NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|30684202|ref|NP_850131|]
View 

NAD-dependent epimerase/dehydratase family protein [Arabidopsis thaliana]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

 Zoom to residue level

show extra options Â»

Show site features     Horizontal zoom: Ã—

List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
4-254 3.23e-145

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05329:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 251  Bit Score: 406.45  E-value: 3.23e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   4 RWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQ 83
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  84 FDGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQ 240
                       250
                ....*....|.
gi 30684202 244 TICVDGGLTVN 254
Cdd:cd05329 241 IIAVDGGLTAN 251
 
Name Accession Description Interval E-value
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
4-254 3.23e-145

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: 406.45  E-value: 3.23e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   4 RWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQ 83
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  84 FDGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQ 240
                       250
                ....*....|.
gi 30684202 244 TICVDGGLTVN 254
Cdd:cd05329 241 IIAVDGGLTAN 251
PRK09242 PRK09242
SDR family oxidoreductase;
1-256 3.34e-97

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 285.10  E-value: 3.34e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEW--EKKGFQVSGSVCDVASRPEREELMQ 78
Cdd:PRK09242   1 TQHRWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeEFPEREVHGLAADVSDDEDRRAILD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   79 TVSSQFDGkLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSI 158
Cdd:PRK09242  81 WVEDHWDG-LHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAAS 238
Cdd:PRK09242 160 YGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAAS 239
                        250
                 ....*....|....*...
gi 30684202  239 YITGQTICVDGGLTVNGF 256
Cdd:PRK09242 240 YITGQCIAVDGGFLRYGF 257
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-253 5.47e-91

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: 268.96  E-value: 5.47e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:COG1028  82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:COG1028 162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVL 241

                ....*...
gi 30684202 246 CVDGGLTV 253
Cdd:COG1028 242 AVDGGLTA 249
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
19-252 7.71e-67

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: 207.28  E-value: 7.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    19 SGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSgsVCDVASRPEREELMQTVSSQFdGKLNILVSNVGVI 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVL--PCDVTDEEQVEALVAAAVEKF-GRLDILVNNAGFA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    99 R--SKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAGVISFDAGSIYGLTKGALIQLAKNLACE 176
Cdd:pfam13561  83 PklKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGG--SIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30684202   177 WAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGGLT 252
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
11-254 1.72e-50

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 166.09  E-value: 1.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:TIGR02415   2 VALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKF-GGFDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGY-GSIIFVSSIAGVISFDAGSIYGLTKGALIQL 169
Cdd:TIGR02415  81 MVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASIAGHEGNPILSAYSSTKFAVRGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   170 AKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVS---------FKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:TIGR02415 161 TQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEETSeiagkpigeGFEEFSSEIALGRPSEPEDVAGLVSFLASEDSDYI 240
                         250
                  ....*....|....
gi 30684202   241 TGQTICVDGGLTVN 254
Cdd:TIGR02415 241 TGQSILVDGGMVYN 254
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
11-151 3.14e-09

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: 54.80  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202     11 TALVTGGASGIGYAIVEELAGFGARiHVC-----DISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGAR-RLVllsrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVE- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30684202     86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPL-LKAsgygsIIFVSSIAGVI 151
Cdd:smart00822  80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLpLDF-----FVLFSSIAGVL 141
 
Name Accession Description Interval E-value
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
4-254 3.23e-145

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: 406.45  E-value: 3.23e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   4 RWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQ 83
Cdd:cd05329   1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  84 FDGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:cd05329  81 FGGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:cd05329 161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPVIQQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQ 240
                       250
                ....*....|.
gi 30684202 244 TICVDGGLTVN 254
Cdd:cd05329 241 IIAVDGGLTAN 251
PRK09242 PRK09242
SDR family oxidoreductase;
1-256 3.34e-97

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 285.10  E-value: 3.34e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEW--EKKGFQVSGSVCDVASRPEREELMQ 78
Cdd:PRK09242   1 TQHRWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeEFPEREVHGLAADVSDDEDRRAILD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   79 TVSSQFDGkLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSI 158
Cdd:PRK09242  81 WVEDHWDG-LHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAAS 238
Cdd:PRK09242 160 YGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSGPLSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAAS 239
                        250
                 ....*....|....*...
gi 30684202  239 YITGQTICVDGGLTVNGF 256
Cdd:PRK09242 240 YITGQCIAVDGGFLRYGF 257
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
6-253 5.47e-91

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: 268.96  E-value: 5.47e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:COG1028  82 GRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYAASKAA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:COG1028 162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVL 241

                ....*...
gi 30684202 246 CVDGGLTV 253
Cdd:COG1028 242 AVDGGLTA 249
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
12-248 6.51e-74

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: 225.24  E-value: 6.51e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLnQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNIL 91
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEAL-AELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEF-GRLDIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  92 VSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLAK 171
Cdd:cd05233  79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30684202 172 NLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKaLLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVD 248
Cdd:cd05233 159 SLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKE-LAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
6-251 5.68e-73

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 223.11  E-value: 5.68e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAF- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK05653  81 GALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYSAAKAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVsfKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:PRK05653 161 VIGFTKALALELASRGITVNAVAPGFIDTDMTEGLPEEV--KAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVI 238

                 ....*.
gi 30684202  246 CVDGGL 251
Cdd:PRK05653 239 PVNGGM 244
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
19-252 7.71e-67

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: 207.28  E-value: 7.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    19 SGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSgsVCDVASRPEREELMQTVSSQFdGKLNILVSNVGVI 98
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEELGAAVL--PCDVTDEEQVEALVAAAVEKF-GRLDILVNNAGFA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    99 R--SKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAGVISFDAGSIYGLTKGALIQLAKNLACE 176
Cdd:pfam13561  83 PklKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGG--SIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30684202   177 WAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGGLT 252
Cdd:pfam13561 161 LGPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGYT 236
FabG-like PRK07231
SDR family oxidoreductase;
7-254 7.98e-67

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 207.76  E-value: 7.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK07231   3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERF-G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVI-RSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK07231  81 SVDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSF--KKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMGEPTPenRAKFLATIPLGRLGTPEDIANAALFLASDEASWITGV 240
                        250
                 ....*....|.
gi 30684202  244 TICVDGGLTVN 254
Cdd:PRK07231 241 TLVVDGGRCVG 251
PRK12826 PRK12826
SDR family oxidoreductase;
6-254 2.11e-66

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 206.69  E-value: 2.11e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDF- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSI-YGLTKG 164
Cdd:PRK12826  82 GRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYPGLAhYAASKA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFkKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQT 244
Cdd:PRK12826 162 GLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWA-EAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQT 240
                        250
                 ....*....|
gi 30684202  245 ICVDGGLTVN 254
Cdd:PRK12826 241 LPVDGGATLP 250
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-253 3.75e-63

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 198.14  E-value: 3.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHV-CDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK05565   3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIaYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKF- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK05565  82 GKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYSASKGA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVsfKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:PRK05565 162 VNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSSFSEED--KEGLAEEIPLGRLGKPEEIAKVVLFLASDDASYITGQII 239

                 ....*...
gi 30684202  246 CVDGGLTV 253
Cdd:PRK05565 240 TVDGGWTC 247
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-253 1.79e-62

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 196.63  E-value: 1.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHV-CDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK12825   3 SLMGRVALVTGAARGLGRAIALRLARAGADVVVhYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK12825  83 -GRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAAKA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKalLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQT 244
Cdd:PRK12825 162 GLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAK--DAETPLGRSGTPEDIARAVAFLCSDASDYITGQV 239

                 ....*....
gi 30684202  245 ICVDGGLTV 253
Cdd:PRK12825 240 IEVTGGVDV 248
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
6-253 2.00e-61

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: 193.73  E-value: 2.00e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDF- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:cd05347  81 GKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYAASKGG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:cd05347 161 VAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVVADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQII 240

                ....*...
gi 30684202 246 CVDGGLTV 253
Cdd:cd05347 241 FVDGGWLA 248
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
11-252 3.40e-61

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: 192.76  E-value: 3.40e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd05333   2 VALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEF-GPVDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKAsGYGSIIFVSSIAGVIsfdaGSI----YGLTKGA 165
Cdd:cd05333  81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQaVIRAMIKR-RSGRIINISSVVGLI----GNPgqanYAASKAG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVsfKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:cd05333 156 VIGFTKSLAKELASRGITVNAVAPGFIDTDMTDALPEKV--KEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVL 233

                ....*..
gi 30684202 246 CVDGGLT 252
Cdd:cd05333 234 HVNGGMY 240
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
6-254 1.11e-60

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 191.95  E-value: 1.11e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHV-CDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK05557   2 SLEGKVALVTGASRGIGRAIAERLAAQGANVVInYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKaSGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:PRK05557  82 -GGVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKaVARPMMK-QRSGRIINISSVVGLMGNPGQANYAASK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVsfKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:PRK05557 160 AGVIGFTKSLARELASRGITVNAVAPGFIETDMTDALPEDV--KEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITGQ 237
                        250
                 ....*....|.
gi 30684202  244 TICVDGGLTVN 254
Cdd:PRK05557 238 TLHVNGGMVMG 248
PRK12829 PRK12829
short chain dehydrogenase; Provisional
1-251 1.74e-60

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 191.81  E-value: 1.74e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEkkGFQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK12829   3 IDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLP--GAKVTATVADVADPAQVERVFDTA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFDGkLNILVSNVGV-IRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYG-SIIFVSSIAGVISFDAGSI 158
Cdd:PRK12829  81 VERFGG-LDVLVNNAGIaGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGgVIIALSSVAGRLGYPGRTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLED---------VSFKKALLSRTPLGRVGEPNEVASLV 229
Cdd:PRK12829 160 YAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRVIEAraqqlgiglDEMEQEYLEKISLGRMVEPEDIAATA 239
                        250       260
                 ....*....|....*....|..
gi 30684202  230 AFLCLPAASYITGQTICVDGGL 251
Cdd:PRK12829 240 LFLASPAARYITGQAISVDGNV 261
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
9-252 8.85e-59

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: 187.10  E-value: 8.85e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKL 88
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAF-GRV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQ 168
Cdd:cd05344  80 DILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAGLIG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 169 LAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDV---------SFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:cd05344 160 LVKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARaekegisveEAEKEVASQIPLGRVGKPEELAALIAFLASEKASY 239
                       250
                ....*....|...
gi 30684202 240 ITGQTICVDGGLT 252
Cdd:cd05344 240 ITGQAILVDGGLT 252
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
6-253 1.01e-58

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: 187.15  E-value: 1.01e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKK-GFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:cd05352   5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKyGVKTKAYKCDVSSQESVEKTFKQIQKDF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAG--SIYGLT 162
Cdd:cd05352  85 -GKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNRPQpqAAYNAS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 163 KGALIQLAKNLACEWAKDGIRANAVAPNVINTPLsqSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:cd05352 164 KAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL--TDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSYTTG 241
                       250
                ....*....|.
gi 30684202 243 QTICVDGGLTV 253
Cdd:cd05352 242 SDLIIDGGYTC 252
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
11-204 6.99e-55

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 175.11  E-value: 6.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERL-GRLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    91 LVSNVGVIRSKPTTEYTEDDF--AFHIssNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQ 168
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWerVIDV--NLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIG 158
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 30684202   169 LAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDV 204
Cdd:pfam00106 159 FTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDE 194
PRK06124 PRK06124
SDR family oxidoreductase;
4-253 1.37e-54

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 176.44  E-value: 1.37e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    4 RWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQ 83
Cdd:PRK06124   6 RFSLAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   84 FdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:PRK06124  86 H-GRLDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:PRK06124 165 QGLTGLMRALAAEFGPHGITSNAIAPGYFATETNAAMAADPAVGPWLAQRTPLGRWGRPEEIAGAAVFLASPAASYVNGH 244
                        250
                 ....*....|
gi 30684202  244 TICVDGGLTV 253
Cdd:PRK06124 245 VLAVDGGYSV 254
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
12-250 2.12e-53

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: 173.14  E-value: 2.12e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNIL 91
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQF-GGITIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  92 VSNVGVIRSKP-TTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:cd05365  81 VNNAGGGGPKPfDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 171 KNLACEWAKDGIRANAVAPNVINTPLSQSYLEDvSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGG 250
Cdd:cd05365 161 RNLAFDLGPKGIRVNAVAPGAVKTDALASVLTP-EIERAMLKHTPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVSGG 239
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
12-253 8.74e-53

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: 171.38  E-value: 8.74e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSL-SEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVaAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERF-GRLDV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:cd05359  80 LVSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 171 KNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGG 250
Cdd:cd05359 160 RYLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDGG 239

                ...
gi 30684202 251 LTV 253
Cdd:cd05359 240 LSI 242
PRK12939 PRK12939
short chain dehydrogenase; Provisional
6-254 8.76e-53

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 171.69  E-value: 8.76e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK12939   4 NLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAAL- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK12939  83 GGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQsYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:PRK12939 163 VIGMTRSLARELGGRGITVNAIAPGLTATEATA-YVPADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLL 241

                 ....*....
gi 30684202  246 CVDGGLTVN 254
Cdd:PRK12939 242 PVNGGFVMN 250
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
7-254 1.11e-52

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 171.61  E-value: 1.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETF-G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK12429  81 GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  167 IQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVS----------FKKALLSRTPLGRVGEPNEVASLVAFLCLPA 236
Cdd:PRK12429 161 IGLTKVVALEGATHGVTVNAICPGYVDTPLVRKQIPDLAkergiseeevLEDVLLPLVPQKRFTTVEEIADYALFLASFA 240
                        250
                 ....*....|....*...
gi 30684202  237 ASYITGQTICVDGGLTVN 254
Cdd:PRK12429 241 AKGVTGQAWVVDGGWTAQ 258
PRK12827 PRK12827
short chain dehydrogenase; Provisional
5-251 1.56e-51

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 168.36  E-value: 1.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDI----SEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK12827   2 ASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIhpmrGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKASGYGSIIFVSSIAGVISFDAGSIY 159
Cdd:PRK12827  82 VEEF-GRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQaALPPMIRARRGGRIVNIASVAGVRGNRGQVNY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLsqsyLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM----ADNAAPTEHLLNPVPVQRLGEPDEVAALVAFLVSDAASY 236
                        250
                 ....*....|..
gi 30684202  240 ITGQTICVDGGL 251
Cdd:PRK12827 237 VTGQVIPVDGGF 248
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
7-252 2.75e-51

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: 167.95  E-value: 2.75e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEA-KLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEdAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ--LSHpLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:cd05358  80 GTLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAReaIKR-FRKSKIKGKIINMSSVHEKIPWPGHVNYAASK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:cd05358 159 GGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQRADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGT 238

                ....*....
gi 30684202 244 TICVDGGLT 252
Cdd:cd05358 239 TLFVDGGMT 247
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
7-253 5.86e-51

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 167.43  E-value: 5.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK08213  10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERF-G 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKASGYGSIIFVSSIAGVISFDAGSI----YGL 161
Cdd:PRK08213  89 HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQaVAKRSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYNT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVsfKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYIT 241
Cdd:PRK08213 169 SKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERL--GEDLLAHTPLGRLGDDEDLKGAALLLASDASKHIT 246
                        250
                 ....*....|..
gi 30684202  242 GQTICVDGGLTV 253
Cdd:PRK08213 247 GQILAVDGGVSA 258
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
11-254 1.72e-50

acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is described as able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also called capable of irreversible reduction of diacetyl with NADH to acetoin. Blomqvist, et al. decline to specify either EC 1.1.1.4 which is (R,R)-butanediol dehydrogenase, or EC 1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry, for this enzyme. This enzyme is a homotetramer in the family of short chain dehydrogenases (pfam00106). Another member of this family, from Corynebacterium glutamicum, is called L-2,3-butanediol dehydrogenase (). [Energy metabolism, Fermentation]


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 166.09  E-value: 1.72e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:TIGR02415   2 VALVTGGAQGIGKGIAERLAKDGFAVAVADLNEETAKETAKEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKF-GGFDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGY-GSIIFVSSIAGVISFDAGSIYGLTKGALIQL 169
Cdd:TIGR02415  81 MVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHgGKIINAASIAGHEGNPILSAYSSTKFAVRGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   170 AKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVS---------FKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:TIGR02415 161 TQTAAQELAPKGITVNAYCPGIVKTPMWEEIDEETSeiagkpigeGFEEFSSEIALGRPSEPEDVAGLVSFLASEDSDYI 240
                         250
                  ....*....|....
gi 30684202   241 TGQTICVDGGLTVN 254
Cdd:TIGR02415 241 TGQSILVDGGMVYN 254
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
1-260 1.91e-49

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 163.69  E-value: 1.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK07097   2 SENLFSLKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYG 160
Cdd:PRK07097  82 EKEV-GVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTP------LSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCL 234
Cdd:PRK07097 161 AAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATPqtaplrELQADGSRHPFDQFIIAKTPAARWGDPEDLAGPAVFLAS 240
                        250       260
                 ....*....|....*....|....*.
gi 30684202  235 PAASYITGQTICVDGGLTVNgFSYQP 260
Cdd:PRK07097 241 DASNFVNGHILYVDGGILAY-IGKQP 265
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
1-250 5.17e-49

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: 162.33  E-value: 5.17e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTV 80
Cdd:cd08936   2 VTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  81 SSQFdGKLNILVSNVGVirsKP----TTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAG 156
Cdd:cd08936  82 VNLH-GGVDILVSNAAV---NPffgnILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAAFHPFPGL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 157 SIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPA 236
Cdd:cd08936 158 GPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALWMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSED 237
                       250
                ....*....|....
gi 30684202 237 ASYITGQTICVDGG 250
Cdd:cd08936 238 ASYITGETVVVGGG 251
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
7-253 1.39e-48

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 161.51  E-value: 1.39e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEaKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISP-EIEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKE-G 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSI-YGLTKGA 165
Cdd:PRK08226  82 RIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVADPGETaYALTKAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLS-----QSYLEDV-SFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK08226 162 IVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAesiarQSNPEDPeSVLTEMAKAIPLRRLADPLEVGELAAFLASDESSY 241
                        250
                 ....*....|....
gi 30684202  240 ITGQTICVDGGLTV 253
Cdd:PRK08226 242 LTGTQNVIDGGSTL 255
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
11-254 7.24e-48

