1.12e-13

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: 68.85  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQ-GGKAIAIRCDVSRFDEVQ-ALAEQSQAWfpAAPT 92
Cdd:cd05346    3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKfPVKVLPLQLDVSDRESIEaALENLPEEF--RDID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPIL--RDAESraprgIINVASAAAFGAAPGMAAYNVSK 170
Cdd:cd05346   81 ILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMiaRNQGH-----IINLGSIAGRYPYAGGNVYCATK 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:cd05346  156 AAVRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-196 1.19e-13

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 69.43  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQT-AAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWfpAA 90
Cdd:PRK07792  12 GKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASAlDASDVLDEIRAAGAKAVAVAGDISQRATADELVATAVGL--GG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdAESRAPRG-----IINVASAAAFGAAPGMAA 165
Cdd:PRK07792  90 LDIVVNNAGITRDRMLFNMSD-EEWDAVIAVHLRGHFLLTRNAAAYWR-AKAKAAGGpvygrIVNTSSEAGLVGPVGQAN 167
                        170       180       190
                 ....*....|....*....|....*....|.
gi 497642378 166 YNVSKAGVLSLSETLAAELAGTPVRVTVLCP 196
Cdd:PRK07792 168 YGAAKAGITALTLSAARALGRYGVRANAICP 198
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
12-266 1.86e-13

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: 68.41  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVV--CSDIDQtaAQKTADAITEQGG--KAIAIRCDVSRFDEVQALAEQSQAWF 87
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIiaCRNEEK--GEEAAAEIKKETGnaKVEVIQLDLSSLASVRQFAEEFLARF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  88 PAAPTLvINNAGVGAGGAAIGDaplDDWAWTLGINLWGPIHGCHVFTPILRDaeSRAPRgIINV--------------AS 153
Cdd:cd05327   79 PRLDIL-INNAGIMAPPRRLTK---DGFELQFAVNYLGHFLLTNLLLPVLKA--SAPSR-IVNVssiahragpidfndLD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 154 AAAFGAAPGMAAYNVSK-AGVLSLSEtLAAELAGTPVRVTVLCPTFVKTNILesgRISEQSSELATKLMRWTGLSAEKVA 232
Cdd:cd05327  152 LENNKEYSPYKAYGQSKlANILFTRE-LARRLEGTGVTVNALHPGVVRTELL---RRNGSFFLLYKLLRPFLKKSPEQGA 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 497642378 233 RTcldahdrgELYC--MPQFDAKVGW-----NIKRLAPQAY 266
Cdd:cd05327  228 QT--------ALYAatSPELEGVSGKyfsdcKIKMSSSEAL 260
PRK07890 PRK07890
short chain dehydrogenase; Provisional
16-199 2.66e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 68.06  E-value: 2.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLVi 95
Cdd:PRK07890   9 VVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDALV- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 NNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdAESRapRGIINVASAAAFGAAPGMAAYNVSKAGVLS 175
Cdd:PRK07890  88 NNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPAL--AESG--GSIVMINSMVLRHSQPKYGAYKMAKGALLA 163
                        170       180
                 ....*....|....*....|....
gi 497642378 176 LSETLAAELAGTPVRVTVLCPTFV 199
Cdd:PRK07890 164 ASQSLATELGPQGIRVNSVAPGYI 187
PRK07074 PRK07074
SDR family oxidoreductase;
15-201 4.49e-13

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 67.49  E-value: 4.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEqgGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:PRK07074   5 ALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGD--ARFVPVACDLTDAASLAAALANAAAERGPVDVLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 iNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRGIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:PRK07074  83 -ANAGAARAASLHDTTP-ASWRADNALNLEAAYLCVEAVLEGML----KRSRGAVVNIGSVNGMAALGHPAYSAAKAGLI 156
                        170       180
                 ....*....|....*....|....*..
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK07074 157 HYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK09242 PRK09242
SDR family oxidoreductase;
11-201 4.98e-13

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 67.08  E-value: 4.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAV--VCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:PRK09242   8 DGQTALITGASKGIGLAIAREFLGLGADVliVARDADALAQARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDHWD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNV 168
Cdd:PRK09242  88 GLHILV-NNAGGNIRKAAIDYTE-DEWRGIFETNLFSAFELSRYAHPLLKQHASSA---IVNIGSVSGLTHVRSGAPYGM 162
                        170       180       190
                 ....*....|....*....|....*....|...
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK09242 163 TKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRT 195
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-201 1.10e-12

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 66.14  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK08217   4 KDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLvINNA--------GVGAGGAAIGDAPLDDWAWTLGINLWGpihgchVFtpiL--RDA-----ESRAPRGIINVaSAA 155
Cdd:PRK08217  84 NGL-INNAgilrdgllVKAKDGKVTSKMSLEQFQSVIDVNLTG------VF---LcgREAaakmiESGSKGVIINI-SSI 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 497642378 156 AFGAAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK08217 153 ARAGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIET 198
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
15-87 1.27e-12

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 67.63  E-value: 1.27e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVsrfdeVQALAEQSQAWF 87
Cdd:COG3347  428 ALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDV-----DVTAEAAVAAAF 495
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
11-196 1.76e-12

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: 65.69  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQ-GGKAIAIRCDVSRFDEVQALAEQSQAWFpA 89
Cdd:cd05369    2 KGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSAtGGRAHPIQCDVRDPEAVEAAVDETLKEF-G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRGIINVASAAAFGAAPGMAAYNVS 169
Cdd:cd05369   81 KIDILINNAAGNFLAPAESLSP-NGFKTVIDIDLNGTFNTTKAVGKRLI--EAKHGGSILNISATYAYTGSPFQVHSAAA 157
                        170       180
                 ....*....|....*....|....*..
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCP 196
Cdd:cd05369  158 KAGVDALTRSLAVEWGPYGIRVNAIAP 184
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
15-191 2.40e-12

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 65.37  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:PRK12745   5 ALVTGGRRGIGLGIARALAAAGFDLAINDRpDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRIDCL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRA---PRGIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK12745  85 VNNAGVGVKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPEelpHRSIVFVSSVNAIMVSPNRGEYCISK 164
                        170       180
                 ....*....|....*....|.
gi 497642378 171 AGVLSLSETLAAELAGTPVRV 191
Cdd:PRK12745 165 AGLSMAAQLFAARLAEEGIGV 185
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
11-201 2.82e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 64.97  E-value: 2.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK08213  11 SGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGpihgchvfTPILRDA---ESRAPRG---IINVASAA----AFGAA 160
Cdd:PRK08213  91 DILV--NNAGATWGAPAEDHPVEAWDKVMNLNVRG--------LFLLSQAvakRSMIPRGygrIINVASVAglggNPPEV 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 497642378 161 PGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK08213 161 MDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPT 201
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
15-208 3.15e-12

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 64.87  E-value: 3.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:cd08945    6 ALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 iNNAGVGAGGAAIGdapLDDWAW--TLGINLWGPIhgcHVFTPILRDAESRA-PRG-IINVASAAAFGAAPGMAAYNVSK 170
Cdd:cd08945   86 -NNAGRSGGGATAE---LADELWldVVETNLTGVF---RVTKEVLKAGGMLErGTGrIINIASTGGKQGVVHAAPYSASK 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGR 208
Cdd:cd08945  159 HGVVGFTKALGLELARTGITVNAVCPGFVETPMAASVR 196
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
12-215 3.49e-12

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: 64.74  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGG---KAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:cd05364    3 GKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVsekKILLVVADLTEEEGQDRIISTTLAKFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdAESRAprGIINVASAAAFGAAPGMAAYNV 168
Cdd:cd05364   83 RLDILV--NNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHL--IKTKG--EIVNVSSVAGGRSFPGVLYYCI 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSE 215
Cdd:cd05364  157 SKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQYI 203
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-233 3.55e-12

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 64.74  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCS-DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPA 89
Cdd:PRK06077   5 KDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNaKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVINNAGVGAGGAAIGDAPLDDWawTLGINLWGPIHGCHVFTPILRDAESraprgIINVASAAAFGAAPGMAAYNVS 169
Cdd:PRK06077  85 ADILVNNAGLGLFSPFLNVDDKLIDK--HISTDFKSVIYCSQELAKEMREGGA-----IVNIASVAGIRPAYGLSIYGAM 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497642378 170 KAGVLSLSETLAAELAgTPVRVTVLCPTFVKTNILESgriseqsselatkLMRWTGLSAEKVAR 233
Cdd:PRK06077 158 KAAVINLTKYLALELA-PKIRVNAIAPGFVKTKLGES-------------LFKVLGMSEKEFAE 207
PRK07791 PRK07791
short chain dehydrogenase; Provisional
12-196 4.48e-12

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 64.69  E-value: 4.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDI---------DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQ 82
Cdd:PRK07791   6 GRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsasGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLVDA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  83 SQAWFPAAPTLViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGpiHGChvftpILRDA------ESRAPRG----IINVA 152
Cdd:PRK07791  86 AVETFGGLDVLV-NNAGILRDRMIANMSE-EEWDAVIAVHLKG--HFA-----TLRHAaaywraESKAGRAvdarIINTS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 497642378 153 SAAAFGAAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCP 196
Cdd:PRK07791 157 SGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP 200
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
12-201 7.13e-12

