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Conserved domains on  [gi|649109145|gb|AIC51542|]
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DHRS7, partial [synthetic construct]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143187)

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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0051287
SCOP:  4000029

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
48-308 2.42e-137

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: 390.02  E-value: 2.42e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGA---PSPHVVPLDMSDLEDAEQVVEEALK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:cd05332   78 LFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 208 HALRGFFNGLRTELAtYPGIIVSNICPGPVQSNIVENSLAGEVTKTIGNNGDQSHKMTTSRCVRLMLISMANDLKEVWIS 287
Cdd:cd05332  158 HALQGFFDSLRAELS-EPNISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTANGMSPEECALEILKAIALRKREVFYA 236
                        250       260
                 ....*....|....*....|.
gi 649109145 288 EQPFLLVTYLWQYMPTWAWWI 308
Cdd:cd05332  237 RQVPLLAVYLRQLFPGLFDWL 257
 
Name Accession Description Interval E-value
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
48-308 2.42e-137

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: 390.02  E-value: 2.42e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGA---PSPHVVPLDMSDLEDAEQVVEEALK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:cd05332   78 LFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 208 HALRGFFNGLRTELAtYPGIIVSNICPGPVQSNIVENSLAGEVTKTIGNNGDQSHKMTTSRCVRLMLISMANDLKEVWIS 287
Cdd:cd05332  158 HALQGFFDSLRAELS-EPNISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTANGMSPEECALEILKAIALRKREVFYA 236
                        250       260
                 ....*....|....*....|.
gi 649109145 288 EQPFLLVTYLWQYMPTWAWWI 308
Cdd:cd05332  237 RQVPLLAVYLRQLFPGLFDWL 257
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
48-312 9.07e-75

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 230.91  E-value: 9.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAG----ARVEVVALDVTDPDAVAALAEAVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:COG0300   79 RFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSlagevtktigNNGDQSHKMTTSRCVRLMLISMANDLKEVWIS 287
Cdd:COG0300  159 AALEGFSESLRAELAPT-GVRVTAVCPGPVDTPFTARA----------GAPAGRPLLSPEEVARAILRALERGRAEVYVG 227
                        250       260
                 ....*....|....*....|....*
gi 649109145 288 eQPFLLVTYLWQYMPTWAWWITNKM 312
Cdd:COG0300  228 -WDARLLARLLRLLPRLFDRLLRRA 251
PRK06181 PRK06181
SDR family oxidoreductase;
52-278 6.51e-63

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 200.97  E-value: 6.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK06181   3 VVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGG----EALVVPTDVSDAEACERLIEAAVARFGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTS-LDVYRKLIELNYLGTVSLTKCVLPHMIERkQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK06181  79 IDILVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHAL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649109145 211 RGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLAGEvTKTIGNNGDQSHK-MTTSRCVRLMLISMA 278
Cdd:PRK06181 158 HGFFDSLRIELAD-DGVAVTVVCPGFVATDIRKRALDGD-GKPLGKSPMQESKiMSAEECAEAILPAIA 224
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
52-249 1.55e-58

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 187.44  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145   52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALG----GKALFIQGDVTDRAQVKALVEQAVERLGR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:pfam00106  78 LDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 649109145  212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:pfam00106 158 GFTRSLALELAPH-GIRVNAVAPGGVDTDMTKELREDE 194
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
52-247 1.07e-30

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 116.70  E-value: 1.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145   52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:TIGR01963   3 TALVTGAASGIGLAIARALAAAGANVVVNDFGEEGAEAAAKVAGDAGG----SVIYLPADVTKEDEIADMIAAAAAEFGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:TIGR01963  79 LDILVNNAGIQHVAPIEEFPPEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHGLVASPFKSAYVAAKHGLI 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 649109145  212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLA 247
Cdd:TIGR01963 159 GLTKVLALEVAEH-GITVNAICPGYVRTPLVEKQIA 193
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
55-254 2.97e-09

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 56.47  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHEL-ERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRID 133
Cdd:NF012208   3 VTGSARGIGRAIALALAREGFDVAVHYRRSAEAaEQTAQEAEALG----VKAITLQADLTDPEQARSLVEEAAEALGGLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNN-GGMSQRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTvnsiLG------IISVPLSIGYCAS 206
Cdd:NF012208  79 VLVNNvGNYLHKPL-LETTDEEWHEMLDSNLNATFYVTQAALPLMRAAGWGRIVN----LGyagaqnLLARPGITPYVIA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGpvqsnIVENSlageVTKTI 254
Cdd:NF012208 154 KTGVIIYSKALAKELAGD-GITVNVVSPG-----VAENS----VSQPL 191
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
52-235 3.92e-07

mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function.


Pssm-ID: 468513 [Multi-domain]  Cd Length: 256  Bit Score: 50.44  E-value: 3.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLV-LSARRVHEL-----ERVKRRCLENGNLKEKDILVLplDLTDTGSHEAATKAV 125
Cdd:NF040491   2 VALVTGAARGIGAATVRRLAARGYAVVaVDACAGDPApyplgTEADLDALVASSPGRVETVVA--DVRDRAALAAAVALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVN-----NGGmsqRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIER---KQGKIVTVNSILGIISV 197
Cdd:NF040491  80 LDRWGRLDAAVAaaaviAGG---RPL-WETPPEELDALWDVDVRGVWNLAAAAVPALLAGpdpRGCRFVAVASAAGHRGL 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 198 PLSIGYCASKHALRGFFNGLRTELATyPGIIVSNICPG 235
Cdd:NF040491 156 FHLAAYCAAKHAVVGLVRGLAADLAG-TGVTACAVSPG 192
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
52-153 4.73e-04

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: 40.54  E-value: 4.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145    52 VVWVTGASSGIGEELAYQLSKLGV-SLVLSARRVHELERVKRRCLENGNLKEkDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAELEAAGA-RVTVVACDVADRDALAAVLAAIPAVEG 80
                           90       100
                   ....*....|....*....|...
gi 649109145   131 RIDILVNNGGMSQRSLCMDTSLD 153
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPE 103
 
Name Accession Description Interval E-value
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
48-308 2.42e-137

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: 390.02  E-value: 2.42e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGA---PSPHVVPLDMSDLEDAEQVVEEALK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:cd05332   78 LFGGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 208 HALRGFFNGLRTELAtYPGIIVSNICPGPVQSNIVENSLAGEVTKTIGNNGDQSHKMTTSRCVRLMLISMANDLKEVWIS 287
Cdd:cd05332  158 HALQGFFDSLRAELS-EPNISVTVVCPGLIDTNIAMNALSGDGSMSAKMDDTTANGMSPEECALEILKAIALRKREVFYA 236
                        250       260
                 ....*....|....*....|.
gi 649109145 288 EQPFLLVTYLWQYMPTWAWWI 308
Cdd:cd05332  237 RQVPLLAVYLRQLFPGLFDWL 257
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
48-312 9.07e-75

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 230.91  E-value: 9.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:COG0300    3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAG----ARVEVVALDVTDPDAVAALAEAVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:COG0300   79 RFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSlagevtktigNNGDQSHKMTTSRCVRLMLISMANDLKEVWIS 287
Cdd:COG0300  159 AALEGFSESLRAELAPT-GVRVTAVCPGPVDTPFTARA----------GAPAGRPLLSPEEVARAILRALERGRAEVYVG 227
                        250       260
                 ....*....|....*....|....*
gi 649109145 288 eQPFLLVTYLWQYMPTWAWWITNKM 312
Cdd:COG0300  228 -WDARLLARLLRLLPRLFDRLLRRA 251
PRK06181 PRK06181
SDR family oxidoreductase;
52-278 6.51e-63

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 200.97  E-value: 6.51e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK06181   3 VVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGG----EALVVPTDVSDAEACERLIEAAVARFGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTS-LDVYRKLIELNYLGTVSLTKCVLPHMIERkQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK06181  79 IDILVNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHAL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 649109145 211 RGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLAGEvTKTIGNNGDQSHK-MTTSRCVRLMLISMA 278
Cdd:PRK06181 158 HGFFDSLRIELAD-DGVAVTVVCPGFVATDIRKRALDGD-GKPLGKSPMQESKiMSAEECAEAILPAIA 224
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
49-254 4.23e-62

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: 198.10  E-value: 4.23e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  49 TDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnlkekdILVLPLDLTDTGSHEAATKAVLQE 128
Cdd:COG4221    4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGR-------ALAVPLDVTDEAAVEAAVAAAVAE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 129 FGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKH 208
Cdd:COG4221   77 FGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKA 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 649109145 209 ALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEVTKTI 254
Cdd:COG4221  157 AVRGLSESLRAELRPT-GIRVTVIEPGAVDTEFLDSVFDGDAEAAA 201
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
52-246 4.20e-61

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: 195.53  E-value: 4.20e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELErvkrrclENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05374    2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLE-------SLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:cd05374   75 IDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALE 154
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVENSL 246
Cdd:cd05374  155 ALSESLRLELAPF-GIKVTIIEPGPVRTGFADNAA 188
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
52-249 1.55e-58

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 187.44  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145   52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALG----GKALFIQGDVTDRAQVKALVEQAVERLGR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:pfam00106  78 LDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVI 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 649109145  212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:pfam00106 158 GFTRSLALELAPH-GIRVNAVAPGGVDTDMTKELREDE 194
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
48-249 7.97e-55

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: 179.60  E-value: 7.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:COG1028    4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGG----RALAVAADVTDEAAVEALVAAAVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:COG1028   80 AFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:COG1028  160 AAVVGLTRSLALELAPR-GIRVNAVAPGPIDTPMTRALLGAE 200
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
53-249 1.67e-53

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: 175.55  E-value: 1.67e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekdILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIEALGGN-----AVAVQADVSDEEDVEALVEEALEEFGRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:cd05233   76 DILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEG 155
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 213 FFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:cd05233  156 LTRSLALELAPY-GIRVNAVAPGLVDTPMLAKLGPEE 191
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
51-239 6.27e-44

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: 151.28  E-value: 6.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  51 MVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRClenGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:cd05346    1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADEL---GAKFPVKVLPLQLDVSDRESIEAALENLPEEFR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSqrsLCMDT----SLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:cd05346   78 DIDILVNNAGLA---LGLDPaqeaDLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCAT 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 207 KHALRGFFNGLRTELATYPgIIVSNICPGPVQS 239
Cdd:cd05346  155 KAAVRQFSLNLRKDLIGTG-IRVTNIEPGLVET 186
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
52-244 6.61e-44

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: 151.24  E-value: 6.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05339    1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGG----KVHYYKCDVSKREEVYEAAKKIKKEVGD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:cd05339   77 VTILINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAV 156
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 212 GFFNGLRTELATY--PGIIVSNICPGPVQSNIVEN 244
Cdd:cd05339  157 GFHESLRLELKAYgkPGIKTTLVCPYFINTGMFQG 191
PRK06182 PRK06182
short chain dehydrogenase; Validated
52-267 1.98e-42

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 148.18  E-value: 1.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELErvkrrclengNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQGYTVYGAARRVDKME----------DLASLGVHPLSLDVTDEASIKAAVDTIIAEEGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:PRK06182  75 IDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPGPVQSN---IVENSLAgEVTKTiGNNGDQSHKMTTS 267
Cdd:PRK06182 155 GFSDALRLEVAPF-GIDVVVIEPGGIKTEwgdIAADHLL-KTSGN-GAYAEQAQAVAAS 210
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
48-264 2.42e-41

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: 144.86  E-value: 2.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnLKEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAG-VSEKKILLVVADLTEEEGQDRIISTTLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKqGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:cd05364   80 KFGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYCISK 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVqsnivenslAGEVTKTIGNNGDQSHKM 264
Cdd:cd05364  159 AALDQFTRCTALELAPK-GVRVNSVSPGVI---------VTGFHRRMGMPEEQYIKF 205
PRK07109 PRK07109
short chain dehydrogenase; Provisional
48-221 2.48e-41

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 146.99  E-value: 2.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK07109   6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGG----EALAVVADVADAEAVQAAADRAEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK07109  82 ELGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAK 161
                        170
                 ....*....|....
gi 649109145 208 HALRGFFNGLRTEL 221
Cdd:PRK07109 162 HAIRGFTDSLRCEL 175
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
52-254 1.60e-40

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: 142.01  E-value: 1.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd08939    3 HVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANASGQKVSYISADLSDYEEVEQAFAQAVEKGGP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGiiSVPLsIG---YCASKH 208
Cdd:cd08939   83 PDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAA--LVGI-YGysaYCPSKF 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 649109145 209 ALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAG--EVTKTI 254
Cdd:cd08939  160 ALRGLAESLRQELKPY-NIRVSVVYPPDTDTPGFEEENKTkpEETKAI 206
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
52-251 4.71e-40

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: 140.58  E-value: 4.71e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRclengnlkEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd08932    2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS--------GGDVEAVPYDARDPEDARALVDALRDRFGR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:cd08932   74 IDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALR 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 649109145 212 GFFNGLRTELAtYPGIIVSNICPGPV------QSNIVENSLAGEVT 251
Cdd:cd08932  154 ALAHALRQEGW-DHGVRVSAVCPGFVdtpmaqGLTLVGAFPPEEMI 198
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
53-246 5.66e-40

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: 140.54  E-value: 5.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRcLENGNlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:cd05350    1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAE-LLNPN---PSVEVEILDVTDEERNQLVIAELEAELGGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:cd05350   77 DLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSS 156
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 213 FFNGLRTELATYpGIIVSNICPGPVQSNIVENSL 246
Cdd:cd05350  157 LAESLRYDVKKR-GIRVTVINPGFIDTPLTANMF 189
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
52-222 7.08e-40

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: 140.21  E-value: 7.08e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05360    2 VVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGG----EAIAVVADVADAAQVERAADTAVERFGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:cd05360   78 IDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVR 157
                        170
                 ....*....|.
gi 649109145 212 GFFNGLRTELA 222
Cdd:cd05360  158 GFTESLRAELA 168
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
48-249 7.87e-39

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: 137.87  E-value: 7.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEG----VEATAFTCDVSDEEAIKAAVEAIEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:cd05347   79 DFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASK 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:cd05347  159 GGVAGLTKALATEWARH-GIQVNAIAPGYFATEMTEAVVADP 199
PRK06180 PRK06180
short chain dehydrogenase; Provisional
48-236 1.33e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 138.12  E-value: 1.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVW-VTGASSGIGEELAYQLSKLGVSLVLSARRvheleRVKRRCLENGNlkEKDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK06180   1 MSSMKTWlITGVSSGFGRALAQAALAAGHRVVGTVRS-----EAARADFEALH--PDRALARLLDVTDFDAIDAVVADAE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPlSIG-YCA 205
Cdd:PRK06180  74 ATFGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMP-GIGyYCG 152
                        170       180       190
                 ....*....|....*....|....*....|.
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPGP 236
Cdd:PRK06180 153 SKFALEGISESLAKEVAPF-GIHVTAVEPGS 182
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
48-254 1.76e-37

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: 134.20  E-value: 1.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGG----KALVLELDVTDEQQVDAAVERTVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:cd08934   77 ALGRLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 649109145 208 HALRGFFNGLRTELaTYPGIIVSNICPGpvqsnIVENSLAGEVTKTI 254
Cdd:cd08934  157 FGVNAFSEGLRQEV-TERGVRVVVIEPG-----TVDTELRDHITHTI 197
PRK06914 PRK06914
SDR family oxidoreductase;
55-248 3.06e-37

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 134.77  E-value: 3.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRcLENGNLKEKdILVLPLDLTDTGSHEAATKaVLQEFGRIDI 134
Cdd:PRK06914   8 VTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQ-ATQLNLQQN-IKVQQLDVTDQNSIHNFQL-VLKEIGRIDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 135 LVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRGFF 214
Cdd:PRK06914  85 LVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYALEGFS 164
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 215 NGLRTELATYpGIIVSNICPGPVQSNIVENSLAG 248
Cdd:PRK06914 165 ESLRLELKPF-GIDVALIEPGSYNTNIWEVGKQL 197
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
48-241 3.12e-37

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 133.81  E-value: 3.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHE--LERVKRrclengnLKEKDILVLPL--DLTDTGSHEAATK 123
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEaaQELLEE-------IKEEGGDAIAVkaDVSSEEDVENLVE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 AVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGY 203
Cdd:PRK05565  76 QIVEKFGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLY 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 204 CASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNI 241
Cdd:PRK05565 156 SASKGAVNAFTKALAKELAPS-GIRVNAVAPGAIDTEM 192
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
48-245 7.96e-37

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 132.59  E-value: 7.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK05653   3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGG----EARVLVFDVSDEAAVRALIEAAVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK05653  79 AFGALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAK 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENS 245
Cdd:PRK05653 159 AGVIGFTKALALELASR-GITVNAVAPGFIDTDMTEGL 195
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
52-247 1.04e-36

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 132.30  E-value: 1.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHE-LERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK12825   8 VALVTGAARGLGRAIALRLARAGADVVVHYRSDEEaAEELVEAVEALG----RRAQAVQADVTDKAALEAAVAAAVERFG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK12825  84 RIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKAGL 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLA 247
Cdd:PRK12825 164 VGLTKALARELAEY-GITVNMVAPGDIDTDMKEATIE 199
PRK06179 PRK06179
short chain dehydrogenase; Provisional
52-246 4.94e-36

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 131.18  E-value: 4.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSAR---RVHELERVKrrclengnlkekdilVLPLDLTDTGSHEAATKAVLQE 128
Cdd:PRK06179   6 VALVTGASSGIGRATAEKLARAGYRVFGTSRnpaRAAPIPGVE---------------LLELDVTDDASVQAAVDEVIAR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 129 FGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKH 208
Cdd:PRK06179  71 AGRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASKH 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 209 ALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSL 246
Cdd:PRK06179 151 AVEGYSESLDHEVRQF-GIRVSLVEPAYTKTNFDANAP 187
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
52-244 7.85e-36

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: 129.98  E-value: 7.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVkrrcLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05333    2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAET----VEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:cd05333   78 VDILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKAGVI 157
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVEN 244
Cdd:cd05333  158 GFTKSLAKELASR-GITVNAVAPGFIDTDMTDA 189
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
47-254 9.14e-36

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 129.93  E-value: 9.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARR-VHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAV 125
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVINYASsEAGAEALVAEIGALG----GKALAVQGDVSDAESVERAVDEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK05557  78 KAEFGGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYAA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVEnSLAGEVTKTI 254
Cdd:PRK05557 158 SKAGVIGFTKSLARELASR-GITVNAVAPGFIETDMTD-ALPEDVKEAI 204
PRK12826 PRK12826
SDR family oxidoreductase;
47-257 3.50e-34

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 125.80  E-value: 3.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRcLENGNLKekdILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAEL-VEAAGGK---ARARQVDVRDRAALKAAVAAGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISV-PLSIGYCA 205
Cdd:PRK12826  79 EDFGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGyPGLAHYAA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEVTKTIGNN 257
Cdd:PRK12826 159 SKAGLVGFTRALALELAAR-NITVNSVHPGGVDTPMAGNLGDAQWAEAIAAA 209
PRK09072 PRK09072
SDR family oxidoreductase;
48-222 5.91e-34

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 125.44  E-value: 5.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKekdilVLPLDLTDtgshEAATKAVLQ 127
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHR-----WVVADLTS----EAGREAVLA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 ---EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYC 204
Cdd:PRK09072  74 rarEMGGINVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYC 153
                        170
                 ....*....|....*...
gi 649109145 205 ASKHALRGFFNGLRTELA 222
Cdd:PRK09072 154 ASKFALRGFSEALRRELA 171
PRK05993 PRK05993
SDR family oxidoreductase;
55-247 8.68e-34