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: 159.46  E-value: 7.24e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDI-SEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLN 89
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAADGFNIVLADLnLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKF-GSFD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  90 ILVSNVGVIRSKPTTEYTEDDFAFHISSNV--------EAAYHFSQLSHPllkasgyGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:cd05366  83 VMVNNAGIAPITPLLTITEEDLKKVYAVNVfgvlfgiqAAARQFKKLGHG-------GKIINASSIAGVQGFPNLGAYSA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVS---------FKKALLSRTPLGRVGEPNEVASLVAFL 232
Cdd:cd05366 156 SKFAVRGLTQTAAQELAPKGITVNAYAPGIVKTEMWDYIDEEVGeiagkpegeGFAEFSSSIPLGRLSEPEDVAGLVSFL 235
                       250       260
                ....*....|....*....|..
gi 30684202 233 CLPAASYITGQTICVDGGLTVN 254
Cdd:cd05366 236 ASEDSDYITGQTILVDGGMVYR 257
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
7-250 7.43e-48

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 159.24  E-value: 7.43e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK06113   9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKL-G 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTtEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK06113  88 KVDILVNNAGGGGPKPF-DMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  167 IQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDvSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTIC 246
Cdd:PRK06113 167 SHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITP-EIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILT 245

                 ....
gi 30684202  247 VDGG 250
Cdd:PRK06113 246 VSGG 249
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-253 2.00e-47

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 158.36  E-value: 2.00e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDiSEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITT-HGTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEF- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIfvsSIAGVISFDAGSI---YGLT 162
Cdd:PRK06935  90 GKIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKII---NIASMLSFQGGKFvpaYTAS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  163 KGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:PRK06935 167 KHGVAGLTKAFANELAAYNIQVNAIAPGYIKTANTAPIRADKNRNDEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNG 246
                        250
                 ....*....|.
gi 30684202  243 QTICVDGGLTV 253
Cdd:PRK06935 247 HILAVDGGWLV 257
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
6-245 3.98e-47

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: 156.88  E-value: 3.98e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWekkGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEF- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:COG4221  78 GRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYL--EDVSFKKALLSRTPLgrvgEPNEVASLVAFLC-LPAASYITG 242
Cdd:COG4221 158 VRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFdgDAEAAAAVYEGLEPL----TPEDVAEAVLFALtQPAHVNVNE 233

                ...
gi 30684202 243 QTI 245
Cdd:COG4221 234 LVL 236
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
6-196 7.64e-47

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 156.57  E-value: 7.64e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARF- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:COG0300  81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAA 160
                       170       180       190
                ....*....|....*....|....*....|.
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPL 196
Cdd:COG0300 161 LEGFSESLRAELAPTGVRVTAVCPGPVDTPF 191
PRK06172 PRK06172
SDR family oxidoreductase;
7-252 1.00e-46

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 156.45  E-value: 1.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK06172   5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAY-G 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGV-IRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK06172  84 RLDYAFNNAGIeIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASKHA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRT-PLGRVGEPNEVASLVAFLCLPAASYITGQT 244
Cdd:PRK06172 164 VIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEADPRKAEFAAAMhPVGRIGKVEEVASAVLYLCSDGASFTTGHA 243

                 ....*...
gi 30684202  245 ICVDGGLT 252
Cdd:PRK06172 244 LMVDGGAT 251
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
6-254 1.11e-46

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: 156.00  E-value: 1.11e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEA---KLNQSLSEwEKKGFQVsgsvcDVASRPEREELMQTVSS 82
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEegqAAAAELGD-AARFFHL-----DVTDEDGWTAVVDTARE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  83 QFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLT 162
Cdd:cd05341  76 AF-GRLDVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNAS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 163 KGALIQLAKNLACEWAK--DGIRANAVAPNVINTPLSQSYLEDVSfKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:cd05341 155 KGAVRGLTKSAALECATqgYGIRVNSVHPGYIYTPMTDELLIAQG-EMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFV 233
                       250
                ....*....|....
gi 30684202 241 TGQTICVDGGLTVN 254
Cdd:cd05341 234 TGSELVVDGGYTAG 247
PRK06484 PRK06484
short chain dehydrogenase; Validated
8-255 2.42e-46

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 161.94  E-value: 2.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    8 KGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQslsEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGK 87
Cdd:PRK06484   4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARE---RADSLGPDHHALAMDVSDEAQIREGFEQLHREF-GR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   88 LNILVSNVGVI--RSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYG-SIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK06484  80 IDVLVNNAGVTdpTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGHGaAIVNVASGAGLVALPKRTAYSASKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTP----LSQSYLEDVSfkkALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:PRK06484 160 AVISLTRSLACEWAAKGIRVNAVLPGYVRTQmvaeLERAGKLDPS---AVRSRIPLGRLGRPEEIAEAVFFLASDQASYI 236
                        250
                 ....*....|....*
gi 30684202  241 TGQTICVDGGLTVNG 255
Cdd:PRK06484 237 TGSTLVVDGGWTVYG 251
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
11-254 4.50e-46

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 154.54  E-value: 4.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEaklNQSLSEW-EKKGF---QVSGSVCDVASRPEREELMQTVSsQFDG 86
Cdd:PRK12824   4 IALVTGAKRGIGSAIARELLNDGYRVIATYFSG---NDCAKDWfEEYGFtedQVRLKELDVTDTEECAEALAEIE-EEEG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK12824  80 PVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  167 IQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKAllSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTIC 246
Cdd:PRK12824 160 IGFTKALASEGARYGITVNCIAPGYIATPMVEQMGPEVLQSIV--NQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETIS 237

                 ....*...
gi 30684202  247 VDGGLTVN 254
Cdd:PRK12824 238 INGGLYMH 245
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
8-252 7.46e-46

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: 154.14  E-value: 7.46e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   8 KGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEW--EKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGlaAKHGVKVLYHGADLSKPAAIEDMVAYAQRQF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:cd08940  80 GGVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKA----------LLSRTPLGRVGEPNEVASLVAFLCLP 235
Cdd:cd08940 160 VVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKQISALAQKNGvpqeqaarelLLEKQPSKQFVTPEQLGDTAVFLASD 239
                       250
                ....*....|....*..
gi 30684202 236 AASYITGQTICVDGGLT 252
Cdd:cd08940 240 AASQITGTAVSVDGGWT 256
PRK06841 PRK06841
short chain dehydrogenase; Provisional
2-253 1.05e-45

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 153.66  E-value: 1.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    2 DKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISE--AKLNQSLSEWEKKGFqvsgsVCDVASRPEREELMQT 79
Cdd:PRK06841   8 DLAFDLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEdvAEVAAQLLGGNAKGL-----VCDVSDSQSVEAAVAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   80 VSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIY 159
Cdd:PRK06841  83 VISAF-GRIDILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSqsyledvsfKKA--------LLSRTPLGRVGEPNEVASLVAF 231
Cdd:PRK06841 162 CASKAGVVGMTKVLALEWGPYGITVNAISPTVVLTELG---------KKAwagekgerAKKLIPAGRFAYPEEIAAAALF 232
                        250       260
                 ....*....|....*....|..
gi 30684202  232 LCLPAASYITGQTICVDGGLTV 253
Cdd:PRK06841 233 LASDAAAMITGENLVIDGGYTI 254
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
5-253 2.31e-45

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: 152.54  E-value: 2.31e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSgsvCDVASRPEREELMQTVSSQF 84
Cdd:cd05345   1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQ---ADVTKRADVEAMVEAALSKF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  85 dGKLNILVSNVGVI-RSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:cd05345  78 -GRLDILVNNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYL-EDVSFKKA-LLSRTPLGRVGEPNEVASLVAFLCLPAASYIT 241
Cdd:cd05345 157 GWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMgEDTPENRAkFRATIPLGRLSTPDDIANAALYLASDEASFIT 236
                       250
                ....*....|..
gi 30684202 242 GQTICVDGGLTV 253
Cdd:cd05345 237 GVALEVDGGRCI 248
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
5-252 7.29e-45

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 151.70  E-value: 7.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    5 W-SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKL-NQSLSEWEkkgfqvsgsvCDVASRPEREELMQTVSS 82
Cdd:PRK06171   4 WlNLQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDGqHENYQFVP----------TDVSSAEEVNHTVAEIIE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   83 QFdGKLNILVSNVGV---------IRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISF 153
Cdd:PRK06171  74 KF-GRIDGLVNNAGIniprllvdeKDPAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEGS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  154 DAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVIN-TPL-SQSY-----------LEDVSFKKALLSRTPLGRVG 220
Cdd:PRK06171 153 EGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEaTGLrTPEYeealaytrgitVEQLRAGYTKTSTIPLGRSG 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 30684202  221 EPNEVASLVAFLCLPAASYITGQTICVDGGLT 252
Cdd:PRK06171 233 KLSEVADLVCYLLSDRASYITGVTTNIAGGKT 264
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
7-250 1.43e-44

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: 150.64  E-value: 1.43e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGF---QVSGSVCDVASRPEREELMQTVSSQ 83
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVsekKILLVVADLTEEEGQDRIISTTLAK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  84 FdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:cd05364  81 F-GRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYCISK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPL-SQSYLEDVSFKKaLLSRT----PLGRVGEPNEVASLVAFLCLPAAS 238
Cdd:cd05364 159 AALDQFTRCTALELAPKGVRVNSVSPGVIVTGFhRRMGMPEEQYIK-FLSRAkethPLGRPGTVDEVAEAIAFLASDASS 237
                       250
                ....*....|..
gi 30684202 239 YITGQTICVDGG 250
Cdd:cd05364 238 FITGQLLPVDGG 249
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
8-250 3.68e-44

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: 149.41  E-value: 3.68e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   8 KGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGF-QVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKnRVIALELDITSKESIKELIESYLEKF-G 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGvIRSK----PTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFD-------- 154
Cdd:cd08930  80 RIDILINNAY-PSPKvwgsRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGVIAPDfriyentq 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 155 --AGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPlsqsylEDVSFKKALLSRTPLGRVGEPNEVASLVAFL 232
Cdd:cd08930 159 mySPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGILNN------QPSEFLEKYTKKCPLKRMLNPEDLRGAIIFL 232
                       250
                ....*....|....*...
gi 30684202 233 CLPAASYITGQTICVDGG 250
Cdd:cd08930 233 LSDASSYVTGQNLVIDGG 250
PRK06138 PRK06138
SDR family oxidoreductase;
7-252 7.24e-44

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 148.76  E-value: 7.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK06138   3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGG-RAFARQGDVGSAEAVEALVDFVAARW-G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  167 IQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDV----SFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHadpeALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240
                        250
                 ....*....|
gi 30684202  243 QTICVDGGLT 252
Cdd:PRK06138 241 TTLVVDGGWL 250
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
7-252 1.02e-43

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: 148.19  E-value: 1.02e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSL-SEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVvAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:cd05362  80 GGVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGG--RIINISSSLTAAYTPNYGAYAGSKAA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPL--SQSYLEDVSFKKAllsRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:cd05362 158 VEAFTRVLAKELGGRGITVNAVAPGPVDTDMfyAGKTEEAVEGYAK---MSPLGRLGEPEDIAPVVAFLASPDGRWVNGQ 234

                ....*....
gi 30684202 244 TICVDGGLT 252
Cdd:cd05362 235 VIRANGGYV 243
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
8-253 2.29e-43

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: 147.23  E-value: 2.29e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   8 KGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSlseweKKGFQVSGSVCDVASRPEREELMQTVssqfdGK 87
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKEL-----ERGPGITTRVLDVTDKEQVAALAKEE-----GR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  88 LNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGS-IYGLTKGAL 166
Cdd:cd05368  71 IDVLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRfVYSTTKAAV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 167 IQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDV----SFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:cd05368 151 IGLTKSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQpdpeEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTG 230
                       250
                ....*....|.
gi 30684202 243 QTICVDGGLTV 253
Cdd:cd05368 231 TAVVIDGGWSL 241
PRK07814 PRK07814
SDR family oxidoreductase;
4-252 2.37e-43

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 148.00  E-value: 2.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    4 RWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQ 83
Cdd:PRK07814   5 RFRLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   84 FdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPL-LKASGYGSIIFVSSIAGVISFDAGSIYGLT 162
Cdd:PRK07814  85 F-GRLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLmLEHSGGGSVINISSTMGRLAGRGFAAYGTA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  163 KGALIQLAKNLACEWAKDgIRANAVAPNVINTplsqSYLEDVS----FKKALLSRTPLGRVGEPNEVASLVAFLCLPAAS 238
Cdd:PRK07814 164 KAALAHYTRLAALDLCPR-IRVNAIAPGSILT----SALEVVAandeLRAPMEKATPLRRLGDPEDIAAAAVYLASPAGS 238
                        250
                 ....*....|....
gi 30684202  239 YITGQTICVDGGLT 252
Cdd:PRK07814 239 YLTGKTLEVDGGLT 252
PRK09135 PRK09135
pteridine reductase; Provisional
6-254 6.12e-43

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 146.23  E-value: 6.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGAR--IHvCDISEAKLNQSLSEWEKkgfQVSGSVC----DVASRPEREELMQT 79
Cdd:PRK09135   3 TDSAKVALITGGARRIGAAIARTLHAAGYRvaIH-YHRSAAEADALAAELNA---LRPGSAAalqaDLLDPDALPELVAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   80 VSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIY 159
Cdd:PRK09135  79 CVAAF-GRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR-GAIVNITDIHAERPLKGYPVY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDgIRANAVAPNVINTPLSQSYLEDVSfKKALLSRTPLGRVGEPNEVASLVAFLcLPAASY 239
Cdd:PRK09135 157 CAAKAALEMLTRSLALELAPE-VRVNAVAPGAILWPEDGNSFDEEA-RQAILARTPLKRIGTPEDIAEAVRFL-LADASF 233
                        250
                 ....*....|....*
gi 30684202  240 ITGQTICVDGGLTVN 254
Cdd:PRK09135 234 ITGQILAVDGGRSLT 248
PRK06500 PRK06500
SDR family oxidoreductase;
7-250 7.36e-43

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 146.25  E-value: 7.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRperEELMQTVSSQFdG 86
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQ---KALAQALAEAF-G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLkASGyGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK06500  80 RLDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLL-ANP-ASIVLNGSINAHIGMPNSSVYAASKAAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  167 IQLAKNLACEWAKDGIRANAVAPNVINTPL------SQSYLEDVSfkKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:PRK06500 158 LSLAKTLSGELLPRGIRVNAVSPGPVQTPLygklglPEATLDAVA--AQIQALVPLGRFGTPEEIAKAVLYLASDESAFI 235
                        250
                 ....*....|
gi 30684202  241 TGQTICVDGG 250
Cdd:PRK06500 236 VGSEIIVDGG 245
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
1-251 1.17e-42

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 153.85  E-value: 1.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK08324 414 MPKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFEEA 492
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFDGkLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASG-YGSIIFVSSIAGVisfDAG--- 156
Cdd:PRK08324 493 ALAFGG-VDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlGGSIVFIASKNAV---NPGpnf 568
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  157 SIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVIN------TP-----------LSQSYLEDVSFKKALLSRTPLgrv 219
Cdd:PRK08324 569 GAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAVVrgsgiwTGewiearaaaygLSEEELEEFYRARNLLKREVT--- 645
                        250       260       270
                 ....*....|....*....|....*....|..
gi 30684202  220 gePNEVASLVAFLCLPAASYITGQTICVDGGL 251
Cdd:PRK08324 646 --PEDVAEAVVFLASGLLSKTTGAIITVDGGN 675
PRK06484 PRK06484
short chain dehydrogenase; Validated
1-255 1.40e-42

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 151.93  E-value: 1.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDIS--EAKLNQSLSEWEKKGFQVsgsvcDVASRPEREELMQ 78
Cdd:PRK06484 261 APSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDaeGAKKLAEALGDEHLSVQA-----DITDEAAVESAFA 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   79 TVSSQFdGKLNILVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYHFSQLShpLLKASGYGSIIFVSSIAGVISFDAGS 157
Cdd:PRK06484 336 QIQARW-GRLDVLVNNAGIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAA--ARLMSQGGVIVNLGSIASLLALPPRN 412
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  158 IYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTP----LSQSYLEDVSfkkALLSRTPLGRVGEPNEVASLVAFLC 233
Cdd:PRK06484 413 AYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIETPavlaLKASGRADFD---SIRRRIPLGRLGDPEEVAEAIAFLA 489
                        250       260
                 ....*....|....*....|..
gi 30684202  234 LPAASYITGQTICVDGGLTVNG 255
Cdd:PRK06484 490 SPAASYVNGATLTVDGGWTAFG 511
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
7-250 3.23e-41

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: 141.96  E-value: 3.23e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGF-QVSGSVCDVasRPErEELMQTVSS--Q 83
Cdd:cd05369   1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGgRAHPIQCDV--RDP-EAVEAAVDEtlK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  84 FDGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHP-LLKASGYGSIIFVSSIAGVISFDAGSIYGLT 162
Cdd:cd05369  78 EFGKIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKrLIEAKHGGSILNISATYAYTGSPFQVHSAAA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 163 KGALIQLAKNLACEWAKDGIRANAVAPNVI-NTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYIT 241
Cdd:cd05369 158 KAGVDALTRSLAVEWGPYGIRVNAIAPGPIpTTEGMERLAPSGKSEKKMIERVPLGRLGTPEEIANLALFLLSDAASYIN 237

                ....*....
gi 30684202 242 GQTICVDGG 250
Cdd:cd05369 238 GTTLVVDGG 246
PRK08589 PRK08589
SDR family oxidoreductase;
7-251 3.98e-41

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 142.22  E-value: 3.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEaKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAE-AVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQF-G 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTT-EYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK08589  82 RVDVLFNNAGVDNAAGRIhEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQAADLYRSGYNAAKGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPL------SQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK08589 161 VINFTKSIAIEYGRDGIRANAIAPGTIETPLvdkltgTSEDEAGKTFRENQKWMTPLGRLGKPEEVAKLVVFLASDDSSF 240
                        250
                 ....*....|..
gi 30684202  240 ITGQTICVDGGL 251
Cdd:PRK08589 241 ITGETIRIDGGV 252
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
7-250 6.08e-41

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: 141.09  E-value: 6.08e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISeakLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADID---GGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEF-G 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRSKPTTEYTE-DDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:cd08944  77 GLDLLVNNAGAMHLTPAIIDTDlAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLED-----VSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:cd08944 157 IRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGfegalGPGGFHLLIHQLQGRLGRPEDVAAAVVFLLSDDASFI 236
                       250
                ....*....|
gi 30684202 241 TGQTICVDGG 250
Cdd:cd08944 237 TGQVLCVDGG 246
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-250 1.43e-40