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 63.89  E-value: 7.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK07067   6 GKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEI---GPAAIAVSLDVTRQDSIDRIVAAAVERFGGID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNagvgagGAAIGDAPLDDWAWT-----LGINLWGPIhgchvFT--PILRDAESRAPRG-IINVASAAAFGAAPGM 163
Cdd:PRK07067  83 ILF-NN------AALFDMAPILDISRDsydrlFAVNVKGLF-----FLmqAVARHMVEQGRGGkIINMASQAGRRGEALV 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 497642378 164 AAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK07067 151 SHYCATKAAVISYTQSAALALIRHGINVNAIAPGVVDT 188
PRK09730 PRK09730
SDR family oxidoreductase;
15-233 7.55e-12

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 63.72  E-value: 7.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAV-VCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAwFPAAPTL 93
Cdd:PRK09730   4 ALVTGGSRGIGRATALLLAQEGYTVaVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQ-HDEPLAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGChvftpilRDAESRAPR-------GIINVASAAAFGAAPGM-AA 165
Cdd:PRK09730  83 LVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCC-------REAVKRMALkhggsggAIVNVSSAASRLGAPGEyVD 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497642378 166 YNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMRWTGLSAEKVAR 233
Cdd:PRK09730 156 YAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGRVDRVKSNIPMQRGGQPEEVAQ 223
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
12-236 8.67e-12

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: 63.64  E-value: 8.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTadaitEQGGKAIAIRCDVSRFDEVQALAEQSQAwfpaap 91
Cdd:cd05368    2 GKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKEL-----ERGPGITTRVLDVTDKEQVAALAKEEGR------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMA-AYNVSK 170
Cdd:cd05368   71 IDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGS---IINMSSVASSIKGVPNRfVYSTTK 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESgRISEQSSE-------LATKLMRWTGlSAEKVARTCL 236
Cdd:cd05368  148 AAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSLEE-RIQAQPDPeealkafAARQPLGRLA-TPEEVAALAV 218
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
17-208 1.02e-11

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: 63.24  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  17 VTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteQGGKAIAIRCDVS-RFDEVQALAEQSQAWFPAAPTLvI 95
Cdd:cd08931    5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAEL--GAENVVAGALDVTdRAAWAAALADFAAATGGRLDAL-F 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 NNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:cd08931   82 NNAGVGRGGPFEDV-PLAAHDRMVDINVKGVLNGAYAALPYLK----ATPGArVINTASSSAIYGQPDLAVYSATKFAVR 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILESGR 208
Cdd:cd08931  157 GLTEALDVEWARHGIRVADVWPWFVDTPILTKGE 190
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
12-213 1.03e-11

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 63.67  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAaQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK08226   6 GKTALITGALQGIGEGIARVFARHGANLILLDISPEI-EKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRID 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINnaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdAESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK08226  85 ILVNN--AGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEM--IARKDGRIVMMSSVTGDMVADPGETAYALTKA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILEsgRISEQS 213
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAE--SIARQS 200
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
11-217 1.54e-11

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: 63.08  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGG--AVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:cd05355   25 KGKKALITGGDSGIGRAVAIAFAREGAdvAINYLPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLViNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHgchvftpILRDAESRAPRG--IINVASAAAFGAAPGMAAY 166
Cdd:cd05355  105 KLDILV-NNAAYQHPQESIEDITTEQLEKTFRTNIFSMFY-------LTKAALPHLKKGssIINTTSVTAYKGSPHLLDY 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497642378 167 NVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELA 217
Cdd:cd05355  177 AATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKVSEFG 227
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
12-201 1.65e-11

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 62.60  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAiteQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd09761    1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEA---EGPNLFFVHGDVADETLVKFVVYAMLEKLGRID 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRaprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:cd09761   78 VLV--NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGR----IINIASTRAFQSEPDSEAYAASKG 151
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELaGTPVRVTVLCPTFVKT 201
Cdd:cd09761  152 GLVALTHALAMSL-GPDIRVNCISPGWINT 180
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
15-201 1.72e-11

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: 62.31  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSrfDEVQALAEQSQAWFPAAP-TL 93
Cdd:cd05325    1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATELAALGASHSRLHILELDVT--DEIAESAEAVAERLGDAGlDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAA---AFGAAPGMAAYNVSK 170
Cdd:cd05325   79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAK---IINISSRVgsiGDNTSGGWYSYRASK 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:cd05325  156 AALNMLTKSLAVELKRDGITVVSLHPGWVRT 186
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
15-205 2.94e-11

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 62.09  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCsdIDQTAAQKTADAITEQGGKAIAIRC---DVSRFDEVQ-ALAEQSQAWFPAa 90
Cdd:PRK12824   5 ALVTGAKRGIGSAIARELLNDGYRVIA--TYFSGNDCAKDWFEEYGFTEDQVRLkelDVTDTEECAeALAEIEEEEGPV- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 pTLVINNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRDaesrapRG---IINVASAAAFGAAPGMAAYN 167
Cdd:PRK12824  82 -DILVNNAGITRDSVFKRM-SHQEWNDVINTNLNSVFNVTQPLFAAMCE------QGygrIINISSVNGLKGQFGQTNYS 153
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 497642378 168 VSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:PRK12824 154 AAKAGMIGFTKALASEGARYGITVNCIAPGYIATPMVE 191
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
12-197 3.86e-11

(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: 61.57  E-value: 3.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDI---------DQTAAQKTADAITEQGGKAIAIRCDVsrfDEVQALAEQ 82
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLggdrkgsgkSSSAADKVVDEIKAAGGKAVANYDSV---EDGEKIVKT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  83 SQAWFPAApTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAES-RaprgIINVASAAAFGAAP 161
Cdd:cd05353   82 AIDAFGRV-DILVNNAGILRDRSFAKMSE-EDWDLVMRVHLKGSFKVTRAAWPYMRKQKFgR----IINTSSAAGLYGNF 155
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 497642378 162 GMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPT 197
Cdd:cd05353  156 GQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
11-249 4.74e-11

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: 61.37  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAI-AIRCDVSRFDEVQALAEQSQAWFPA 89
Cdd:cd05343    5 RGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGYPTLfPYQCDLSNEEQILSMFSAIRTQHQG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLvINNAGVGAGGAAIGDAPlDDWAWTLGINLwgpihgchVFTPI-LRDA-ESRAPRGI-------INVASAAAFGAA 160
Cdd:cd05343   85 VDVC-INNAGLARPEPLLSGKT-EGWKEMFDVNV--------LALSIcTREAyQSMKERNVddghiinINSMSGHRVPPV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 161 PGMAAYNVSKAGVLSLSETLAAEL--AGTPVRVTVLCPTFVKTNILEsgRISEQSSELATKLMRWTglsaekvarTCLDA 238
Cdd:cd05343  155 SVFHFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAF--KLHDNDPEKAAATYESI---------PCLKP 223
                        250
                 ....*....|...
gi 497642378 239 HDRGE--LYCMPQ 249
Cdd:cd05343  224 EDVANavLYVLST 236
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
15-202 5.63e-11

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: 61.20  E-value: 5.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGG-KAIAIRCDVSRFDEVQALAEQSQAWFpAAPTL 93
Cdd:cd08930    5 ILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKnRVIALELDITSKESIKELIESYLEKF-GRIDI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIG--DAPLDDWAWTLGINLWGPIHGCHVFTPILRDAEsrapRG-IINVASAA----------AFGAA 160
Cdd:cd08930   84 LINNAYPSPKVWGSRfeEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQG----KGsIINIASIYgviapdfriyENTQM 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 497642378 161 PGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTN 202
Cdd:cd08930  160 YSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNN 201
PRK05717 PRK05717
SDR family oxidoreductase;
12-201 6.09e-11

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 61.06  E-value: 6.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKAL---GENAWFIAMDVADEAQVAAGVAEVLGQFGRLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdaesRAPRG-IINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK05717  87 ALVCNAAIADPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYL-----RAHNGaIVNLASTRARQSEPDTEAYAASK 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 497642378 171 AGVLSLSETLAAELaGTPVRVTVLCPTFVKT 201
Cdd:PRK05717 162 GGLLALTHALAISL-GPEIRVNAVSPGWIDA 191
PRK05872 PRK05872
short chain dehydrogenase; Provisional
11-201 7.90e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 61.14  E-value: 7.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAItEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAA 90
Cdd:PRK05872   8 AGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAEL-GGDDRVLTVVADVTDLAAMQAAAEEAVERF-GG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAesrapRG-IINVASAAAFGAAPGMAAYNVS 169
Cdd:PRK05872  86 IDVVVANAGIASGGSVAQVDP-DAFRRVIDVNLLGVFHTVRATLPALIER-----RGyVLQVSSLAAFAAAPGMAAYCAS 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK05872 160 KAGVEAFANALRLEVAHHGVTVGSAYLSWIDT 191
PRK12827 PRK12827
short chain dehydrogenase; Provisional
12-205 8.21e-11