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 125.52  E-value: 8.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERvkrrcLENGNLKekdilVLPLDLTDTGSHEAATKAVLQEF-GRID 133
Cdd:PRK05993   9 ITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA-----LEAEGLE-----AFQLDYAEPESIAALVAQVLELSgGRLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRGF 213
Cdd:PRK05993  79 ALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKFAIEGL 158
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 214 FNGLRTELATyPGIIVSNICPGPVQSNIVENSLA 247
Cdd:PRK05993 159 SLTLRMELQG-SGIHVSLIEPGPIETRFRANALA 191
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
47-286 3.57e-33

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: 122.96  E-value: 3.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclENGNLKekdilVLPLDLTDTGSHEAATKAVL 126
Cdd:COG3967    2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAA---ANPGLH-----TIVLDVADPASIAALAEQVT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTS--LDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIisVPLSI--G 202
Cdd:COG3967   74 AEFPDLNVLINNAGIMRAEDLLDEAedLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAF--VPLAVtpT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 203 YCASKHALRGFFNGLRTELATYPgIIVSNICPGPVQsnivenslagevTKTIGNNGDQSHKMTTSRCVRLMLISMANDLK 282
Cdd:COG3967  152 YSATKAALHSYTQSLRHQLKDTS-VKVIELAPPAVD------------TDLTGGQGGDPRAMPLDEFADEVMAGLETGKY 218

                 ....
gi 649109145 283 EVWI 286
Cdd:COG3967  219 EILV 222
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
47-284 3.85e-33

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: 122.42  E-value: 3.85e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclENGNLKEKDilvlpLDLTDTGSHEAATKAVL 126
Cdd:cd05370    2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKK---ELPNIHTIV-----LDVGDAESVEALAEALL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMsQRSLCM---DTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGY 203
Cdd:cd05370   74 SEYPNLDILINNAGI-QRPIDLrdpASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 204 CASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLAGEvtktignnGDQSHKMTTSRCVRLMLISMANDLKE 283
Cdd:cd05370  153 CATKAALHSYTLALRHQLKD-TGVEVVEIVPPAVDTELHEERRNPD--------GGTPRKMPLDEFVDEVVAGLERGREE 223

                 .
gi 649109145 284 V 284
Cdd:cd05370  224 I 224
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
52-255 5.82e-33

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: 121.96  E-value: 5.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLG-VSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:cd05324    2 VALVTGANRGIGFEIVRQLAKSGpGTVILTARDVERGQAAVEKLRAEGL----SVRFHQLDVTDDASIEAAADFVEEKYG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDT-SLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPlsigYCASKHA 209
Cdd:cd05324   78 GLDILVNNAGIAFKGFDDSTpTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLTSA----YGVSKAA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 649109145 210 LrgffNGLRTELA---TYPGIIVSNICPGPVQSNIveNSLAGEVTKTIG 255
Cdd:cd05324  154 L----NALTRILAkelKETGIKVNACCPGWVKTDM--GGGKAPKTPEEG 196
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
48-235 6.06e-33

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 122.75  E-value: 6.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALG----IDALWIAADVADEADIERLAEETLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPH-MIERKQGKIVTVNSILGI----ISVPLSIG 202
Cdd:PRK08213  86 RFGHVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGLggnpPEVMDTIA 165
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 203 YCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK08213 166 YNTSKGAVINFTRALAAEWGPH-GIRVNAIAPG 197
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
48-255 1.28e-32

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 121.92  E-value: 1.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAG----GKAIGVAMDVTDEEAINAGIDYAVE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK12429  78 TFGGVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAK 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAgEVTKTIG 255
Cdd:PRK12429 158 HGLIGLTKVVALEGATH-GVTVNAICPGYVDTPLVRKQIP-DLAKERG 203
PRK09291 PRK09291
SDR family oxidoreductase;
55-236 1.59e-32

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 121.64  E-value: 1.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSAR---RVHEL-ERVKRRCLengnlkekDILVLPLDLTDTGSHEAAtkavlQEFG 130
Cdd:PRK09291   7 ITGAGSGFGREVALRLARKGHNVIAGVQiapQVTALrAEAARRGL--------ALRVEKLDLTDAIDRAQA-----AEWD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 rIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK09291  74 -VDVLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASKHAL 152
                        170       180
                 ....*....|....*....|....*.
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPGP 236
Cdd:PRK09291 153 EAIAEAMHAELKPF-GIQVATVNPGP 177
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
55-253 1.86e-32

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: 120.79  E-value: 1.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEKDILVlplDLTDTGSHEAATKAVLQEFgRIDI 134
Cdd:cd05356    6 VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAA---DFSAGDDIYERIEKELEGL-DIGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 135 LVNNGGMSQRSLC--MDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:cd05356   82 LVNNVGISHSIPEyfLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDF 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 649109145 213 FFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEVTKT 253
Cdd:cd05356  162 FSRALYEEYKSQ-GIDVQSLLPYLVATKMSKIRKSSLFVPS 201
PRK07454 PRK07454
SDR family oxidoreductase;
53-279 7.12e-32

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 119.29  E-value: 7.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:PRK07454   9 ALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTG----VKAAAYSIDLSNPEAIAPGIAELLEQFGCP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:PRK07454  85 DVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 649109145 213 FFNGLRTELATYpGIIVSNICPGPVQSNIVEnslagevTKTIGNNGDQShKMTTSRCVRLMLISMAN 279
Cdd:PRK07454 165 FTKCLAEEERSH-GIRVCTITLGAVNTPLWD-------TETVQADFDRS-AMLSPEQVAQTILHLAQ 222
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
52-289 9.81e-32

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: 119.33  E-value: 9.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLsarrVHELERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05323    2 VAIITGGASGIGLATAKLLLKKGAKVAI----LDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVY--RKLIELNYLGTVSLTKCVLPHMIERKQGK---IVTVNSILGIISVPLSIGYCAS 206
Cdd:cd05323   78 VDILINNAGILDEKSYLFAGKLPPpwEKTIDVNLTGVINTTYLALHYMDKNKGGKggvIVNIGSVAGLYPAPQFPVYSAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 207 KHALRGFFNGLRTELATYPGIIVSNICPGPVQSNIVEN---SLAGEVTKTignngdqsHKMTTSRCVRLMLISMANDLK- 282
Cdd:cd05323  158 KHGVVGFTRSLADLLEYKTGVRVNAICPGFTNTPLLPDlvaKEAEMLPSA--------PTQSPEVVAKAIVYLIEDDEKn 229

                 ....*...
gi 649109145 283 -EVWISEQ 289
Cdd:cd05323  230 gAIWIVDG 237
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
47-243 2.50e-31

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: 118.38  E-value: 2.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkeKDILVLPLDLTDTGSHEAATKAVL 126
Cdd:cd05343    3 RWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGY---PTLFPYQCDLSNEEQILSMFSAIR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERK--QGKIVTVNSILG--IISVPLSIG 202
Cdd:cd05343   80 TQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvdDGHIININSMSGhrVPPVSVFHF 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 649109145 203 YCASKHALRGFFNGLRTEL-ATYPGIIVSNICPGPVQSNIVE 243
Cdd:cd05343  160 YAATKHAVTALTEGLRQELrEAKTHIRATSISPGLVETEFAF 201
PRK07201 PRK07201
SDR family oxidoreductase;
42-232 3.43e-31

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 123.91  E-value: 3.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  42 RRPEWELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAA 121
Cdd:PRK07201 363 RDLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGG----TAHAYTCDLTDSAAVDHT 438
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 122 TKAVLQEFGRIDILVNNGGMS-QRSLcmDTSLDV---YRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISV 197
Cdd:PRK07201 439 VKDILAEHGHVDYLVNNAGRSiRRSV--ENSTDRfhdYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNA 516
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 198 PLSIGYCASKHALRGFFNGLRTELATyPGIIVSNI 232
Cdd:PRK07201 517 PRFSAYVASKAALDAFSDVAASETLS-DGITFTTI 550
PRK05866 PRK05866
SDR family oxidoreductase;
43-222 3.58e-31

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 119.08  E-value: 3.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  43 RPEWELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAAT 122
Cdd:PRK05866  33 RQPVDLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGG----DAMAVPCDLSDLDAVDALV 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 123 KAVLQEFGRIDILVNNGGMSQRSLCMDtSLDV---YRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVnSILGIIS--V 197
Cdd:PRK05866 109 ADVEKRIGGVDILINNAGRSIRRPLAE-SLDRwhdVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINV-ATWGVLSeaS 186
                        170       180
                 ....*....|....*....|....*
gi 649109145 198 PLSIGYCASKHALRGFFNGLRTELA 222
Cdd:PRK05866 187 PLFSVYNASKAALSAVSRVIETEWG 211
FabG-like PRK07231
SDR family oxidoreductase;
48-235 5.36e-31

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 117.24  E-value: 5.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRcLENGnlkEKDILVlPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAE-ILAG---GRAIAV-AADVSDEADVEAAVAAALE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQR--SLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK07231  78 RFGSVDILVNNAGTTHRngPL-LDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNA 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK07231 157 SKGAVITLTKALAAELGPD-KIRVNAVAPV 185
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-256 5.85e-31

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 117.10  E-value: 5.85e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRcLENGNLKekdILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEE-VEAYGVK---VVIATADVSDYEEVTAAIEQLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK07666  80 NELGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSAS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQSNivensLAGEVTKTIGN 256
Cdd:PRK07666 160 KFGVLGLTESLMQEVRKH-NIRVTALTPSTVATD-----MAVDLGLTDGN 203
PRK07825 PRK07825
short chain dehydrogenase; Provisional
47-238 9.09e-31

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 117.35  E-value: 9.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVhelERVKRRCLENGNLkekdiLVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDE---ALAKETAAELGLV-----VGGPLDVTDPASFAAFLDAVE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGG-MSQRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK07825  74 ADLGPIDVLVNNAGvMPVGPF-LDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCA 152
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPGPVQ 238
Cdd:PRK07825 153 SKHAVVGFTDAARLELRGT-GVHVSVVLPSFVN 184
PHB_DH TIGR01963
3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain ...
52-247 1.07e-30

3-hydroxybutyrate dehydrogenase; This model represents a subfamily of the short chain dehydrogenases. Characterized members so far as 3-hydroxybutyrate dehydrogenases and are found in species that accumulate ester polmers called polyhydroxyalkanoic acids (PHAs) under certain conditions. Several members of the family are from species not known to accumulate PHAs, including Oceanobacillus iheyensis and Bacillus subtilis. However, polymer formation is not required for there be a role for 3-hydroxybutyrate dehydrogenase; it may be members of this family have the same function in those species.


Pssm-ID: 211705 [Multi-domain]  Cd Length: 255  Bit Score: 116.70  E-value: 1.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145   52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:TIGR01963   3 TALVTGAASGIGLAIARALAAAGANVVVNDFGEEGAEAAAKVAGDAGG----SVIYLPADVTKEDEIADMIAAAAAEFGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:TIGR01963  79 LDILVNNAGIQHVAPIEEFPPEDWDRIIAVMLTSAFHTIRAALPHMKKQGWGRIINIASAHGLVASPFKSAYVAAKHGLI 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 649109145  212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLA 247
Cdd:TIGR01963 159 GLTKVLALEVAEH-GITVNAICPGYVRTPLVEKQIA 193
PRK06139 PRK06139
SDR family oxidoreductase;
47-235 1.17e-30

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 118.28  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEA-ATKAv 125
Cdd:PRK06139   4 PLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALG----AEVLVVPTDVTDADQVKAlATQA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 lQEF-GRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPhmIERKQGKIVTVN--SILGIISVPLSIG 202
Cdd:PRK06139  79 -ASFgGRIDVWVNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALP--IFKKQGHGIFINmiSLGGFAAQPYAAA 155
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 203 YCASKHALRGFFNGLRTELATYPGIIVSNICPG 235
Cdd:PRK06139 156 YSASKFGLRGFSEALRGELADHPDIHVCDVYPA 188
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
57-237 2.40e-30

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: 115.22  E-value: 2.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145   57 GA--SSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclengNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGRIDI 134
Cdd:pfam13561   1 GAanESGIGWAIARALAEEGAEVVLTDLNEALAKRVEE------LAEELGAAVLPCDVTDEEQVEALVAAAVEKFGRLDI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  135 LVNNGGMSQRSLC--MDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:pfam13561  75 LVNNAGFAPKLKGpfLDTSREDFDRALDVNLYSLFLLAKAALPLM--KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEA 152
                         170       180
                  ....*....|....*....|....*
gi 649109145  213 FFNGLRTELATYpGIIVSNICPGPV 237
Cdd:pfam13561 153 LTRYLAVELGPR-GIRVNAISPGPI 176
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
52-246 3.30e-30

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 115.62  E-value: 3.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRvhELERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd08940    4 VALVTGSTSGIGLGIARALAAAGANIVLNGFG--DAAEIEAVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:cd08940   82 VDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHGVV 161
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVENSL 246
Cdd:cd08940  162 GLTKVVALETAGT-GVTCNAICPGWVLTPLVEKQI 195
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
50-239 4.88e-30

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: 115.06  E-value: 4.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  50 DMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKrrclENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEF 129
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAA----SELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 GRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIisVPLSIGYCAS--K 207
Cdd:cd05344   77 GRVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVK--EPEPNLVLSNvaR 154
                        170       180       190
                 ....*....|....*....|....*....|..
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:cd05344  155 AGLIGLVKTLSRELAPD-GVTVNSVLPGYIDT 185
PRK06138 PRK06138
SDR family oxidoreductase;
48-247 1.76e-29

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 113.32  E-value: 1.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGG-----RAFARQGDVGSAEAVEALVDFVAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK06138  78 RWGRLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASK 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 649109145 208 HALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLA 247
Cdd:PRK06138 158 GAIASLTRAMALDHAT-DGIRVNAVAPGTIDTPYFRRIFA 196
PRK08264 PRK08264
SDR family oxidoreductase;
50-237 2.36e-29

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 112.68  E-value: 2.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  50 DMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRvhELERVKRRclengnlkEKDILVLPLDLTDTGSHEAATKAVlqef 129
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGAAKVYAAAR--DPESVTDL--------GPRVVPLQLDVTDPASVAAAAEAA---- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 GRIDILVNNGG-MSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKH 208
Cdd:PRK08264  72 SDVTILVNNAGiFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSASKA 151
                        170       180
                 ....*....|....*....|....*....
gi 649109145 209 ALRGFFNGLRTELATYpGIIVSNICPGPV 237
Cdd:PRK08264 152 AAWSLTQALRAELAPQ-GTRVLGVHPGPI 179
PRK06841 PRK06841
short chain dehydrogenase; Provisional
48-250 6.08e-29

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 112.06  E-value: 6.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLsARRVHELERVKRRcLENGNLKEkdilvLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK06841  13 LSGKVAVVTGGASGIGHAIAELFAAKGARVAL-LDRSEDVAEVAAQ-LLGGNAKG-----LVCDVSDSQSVEAAVAAVIS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK06841  86 AFGRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCASK 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEV 250
Cdd:PRK06841 166 AGVVGMTKVLALEWGPY-GITVNAISPTVVLTELGKKAWAGEK 207
PRK07832 PRK07832
SDR family oxidoreductase;
53-243 1.32e-28

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 111.67  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVA---DARALGGTVPEHRALDISDYDAVAAFAADIHAAHGSM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIE-RKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:PRK07832  80 DVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAaGRGGHLVNVSSAAGLVALPWHAAYSASKFGLR 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVE 243
Cdd:PRK07832 160 GLSEVLRFDLARH-GIGVSVVVPGAVKTPLVN 190
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
47-244 2.22e-28

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 110.66  E-value: 2.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRvHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK08226   3 KLTGKTALITGALQGIGEGIARVFARHGANLILLDIS-PEIEKLADELCGRGH----RCTAVVADVRDPASVAAAIKRAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILG-IISVPLSIGYCA 205
Cdd:PRK08226  78 EKEGRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGdMVADPGETAYAL 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVEN 244
Cdd:PRK08226 158 TKAAIVGLTKSLAVEYAQS-GIRVNAICPGYVRTPMAES 195
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
48-245 3.54e-28

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: 109.42  E-value: 3.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRvhELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATkAVLQ 127
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVYAAVR--DPGSAAHLVAKYGD----KVVPLRLDVTDPESIKAAA-AQAK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EfgrIDILVNNGGMSQ-RSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:cd05354   74 D---VDVVINNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTYSAS 150
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENS 245
Cdd:cd05354  151 KSAAYSLTQGLRAELAAQ-GTLVLSVHPGPIDTRMAAGA 188
PRK07024 PRK07024
SDR family oxidoreductase;
53-235 3.94e-28

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 110.02  E-value: 3.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAA-----RVSVYAADVRDADALAAAAADFIAAHGLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRslcMDTS----LDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKH 208
Cdd:PRK07024  80 DVVIANAGISVG---TLTEeredLAVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKA 156
                        170       180
                 ....*....|....*....|....*..
gi 649109145 209 ALRGFFNGLRTELATyPGIIVSNICPG 235
Cdd:PRK07024 157 AAIKYLESLRVELRP-AGVRVVTIAPG 182
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
48-246 4.75e-28

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: 109.92  E-value: 4.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIAP--DAEVLLIKADVSDEAQVEAYVDATVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQR-SLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:cd05330   79 QFGRIDGFFNNAGIEGKqNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSL 246
Cdd:cd05330  159 KHGVVGLTRNSAVEYGQY-GIRINAIAPGAILTPMVEGSL 197
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
52-247 6.75e-28

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 109.47  E-value: 6.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLgvslvlSARRVHELERVKrrclengNLKEKDILV-------------LPLDLTDTGSH 118
Cdd:cd09806    2 VVLITGCSSGIGLHLAVRLASD------PSKRFKVYATMR-------DLKKKGRLWeaagalaggtletLQLDVCDSKSV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 119 EAATKAVLQefGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVP 198
Cdd:cd09806   69 AAAVERVTE--RHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLP 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 649109145 199 LSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLA 247
Cdd:cd09806  147 FNDVYCASKFALEGLCESLAVQLLPF-NVHLSLIECGPVHTAFMEKVLG 194
PRK07890 PRK07890
short chain dehydrogenase; Provisional
48-235 1.45e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 108.51  E-value: 1.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLG----RRALAVPTDITDEDQCANLVALALE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGM--SQRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKqGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK07890  79 RFGRVDALVNNAFRvpSMKPL-ADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAYKM 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK07890 157 AKGALLAASQSLATELGPQ-GIRVNSVAPG 185
PRK07326 PRK07326
SDR family oxidoreductase;
47-245 2.62e-27

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 107.02  E-value: 2.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekdILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGN-----VLGLAADVRDEADVQRAVDAIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKqGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK07326  78 AAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGGAAYNAS 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENS 245
Cdd:PRK07326 157 KFGLVGFSEAAMLDLRQY-GIKVSTIMPGSVATHFNGHT 194
PRK05872 PRK05872
short chain dehydrogenase; Provisional
42-222 1.15e-26

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 106.98  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  42 RRPEWELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLEngnlkEKDILVLPLDLTDTGSHEAA 121
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGG-----DDRVLTVVADVTDLAAMQAA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 122 TKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKqGKIVTVNSILGIISVPLSI 201
Cdd:PRK05872  76 AEEAVERFGGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAAFAAAPGMA 154
                        170       180
                 ....*....|....*....|.
gi 649109145 202 GYCASKHALRGFFNGLRTELA 222
Cdd:PRK05872 155 AYCASKAGVEAFANALRLEVA 175
PRK08263 PRK08263
short chain dehydrogenase; Provisional
53-236 1.31e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 106.28  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VW-VTGASSGIGEELAYQLSKLGVSLVLSARRVHELErvkrrclengNLKEK---DILVLPLDLTDTGSHEAATKAVLQE 128
Cdd:PRK08263   5 VWfITGASRGFGRAWTEAALERGDRVVATARDTATLA----------DLAEKygdRLLPLALDVTDRAAVFAAVETAVEH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 129 FGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKH 208
Cdd:PRK08263  75 FGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKW 154
                        170       180
                 ....*....|....*....|....*...
gi 649109145 209 ALRGFFNGLRTELATYpGIIVSNICPGP 236
Cdd:PRK08263 155 ALEGMSEALAQEVAEF-GIKVTLVEPGG 181
PRK07775 PRK07775
SDR family oxidoreductase;
42-239 1.46e-26