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 140.30  E-value: 1.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHV---CDISEAKlnqslsEWEKKGFQVSGsvCDVASRPEREELMQTVSSQ 83
Cdd:PRK06463   5 FKGKVALITGGTRGIGRAIAEAFLREGAKVAVlynSAENEAK------ELREKGVFTIK--CDVGNRDQVKKSKEVVEKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   84 FdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGS-IYGLT 162
Cdd:PRK06463  77 F-GRVDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGTtFYAIT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  163 KGALIQLAKNLACEWAKDGIRANAVAPNVINTPLS---QSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK06463 156 KAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTlsgKSQEEAEKLRELFRNKTVLKTTGKPEDIANIVLFLASDDARY 235
                        250
                 ....*....|.
gi 30684202  240 ITGQTICVDGG 250
Cdd:PRK06463 236 ITGQVIVADGG 246
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
6-254 1.55e-40

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: 139.91  E-value: 1.55e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLnQSLSEwEKKGFQvsgSVC-DVASRPEREELMQTVssqf 84
Cdd:cd05351   4 DFAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADL-DSLVR-ECPGIE---PVCvDLSDWDATEEALGSV---- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGY-GSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:cd05351  75 -GPVDLLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQRALTNHTVYCSTK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:cd05351 154 AALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMLNRIPLGKFAEVEDVVNAILFLLSDKSSMTTGS 233
                       250
                ....*....|.
gi 30684202 244 TICVDGGLTVN 254
Cdd:cd05351 234 TLPVDGGFLAS 244
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
5-253 2.15e-40

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 139.90  E-value: 2.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK07523   6 FDLTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK07523  86 -GPIDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIAPYTATKG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQT 244
Cdd:PRK07523 165 AVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAALVADPEFSAWLEKRTPAGRWGKVEELVGACVFLASDASSFVNGHV 244

                 ....*....
gi 30684202  245 ICVDGGLTV 253
Cdd:PRK07523 245 LYVDGGITA 253
PRK07035 PRK07035
SDR family oxidoreductase;
6-253 4.52e-40

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 139.00  E-value: 4.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARihvCDISEAKLN--QSLSEW-EKKGFQVSGSVCDVASRPEREELMQTVSS 82
Cdd:PRK07035   5 DLTGKIALVTGASRGIGEAIAKLLAQQGAH---VIVSSRKLDgcQAVADAiVAAGGKAEALACHIGEMEQIDALFAHIRE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   83 QFdGKLNILVSNVGvirskpTTEY-----TEDDFAFH--ISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDA 155
Cdd:PRK07035  82 RH-GRLDILVNNAA------ANPYfghilDTDLGAFQktVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  156 GSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLP 235
Cdd:PRK07035 155 QGIYSITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKFASALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASD 234
                        250
                 ....*....|....*...
gi 30684202  236 AASYITGQTICVDGGLTV 253
Cdd:PRK07035 235 ASSYTTGECLNVDGGYLS 252
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
6-252 4.92e-40

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 139.26  E-value: 4.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERF- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHP-LLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK13394  83 GSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKhMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYL----------EDVSFKKALLSRTPLGRVGEPNEVASLVAFLCL 234
Cdd:PRK13394 163 GLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIpeqakelgisEEEVVKKVMLGKTVDGVFTTVEDVAQTVLFLSS 242
                        250
                 ....*....|....*...
gi 30684202  235 PAASYITGQTICVDGGLT 252
Cdd:PRK13394 243 FPSAALTGQSFVVSHGWF 260
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-252 9.11e-40

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 137.92  E-value: 9.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVsgsvcDVASRPEREELMQTv 80
Cdd:PRK07060   1 MNMAFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRL-----DVGDDAAIRAALAA- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 ssqfDGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKASGYGSIIFVSSIAGVISFDAGSIY 159
Cdd:PRK07060  75 ----AGAFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARhVARAMIAAGRGGSIVNVSSQAALVGLPDHLAY 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK07060 151 CASKAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASM 230
                        250
                 ....*....|...
gi 30684202  240 ITGQTICVDGGLT 252
Cdd:PRK07060 231 VSGVSLPVDGGYT 243
PRK06701 PRK06701
short chain dehydrogenase; Provisional
7-255 9.77e-40

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 139.40  E-value: 9.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISE---AKLNQSLSEWE-KKGFQVSGSVCDVASRpeREELMQTVSs 82
Cdd:PRK06701  44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEhedANETKQRVEKEgVKCLLIPGDVSDEAFC--KDAVEETVR- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   83 QFdGKLNILVSNVGV-IRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKaSGyGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:PRK06701 121 EL-GRLDILVNNAAFqYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLK-QG-SAIINTGSITGYEGNETLIDYSA 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINTPL--SQSYLEDVS-FKkallSRTPLGRVGEPNEVASLVAFLCLPAAS 238
Cdd:PRK06701 198 TKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLipSDFDEEKVSqFG----SNTPMQRPGQPEELAPAYVFLASPDSS 273
                        250
                 ....*....|....*..
gi 30684202  239 YITGQTICVDGGLTVNG 255
Cdd:PRK06701 274 YITGQMLHVNGGVIVNG 290
PRK12828 PRK12828
short chain dehydrogenase; Provisional
6-251 1.18e-39

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 137.62  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGsvCDVASRPEREELMQTVSSQFd 85
Cdd:PRK12828   4 SLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGG--IDLVDPQAARRAVDEVNRQF- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK12828  81 GRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAAAKAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFkkallsrtplGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:PRK12828 161 VARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADF----------SRWVTPEQIAAVIAFLLSDEAQAITGASI 230

                 ....*.
gi 30684202  246 CVDGGL 251
Cdd:PRK12828 231 PVDGGV 236
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
7-252 7.86e-39

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: 135.66  E-value: 7.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAkLNQSLSEwEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDD-AGQAVAA-ELGDPDISFVHCDVTVEADVRAAVDTAVARF-G 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRSKPTT--EYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:cd05326  79 RLDIMFNNAGVLGAPCYSilETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAYTASKH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPL-------SQSYLEDVSFKKAllsrTPLGRVGEPNEVASLVAFLCLPAA 237
Cdd:cd05326 159 AVLGLTRSAATELGEHGIRVNCVSPYGVATPLltagfgvEDEAIEEAVRGAA----NLKGTALRPEDIAAAVLYLASDDS 234
                       250
                ....*....|....*
gi 30684202 238 SYITGQTICVDGGLT 252
Cdd:cd05326 235 RYVSGQNLVVDGGLT 249
PRK06398 PRK06398
aldose dehydrogenase; Validated
7-253 1.06e-38

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 135.73  E-value: 1.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSlsewekKGFQvsgsvCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK06398   4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDV------DYFK-----VDVSNKEQVIKGIDYVISKY-G 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK06398  72 RIDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  167 IQLAKNLACEWAKdGIRANAVAPNVINTPLSQSYLE-DVSFKKALLSRT--------PLGRVGEPNEVASLVAFLCLPAA 237
Cdd:PRK06398 152 LGLTRSIAVDYAP-TIRCVAVCPGSIRTPLLEWAAElEVGKDPEHVERKirewgemhPMKRVGKPEEVAYVVAFLASDLA 230
                        250
                 ....*....|....*.
gi 30684202  238 SYITGQTICVDGGLTV 253
Cdd:PRK06398 231 SFITGECVTVDGGLRA 246
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
6-250 1.28e-38

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: 135.66  E-value: 1.28e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQF- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKPTT--------------EYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKASGyGSIIFVSSIAGV 150
Cdd:cd08935  81 GTVDILINGAGGNHPDATTdpehyepeteqnffDLDEEGWEFVFDLNLNGSFLPSQvFGKDMLEQKG-GSIINISSMNAF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 151 ISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYL--EDVSFK---KALLSRTPLGRVGEPNEV 225
Cdd:cd08935 160 SPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLinPDGSYTdrsNKILGRTPMGRFGKPEEL 239
                       250       260
                ....*....|....*....|....*.
gi 30684202 226 ASLVAFLC-LPAASYITGQTICVDGG 250
Cdd:cd08935 240 LGALLFLAsEKASSFVTGVVIPVDGG 265
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
12-254 2.66e-38

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 134.47  E-value: 2.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNIL 91
Cdd:PRK08643   5 ALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTF-GDLNVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   92 VSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYG-SIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:PRK08643  84 VNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGgKIINATSQAGVVGNPELAVYSSTKFAVRGLT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  171 KNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVS-------------FKKallsRTPLGRVGEPNEVASLVAFLCLPAA 237
Cdd:PRK08643 164 QTAARDLASEGITVNAYAPGIVKTPMMFDIAHQVGenagkpdewgmeqFAK----DITLGRLSEPEDVANCVSFLAGPDS 239
                        250
                 ....*....|....*..
gi 30684202  238 SYITGQTICVDGGLTVN 254
Cdd:PRK08643 240 DYITGQTIIVDGGMVFH 256
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
1-253 2.85e-38

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 134.50  E-value: 2.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK08085   1 MNDLFSLAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYG 160
Cdd:PRK08085  81 EKDI-GPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:PRK08085 160 ASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFV 239
                        250
                 ....*....|...
gi 30684202  241 TGQTICVDGGLTV 253
Cdd:PRK08085 240 NGHLLFVDGGMLV 252
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
6-252 5.25e-38

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 134.08  E-value: 5.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDIS-EAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK08936   4 DLEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQlshpllKASGY-------GSIIFVSSIAGVISFDAGS 157
Cdd:PRK08936  84 -GTLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSR------EAIKYfvehdikGNIINMSSVHEQIPWPLFV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  158 IYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAA 237
Cdd:PRK08936 157 HYAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKFADPKQRADVESMIPMGYIGKPEEIAAVAAWLASSEA 236
                        250
                 ....*....|....*
gi 30684202  238 SYITGQTICVDGGLT 252
Cdd:PRK08936 237 SYVTGITLFADGGMT 251
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-251 9.85e-38

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 133.16  E-value: 9.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK08217   3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDF-G 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRS---------KPTTEYTEDDFAFHISSNV--------EAAYHfsqlshpLLKASGYGSIIFVSSIAg 149
Cdd:PRK08217  82 QLNGLINNAGILRDgllvkakdgKVTSKMSLEQFQSVIDVNLtgvflcgrEAAAK-------MIESGSKGVIINISSIA- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  150 visfDAGSI----YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVsfKKALLSRTPLGRVGEPNEV 225
Cdd:PRK08217 154 ----RAGNMgqtnYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKPEA--LERLEKMIPVGRLGEPEEI 227
                        250       260
                 ....*....|....*....|....*.
gi 30684202  226 ASLVAFLClpAASYITGQTICVDGGL 251
Cdd:PRK08217 228 AHTVRFII--ENDYVTGRVLEIDGGL 251
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
11-251 1.61e-37

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: 132.66  E-value: 1.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd08945   5 VALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARY-GPIDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ--LSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQ 168
Cdd:cd08945  84 LVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKevLKAGGMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVVG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 169 LAKNLACEWAKDGIRANAVAPNVINTPLSQSYLE------DVSFKKAL---LSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:cd08945 164 FTKALGLELARTGITVNAVCPGFVETPMAASVREhyadiwEVSTEEAFdriTARVPLGRYVTPEEVAGMVAYLIGDGAAA 243
                       250
                ....*....|..
gi 30684202 240 ITGQTICVDGGL 251
Cdd:cd08945 244 VTAQALNVCGGL 255
PRK07774 PRK07774
SDR family oxidoreductase;
7-253 1.83e-37

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 132.18  E-value: 1.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK07774   4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAF-G 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNV---GVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAgviSFDAGSIYGLTK 163
Cdd:PRK07774  83 GIDYLVNNAaiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTA---AWLYSNFYGLAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDvSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:PRK07774 160 VGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRTVTPK-EFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQ 238
                        250
                 ....*....|
gi 30684202  244 TICVDGGLTV 253
Cdd:PRK07774 239 IFNVDGGQII 248
PRK08265 PRK08265
short chain dehydrogenase; Provisional
6-255 3.07e-37

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 132.05  E-value: 3.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAK---LNQSLSEwekkgfQVSGSVCDVASRPEREELMQTVSS 82
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNgaaVAASLGE------RARFIATDITDDAAIERAVATVVA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   83 QFdGKLNILVSNVGVirskptteYTEDDFAfhiSS----------NVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVIS 152
Cdd:PRK08265  77 RF-GRVDILVNLACT--------YLDDGLA---SSradwlaaldvNLVSAAMLAQAAHPHLARGG-GAIVNFTSISAKFA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  153 FDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAP-----NVINTpLSQSyleDVSFKKALLSRT-PLGRVGEPNEVA 226
Cdd:PRK08265 144 QTGRWLYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPgwtwsRVMDE-LSGG---DRAKADRVAAPFhLLGRVGDPEEVA 219
                        250       260
                 ....*....|....*....|....*....
gi 30684202  227 SLVAFLCLPAASYITGQTICVDGGLTVNG 255
Cdd:PRK08265 220 QVVAFLCSDAASFVTGADYAVDGGYSALG 248
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-253 3.14e-37

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 131.24  E-value: 3.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISE-AKLNQSLSEwekkgFQVsgsvcDVASrpEREELMQTVSsQFD 85
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDkPDLSGNFHF-----LQL-----DLSD--DLEPLFDWVP-SVD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 gklnILVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK06550  70 ----ILCNTAGILDDyKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKH 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQT 244
Cdd:PRK06550 146 ALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAADFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTI 225

                 ....*....
gi 30684202  245 ICVDGGLTV 253
Cdd:PRK06550 226 VPIDGGWTL 234
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
5-254 3.64e-37

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 131.54  E-value: 3.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAklnqslsewEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK08220   4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFL---------TQEDYPFATFVLDVSDAAAVAQVCQRLLAET 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK08220  75 -GPLDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLS------RT--PLGRVGEPNEVASLVAFLCLPA 236
Cdd:PRK08220 154 ALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWVDEDGEQQVIAgfpeqfKLgiPLGKIARPQEIANAVLFLASDL 233
                        250
                 ....*....|....*...
gi 30684202  237 ASYITGQTICVDGGLTVN 254
Cdd:PRK08220 234 ASHITLQDIVVDGGATLG 251
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
7-250 4.29e-37

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 131.50  E-value: 4.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAkLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSEL-VHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERF-G 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVG-VIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIA--GVISFDagsiYGLTK 163
Cdd:cd08937  80 RVDVLINNVGgTIWAKPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIAtrGIYRIP----YSAAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 164 GALIQLAKNLACEWAKDGIRANAVAPNVINTP--------LSQSYLEDVSFKKAL---LSRTPLGRVGEPNEVASLVAFL 232
Cdd:cd08937 156 GGVNALTASLAFEHARDGIRVNAVAPGGTEAPprkiprnaAPMSEQEKVWYQRIVdqtLDSSLMGRYGTIDEQVRAILFL 235
                       250
                ....*....|....*...
gi 30684202 233 CLPAASYITGQTICVDGG 250
Cdd:cd08937 236 ASDEASYITGTVLPVGGG 253
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
9-250 4.66e-37

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: 130.98  E-value: 4.66e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVsGSVCDVASRPEREELMQTVSSQFDGkL 88
Cdd:cd08943   1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRAL-GVQCDVTSEAQVQSAFEQAVLEFGG-L 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYG-SIIFVSSIAGVISFDAGSIYGLTKGALI 167
Cdd:cd08943  79 DIVVSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGgNIVFNASKNAVAPGPNAAAYSAAKAAEA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 168 QLAKNLACEWAKDGIRANAVAPNVIntpLSQSYLEDVSFKKA-----------LLSRTPLGRVGEPNEVASLVAFLCLPA 236
Cdd:cd08943 159 HLARCLALEGGEDGIRVNTVNPDAV---FRGSKIWEGVWRAArakayglleeeYRTRNLLKREVLPEDVAEAVVAMASED 235
                       250
                ....*....|....
gi 30684202 237 ASYITGQTICVDGG 250
Cdd:cd08943 236 FGKTTGAIVTVDGG 249
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
5-250 5.48e-37

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: 131.06  E-value: 5.48e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:cd08942   2 FSVAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYG-ECIAIPADLSSEEGIEALVARVAERS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  85 DgKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGY----GSIIFVSSIAG-VISFDAGSIY 159
Cdd:cd08942  81 D-RLDVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGiVVSGLENYSY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:cd08942 160 GASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFLLNDPAALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAY 239
                       250
                ....*....|.
gi 30684202 240 ITGQTICVDGG 250
Cdd:cd08942 240 LTGAVIPVDGG 250
PRK07074 PRK07074
SDR family oxidoreductase;
11-252 5.52e-37

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 131.05  E-value: 5.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFqvSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:PRK07074   4 TALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARF--VPVACDLTDAASLAAALANAAAER-GPVDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYH-FSQLSHPLLKASgYGSIIFVSSIAGVISFDAGSiYGLTKGALIQL 169
Cdd:PRK07074  81 LVANAGAARAASLHDTTPASWRADNALNLEAAYLcVEAVLEGMLKRS-RGAVVNIGSVNGMAALGHPA-YSAAKAGLIHY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  170 AKNLACEWAKDGIRANAVAPNVINTPLSQSYLE---DVsFKKAllsRT--PLGRVGEPNEVASLVAFLCLPAASYITGQT 244
Cdd:PRK07074 159 TKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAanpQV-FEEL---KKwyPLQDFATPDDVANAVLFLASPAARAITGVC 234

                 ....*...
gi 30684202  245 ICVDGGLT 252
Cdd:PRK07074 235 LPVDGGLT 242
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
13-250 7.22e-37

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: 130.72  E-value: 7.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  13 LVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKG--FQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd05330   7 LITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIApdAEVLLIKADVSDEAQVEAYVDATVEQF-GRIDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVI-RSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQL 169
Cdd:cd05330  86 FFNNAGIEgKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKHGVVGL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 170 AKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDV---SFKKA---LLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:cd05330 166 TRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKQLgpeNPEEAgeeFVSVNPMKRFGEPEEVAAVVAFLLSDDAGYVNAA 245

                ....*..
gi 30684202 244 TICVDGG 250
Cdd:cd05330 246 VVPIDGG 252
PRK07478 PRK07478
short chain dehydrogenase; Provisional
6-254 1.95e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 129.66  E-value: 1.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK07478   3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERF- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVI-RSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGV-ISFDAGSIYGLTK 163
Cdd:PRK07478  82 GGLDIAFNNAGTLgEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHtAGFPGMAAYAASK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:PRK07478 162 AGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALAFVAGLHALKRMAQPEEIAQAALFLASDAASFVTGT 241
                        250
                 ....*....|.
gi 30684202  244 TICVDGGLTVN 254
Cdd:PRK07478 242 ALLVDGGVSIT 252
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
11-256 2.14e-36