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 60.89  E-value: 8.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTA----AQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWF 87
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRgraeADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEEF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  88 paAPTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdaeSRAPRG--IINVASAAAFGAAPGMAA 165
Cdd:PRK12827  86 --GRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPM----IRARRGgrIVNIASVAGVRGNRGQVN 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497642378 166 YNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:PRK12827 160 YAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMAD 199
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
12-221 1.07e-10

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: 60.62  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTaAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd08937    4 GKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSEL-VHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLvINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVasAAAFGAAPGMAAYNVSKA 171
Cdd:cd08937   83 VL-INNVGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGV---IVNV--SSIATRGIYRIPYSAAKG 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTN----ILESGRISEQSSELATKLM 221
Cdd:cd08937  157 GVNALTASLAFEHARDGIRVNAVAPGGTEAPprkiPRNAAPMSEQEKVWYQRIV 210
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
1-229 1.13e-10

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 60.31  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   1 MFGLNkpkisrGASAVVTGAGSGIGAAFAVELGRRGGAVvcsDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALA 80
Cdd:PRK12936   1 MFDLS------GRKALVTGASGGIGEEIARLLHAQGAIV---GLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  81 EQSQAWFPAAPTLVINNAGVGAGGAAIGDAPldDWAWTLGINLWGPIHGCHVFT-PILRDAESRaprgIINVASAAAFGA 159
Cdd:PRK12936  72 QKAEADLEGVDILVNNAGITKDGLFVRMSDE--DWDSVLEVNLTATFRLTRELThPMMRRRYGR----IINITSVVGVTG 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642378 160 APGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNIleSGRISEQSSE--LATKLMRWTGLSAE 229
Cdd:PRK12936 146 NPGQANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAM--TGKLNDKQKEaiMGAIPMKRMGTGAE 215
PRK07478 PRK07478
short chain dehydrogenase; Provisional
12-196 1.14e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 60.33  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:PRK07478   6 GKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERF-GGL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDaesrapRG----IINVASAAAFGAAPGMAAYN 167
Cdd:PRK07478  85 DIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLA------RGggslIFTSTFVGHTAGFPGMAAYA 158
                        170       180
                 ....*....|....*....|....*....
gi 497642378 168 VSKAGVLSLSETLAAELAGTPVRVTVLCP 196
Cdd:PRK07478 159 ASKAGLIGLTQVLAAEYGAQGIRVNALLP 187
PRK07775 PRK07775
SDR family oxidoreductase;
15-201 1.18e-10

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 60.54  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpaAPTLV 94
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEAL--GEIEV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGGAAIGDAPLDDWAWTLGINLWGpihGCHVFTPILRDAESRAPRGIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:PRK07775  91 LVSGAGDTYFGKLHEISTEQFESQVQIHLVG---ANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLE 167
                        170       180
                 ....*....|....*....|....*..
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK07775 168 AMVTNLQMELEGTGVRASIVHPGPTLT 194
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
3-202 1.28e-10

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: 60.25  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   3 GLNKPKISRGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQ 82
Cdd:cd08936    1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  83 SQAWFPAAPTLViNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPilrDAESRAPRGIINVASAAAFGAAPG 162
Cdd:cd08936   81 AVNLHGGVDILV-SNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVP---EMEKRGGGSVVIVSSVAAFHPFPG 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497642378 163 MAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTN 202
Cdd:cd08936  157 LGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTS 196
PRK08265 PRK08265
short chain dehydrogenase; Provisional
12-206 1.43e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 60.02  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK08265   6 GKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGRVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNAGVGAGGAAIGDAplDDWAWTLGINLWGPIhgchVFTPILRDAESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK08265  83 ILV-NLACTYLDDGLASSR--ADWLAALDVNLVSAA----MLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYPASKA 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:PRK08265 156 AIRQLTRSMAMDLAPDGIRVNSVSPGWTWSRVMDE 190
PRK06947 PRK06947
SDR family oxidoreductase;
14-222 2.26e-10

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 59.43  E-value: 2.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  14 SAVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPT 92
Cdd:PRK06947   4 VVLITGASRGIGRATAVLAAARGWSVGINYArDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LViNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPiHGChVFTPILRDAESRAPRG--IINVASAAAFGAAPGM-AAYNVS 169
Cdd:PRK06947  84 LV-NNAGIVAPSMPLADMDAARLRRMFDTNVLGA-YLC-AREAARRLSTDRGGRGgaIVNVSSIASRLGSPNEyVDYAGS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSEL--ATKLMR 222
Cdd:PRK06947 161 KGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAARLgaQTPLGR 215
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
15-206 3.64e-10

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: 59.02  E-value: 3.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQktadaitEQGGKAIAIRCDVSrfdEVQALAEQSQAWFPA-APTL 93
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLL-------EYGDPLRLTPLDVA---DAAAVREVCSRLLAEhGPID 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:cd05331   71 ALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGA---IVTVASNAAHVPRISMAAYGASKAAL 147
                        170       180       190
                 ....*....|....*....|....*....|...
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILES 206
Cdd:cd05331  148 ASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRT 180
PRK09134 PRK09134
SDR family oxidoreductase;
14-213 6.93e-10

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 58.02  E-value: 6.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  14 SAVVTGAGSGIGAAFAVELGRRGGAVV--CSDiDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQAL-AEQSQAWFPaa 90
Cdd:PRK09134  11 AALVTGAARRIGRAIALDLAAHGFDVAvhYNR-SRDEAEALAAEIRALGRRAVALQADLADEAEVRALvARASAALGP-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIhgchVFTPILRDAESRAPRG-IINVASAAAFGAAPGMAAYNVS 169
Cdd:PRK09134  88 ITLLVNNASLFEYDSAASFTR-ASWDRHMATNLRAPF----VLAQAFARALPADARGlVVNMIDQRVWNLNPDFLSYTLS 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 497642378 170 KAGVLSLSETLAAELAgtP-VRVTVLCPTFVktniLESGRISEQS 213
Cdd:PRK09134 163 KAALWTATRTLAQALA--PrIRVNAIGPGPT----LPSGRQSPED 201
PRK06720 PRK06720
hypothetical protein; Provisional
3-72 8.14e-10

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 56.52  E-value: 8.14e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   3 GLNKPKISrGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSR 72
Cdd:PRK06720   8 GVMKMKLA-GKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEK 76
PRK07060 PRK07060
short chain dehydrogenase; Provisional
12-201 1.06e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 57.42  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAaqktADAITEQGGkAIAIRCDVSRfDEVQALAEQSqawFPAAP 91
Cdd:PRK07060   9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAA----LDRLAGETG-CEPLRLDVGD-DAAIRAALAA---AGAFD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPilrdAESRAPRG--IINVASAAAFGAAPGMAAYNVS 169
Cdd:PRK07060  80 GLV--NCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVAR----AMIAAGRGgsIVNVSSQAALVGLPDHLAYCAS 153
                        170       180       190
                 ....*....|....*....|....*....|..
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK07060 154 KAALDAITRVLCVELGPHGIRVNSVNPTVTLT 185
PRK06123 PRK06123
SDR family oxidoreductase;
15-236 1.22e-09

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 57.48  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVCLNYLrNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLDAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 ViNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHvfTPILRDAESRAPRG--IINVASAAAFGAAPGM-AAYNVSK 170
Cdd:PRK06123  85 V-NNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAR--EAVKRMSTRHGGRGgaIVNVSSMAARLGSPGEyIDYAASK 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMRWTGLSAEKVARTCL 236
Cdd:PRK06123 162 GAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDRVKAGIPMGRGGTAEEVARAIL 227
PRK08303 PRK08303
short chain dehydrogenase; Provisional
11-82 1.36e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 57.70  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVC---------SDIDQTAA-QKTADAITEQGGKAIAIRCDVSRFDEVQALA 80
Cdd:PRK08303   7 RGKVALVAGATRGAGRGIAVELGAAGATVYVtgrstrarrSEYDRPETiEETAELVTAAGGRGIAVQVDHLVPEQVRALV 86

                 ..
gi 497642378  81 EQ 82
Cdd:PRK08303  87 ER 88
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
17-229 1.43e-09

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: 57.29  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  17 VTGAGSGIGAAFAVELGRRGGAVVcsdidqtaaqktADAITEQGGKAIAIR--C---------DVSRFDEVQALAEQSQA 85
Cdd:cd09805    5 ITGCDSGFGNLLAKKLDSLGFTVL------------AGCLTKNGPGAKELRrvCsdrlrtlqlDVTKPEQIKRAAQWVKE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  86 WFPAAPTL-VINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRaprgIINVASAAAFGAAPGMA 164
Cdd:cd09805   73 HVGEKGLWgLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGR----VVNVSSMGGRVPFPAGG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNIlesGRISEQSSELATKLmrWTGLSAE 229
Cdd:cd09805  149 AYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGI---TGNSELWEKQAKKL--WERLPPE 208
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
12-196 1.82e-09