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 105.99  E-value: 1.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  42 RRPeweltdmvVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAA 121
Cdd:PRK07775  10 RRP--------ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGG----EAVAFPLDVTDPDSVKSF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 122 TKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSI 201
Cdd:PRK07775  78 VAQAEEALGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMG 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 202 GYCASKHALRGFFNGLRTELATyPGIIVSNICPGPVQS 239
Cdd:PRK07775 158 AYGAAKAGLEAMVTNLQMELEG-TGVRASIVHPGPTLT 194
PRK05693 PRK05693
SDR family oxidoreductase;
52-245 1.58e-26

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 106.03  E-value: 1.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERvkrrclengnLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEA----------LAAAGFTAVQLDVNDGAALARLAEELEAEHGG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPhMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:PRK05693  73 LDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFP-LLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVH 151
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPGPVQSNIVENS 245
Cdd:PRK05693 152 ALSDALRLELAPF-GVQVMEVQPGAIASQFASNA 184
SDR_subfam_1 TIGR03971
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
48-244 1.63e-26

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. See EC 1.1.99.36. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274889 [Multi-domain]  Cd Length: 270  Bit Score: 106.02  E-value: 1.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145   48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVL----------------------SARRVHELERvkrrclengnlkekDI 105
Cdd:TIGR03971   1 LEGKVAFITGAARGQGRSHAVRLAEEGADIIAvdicadidtvpyplatpddlaeTVRLVEALGR--------------RI 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  106 LVLPLDLTDTGSHEAATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKI 185
Cdd:TIGR03971  67 VARQADVRDRAALQAAVDAGVAEFGRLDIVVANAGICSIGPLWELTEEQWDDMIDVNLTGVWNTVKAAAPHMIERGGGSI 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 649109145  186 VTVNSILGIISVPLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVEN 244
Cdd:TIGR03971 147 VLTSSTAGLKGGPGGAHYVAAKHGVVGLMRSLALELAPH-GIRVNAVHPTGVNTPMIDN 204
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
53-245 2.27e-26

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: 105.82  E-value: 2.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVsLVLSA---RRVHELERVKRRCleNGNLKekdilVLPLDLTDTGSHEAATKAVLQEF 129
Cdd:cd09805    3 VLITGCDSGFGNLLAKKLDSLGF-TVLAGcltKNGPGAKELRRVC--SDRLR-----TLQLDVTKPEQIKRAAQWVKEHV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 GRIDI--LVNNGGMSQRS-LCMDTSLDVYRKLIELNYLGTVSLTKCVLPhMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:cd09805   75 GEKGLwgLVNNAGILGFGgDEELLPMDDYRKCMEVNLFGTVEVTKAFLP-LLRRAKGRVVNVSSMGGRVPFPAGGAYCAS 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENS 245
Cdd:cd09805  154 KAAVEAFSDSLRRELQPW-GVKVSIIEPGNFKTGITGNS 191
PRK07774 PRK07774
SDR family oxidoreductase;
47-254 2.47e-26

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 104.83  E-value: 2.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK07774   3 RFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGG----TAIAVQVDVSDPDSAKAMADATV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNN----GGMSQRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSilgIISVPLSIG 202
Cdd:PRK07774  79 SAFGGIDYLVNNaaiyGGMKLDLL-ITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSS---TAAWLYSNF 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 649109145 203 YCASKHALrgffNGLRTELATYPG---IIVSNICPGPVQSNIVENSLAGEVTKTI 254
Cdd:PRK07774 155 YGLAKVGL----NGLTQQLARELGgmnIRVNAIAPGPIDTEATRTVTPKEFVADM 205
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
52-251 3.68e-26

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: 104.40  E-value: 3.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHE------------LERVKRRCLENGNlkekDILVLPLDLTDTGSHE 119
Cdd:cd05338    5 VAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEgdngsakslpgtIEETAEEIEAAGG----QALPIVVDVRDEDQVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 120 AATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPL 199
Cdd:cd05338   81 ALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPARG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 649109145 200 SIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEVT 251
Cdd:cd05338  161 DVAYAAGKAGMSRLTLGLAAELRRH-GIAVNSLWPSTAIETPAATELSGGSD 211
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
46-239 5.51e-26

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 103.84  E-value: 5.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKrrclenGNLKEKdILVLPLDLTDTGSHEAATKAV 125
Cdd:PRK12936   2 FDLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALA------AELGER-VKIFPANLSDRDEVKALGQKA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK12936  75 EADLEGVDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCA 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:PRK12936 155 SKAGMIGFSKSLAQEIATR-NVTVNCVAPGFIES 187
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
48-246 1.48e-25

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: 102.85  E-value: 1.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRclengnLKEKDILVlPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05341    3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAE------LGDAARFF-HLDVTDEDGWTAVVDTARE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:cd05341   76 AFGRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNASK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 649109145 208 HALRGFFNGLRTELATYP-GIIVSNICPGPVQSNIVENSL 246
Cdd:cd05341  156 GAVRGLTKSAALECATQGyGIRVNSVHPGYIYTPMTDELL 195
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
52-248 1.51e-25

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: 103.00  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd08945    5 VALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAG----VEADGRTCDVRSVPEIEALVAAAVARYGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPH--MIERKQGKIVTVNSILGIISVPLSIGYCASKHA 209
Cdd:cd08945   81 IDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAAPYSASKHG 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 210 LRGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLAG 248
Cdd:cd08945  161 VVGFTKALGLELAR-TGITVNAVCPGFVETPMAASVREH 198
PRK12939 PRK12939
short chain dehydrogenase; Provisional
52-249 1.82e-25

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 102.36  E-value: 1.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK12939   9 RALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGG----RAHAIAADLADPASVQRFFDAAAAALGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:PRK12939  85 LDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVI 164
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPGPVQsniVENSLAGE 249
Cdd:PRK12939 165 GMTRSLARELGGR-GITVNAIAPGLTA---TEATAYVP 198
PRK08219 PRK08219
SDR family oxidoreductase;
51-243 1.89e-25

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 101.93  E-value: 1.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  51 MVVWVTGASSGIGEELAYQLSKlGVSLVLSARRVhelERVKRRCLENGNLKekdilVLPLDLTDTGSHEAAtkavLQEFG 130
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP-THTLLLGGRPA---ERLDELAAELPGAT-----PFPVDLTDPEAIAAA----VEQLG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPhMIERKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK08219  71 RLDVLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLP-ALRAAHGHVVFINSGAGLRANPGWGSYAASKFAL 149
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 211 RGFFNGLRTELATYpgIIVSNICPGPV----QSNIVE 243
Cdd:PRK08219 150 RALADALREEEPGN--VRVTSVHPGRTdtdmQRGLVA 184
PRK12827 PRK12827
short chain dehydrogenase; Provisional
46-244 3.85e-25

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 101.72  E-value: 3.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVL----SARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAA 121
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVldihPMRGRAEADAVAAGIEAAGG----KALGLAFDVRDFAATRAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 122 TKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIE-RKQGKIVTVNSILGIISVPLS 200
Cdd:PRK12827  78 LDAGVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRaRRGGRIVNIASVAGVRGNRGQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 649109145 201 IGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVEN 244
Cdd:PRK12827 158 VNYAASKAGLIGLTKTLANELAPR-GITVNAVAPGAINTPMADN 200
PRK06124 PRK06124
SDR family oxidoreductase;
48-235 5.16e-25

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 101.33  E-value: 5.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEkdilVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAE----ALAFDIADEEAVAAAFARIDA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK06124  85 EHGRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAK 164
                        170       180
                 ....*....|....*....|....*...
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK06124 165 QGLTGLMRALAAEFGPH-GITSNAIAPG 191
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
55-235 9.95e-25

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 100.61  E-value: 9.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRcLENGNLKEKdilVLPLDLTDtgsHEAATKAV---LQEFGR 131
Cdd:PRK07523  15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAES-LKGQGLSAH---ALAFDVTD---HDAVRAAIdafEAEIGP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:PRK07523  88 IDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKGAVG 167
                        170       180
                 ....*....|....*....|....
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK07523 168 NLTKGMATDWAKH-GLQCNAIAPG 190
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
48-240 1.47e-24

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 100.19  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRvHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK06935  13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHG-TNWDETRRLIEKEG----RKVTFVQVDLTKPESAEKVVKEALE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSIL---GIISVPlsiGYC 204
Cdd:PRK06935  88 EFGKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMLsfqGGKFVP---AYT 164
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 649109145 205 ASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSN 240
Cdd:PRK06935 165 ASKHGVAGLTKAFANELAAY-NIQVNAIAPGYIKTA 199
PRK07063 PRK07063
SDR family oxidoreductase;
48-243 1.72e-24

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 100.13  E-value: 1.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDVA--GARVLAVPADVTDAASVAAAVAAAEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK07063  83 AFGPLDVLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYPVAK 162
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVE 243
Cdd:PRK07063 163 HGLLGLTRALGIEYAAR-NVRVNAIAPGYIETQLTE 197
PRK06949 PRK06949
SDR family oxidoreductase;
47-241 2.33e-24

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 99.84  E-value: 2.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK06949   6 NLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGG----AAHVVSLDVTDYQSIKAAVAHAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIER--------KQGKIVTVNSILGIISVP 198
Cdd:PRK06949  82 TEAGTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARakgagntkPGGRIINIASVAGLRVLP 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 649109145 199 lSIG-YCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNI 241
Cdd:PRK06949 162 -QIGlYCMSKAAVVHMTRAMALEWGRH-GINVNAICPGYIDTEI 203
PRK06482 PRK06482
SDR family oxidoreductase;
54-240 2.75e-24

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 99.80  E-value: 2.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  54 W-VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnlkekdILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:PRK06482   5 WfITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDR-------LWVLQLDVTDSAAVRAVVDRAFAALGRI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQ--GKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK06482  78 DVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHL--RRQggGRIVQVSSEGGQIAYPGFSLYHATKWGI 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPGPVQSN 240
Cdd:PRK06482 156 EGFVEAVAQEVAPF-GIEFTIVEPGPARTN 184
PRK08017 PRK08017
SDR family oxidoreductase;
53-258 3.17e-24

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 99.39  E-value: 3.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnlkekdilvLPLDLTDTGSHEAATKAVLQ-EFGR 131
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNSLGFTG----------ILLDLDDPESVERAADEVIAlTDNR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:PRK08017  75 LYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALE 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 649109145 212 GFFNGLRTELAtYPGIIVSNICPGPVQSNIVENSLAGEVTKTIGNNG 258
Cdd:PRK08017 155 AWSDALRMELR-HSGIKVSLIEPGPIRTRFTDNVNQTQSDKPVENPG 200
PRK06398 PRK06398
aldose dehydrogenase; Validated
47-252 7.51e-24

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 98.37  E-value: 7.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGvSLVLSARrVHELERVKRRCLEngnlkekdilvlpLDLTDTGSHEAATKAVL 126
Cdd:PRK06398   3 GLKDKVAIVTGGSQGIGKAVVNRLKEEG-SNVINFD-IKEPSYNDVDYFK-------------VDVSNKEQVIKGIDYVI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK06398  68 SKYGRIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTS 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 649109145 207 KHALRGFFNGLRTELAtyPGIIVSNICPGPVQSNIVENSLAGEVTK 252
Cdd:PRK06398 148 KHAVLGLTRSIAVDYA--PTIRCVAVCPGSIRTPLLEWAAELEVGK 191
PRK05650 PRK05650
SDR family oxidoreductase;
53-243 1.02e-23

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 98.19  E-value: 1.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGG----DGFYQRCDVRDYSQLTALAQACEEKWGGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:PRK05650  79 DVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVA 158
                        170       180       190
                 ....*....|....*....|....*....|.
gi 649109145 213 FFNGLRTELATYpGIIVSNICPGPVQSNIVE 243
Cdd:PRK05650 159 LSETLLVELADD-EIGVHVVCPSFFQTNLLD 188
PRK06484 PRK06484
short chain dehydrogenase; Validated
52-242 1.04e-23

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 101.46  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGvslvlsaRRVHELERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK06484   7 VVLVTGAAGGIGRAACQRFARAG-------DQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQR--SLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGK-IVTVNSILGIISVPLSIGYCASKH 208
Cdd:PRK06484  80 IDVLVNNAGVTDPtmTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLVALPKRTAYSASKA 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 209 ALRGFFNGLRTELATyPGIIVSNICPGPVQSNIV 242
Cdd:PRK06484 160 AVISLTRSLACEWAA-KGIRVNAVLPGYVRTQMV 192
PRK05855 PRK05855
SDR family oxidoreductase;
40-244 1.27e-23

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 101.60  E-value: 1.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  40 QGRRPEWELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHE 119
Cdd:PRK05855 305 RVGRPRGPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAG----AVAHAYRVDVSDADAME 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 120 AATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSILGIisVP 198
Cdd:PRK05855 381 AFAEWVRAEHGVPDIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAY--AP 458
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 649109145 199 LSI--GYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVEN 244
Cdd:PRK05855 459 SRSlpAYATSKAAVLMLSECLRAELAAA-GIGVTAICPGFVDTNIVAT 505
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
52-237 3.04e-23

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: 96.19  E-value: 3.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLS-ARRVHELERVKRRCLENGNlkeKDILVlPLDLTDTGSHEAATKAVLQEFG 130
Cdd:cd05362    5 VALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEIEAAGG---KAIAV-QADVSDPSQVARLFDAAEKAFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:cd05362   81 GVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL--RDGGRIINISSSLTAAYTPNYGAYAGSKAAV 158
                        170       180
                 ....*....|....*....|....*..
gi 649109145 211 RGFFNGLRTELATyPGIIVSNICPGPV 237
Cdd:cd05362  159 EAFTRVLAKELGG-RGITVNAVAPGPV 184
PRK06172 PRK06172
SDR family oxidoreductase;
47-249 3.89e-23

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 96.36  E-value: 3.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK06172   4 TFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGG----EALFVACDVTRDAEVKALVEQTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMS-QRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK06172  80 AAYGRLDYAFNNAGIEiEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 649109145 206 SKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:PRK06172 160 SKHAVIGLTKSAAIEYAK-KGIRVNAVCPAVIDTDMFRRAYEAD 202
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
53-237 4.22e-23

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 95.65  E-value: 4.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnlkekdILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:cd08929    3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEG-------VLGLAGDVRDEADVRRAVDAMEEAFGGL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:cd08929   76 DALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLG 155
                        170       180
                 ....*....|....*....|....*
gi 649109145 213 FFNGLRTELATYpGIIVSNICPGPV 237
Cdd:cd08929  156 LSEAAMLDLREA-NIRVVNVMPGSV 179
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
55-253 5.02e-23

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: 95.82  E-value: 5.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLG--VSLVLSARRVHELERVKRRCLENGNlkekdILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:cd05367    4 LTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELRPGLR-----VTTVKADLSDAAGVEQLLEAIRKLDGER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGM-SQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERK-QGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:cd05367   79 DLLINNAGSlGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGlKKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 649109145 211 RGFFNGLRTELatyPGIIVSNICPGPV----QSNIVENSLAGEVTKT 253
Cdd:cd05367  159 DMFFRVLAAEE---PDVRVLSYAPGVVdtdmQREIRETSADPETRSR 202
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
48-255 5.67e-23

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 95.86  E-value: 5.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARrvhELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADI---KPARARLAALEIGP----AAIAVSLDVTRQDSIDRIVAAAVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQG-KIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK07067  77 RFGGIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGgKIINMASQAGRRGEALVSHYCAT 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQS---NIV-------ENSLAGEVTKTIG 255
Cdd:PRK07067 157 KAAVISYTQSAALALIRH-GINVNAIAPGVVDTpmwDQVdalfaryENRPPGEKKRLVG 214
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
52-249 6.28e-23

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: 95.63  E-value: 6.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekdiLVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd08944    5 VAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGA-------LALRVDVTDEQQVAALFERAVEEFGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGG-MSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:cd08944   78 LDLLVNNAGaMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAI 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 211 RGFFNGLRTELAtYPGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:cd08944  158 RNLTRTLAAELR-HAGIRCNALAPGLIDTPLLLAKLAGF 195
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
55-243 6.62e-23

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 95.60  E-value: 6.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSAR----RVHELERVKrrclengNLKEKDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK12824   7 VTGAKRGIGSAIARELLNDGYRVIATYFsgndCAKDWFEEY-------GFTEDQVRLKELDVTDTEECAEALAEIEEEEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK12824  80 PVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGM 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPGPVQSNIVE 243
Cdd:PRK12824 160 IGFTKALASEGARY-GITVNCIAPGYIATPMVE 191
PRK12828 PRK12828
short chain dehydrogenase; Provisional
52-237 7.78e-23

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 95.25  E-value: 7.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELER-VKRRCLENGNLKEkdilvlpLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK12828   9 VVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQtLPGVPADALRIGG-------IDLVDPQAARRAVDEVNRQFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK12828  82 RLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161
                        170       180
                 ....*....|....*....|....*..
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPGPV 237
Cdd:PRK12828 162 ARLTEALAAELLDR-GITVNAVLPSII 187
PRK06523 PRK06523
short chain dehydrogenase; Provisional
47-239 1.00e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 95.36  E-value: 1.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVhelervkrrcleNGNLKEkDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSR------------PDDLPE-GVEFVAADLTTAEGCAAVARAVL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSL--DVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLS-IGY 203
Cdd:PRK06523  73 ERLGGVDILVHVLGGSSAPAGGFAALtdEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPEStTAY 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 204 CASKHALRGFFNGLRTELAtyP-GIIVSNICPGPVQS 239
Cdd:PRK06523 153 AAAKAALSTYSKSLSKEVA--PkGVRVNTVSPGWIET 187
PRK07814 PRK07814
SDR family oxidoreductase;
48-243 1.39e-22

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 94.85  E-value: 1.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK07814   8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAG----RRAHVVAADLAHPEATAGLAGQAVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERK-QGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK07814  84 AFGRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgGGSVINISSTMGRLAGRGFAAYGTA 163
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 207 KHALRGFFNGLRTELAtyPGIIVSNICPGPVQSNIVE 243
Cdd:PRK07814 164 KAALAHYTRLAALDLC--PRIRVNAIAPGSILTSALE 198
PRK12829 PRK12829
short chain dehydrogenase; Provisional
48-244 1.65e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 94.74  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRclengnLKEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK12829   9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAAR------LPGAKVTATVADVADPAQVERVFDTAVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDT-SLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGK-IVTVNSILGIISVPLSIGYCA 205
Cdd:PRK12829  83 RFGGLDVLVNNAGIAGPTGGIDEiTPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGvIIALSSVAGRLGYPGRTPYAA 162
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 206 SKHALRGFFNGLRTELAtYPGIIVSNICPGPVQSNIVEN 244
Cdd:PRK12829 163 SKWAVVGLVKSLAIELG-PLGIRVNAILPGIVRGPRMRR 200
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
51-239 2.42e-22

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 94.26  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  51 MVVWVTGASSGIGEELAYQLSKLGVSL-VLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEF 129
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLaINDRPDDEELAATQQELRALG----VEVIFFPADVADLSAHEAMLDAAQAAW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 GRIDILVNNGGMS--QRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ------GKIVTVNSILGIISVPLSI 201
Cdd:PRK12745  79 GRIDCLVNNAGVGvkVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphRSIVFVSSVNAIMVSPNRG 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 202 GYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:PRK12745 159 EYCISKAGLSMAAQLFAARLAEE-GIGVYEVRPGLIKT 195
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
46-235 3.08e-22