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: 129.50  E-value: 2.14e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEA-KLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLN 89
Cdd:cd05337   3 VAIVTGASRGIGRAIATELAARGFDIAINDLPDDdQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDF-GRLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  90 ILVSNVGVIRSKPTT--EYTEDDFAFHISSNVEAAYHFSQ------LSHPLLKASGYGSIIFVSSI-AGVISFDAGSiYG 160
Cdd:cd05337  82 CLVNNAGIAVRPRGDllDLTEDSFDRLIAINLRGPFFLTQavarrmVEQPDRFDGPHRSIIFVTSInAYLVSPNRGE-YC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALlSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:cd05337 161 ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAA-GLVPIRRWGQPEDIAKAVRTLASGLLPYS 239
                       250
                ....*....|....*.
gi 30684202 241 TGQTICVDGGLTVNGF 256
Cdd:cd05337 240 TGQPINIDGGLSMRRL 255
PRK07856 PRK07856
SDR family oxidoreductase;
6-250 6.44e-36

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 128.13  E-value: 6.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEaklnqslsewekkGFQVSGSV-----CDVASRPEREELMQTV 80
Cdd:PRK07856   3 DLTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRA-------------PETVDGRPaefhaADVRDPDQVAALVDAI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVIRSKPTTEYTEddfAFH---ISSNVEAAYHFSQLSHPLLKA-SGYGSIIFVSSIAGVISFDAG 156
Cdd:PRK07856  70 VERH-GRLDVLVNNAGGSPYALAAEASP---RFHekiVELNLLAPLLVAQAANAVMQQqPGGGSIVNIGSVSGRRPSPGT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  157 SIYGLTKGALIQLAKNLACEWAKDgIRANAVAPNVINTPLSQS-YLEDVSFkkALLSRT-PLGRVGEPNEVASLVAFLCL 234
Cdd:PRK07856 146 AAYGAAKAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQSELhYGDAEGI--AAVAATvPLGRLATPADIAWACLFLAS 222
                        250
                 ....*....|....*.
gi 30684202  235 PAASYITGQTICVDGG 250
Cdd:PRK07856 223 DLASYVSGANLEVHGG 238
PRK06114 PRK06114
SDR family oxidoreductase;
3-252 8.62e-36

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 127.98  E-value: 8.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    3 KRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDI-SEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVS 81
Cdd:PRK06114   2 QLFDLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLrTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   82 SQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISfDAG---SI 158
Cdd:PRK06114  82 AEL-GALTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIV-NRGllqAH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSqSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAAS 238
Cdd:PRK06114 160 YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMN-TRPEMVHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAAS 238
                        250
                 ....*....|....
gi 30684202  239 YITGQTICVDGGLT 252
Cdd:PRK06114 239 FCTGVDLLVDGGFV 252
PRK12743 PRK12743
SDR family oxidoreductase;
11-255 1.13e-35

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 127.84  E-value: 1.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEwEKKGFQVSGSV--CDVASRPEREELMQTVSSQFdGKL 88
Cdd:PRK12743   4 VAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAE-EVRSHGVRAEIrqLDLSDLPEGAQALDKLIQRL-GRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLS-HPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALI 167
Cdd:PRK12743  82 DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAaRHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  168 QLAKNLACEWAKDGIRANAVAPNVINTPLSQsyLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICV 247
Cdd:PRK12743 162 GLTKAMALELVEHGILVNAVAPGAIATPMNG--MDDSDVKPDSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIV 239

                 ....*...
gi 30684202  248 DGGLTVNG 255
Cdd:PRK12743 240 DGGFMLAN 247
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
7-250 5.31e-35

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 125.91  E-value: 5.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEwekKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK07067   4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALE---IGPAAIAVSLDVTRQDSIDRIVAAAVERF-G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ--LSHPLLKASGyGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK07067  80 GIDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQavARHMVEQGRG-GKIINMASQAGRRGEALVSHYCATKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYleDVSF----------KKALLSRT-PLGRVGEPNEVASLVAFLC 233
Cdd:PRK07067 159 AVISYTQSAALALIRHGINVNAIAPGVVDTPMWDQV--DALFaryenrppgeKKRLVGEAvPLGRMGVPDDLTGMALFLA 236
                        250
                 ....*....|....*..
gi 30684202  234 LPAASYITGQTICVDGG 250
Cdd:PRK07067 237 SADADYIVAQTYNVDGG 253
PRK07063 PRK07063
SDR family oxidoreductase;
7-253 5.80e-35

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 125.93  E-value: 5.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEW--EKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIarDVAGARVLAVPADVTDAASVAAAVAAAEEAF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGV-IRSKPTTeYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIfvsSIAGVISFdagSI----- 158
Cdd:PRK07063  85 -GPLDVLVNNAGInVFADPLA-MTDEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIV---NIASTHAF---KIipgcf 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 -YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRT----PLGRVGEPNEVASLVAFLC 233
Cdd:PRK07063 157 pYPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAETlalqPMKRIGRPEEVAMTAVFLA 236
                        250       260
                 ....*....|....*....|
gi 30684202  234 LPAASYITGQTICVDGGLTV 253
Cdd:PRK07063 237 SDEAPFINATCITIDGGRSV 256
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
7-254 1.58e-34

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: 125.10  E-value: 1.58e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEA--KLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:cd05355  24 LKGKKALITGGDSGIGRAVAIAFAREGADVAINYLPEEedDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEF 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  85 dGKLNILVSNVGVIRSKPTTEY-TEDDFAFHISSNVEAAYHFSQLSHPLLKaSGyGSIIFVSSIAG----VISFDagsiY 159
Cdd:cd05355 104 -GKLDILVNNAAYQHPQESIEDiTTEQLEKTFRTNIFSMFYLTKAALPHLK-KG-SSIINTTSVTAykgsPHLLD----Y 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKaLLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:cd05355 177 AATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKVSE-FGSQVPMGRAGQPAEVAPAYVFLASQDSSY 255
                       250
                ....*....|....*
gi 30684202 240 ITGQTICVDGGLTVN 254
Cdd:cd05355 256 VTGQVLHVNGGEIIN 270
PRK06057 PRK06057
short chain dehydrogenase; Provisional
7-252 1.74e-34

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 124.46  E-value: 1.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEwekkgfqVSGSV--CDVASRPEREELMQTVSSQF 84
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADE-------VGGLFvpTDVTDEDAVNALFDTAAETY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVirSKPtteytEDDFAFHIS---------SNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDA 155
Cdd:PRK06057  78 -GSVDIAFNNAGI--SPP-----EDDSILNTGldawqrvqdVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSAT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  156 GSI-YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQS-YLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLC 233
Cdd:PRK06057 150 SQIsYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQElFAKDPERAARRLVHVPMGRFAEPEEIAAAVAFLA 229
                        250
                 ....*....|....*....
gi 30684202  234 LPAASYITGQTICVDGGLT 252
Cdd:PRK06057 230 SDDASFITASTFLVDGGIS 248
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
6-251 2.08e-34

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 124.35  E-value: 2.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSL-SEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK12935   3 QLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLvNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK12935  83 -GKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVsfKKALLSRTPLGRVGEPNEVASLVAFLCLPAAsYITGQT 244
Cdd:PRK12935 162 GMLGFTKSLALELAKTNVTVNAICPGFIDTEMVAEVPEEV--RQKIVAKIPKKRFGQADEIAKGVVYLCRDGA-YITGQQ 238

                 ....*..
gi 30684202  245 ICVDGGL 251
Cdd:PRK12935 239 LNINGGL 245
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
12-252 2.98e-34

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: 123.73  E-value: 2.98e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLnqslsewEKKGFQVSGSVCDVASRPEREELMQTVSSQfDGKLNIL 91
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLL-------LEYGDPLRLTPLDVADAAAVREVCSRLLAE-HGPIDAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  92 VSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSS-IAGVISFDAGSiYGLTKGALIQLA 170
Cdd:cd05331  73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASnAAHVPRISMAA-YGASKAALASLS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 171 KNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLS------RT--PLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:cd05331 152 KCLGLELAPYGVRCNVVSPGSTDTAMQRTLWHDEDGAAQVIAgvpeqfRLgiPLGKIAQPADIANAVLFLASDQAGHITM 231
                       250
                ....*....|
gi 30684202 243 QTICVDGGLT 252
Cdd:cd05331 232 HDLVVDGGAT 241
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-253 4.48e-34

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 123.53  E-value: 4.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELAGFGARIHVCDIS-EAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKL 88
Cdd:PRK12745   3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPdDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAW-GRI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSN--VGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ------LSHPLLKASGYGSIIFVSSI-AGVISFDAGSiY 159
Cdd:PRK12745  82 DCLVNNagVGVKVRGDLLDLTPESFDRVLAINLRGPFFLTQavakrmLAQPEPEELPHRSIVFVSSVnAIMVSPNRGE-Y 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLE--DVSFKKALlsrTPLGRVGEPNEVASLVAFLCLPAA 237
Cdd:PRK12745 161 CISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTAPVTAkyDALIAKGL---VPMPRWGEPEDVARAVAALASGDL 237
                        250
                 ....*....|....*.
gi 30684202  238 SYITGQTICVDGGLTV 253
Cdd:PRK12745 238 PYSTGQAIHVDGGLSI 253
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
12-252 6.50e-34

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 122.91  E-value: 6.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSL-SEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:PRK08063   7 ALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETaEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEF-GRLDV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNV--GVIRskPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQ 168
Cdd:PRK08063  86 FVNNAasGVLR--PAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGSIRYLENYTTVGVSKAALEA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  169 LAKNLACEWAKDGIRANAVAPNVINT------PLSQSYLEDVSfkkallSRTPLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:PRK08063 164 LTRYLAVELAPKGIAVNAVSGGAVDTdalkhfPNREELLEDAR------AKTPAGRMVEPEDVANAVLFLCSPEADMIRG 237
                        250
                 ....*....|
gi 30684202  243 QTICVDGGLT 252
Cdd:PRK08063 238 QTIIVDGGRS 247
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
7-256 1.44e-33

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 122.37  E-value: 1.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWekkGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK06200   4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRF---GDHVLVVEGDVTSYADNQRAVDQTVDAF-G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIR-SKPTTEYTEDDFA------FHIssNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIY 159
Cdd:PRK06200  80 KLDCFVGNAGIWDyNTSLVDIPAETLDtafdeiFNV--NVKGYLLGAKAALPALKASG-GSMIFTLSNSSFYPGGGGPLY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDgIRANAVAPNVINTPL--------SQSYLEDV-SFKKALLSRTPLGRVGEPNEVASLVA 230
Cdd:PRK06200 157 TASKHAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDLrgpaslgqGETSISDSpGLADMIAAITPLQFAPQPEDHTGPYV 235
                        250       260
                 ....*....|....*....|....*..
gi 30684202  231 FLCLPAAS-YITGQTICVDGGLTVNGF 256
Cdd:PRK06200 236 LLASRRNSrALTGVVINADGGLGIRGI 262
PRK12937 PRK12937
short chain dehydrogenase; Provisional
7-251 1.67e-33

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 121.77  E-value: 1.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSL-SEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELvAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAF- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAyhFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK12937  82 GRIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGA--FVVLREAARHLGQGGRIINLSTSVIALPLPGYGPYAASKAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYlEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:PRK12937 160 VEGLVHVLANELRGRGITVNAVAPGPVATELFFNG-KSAEQIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVL 238

                 ....*.
gi 30684202  246 CVDGGL 251
Cdd:PRK12937 239 RVNGGF 244
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-255 2.71e-33

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 121.37  E-value: 2.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVcdisEAK-----LNQSLSEWEKKGFQVSGSVCDVASRPEREELMQT 79
Cdd:PRK06077   2 YSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVV----NAKkraeeMNETLKMVKENGGEGIGVLADVSTREGCETLAKA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   80 VSSQFDGkLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAGVISFDAGSIY 159
Cdd:PRK06077  78 TIDRYGV-ADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGG--AIVNIASVAGIRPAYGLSIY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDgIRANAVAPNVINTPLSQSYLE--DVSFKKALLSRTPLGRVGEPNEVASLVAFLClpAA 237
Cdd:PRK06077 155 GAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKLGESLFKvlGMSEKEFAEKFTLMGKILDPEEVAEFVAAIL--KI 231
                        250
                 ....*....|....*...
gi 30684202  238 SYITGQTICVDGGLTVNG 255
Cdd:PRK06077 232 ESITGQVFVLDSGESLKG 249
PRK07069 PRK07069
short chain dehydrogenase; Validated
12-251 4.87e-33

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 120.59  E-value: 4.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEW--EKKGFQVS-GSVCDVASRPEREELMQTVSSQFDGkL 88
Cdd:PRK07069   2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAEinAAHGEGVAfAAVQDVTDEAQWQALLAQAADAMGG-L 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQ 168
Cdd:PRK07069  81 SVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  169 LAKNLACEWAKDG--IRANAVAPNVINTP----LSQSYLEDVSFKKaLLSRTPLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:PRK07069 161 LTKSIALDCARRGldVRCNSIHPTFIRTGivdpIFQRLGEEEATRK-LARGVPLGRLGEPDDVAHAVLYLASDESRFVTG 239

                 ....*....
gi 30684202  243 QTICVDGGL 251
Cdd:PRK07069 240 AELVIDGGI 248
PRK08628 PRK08628
SDR family oxidoreductase;
7-252 5.68e-33

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 120.83  E-value: 5.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKlNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK08628   5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPD-DEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKF-G 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKpTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK08628  83 RIDGLVNNAGVNDGV-GLEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNISSKTALTGQGGTSGYAAAKGAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  167 IQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEdvSF------KKALLSRTPLG-RVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK08628 161 LALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIA--TFddpeakLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSH 238
                        250
                 ....*....|...
gi 30684202  240 ITGQTICVDGGLT 252
Cdd:PRK08628 239 TTGQWLFVDGGYV 251
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-250 1.34e-32

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 119.59  E-value: 1.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKlnQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK08993   6 FSLEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEPT--ETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFvsSIAGVISFDAG---SIYGL 161
Cdd:PRK08993  84 -GHIDILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKII--NIASMLSFQGGirvPSYTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYIT 241
Cdd:PRK08993 161 SKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQLRADEQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYIN 240

                 ....*....
gi 30684202  242 GQTICVDGG 250
Cdd:PRK08993 241 GYTIAVDGG 249
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
11-252 1.48e-32

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: 119.48  E-value: 1.48e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEweKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAVAA--EAGERAIAIQADVRDRDQVQAMIEEAKNHF-GPVDT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNV-------GVIRSKPTTEyTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSS---IAGVISFDAgsiYG 160
Cdd:cd05349  79 IVNNAlidfpfdPDQRKTFDTI-DWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVINIGTnlfQNPVVPYHD---YT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDvSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:cd05349 155 TAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAATPK-EVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAV 233
                       250
                ....*....|..
gi 30684202 241 TGQTICVDGGLT 252
Cdd:cd05349 234 TGQNLVVDGGLV 245
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
8-251 8.64e-32

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: 117.39  E-value: 8.64e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   8 KGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSlsewEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGK 87
Cdd:cd05371   1 KGLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETV----AKLGDNCRFVPVDVTSEKDVKAALALAKAKF-GR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  88 LNILVSNVGV------IRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKA----SGY--GSIIFVSSIAGvisFDa 155
Cdd:cd05371  76 LDIVVNCAGIavaaktYNKKGQQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKnepdQGGerGVIINTASVAA---FE- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 156 GSI----YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVsfKKALLSRTP-LGRVGEPNEVASLVA 230
Cdd:cd05371 152 GQIgqaaYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGLPEKV--RDFLAKQVPfPSRLGDPAEYAHLVQ 229
                       250       260
                ....*....|....*....|.
gi 30684202 231 FLCLpaASYITGQTICVDGGL 251
Cdd:cd05371 230 HIIE--NPYLNGEVIRLDGAI 248
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
11-233 9.93e-32

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: 116.69  E-value: 9.93e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEwEKKGFQVSgsvCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd08932   2 VALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVP---YDARDPEDARALVDALRDRF-GRIDV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:cd08932  77 LVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALA 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684202 171 KNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFkkallsrtPLGRVGEPNEVASLVAFLC 233
Cdd:cd08932 157 HALRQEGWDHGVRVSAVCPGFVDTPMAQGLTLVGAF--------PPEEMIQPKDIANLVRMVI 211
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
11-250 1.43e-31

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: 116.22  E-value: 1.43e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHV-CDISEAKLNQSLSEWEKKG---FQVSGSVCDVASrpeREELMQTVSSQFdG 86
Cdd:cd05357   2 VALVTGAAKRIGRAIAEALAAEGYRVVVhYNRSEAEAQRLKDELNALRnsaVLVQADLSDFAA---CADLVAAAFRAF-G 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIagVIS--FDAGSIYGLTKG 164
Cdd:cd05357  78 RCDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDA--MTDrpLTGYFAYCMSKA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 165 ALIQLAKNLACEWAKDgIRANAVAPNVINTPLSQsyleDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPaaSYITGQT 244
Cdd:cd05357 156 ALEGLTRSAALELAPN-IRVNGIAPGLILLPEDM----DAEYRENALRKVPLKRRPSAEEIADAVIFLLDS--NYITGQI 228

                ....*.
gi 30684202 245 ICVDGG 250
Cdd:cd05357 229 IKVDGG 234
PRK05867 PRK05867
SDR family oxidoreductase;
5-252 2.66e-31

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 116.29  E-value: 2.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK05867   5 FDLHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 DGkLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYG-SIIFVSSIAG-VISFDAG-SIYGL 161
Cdd:PRK05867  85 GG-IDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGgVIINTASMSGhIINVPQQvSHYCA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEdvsFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYIT 241
Cdd:PRK05867 164 SKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTE---YQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYMT 240
                        250
                 ....*....|.
gi 30684202  242 GQTICVDGGLT 252
Cdd:PRK05867 241 GSDIVIDGGYT 251
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
11-251 2.92e-31

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: 116.05  E-value: 2.92e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNqslsewekkgfqvsgsvCDVASRPEREELMQTVSSQFDGKLNI 90
Cdd:cd05328   1 TIVITGAASGIGAATAELLEDAGHTVIGIDLREADVI-----------------ADLSTPEGRAAAIADVLARCSGVLDG 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVirskPTTEYTEDDfafhISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAG----------VISFDAGS--- 157
Cdd:cd05328  64 LVNCAGV----GGTTVAGLV----LKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGagwaqdklelAKALAAGTear 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 158 --------------IYGLTKGALIQLAKNLACEWAKD-GIRANAVAPNVINTPLSQSYLEDVSFKKALLS-RTPLGRVGE 221
Cdd:cd05328 136 avalaehagqpgylAYAGSKEALTVWTRRRAATWLYGaGVRVNTVAPGPVETPILQAFLQDPRGGESVDAfVTPMGRRAE 215
                       250       260       270
                ....*....|....*....|....*....|
gi 30684202 222 PNEVASLVAFLCLPAASYITGQTICVDGGL 251
Cdd:cd05328 216 PDEIAPVIAFLASDAASWINGANLFVDGGL 245
PRK07577 PRK07577
SDR family oxidoreductase;
11-250 6.81e-31