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 56.82  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDqtaaqktadAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK08220   8 GKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQA---------FLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK08220  79 VLV--NAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGA---IVTVGSNAAHVPRIGMAAYGASKA 153
                        170       180
                 ....*....|....*....|....*
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCP 196
Cdd:PRK08220 154 ALTSLAKCVGLELAPYGVRCNVVSP 178
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
12-196 2.35e-09

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: 56.72  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGgKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:cd08942    6 GKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERSDRLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAES-RAPRGIINVASAAAFGAAPGMA-AYNVS 169
Cdd:cd08942   85 VLV--NNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaENPARVINIGSIAGIVVSGLENySYGAS 162
                        170       180
                 ....*....|....*....|....*..
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCP 196
Cdd:cd08942  163 KAAVHQLTRKLAKELAGEHITVNAIAP 189
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
16-236 2.41e-09

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: 56.53  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGA--VVCSDIDQTAAQKTADAITEqGGKAIAIRCDVSRFDEVQALAEQSQaWFPAAPTL 93
Cdd:cd05367    3 ILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELRP-GLRVTTVKADLSDAAGVEQLLEAIR-KLDGERDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRGIINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:cd05367   81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFK--KRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497642378 174 LSLSETLAAELAGtpVRVTVLCPTFVKTN----ILESGRISEQSSELATklMRWTG--LSAEKVARTCL 236
Cdd:cd05367  159 DMFFRVLAAEEPD--VRVLSYAPGVVDTDmqreIRETSADPETRSRFRS--LKEKGelLDPEQSAEKLA 223
PLN02253 PLN02253
xanthoxin dehydrogenase
12-203 2.44e-09

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 56.76  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFaVELGRRGGAVVC-SDIDQTAAQKTADAIteqGGK--AIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:PLN02253  18 GKVALVTGGATGIGESI-VRLFHKHGAKVCiVDLQDDLGQNVCDSL---GGEpnVCFFHCDVTVEDDVSRAVDFTVDKFG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHG----CHVFTPILRDAesraprgIINVASAAAFGAAPGMA 164
Cdd:PLN02253  94 TLDIMVNNAGLTGPPCPDIRNVELSEFEKVFDVNVKGVFLGmkhaARIMIPLKKGS-------IVSLCSVASAIGGLGPH 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:PLN02253 167 AYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTAL 205
PRK09072 PRK09072
SDR family oxidoreductase;
12-219 2.66e-09

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 56.49  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIaIRCDVSRFDEVQALAEQSQAWfpAAP 91
Cdd:PRK09072   5 DKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHRW-VVADLTSEAGREAVLARAREM--GGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRGII-NVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK09072  82 NVLINNAGVNHFALLEDQDP-EAIERLLALNLTAPMQLTRALLPLLR----AQPSAMVvNVGSTFGSIGYPGYASYCASK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTNiLESGRISEQSSELATK 219
Cdd:PRK09072 157 FALRGFSEALRRELADTGVRVLYLAPRATRTA-MNSEAVQALNRALGNA 204
PRK07806 PRK07806
SDR family oxidoreductase;
10-96 2.87e-09

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 56.27  E-value: 2.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  10 SRGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTA-AQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:PRK07806   4 LPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPrANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFG 83

                 ....*...
gi 497642378  89 AAPTLVIN 96
Cdd:PRK07806  84 GLDALVLN 91
PRK12746 PRK12746
SDR family oxidoreductase;
12-203 3.11e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 56.20  E-value: 3.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAV-VCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQS----QAW 86
Cdd:PRK12746   6 GKVALVTGASRGIGRAIAMRLANDGALVaIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLknelQIR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  87 FPAAPTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdAESRaprgIINVASAAAFGAAPGMAAY 166
Cdd:PRK12746  86 VGTSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGR----VINISSAEVRLGFTGSIAY 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 497642378 167 NVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:PRK12746 161 GLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDI 197
PRK12828 PRK12828
short chain dehydrogenase; Provisional
12-201 3.47e-09

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 55.96  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIrcDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK12828   7 GKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEVNRQFGRLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdAESRAPRgIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK12828  85 ALV--NIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPAL--TASGGGR-IVNIGAGAALKAGPGMGAYAAAKA 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK12828 160 GVARLTEALAAELLDRGITVNAVLPSIIDT 189
PRK06180 PRK06180
short chain dehydrogenase; Provisional
17-196 4.15e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 56.08  E-value: 4.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  17 VTGAGSGIGAAFAVELGRRGGAVVCsdidqTA--AQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:PRK06180   9 ITGVSSGFGRALAQAALAAGHRVVG-----TVrsEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 inNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRapRG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:PRK06180  84 --NNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMR--ARR--RGhIVNITSMGGLITMPGIGYYCGSKFAL 157
                        170       180
                 ....*....|....*....|...
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCP 196
Cdd:PRK06180 158 EGISESLAKEVAPFGIHVTAVEP 180
PRK06949 PRK06949
SDR family oxidoreductase;
12-222 7.27e-09

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 55.15  E-value: 7.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK06949   9 GKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHgchVFTPILRDAESRA-------PRG-IINVASAAAFGAAPGM 163
Cdd:PRK06949  89 ILV-NNSGVSTTQKLVDVTP-ADFDFVFDTNTRGAFF---VAQEVAKRMIARAkgagntkPGGrIINIASVAGLRVLPQI 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497642378 164 AAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMR 222
Cdd:PRK06949 164 GLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQGQKLVSMLPR 222
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
12-210 7.54e-09

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: 54.92  E-value: 7.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGG-KAIAIRCDVSRFDEV-QALAEQSQawfpa 89
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGvETKTIAADFSAGDDIyERIEKELE----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 apTL----VINNAGVGAGGAAIGDAPLDDWAW-TLGINLWGPIHGCHVFTPILrdaESRaPRG-IINVASAAAFGAAPGM 163
Cdd:cd05356   76 --GLdigiLVNNVGISHSIPEYFLETPEDELQdIINVNVMATLKMTRLILPGM---VKR-KKGaIVNISSFAGLIPTPLL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 497642378 164 AAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNiLESGRIS 210
Cdd:cd05356  150 ATYSASKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATK-MSKIRKS 195
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
11-82 1.18e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 54.68  E-value: 1.18e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQ 82
Cdd:PRK07097   9 KGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQ 80
PRK07814 PRK07814
SDR family oxidoreductase;
12-97 1.35e-08

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 54.40  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVC-----SDIDQTAAQktadaITEQGGKAIAIRCDVSRFDEVQALAEQSQAW 86
Cdd:PRK07814  10 DQVAVVTGAGRGLGAAIALAFAEAGADVLIaarteSQLDEVAEQ-----IRAAGRRAHVVAADLAHPEATAGLAGQAVEA 84
                         90
                 ....*....|.
gi 497642378  87 FpAAPTLVINN 97
Cdd:PRK07814  85 F-GRLDIVVNN 94
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
15-237 1.36e-08

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: 54.39  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAI-TEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:cd05322    5 AVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEInAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVDLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINnaGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprGIINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:cd05322   85 VYS--AGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIQG--RIIQINSKSGKVGSKHNSGYSAAKFGG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPtfvkTNILESGRISEQSSELATKLmrwtGLSAEKVARTCLD 237
Cdd:cd05322  161 VGLTQSLALDLAEHGITVNSLML----GNLLKSPMFQSLLPQYAKKL----GIKESEVEQYYID 216
PRK07201 PRK07201
SDR family oxidoreductase;
16-241 1.49e-08

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 55.34  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLVI 95
Cdd:PRK07201 375 LITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDYLVN 454
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 NNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRapRG-IINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:PRK07201 455 NAGRSIRRSVENSTDRFHDYERTMAVNYFGAVRLILGLLPHMR--ERR--FGhVVNVSSIGVQTNAPRFSAYVASKAALD 530
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642378 175 SLSETLAAELAGTPVRVT------VLCPTFVKTNILESGRISeqSSELAtklmrwtglsAEKVARTCLDAHDR 241
Cdd:PRK07201 531 AFSDVAASETLSDGITFTtihmplVRTPMIAPTKRYNNVPTI--SPEEA----------ADMVVRAIVEKPKR 591
PRK06128 PRK06128
SDR family oxidoreductase;
12-207 2.29e-08

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 54.09  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDI--DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPA 89
Cdd:PRK06128  55 GRKALITGADSGIGRATAIAFAREGADIALNYLpeEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLViNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESraprgIINVASAAAFGAAPGMAAYNVS 169
Cdd:PRK06128 135 LDILV-NIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGAS-----IINTGSIQSYQPSPTLLDYAST 208
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESG 207
Cdd:PRK06128 209 KAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSG 246
PRK12743 PRK12743
SDR family oxidoreductase;
15-185 2.78e-08

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 53.50  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAV-VCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDE----VQALAEQsqawFPA 89
Cdd:PRK12743   5 AIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEgaqaLDKLIQR----LGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPihgchvFTPILRDAESRAPRG----IINVASAAAFGAAPGMAA 165
Cdd:PRK12743  81 IDVLV--NNAGAMTKAPFLDMDFDEWRKIFTVDVDGA------FLCSQIAARHMVKQGqggrIINITSVHEHTPLPGASA 152
                        170       180
                 ....*....|....*....|
gi 497642378 166 YNVSKAGVLSLSETLAAELA 185
Cdd:PRK12743 153 YTAAKHALGGLTKAMALELV 172
PRK07831 PRK07831
SDR family oxidoreductase;
11-219 3.33e-08