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 93.80  E-value: 3.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRClengnlkekdilvLPLDLTDTGSHEAATKAV 125
Cdd:PRK08220   4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQEDYPFAT-------------FVLDVSDAAAVAQVCQRL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSilGIISVP-LSIG-Y 203
Cdd:PRK08220  71 LAETGPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGS--NAAHVPrIGMAaY 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 649109145 204 CASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK08220 149 GASKAALTSLAKCVGLELAPY-GVRCNVVSPG 179
PRK12743 PRK12743
SDR family oxidoreductase;
55-235 3.12e-22

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 93.94  E-value: 3.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHE-LERVKRRCLENGNLKEkdilVLPLDLTDTGSHEAATKAVLQEFGRID 133
Cdd:PRK12743   7 VTASDSGIGKACALLLAQQGFDIGITWHSDEEgAKETAEEVRSHGVRAE----IRQLDLSDLPEGAQALDKLIQRLGRID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:PRK12743  83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQgGRIINITSVHEHTPLPGASAYTAAKHALGG 162
                        170       180
                 ....*....|....*....|...
gi 649109145 213 FFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK12743 163 LTKAMALELVEH-GILVNAVAPG 184
PRK07062 PRK07062
SDR family oxidoreductase;
47-239 3.67e-22

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 93.95  E-value: 3.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnLKEKDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK07062   5 QLEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREK--FPGARLLAARCDVLDEADVAAFAAAVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK07062  83 ARFGGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAA 162
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:PRK07062 163 RAGLLNLVKSLATELAPK-GVRVNSILLGLVES 194
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
52-248 4.95e-22

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: 92.83  E-value: 4.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVkrrCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05373    1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEAL---LVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:cd05373   78 LEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALR 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 212 GFFNGLRTELATyPGIIVSN-ICPGPVQSNIVENSLAG 248
Cdd:cd05373  158 ALAQSMARELGP-KGIHVAHvIIDGGIDTDFIRERFPK 194
PRK07060 PRK07060
short chain dehydrogenase; Provisional
52-235 7.49e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 92.47  E-value: 7.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKrrclengnlKEKDILVLPLDLTDtgshEAATKAVLQEFGR 131
Cdd:PRK07060  11 SVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLA---------GETGCEPLRLDVGD----DAAIRAALAAAGA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIE-RKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK07060  78 FDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAaGRGGSIVNVSSQAALVGLPDHLAYCASKAAL 157
                        170       180
                 ....*....|....*....|....*
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK07060 158 DAITRVLCVELGPH-GIRVNSVNPT 181
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
51-237 1.26e-21

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 92.13  E-value: 1.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  51 MVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnlkekdILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK10538   1 MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDN-------LYIAQLDVRNRAAIEEMLASLPAEWR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSqrsLCMD----TSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGiiSVPLSIG--YC 204
Cdd:PRK10538  74 NIDVLVNNAGLA---LGLEpahkASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAG--SWPYAGGnvYG 148
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 205 ASKHALRGFFNGLRTELATyPGIIVSNICPGPV 237
Cdd:PRK10538 149 ATKAFVRQFSLNLRTDLHG-TAVRVTDIEPGLV 180
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
48-235 1.29e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 92.43  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERvkrrCLENgnLKEKDILVLPL--DLTDTGSHEAATKAV 125
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDK----GLAA--YRELGIEAHGYvcDVTDEDGVQAMVSQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSI---LGIISVPlsiG 202
Cdd:PRK07097  82 EKEVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMmseLGRETVS---A 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 203 YCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK07097 159 YAAAKGGLKMLTKNIASEYGEA-NIQCNGIGPG 190
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
46-243 1.42e-21

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: 92.13  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERvkrrCLENGNLKEKDILVLPLDLTDTGSHEAATKAV 125
Cdd:cd05329    2 WNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDE----CLTEWREKGFKVEGSVCDVSSRSERQELMDTV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEF-GRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYC 204
Cdd:cd05329   78 ASHFgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYG 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 205 ASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVE 243
Cdd:cd05329  158 ATKGALNQLTRSLACEWAK-DNIRVNAVAPWVIATPLVE 195
PRK08251 PRK08251
SDR family oxidoreductase;
55-245 1.80e-21

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 91.54  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLE-NGNLKekdILVLPLDLTDtgsHEA---ATKAVLQEFG 130
Cdd:PRK08251   7 ITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLArYPGIK---VAVAALDVND---HDQvfeVFAEFRDELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGtvSLTKCVLPHMIERKQ--GKIVTVNSILGIISVPLSIG-YCASK 207
Cdd:PRK08251  81 GLDRVIVNAGIGKGARLGTGKFWANKATAETNFVA--ALAQCEAAMEIFREQgsGHLVLISSVSAVRGLPGVKAaYAASK 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 208 HALRGFFNGLRTELATYPgIIVSNICPGPVQSNIVENS 245
Cdd:PRK08251 159 AGVASLGEGLRAELAKTP-IKVSTIEPGYIRSEMNAKA 195
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
48-239 1.84e-21

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: 91.82  E-value: 1.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARR--VHELervkrrcLENGNLKEKDILVLPLDLTDTGSHEAATKAV 125
Cdd:cd08937    2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSelVHEV-------LAEILAAGDAAHVHTADLETYAGAQGVVRAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNN-GGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSIL--GIISVPlsig 202
Cdd:cd08937   75 VERFGRVDVLINNvGGTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIYRIP---- 150
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 203 YCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:cd08937  151 YSAAKGGVNALTASLAFEHARD-GIRVNAVAPGGTEA 186
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
52-280 2.22e-21

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: 91.67  E-value: 2.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELerVKRRCLEngnLKEKD--ILVLPLDLTDTGSHEAATKAVLQEF 129
Cdd:cd05366    4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEA--AKSTIQE---ISEAGynAVAVGADVTDKDDVEALIDQAVEKF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 GRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSILGIISVPLSIGYCASKH 208
Cdd:cd05366   79 GSFDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHgGKIINASSIAGVQGFPNLGAYSASKF 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 649109145 209 ALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVEnSLAGEVTKTIGNNgDQSHKMTTSRCVRLMLISMAND 280
Cdd:cd05366  159 AVRGLTQTAAQELAPK-GITVNAYAPGIVKTEMWD-YIDEEVGEIAGKP-EGEGFAEFSSSIPLGRLSEPED 227
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
55-243 2.46e-21

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 91.50  E-value: 2.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGRIDI 134
Cdd:PRK13394  12 VTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGG----KAIGVAMDVTNEDAVNAGIDKVAERFGSVDI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 135 LVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMI-ERKQGKIVTVNSILGIISVPLSIGYCASKHALRGF 213
Cdd:PRK13394  88 LVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYkDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGL 167
                        170       180       190
                 ....*....|....*....|....*....|
gi 649109145 214 FNGLRTELATYpGIIVSNICPGPVQSNIVE 243
Cdd:PRK13394 168 ARVLAKEGAKH-NVRSHVVCPGFVRTPLVD 196
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
50-232 2.99e-21

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: 91.52  E-value: 2.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  50 DMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlKEKDILVLPLDLTDTGSHEAATKAVLQEF 129
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKET--GNAKVEVIQLDLSSLASVRQFAEEFLARF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 GRIDILVNNGG--MSQRSLcmdtSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSIL---GIISVPLSIG-- 202
Cdd:cd05327   79 PRLDILINNAGimAPPRRL----TKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAhraGPIDFNDLDLen 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 649109145 203 ---------YCASKHALRGFFNGLRTEL--------ATYPGIIVSNI 232
Cdd:cd05327  155 nkeyspykaYGQSKLANILFTRELARRLegtgvtvnALHPGVVRTEL 201
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
47-235 3.28e-21

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 91.50  E-value: 3.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK08277   7 SLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGG----EALAVKADVLDKESLEQARQQIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGG----------------MSQRSLCmDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNS 190
Cdd:PRK08277  83 EDFGPCDILINGAGgnhpkattdnefheliEPTKTFF-DLDEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 649109145 191 ILGIIsvPLS--IGYCASKHALRGFFNGLRTELATyPGIIVSNICPG 235
Cdd:PRK08277 162 MNAFT--PLTkvPAYSAAKAAISNFTQWLAVHFAK-VGIRVNAIAPG 205
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
55-237 3.73e-21

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: 90.49  E-value: 3.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHEL-ERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRID 133
Cdd:cd05359    3 VTGGSRGIGKAIALRLAERGADVVINYRKSKDAaAEVAAEIEELG----GKAVVVRADVSQPQDVEEMFAAVKERFGRLD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVP--LSIGycASKHALR 211
Cdd:cd05359   79 VLVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPnyLAVG--TAKAALE 156
                        170       180
                 ....*....|....*....|....*.
gi 649109145 212 GFFNGLRTELATYpGIIVSNICPGPV 237
Cdd:cd05359  157 ALVRYLAVELGPR-GIRVNAVSPGVI 181
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
55-239 9.38e-21

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: 89.28  E-value: 9.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVL----SARRVHELERVKRrclengnlKEKDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:cd05325    3 ITGASRGIGLELVRQLLARGNNTVIatcrDPSAATELAALGA--------SHSRLHILELDVTDEIAESAEAVAERLGDA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGM-SQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIIS--VPL-SIGYCAS 206
Cdd:cd05325   75 GLDVLINNAGIlHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGdnTSGgWYSYRAS 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 649109145 207 KHALRGFFNGLRTELATyPGIIVSNICPGPVQS 239
Cdd:cd05325  155 KAALNMLTKSLAVELKR-DGITVVSLHPGWVRT 186
PRK07478 PRK07478
short chain dehydrogenase; Provisional
47-235 1.16e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 89.60  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELER-VKRRCLENGnlkekDILVLPLDLTDTGSHEAATKAV 125
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQlVAEIRAEGG-----EAVALAGDVRDEAYAKALVALA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCM-DTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILG-IISVPLSIGY 203
Cdd:PRK07478  78 VERFGGLDIAFNNAGTLGEMGPVaEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGhTAGFPGMAAY 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 649109145 204 CASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK07478 158 AASKAGLIGLTQVLAAEYGAQ-GIRVNALLPG 188
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
48-258 1.20e-20

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: 89.66  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLS--------ARRVHEL-ERVKRRCLengnlkekdilVLPLDLTDTGSH 118
Cdd:cd05355   24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINylpeeeddAEETKKLiEEEGRKCL-----------LIPGDLGDESFC 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 119 EAATKAVLQEFGRIDILVNNGGMSQRSLCMDT-SLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISV 197
Cdd:cd05355   93 RDLVKEVVKEFGKLDILVNNAAYQHPQESIEDiTTEQLEKTFRTNIFSMFYLTKAALPHL--KKGSSIINTTSVTAYKGS 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 649109145 198 PLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEVTKTIGNNG 258
Cdd:cd05355  171 PHLLDYAATKGAIVAFTRGLSLQLAEK-GIRVNAVAPGPIWTPLIPSSFPEEKVSEFGSQV 230
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
48-241 1.50e-20

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: 89.36  E-value: 1.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSAR----RVHELERVKRrclengNLKEKDILVlPLDLTDTGSHEAATK 123
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRskedAAEEVVEEIK------AVGGKAIAV-QADVSKEEDVVALFQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 AVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIE-RKQGKIVTVNSILGIISVPLSIG 202
Cdd:cd05358   74 SAIKEFGTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKsKIKGKIINMSSVHEKIPWPGHVN 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 203 YCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNI 241
Cdd:cd05358  154 YAASKGGVKMMTKTLAQEYAPK-GIRVNAIAPGAINTPI 191
PRK06198 PRK06198
short chain dehydrogenase; Provisional
48-212 3.03e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 88.52  E-value: 3.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGV-SLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAELEALG----AKAVFVQADLSDVEDCRRVVAAAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERK-QGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK06198  80 EAFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaEGTIVNIGSMSAHGGQPFLAAYCA 159

                 ....*..
gi 649109145 206 SKHALRG 212
Cdd:PRK06198 160 SKGALAT 166
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
47-242 5.32e-20

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 87.75  E-value: 5.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHE-LERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAV 125
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEaAENLVNELGKEGH----DVYAVQADVSKVEDANRLVEEA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK12935  79 VNHFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSA 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 206 SKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIV 242
Cdd:PRK12935 159 AKAGMLGFTKSLALELAK-TNVTVNAICPGFIDTEMV 194
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
49-240 6.40e-20

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: 87.39  E-value: 6.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  49 TDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARrvhELERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQE 128
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADI---NAPALEQLKEELTNLYKNRVIALELDITSKESIKELIESYLEK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 129 FGRIDILVNNGGMSQR---SLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGII---------- 195
Cdd:cd08930   78 FGRIDILINNAYPSPKvwgSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIapdfriyent 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 649109145 196 SVPLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSN 240
Cdd:cd08930  158 QMYSPVEYSVIKAGIIHLTKYLAKYYADT-GIRVNAISPGGILNN 201
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
55-241 8.05e-20

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: 87.13  E-value: 8.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARR--------VHELERVKRRCLengnlkekdilVLPLDLTDTGSHEAATKAVL 126
Cdd:cd05337    6 VTGASRGIGRAIATELAARGFDIAINDLPdddqatevVAEVLAAGRRAI-----------YFQADIGELSDHEALLDQAW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSL--CMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ------GKIVTVNSILGIISVP 198
Cdd:cd05337   75 EDFGRLDCLVNNAGIAVRPRgdLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDrfdgphRSIIFVTSINAYLVSP 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 649109145 199 LSIGYCASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNI 241
Cdd:cd05337  155 NRGEYCISKAGLSMATRLLAYRLAD-EGIAVHEIRPGLIHTDM 196
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-238 1.03e-19

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 86.56  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGeelayqLSKLGVSLVLSARrVHELErvkrrCLENGNLkEKDILVLPLDLTDtgsheaATKAVL 126
Cdd:PRK06550   2 EFMTKTVLITGAASGIG------LAQARAFLAQGAQ-VYGVD-----KQDKPDL-SGNFHFLQLDLSD------DLEPLF 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGM---SQRSLcmDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGY 203
Cdd:PRK06550  63 DWVPSVDILCNTAGIlddYKPLL--DTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAY 140
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 204 CASKHALRGFFNGLRTELATyPGIIVSNICPGPVQ 238
Cdd:PRK06550 141 TASKHALAGFTKQLALDYAK-DGIQVFGIAPGAVK 174
PRK12937 PRK12937
short chain dehydrogenase; Provisional
48-250 1.07e-19

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 86.72  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLS-ARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGG----RAIAVQADVADAAAVTRLFDAAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK12937  79 TAFGRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL--GQGGRIINLSTSVIALPLPGYGPYAAS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEV 250
Cdd:PRK12937 157 KAAVEGLVHVLANELRGR-GITVNAVAPGPVATELFFNGKSAEQ 199
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
46-243 1.17e-19

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 86.70  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSA-RRVHELERVKRRCLENGNlkeKDILVLPLDLTDTGSHEAAtKA 124
Cdd:PRK06077   2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAkKRAEEMNETLKMVKENGG---EGIGVLADVSTREGCETLA-KA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 125 VLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVP-LSIgY 203
Cdd:PRK06077  78 TIDRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYgLSI-Y 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 649109145 204 CASKHALRGFFNGLRTELAtyPGIIVSNICPGPVQSNIVE 243
Cdd:PRK06077 155 GAMKAAVINLTKYLALELA--PKIRVNAIAPGFVKTKLGE 192
PRK09242 PRK09242
SDR family oxidoreductase;
46-234 1.35e-19

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 86.72  E-value: 1.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnLKEKDILVLPLDLTDTGSHEAATKAV 125
Cdd:PRK09242   5 WRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEE--FPEREVHGLAADVSDDEDRRAILDWV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK09242  83 EDHWDGLHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGM 162
                        170       180
                 ....*....|....*....|....*....
gi 649109145 206 SKHALRGFFNGLRTELATyPGIIVSNICP 234
Cdd:PRK09242 163 TKAALLQMTRNLAVEWAE-DGIRVNAVAP 190
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
50-237 1.60e-19

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: 86.43  E-value: 1.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  50 DMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRV---HELERVKRRCLENGnlkekdILVLPLDLTDTGSHEAATKAVL 126
Cdd:cd08933    9 DKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEaagQALESELNRAGPGS------CKFVPCDVTKEEDIKTLISVTV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGM---SQRSlcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMiERKQGKIVTVNSILGIISVPLSIGY 203
Cdd:cd08933   83 ERFGRIDCLVNNAGWhppHQTT--DETSAQEFRDLLNLNLISYFLASKYALPHL-RKSQGNIINLSSLVGSIGQKQAAPY 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 204 CASKHALRGFFNGLRTELATYpGIIVSNICPGPV 237
Cdd:cd08933  160 VATKGAITAMTKALAVDESRY-GVRVNCISPGNI 192
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
48-253 2.32e-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: 85.97  E-value: 2.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclengNLKEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05326    2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAA------ELGDPDISFVHCDVTVEADVRAAVDTAVA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSL--CMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:cd05326   76 RFGRLDIMFNNAGVLGAPCysILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEVTKT 253
Cdd:cd05326  156 SKHAVLGLTRSAATELGEH-GIRVNCVSPYGVATPLLTAGFGVEDEAI 202
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
48-237 3.58e-19

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: 85.33  E-value: 3.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRvheLERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRK---PEVLEAAAEEISSATGGRAHPIQCDVRDPEAVEAAVDETLK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSILGIISVPLSIGYCAS 206
Cdd:cd05369   78 EFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSAAA 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPV 237
Cdd:cd05369  158 KAGVDALTRSLAVEWGPY-GIRVNAIAPGPI 187
PRK06484 PRK06484
short chain dehydrogenase; Validated
52-239 4.33e-19

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 87.98  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKrrclenGNLKEKDiLVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK06484 271 VVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLA------EALGDEH-LSVQADITDEAAVESAFAQIQARWGR 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSL-CMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK06484 344 LDVLVNNAGIAEVFKpSLEQSAEDFTRVYDVNLSGAFACARAAARLM--SQGGVIVNLGSIASLLALPPRNAYCASKAAV 421
                        170       180
                 ....*....|....*....|....*....
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:PRK06484 422 TMLSRSLACEWAPA-GIRVNTVAPGYIET 449
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
46-234 1.24e-18

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: 83.59  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekdiLVLPLDLTDTGSHEAATKAV 125
Cdd:cd05345    1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAA-------IAIQADVTKRADVEAMVEAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCM-DTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYC 204
Cdd:cd05345   74 LSKFGRLDILVNNAGITHRNKPMlEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYN 153
                        170       180       190
                 ....*....|....*....|....*....|
gi 649109145 205 ASKHALRGFFNGLRTELATYpGIIVSNICP 234
Cdd:cd05345  154 ASKGWVVTATKAMAVELAPR-NIRVNCLCP 182
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
52-252 1.71e-18

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: 83.39  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05365    1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGG----QAIGLECNVTSEQDLEAVVKATVSQFGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNN-GGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:cd05365   77 ITILVNNaGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAV 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 649109145 211 RGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLAGEVTK 252
Cdd:cd05365  157 NHMTRNLAFDLGP-KGIRVNAVAPGAVKTDALASVLTPEIER 197
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
53-249 3.12e-18

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: 82.52  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSlVLSARRVHELERVKRRCLEngnlkekdilVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGAT-VIALDLPFVLLLEYGDPLR----------LTPLDVADAAAVREVCSRLLAEHGPI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSilGIISVP-LSIG-YCASKHAL 210
Cdd:cd05331   70 DALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVAS--NAAHVPrISMAaYGASKAAL 147
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:cd05331  148 ASLSKCLGLELAPY-GVRCNVVSPGSTDTAMQRTLWHDE 185
PRK07074 PRK07074
SDR family oxidoreductase;
49-239 3.16e-18