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 114.82  E-value: 6.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIhvcdISEAKLNQSlsewekkGFQVSGSVCDVASRPEREELMQTVSSQFDgkLNI 90
Cdd:PRK07577   5 TVLVTGATKGIGLALSLRLANLGHQV----IGIARSAID-------DFPGELFACDLADIEQTAATLAQINEIHP--VDA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSiYGLTKGALIQLA 170
Cdd:PRK07577  72 IVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRAIFGALDRTS-YSAAKSALVGCT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  171 KNLACEWAKDGIRANAVAPNVINTPL-SQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDG 249
Cdd:PRK07577 151 RTWALELAEYGITVNAVAPGPIETELfRQTRPVGSEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVLGVDG 230

                 .
gi 30684202  250 G 250
Cdd:PRK07577 231 G 231
PRK06125 PRK06125
short chain dehydrogenase; Provisional
1-255 1.07e-30

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 114.76  E-value: 1.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRwsLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKK-GFQVSGSVCDVASRPEREELMQT 79
Cdd:PRK06125   1 MDLH--LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAhGVDVAVHALDLSSPEAREQLAAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   80 VssqfdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGViSFDAGSIY 159
Cdd:PRK06125  79 A-----GDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGE-NPDADYIC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLT-KGALIQLAKNLACEWAKDGIRANAVAPNVINTPL--------SQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVA 230
Cdd:PRK06125 153 GSAgNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRmltllkgrARAELGDESRWQELLAGLPLGRPATPEEVADLVA 232
                        250       260
                 ....*....|....*....|....*
gi 30684202  231 FLCLPAASYITGQTICVDGGLTVNG 255
Cdd:PRK06125 233 FLASPRSGYTSGTVVTVDGGISARG 257
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
7-251 2.16e-30

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 113.47  E-value: 2.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWekkGFQVSGSVCDVASRPEREELMQTVSSQFDG 86
Cdd:PRK12936   4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 kLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFS-QLSHPLLKASgYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK12936  81 -VDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTrELTHPMMRRR-YGRIINITSVVGVTGNPGQANYCASKAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSyLEDVSfKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:PRK12936 159 MIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGK-LNDKQ-KEAIMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTI 236

                 ....*.
gi 30684202  246 CVDGGL 251
Cdd:PRK12936 237 HVNGGM 242
PRK06523 PRK06523
short chain dehydrogenase; Provisional
1-250 4.99e-30

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 113.08  E-value: 4.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIhvcdISEAKlNQSLSEWEKKGFqVSGsvcDVASRPEREELMQTV 80
Cdd:PRK06523   1 MSFFLELAGKRALVTGGTKGIGAATVARLLEAGARV----VTTAR-SRPDDLPEGVEF-VAA---DLTTAEGCAAVARAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVIRSkPTTEY---TEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVI-SFDAG 156
Cdd:PRK06523  72 LERL-GGVDILVHVLGGSSA-PAGGFaalTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLpLPEST 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  157 SIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDV---------SFKKALLSRT---PLGRVGEPNE 224
Cdd:PRK06523 150 TAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAVALAERLaeaagtdyeGAKQIIMDSLggiPLGRPAEPEE 229
                        250       260
                 ....*....|....*....|....*.
gi 30684202  225 VASLVAFLCLPAASYITGQTICVDGG 250
Cdd:PRK06523 230 VAELIAFLASDRAASITGTEYVIDGG 255
PRK07062 PRK07062
SDR family oxidoreductase;
7-251 7.16e-30

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 112.83  E-value: 7.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSE--WEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARlrEKFPGARLLAARCDVLDEADVAAFAAAVEARF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSI------AGVISFDAGsi 158
Cdd:PRK07062  86 -GGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLlalqpePHMVATSAA-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 ygltKGALIQLAKNLACEWAKDGIRANAVAPNVINT-----------PLSQSYlEDVSFKKALLSRTPLGRVGEPNEVAS 227
Cdd:PRK07062 163 ----RAGLLNLVKSLATELAPKGVRVNSILLGLVESgqwrrryearaDPGQSW-EAWTAALARKKGIPLGRLGRPDEAAR 237
                        250       260
                 ....*....|....*....|....
gi 30684202  228 LVAFLCLPAASYITGQTICVDGGL 251
Cdd:PRK07062 238 ALFFLASPLSSYTTGSHIDVSGGF 261
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
1-250 7.38e-30

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 112.73  E-value: 7.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSlkGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAkLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK12823   2 MNQRFA--GKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSEL-VHEVAAELRAAGGEALALTADLETYAGAQAAMAAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNV-GVIRSKPTTEYTEDDfafhissnVEAAYH---FSQL--SH---PLLKASGYGSIIFVSSIAgvi 151
Cdd:PRK12823  79 VEAF-GRIDVLINNVgGTIWAKPFEEYEEEQ--------IEAEIRrslFPTLwcCRavlPHMLAQGGGAIVNVSSIA--- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  152 sfdAGSI----YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTP--------LSQSYLEDVSFKKAL---LSRTPL 216
Cdd:PRK12823 147 ---TRGInrvpYSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPprrvprnaAPQSEQEKAWYQQIVdqtLDSSLM 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 30684202  217 GRVGEPNEVASLVAFLCLPAASYITGQTICVDGG 250
Cdd:PRK12823 224 KRYGTIDEQVAAILFLASDEASYITGTVLPVGGG 257
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
11-240 7.97e-30

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


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 111.95  E-value: 7.97e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEV-GDVTI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:cd05339  80 LINNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 171 KNLACE---WAKDGIRANAVAPNVINTPLsqsyledvsFKKALLSRTPLGRVGEPNEVASLVA--------FLCLPAASY 239
Cdd:cd05339 160 ESLRLElkaYGKPGIKTTLVCPYFINTGM---------FQGVKTPRPLLAPILEPEYVAEKIVrailtnqqMLYLPFYAY 230

                .
gi 30684202 240 I 240
Cdd:cd05339 231 F 231
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
8-250 1.86e-29

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 111.67  E-value: 1.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    8 KGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVS--GSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEGMayGFGADATSEQSVLALSRGVDEIF- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEA----AYHFSQLshpLLKASGYGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:PRK12384  80 GRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGyflcAREFSRL---MIRDGIQGRIIQINSKSGKVGSKHNSGYSA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  162 TKGALIQLAKNLACEWAKDGIRANAVAP-NVINTPLSQSYLEDVSFK---------KALLSRTPLGRVGEPNEVASLVAF 231
Cdd:PRK12384 157 AKFGGVGLTQSLALDLAEYGITVHSLMLgNLLKSPMFQSLLPQYAKKlgikpdeveQYYIDKVPLKRGCDYQDVLNMLLF 236
                        250
                 ....*....|....*....
gi 30684202  232 LCLPAASYITGQTICVDGG 250
Cdd:PRK12384 237 YASPKASYCTGQSINVTGG 255
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-250 2.37e-29

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 111.32  E-value: 2.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGA--SGIGYAIVEELAGFGARIHV-----CDISEAKLNQSLSEW------EKKGFQVSGSVCDVASRPE 72
Cdd:PRK12748   2 PLMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspYDKTMPWGMHDKEPVllkeeiESYGVRCEHMEIDLSQPYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   73 REELMQTVSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQL--SHPLLKASGygSIIFVSS---- 146
Cdd:PRK12748  82 PNRVFYAVSERL-GDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAfaKQYDGKAGG--RIINLTSgqsl 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  147 --IAGVISfdagsiYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTplsqSYLEDvSFKKALLSRTPLGRVGEPNE 224
Cdd:PRK12748 159 gpMPDELA------YAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT----GWITE-ELKHHLVPKFPQGRVGEPVD 227
                        250       260
                 ....*....|....*....|....*.
gi 30684202  225 VASLVAFLCLPAASYITGQTICVDGG 250
Cdd:PRK12748 228 AARLIAFLVSEEAKWITGQVIHSEGG 253
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
11-250 5.19e-29

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: 109.97  E-value: 5.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNqslsewEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd05361   3 IALVTHARHFAGPASAEALTEDGYTVVCHDASFADAA------ERQAFESENPGTKALSEQKPEELVDAVLQAG-GAIDV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRS-KPTTEYTEDDfafhISSNVEAAYHFS----QLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:cd05361  76 LVSNDYIPRPmNPIDGTSEAD----IRQAFEALSIFPfallQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTP--LSQSYLE-DVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:cd05361 152 AVALAESLAKELSRDNILVYAIGPNFFNSPtyFPTSDWEnNPELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITG 231

                ....*...
gi 30684202 243 QTICVDGG 250
Cdd:cd05361 232 QFFAFAGG 239
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
7-250 6.33e-29

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: 110.01  E-value: 6.33e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSgsvCDVASRPEREELMQTVSSQFdG 86
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAIS---LDVTDQASIDRCVAALVDRW-G 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYG-SIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:cd05363  77 SIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGgKIINMASQAGRRGEALVGVYCATKAA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYleDVSF-----------KKALLSRTPLGRVGEPNEVASLVAFLCL 234
Cdd:cd05363 157 VISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGV--DAKFaryenrprgekKRLVGEAVPFGRMGRAEDLTGMAIFLAS 234
                       250
                ....*....|....*.
gi 30684202 235 PAASYITGQTICVDGG 250
Cdd:cd05363 235 TDADYIVAQTYNVDGG 250
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
1-250 1.01e-28

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 109.99  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK08277   2 MPNLFSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVIRSKPTTEY---------------TEDDFAFHISSNVEAAYHFSQL-SHPLLKASGyGSIIFV 144
Cdd:PRK08277  82 LEDF-GPCDILINGAGGNHPKATTDNefhelieptktffdlDEEGFEFVFDLNLLGTLLPTQVfAKDMVGRKG-GNIINI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  145 SSIAGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYL--EDVSFK---KALLSRTPLGRV 219
Cdd:PRK08277 160 SSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTEQNRALLfnEDGSLTeraNKILAHTPMGRF 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 30684202  220 GEPNEVASLVAFLCLP-AASYITGQTICVDGG 250
Cdd:PRK08277 240 GKPEELLGTLLWLADEkASSFVTGVVLPVDGG 271
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-250 2.10e-28

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 108.45  E-value: 2.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    5 WSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSgsVCDVASRPEREELMQTVSSQF 84
Cdd:PRK12481   4 FDLNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEAPETQAQVEALGRKFHFI--TADLIQQKDIDSIVSQAVEVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKASGYGSIIfvsSIAGVISFDAG---SIYG 160
Cdd:PRK12481  82 -GHIDILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQaVAKQFVKQGNGGKII---NIASMLSFQGGirvPSYT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:PRK12481 158 ASKSAVMGLTRALATELSQYNINVNAIAPGYMATDNTAALRADTARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYV 237
                        250
                 ....*....|
gi 30684202  241 TGQTICVDGG 250
Cdd:PRK12481 238 TGYTLAVDGG 247
PRK06949 PRK06949
SDR family oxidoreductase;
1-251 4.70e-28

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 107.93  E-value: 4.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKG---FQVSGSVCDVAS------RP 71
Cdd:PRK06949   1 MGRSINLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGgaaHVVSLDVTDYQSikaavaHA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   72 EREElmqtvssqfdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ--LSHPLLKASGYGS------IIF 143
Cdd:PRK06949  81 ETEA----------GTIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQevAKRMIARAKGAGNtkpggrIIN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  144 VSSIAGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKaLLSRTPLGRVGEPN 223
Cdd:PRK06949 151 IASVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQGQK-LVSMLPRKRVGKPE 229
                        250       260
                 ....*....|....*....|....*...
gi 30684202  224 EVASLVAFLCLPAASYITGQTICVDGGL 251
Cdd:PRK06949 230 DLDGLLLLLAADESQFINGAIISADDGF 257
PRK07576 PRK07576
short chain dehydrogenase; Provisional
1-257 2.12e-27

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 106.19  E-value: 2.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK07576   1 MTTMFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIYG 160
Cdd:PRK07576  81 ADEF-GPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPG-ASIIQISAPQAFVPMPMQAHVC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLE-DVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK07576 159 AAKAGVDMLTRTLALEWGPEGIRVNSIVPGPIAGTEGMARLApSPELQAAVAQSVPLKRNGTKQDIANAALFLASDMASY 238
                        250
                 ....*....|....*...
gi 30684202  240 ITGQTICVDGGLTVNGFS 257
Cdd:PRK07576 239 ITGVVLPVDGGWSLGGAS 256
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
9-196 2.73e-27

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: 106.15  E-value: 2.73e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSE--WEKKGFQVSGSVCDVASRPEREELMQTVSSQFDg 86
Cdd:cd05327   1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEikKETGNAKVEVIQLDLSSLASVRQFAEEFLARFP- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRskPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVI--------------S 152
Cdd:cd05327  80 RLDILINNAGIMA--PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAgpidfndldlennkE 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 30684202 153 FDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPL 196
Cdd:cd05327 158 YSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL 201
PRK07677 PRK07677
short chain dehydrogenase; Provisional
9-250 3.56e-27

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 105.15  E-value: 3.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASrPEREELMQTVSSQFDGKL 88
Cdd:PRK07677   1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRN-PEDVQKMVEQIDEKFGRI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKASGYGSII-FVSSIA-----GVISFDAGsiygl 161
Cdd:PRK07677  80 DALINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQaVGKYWIEKGIKGNIInMVATYAwdagpGVIHSAAA----- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  162 tKGALIQLAKNLACEWAKD-GIRANAVAPNVI-NTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK07677 155 -KAGVLAMTRTLAVEWGRKyGIRVNAIAPGPIeRTGGADKLWESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAY 233
                        250
                 ....*....|.
gi 30684202  240 ITGQTICVDGG 250
Cdd:PRK07677 234 INGTCITMDGG 244
PRK05876 PRK05876
short chain dehydrogenase; Provisional
9-196 3.79e-27

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 105.81  E-value: 3.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTvSSQFDGKL 88
Cdd:PRK05876   6 GRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADE-AFRLLGHV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHP-LLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALI 167
Cdd:PRK05876  85 DVVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPrLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVV 164
                        170       180
                 ....*....|....*....|....*....
gi 30684202  168 QLAKNLACEWAKDGIRANAVAPNVINTPL 196
Cdd:PRK05876 165 GLAETLAREVTADGIGVSVLCPMVVETNL 193
PRK07326 PRK07326
SDR family oxidoreductase;
6-197 7.07e-27

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 104.32  E-value: 7.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK07326   3 SLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAF- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK07326  81 GGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTNFFAGGAAYNASKFG 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLS 197
Cdd:PRK07326 160 LVGFSEAAMLDLRQYGIKVSTIMPGSVATHFN 191
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
7-253 8.61e-27

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: 104.36  E-value: 8.61e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWekkGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:cd05348   2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADF---GDAVVGVEGDVRSLADNERAVARCVERF-G 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVI-RSKPTTEYTED------DFAFHIssNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIY 159
Cdd:cd05348  78 KLDCFIGNAGIWdYSTSLVDIPEEkldeafDELFHI--NVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPGGGGPLY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 160 GLTKGALIQLAKNLACEWAKDgIRANAVAPNVINT----PLSQSYLEDVSFKKALL----SRTPLGRVGEPNEVASLVAF 231
Cdd:cd05348 155 TASKHAVVGLVKQLAYELAPH-IRVNGVAPGGMVTdlrgPASLGQGETSISTPPLDdmlkSILPLGFAPEPEDYTGAYVF 233
                       250       260
                ....*....|....*....|...
gi 30684202 232 LCLPAAS-YITGQTICVDGGLTV 253
Cdd:cd05348 234 LASRGDNrPATGTVINYDGGMGV 256
PRK08340 PRK08340
SDR family oxidoreductase;
10-252 8.82e-27

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 104.50  E-value: 8.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSVCDVASRPEREELMQTvSSQFDGKLN 89
Cdd:PRK08340   1 MNVLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKE-AWELLGGID 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVSNVGVIRSKPTT--EYTEDDF----AFHIssnVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:PRK08340  79 ALVWNAGNVRCEPCMlhEAGYSDWleaaLLHL---VAPGYLTTLLIQAWLEKKMKGVLVYLSSVSVKEPMPPLVLADVTR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVS----------FKKALLSRTPLGRVGEPNEVASLVAFLC 233
Cdd:PRK08340 156 AGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTPGARENLARIAeergvsfeetWEREVLERTPLKRTGRWEELGSLIAFLL 235
                        250
                 ....*....|....*....
gi 30684202  234 LPAASYITGQTICVDGGLT 252
Cdd:PRK08340 236 SENAEYMLGSTIVFDGAMT 254
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
9-253 9.11e-27

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: 104.20  E-value: 9.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKlnqSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKL 88
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEER---GADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKL-GRI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIYGLTKGALIQ 168
Cdd:cd09761  77 DVLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASKGGLVA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 169 LAKNLACEWAKDgIRANAVAPNVINTPLSQSYlEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVD 248
Cdd:cd09761 156 LTHALAMSLGPD-IRVNCISPGWINTTEQQEF-TAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVD 233

                ....*
gi 30684202 249 GGLTV 253
Cdd:cd09761 234 GGMTK 238
PRK07890 PRK07890
short chain dehydrogenase; Provisional
7-250 1.13e-26

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 104.27  E-value: 1.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERF-G 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK07890  82 RVDALVNNAFRVPSmKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAYKMAKGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFK---------KALLSRTPLGRVGEPNEVASLVAFLCLPA 236
Cdd:PRK07890 161 LLAASQSLATELGPQGIRVNSVAPGYIWGDPLKGYFRHQAGKygvtveqiyAETAANSDLKRLPTDDEVASAVLFLASDL 240
                        250
                 ....*....|....
gi 30684202  237 ASYITGQTICVDGG 250
Cdd:PRK07890 241 ARAITGQTLDVNCG 254
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-254 1.17e-26