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 53.11  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGA-GSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGG--KAIAIRCDVSRFDEVQALAEQSQAWF 87
Cdd:PRK07831  16 AGKVVLVTAAaGTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGlgRVEAVVCDVTSEAQVDALIDAAVERL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  88 pAAPTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAESRAPrgIINVASAAAFGAAPGMAAYN 167
Cdd:PRK07831  96 -GRLDVLVNNAGLGGQTPVVDMTD-DEWSRVLDVTLTGTFRATRAALRYMRARGHGGV--IVNNASVLGWRAQHGQAHYA 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497642378 168 VSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATK 219
Cdd:PRK07831 172 AAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVTSAELLDELAAR 223
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
12-82 5.64e-08

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 53.30  E-value: 5.64e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAA--QKTADAIteqGGKAIAirCDVSRFDEVQALAEQ 82
Cdd:PRK08261 210 GKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAGEalAAVANRV---GGTALA--LDITAPDAPARIAEH 277
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-199 5.73e-08

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 52.46  E-value: 5.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVeLGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK05786   4 KGKKVAIIGVSEGLGYAVAY-FALKEGAQVCINSRNENKLKRMKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLNAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINnAGVGAGGAAIGDAPLDDwawTLGINLWGPIHGCHVFTPILRDAES----RAPRGIinvasaaaFGAAPGMAAY 166
Cdd:PRK05786  83 DGLVVT-VGGYVEDTVEEFSGLEE---MLTNHIKIPLYAVNASLRFLKEGSSivlvSSMSGI--------YKASPDQLSY 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 497642378 167 NVSKAGVLSLSETLAAELAGTPVRVTVLCPTFV 199
Cdd:PRK05786 151 AVAKAGLAKAVEILASELLGRGIRVNGIAPTTI 183
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
12-202 6.77e-08

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 52.43  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDqTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK06935  15 GKVAIVTGGNTGLGQGYAVALAKAGADIIITTHG-TNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKID 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNAGVGAGGaaigdaPL-----DDWAWTLGINLwgpihgCHVFTPILRDAESRAPRG---IINVASAAAFGAAPGM 163
Cdd:PRK06935  94 ILV-NNAGTIRRA------PLleykdEDWNAVMDINL------NSVYHLSQAVAKVMAKQGsgkIINIASMLSFQGGKFV 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 497642378 164 AAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTN 202
Cdd:PRK06935 161 PAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKTA 199
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
15-205 8.99e-08

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: 51.94  E-value: 8.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDI-----DQTAAQKTA---DAITEQ-GGKAIAIRCDVSRFDEVQALAEQSQA 85
Cdd:TIGR04504   4 ALVTGAARGIGAATVRRLAADGWRVVAVDLcaddpAVGYPLATRaelDAVAAAcPDQVLPVIADVRDPAALAAAVALAVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   86 WFPAAPTLVinnagvGAGGAAIGDAPL-----DDWAWTLGINLWGPIHGCHVFTPILRDAEsrAPRG--IINVASAAAFG 158
Cdd:TIGR04504  84 RWGRLDAAV------AAAGVIAGGRPLwettdAELDLLLDVNLRGVWNLARAAVPAMLARP--DPRGgrFVAVASAAATR 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 497642378  159 AAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:TIGR04504 156 GLPHLAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMLA 202
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
12-201 9.21e-08

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: 51.85  E-value: 9.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAIteqGGKAIAIRCDVSRFDEV-QALAEQSQAWfpAA 90
Cdd:cd05363    3 GKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEI---GPAACAISLDVTDQASIdRCVAALVDRW--GS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNagvgagGAAIGDAPLDDWAWT-----LGINLWGpihgchVFTPILRDAESRAPRG----IINVASAAAFGAAP 161
Cdd:cd05363   78 IDILVNN------AALFDLAPIVDITREsydrlFAINVSG------TLFMMQAVARAMIAQGrggkIINMASQAGRRGEA 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497642378 162 GMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:cd05363  146 LVGVYCATKAAVISLTQSAGLNLIRHGINVNAIAPGVVDG 185
PRK06701 PRK06701
short chain dehydrogenase; Provisional
11-219 1.06e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 51.96  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGG--AVVCSDIDQTAAQkTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:PRK06701  45 KGKVALITGGDSGIGRAVAVLFAKEGAdiAIVYLDEHEDANE-TKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELG 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLViNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESraprgIINVASAAAFGAAPGMAAYNV 168
Cdd:PRK06701 124 RLDILV-NNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGSA-----IINTGSITGYEGNETLIDYSA 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATK 219
Cdd:PRK06701 198 TKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEKVSQFGSN 248
PRK06398 PRK06398
aldose dehydrogenase; Validated
11-205 1.09e-07

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 51.76  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTAdaiteqggkaiAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK06398   5 KDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVD-----------YFKVDVSNKEQVIKGIDYVISKYGRI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILrdAESRAPrGIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK06398  74 DILV--NNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYM--LKQDKG-VIINIASVQSFAVTRNAAAYVTSK 148
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 171 AGVLSLSETLAAELAGTpVRVTVLCPTFVKTNILE 205
Cdd:PRK06398 149 HAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTPLLE 182
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
16-205 1.22e-07

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: 51.37  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKA--IAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:cd05330    7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAPDAevLLIKADVSDEAQVEAYVDATVEQFGRIDGF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 vINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:cd05330   87 -FNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGM---IVNTASVGGIRGVGNQSGYAAAKHGV 162
                        170       180       190
                 ....*....|....*....|....*....|..
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:cd05330  163 VGLTRNSAVEYGQYGIRINAIAPGAILTPMVE 194
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
11-221 1.23e-07

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: 51.32  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCsdIDQTAAQktADAITEQGGKAIAIRCDVSRFDEVQAlaeqsqAWFPAA 90
Cdd:cd05351    6 AGKRALVTGAGKGIGRATVKALAKAGARVVA--VSRTQAD--LDSLVRECPGIEPVCVDLSDWDATEE------ALGSVG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PT-LVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHgchVFTPILRDAESRAPRG-IINVASAAAFGAAPGMAAYNV 168
Cdd:cd05351   76 PVdLLVNNAAVAILQPFLEVTK-EAFDRSFDVNVRAVIH---VSQIVARGMIARGVPGsIVNVSSQASQRALTNHTVYCS 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTnilESGRISEQSSELATKLM 221
Cdd:cd05351  152 TKAALDMLTKVMALELGPHKIRVNSVNPTVVMT---DMGRDNWSDPEKAKKML 201
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
12-203 1.28e-07

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: 51.70  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAI--TEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPA 89
Cdd:cd09807    1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIrrDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  90 APTLvINNAGVGAGGAAIGDaplDDWAWTLGINlwgpiHGCH-VFTPILRDA-ESRAPRGIINVASAAAFG--------- 158
Cdd:cd09807   81 LDVL-INNAGVMRCPYSKTE---DGFEMQFGVN-----HLGHfLLTNLLLDLlKKSAPSRIVNVSSLAHKAgkinfddln 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 497642378 159 ---AAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:cd09807  152 sekSYNTGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTEL 199
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
12-201 1.46e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 51.29  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK08085   9 GKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLvINNaGVGAGGAAIGDAPLDDWAWTLGINLWGpihgchVF---TPILRDAESRAPRGIINVASAAAFGAAPGMAAYNV 168
Cdd:PRK08085  89 VL-INN-AGIQRRHPFTEFPEQEWNDVIAVNQTA------VFlvsQAVARYMVKRQAGKIINICSMQSELGRDTITPYAA 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK08085 161 SKGAVKMLTRGMCVELARHNIQVNGIAPGYFKT 193
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
15-195 2.83e-07

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 50.49  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDI-DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:PRK08063   7 ALVTGSSRGIGKAIALRLAEEGYDIAVNYArSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLDVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VINnagvgagGAAIGDAPLDD-----WAWTLGINLWGPIHGCHVFTPILrdaESRAPRGIINVASAAAFGAAPGMAAYNV 168
Cdd:PRK08063  87 VNN-------AASGVLRPAMEleeshWDWTMNINAKALLFCAQEAAKLM---EKVGGGKIISLSSLGSIRYLENYTTVGV 156
                        170       180
                 ....*....|....*....|....*..
gi 497642378 169 SKAGVLSLSETLAAELAgtPVRVTVLC 195
Cdd:PRK08063 157 SKAALEALTRYLAVELA--PKGIAVNA 181
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
16-201 4.82e-07

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 49.50  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKA---IAIRCDVSRFDEVQALAEQSQAWFPAAPT 92
Cdd:cd05340    8 LVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQpqwFILDLLTCTSENCQQLAQRIAVNYPRLDG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 lVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFGAAPGMAAYNVSKAG 172
Cdd:cd05340   88 -VLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGS---LVFTSSSVGRQGRANWGAYAVSKFA 163
                        170       180
                 ....*....|....*....|....*....
gi 497642378 173 VLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:cd05340  164 TEGL*QVLADEYQQRNLRVNCINPGGTRT 192
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
7-89 4.90e-07