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 82.90  E-value: 3.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  49 TDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRclengnLKEKDILVLPLDLTDTGSHEAATKAVLQE 128
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADA------LGDARFVPVACDLTDAASLAAALANAAAE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 129 FGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGiISVPLSIGYCASKH 208
Cdd:PRK07074  75 RGPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNG-MAALGHPAYSAAKA 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 649109145 209 ALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:PRK07074 154 GLIHYTKLLAVEYGRF-GIRANAVAPGTVKT 183
PRK06057 PRK06057
short chain dehydrogenase; Provisional
48-237 3.68e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 82.47  E-value: 3.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVlsarrVHELERVKRRCLENgnlkEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVV-----VGDIDPEAGKAAAD----EVGGLFVPTDVTDEDAVNALFDTAAE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMS--QRSLCMDTSLDVYRKLIELNyLGTVSL-TKCVLPHMIERKQGKIVTVNSILGIISVPLS-IGY 203
Cdd:PRK06057  76 TYGSVDIAFNNAGISppEDDSILNTGLDAWQRVQDVN-LTSVYLcCKAALPHMVRQGKGSIINTASFVAVMGSATSqISY 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 204 CASKHALRGFFNGLRTELATyPGIIVSNICPGPV 237
Cdd:PRK06057 155 TASKGGVLAMSRELGVQFAR-QGIRVNALCPGPV 187
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
53-285 4.23e-18

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: 81.73  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRcLENGNLkekdiLVLPLDLTDtgshEAATKAVLQEF--- 129
Cdd:cd08931    3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAE-LGAENV-----VAGALDVTD----RAAWAAALADFaaa 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 --GRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:cd08931   73 tgGRLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATK 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVenslagevtktigNNGDQSHKMTTSRCVRLMLISMAndlKEVW 285
Cdd:cd08931  153 FAVRGLTEALDVEWARH-GIRVADVWPWFVDTPIL-------------TKGETGAAPKKGLGRVLPVSDVA---KVVW 213
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
49-235 4.74e-18

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: 82.34  E-value: 4.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  49 TDMVVWVTGASSGIGEELAYQLSKLGVSLVLsarrvheLERVKRRCLENGNLKEKDILVlPLDLTDTGSHEAATKAVLQE 128
Cdd:cd05371    1 KGLVAVVTGGASGLGLATVERLLAQGAKVVI-------LDLPNSPGETVAKLGDNCRFV-PVDVTSEKDVKAALALAKAK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 129 FGRIDILVNNGG--MSQRSLCMDT----SLDVYRKLIELNYLGTVSLTKCVLPHM------IERKQGKIVTVNSILGIIS 196
Cdd:cd05371   73 FGRLDIVVNCAGiaVAAKTYNKKGqqphSLELFQRVINVNLIGTFNVIRLAAGAMgknepdQGGERGVIINTASVAAFEG 152
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 197 VPLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:cd05371  153 QIGQAAYSASKGGIVGMTLPIARDLAPQ-GIRVVTIAPG 190
PRK06125 PRK06125
short chain dehydrogenase; Provisional
48-249 4.93e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 82.40  E-value: 4.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLkekDILVLPLDLTDTGSHEaatkAVLQ 127
Cdd:PRK06125   5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGV---DVAVHALDLSSPEARE----QLAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVnsiLGIISVPLSIGY-CAS 206
Cdd:PRK06125  78 EAGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNV---IGAAGENPDADYiCGS 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 649109145 207 --KHALRGFFNGLRTElATYPGIIVSNICPGPVQSNIVENSLAGE 249
Cdd:PRK06125 155 agNAALMAFTRALGGK-SLDDGVRVVGVNPGPVATDRMLTLLKGR 198
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
52-239 7.59e-18

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: 81.36  E-value: 7.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLV---LSARRVHELERVKRrclengnlkekdILVLPLDLTDtgshEAATKAVLQE 128
Cdd:cd05368    4 VALITAAAQGIGRAIALAFAREGANVIatdINEEKLKELERGPG------------ITTRVLDVTD----KEQVAALAKE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 129 FGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILG-IISVPLSIGYCASK 207
Cdd:cd05368   68 EGRIDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASsIKGVPNRFVYSTTK 147
                        170       180       190
                 ....*....|....*....|....*....|..
gi 649109145 208 HALRGFFNGLRTELATyPGIIVSNICPGPVQS 239
Cdd:cd05368  148 AAVIGLTKSVAADFAQ-QGIRCNAICPGTVDT 178
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
47-241 8.03e-18

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 81.70  E-value: 8.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHE-LERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAV 125
Cdd:PRK08936   4 DLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEeANDVAEEIKKAGG----EAIAVKGDVTVESDVVNLIQTA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIER-KQGKIVTVNSILGIISVPLSIGYC 204
Cdd:PRK08936  80 VKEFGTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHdIKGNIINMSSVHEQIPWPLFVHYA 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 205 ASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNI 241
Cdd:PRK08936 160 ASKGGVKLMTETLAMEYAP-KGIRVNNIGPGAINTPI 195
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
40-210 8.88e-18

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 84.13  E-value: 8.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  40 QGRRPEWELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekDILVLPLDLTDTGSHE 119
Cdd:PRK08324 412 QRMPKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-----RALGVACDVTDEAAVQ 486
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 120 AATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGK---IVTVNSILGIIS 196
Cdd:PRK08324 487 AAFEEAALAFGGVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIM--KAQGLggsIVFIASKNAVNP 564
                        170
                 ....*....|....
gi 649109145 197 VPLSIGYCASKHAL 210
Cdd:PRK08324 565 GPNFGAYGAAKAAE 578
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
48-241 1.00e-17

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: 81.22  E-value: 1.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEKDILVlplDLTDTGSHEAATKAVLQ 127
Cdd:cd05352    6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKC---DVSSQESVEKTFKQIQK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILG-IISVPLSIG-YCA 205
Cdd:cd05352   83 DFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGtIVNRPQPQAaYNA 162
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNI 241
Cdd:cd05352  163 SKAAVIHLAKSLAVEWAKY-FIRVNSISPGYIDTDL 197
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
48-254 1.20e-17

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 81.05  E-value: 1.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVkrrcLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHV----VDEIQQLGGQAFACRCDITSEQELSALADFALS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNN-GGMSQRSLcmDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK06113  85 KLGKVDILVNNaGGGGPKPF--DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASS 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 649109145 207 KHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLAGEVTKTI 254
Cdd:PRK06113 163 KAAASHLVRNMAFDLGE-KNIRVNGIAPGAILTDALKSVITPEIEQKM 209
PRK08628 PRK08628
SDR family oxidoreductase;
48-268 1.84e-17

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 80.77  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLG---VSLVLSARRVHELERVKRRclengnlkEKDILVLPLDLTDTGSHEAATKA 124
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGaipVIFGRSAPDDEFAEELRAL--------QPRAEFVQVDLTDDAQCRDAVEQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 125 VLQEFGRIDILVNNGGMSQrSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKqGKIVTVNSILGIISVPLSIGYC 204
Cdd:PRK08628  77 TVAKFGRIDGLVNNAGVND-GVGLEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNISSKTALTGQGGTSGYA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 649109145 205 ASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAG---------EVTKTIgnngDQSHKMTTSR 268
Cdd:PRK08628 155 AAKGAQLALTREWAVALAKD-GVRVNAVIPAEVMTPLYENWIATfddpeaklaAITAKI----PLGHRMTTAE 222
PRK07577 PRK07577
SDR family oxidoreductase;
48-239 1.95e-17

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 80.16  E-value: 1.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGvslvlsarrvHELERVKRRCLEN--GNLkekdilvLPLDLTDTGSHEAATKAV 125
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLG----------HQVIGIARSAIDDfpGEL-------FACDLADIEQTAATLAQI 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGrIDILVNNGGMS--QR--SLCMDTSLDVYrkliELNYLGTVSLTKCVLPHMIERKQGKIVTVNSiLGIISVPLSI 201
Cdd:PRK07577  64 NEIHP-VDAIVNNVGIAlpQPlgKIDLAALQDVY----DLNVRAAVQVTQAFLEGMKLREQGRIVNICS-RAIFGALDRT 137
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 202 GYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:PRK07577 138 SYSAAKSALVGCTRTWALELAEY-GITVNAVAPGPIET 174
PRK07856 PRK07856
SDR family oxidoreductase;
48-238 2.98e-17

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 79.98  E-value: 2.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRvhELERVKRRCLEngnlkekdilVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRR--APETVDGRPAE----------FHAADVRDPDQVAALVDAIVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQ---GKIVTVNSILGIISVPLSIGYC 204
Cdd:PRK07856  72 RHGRLDVLVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVM--QQQpggGSIVNIGSVSGRRPSPGTAAYG 149
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 205 ASKHALRGFFNGLRTELAtyPGIIVSNICPGPVQ 238
Cdd:PRK07856 150 AAKAGLLNLTRSLAVEWA--PKVRVNAVVVGLVR 181
PRK06701 PRK06701
short chain dehydrogenase; Provisional
48-237 3.87e-17

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 80.46  E-value: 3.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLEngnlKE-KDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVE----KEgVKCLLIPGDVSDEAFCKDAVEETV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMS--QRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMierKQGK-IVTVNSILGIISVPLSIGY 203
Cdd:PRK06701 120 RELGRLDILVNNAAFQypQQSL-EDITAEQLDKTFKTNIYSYFHMTKAALPHL---KQGSaIINTGSITGYEGNETLIDY 195
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 204 CASKHALRGFFNGLRTELATyPGIIVSNICPGPV 237
Cdd:PRK06701 196 SATKGAIHAFTRSLAQSLVQ-KGIRVNAVAPGPI 228
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
48-243 6.27e-17

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 78.90  E-value: 6.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVL-----SARRVHELERVKRRCLengnlkekDILVLPLDLTDTGSHEAAT 122
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnSPRRVKWLEDQKALGF--------DFIASEGNVGDWDSTKAAF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 123 KAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIG 202
Cdd:PRK12938  73 DKVKAEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTN 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 649109145 203 YCASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVE 243
Cdd:PRK12938 153 YSTAKAGIHGFTMSLAQEVAT-KGVTVNTVSPGYIGTDMVK 192
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
48-237 8.01e-17

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: 78.81  E-value: 8.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRvheLERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADIN---LEAARATAAEIG----PAACAISLDVTDQASIDRCVAALVD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIER-KQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:cd05363   74 RWGSIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQgRGGKIINMASQAGRRGEALVGVYCAT 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPV 237
Cdd:cd05363  154 KAAVISLTQSAGLNLIRH-GINVNAIAPGVV 183
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
44-210 1.06e-16

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: 78.28  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  44 PEWELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRClengnlkeKDILVLPLDLTDTgsheAATK 123
Cdd:cd05351    1 MELDFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVREC--------PGIEPVCVDLSDW----DATE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 AVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERK-QGKIVTVNSILGIISVPLSIG 202
Cdd:cd05351   69 EALGSVGPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGvPGSIVNVSSQASQRALTNHTV 148

                 ....*...
gi 649109145 203 YCASKHAL 210
Cdd:cd05351  149 YCSTKAAL 156
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
49-235 1.08e-16

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 78.45  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  49 TDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARR--VHElerVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSelVHE---VAAELRAAGG----EALALTADLETYAGAQAAMAAAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMS------------------QRSLcMDTsldvyrklielnylgtvsLTKC--VLPHMIERKQGKIV 186
Cdd:PRK12823  80 EAFGRIDVLINNVGGTiwakpfeeyeeeqieaeiRRSL-FPT------------------LWCCraVLPHMLAQGGGAIV 140
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 649109145 187 TVNSIL--GIISVPlsigYCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK12823 141 NVSSIAtrGINRVP----YSAAKGGVNALTASLAFEYAEH-GIRVNAVAPG 186
PRK05867 PRK05867
SDR family oxidoreductase;
55-243 1.08e-16

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 78.54  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGRIDI 134
Cdd:PRK05867  14 ITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGG----KVVPVCCDVSQHQQVTSMLDQVTAELGGIDI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 135 LVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIER-KQGKIVTVNSILG-IISVPLSIG-YCASKHALR 211
Cdd:PRK05867  90 AVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQgQGGVIINTASMSGhIINVPQQVShYCASKAAVI 169
                        170       180       190
                 ....*....|....*....|....*....|..
gi 649109145 212 GFFNGLRTELATYPgIIVSNICPGPVQSNIVE 243
Cdd:PRK05867 170 HLTKAMAVELAPHK-IRVNSVSPGYILTELVE 200
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
46-235 1.66e-16

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 78.13  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 W-ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSArrvhelervkrrcLENGNLKEKDILVLPLDLTDTGSHEAATKA 124
Cdd:PRK06171   4 WlNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNAD-------------IHGGDGQHENYQFVPTDVSSAEEVNHTVAE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 125 VLQEFGRIDILVNNGGMSQRSLCMDTS-------LD--VYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGII 195
Cdd:PRK06171  71 IIEKFGRIDGLVNNAGINIPRLLVDEKdpagkyeLNeaAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLE 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 649109145 196 -SVPLSIgYCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK06171 151 gSEGQSC-YAATKAALNSFTRSWAKELGKH-NIRVVGVAPG 189
PRK08589 PRK08589
SDR family oxidoreductase;
48-248 5.01e-16

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 76.74  E-value: 5.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGvSLVLSARRVHELERVKRRCLENGNLKEKDILvlplDLTDTGSHEAATKAVLQ 127
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEG-AYVLAVDIAEAVSETVDKIKSNGGKAKAYHV----DISDEQQVKDFASEIKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRS-LCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIErKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK08589  79 QFGRVDVLFNNAGVDNAAgRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQAADLYRSGYNAA 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 649109145 207 KHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVENsLAG 248
Cdd:PRK08589 158 KGAVINFTKSIAIEYGR-DGIRANAIAPGTIETPLVDK-LTG 197
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
52-235 5.89e-16

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: 76.34  E-value: 5.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRvhELERVKRRCLENGnlkEKDILVlPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05349    2 VVLVTGASRGLGAAIARSFAREGARVVVNYYR--STESAEAVAAEAG---ERAIAI-QADVRDRDQVQAMIEEAKNHFGP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNN--GGMS----QRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCA 205
Cdd:cd05349   76 VDTIVNNalIDFPfdpdQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHDYTT 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 649109145 206 SKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:cd05349  156 AKAALLGFTRNMAKELGPY-GITVNMVSGG 184
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
52-245 6.33e-16

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: 76.21  E-value: 6.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145   52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVH------------ELERVKRRClengnlkEKDILVLPLDLTDTGSHE 119
Cdd:TIGR04504   3 VALVTGAARGIGAATVRRLAADGWRVVAVDLCADdpavgyplatraELDAVAAAC-------PDQVLPVIADVRDPAALA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  120 AATKAVLQEFGRIDILVNNGG-MSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ---GKIVTVNSILGII 195
Cdd:TIGR04504  76 AAVALAVERWGRLDAAVAAAGvIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARPDprgGRFVAVASAAATR 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 649109145  196 SVPLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENS 245
Cdd:TIGR04504 156 GLPHLAAYCAAKHAVVGLVRGLAADLGGT-GVTANAVSPGSTRTAMLAAT 204
PRK08265 PRK08265
short chain dehydrogenase; Provisional
47-253 7.28e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 76.20  E-value: 7.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLEngnlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGE-------RARFIATDITDDAAIERAVATVV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNN-------GGMSQRSLCMDTsLDVyrklielNYLGTVSLTKCVLPHMIeRKQGKIVTVNSILGIISVPL 199
Cdd:PRK08265  76 ARFGRVDILVNLactylddGLASSRADWLAA-LDV-------NLVSAAMLAQAAHPHLA-RGGGAIVNFTSISAKFAQTG 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649109145 200 SIGYCASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVENSLAGEVTKT 253
Cdd:PRK08265 147 RWLYPASKAAIRQLTRSMAMDLAP-DGIRVNSVSPGWTWSRVMDELSGGDRAKA 199
PRK08267 PRK08267
SDR family oxidoreductase;
53-258 1.16e-15

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 75.74  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRcLENGNLkekdiLVLPLDLTDTGSHEAAtkavLQEF--- 129
Cdd:PRK08267   4 IFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAE-LGAGNA-----WTGALDVTDRAAWDAA----LADFaaa 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 --GRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK08267  74 tgGRLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 649109145 208 HALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEVTKTIGNNG 258
Cdd:PRK08267 154 FAVRGLTEALDLEWRRH-GIRVADVMPLFVDTAMLDGTSNEVDAGSTKRLG 203
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
47-235 1.18e-15

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: 75.96  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVL 126
Cdd:cd08935    2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALG----GRAIALAADVLDRASLERAREEIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGG---------------MSQRSLCmDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSI 191
Cdd:cd08935   78 AQFGTVDILINGAGgnhpdattdpehyepETEQNFF-DLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSM 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 649109145 192 LGIISVPLSIGYCASKHALRGFFNGLRTELATyPGIIVSNICPG 235
Cdd:cd08935  157 NAFSPLTKVPAYSAAKAAVSNFTQWLAVEFAT-TGVRVNAIAPG 199
PRK07035 PRK07035
SDR family oxidoreductase;
48-235 1.23e-15

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 75.44  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEkdilVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAE----ALACHIGEMEQIDALFAHIRE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMS-QRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK07035  82 RHGRLDILVNNAAANpYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYSIT 161
                        170       180
                 ....*....|....*....|....*....
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK07035 162 KAAVISMTKAFAKECAPF-GIRVNALLPG 189
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
52-235 1.40e-15

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 75.46  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCleNGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK12384   4 VAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEI--NAEYGEGMAYGFGADATSEQSVLALSRGVDEIFGR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERK-QGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:PRK12384  82 VDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFGG 161
                        170       180
                 ....*....|....*....|....*
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK12384 162 VGLTQSLALDLAEY-GITVHSLMLG 185
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
53-235 1.83e-15

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 74.79  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:PRK08085  12 ILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEG----IKAHAAPFNVTHKQEVEAAIEHIEKDIGPI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:PRK08085  88 DVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAASKGAVKM 167
                        170       180
                 ....*....|....*....|...
gi 649109145 213 FFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK08085 168 LTRGMCVELARH-NIQVNGIAPG 189
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
50-235 2.52e-15

(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: 74.67  E-value: 2.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  50 DMVVWVTGASSGIGEELAYQLSKLGVSLVlsarrVHELerVKRRCLENGNLKEKDILVLPLD------LTDTGSHEAATK 123
Cdd:cd05353    5 GRVVLVTGAGGGLGRAYALAFAERGAKVV-----VNDL--GGDRKGSGKSSSAADKVVDEIKaaggkaVANYDSVEDGEK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 ---AVLQEFGRIDILVNNGG-MSQRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISvpl 199
Cdd:cd05353   78 ivkTAIDAFGRVDILVNNAGiLRDRSF-AKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYG--- 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 200 SIG---YCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:cd05353  154 NFGqanYSAAKLGLLGLSNTLAIEGAKY-NITCNTIAPA 191
PRK06194 PRK06194
hypothetical protein; Provisional
55-243 2.82e-15

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 75.05  E-value: 2.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRIDI 134
Cdd:PRK06194  11 ITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQG----AEVLGVRTDVSDAAQVEALADAALERFGAVHL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 135 LVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIER------KQGKIVTVNSILGIISVPLSIGYCASKH 208
Cdd:PRK06194  87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAaekdpaYEGHIVNTASMAGLLAPPAMGIYNVSKH 166
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 649109145 209 ALRGFFNGLRTELATYPGII-VSNICPGPVQSNIVE 243
Cdd:PRK06194 167 AVVSLTETLYQDLSLVTDQVgASVLCPYFVPTGIWQ 202
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-235 3.13e-15