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 104.02  E-value: 1.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHV-CDISEAKLNQSLSEWEKKGFQVSGsvcDVASRPEREELMQTVSSQFDGKLN 89
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVVVnYHQSEDAAEALADELGDRAIALQA---DVTDREQVQAMFATATEHFGKPIT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVSNV-------GVIRSKPTTeYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSS---IAGVISFDAgsiY 159
Cdd:PRK08642  84 TVVNNAladfsfdGDARKKADD-ITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRIINIGTnlfQNPVVPYHD---Y 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKkALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK08642 160 TTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDEVFD-LIAATTPLRKVTTPQEFADAVLFFASPWARA 238
                        250
                 ....*....|....*
gi 30684202  240 ITGQTICVDGGLTVN 254
Cdd:PRK08642 239 VTGQNLVVDGGLVMN 253
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-235 1.67e-26

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 103.23  E-value: 1.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK07666   4 SLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNEL- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK07666  83 GSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASKFG 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTplsqsyleDVSFKKALLSRTPlGRVGEPNEVASL-VAFLCLP 235
Cdd:PRK07666 163 VLGLTESLMQEVRKHNIRVTALTPSTVAT--------DMAVDLGLTDGNP-DKVMQPEDLAEFiVAQLKLN 224
PRK08416 PRK08416
enoyl-ACP reductase;
7-252 2.24e-26

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 103.31  E-value: 2.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLS-EWEKK-GFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK08416   6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEANKIAeDLEQKyGIKAKAYPLNILEPETYKELFKKIDEDF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 DgKLNILVSN--------VG----VIRSKP---TTEYTEDDFAFHISSNvEAAYHfsqlshplLKASGYGSIIFVSSIAG 149
Cdd:PRK08416  86 D-RVDFFISNaiisgravVGgytkFMRLKPkglNNIYTATVNAFVVGAQ-EAAKR--------MEKVGGGSIISLSSTGN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  150 VISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLV 229
Cdd:PRK08416 156 LVYIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNYEEVKAKTEELSPLNRMGQPEDLAGAC 235
                        250       260
                 ....*....|....*....|...
gi 30684202  230 AFLCLPAASYITGQTICVDGGLT 252
Cdd:PRK08416 236 LFLCSEKASWLTGQTIVVDGGTT 258
PRK07041 PRK07041
SDR family oxidoreductase;
13-250 3.08e-26

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 102.42  E-value: 3.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   13 LVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSVCDVASRPEREELMQTVssqfdGKLNILV 92
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGA-PVRTAALDITDEAAVDAFFAEA-----GPFDHVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   93 SNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQlsHPLLKASgyGSIIFVSSIAGVISFDAGSIYGLTKGALIQLAKN 172
Cdd:PRK07041  75 ITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVAR--AARIAPG--GSLTFVSGFAAVRPSASGVLQGAINAALEALARG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  173 LACEWAKdgIRANAVAPNVINTPLSQSYLEDVsfKKALLS----RTPLGRVGEPNEVASLVAFLClpAASYITGQTICVD 248
Cdd:PRK07041 151 LALELAP--VRVNTVSPGLVDTPLWSKLAGDA--REAMFAaaaeRLPARRVGQPEDVANAILFLA--ANGFTTGSTVLVD 224

                 ..
gi 30684202  249 GG 250
Cdd:PRK07041 225 GG 226
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
6-199 3.70e-26

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: 102.00  E-value: 3.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKlnqsLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFD 85
Cdd:cd05370   2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREER----LAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 gKLNILVSNVGVIR----SKPTTeyTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:cd05370  78 -NLDILINNAGIQRpidlRDPAS--DLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCA 154
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 30684202 162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQS 199
Cdd:cd05370 155 TKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEE 192
PRK12742 PRK12742
SDR family oxidoreductase;
7-250 4.63e-26

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 102.14  E-value: 4.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSewekkgfQVSGSVCDVASRPEREELMQTVSSQfdG 86
Cdd:PRK12742   4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLA-------QETGATAVQTDSADRDAVIDVVRKS--G 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSqlSHPLLKASGYGSIIFVSSIAG-VISFDAGSIYGLTKGA 165
Cdd:PRK12742  75 ALDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHAS--VEAARQMPEGGRIIIIGSVNGdRMPVAGMAAYAASKSA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTPLSQsylEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTI 245
Cdd:PRK12742 153 LQGMARGLARDFGPRGITINVVQPGPIDTDANP---ANGPMKDMMHSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGAMH 229

                 ....*
gi 30684202  246 CVDGG 250
Cdd:PRK12742 230 TIDGA 234
PRK06128 PRK06128
SDR family oxidoreductase;
7-251 8.10e-26

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 102.63  E-value: 8.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDI--SEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK06128  53 LQGRKALITGADSGIGRATAIAFAREGADIALNYLpeEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKEL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 DGkLNILVSNVG-VIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAgviSFDAGSI---YG 160
Cdd:PRK06128 133 GG-LDILVNIAGkQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGA--SIINTGSIQ---SYQPSPTlldYA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:PRK06128 207 STKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLASQESSYV 286
                        250
                 ....*....|.
gi 30684202  241 TGQTICVDGGL 251
Cdd:PRK06128 287 TGEVFGVTGGL 297
PRK05875 PRK05875
short chain dehydrogenase; Provisional
6-250 8.33e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 102.19  E-value: 8.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWE--KKGFQVSGSVCDVASRPEREELMQTVSSq 83
Cdd:PRK05875   4 SFQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEalKGAGAVRYEPADVTDEDQVARAVDAATA- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   84 FDGKLNILVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLT 162
Cdd:PRK05875  83 WHGRLHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  163 KGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASYITG 242
Cdd:PRK05875 163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSADYRACTPLPRVGEVEDVANLAMFLLSDAASWITG 242

                 ....*...
gi 30684202  243 QTICVDGG 250
Cdd:PRK05875 243 QVINVDGG 250
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-250 1.58e-25

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 101.02  E-value: 1.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGG--ASGIGYAIVEELAGFGARIHVC-----DISEAKLNQSLSEW------EKKGFQVSGSVCDVASRPE 72
Cdd:PRK12859   3 QLKNKVAVVTGVsrLDGIGAAICKELAEAGADIFFTywtayDKEMPWGVDQDEQIqlqeelLKNGVKVSSMELDLTQNDA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   73 REELMQTVSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFS-QLSHPLLKASGyGSIIFVSSIAGVI 151
Cdd:PRK12859  83 PKELLNKVTEQL-GYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSsQFARGFDKKSG-GRIINMTSGQFQG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  152 SFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLedvsfKKALLSRTPLGRVGEPNEVASLVAF 231
Cdd:PRK12859 161 PMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGWMTEEI-----KQGLLPMFPFGRIGEPKDAARLIKF 235
                        250
                 ....*....|....*....
gi 30684202  232 LCLPAASYITGQTICVDGG 250
Cdd:PRK12859 236 LASEEAEWITGQIIHSEGG 254
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
12-251 7.39e-25

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 98.93  E-value: 7.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   12 ALVTGGASGIGYAIVEELAGFGARIHV-CDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:PRK12938   6 AYVTGGMGGIGTSICQRLHKDGFKVVAgCGPNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEV-GEIDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:PRK12938  85 LVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQTNYSTAKAGIHGFT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  171 KNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKkaLLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGG 250
Cdd:PRK12938 165 MSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPDVLEK--IVATIPVRRLGSPDEIGSIVAWLASEESGFSTGADFSLNGG 242

                 .
gi 30684202  251 L 251
Cdd:PRK12938 243 L 243
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
8-255 1.40e-24

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: 98.76  E-value: 1.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   8 KGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSV-CDVASRPEREELMQTVSSQFdG 86
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVpCDVTKEEDIKTLISVTVERF-G 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGV-IRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASgYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:cd08933  87 RIDCLVNNAGWhPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKS-QGNIINLSSLVGSIGQKQAAPYVATKGA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAPNVINTPL-----SQSYLEDVSFKKALLSRtPLGRVGEPNEVASLVAFLClPAASYI 240
Cdd:cd08933 166 ITAMTKALAVDESRYGVRVNCISPGNIWTPLweelaAQTPDTLATIKEGELAQ-LLGRMGTEAESGLAALFLA-AEATFC 243
                       250
                ....*....|....*
gi 30684202 241 TGQTICVDGGLTVNG 255
Cdd:cd08933 244 TGIDLLLSGGAELGY 258
PRK09186 PRK09186
flagellin modification protein A; Provisional
6-253 1.96e-24

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 98.14  E-value: 1.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSV--CDVASRPEREELMQTVSSQ 83
Cdd:PRK09186   1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLveLDITDQESLEEFLSKSAEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   84 FdGKLNILVsNVGVIRSKPT----TEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVIS-----FD 154
Cdd:PRK09186  81 Y-GKIDGAV-NCAYPRNKDYgkkfFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVApkfeiYE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  155 AGSI-----YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVI----NTPLSQSYLEDVSFKKALlsrtplgrvgEPNEV 225
Cdd:PRK09186 159 GTSMtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIldnqPEAFLNAYKKCCNGKGML----------DPDDI 228
                        250       260
                 ....*....|....*....|....*...
gi 30684202  226 ASLVAFLCLPAASYITGQTICVDGGLTV 253
Cdd:PRK09186 229 CGTLVFLLSDQSKYITGQNIIVDDGFSL 256
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
7-256 2.21e-24

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


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 97.79  E-value: 2.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGA--SGIGYAIVEELAGFGARIHVCDISEA------KLNQSLsewekkgfqvsGS----VCDVASRPERE 74
Cdd:COG0623   3 LKGKRGLITGVAndRSIAWGIAKALHEEGAELAFTYQGEAlkkrvePLAEEL-----------GSalvlPCDVTDDEQID 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  75 ELMQTVSSQFdGKLNILVSNVG----VIRSKPTTEYTEDDF--AFHISsnveaAYHF---SQLSHPLLKasGYGSIIFVS 145
Cdd:COG0623  72 ALFDEIKEKW-GKLDFLVHSIAfapkEELGGRFLDTSREGFllAMDIS-----AYSLvalAKAAEPLMN--EGGSIVTLT 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 146 SIAGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDvsFKKALL---SRTPLGRVGEP 222
Cdd:COG0623 144 YLGAERVVPNYNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKT-LAASGIPG--FDKLLDyaeERAPLGRNVTI 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 30684202 223 NEVASLVAFLCLPAASYITGQTICVDGGLTVNGF 256
Cdd:COG0623 221 EEVGNAAAFLLSDLASGITGEIIYVDGGYHIMGM 254
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
12-236 2.40e-24

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: 97.19  E-value: 2.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEwekKGFQVSGSVCDVASRPEREELMQTVSSQFDGkLNIL 91
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQ---ELEGVLGLAGDVRDEADVRRAVDAMEEAFGG-LDAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  92 VSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLAK 171
Cdd:cd08929  79 VNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSE 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30684202 172 NLACEWAKDGIRANAVAPNVINTPLSQSyLEDVSFKKAllsrtplgrvgePNEVASLVAF-LCLPA 236
Cdd:cd08929 159 AAMLDLREANIRVVNVMPGSVDTGFAGS-PEGQAWKLA------------PEDVAQAVLFaLEMPA 211
PRK12746 PRK12746
SDR family oxidoreductase;
6-251 2.42e-24

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 97.80  E-value: 2.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHV-CDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK12746   3 NLDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 D-----GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAGVISFDAGSIY 159
Cdd:PRK12746  83 QirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEG--RVINISSAEVRLGFTGSIAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK12746 161 GLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLLDDPEIRNFATNSSVFGRIGQVEDIADAVAFLASSDSRW 240
                        250
                 ....*....|..
gi 30684202  240 ITGQTICVDGGL 251
Cdd:PRK12746 241 VTGQIIDVSGGF 252
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
12-250 2.55e-24

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: 97.37  E-value: 2.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLN-QSLSEWEKKG----FQvsgsvCDVASRPEREELMQTVSSQFdG 86
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAaAELQAINPKVkatfVQ-----CDVTSWEQLAAAFKKAIEKF-G 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRSKPTTEYTEDDFAFH--ISSNVEAAYHFSQLSHPLLKAS---GYGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:cd05323  77 RVDILINNAGILDEKSYLFAGKLPPPWEktIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAGLYPAPQFPVYSA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 162 TKGALIQLAKNLACEW-AKDGIRANAVAPNVINTPLSQsylEDVSFKKALLSRTPlgrVGEPNEVAslVAFLCLPAASYI 240
Cdd:cd05323 157 SKHGVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLP---DLVAKEAEMLPSAP---TQSPEVVA--KAIVYLIEDDEK 228
                       250
                ....*....|
gi 30684202 241 TGQTICVDGG 250
Cdd:cd05323 229 NGAIWIVDGG 238
PRK12747 PRK12747
short chain dehydrogenase; Provisional
7-250 2.76e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 97.84  E-value: 2.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGA--RIHVCDISEaKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGAlvAIHYGNRKE-EAEETVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 -----DGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAGVISFDAGSIY 159
Cdd:PRK12747  81 qnrtgSTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNS--RIINISSAATRISLPDFIAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK12747 159 SMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAFNRLGEVEDIADTAAFLASPDSRW 238
                        250
                 ....*....|.
gi 30684202  240 ITGQTICVDGG 250
Cdd:PRK12747 239 VTGQLIDVSGG 249
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
11-194 6.12e-24

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: 96.15  E-value: 6.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGA-RIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLN 89
Cdd:cd05324   2 VALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKY-GGLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  90 ILVSNVGV-----IRSKPTTEYTEDDFafhiSSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISfdagSIYGLTKG 164
Cdd:cd05324  81 ILVNNAGIafkgfDDSTPTREQARETM----KTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLT----SAYGVSKA 152
                       170       180       190
                ....*....|....*....|....*....|
gi 30684202 165 ALIQLAKNLACEWAKDGIRANAVAPNVINT 194
Cdd:cd05324 153 ALNALTRILAKELKETGIKVNACCPGWVKT 182
PLN02253 PLN02253
xanthoxin dehydrogenase
7-260 8.55e-24

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 96.82  E-value: 8.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEaKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PLN02253  16 LLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQD-DLGQNVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDKF-G 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPT----TEYTEDDFAFHIssNVEAAY----HFSQLSHPLLKasgyGSIIFVSSIAGVISFDAGSI 158
Cdd:PLN02253  94 TLDIMVNNAGLTGPPCPdirnVELSEFEKVFDV--NVKGVFlgmkHAARIMIPLKK----GSIVSLCSVASAIGGLGPHA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYL------ED--VSFKKALLSRTPLGRVG-EPNEVASLV 229
Cdd:PLN02253 168 YTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLpedertEDalAGFRAFAGKNANLKGVElTVDDVANAV 247
                        250       260       270
                 ....*....|....*....|....*....|.
gi 30684202  230 AFLCLPAASYITGQTICVDGGLTVNGFSYQP 260
Cdd:PLN02253 248 LFLASDEARYISGLNLMIDGGFTCTNHSLRV 278
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
8-250 4.54e-23

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: 94.45  E-value: 4.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   8 KGMTALVTGGASGIGYAIVEELAGFGARIHVCDI-SEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFDg 86
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADInSENAEKVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFK- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFS-QLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:cd05322  80 RVDLLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCArEFSKLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 166 LIQLAKNLACEWAKDGIRANAVAP-NVINTPLSQSYLEDVSFK---------KALLSRTPLGRVGEPNEVASLVAFLCLP 235
Cdd:cd05322 160 GVGLTQSLALDLAEHGITVNSLMLgNLLKSPMFQSLLPQYAKKlgikeseveQYYIDKVPLKRGCDYQDVLNMLLFYASP 239
                       250
                ....*....|....*
gi 30684202 236 AASYITGQTICVDGG 250
Cdd:cd05322 240 KASYCTGQSINITGG 254
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
9-255 6.21e-23

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: 93.80  E-value: 6.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGAS--GIGYAIVEELAGFGARI---HVCDISEAKLnQSLSEWEKKGFQVSgsVCDVASRPEREELMQTVSSQ 83
Cdd:cd05372   1 GKRILITGIANdrSIAWGIAKALHEAGAELaftYQPEALRKRV-EKLAERLGESALVL--PCDVSNDEEIKELFAEVKKD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  84 FdGKLNILVSNVG----VIRSKPTTEYTEDDF--AFHISsnveaAYHFSQLSHPLLKASG-YGSIIFVSSIAGVISFDAG 156
Cdd:cd05372  78 W-GKLDGLVHSIAfapkVQLKGPFLDTSRKGFlkALDIS-----AYSLVSLAKAALPIMNpGGSIVTLSYLGSERVVPGY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 157 SIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDvsFKKALL---SRTPLGRVGEPNEVASLVAFLC 233
Cdd:cd05372 152 NVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKT-LAASGITG--FDKMLEyseQRAPLGRNVTAEEVGNTAAFLL 228
                       250       260
                ....*....|....*....|..
gi 30684202 234 LPAASYITGQTICVDGGLTVNG 255
Cdd:cd05372 229 SDLSSGITGEIIYVDGGYHIMG 250
PRK12744 PRK12744
SDR family oxidoreductase;
6-252 9.39e-23

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 93.65  E-value: 9.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGAR---IHV-CDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVS 81
Cdd:PRK12744   5 SLKGKVVLIAGGAKNLGGLIARDLAAQGAKavaIHYnSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   82 SQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFsqlshplLKASG-----YGSII-FVSSIAGVISfDA 155
Cdd:PRK12744  85 AAF-GRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFF-------IKEAGrhlndNGKIVtLVTSLLGAFT-PF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  156 GSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPL--SQSYLEDVSFKK--ALLSRTPLGRVGEPNEVASLVAF 231
Cdd:PRK12744 156 YSAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFfyPQEGAEAVAYHKtaAALSPFSKTGLTDIEDIVPFIRF 235
                        250       260
                 ....*....|....*....|.
gi 30684202  232 LcLPAASYITGQTICVDGGLT 252
Cdd:PRK12744 236 L-VTDGWWITGQTILINGGYT 255
PRK07831 PRK07831
SDR family oxidoreductase;
7-247 1.27e-22

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 93.56  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGA-SGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGF--QVSGSVCDVASRPEREELMQTVSSQ 83
Cdd:PRK07831  15 LAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAELGlgRVEAVVCDVTSEAQVDALIDAAVER 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   84 FdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIfVSSiAGVISFDAG---SIYG 160
Cdd:PRK07831  95 L-GRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVI-VNN-ASVLGWRAQhgqAHYA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTP-LSQSYLEDVSFKkaLLSRTPLGRVGEPNEVASLVAFLCLPAASY 239
Cdd:PRK07831 172 AAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPfLAKVTSAELLDE--LAAREAFGRAAEPWEVANVIAFLASDYSSY 249

                 ....*...
gi 30684202  240 ITGQTICV 247
Cdd:PRK07831 250 LTGEVVSV 257
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
10-197 1.44e-22