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: 50.44  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   7 PKISRGASAVVTGAGSGIGAAFAVELGRRGGA--VVCS----DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALA 80
Cdd:cd08953  200 APLKPGGVYLVTGGAGGIGRALARALARRYGArlVLLGrsplPPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLL 279

                 ....*....
gi 497642378  81 EQSQAWFPA 89
Cdd:cd08953  280 EKVRERYGA 288
PRK07024 PRK07024
SDR family oxidoreductase;
16-201 1.15e-06

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 48.77  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGG--AVVCSDIDqtAAQKTADAIteQGGKAIAIRC-DVSRFDEVQALAEQSQAWFpAAPT 92
Cdd:PRK07024   6 FITGASSGIGQALAREYARQGAtlGLVARRTD--ALQAFAARL--PKAARVSVYAaDVRDADALAAAAADFIAAH-GLPD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAPRGIINVASAAAFGAAPGmaaYNVSKAG 172
Cdd:PRK07024  81 VVIANAGISVGTLTEEREDLAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGA---YSASKAA 157
                        170       180
                 ....*....|....*....|....*....
gi 497642378 173 VLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK07024 158 AIKYLESLRVELRPAGVRVVTIAPGYIRT 186
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
16-205 3.78e-06

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: 47.14  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQG-GKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:cd08933   13 IVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLISVTVERFGRIDCLV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 iNNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRaprgIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:cd08933   93 -NNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGN----IINLSSLVGSIGQKQAAPYVATKGAIT 167
                        170       180       190
                 ....*....|....*....|....*....|.
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILE 205
Cdd:cd08933  168 AMTKALAVDESRYGVRVNCISPGNIWTPLWE 198
PRK09135 PRK09135
pteridine reductase; Provisional
15-196 4.56e-06

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 46.84  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVV--CSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPT 92
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAihYHRSAAEADALAAELNALRPGSAAALQADLLDPDALPELVAACVAAFGRLDA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAesrapRG-IINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK09135  89 LV-NNASSFYPTPLGSITE-AQWDDLFASNLKAPFFLSQAAAPQLRKQ-----RGaIVNITDIHAERPLKGYPVYCAAKA 161
                        170       180
                 ....*....|....*....|....*.
gi 497642378 172 GVLSLSETLAAELAgtP-VRVTVLCP 196
Cdd:PRK09135 162 ALEMLTRSLALELA--PeVRVNAVAP 185
PRK06914 PRK06914
SDR family oxidoreductase;
15-207 5.81e-06

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 46.56  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQG-GKAIAI-RCDVSRFDEVQALAEQSQAWFPAapT 92
Cdd:PRK06914   6 AIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNlQQNIKVqQLDVTDQNSIHNFQLVLKEIGRI--D 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LVINNAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVSKAG 172
Cdd:PRK06914  84 LLVNNAGYANGGFVEEI-PVEEYRKQFETNVFGAISVTQAVLPYMR--KQKSGK-IINISSISGRVGFPGLSPYVSSKYA 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 173 VLSLSETLAAELAGTPVRVTVLCPTFVKTNILESG 207
Cdd:PRK06914 160 LEGFSESLRLELKPFGIDVALIEPGSYNTNIWEVG 194
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
12-97 6.43e-06

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 46.48  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQkTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAP 91
Cdd:PRK12823   8 GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSELVHE-VAAELRAAGGEALALTADLETYAGAQAAMAAAVEAF-GRI 85

                 ....*.
gi 497642378  92 TLVINN 97
Cdd:PRK12823  86 DVLINN 91
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
16-88 6.52e-06

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: 45.55  E-value: 6.52e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642378    16 VVTGAGSGIGAAFAVELGRRGGA--VVCS--DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrlVLLSrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEG 80
PRK08251 PRK08251
SDR family oxidoreductase;
166-203 7.57e-06

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 46.08  E-value: 7.57e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 497642378 166 YNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:PRK08251 154 YAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEM 191
PRK08278 PRK08278
SDR family oxidoreductase;
11-97 7.85e-06

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 46.05  E-value: 7.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVcsdidqtAAQKTADA--------------ITEQGGKAIAIRCDVSRFDEV 76
Cdd:PRK08278   5 SGKTLFITGASRGIGLAIALRAARDGANIV-------IAAKTAEPhpklpgtihtaaeeIEAAGGQALPLVGDVRDEDQV 77
                         90       100
                 ....*....|....*....|.
gi 497642378  77 QALAEQSQAWFpAAPTLVINN 97
Cdd:PRK08278  78 AAAVAKAVERF-GGIDICVNN 97
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
15-234 8.76e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 45.83  E-value: 8.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCsdIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQ---SQAWFPAAP 91
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVIS--ISRTENKELTKLAEQYNSNLTFHSLDLQDVHELETNFNEilsSIQEDNVSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPilRDAESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK06924  82 IHLINNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMK--HTKDWKVDKRVINISSGAAKNPYFGWSAYCSSKA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497642378 172 GVLSLSETLAAE--LAGTPVRVTVLCPTFVKTNIleSGRISEQSSELATKLMRWTGLSAEKVART 234
Cdd:PRK06924 160 GLDMFTQTVATEqeEEEYPVKIVAFSPGVMDTNM--QAQIRSSSKEDFTNLDRFITLKEEGKLLS 222
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
11-215 1.01e-05

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 45.63  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQtaAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK08993   9 EGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVE--PTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGpihgchVFTPILRDAESRAPRG----IINVASAAAFGAAPGMAAY 166
Cdd:PRK08993  87 DILV--NNAGLIRREDAIEFSEKDWDDVMNLNIKS------VFFMSQAAAKHFIAQGnggkIINIASMLSFQGGIRVPSY 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 497642378 167 NVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSE 215
Cdd:PRK08993 159 TASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSA 207
PRK08263 PRK08263
short chain dehydrogenase; Provisional
17-196 1.06e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 45.80  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  17 VTGAGSGIGAAFAVELGRRGGAVVCSDIDqtaAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAAPTLVIN 96
Cdd:PRK08263   8 ITGASRGFGRAWTEAALERGDRVVATARD---TATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHF-GRLDIVVN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  97 NAGVGAGGAAIGDaPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRgIINVASAAAFGAAPGMAAYNVSKAGVLSL 176
Cdd:PRK08263  84 NAGYGLFGMIEEV-TESEARAQIDTNFFGALWVTQAVLPYLR--EQRSGH-IIQISSIGGISAFPMSGIYHASKWALEGM 159
                        170       180
                 ....*....|....*....|
gi 497642378 177 SETLAAELAGTPVRVTVLCP 196
Cdd:PRK08263 160 SEALAQEVAEFGIKVTLVEP 179
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
14-97 1.39e-05

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: 45.07  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  14 SAVVTGAGSGIGAAFAVELGRRGGAVVCsdIDQTAAQKTA---DAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFpAA 90
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVAL--AARREAKLEAllvDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEI-GP 77

                 ....*..
gi 497642378  91 PTLVINN 97
Cdd:cd05373   78 LEVLVYN 84
PRK12747 PRK12747
short chain dehydrogenase; Provisional
11-203 1.69e-05

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 45.07  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAV-VCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQAL-----AEQSQ 84
Cdd:PRK12747   3 KGKVALVTGASRGIGRAIAKRLANDGALVaIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALyssldNELQN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  85 AWFPAAPTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDaESRaprgIINVASAAAFGAAPGMA 164
Cdd:PRK12747  83 RTGSTKFDILINNAGIGPGAFIEETTE-QFFDRMVSVNAKAPFFIIQQALSRLRD-NSR----IINISSAATRISLPDFI 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNI 203
Cdd:PRK12747 157 AYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDM 195
PRK12744 PRK12744
SDR family oxidoreductase;
11-96 2.30e-05

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 44.73  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVC----SDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAW 86
Cdd:PRK12744   7 KGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAA 86
                         90
                 ....*....|
gi 497642378  87 FpAAPTLVIN 96
Cdd:PRK12744  87 F-GRPDIAIN 95
PRK08628 PRK08628
SDR family oxidoreductase;
16-201 3.89e-05

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 44.18  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGG-AVVCSDidQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLV 94
Cdd:PRK08628  11 IVTGGASGIGAAISLRLAEEGAiPVIFGR--SAPDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 iNNAGVGAGGAAIGDAplDDWAWTLGINLWGPIHGCHVFTPILRdaesrAPRG-IINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:PRK08628  89 -NNAGVNDGVGLEAGR--EAFVASLERNLIHYYVMAHYCLPHLK-----ASRGaIVNISSKTALTGQGGTSGYAAAKGAQ 160
                        170       180
                 ....*....|....*....|....*...
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK08628 161 LALTREWAVALAKDGVRVNAVIPAEVMT 188
PRK07985 PRK07985
SDR family oxidoreductase;
11-207 4.18e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 44.22  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDI--DQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:PRK07985  48 KDRKALVTGGDSGIGRAAAIAYAREGADVAISYLpvEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  89 AAPTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAESraprgIINVASAAAFGAAPGMAAYNV 168
Cdd:PRK07985 128 GLDIMALVAGKQVAIPDIADLTS-EQFQKTFAINVFALFWLTQEAIPLLPKGAS-----IITTSSIQAYQPSPHLLDYAA 201
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 497642378 169 SKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESG 207
Cdd:PRK07985 202 TKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISG 240
PRK07856 PRK07856
SDR family oxidoreductase;
12-201 4.41e-05