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 74.23  E-value: 3.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGT----EVRGYAANVTDEEDVEATFAQIA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDT---------SLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSilgiIS 196
Cdd:PRK08217  78 EDFGQLNGLINNAGILRDGLLVKAkdgkvtskmSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSkGVIINISS----IA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 649109145 197 VPLSIG---YCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK08217 154 RAGNMGqtnYSASKAGVAAMTVTWAKELARY-GIRVAAIAPG 194
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
48-240 3.45e-15

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 73.99  E-value: 3.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARR--------VHELERVKRRClengnlkekdiLVLPLDLTDTGSHE 119
Cdd:PRK08063   2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARsrkaaeetAEEIEALGRKA-----------LAVKANVGDVEKIK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 120 AATKAVLQEFGRIDILVNNG--GMSQRSLCMDTSLdvYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISV 197
Cdd:PRK08063  71 EMFAQIDEEFGRLDVFVNNAasGVLRPAMELEESH--WDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 649109145 198 P--LSIGycASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSN 240
Cdd:PRK08063 149 EnyTTVG--VSKAALEALTRYLAVELAPK-GIAVNAVSGGAVDTD 190
PRK06114 PRK06114
SDR family oxidoreductase;
46-235 3.64e-15

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 74.05  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARR--------VHELERVKRRClengnlkekdiLVLPLDLTDTGS 117
Cdd:PRK06114   4 FDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRtddglaetAEHIEAAGRRA-----------IQIAADVTSKAD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 118 HEAATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISV 197
Cdd:PRK06114  73 LRAAVARTEAELGALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVN 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 649109145 198 P--LSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK06114 153 RglLQAHYNASKAGVIHLSKSLAMEWVGR-GIRVNSISPG 191
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
52-237 4.99e-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: 73.47  E-value: 4.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVH--------ELERVKRRCLengnlkekdilVLPLDLTDTGSHEAATK 123
Cdd:cd05357    2 VALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEaeaqrlkdELNALRNSAV-----------LVQADLSDFAACADLVA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 AVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSIlgIISVPLS--I 201
Cdd:cd05357   71 AAFRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDA--MTDRPLTgyF 148
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 649109145 202 GYCASKHALRGFFNGLRTELAtyPGIIVSNICPGPV 237
Cdd:cd05357  149 AYCMSKAALEGLTRSAALELA--PNIRVNGIAPGLI 182
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
48-253 6.09e-15

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: 73.34  E-value: 6.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekdilvlpLDLTDTGSH-------EA 120
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEG-----------LSVTGTVCHvgkaedrER 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 121 ATKAVLQEFGRIDILVNNGGMSQ-RSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPL 199
Cdd:cd08936   77 LVATAVNLHGGVDILVSNAAVNPfFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPG 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649109145 200 SIGYCASKHALRGFFNGLRTELAtypgiivsnicpgpvQSNIVENSLAGEVTKT 253
Cdd:cd08936  157 LGPYNVSKTALLGLTKNLAPELA---------------PRNIRVNCLAPGLIKT 195
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
52-239 9.51e-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: 72.81  E-value: 9.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVL------SARRVHELERVKRRclengnlkekdILVLPLDLTDTGSHEAATKAV 125
Cdd:cd08943    3 VALVTGGASGIGLAIAKRLAAEGAAVVVadidpeIAEKVAEAAQGGPR-----------ALGVQCDVTSEAQVQSAFEQA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERK-QGKIVTVNSILGIISVPLSIGYC 204
Cdd:cd08943   72 VLEFGGLDIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGiGGNIVFNASKNAVAPGPNAAAYS 151
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 205 ASKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:cd08943  152 AAKAAEAHLARCLALEGGED-GIRVNTVNPDAVFR 185
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
46-240 1.25e-14

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 72.60  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSK-----LGVSLVLSARRVHELERVKRRCLEngnlkekdilvLPLDLTDTGSHEA 120
Cdd:PRK08993   6 FSLEGKVAVVTGCDTGLGQGMALGLAEagcdiVGINIVEPTETIEQVTALGRRFLS-----------LTADLRKIDGIPA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 121 ATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIER-KQGKIVTVNSIL---GIIS 196
Cdd:PRK08993  75 LLERAVAEFGHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQgNGGKIINIASMLsfqGGIR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 649109145 197 VPlsiGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSN 240
Cdd:PRK08993 155 VP---SYTASKSGVMGVTRLMANEWAKH-NINVNAIAPGYMATN 194
PRK08703 PRK08703
SDR family oxidoreductase;
48-239 3.92e-14

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 70.73  E-value: 3.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEKDIlvlPLDLTDTGSHE----AATk 123
Cdd:PRK08703   4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAI---RFDLMSAEEKEfeqfAAT- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 aVLQEF-GRIDILVNNGG-MSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSI 201
Cdd:PRK08703  80 -IAEATqGKLDGIVHCAGyFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWG 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 202 GYCASKHALRGFFNGLRTELATYPGIIVSNICPGPVQS 239
Cdd:PRK08703 159 GFGASKAALNYLCKVAADEWERFGNLRANVLVPGPINS 196
PRK06197 PRK06197
short chain dehydrogenase; Provisional
52-191 4.88e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 71.60  E-value: 4.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK06197  18 VAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAA--TPGADVTLQELDLTSLASVRAAADALRAAYPR 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 649109145 132 IDILVNNGGMsqrslcMDTSLDVYRKLIEL----NYLGTVSLTKCVLPHMIERKQGKIVTVNSI 191
Cdd:PRK06197  96 IDLLINNAGV------MYTPKQTTADGFELqfgtNHLGHFALTGLLLDRLLPVPGSRVVTVSSG 153
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
48-241 1.11e-13

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 69.81  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHElervkrrclENGNLKEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---------EAKELREKGVFTIKCDVGNRDQVKKSKEVVEK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGI-ISVPLSIGYCAS 206
Cdd:PRK06463  76 EFGRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAIT 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQSNI 241
Cdd:PRK06463 156 KAGIIILTRRLAFELGKY-GIRVNAVAPGWVETDM 189
PRK07677 PRK07677
short chain dehydrogenase; Provisional
52-238 1.39e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 69.71  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnlkEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK07677   3 VVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQF----PGQVLTVQMDVRNPEDVQKMVEQIDEKFGR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGgmSQRSLC--MDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGkivtvNSILGIISV---PLSIGYCAS 206
Cdd:PRK07677  79 IDALINNA--AGNFICpaEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIK-----GNIINMVATyawDAGPGVIHS 151
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 207 KHALRGFFNGLRT---ELATYPGIIVSNICPGPVQ 238
Cdd:PRK07677 152 AAAKAGVLAMTRTlavEWGRKYGIRVNAIAPGPIE 186
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
48-243 1.43e-13

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 69.43  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG-----ECIAIPADLSSEEGIEALVARVAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQG------KIVTVNSILGIISVPL-S 200
Cdd:cd08942   79 RSDRLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLL--RAAAtaenpaRVINIGSIAGIVVSGLeN 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 649109145 201 IGYCASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVE 243
Cdd:cd08942  157 YSYGASKAAVHQLTRKLAKELAG-EHITVNAIAPGRFPSKMTA 198
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
52-245 1.59e-13

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: 69.80  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCleNGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd09807    3 TVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEI--RRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEEDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQrslC-MDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGII------------SVP 198
Cdd:cd09807   81 LDVLINNAGVMR---CpYSKTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAgkinfddlnsekSYN 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 649109145 199 LSIGYCASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNIVENS 245
Cdd:cd09807  158 TGFAYCQSKLANVLFTRELARRLQG-TGVTVNALHPGVVRTELGRHT 203
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
48-235 2.41e-13

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 68.92  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQL----SKLGVsLVLSARRVHELERvkrrclENGNlkekDILVLPLDLTDTGSHEAATK 123
Cdd:cd05348    2 LKGEVALITGGGSGLGRALVERFvaegAKVAV-LDRSAEKVAELRA------DFGD----AVVGVEGDVRSLADNERAVA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 AVLQEFGRIDILVNNGGMSQRSLCM--------DTSLDvyrKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVnSILGII 195
Cdd:cd05348   71 RCVERFGKLDCFIGNAGIWDYSTSLvdipeeklDEAFD---ELFHINVKGYILGAKAALPALYATEGSVIFTV-SNAGFY 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 649109145 196 SVPLSIGYCASKHALRGFFNGLRTELAtyPGIIVSNICPG 235
Cdd:cd05348  147 PGGGGPLYTASKHAVVGLVKQLAYELA--PHIRVNGVAPG 184
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
48-235 2.68e-13

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 68.83  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQL----SKLGVsLVLSARRVHELervkRRCLEngnlkeKDILVLPLDLTDTGSHEAATK 123
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFlaegARVAV-LERSAEKLASL----RQRFG------DHVLVVEGDVTSYADNQRAVD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 AVLQEFGRIDILVNNGGMSQRSLCM--------DTSLDvyrKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVnSILGII 195
Cdd:PRK06200  73 QTVDAFGKLDCFVGNAGIWDYNTSLvdipaetlDTAFD---EIFNVNVKGYLLGAKAALPALKASGGSMIFTL-SNSSFY 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 649109145 196 SVPLSIGYCASKHALRGFFNGLRTELAtyPGIIVSNICPG 235
Cdd:PRK06200 149 PGGGGPLYTASKHAVVGLVRQLAYELA--PKIRVNGVAPG 186
PRK06500 PRK06500
SDR family oxidoreductase;
53-238 3.36e-13

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 68.44  E-value: 3.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:PRK06500   9 ALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARA---ELGE----SALVIRADAGDVAAQKALAQALAEAFGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPhmIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:PRK06500  82 DAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLP--LLANPASIVLNGSINAHIGMPNSSVYAASKAALLS 159
                        170       180
                 ....*....|....*....|....*.
gi 649109145 213 FFNGLRTELATYpGIIVSNICPGPVQ 238
Cdd:PRK06500 160 LAKTLSGELLPR-GIRVNAVSPGPVQ 184
PRK09135 PRK09135
pteridine reductase; Provisional
52-238 5.64e-13

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 67.65  E-value: 5.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARR-VHELERvkrRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK09135   8 VALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADA---LAAELNALRPGSAAALQADLLDPDALPELVAACVAAFG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMiERKQGKIVtvnSILGI-ISVPLS--IGYCASK 207
Cdd:PRK09135  85 RLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQL-RKQRGAIV---NITDIhAERPLKgyPVYCAAK 160
                        170       180       190
                 ....*....|....*....|....*....|.
gi 649109145 208 HALRGFFNGLRTELAtyPGIIVSNICPGPVQ 238
Cdd:PRK09135 161 AALEMLTRSLALELA--PEVRVNAVAPGAIL 189
PLN02780 PLN02780
ketoreductase/ oxidoreductase
43-220 6.57e-13

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 68.35  E-value: 6.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  43 RPEWELTDMVVW--VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLEN-GNLKEKDILVlplDLTdtGSHE 119
Cdd:PLN02780  44 RPAKNLKKYGSWalVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKySKTQIKTVVV---DFS--GDID 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 120 AATKAVLQEFGRID--ILVNNGGMSQ--RSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGII 195
Cdd:PLN02780 119 EGVKRIKETIEGLDvgVLINNVGVSYpyARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIV 198
                        170       180
                 ....*....|....*....|....*..
gi 649109145 196 --SVPLSIGYCASKHALRGFFNGLRTE 220
Cdd:PLN02780 199 ipSDPLYAVYAATKAYIDQFSRCLYVE 225
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
46-240 9.68e-13

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 67.24  E-value: 9.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  46 WELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLEngnlkeKDILVLPLDLTDTGSHEAATKAV 125
Cdd:PRK12481   4 FDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEALG------RKFHFITADLIQQKDIDSIVSQA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSIL---GIISVPlsi 201
Cdd:PRK12481  78 VEVMGHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNgGKIINIASMLsfqGGIRVP--- 154
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 649109145 202 GYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSN 240
Cdd:PRK12481 155 SYTASKSAVMGLTRALATELSQY-NINVNAIAPGYMATD 192
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
55-237 9.93e-13

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: 66.39  E-value: 9.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclengnlkEKDILVLPLDLTdtgsHEAATKAVLQEFGRIDI 134
Cdd:cd11730    3 ILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAA---------EVGALARPADVA----AELEVWALAQELGPLDL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 135 LVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIErkQGKIVTVNSILGIISVPLSIGYCASKHALRGFF 214
Cdd:cd11730   70 LVYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAA--GARLVFLGAYPELVMLPGLSAYAAAKAALEAYV 147
                        170       180
                 ....*....|....*....|...
gi 649109145 215 NGLRTELAtypGIIVSNICPGPV 237
Cdd:cd11730  148 EVARKEVR---GLRLTLVRPPAV 167
PRK06123 PRK06123
SDR family oxidoreductase;
52-241 1.24e-12

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 66.73  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHEL-ERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK06123   4 VMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAaEAVVQAIRRQGG----EALAVAADVADEADVLRLFEAVDRELG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQRSLCMDtSLDVYR--KLIELNYLGTVSLTKCVLPHMIER---KQGKIVTVNSILGIISVPLS-IGYC 204
Cdd:PRK06123  80 RLDALVNNAGILEAQMRLE-QMDAARltRIFATNVVGSFLCAREAVKRMSTRhggRGGAIVNVSSMAARLGSPGEyIDYA 158
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 205 ASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNI 241
Cdd:PRK06123 159 ASKGAIDTMTIGLAKEVAA-EGIRVNAVRPGVIYTEI 194
PLN02253 PLN02253
xanthoxin dehydrogenase
44-241 2.41e-12

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 66.39  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  44 PEWELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLsARRVHELERVKRRCLENgnlkEKDILVLPLDLTDTGSHEAATK 123
Cdd:PLN02253  12 PSQRLLGKVALVTGGATGIGESIVRLFHKHGAKVCI-VDLQDDLGQNVCDSLGG----EPNVCFFHCDVTVEDDVSRAVD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 124 AVLQEFGRIDILVNNGGMSQRSlCMD---TSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLS 200
Cdd:PLN02253  87 FTVDKFGTLDIMVNNAGLTGPP-CPDirnVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGP 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 649109145 201 IGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNI 241
Cdd:PLN02253 166 HAYTGSKHAVLGLTRSVAAELGKH-GIRVNCVSPYAVPTAL 205
PRK07069 PRK07069
short chain dehydrogenase; Validated
55-211 6.20e-12

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 64.73  E-value: 6.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLS--------ARRVHELervkrrcleNGNLKEKDILVLPLDLTDtgshEAATKAVL 126
Cdd:PRK07069   4 ITGAAGGLGRAIARRMAEQGAKVFLTdindaaglDAFAAEI---------NAAHGEGVAFAAVQDVTD----EAQWQALL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QE----FGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIG 202
Cdd:PRK07069  71 AQaadaMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTA 150

                 ....*....
gi 649109145 203 YCASKHALR 211
Cdd:PRK07069 151 YNASKAAVA 159
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
52-255 6.88e-12

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 64.75  E-value: 6.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK08643   4 VALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGG----KAIAVKADVSDRDQVFAAVRQVVDTFGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSILGIISVP-LSIgYCASKHA 209
Cdd:PRK08643  80 LNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHgGKIINATSQAGVVGNPeLAV-YSSTKFA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 649109145 210 LRGFFNGLRTELATyPGIIVSNICPGPVQSNIVEnSLAGEVTKTIG 255
Cdd:PRK08643 159 VRGLTQTAARDLAS-EGITVNAYAPGIVKTPMMF-DIAHQVGENAG 202
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
48-239 9.35e-12

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


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 64.13  E-value: 9.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEkdiLVLPLDLTDTGSH--EAATKAV 125
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQP---QWFILDLLTCTSEncQQLAQRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLD-VYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYC 204
Cdd:cd05340   79 AVNYPRLDGVLHNAGLLGDVCPLSEQNPqVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 205 ASKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:cd05340  159 VSKFATEGL*QVLADEYQQR-NLRVNCINPGGTRT 192
PRK07102 PRK07102
SDR family oxidoreductase;
53-237 1.45e-11

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 63.40  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclengNLKEK---DILVLPLDLTDTGSHEAATKAVLqef 129
Cdd:PRK07102   4 ILIIGATSDIARACARRYAAAGARLYLAARDVERLERLAD------DLRARgavAVSTHELDILDTASHAAFLDSLP--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 GRIDI-LVNNGGMSQRSLCmDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKH 208
Cdd:PRK07102  75 ALPDIvLIAVGTLGDQAAC-EADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGSAKA 153
                        170       180
                 ....*....|....*....|....*....
gi 649109145 209 ALRGFFNGLRTELATyPGIIVSNICPGPV 237
Cdd:PRK07102 154 ALTAFLSGLRNRLFK-SGVHVLTVKPGFV 181
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
52-235 1.66e-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: 63.37  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSarrvhelERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd09761    3 VAIVTGGGHGIGKQICLDFLEAGDKVVFA-------DIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKqGKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:cd09761   76 IDVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASKGGLV 154
                        170       180
                 ....*....|....*....|....
gi 649109145 212 GFFNGLRTELAtyPGIIVSNICPG 235
Cdd:cd09761  155 ALTHALAMSLG--PDIRVNCISPG 176
PRK06128 PRK06128
SDR family oxidoreductase;
55-237 2.29e-11

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 63.72  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSarRVHELERVKRRCLENGNLKEKDILVLPLDLTDTG-SHEAATKAVlQEFGRID 133
Cdd:PRK06128  60 ITGADSGIGRATAIAFAREGADIALN--YLPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAfCRQLVERAV-KELGGLD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNNGGMSQ-RSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:PRK06128 137 ILVNIAGKQTaVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL--PPGASIINTGSIQSYQPSPTLLDYASTKAAIVA 214
                        170       180
                 ....*....|....*....|....*
gi 649109145 213 FFNGLRTELATyPGIIVSNICPGPV 237
Cdd:PRK06128 215 FTKALAKQVAE-KGIRVNAVAPGPV 238
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
53-239 3.20e-11

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: 61.38  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLsarrvhelervkrrclengnlkekdilvlpldLTDtgsheaatkavlqefgRI 132
Cdd:cd02266    1 VLVTGGSGGIGGAIARWLASRGSPKVL--------------------------------VVS----------------RR 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCASKHALRG 212
Cdd:cd02266   33 DVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDG 112
                        170       180
                 ....*....|....*....|....*..
gi 649109145 213 FFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:cd02266  113 LAQQWASEGWGN-GLPATAVACGTWAG 138
PRK07831 PRK07831
SDR family oxidoreductase;
48-193 3.64e-11

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 62.74  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGAS-SGIGEELAYQLSKLGVSLVLS---ARRVHE-LERVKrrclenGNLKEKDILVLPLDLTDTGSHEAAT 122
Cdd:PRK07831  15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISdihERRLGEtADELA------AELGLGRVEAVVCDVTSEAQVDALI 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 649109145 123 KAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSILG 193
Cdd:PRK07831  89 DAAVERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHgGVIVNNASVLG 160
PRK07985 PRK07985
SDR family oxidoreductase;
48-237 7.82e-11

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 61.93  E-value: 7.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHE--LERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAV 125
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEedAQDVKKIIEECG----RKAVLLPGDLSDEKFARSLVHEA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGmSQRSL--CMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSIGY 203
Cdd:PRK07985 123 HKALGGLDIMALVAG-KQVAIpdIADLTSEQFQKTFAINVFALFWLTQEAIPLL--PKGASIITTSSIQAYQPSPHLLDY 199
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 204 CASKHALRGFFNGLRTELATyPGIIVSNICPGPV 237
Cdd:PRK07985 200 AATKAAILNYSRGLAKQVAE-KGIRVNIVAPGPI 232
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
53-201 2.02e-10

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: 60.15  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRV--------------HELERVKRRCLEngnlkekdilvLPLDLTDTGSH 118
Cdd:cd09762    6 LFITGASRGIGKAIALKAARDGANVVIAAKTAephpklpgtiytaaEEIEAAGGKALP-----------CIVDIRDEDQV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 119 EAATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTvnsilgiISVP 198
Cdd:cd09762   75 RAAVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILN-------LSPP 147