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: 93.11  E-value: 1.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  10 MTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKgFQVSGSVC--DVASRPEREELMQTVSSQFDgK 87
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAK-FPVKVLPLqlDVSDRESIEAALENLPEEFR-D 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  88 LNILVSNVG-VIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:cd05346  79 IDILVNNAGlALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158
                       170       180       190
                ....*....|....*....|....*....|.
gi 30684202 167 IQLAKNLACEWAKDGIRANAVAPNVINTPLS 197
Cdd:cd05346 159 RQFSLNLRKDLIGTGIRVTNIEPGLVETEFS 189
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-250 1.60e-22

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 94.08  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEA-KLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTvsSQF 84
Cdd:PRK07792   9 DLSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASAlDASDVLDEIRAAGAKAVAVAGDISQRATADELVAT--AVG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 DGKLNILVSNVGVIRSKPTTEYTEDDF----AFHISSNV----EAAYHFSQLShpllKASG---YGSIIFVSSIAGVISF 153
Cdd:PRK07792  87 LGGLDIVVNNAGITRDRMLFNMSDEEWdaviAVHLRGHFlltrNAAAYWRAKA----KAAGgpvYGRIVNTSSEAGLVGP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  154 DAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVintplSQSYLEDVsFKKALLSRT----PLGrvgePNEVASLV 229
Cdd:PRK07792 163 VGQANYGAAKAGITALTLSAARALGRYGVRANAICPRA-----RTAMTADV-FGDAPDVEAggidPLS----PEHVVPLV 232
                        250       260
                 ....*....|....*....|.
gi 30684202  230 AFLCLPAASYITGQTICVDGG 250
Cdd:PRK07792 233 QFLASPAAAEVNGQVFIVYGP 253
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
9-195 1.69e-22

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: 92.70  E-value: 1.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKK----GFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:cd08939   1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEanasGQKVSYISADLSDYEEVEQAFAQAVEKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:cd08939  81 -GPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKF 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 30684202 165 ALIQLAKNLACEWAKDGIRANAVAPNVINTP 195
Cdd:cd08939 160 ALRGLAESLRQELKPYNIRVSVVYPPDTDTP 190
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-249 3.31e-22

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 94.90  E-value: 3.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKlnQSLSEWEKKgfqVSGS--VCDVASRPEREELMQTVSSQF 84
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVPAAG--EALAAVANR---VGGTalALDITAPDAPARIAEHLAERH 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 dGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYhfsQLSHPLLKASGY---GSIIFVSSIAGVisfdAG----S 157
Cdd:PRK08261 283 -GGLDIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPL---RITEALLAAGALgdgGRIVGVSSISGI----AGnrgqT 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  158 IYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSqsyledvsfkkallSRTPL-----GRV-------GEPNEV 225
Cdd:PRK08261 355 NYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMT--------------AAIPFatreaGRRmnslqqgGLPVDV 420
                        250       260
                 ....*....|....*....|....
gi 30684202  226 ASLVAFLCLPAASYITGQTICVDG 249
Cdd:PRK08261 421 AETIAWLASPASGGVTGNVVRVCG 444
PRK06940 PRK06940
short chain dehydrogenase; Provisional
13-252 3.55e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 92.39  E-value: 3.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   13 LVTGGASGIGYAIVEELaGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTvsSQFDGKLNILV 92
Cdd:PRK06940   5 VVVIGAGGIGQAIARRV-GAGKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAAT--AQTLGPVTGLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   93 SNVGVirsKPTTEYTEDDFAFHISSNVEAAYHFSQLShpllkASGyGSIIFVSSIAG---------------------VI 151
Cdd:PRK06940  82 HTAGV---SPSQASPEAILKVDLYGTALVLEEFGKVI-----APG-GAGVVIASQSGhrlpaltaeqeralattpteeLL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  152 SF---------DAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVS--FKKALLSRTPLGRVG 220
Cdd:PRK06940 153 SLpflqpdaieDSLHAYQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAQDELNGPRgdGYRNMFAKSPAGRPG 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 30684202  221 EPNEVASLVAFLCLPAASYITGQTICVDGGLT 252
Cdd:PRK06940 233 TPDEIAALAEFLMGPRGSFITGSDFLVDGGAT 264
PRK06198 PRK06198
short chain dehydrogenase; Provisional
7-248 1.60e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 90.45  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGAR-IHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK06198   4 LDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAF- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGY-GSIIFVSSI---AGViSFDAgsIYGL 161
Cdd:PRK06198  83 GRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMsahGGQ-PFLA--AYCA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINTP----LSQSYL--EDVSFKKALlSRTPLGRVGEPNEVASLVAFLCLP 235
Cdd:PRK06198 160 SKGALATLTRNAAYALLRNRIRVNGLNIGWMATEgedrIQREFHgaPDDWLEKAA-ATQPFGRLLDPDEVARAVAFLLSD 238
                        250
                 ....*....|...
gi 30684202  236 AASYITGQTICVD 248
Cdd:PRK06198 239 ESGLMTGSVIDFD 251
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
6-250 2.15e-21

(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: 89.69  E-value: 2.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLS---------EWEKKGFQvsgSVCDVASRPEREEL 76
Cdd:cd05353   2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNDLGGDRKGSGKSssaadkvvdEIKAAGGK---AVANYDSVEDGEKI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  77 MQTVSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVI-SFDA 155
Cdd:cd05353  79 VKTAIDAF-GRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYgNFGQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 156 GSiYGLTKGALIQLAKNLACEWAKDGIRANAVAPNViNTPLSQSYLEDVSFKKAllsrtplgrvgEPNEVASLVAFLClP 235
Cdd:cd05353 158 AN-YSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAA-GSRMTETVMPEDLFDAL-----------KPEYVAPLVLYLC-H 223
                       250
                ....*....|....*
gi 30684202 236 AASYITGQTICVDGG 250
Cdd:cd05353 224 ESCEVTGGLFEVGAG 238
PRK05650 PRK05650
SDR family oxidoreductase;
13-200 5.48e-21

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 89.33  E-value: 5.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   13 LVTGGASGIGYAIVEELAGFGARIHVCDISEAKLN---QSLSEWEKKGFQVSgsvCDVASRPEREELMQTVSSQFDGkLN 89
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEetlKLLREAGGDGFYQR---CDVRDYSQLTALAQACEEKWGG-ID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQL 169
Cdd:PRK05650  80 VIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVAL 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 30684202  170 AKNLACEWAKDGIRANAVAPNVINTPLSQSY 200
Cdd:PRK05650 160 SETLLVELADDEIGVHVVCPSFFQTNLLDSF 190
PRK07825 PRK07825
short chain dehydrogenase; Provisional
6-197 7.73e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 88.84  E-value: 7.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEkkgfQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG----LVVGGPLDVTDPASFAAFLDAVEADL- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEytEDDFAFH--ISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:PRK07825  77 GPIDVLVNNAGVMPVGPFLD--EPDAVTRriLDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASK 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 30684202  164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLS 197
Cdd:PRK07825 155 HAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
7-203 1.36e-20

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: 87.89  E-value: 1.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDIS-EAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFD 85
Cdd:cd09763   1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTiLPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFERVAREQQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNV-------GVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGvISFDAGSI 158
Cdd:cd09763  81 GRLDILVNNAyaavqliLVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGG-LEYLFNVA 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30684202 159 YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLED 203
Cdd:cd09763 160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPED 204
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
7-196 1.61e-20

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: 87.21  E-value: 1.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEAL-G 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:cd08934  80 RLDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGV 159
                       170       180       190
                ....*....|....*....|....*....|
gi 30684202 167 IQLAKNLACEWAKDGIRANAVAPNVINTPL 196
Cdd:cd08934 160 NAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
PRK06947 PRK06947
SDR family oxidoreductase;
11-250 3.72e-20

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 86.40  E-value: 3.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDIS-EAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLN 89
Cdd:PRK06947   4 VVLITGASRGIGRATAVLAAARGWSVGINYARdAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAF-GRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVSNVGVIR-SKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKAS---GYGSIIFVSSIAGVIsfdaGSI-----YG 160
Cdd:PRK06947  83 ALVNNAGIVApSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrggRGGAIVNVSSIASRL----GSPneyvdYA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKaLLSRTPLGRVGEPNEVASLVAFLCLPAASYI 240
Cdd:PRK06947 159 GSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAAR-LGAQTPLGRAGEADEVAETIVWLLSDAASYV 237
                        250
                 ....*....|
gi 30684202  241 TGQTICVDGG 250
Cdd:PRK06947 238 TGALLDVGGG 247
PRK07985 PRK07985
SDR family oxidoreductase;
7-250 6.59e-20

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 86.59  E-value: 6.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVC-------DISEAKlnQSLSEWEKKGFQVSGsvcDVASRPEREELMQT 79
Cdd:PRK07985  47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAISylpveeeDAQDVK--KIIEECGRKAVLLPG---DLSDEKFARSLVHE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   80 VSSQFDGkLNILVSNVGVIRSKPT-TEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAGVISFDAGSI 158
Cdd:PRK07985 122 AHKALGG-LDIMALVAGKQVAIPDiADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGA--SIITTSSIQAYQPSPHLLD 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 YGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFLCLPAAS 238
Cdd:PRK07985 199 YAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESS 278
                        250
                 ....*....|..
gi 30684202  239 YITGQTICVDGG 250
Cdd:PRK07985 279 YVTAEVHGVCGG 290
PRK09730 PRK09730
SDR family oxidoreductase;
11-250 1.07e-19

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 85.29  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQS-LSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQfDGKLN 89
Cdd:PRK09730   3 IALVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEvVNLITQAGGKAFVLQADISDENQVVAMFTAIDQH-DEPLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVSNVGVIRSKPTTE-YTEDDFAFHISSNV--------EAAYHFSqLSHpllKASGyGSIIFVSSIAGVISFDAGSI-Y 159
Cdd:PRK09730  82 ALVNNAGILFTQCTVEnLTAERINRVLSTNVtgyflccrEAVKRMA-LKH---GGSG-GAIVNVSSAASRLGAPGEYVdY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLED--VSFKKALLsrtPLGRVGEPNEVASLVAFLCLPAA 237
Cdd:PRK09730 157 AASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPgrVDRVKSNI---PMQRGGQPEEVAQAIVWLLSDKA 233
                        250
                 ....*....|...
gi 30684202  238 SYITGQTICVDGG 250
Cdd:PRK09730 234 SYVTGSFIDLAGG 246
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
12-198 1.34e-19

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: 84.58  E-value: 1.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKK-GFQVSGSVCDVASRPEREELMQTVSSQFDgkLNI 90
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKyGVETKTIAADFSAGDDIYERIEKELEGLD--IGI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRSKPT--TEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQ 168
Cdd:cd05356  82 LVNNVGISHSIPEyfLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDF 161
                       170       180       190
                ....*....|....*....|....*....|
gi 30684202 169 LAKNLACEWAKDGIRANAVAPNVINTPLSQ 198
Cdd:cd05356 162 FSRALYEEYKSQGIDVQSLLPYLVATKMSK 191
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
11-197 1.68e-19

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: 84.59  E-value: 1.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLnQSLSEWEKKGFQVSgsVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKL-ESLGELLNDNLEVL--ELDVTDEESIKAAVKEVIERF-GRIDV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:cd05374  78 LVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEALS 157
                       170       180
                ....*....|....*....|....*..
gi 30684202 171 KNLACEWAKDGIRANAVAPNVINTPLS 197
Cdd:cd05374 158 ESLRLELAPFGIKVTIIEPGPVRTGFA 184
PRK06194 PRK06194
hypothetical protein; Provisional
7-200 2.22e-19

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 85.07  E-value: 2.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK06194   4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERF-G 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASG------YGSIIFVSSIAGVISFDAGSIYG 160
Cdd:PRK06194  83 AVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAekdpayEGHIVNTASMAGLLAPPAMGIYN 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30684202  161 LTKGALIQLAKNL--ACEWAKDGIRANAVAPNVINTPLSQSY 200
Cdd:PRK06194 163 VSKHAVVSLTETLyqDLSLVTDQVGASVLCPYFVPTGIWQSE 204
PRK09134 PRK09134
SDR family oxidoreductase;
10-250 2.94e-19

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 84.21  E-value: 2.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELA--GFGARIHvCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGK 87
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAahGFDVAVH-YNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAAL-GP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   88 LNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSII-------------FVSsiagvisfd 154
Cdd:PRK09134  88 ITLLVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVnmidqrvwnlnpdFLS--------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  155 agsiYGLTKGALIQLAKNLACEWAKDgIRANAVAPNvintPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASLVAFL-C 233
Cdd:PRK09134 159 ----YTLSKAALWTATRTLAQALAPR-IRVNAIGPG----PTLPSGRQSPEDFARQHAATPLGRGSTPEEIAAAVRYLlD 229
                        250
                 ....*....|....*..
gi 30684202  234 LPAasyITGQTICVDGG 250
Cdd:PRK09134 230 APS---VTGQMIAVDGG 243
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
124-251 4.03e-19

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 83.51  E-value: 4.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  124 HFSQLSHPLLKASGygSIIFVSSIAGV---------------ISFDAGSI------------YGLTKGALIQLAKNLACE 176
Cdd:PRK12428  77 HLTEALLPRMAPGG--AIVNVASLAGAewpqrlelhkalaatASFDEGAAwlaahpvalatgYQLSKEALILWTMRQAQP 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  177 WAKD-GIRANAVAPNVINTP--------LSQSYLEDVSfkkallsrTPLGRVGEPNEVASLVAFLCLPAASYITGQTICV 247
Cdd:PRK12428 155 WFGArGIRVNCVAPGPVFTPilgdfrsmLGQERVDSDA--------KRMGRPATADEQAAVLVFLCSDAARWINGVNLPV 226

                 ....
gi 30684202  248 DGGL 251
Cdd:PRK12428 227 DGGL 230
PRK06181 PRK06181
SDR family oxidoreductase;
9-201 9.40e-19

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 83.10  E-value: 9.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKL 88
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARF-GGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGVIRSKPTTEyTEDDFAFH--ISSNVEAAYHFSQLSHPLLKASgYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK06181  80 DILVNNAGITMWSRFDE-LTDLSVFErvMRVNYLGAVYCTHAALPHLKAS-RGQIVVVSSLAGLTGVPTRSGYAASKHAL 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 30684202  167 IQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYL 201
Cdd:PRK06181 158 HGFFDSLRIELADDGVAVTVVCPGFVATDIRKRAL 192
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
12-196 2.53e-18

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


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 81.22  E-value: 2.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASrperEELMQTVSSQFD---GKL 88
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTD----EERNQLVIAELEaelGGL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  89 NILVSNVGVIRSKPT-TEYTEDDFAFhISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALI 167
Cdd:cd05350  77 DLVIINAGVGKGTSLgDLSFKAFRET-IDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALS 155
                       170       180
                ....*....|....*....|....*....
gi 30684202 168 QLAKNLACEWAKDGIRANAVAPNVINTPL 196
Cdd:cd05350 156 SLAESLRYDVKKRGIRVTVINPGFIDTPL 184
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
14-229 2.86e-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: 80.96  E-value: 2.86e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  14 VTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEkkGFQVSGSVCDVASRPEREELMQTVSSQFDGKLNILVS 93
Cdd:cd08931   5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELG--AENVVAGALDVTDRAAWAAALADFAAATGGRLDALFN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  94 NVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLAKNL 173
Cdd:cd08931  83 NAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEAL 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30684202 174 ACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPlgrvgePNEVASLV 229
Cdd:cd08931 163 DVEWARHGIRVADVWPWFVDTPILTKGETGAAPKKGLGRVLP------VSDVAKVV 212
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
7-195 3.62e-18

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: 80.90  E-value: 3.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARI-------HVCDISEAK-----LNQSLSEWEKKGFQVSGSVCDVASRPERE 74
Cdd:cd05338   1 LSGKVAFVTGASRGIGRAIALRLAKAGATVvvaaktaSEGDNGSAKslpgtIEETAEEIEAAGGQALPIVVDVRDEDQVR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  75 ELMQTVSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFD 154
Cdd:cd05338  81 ALVEATVDQF-GRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSLRPAR 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 30684202 155 AGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAP-NVINTP 195
Cdd:cd05338 160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPsTAIETP 201
PRK08267 PRK08267
SDR family oxidoreductase;
13-204 8.81e-18

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 80.37  E-value: 8.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   13 LVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEkkGFQVSGSVCDVASRPEREELMQTVSSQFDGKLNILV 92
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELG--AGNAWTGALDVTDRAAWDAALADFAAATGGRLDVLF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   93 SNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLAKN 172
Cdd:PRK08267  83 NNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASAIYGQPGLAVYSATKFAVRGLTEA 162
                        170       180       190
                 ....*....|....*....|....*....|..
gi 30684202  173 LACEWAKDGIRANAVAPNVINTPLSQSYLEDV 204
Cdd:PRK08267 163 LDLEWRRHGIRVADVMPLFVDTAMLDGTSNEV 194
PRK08339 PRK08339
short chain dehydrogenase; Provisional
7-256 1.01e-17

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 80.28  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSE-WEKKGFQVSGSVCDVAsrpEREELMQTVSSQFD 85
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKiKSESNVDVSYIVADLT---KREDLERTVKELKN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 -GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK08339  83 iGEPDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNVVRI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLED------VSFKKALLSRT---PLGRVGEPNEVASLVAFLCLP 235
Cdd:PRK08339 163 SMAGLVRTLAKELGPKGITVNGIMPGIIRTDRVIQLAQDrakregKSVEEALQEYAkpiPLGRLGEPEEIGYLVAFLASD 242
                        250       260
                 ....*....|....*....|.
gi 30684202  236 AASYITGQTICVDGGLTVNGF 256
Cdd:PRK08339 243 LGSYINGAMIPVDGGRLNSVF 263
PRK06123 PRK06123
SDR family oxidoreductase;
12-250 1.81e-17

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 79.05  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   12 ALVTGGASGIGYAIVEELA--GFGARIHVCDISEAKlNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLN 89
Cdd:PRK06123   5 MIITGASRGIGAATALLAAerGYAVCLNYLRNRDAA-EAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDREL-GRLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVSNVGVIRSKPTTEYTEDD-----FAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSI-YGLTK 163
Cdd:PRK06123  83 ALVNNAGILEAQMRLEQMDAArltriFATNVVGSFLCAREAVKRMSTRHGGRG-GAIVNVSSMAARLGSPGEYIdYAASK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  164 GALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKaLLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQ 243
Cdd:PRK06123 162 GAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDR-VKAGIPMGRGGTAEEVARAILWLLSDEASYTTGT 240

                 ....*..
gi 30684202  244 TICVDGG 250
Cdd:PRK06123 241 FIDVSGG 247
PRK05717 PRK05717
SDR family oxidoreductase;
9-252 2.91e-17