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 43.77  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVcsdidqTAAQKTADAIteQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK07856   6 GRVVLVTGGTRGIGAGIARAFLAAGATVV------VCGRRAPETV--DGRPAEFHAADVRDPDQVAALVDAIVERHGRLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNAGVGAGGAAIGDAPLDDWAwTLGINLWGPIHGCHVFTPILRDAESRAprGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK07856  78 VLV-NNAGGSPYALAAEASPRFHEK-IVELNLLAPLLVAQAANAVMQQQPGGG--SIVNIGSVSGRRPSPGTAAYGAAKA 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTpVRVTVLCPTFVKT 201
Cdd:PRK07856 154 GLLNLTRSLAVEWAPK-VRVNAVVVGLVRT 182
PRK06198 PRK06198
short chain dehydrogenase; Provisional
12-201 4.95e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 43.84  E-value: 4.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGA-VVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK06198   6 GKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaESRAPRGIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK06198  86 DALV--NAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMR--RRKAEGTIVNIGSMSAHGGQPFLAAYCASK 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK06198 162 GALATLTRNAAYALLRNRIRVNGLNIGWMAT 192
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
13-89 6.28e-05

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: 42.55  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   13 ASAVVTGAGSGIGAAFAVELGRRGGA--VVCS--DIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFP 88
Cdd:pfam08659   1 GTYLITGGLGGLGRELARWLAERGARhlVLLSrsAAPRPDAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGP 80

                  .
gi 497642378   89 A 89
Cdd:pfam08659  81 P 81
PRK06179 PRK06179
short chain dehydrogenase; Provisional
15-238 8.21e-05

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 42.97  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSdidqtaAQKTADAITEQGGKAIAirCDVSRFDEVQALAEQ--SQAwfpAAPT 92
Cdd:PRK06179   7 ALVTGASSGIGRATAEKLARAGYRVFGT------SRNPARAAPIPGVELLE--LDVTDDASVQAAVDEviARA---GRID 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LVINNAGVGAGGAAIGDAPldDWAWTL-GINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK06179  76 VLVNNAGVGLAGAAEESSI--AQAQALfDTNVFGILRMTRAVLPHMR----AQGSGrIINISSVLGFLPAPYMALYAASK 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497642378 171 AGVLSLSETLAAELAGTPVRVTVLCPTFVKTN-----------ILESGRISEQSSELATKLMRwTGLSAEKVARTCLDA 238
Cdd:PRK06179 150 HAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNfdanapepdspLAEYDRERAVVSKAVAKAVK-KADAPEVVADTVVKA 227
PRK06940 PRK06940
short chain dehydrogenase; Provisional
16-85 8.23e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 43.08  E-value: 8.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGsGIGAAFAVELGRrGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQA 85
Cdd:PRK06940   6 VVIGAG-GIGQAIARRVGA-GKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQT 73
PRK06124 PRK06124
SDR family oxidoreductase;
12-201 8.50e-05

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 43.16  E-value: 8.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK06124  11 GQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLViNNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGChvftpilRDAESRAPRG----IINVASAAAFGAAPGMAAYN 167
Cdd:PRK06124  91 ILV-NNVGARDRRPLAELDD-AAIRALLETDLVAPILLS-------RLAAQRMKRQgygrIIAITSIAGQVARAGDAVYP 161
                        170       180       190
                 ....*....|....*....|....*....|....
gi 497642378 168 VSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK06124 162 AAKQGLTGLMRALAAEFGPHGITSNAIAPGYFAT 195
PRK06523 PRK06523
short chain dehydrogenase; Provisional
11-238 1.23e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 42.58  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAfAVELGRRGGAVVCsdidqTAAQKTADAITEQggkAIAIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK06523   8 AGKRALVTGGTKGIGAA-TVARLLEAGARVV-----TTARSRPDDLPEG---VEFVAADLTTAEGCAAVARAVLERLGGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRDAESRAprgIINVASAAAFG-AAPGMAAYNVS 169
Cdd:PRK06523  79 DILVHVLGGSSAPAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGV---IIHVTSIQRRLpLPESTTAYAAA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTnilesgrisEQSSELATKLMRWTGLSAEKVARTCLDA 238
Cdd:PRK06523 156 KAALSTYSKSLSKEVAPKGVRVNTVSPGWIET---------EAAVALAERLAEAAGTDYEGAKQIIMDS 215
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
12-96 1.28e-04

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: 42.43  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVcsdidqtAAQKTADA--------------ITEQGGKAIAIRCDVSRFDEVQ 77
Cdd:cd09762    3 GKTLFITGASRGIGKAIALKAARDGANVV-------IAAKTAEPhpklpgtiytaaeeIEAAGGKALPCIVDIRDEDQVR 75
                         90
                 ....*....|....*....
gi 497642378  78 ALAEQSQAWFPAAPTLVIN 96
Cdd:cd09762   76 AAVEKAVEKFGGIDILVNN 94
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
12-201 1.28e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 42.45  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAP 91
Cdd:PRK07523  10 GRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  92 TLVinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIhgcHVFTPILRDAESRAPRGIINVASAAAFGAAPGMAAYNVSKA 171
Cdd:PRK07523  90 ILV--NNAGMQFRTPLEDFPADAFERLLRTNISSVF---YVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKG 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 497642378 172 GVLSLSETLAAELAGTPVRVTVLCPTFVKT 201
Cdd:PRK07523 165 AVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK06125 PRK06125
short chain dehydrogenase; Provisional
11-151 1.35e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 42.34  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRC-DVSRFDEVQALAEQSqawfpA 89
Cdd:PRK06125   6 AGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHAlDLSSPEAREQLAAEA-----G 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497642378  90 APTLVINNAGVGAGGAAIGdapLDDWAWTLGINL--WGPIHGCHVFTPILRdaeSRAPRGIINV 151
Cdd:PRK06125  81 DIDILVNNAGAIPGGGLDD---VDDAAWRAGWELkvFGYIDLTRLAYPRMK---ARGSGVIVNV 138
PRK06197 PRK06197
short chain dehydrogenase; Provisional
12-97 2.19e-04

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 41.93  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQ--GGKAIAIRCDVSRFDEVQALAEQSQAWFPA 89
Cdd:PRK06197  16 GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAAtpGADVTLQELDLTSLASVRAAADALRAAYPR 95

                 ....*...
gi 497642378  90 ApTLVINN 97
Cdd:PRK06197  96 I-DLLINN 102
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
12-82 2.20e-04

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 41.92  E-value: 2.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTaaqktadaiTEQGGKAIAIRCDVSRFDEVQALAEQ 82
Cdd:PRK06171   9 GKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGG---------DGQHENYQFVPTDVSSAEEVNHTVAE 70
PRK05875 PRK05875
short chain dehydrogenase; Provisional
14-211 2.23e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 41.71  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  14 SAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAiAIR---CDVSRFDEVQALAEQSQAWFPAA 90
Cdd:PRK05875   9 TYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKGAG-AVRyepADVTDEDQVARAVDAATAWHGRL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  91 PTLVinnAGVGAGGAAIGDAPLDDWAW--TLGINLWGPIHgchvftpILRDAESRAPRG----IINVASAAAFGAAPGMA 164
Cdd:PRK05875  88 HGVV---HCAGGSETIGPITQIDSDAWrrTVDLNVNGTMY-------VLKHAARELVRGgggsFVGISSIAASNTHRWFG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497642378 165 AYNVSKAGVLSLSETLAAELAGTPVRVTVLCPTFVKTN----ILESGRISE 211
Cdd:PRK05875 158 AYGVTKSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDlvapITESPELSA 208
PRK05693 PRK05693
SDR family oxidoreductase;
14-233 2.23e-04

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 41.70  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  14 SAVVTGAGSGIGAAFAVELGRRGGAVVCSdidqtaAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTL 93
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWAT------ARKAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGLDVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 VinNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRGIINVASAAAFGAAPGMAAYNVSKAGV 173
Cdd:PRK05693  77 I--NNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLR----RSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378 174 LSLSETLAAELAGTPVRVTVLCPTFVKTNILESGriSEQSSELATKLMRWTGLSAEKVAR 233
Cdd:PRK05693 151 HALSDALRLELAPFGVQVMEVQPGAIASQFASNA--SREAEQLLAEQSPWWPLREHIQAR 208
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
12-82 2.39e-04

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: 41.81  E-value: 2.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAV--VCSDIDQtAAQKTADAITEQGGKAIAIR-CDVSRFDEVQALAEQ 82
Cdd:cd09808    1 GRSFLITGANSGIGKAAALAIAKRGGTVhmVCRNQTR-AEEARKEIETESGNQNIFLHiVDMSDPKQVWEFVEE 73
PRK07677 PRK07677
short chain dehydrogenase; Provisional
16-183 2.61e-04