                 ...
gi 649109145 199 LSI 201
Cdd:cd09762  148 LNL 150
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
52-247 3.07e-10

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: 59.82  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGvslvlsarrvHELERVkrrclengNLKEKDILVlplDLTDTGSHEAATKAVL-QEFG 130
Cdd:cd05328    1 TIVITGAASGIGAATAELLEDAG----------HTVIGI--------DLREADVIA---DLSTPEGRAAAIADVLaRCSG 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGMSQrSLCMDTSLDVyrklielNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGI---------------- 194
Cdd:cd05328   60 VLDGLVNCAGVGG-TTVAGLVLKV-------NYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAgwaqdklelakalaag 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 649109145 195 -----ISV------PLSIGYCASKHAL-RGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLA 247
Cdd:cd05328  132 tearaVALaehagqPGYLAYAGSKEALtVWTRRRAATWLYGA-GVRVNTVAPGPVETPILQAFLQ 195
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
52-235 5.55e-10

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: 59.02  E-value: 5.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRclENGNLKEKDiLVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:cd05322    4 VAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADE--INAEYGEKA-YGFGADATNEQSVIALSKGVDEIFKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERK-QGKIVTVNSILGIISVPLSIGYCASKHAL 210
Cdd:cd05322   81 VDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGKVGSKHNSGYSAAKFGG 160
                        170       180
                 ....*....|....*....|....*
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPG 235
Cdd:cd05322  161 VGLTQSLALDLAEH-GITVNSLMLG 184
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
48-235 6.61e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 58.73  E-value: 6.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEkdiLVLPLDLtdtgshEAATKA--- 124
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQP---AIIPLDL------LTATPQnyq 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 125 -----VLQEFGRIDILVNNGG-------MSQrsLCMDTSLDVYRklieLNYLGTVSLTKCVLPHMIERKQGKIVTVNSil 192
Cdd:PRK08945  81 qladtIEEQFGRLDGVLHNAGllgelgpMEQ--QDPEVWQDVMQ----VNVNATFMLTQALLPLLLKSPAASLVFTSS-- 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 649109145 193 giisvplSIG---------YCASKHALRGFFNGLRTELaTYPGIIVSNICPG 235
Cdd:PRK08945 153 -------SVGrqgranwgaYAVSKFATEGMMQVLADEY-QGTNLRVNCINPG 196
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
55-241 7.82e-10

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 58.77  E-value: 7.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145   55 VTGASSGIGEELAYQLSKL----GVSLVLSARRVHELERVKRRCLENGNlkEKDILVLPLDLTDTGSHEAATKAVLQ--- 127
Cdd:TIGR01500   5 VTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIGAERS--GLRVVRVSLDLGAEAGLEQLLKALRElpr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  128 --EFGRIdILVNNGG----MSQRSLCMDTSlDVYRKLIELNYLGTVSLTkCVLPHMIERKQG---KIVTVNSILGIISVP 198
Cdd:TIGR01500  83 pkGLQRL-LLINNAGtlgdVSKGFVDLSDS-TQVQNYWALNLTSMLCLT-SSVLKAFKDSPGlnrTVVNISSLCAIQPFK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 649109145  199 LSIGYCASKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNI 241
Cdd:TIGR01500 160 GWALYCAGKAARDMLFQVLALEEKN-PNVRVLNYAPGVLDTDM 201
PRK06947 PRK06947
SDR family oxidoreductase;
52-241 9.41e-10

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 58.28  E-value: 9.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARR--------VHELERV-KRRCLENGNL-KEKDILVLpldltdtgsHEAA 121
Cdd:PRK06947   4 VVLITGASRGIGRATAVLAAARGWSVGINYARdaaaaeetADAVRAAgGRACVVAGDVaNEADVIAM---------FDAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 122 TkavlQEFGRIDILVNNGGMSQRSLCM-DTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGK---IVTVNSILGIISV 197
Cdd:PRK06947  75 Q----SAFGRLDALVNNAGIVAPSMPLaDMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRggaIVNVSSIASRLGS 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 649109145 198 PLS-IGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNI 241
Cdd:PRK06947 151 PNEyVDYAGSKGAVDTLTLGLAKELGPH-GVRVNAVRPGLIETEI 194
PRK08339 PRK08339
short chain dehydrogenase; Provisional
47-263 1.22e-09

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 57.94  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLkekDILVLPLDLTDTGSHEAATKAvL 126
Cdd:PRK08339   5 DLSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNV---DVSYIVADLTKREDLERTVKE-L 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVPLSIGYCAS 206
Cdd:PRK08339  81 KNIGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVV 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENsLAGEVTKTIGNNGDQSHK 263
Cdd:PRK08339 161 RISMAGLVRTLAKELGPK-GITVNGIMPGIIRTDRVIQ-LAQDRAKREGKSVEEALQ 215
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
47-235 2.13e-09

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 57.41  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHElervKRRCLEnGNLKEKDIlVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSED----AAEALA-DELGDRAI-ALQADVTDREQVQAMFATAT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGR-IDILVNNG-------GMSQRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVP 198
Cdd:PRK08642  76 EHFGKpITTVVNNAladfsfdGDARKKA-DDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVV 154
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 649109145 199 LSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK08642 155 PYHDYTTAKAALLGLTRNLAAELGPY-GITVNMVSGG 190
PRK06196 PRK06196
oxidoreductase; Provisional
47-191 2.35e-09

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 57.77  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRrclengNLKEKDilVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK06196  23 DLSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALA------GIDGVE--VVMLDLADLESVRAFAERFL 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 649109145 127 QEFGRIDILVNNGG-MSqrslCMDTSL-DVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSI 191
Cdd:PRK06196  95 DSGRRIDILINNAGvMA----CPETRVgDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSA 157
SDR_dihy_bifunc NF012208
bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family ...
55-254 2.97e-09

bifunctional dihydropteridine reductase/dihydrofolate reductase TmpR; Members of this family are SDR family oxidoreductases, unrelated to previously known families of dihydrofolate reductase (DHFR), one of which was demonstrated to be a bifunctional dihydropteridine reductase/dihydrofolate reductase. The DHFR activity can give a heterologously expressed protein the ability to confer resistance to trimethoprim, an inhibitor of most forms of DHFR.


Pssm-ID: 411089 [Multi-domain]  Cd Length: 233  Bit Score: 56.47  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHEL-ERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRID 133
Cdd:NF012208   3 VTGSARGIGRAIALALAREGFDVAVHYRRSAEAaEQTAQEAEALG----VKAITLQADLTDPEQARSLVEEAAEALGGLS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNN-GGMSQRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTvnsiLG------IISVPLSIGYCAS 206
Cdd:NF012208  79 VLVNNvGNYLHKPL-LETTDEEWHEMLDSNLNATFYVTQAALPLMRAAGWGRIVN----LGyagaqnLLARPGITPYVIA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 649109145 207 KHALRGFFNGLRTELATYpGIIVSNICPGpvqsnIVENSlageVTKTI 254
Cdd:NF012208 154 KTGVIIYSKALAKELAGD-GITVNVVSPG-----VAENS----VSQPL 191
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
55-248 3.16e-09

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: 56.83  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCL-ENGNlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRID 133
Cdd:cd09808    6 ITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIEtESGN---QNIFLHIVDMSDPKQVWEFVEEFKEEGKKLH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNNGG--MSQRSLcmdtSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSiLGIISVPLSIGYCASKhalR 211
Cdd:cd09808   83 VLINNAGcmVNKREL----TEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSS-GGMLVQKLNTNNLQSE---R 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 649109145 212 GFFNG------------LRTE--LATYPGIIVSNICPGPVQSNIVENSLAG 248
Cdd:cd09808  155 TAFDGtmvyaqnkrqqvIMTEqwAKKHPEIHFSVMHPGWADTPAVRNSMPD 205
PRK08278 PRK08278
SDR family oxidoreductase;
48-201 3.75e-09

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 56.84  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRV--HE-----LERVKRRCLENGNlkekDILVLPLDLTDTGSHEA 120
Cdd:PRK08278   4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAepHPklpgtIHTAAEEIEAAGG----QALPLVGDVRDEDQVAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 121 ATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTvnsilgiISVPLS 200
Cdd:PRK08278  80 AVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILT-------LSPPLN 152

                 .
gi 649109145 201 I 201
Cdd:PRK08278 153 L 153
PRK09730 PRK09730
SDR family oxidoreductase;
52-241 5.90e-09

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 56.01  E-value: 5.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLS-ARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNyQQNLHAAQEVVNLITQAGG----KAFVLQADISDENQVVAMFTAIDQHDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGG-MSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGK---IVTVNSILGIISVPLS-IGYCA 205
Cdd:PRK09730  79 PLAALVNNAGiLFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASRLGAPGEyVDYAA 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 649109145 206 SKHALRGFFNGLRTELATyPGIIVSNICPGPVQSNI 241
Cdd:PRK09730 159 SKGAIDTLTTGLSLEVAA-QGIRVNCVRPGFIYTEM 193
PRK05876 PRK05876
short chain dehydrogenase; Provisional
55-245 9.96e-09

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 55.35  E-value: 9.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERvkrrCLENGNLKEKDILVLPLDLT--DTGSHEAATKAVLqeFGRI 132
Cdd:PRK05876  11 ITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQ----AVNHLRAEGFDVHGVMCDVRhrEEVTHLADEAFRL--LGHV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQ-GKIVTVNSILGIISVPLSIGYCASKHALR 211
Cdd:PRK05876  85 DVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTgGHVVFTASFAGLVPNAGLGAYGVAKYGVV 164
                        170       180       190
                 ....*....|....*....|....*....|....
gi 649109145 212 GFFNGLRTELaTYPGIIVSNICPGPVQSNIVENS 245
Cdd:PRK05876 165 GLAETLAREV-TADGIGVSVLCPMVVETNLVANS 197
PRK12746 PRK12746
SDR family oxidoreductase;
48-241 2.21e-08

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 54.27  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLS-ARRVHELERVKRRCLENGN---LKEKDILVLP--LDLTDTGSHEAA 121
Cdd:PRK12746   4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIESNGGkafLIEADLNSIDgvKKLVEQLKNELQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 122 TKAVLQEfgrIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSI 201
Cdd:PRK12746  84 IRVGTSE---IDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL--RAEGRVINISSAEVRLGFTGSI 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 649109145 202 GYCASKHALrgffNGLRTELATY---PGIIVSNICPGPVQSNI 241
Cdd:PRK12746 159 AYGLSKGAL----NTMTLPLAKHlgeRGITVNTIMPGYTKTDI 197
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
28-235 4.47e-08

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 54.46  E-value: 4.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  28 ADGDLTLLWAewqgrRPeweLTDMVVWVTGASSGIGEELAYQLSKLGVSLVL----SARRvhELERVKRRCleNGNlkek 103
Cdd:PRK08261 196 ADAAPPADWD-----RP---LAGKVALVTGAARGIGAAIAEVLARDGAHVVCldvpAAGE--ALAAVANRV--GGT---- 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 104 dilVLPLDLTDTGSHEAATKAVLQEFGRIDILVNNGGMSQ-RSLC-MDTslDVYRKLIELNYLGTVSLTKCVLPHMIERK 181
Cdd:PRK08261 260 ---ALALDITAPDAPARIAEHLAERHGGLDIVVHNAGITRdKTLAnMDE--ARWDSVLAVNLLAPLRITEALLAAGALGD 334
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649109145 182 QGKIVTVNSILGIISVPLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK08261 335 GGRIVGVSSISGIAGNRGQTNYAASKAGVIGLVQALAPLLAER-GITINAVAPG 387
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
52-140 7.15e-08

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 53.16  E-value: 7.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQL-----SKLGVSLVLSARRVHELERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVL 126
Cdd:cd08941    3 VVLVTGANSGLGLAICERLlaeddENPELTLILACRNLQRAEAACRALLASHPDARVVFDYVLVDLSNMVSVFAAAKELK 82
                         90
                 ....*....|....
gi 649109145 127 QEFGRIDILVNNGG 140
Cdd:cd08941   83 KRYPRLDYLYLNAG 96
PRK07806 PRK07806
SDR family oxidoreductase;
47-230 8.86e-08

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 52.41  E-value: 8.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARR--------VHELERVKRRCLENGNlkekdilvlplDLTDTGSH 118
Cdd:PRK07806   3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkaprankvVAEIEAAGGRASAVGA-----------DLTDEESV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 119 EAATKAVLQEFGRIDILVNN--GGMSQRslcMDTsldvyRKLIELNYLGTVSLTKCVLPHMIErkQGKIVTVNS-----I 191
Cdd:PRK07806  72 AALMDTAREEFGGLDALVLNasGGMESG---MDE-----DYAMRLNRDAQRNLARAALPLMPA--GSRVVFVTShqahfI 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 649109145 192 LGIISVPLSIGYCASKHALRGFFNGLRTELAtYPGI---IVS 230
Cdd:PRK07806 142 PTVKTMPEYEPVARSKRAGEDALRALRPELA-EKGIgfvVVS 182
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
55-245 9.06e-08

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 52.38  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHElERVKRRCLENGNLKEkdilvLPLDLTDTGSHEAATKAVL-----QEF 129
Cdd:PRK06924   6 ITGTSQGLGEAIANQLLEKGTHVISISRTENK-ELTKLAEQYNSNLTF-----HSLDLQDVHELETNFNEILssiqeDNV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 130 GRIdILVNNGGM------SQRSlcmdtSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVtVNSILGIISVPLS--I 201
Cdd:PRK06924  80 SSI-HLINNAGMvapikpIEKA-----ESEELITNVHLNLLAPMILTSTFMKHTKDWKVDKRV-INISSGAAKNPYFgwS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649109145 202 GYCASKHALRGFFNGLRTE----------LATYPGIIVSNIcpgpvQSNIVENS 245
Cdd:PRK06924 153 AYCSSKAGLDMFTQTVATEqeeeeypvkiVAFSPGVMDTNM-----QAQIRSSS 201
PRK05717 PRK05717
SDR family oxidoreductase;
52-235 1.12e-07

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 52.20  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekdiLVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK05717  12 VALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENA-------WFIAMDVADEAQVAAGVAEVLGQFGR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDV--YRKLIELNYLGTVSLTKCVLPHMiERKQGKIVTVNSILGIISVPLSIGYCASKHA 209
Cdd:PRK05717  85 LDALVCNAAIADPHNTTLESLSLahWNRVLAVNLTGPMLLAKHCAPYL-RAHNGAIVNLASTRARQSEPDTEAYAASKGG 163
                        170       180
                 ....*....|....*....|....*.
gi 649109145 210 LRGFFNGLRTELAtyPGIIVSNICPG 235
Cdd:PRK05717 164 LLALTHALAISLG--PEIRVNAVSPG 187
PRK12747 PRK12747
short chain dehydrogenase; Provisional
48-252 1.66e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 51.61  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLS-ARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVL 126
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHyGNRKEEAEETVYEIQSNGG----SAFSIGANLESLHGVEALYSSLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEF------GRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLS 200
Cdd:PRK12747  78 NELqnrtgsTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPDF 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 649109145 201 IGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVENSLAGEVTK 252
Cdd:PRK12747 156 IAYSMTKGAINTMTFTLAKQLGAR-GITVNAILPGFIKTDMNAELLSDPMMK 206
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
55-239 1.77e-07

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 51.71  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGAS--SGIGEELAYQLSKLGVSLVL------------------SARRVHELERVKRRClenGNLKekdilvlpLDLTD 114
Cdd:PRK12859  11 VTGVSrlDGIGAAICKELAEAGADIFFtywtaydkempwgvdqdeQIQLQEELLKNGVKV---SSME--------LDLTQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 115 TGSHEAATKAVLQEFGRIDILVNNGgmsqrslCMDTSLDvYRKLIE--------LNYLGTVSLTkCVLPHMIERKQ-GKI 185
Cdd:PRK12859  80 NDAPKELLNKVTEQLGYPHILVNNA-------AYSTNND-FSNLTAeeldkhymVNVRATTLLS-SQFARGFDKKSgGRI 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649109145 186 VTVNSILGIISVPLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:PRK12859 151 INMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHL-GITVNAINPGPTDT 203
PRK05854 PRK05854
SDR family oxidoreductase;
55-191 1.78e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 51.99  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSAR--RVHE--LERVKRRclengnLKEKDILVLPLDLTDTGSHEAATKAVLQEfG 130
Cdd:PRK05854  19 VTGASDGLGLGLARRLAAAGAEVILPVRnrAKGEaaVAAIRTA------VPDAKLSLRALDLSSLASVAALGEQLRAE-G 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 649109145 131 R-IDILVNNGG-MS--QRslcmDTSLDVYRKLIELNYLGTVSLTKCVLPhMIERKQGKIVTVNSI 191
Cdd:PRK05854  92 RpIHLLINNAGvMTppER----QTTADGFELQFGTNHLGHFALTAHLLP-LLRAGRARVTSQSSI 151
PRK06101 PRK06101
SDR family oxidoreductase;
52-239 2.23e-07

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 51.02  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARrvhelervKRRCLENGNLKEKDILVLPLDLTDtgsHEaATKAVLQEFGR 131
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGR--------NQSVLDELHTQSANIFTLAFDVTD---HP-GTKAALSQLPF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 I-DILVNNGGMSQRslcMDTSL---DVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSIGYCASK 207
Cdd:PRK06101  71 IpELWIFNAGDCEY---MDDGKvdaTLMARVFNVNVLGVANCIEGIQPHL--SCGHRVVIVGSIASELALPRAEAYGASK 145
                        170       180       190
                 ....*....|....*....|....*....|..
gi 649109145 208 HALRGFFNGLRTELATyPGIIVSNICPGPVQS 239
Cdd:PRK06101 146 AAVAYFARTLQLDLRP-KGIEVVTVFPGFVAT 176
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
55-239 2.38e-07

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 51.23  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGAS--SGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKEKDILV-------LPLDLTDTGSHEAATKAV 125
Cdd:PRK12748  10 VTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWGMHDKEPVLLKEEIESygvrcehMEIDLSQPYAPNRVFYAV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNS--ILGiiSVPLSIGY 203
Cdd:PRK12748  90 SERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGGRIINLTSgqSLG--PMPDELAY 167
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 649109145 204 CASKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:PRK12748 168 AATKGAIEAFTKSLAPELAEK-GITVNAVNPGPTDT 202
PRK08340 PRK08340
SDR family oxidoreductase;
51-191 3.42e-07

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 50.57  E-value: 3.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  51 MVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGnlkekDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK08340   1 MNVLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-----EVYAVKADLSDKDDLKNLVKEAWELLG 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 649109145 131 RIDILVNNGGMSQRSLCMDTSLDvYRKLIELNYLGTVS---LTKCVLPHMIERK-QGKIVTVNSI 191
Cdd:PRK08340  76 GIDALVWNAGNVRCEPCMLHEAG-YSDWLEAALLHLVApgyLTTLLIQAWLEKKmKGVLVYLSSV 139
SDR_subfam_4 NF040491
mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR ...
52-235 3.92e-07

mycofactocin-coupled SDR family oxidoreductase; Members of this family are uncharacterized SDR family oxidoreductase regularly found encoded next to genes for mycofactocin biosynthesis proteins, and never found in genomes lacking mycofactocin. Members of this family are likely to represent a family of proteins that share a specific function.