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 41.59  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPTLvI 95
Cdd:PRK07677   5 IITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDAL-I 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 NNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVftpILRDAESRAPRG-IINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:PRK07677  84 NNAAGNFICPAEDLSV-NGWNSVIDIVLNGTFYCSQA---VGKYWIEKGIKGnIINMVATYAWDAGPGVIHSAAAKAGVL 159

                 ....*....
gi 497642378 175 SLSETLAAE 183
Cdd:PRK07677 160 AMTRTLAVE 168
PRK07576 PRK07576
short chain dehydrogenase; Provisional
12-87 3.45e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 41.09  E-value: 3.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497642378  12 GASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWF 87
Cdd:PRK07576   9 GKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEF 84
PRK07023 PRK07023
SDR family oxidoreductase;
15-214 4.10e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 40.77  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCsdidqTAAQKTADAITEQGGKAIAIRCDVSRFDEVQA-LAEQSQAWFPAAPTL 93
Cdd:PRK07023   4 AIVTGHSRGLGAALAEQLLQPGIAVLG-----VARSRHPSLAAAAGERLAEVELDLSDAAAAAAwLAGDLLAAFVDGASR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  94 V--INNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIhgchVFTPILRDAESR-APRGIINVASAAAFGAAPGMAAYNVSK 170
Cdd:PRK07023  79 VllINNAGTVEPIGPLATLDAAAIARAVGLNVAAPL----MLTAALAQAASDaAERRILHISSGAARNAYAGWSVYCATK 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 497642378 171 AGVLSLSETLAAElAGTPVRVTVLCPTFVKTNILESGRISEQSS 214
Cdd:PRK07023 155 AALDHHARAVALD-ANRALRIVSLAPGVVDTGMQATIRATDEER 197
PRK08703 PRK08703
SDR family oxidoreductase;
7-196 6.25e-04

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 40.30  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378   7 PKISRGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGG-KAIAIRCDV--SRFDEVQALAEQS 83
Cdd:PRK08703   1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHpEPFAIRFDLmsAEEKEFEQFAATI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  84 QAWFPAAPTLVINNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPILRdaesRAPRG-IINVASAAAFGAAPG 162
Cdd:PRK08703  81 AEATQGKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLK----QSPDAsVIFVGESHGETPKAY 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 497642378 163 MAAYNVSKAGVLSLSETLAAELAGTP-VRVTVLCP 196
Cdd:PRK08703 157 WGGFGASKAALNYLCKVAADEWERFGnLRANVLVP 191
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
15-235 7.94e-04

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 40.00  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVV--CSDiDQTAAQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQAWFPAAPT 92
Cdd:PRK12938   6 AYVTGGMGGIGTSICQRLHKDGFKVVagCGP-NSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEIDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  93 LVinNAGVGAGGAAIGDAPLDDWAWTLGINLwgpihgCHVFTPILRDAESRAPRG---IINVASAAAFGAAPGMAAYNVS 169
Cdd:PRK12938  85 LV--NNAGITRDVVFRKMTREDWTAVIDTNL------TSLFNVTKQVIDGMVERGwgrIINISSVNGQKGQFGQTNYSTA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497642378 170 KAGVLSLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMRWTGLSAEkVARTC 235
Cdd:PRK12938 157 KAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVATIPVRRLGSPDE-IGSIV 221
PRK05854 PRK05854
SDR family oxidoreductase;
11-97 8.94e-04

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 40.05  E-value: 8.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  11 RGASAVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKA-IAIR-CDVSRFDEVQALAEQSQAwfP 88
Cdd:PRK05854  13 SGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAVPDAkLSLRaLDLSSLASVAALGEQLRA--E 90
                         90
                 ....*....|
gi 497642378  89 AAPT-LVINN 97
Cdd:PRK05854  91 GRPIhLLINN 100
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
17-85 1.99e-03

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: 39.01  E-value: 1.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497642378  17 VTGAGSGIGAAFAVELGRRGGAVVCSDIDQtaaQKTADAITEQGGKAIAIRCDVSRFDEVQALAEQSQA 85
Cdd:cd08951   12 ITGSSDGLGLAAARTLLHQGHEVVLHARSQ---KRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNA 77
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
20-79 2.10e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.66  E-value: 2.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642378  20 AGSGIGAaFAVELGRRGGAVVCSDIDQTAAQKTADAITEQGGKAiAIRCDVS-------RFDEVQAL 79
Cdd:PRK07580  70 AGCGVGS-LSIPLARRGAKVVASDISPQMVEEARERAPEAGLAG-NITFEVGdlesllgRFDTVVCL 134
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
15-242 2.93e-03

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: 37.88  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSdidqtaaqktadaiteqggkaiaircdVSRFDEVqalaeqsqawFPAAPTLV 94
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSPKVLV---------------------------VSRRDVV----------VHNAAILD 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 INNAGVGAGgaaigdaplDDWAWTLGINLWGPIHGCHVFTPIlrDAESRAPRgIINVASAAAFGAAPGMAAYNVSKAGVL 174
Cdd:cd02266   44 DGRLIDLTG---------SRIERAIRANVVGTRRLLEAAREL--MKAKRLGR-FILISSVAGLFGAPGLGGYAASKAALD 111
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497642378 175 SLSETLAAELAGTPVRVTVLCPTFVKTNILESGRISEQSSELATKLMRWTGlSAEKVARTCLDAHDRG 242
Cdd:cd02266  112 GLAQQWASEGWGNGLPATAVACGTWAGSGMAKGPVAPEEILGNRRHGVRTM-PPEEVARALLNALDRP 178
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
14-149 3.82e-03

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: 38.27  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  14 SAVVTGAGSGIGAAFAVELGRRGG---AVVCSDIDQtAAQKTADAITEQGGKAIaIRCDVSRFDEVQALAEQSQAWFPAA 90
Cdd:cd09810    3 TVVITGASSGLGLAAAKALARRGEwhvVMACRDFLK-AEQAAQEVGMPKDSYSV-LHCDLASLDSVRQFVDNFRRTGRPL 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497642378  91 PTLVINNAGVGAGGAAIGDAPlDDWAWTLGINLWGPIHGCHVFTPILRDAESRAPRGII 149
Cdd:cd09810   81 DALVCNAAVYLPTAKEPRFTA-DGFELTVGVNHLGHFLLTNLLLEDLQRSENASPRIVI 138
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
121-194 4.08e-03

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: 37.69  E-value: 4.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497642378 121 INLWGPIHGCHVFTPILRDAesraprG-IINVASAAAFGAAPGMAAYNVSKAGVLSLSETLAAELAGTPVRVTVL 194
Cdd:cd05334   99 QNLWTSFIASHLATKHLLSG------GlLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENSGLPAGSTAN 167
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
17-199 4.75e-03

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 37.81  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  17 VTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADaitEQGGKAIAIRCDV-SRFDEVQALAEQSQAWfpAAPTLVI 95
Cdd:PRK10538   5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKD---ELGDNLYIAQLDVrNRAAIEEMLASLPAEW--RNIDVLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  96 NNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHGCHVFTPilrDAESRAPRGIINVASAAAFGAAPGMAAYNVSKAGVLS 175
Cdd:PRK10538  80 NNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLP---GMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQ 156
                        170       180
                 ....*....|....*....|....
gi 497642378 176 LSETLAAELAGTPVRVTVLCPTFV 199
Cdd:PRK10538 157 FSLNLRTDLHGTAVRVTDIEPGLV 180
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
15-242 5.95e-03

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 37.12  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  15 AVVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAITeqggkAIAIRCDVSRFDEVQALAEQSqawfPAAPTLV 94
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVG-----ALARPADVAAELEVWALAQEL----GPLDLLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497642378  95 inNAGVGAGGAAIGDAPLDDWAWTLGINLWGPIHgchvftpILRDAESRAPRG--IINVASAAAFGAAPGMAAYNVSKAG 172
Cdd:cd11730   72 --YAAGAILGKPLARTKPAAWRRILDANLTGAAL-------VLKHALALLAAGarLVFLGAYPELVMLPGLSAYAAAKAA 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497642378 173 VLSLSETLAAELAGtpVRVTVLCPTFVKTNILES-GRISEQSselatklmrwtgLSAEKVARTCLDAHDRG 242
Cdd:cd11730  143 LEAYVEVARKEVRG--LRLTLVRPPAVDTGLWAPpGRLPKGA------------LSPEDVAAAILEAHQGE 199
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
16-82 7.57e-03

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 37.27  E-value: 7.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQTAAQKTADAiteqgGKAIAIRCDVSRFDEVQALAEQ 82
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAAL-----PGVEFVRGDLRDPEALAAALAG 64
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
16-64 7.57e-03

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: 37.09  E-value: 7.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 497642378  16 VVTGAGSGIGAAFAVELGRRGGAVVCSDIDQtaAQKTADAITEQGGKAI 64
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGIDLRE--ADVIADLSTPEGRAAA 49
 
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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