Pssm-ID: 468513 [Multi-domain]  Cd Length: 256  Bit Score: 50.44  E-value: 3.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLV-LSARRVHEL-----ERVKRRCLENGNLKEKDILVLplDLTDTGSHEAATKAV 125
Cdd:NF040491   2 VALVTGAARGIGAATVRRLAARGYAVVaVDACAGDPApyplgTEADLDALVASSPGRVETVVA--DVRDRAALAAAVALA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 126 LQEFGRIDILVN-----NGGmsqRSLcMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIER---KQGKIVTVNSILGIISV 197
Cdd:NF040491  80 LDRWGRLDAAVAaaaviAGG---RPL-WETPPEELDALWDVDVRGVWNLAAAAVPALLAGpdpRGCRFVAVASAAGHRGL 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 198 PLSIGYCASKHALRGFFNGLRTELATyPGIIVSNICPG 235
Cdd:NF040491 156 FHLAAYCAAKHAVVGLVRGLAADLAG-TGVTACAVSPG 192
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
48-244 3.93e-07

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: 50.52  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVH-ELERVKRRCLENGNlkeKDILVLpLDLTDtgshEAATKAVL 126
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGG---KCIPVR-CDHSD----DDEVEALF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEF-----GRIDILVNNgGMSQRSLCMDTsldVYRKLIEL--------NYLGTVSLTKC---VLPHMIERKQGKIVTVNS 190
Cdd:cd09763   73 ERVareqqGRLDILVNN-AYAAVQLILVG---VAKPFWEEpptiwddiNNVGLRAHYACsvyAAPLMVKAGKGLIVIISS 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 649109145 191 iLGIISVPLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNIVEN 244
Cdd:cd09763  149 -TGGLEYLFNVAYGVGKAAIDRMAADMAHELKPH-GVAVVSLWPGFVRTELVLE 200
PRK05875 PRK05875
short chain dehydrogenase; Provisional
48-191 9.25e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 49.42  E-value: 9.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKG--AGAVRYEPADVTDEDQVARAVDAATA 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 649109145 128 EFGRIDILVNNGGMSQrSLCMDTSLDV--YRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSI 191
Cdd:PRK05875  83 WHGRLHGVVHCAGGSE-TIGPITQIDSdaWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSI 147
PRK12742 PRK12742
SDR family oxidoreductase;
47-241 1.51e-06

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 48.60  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSarRVHELERVKRRCLENGNlkekdilvlPLDLTDTGSHEAATKAVl 126
Cdd:PRK12742   3 AFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFT--YAGSKDAAERLAQETGA---------TAVQTDSADRDAVIDVV- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 127 QEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELN----YLGTVSLTKcvlpHMIErkQGKIVTVNSILG-IISVPLSI 201
Cdd:PRK12742  71 RKSGALDILVVNAGIAVFGDALELDADDIDRLFKINihapYHASVEAAR----QMPE--GGRIIIIGSVNGdRMPVAGMA 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 649109145 202 GYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSNI 241
Cdd:PRK12742 145 AYAASKSALQGMARGLARDFGPR-GITINVVQPGPIDTDA 183
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
27-173 2.37e-06

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: 48.90  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  27 RADGDLTLLWAEWQGRRPEWELTDM--------------VVWVTGASSGIGEELA-YQLSKLGVSLVLSARRVHELERVK 91
Cdd:cd08953  168 AAPGAAEVRYRDGLRYVQTLEPLPLpagaaasaplkpggVYLVTGGAGGIGRALArALARRYGARLVLLGRSPLPPEEEW 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  92 -----RRCLENGnlkeKDILVLPLDLTDTGSHEAATKAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGT 166
Cdd:cd08953  248 kaqtlAALEALG----ARVLYISADVTDAAAVRRLLEKVRERYGAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGL 323

                 ....*..
gi 649109145 167 VSLTKCV 173
Cdd:cd08953  324 LNLAQAL 330
PRK09186 PRK09186
flagellin modification protein A; Provisional
48-240 3.04e-06

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 47.68  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENgnLKEKDILVLPLDLTDTGSHEAATKAVLQ 127
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKE--FKSKKLSLVELDITDQESLEEFLSKSAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGRIDILVNNGGMSQRS---LCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGII--------- 195
Cdd:PRK09186  80 KYGKIDGAVNCAYPRNKDygkKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVapkfeiyeg 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 649109145 196 -SVPLSIGYCASKHALrgffNGLRTELATY---PGIIVSNICPGPVQSN 240
Cdd:PRK09186 160 tSMTSPVEYAAIKAGI----IHLTKYLAKYfkdSNIRVNCVSPGGILDN 204
PRK12744 PRK12744
SDR family oxidoreductase;
47-236 3.94e-06

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 47.43  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  47 ELTDMVVWVTGASSGIGEELAYQLSKLGVSLVL----SARRVHELERVKRRCLENGnlkeKDILVLPLDLTDTGSHEAAT 122
Cdd:PRK12744   5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynSAASKADAEETVAAVKAAG----AKAVAFQADLTTAAAVEKLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 123 KAVLQEFGRIDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVT-VNSILGIISvPLSI 201
Cdd:PRK12744  81 DDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL--NDNGKIVTlVTSLLGAFT-PFYS 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 202 GYCASKHALRGFFNGLRTELATYpGIIVSNICPGP 236
Cdd:PRK12744 158 AYAGSKAPVEHFTRAASKEFGAR-GISVTAVGPGP 191
PRK08177 PRK08177
SDR family oxidoreductase;
55-258 4.53e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 46.95  E-value: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHelervkrrclENGNLKEKDIL-VLPLDLTDTGSHEAATKAVLQEfgRID 133
Cdd:PRK08177   6 IIGASRGLGLGLVDRLLERGWQVTATVRGPQ----------QDTALQALPGVhIEKLDMNDPASLDQLLQRLQGQ--RFD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNNGGMS--QRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHmIERKQGKIVTVNSILGIISVPLSIG---YCASKH 208
Cdd:PRK08177  74 LLFVNAGISgpAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQ-VRPGQGVLAFMSSQLGSVELPDGGEmplYKASKA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 649109145 209 ALRGFFNGLRTELATyPGIIVSNICPGPVQSNI--------VENSLAG---EVTKTIGNNG 258
Cdd:PRK08177 153 ALNSMTRSFVAELGE-PTLTVLSMHPGWVKTDMggdnapldVETSVKGlveQIEAASGKGG 212
PRK07576 PRK07576
short chain dehydrogenase; Provisional
53-237 7.03e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 46.87  E-value: 7.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELER-VKRRCLENGNlkekdILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK07576  12 VVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAaVAQLQQAGPE-----GLGVSADVRDYAAVEAAFAQIADEFGP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 132 IDILVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMiERKQGKIVTVNSILGIISVPLSIGYCASKHALr 211
Cdd:PRK07576  87 IDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLL-RRPGASIIQISAPQAFVPMPMQAHVCAAKAGV- 164
                        170       180
                 ....*....|....*....|....*....
gi 649109145 212 gffNGLRTELAT---YPGIIVSNICPGPV 237
Cdd:PRK07576 165 ---DMLTRTLALewgPEGIRVNSIVPGPI 190
PRK05599 PRK05599
SDR family oxidoreductase;
51-302 9.97e-06

SDR family oxidoreductase;


Pssm-ID: 235527 [Multi-domain]  Cd Length: 246  Bit Score: 46.03  E-value: 9.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  51 MVVWVTGASSGIGEELAYQLSKlGVSLVLSARRVHELERVKRRCLENGnlkEKDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:PRK05599   1 MSILILGGTSDIAGEIATLLCH-GEDVVLAARRPEAAQGLASDLRQRG---ATSVHVLSFDAQDLDTHRELVKQTQELAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 131 RIDILVNNGGM--SQRSLCMDTSLDVyrKLIELNYLGTVS-LTkcVLPHMIERK--QGKIVTVNSILGIISVPLSIGYCA 205
Cdd:PRK05599  77 EISLAVVAFGIlgDQERAETDEAHAV--EIATVDYTAQVSmLT--VLADELRAQtaPAAIVAFSSIAGWRARRANYVYGS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 206 SKHALRGFFNGLRTEL--------ATYPGIIVSNICPG--PVQSNIVENSLAGEVTKTIgNNGDQSHKMTTSRCVRLMli 275
Cdd:PRK05599 153 TKAGLDAFCQGLADSLhgshvrliIARPGFVIGSMTTGmkPAPMSVYPRDVAAAVVSAI-TSSKRSTTLWIPGRLRVL-- 229
                        250       260
                 ....*....|....*....|....*..
gi 649109145 276 smandlkeVWISEqpfLLVTYLWQYMP 302
Cdd:PRK05599 230 --------AWIMR---LVPRPIWRKMP 245
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
119-239 1.26e-05

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 46.03  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 119 EAATKAVLQEFGRIDILVNNGGMSQRSLCMD-TSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISV 197
Cdd:cd05361   60 EELVDAVLQAGGAIDVLVSNDYIPRPMNPIDgTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPL 139
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 649109145 198 PLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQS 239
Cdd:cd05361  140 AYNSLYGPARAAAVALAESLAKELSRD-NILVYAIGPNFFNS 180
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
48-131 1.66e-05

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


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 46.22  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  48 LTDMVVWVTGASSGIGEELAYQLSKLGV-SLVLSARRVHELERVKR-RCLENGNLkekDILVLPLDLTDtgshEAATKAV 125
Cdd:cd05274  148 GLDGTYLITGGLGGLGLLVARWLAARGArHLVLLSRRGPAPRAAARaALLRAGGA---RVSVVRCDVTD----PAALAAL 220

                 ....*.
gi 649109145 126 LQEFGR 131
Cdd:cd05274  221 LAELAA 226
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
53-235 3.27e-05

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 44.75  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekdILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:PRK05786   8 VAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYGN-----IHYVVGDVSSTESARNVIEKAAKVLNAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DIL-VNNGGMSQRSLCMDTSLDvyrKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISV-PLSIGYCASKHAL 210
Cdd:PRK05786  83 DGLvVTVGGYVEDTVEEFSGLE---EMLTNHIKIPLYAVNASLRFL--KEGSSIVLVSSMSGIYKAsPDQLSYAVAKAGL 157
                        170       180
                 ....*....|....*....|....*
gi 649109145 211 RGFFNGLRTELATYpGIIVSNICPG 235
Cdd:PRK05786 158 AKAVEILASELLGR-GIRVNGIAPT 181
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
111-193 7.60e-05

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 43.45  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 111 DLTDTGSHEAATKAVLqefGRIDILVNNGGMSQRSlcmdTSLDVYRklieLNYLGTVSLTKCVLPHMieRKQGKIVTVNS 190
Cdd:PRK12428  31 DLGDPASIDAAVAALP---GRIDALFNIAGVPGTA----PVELVAR----VNFLGLRHLTEALLPRM--APGGAIVNVAS 97

                 ...
gi 649109145 191 ILG 193
Cdd:PRK12428  98 LAG 100
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
53-218 8.63e-05

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: 43.66  E-value: 8.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRvhELERVKRRCLENGnLKEKDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:cd09810    4 VVITGASSGLGLAAAKALARRGEWHVVMACR--DFLKAEQAAQEVG-MPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 133 DILVNNGGMSQRSLCMDT-SLDVYRKLIELNYLGTVSLTKCVLPHM--IERKQGKIVTVNSILGIISVPL-SIGYCASKH 208
Cdd:cd09810   81 DALVCNAAVYLPTAKEPRfTADGFELTVGVNHLGHFLLTNLLLEDLqrSENASPRIVIVGSITHNPNTLAgNVPPRATLG 160
                        170
                 ....*....|
gi 649109145 209 ALRGFFNGLR 218
Cdd:cd09810  161 DLEGLAGGLK 170
PRK07041 PRK07041
SDR family oxidoreductase;
55-249 9.36e-05

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 43.10  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNLKekdilVLPLDLTDtgshEAATKAVLQEFGRIDI 134
Cdd:PRK07041   2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVR-----TAALDITD----EAAVDAFFAEAGPFDH 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 135 LVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCvlPHMIERkqGKIVTVNSILGIISVPLSIGYCASKHALRGFF 214
Cdd:PRK07041  73 VVITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARA--ARIAPG--GSLTFVSGFAAVRPSASGVLQGAINAALEALA 148
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 649109145 215 NGLRTELAtyPgIIVSNICPGPVQSNIVeNSLAGE 249
Cdd:PRK07041 149 RGLALELA--P-VRVNTVSPGLVDTPLW-SKLAGD 179
PRK07023 PRK07023
SDR family oxidoreductase;
50-228 1.92e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 42.31  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  50 DMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVH-ELERVKRRCLENGNlkekdilvlpLDLTDTGSHEA-ATKAVLQ 127
Cdd:PRK07023   1 AVRAIVTGHSRGLGAALAEQLLQPGIAVLGVARSRHpSLAAAAGERLAEVE----------LDLSDAAAAAAwLAGDLLA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 128 EFGR---IDILVNNGGMSQ-----RSLCMDTSLdvyrKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNSILGIISVP- 198
Cdd:PRK07023  71 AFVDgasRVLLINNAGTVEpigplATLDAAAIA----RAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAg 146
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 199 LSIgYCASKHALRGFF--------NGLRTeLATYPGII 228
Cdd:PRK07023 147 WSV-YCATKAALDHHAravaldanRALRI-VSLAPGVV 182
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
55-242 4.00e-04

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 41.03  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKlgvslvlsarRVHELERVKRrclengnlKEKDILVlplDLTDtgshEAATKAVLQEFGRIDI 134
Cdd:cd11731    3 VIGATGTIGLAVAQLLSA----------HGHEVITAGR--------SSGDYQV---DITD----EASIKALFEKVGHFDA 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 135 LVNNGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVNSILGIISVPLSIGYCASKHALRGFF 214
Cdd:cd11731   58 IVSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL--NDGGSITLTSGILAQRPIPGGAAAATVNGALEGFV 135
                        170       180
                 ....*....|....*....|....*...
gi 649109145 215 NGLRTELAtyPGIIVSNICPGPVQSNIV 242
Cdd:cd11731  136 RAAAIELP--RGIRINAVSPGVVEESLE 161
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
52-153 4.73e-04

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: 40.54  E-value: 4.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145    52 VVWVTGASSGIGEELAYQLSKLGV-SLVLSARRVHELERVKRRCLENGNLKEkDILVLPLDLTDTGSHEAATKAVLQEFG 130
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAELEAAGA-RVTVVACDVADRDALAAVLAAIPAVEG 80
                           90       100
                   ....*....|....*....|...
gi 649109145   131 RIDILVNNGGMSQRSLCMDTSLD 153
Cdd:smart00822  81 PLTGVIHAAGVLDDGVLASLTPE 103
PRK07791 PRK07791
short chain dehydrogenase; Provisional
52-140 5.74e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 41.20  E-value: 5.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVL----------------SARRVHELERVKRRCLENGNlkekdilvlplDLTDT 115
Cdd:PRK07791   8 VVIVTGAGGGIGRAHALAFAAEGARVVVndigvgldgsasggsaAQAVVDEIVAAGGEAVANGD-----------DIADW 76
                         90       100
                 ....*....|....*....|....*
gi 649109145 116 GSHEAATKAVLQEFGRIDILVNNGG 140
Cdd:PRK07791  77 DGAANLVDAAVETFGGLDVLVNNAG 101
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
50-190 6.13e-04

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 41.04  E-value: 6.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  50 DMVVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkEKDILVLPLDLTDTGSHEAATKAVLQEF 129
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEWH--KARVEAMTLDLASLRSVQRFAEAFKAKN 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 649109145 130 GRIDILVNNGGMSQRSLCMdtSLDVYRKLIELNYLGTVSLTKCVLPHMIERKQGKIVTVNS 190
Cdd:cd09809   79 SPLHVLVCNAAVFALPWTL--TEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSS 137
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
103-235 1.67e-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: 39.23  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 103 KDILVLPLDLtDTGSHEAATKAVLQEFGRIDILVN-NGGMSQRSLCMDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRK 181
Cdd:cd05334   41 ASIIVLDSDS-FTEQAKQVVASVARLSGKVDALICvAGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHL--LS 117
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 649109145 182 QGKIVTVNSILGIISVPLSIGYCASKHALRGFFNGLRTELA-TYPGIIVSNICPG 235
Cdd:cd05334  118 GGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENSgLPAGSTANAILPV 172
PRK08416 PRK08416
enoyl-ACP reductase;
55-240 2.12e-03

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 39.37  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASSGIGEELAYQLSKLGVSLVLSARRVHEL-ERVKRRCLENGNLKEKdilVLPLDLTDTGSHEAATKAVLQEFGRID 133
Cdd:PRK08416  13 ISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEaNKIAEDLEQKYGIKAK---AYPLNILEPETYKELFKKIDEDFDRVD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 134 ILVNNGGMSQRSLcmdtsLDVYRKLIELN-------YLGTVSLTKCVLPHMIERKQ----GKIVTVNSILGIISVPLSIG 202
Cdd:PRK08416  90 FFISNAIISGRAV-----VGGYTKFMRLKpkglnniYTATVNAFVVGAQEAAKRMEkvggGSIISLSSTGNLVYIENYAG 164
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 649109145 203 YCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSN 240
Cdd:PRK08416 165 HGTSKAAVETMVKYAATELGEK-NIRVNAVSGGPIDTD 201
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
53-141 3.26e-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: 38.63  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekdilVLPLDLTDTgsheAATKAVLQE---F 129
Cdd:cd08951   10 IFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAG-------VLIGDLSSL----AETRKLADQvnaI 78
                         90
                 ....*....|..
gi 649109145 130 GRIDILVNNGGM 141
Cdd:cd08951   79 GRFDAVIHNAGI 90
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
55-193 3.58e-03

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


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 38.33  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  55 VTGASS--GIGEELAYQLSKLGVSLVLSARRvhelERVKRRCLENGNLKEKDILVLPLDLTDTGSHEAATKAVLQEFGRI 132
Cdd:cd05372    6 ITGIANdrSIAWGIAKALHEAGAELAFTYQP----EALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 649109145 133 DILVNNGGMSQRSLC----MDTSLDVYRKLIELNYLGTVSLTKCVLPHMieRKQGKIVTVnSILG 193
Cdd:cd05372   82 DGLVHSIAFAPKVQLkgpfLDTSRKGFLKALDISAYSLVSLAKAALPIM--NPGGSIVTL-SYLG 143
PRK08862 PRK08862
SDR family oxidoreductase;
52-138 4.54e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 38.17  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  52 VVWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLENGNlkekDILVLPLDLTDTGSHEAATKAVLQEFGR 131
Cdd:PRK08862   7 IILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTD----NVYSFQLKDFSQESIRHLFDAIEQQFNR 82

                 ....*...
gi 649109145 132 -IDILVNN 138
Cdd:PRK08862  83 aPDVLVNN 90
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
53-140 5.16e-03

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 38.05  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145  53 VWVTGASSGIGEELAYQLSKLGVSLVLSARRVHELERVKRRCLEngnlKEKDILVLPLDLTDTGSHEAATKAvLQEFGR- 131
Cdd:COG5748    9 VIITGASSGVGLYAAKALADRGWHVIMACRDLEKAEAAAQELGI----PPDSYTIIHIDLASLESVRRFVAD-FRALGRp 83

                 ....*....
gi 649109145 132 IDILVNNGG 140
Cdd:COG5748   84 LDALVCNAA 92
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
103-240 5.21e-03

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 38.15  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 103 KDILVLPLDLTDTGSHEAATKAVLQEfGRIDILVNNGGM--SQRSLCMDTSLDVyrKLIELNYLGTVSLTKCVLPHMIER 180
Cdd:PRK07904  60 SSVEVIDFDALDTDSHPKVIDAAFAG-GDVDVAIVAFGLlgDAEELWQNQRKAV--QIAEINYTAAVSVGVLLGEKMRAQ 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 649109145 181 KQGKIVTVNSILGIISVPLSIGYCASKHALRGFFNGLRTELATYpGIIVSNICPGPVQSN 240
Cdd:PRK07904 137 GFGQIIAMSSVAGERVRRSNFVYGSTKAGLDGFYLGLGEALREY-GVRVLVVRPGQVRTR 195
 
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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