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 78.78  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEaklnqslseweKKGFQVSGSV--------CDVASRPEREELMQTV 80
Cdd:PRK05717  10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDR-----------ERGSKVAKALgenawfiaMDVADEAQVAAGVAEV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVI--RSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSI 158
Cdd:PRK05717  79 LGQF-GRLDALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRARQSEPDTEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  159 YGLTKGALIQLAKNLACEWAKDgIRANAVAPNVINT-PLSQSYLEDVSfkKALLSRTPLGRVGEPNEVASLVAFLCLPAA 237
Cdd:PRK05717 157 YAASKGGLLALTHALAISLGPE-IRVNAVSPGWIDArDPSQRRAEPLS--EADHAQHPAGRVGTVEDVAAMVAWLLSRQA 233
                        250
                 ....*....|....*
gi 30684202  238 SYITGQTICVDGGLT 252
Cdd:PRK05717 234 GFVTGQEFVVDGGMT 248
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
7-197 4.34e-17

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


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 77.89  E-value: 4.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSlseweKKGF-QVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:COG3967   3 LTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEA-----AAANpGLHTIVLDVADPASIAALAEQVTAEF- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  86 GKLNILVSNVGVIRSKP--TTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTK 163
Cdd:COG3967  77 PDLNVLINNAGIMRAEDllDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATK 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 30684202 164 GAL--------IQLaknlacewAKDGIRANAVAPNVINTPLS 197
Cdd:COG3967 157 AALhsytqslrHQL--------KDTSVKVIELAPPAVDTDLT 190
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
12-200 4.55e-17

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: 77.72  E-value: 4.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASrpEREELMQTVSSQF-DGKLNI 90
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATELAALGASHSRLHILELDVTD--EIAESAEAVAERLgDAGLDV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISF--DAGSI-YGLTKGAL 166
Cdd:cd05325  79 LINNAGILHSyGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGDntSGGWYsYRASKAAL 158
                       170       180       190
                ....*....|....*....|....*....|....
gi 30684202 167 IQLAKNLACEWAKDGIRANAVAPNVINTPLSQSY 200
Cdd:cd05325 159 NMLTKSLAVELKRDGITVVSLHPGWVRTDMGGPF 192
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
14-195 1.70e-16

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: 76.27  E-value: 1.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  14 VTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNILVS 93
Cdd:cd05360   5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERF-GRIDTWVN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  94 NVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLAKNL 173
Cdd:cd05360  84 NAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESL 163
                       170       180
                ....*....|....*....|....
gi 30684202 174 ACEWAKDG--IRANAVAPNVINTP 195
Cdd:cd05360 164 RAELAHDGapISVTLVQPTAMNTP 187
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
7-198 2.85e-16

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: 76.09  E-value: 2.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKL----NQSLSEWEKKGFQVSGsvcDVASRPEREELMQTVSS 82
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLeevkSECLELGAPSPHVVPL---DMSDLEDAEQVVEEALK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  83 QFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLT 162
Cdd:cd05332  78 LF-GGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAAS 156
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30684202 163 KGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQ 198
Cdd:cd05332 157 KHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAM 192
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
12-253 3.17e-16

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 76.12  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVC-----DVASRPER-EELMQTVSSQFd 85
Cdd:TIGR02685   4 AVVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPNSAVTCqadlsNSATLFSRcEAIIDACFRAF- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    86 GKLNILVSNVGVIRSKP-----------TTEYTEDDFAFHISSNVEAAY----HFSQL---SHPLLKASGYgSIIFVSSI 147
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPllrgdagegvgDKKSLEVQVAELFGSNAIAPYflikAFAQRqagTRAEQRSTNL-SIVNLCDA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   148 AGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKallsRTPLG-RVGEPNEVA 226
Cdd:TIGR02685 162 MTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGLSLLPDAMPFEVQEDYRR----KVPLGqREASAEQIA 237
                         250       260
                  ....*....|....*....|....*..
gi 30684202   227 SLVAFLCLPAASYITGQTICVDGGLTV 253
Cdd:TIGR02685 238 DVVIFLVSPKAKYITGTCIKVDGGLSL 264
PRK07454 PRK07454
SDR family oxidoreductase;
11-232 3.67e-16

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 75.38  E-value: 3.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:PRK07454   8 RALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQF-GCPDV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:PRK07454  87 LINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFT 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684202  171 KNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSF-KKALLSrtplgrvgePNEVASLVAFL 232
Cdd:PRK07454 167 KCLAEEERSHGIRVCTITLGAVNTPLWDTETVQADFdRSAMLS---------PEQVAQTILHL 220
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-250 3.77e-16

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 75.18  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSVCDVASRPEREELMQTVSSQFDG 86
Cdd:PRK05786   3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYG-NIHYVVGDVSSTESARNVIEKAAKVLNA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 kLNILVSNVGVIRSKPTTEYTE-DDFafhISSNVEAAYHFSQLSHPLLKASGygSIIFVSSIAGVISFDAGSI-YGLTKG 164
Cdd:PRK05786  82 -IDGLVVTVGGYVEDTVEEFSGlEEM---LTNHIKIPLYAVNASLRFLKEGS--SIVLVSSMSGIYKASPDQLsYAVAKA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVIntplSQSYLEDVSFKKAllsrTPLGRVGEPNE-VASLVAFLCLPAASYITGQ 243
Cdd:PRK05786 156 GLAKAVEILASELLGRGIRVNGIAPTTI----SGDFEPERNWKKL----RKLGDDMAPPEdFAKVIIWLLTDEADWVDGV 227

                 ....*..
gi 30684202  244 TICVDGG 250
Cdd:PRK05786 228 VIPVDGG 234
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
7-256 7.03e-16

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 74.75  E-value: 7.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGAS--GIGYAIVEELAGFGARIHVCDISEAKlnqslSEWEKKGFQVSGSV-------CDVASRPEREELM 77
Cdd:PRK07370   4 LTGKKALVTGIANnrSIAWGIAQQLHAAGAELGITYLPDEK-----GRFEKKVRELTEPLnpslflpCDVQDDAQIEETF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   78 QTVSSQFdGKLNILVSNVGVIR----SKPTTEYTEDDF--AFHISsnveaAYHFSQLSH---PLLKASGygSIIFVSSIA 148
Cdd:PRK07370  79 ETIKQKW-GKLDILVHCLAFAGkeelIGDFSATSREGFarALEIS-----AYSLAPLCKaakPLMSEGG--SIVTLTYLG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  149 GVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVASL 228
Cdd:PRK07370 151 GVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAVGGILDMIHHVEEKAPLRRTVTQTEVGNT 230
                        250       260
                 ....*....|....*....|....*...
gi 30684202  229 VAFLCLPAASYITGQTICVDGGLTVNGF 256
Cdd:PRK07370 231 AAFLLSDLASGITGQTIYVDAGYCIMGM 258
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
7-244 7.97e-16

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: 74.54  E-value: 7.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfQVSGSV----CDVASRPEREELMQTVSS 82
Cdd:cd05340   2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEG-GRQPQWfildLLTCTSENCQQLAQRIAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  83 QFdGKLNILVSNVGVIRSK-PTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:cd05340  81 NY-PRLDGVLHNAGLLGDVcPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSqsyledvsfKKALLSRTPLgRVGEPNEVASLVAFLCLPAASYIT 241
Cdd:cd05340 160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMR---------ASAFPTEDPQ-KLKTPADIMPLYLWLMGDDSRRKT 229

                ...
gi 30684202 242 GQT 244
Cdd:cd05340 230 GMT 232
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
4-229 1.50e-15

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: 74.09  E-value: 1.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   4 RWSlkGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGfqvSGSV----CDVASRPEREELMQT 79
Cdd:cd05343   3 RWR--GRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAG---YPTLfpyqCDLSNEEQILSMFSA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  80 VSSQFDGkLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGY--GSIIFVSSIAG--VISFDA 155
Cdd:cd05343  78 IRTQHQG-VDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGhrVPPVSV 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30684202 156 GSIYGLTKGALIQLAKNLACE--WAKDGIRANAVAPNVINTPLSQSYLEDVSFKKAL-LSRTPlgrVGEPNEVASLV 229
Cdd:cd05343 157 FHFYAATKHAVTALTEGLRQElrEAKTHIRATSISPGLVETEFAFKLHDNDPEKAAAtYESIP---CLKPEDVANAV 230
PRK09072 PRK09072
SDR family oxidoreductase;
7-196 1.79e-15

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 73.82  E-value: 1.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLnQSLSEWEKKGFQVSGSVCDVASRPEREELMQtVSSQFDG 86
Cdd:PRK09072   3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKL-EALAARLPYPGRHRWVVADLTSEAGREAVLA-RAREMGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 kLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:PRK09072  81 -INVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFAL 159
                        170       180       190
                 ....*....|....*....|....*....|
gi 30684202  167 IQLAKNLACEWAKDGIRANAVAPNVINTPL 196
Cdd:PRK09072 160 RGFSEALRRELADTGVRVLYLAPRATRTAM 189
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
11-243 8.68e-15

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: 71.55  E-value: 8.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELA--GFGARIHVCDISEAKLnQSLSEWEKKGFQVSGSVCDVASrPEREELMQTVSSQFDGKL 88
Cdd:cd05367   1 VIILTGASRGIGRALAEELLkrGSPSVVVLLARSEEPL-QELKEELRPGLRVTTVKADLSD-AAGVEQLLEAIRKLDGER 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  89 NILVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGY-GSIIFVSSIAGVISFDAGSIYGLTKGAL 166
Cdd:cd05367  79 DLLINNAGSLGPvSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAAR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 167 IQLAKNLACEwaKDGIRANAVAPNVINTPLSQSYLEDvSFKKALLSRTP----LGRVGEPNEVASLVAFLcLPAASYITG 242
Cdd:cd05367 159 DMFFRVLAAE--EPDVRVLSYAPGVVDTDMQREIRET-SADPETRSRFRslkeKGELLDPEQSAEKLANL-LEKDKFESG 234

                .
gi 30684202 243 Q 243
Cdd:cd05367 235 A 235
PRK05872 PRK05872
short chain dehydrogenase; Provisional
1-226 1.55e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 71.54  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNqSLSEWEKKGFQVSGSVCDVASRPEREELMQTV 80
Cdd:PRK05872   1 GPPMTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELA-ALAAELGGDDRVLTVVADVTDLAAMQAAAEEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHP-LLKASGYgsIIFVSSIAGVISFDAGSIY 159
Cdd:PRK05872  80 VERF-GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPaLIERRGY--VLQVSSLAAFAAAPGMAAY 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30684202  160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTP--LGRVGEPNEVA 226
Cdd:PRK05872 157 CASKAGVEAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADADLPAFRELRARLPwpLRRTTSVEKCA 225
PRK05855 PRK05855
SDR family oxidoreductase;
9-199 1.96e-14

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 72.71  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKL 88
Cdd:PRK05855 315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEH-GVP 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGY-GSIIFVSSIAGVISFDAGSIYGLTKGALI 167
Cdd:PRK05855 394 DIVVNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTgGHIVNVASAAAYAPSRSLPAYATSKAAVL 473
                        170       180       190
                 ....*....|....*....|....*....|..
gi 30684202  168 QLAKNLACEWAKDGIRANAVAPNVINTPLSQS 199
Cdd:PRK05855 474 MLSECLRAELAAAGIGVTAICPGFVDTNIVAT 505
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
7-200 2.73e-14

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 70.13  E-value: 2.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGAR---IHVCDI-SEAKLNqslsewEKKGFQVSGSVCDVASRPEREELMQTVSS 82
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKkvyAAVRDPgSAAHLV------AKYGDKVVPLRLDVTDPESIKAAAAQAKD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  83 qfdgkLNILVSNVGVirSKPTTEYTEDDFA---FHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIY 159
Cdd:cd05354  75 -----VDVVINNAGV--LKPATLLEEGALEalkQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMGTY 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 30684202 160 GLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSY 200
Cdd:cd05354 148 SASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGA 188
PRK08263 PRK08263
short chain dehydrogenase; Provisional
1-189 3.42e-14

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 70.45  E-value: 3.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWslkgmtaLVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDvasrpeREELMQTV 80
Cdd:PRK08263   2 MEKVW-------FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTD------RAAVFAAV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFD--GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSI 158
Cdd:PRK08263  69 ETAVEhfGRLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGI 148
                        170       180       190
                 ....*....|....*....|....*....|.
gi 30684202  159 YGLTKGALIQLAKNLACEWAKDGIRANAVAP 189
Cdd:PRK08263 149 YHASKWALEGMSEALAQEVAEFGIKVTLVEP 179
PRK07832 PRK07832
SDR family oxidoreductase;
10-196 7.91e-14

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 69.30  E-value: 7.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVC-DVASRPEREELMQTVSSQFdGKL 88
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRAlDISDYDAVAAFAADIHAAH-GSM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQ-LSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALI 167
Cdd:PRK07832  80 DVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIEtFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLR 159
                        170       180
                 ....*....|....*....|....*....
gi 30684202  168 QLAKNLACEWAKDGIRANAVAPNVINTPL 196
Cdd:PRK07832 160 GLSEVLRFDLARHGIGVSVVVPGAVKTPL 188
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
7-257 9.40e-14

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 69.23  E-value: 9.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGAS--GIGYAIVEELAGFGArihvcDISEAKLNQSLSEWEKKGFQVSGS----VCDVASRPEREELMQTV 80
Cdd:PRK08690   4 LQGKKILITGMISerSIAYGIAKACREQGA-----ELAFTYVVDKLEERVRKMAAELDSelvfRCDVASDDEINQVFADL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFDGkLNILVSNVGVirskPTTEYTEDDF-------AFHISSNVeAAYHFSQLS---HPLLKASGyGSIIFVSSIAGV 150
Cdd:PRK08690  79 GKHWDG-LDGLVHSIGF----APKEALSGDFldsisreAFNTAHEI-SAYSLPALAkaaRPMMRGRN-SAIVALSYLGAV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  151 ISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDvsFKKAL---LSRTPLGRVGEPNEVAS 227
Cdd:PRK08690 152 RAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKT-LAASGIAD--FGKLLghvAAHNPLRRNVTIEEVGN 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 30684202  228 LVAFLCLPAASYITGQTICVDGGLTVNGFS 257
Cdd:PRK08690 229 TAAFLLSDLSSGITGEITYVDGGYSINALS 258
PRK07791 PRK07791
short chain dehydrogenase; Provisional
7-250 1.51e-13

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 68.93  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDI---------SEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELM 77
Cdd:PRK07791   4 LDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNDIgvgldgsasGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAANLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   78 QTVSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHIssNVEAAYHFSQLSHpllkASGY------------GSIIFVS 145
Cdd:PRK07791  84 DAAVETF-GGLDVLVNNAGILRDRMIANMSEEEWDAVI--AVHLKGHFATLRH----AAAYwraeskagravdARIINTS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  146 SIAGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPnVINTPLSQSYLedvsfkkALLSRTPLGrvGE---- 221
Cdd:PRK07791 157 SGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP-AARTRMTETVF-------AEMMAKPEE--GEfdam 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 30684202  222 -PNEVASLVAFLCLPAASYITGQTICVDGG 250
Cdd:PRK07791 227 aPENVSPLVVWLGSAESRDVTGKVFEVEGG 256
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
9-226 3.85e-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: 67.49  E-value: 3.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGASGIGYAIVEELAGFGARIHV-C-DISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFDg 86
Cdd:cd09807   1 GKTVIITGANTGIGKETARELARRGARVIMaCrDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKSIRAFAAEFLAEED- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  87 KLNILVSNVGVIRSKPTTeyTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIA---GVISFD--------- 154
Cdd:cd09807  80 RLDVLINNAGVMRCPYSK--TEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAhkaGKINFDdlnseksyn 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30684202 155 AGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSFKKALLSRTPLGRVGEPNEVA 226
Cdd:cd09807 158 TGFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTGIHHLFLSTLLNPLFWPFVKTPREGA 229
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
12-255 6.72e-13

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 68.02  E-value: 6.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQ--VSGSVCDVASRPEREELMQTVSSQFDGkLN 89
Cdd:COG3347 428 ALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGAdaVDATDVDVTAEAAVAAAFGFAGLDIGG-SD 506
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  90 ILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIfvsSIAGVISFDAGSiYGLTKGALIQL 169
Cdd:COG3347 507 IGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSS---VFAVSKNAAAAA-YGAAAAATAKA 582
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 170 AKNLACEWAKDGIRANAVAPNVINTPLsqsyLEDVSFK-----KALLSRTPLGRVGEPNEVASLVAFLCLPAASYITGQT 244
Cdd:COG3347 583 AAQHLLRALAAEGGANGINANRVNPDA----VLDGSAIwasaaRAERAAAYGIGNLLLEEVYRKRVALAVLVLAEDIAEA 658
                       250
                ....*....|.
gi 30684202 245 ICVDGGLTVNG 255
Cdd:COG3347 659 AAFFASDGGNK 669
PRK08219 PRK08219
SDR family oxidoreductase;
10-225 3.10e-12

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 64.18  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELAGfGARIHVCDISEAKLNQSLSEWEkkgfQVSGSVCDVAsrpeREELMQTVSSQFDgKLN 89
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAELP----GATPFPVDLT----DPEAIAAAVEQLG-RLD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSSIAGVISFDAGSIYGLTKGALIQL 169
Cdd:PRK08219  74 VLVHNAGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGLRANPGWGSYAASKFALRAL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30684202  170 AKNLACEWAkDGIRANAVAPNVINTPLSQ-------------SYLEDVSFKKALLSRTPLGRVGEPNEV 225
Cdd:PRK08219 153 ADALREEEP-GNVRVTSVHPGRTDTDMQRglvaqeggeydpeRYLRPETVAKAVRFAVDAPPDAHITEV 220
PRK06196 PRK06196
oxidoreductase; Provisional
7-197 3.39e-12

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 65.09  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEkkgfQVSGSVCDVASrPEREELMQTVSSQFDG 86
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGID----GVEVVMLDLAD-LESVRAFAERFLDSGR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSkPTTeYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVIS------------FD 154
Cdd:PRK06196  99 RIDILINNAGVMAC-PET-RVGDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRSpirwddphftrgYD 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 30684202  155 AGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLS 197
Cdd:PRK06196 177 KWLAYGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPLQ 219
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
1-253 4.66e-12

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 64.19  E-value: 4.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWSLKGMTALVTGGASG--IGYAIVEELAGFGARIHVCDISE--AKLNQSLSEwekkgfQVSGSV---CDVASRPER 73
Cdd:PRK07533   2 MQPLLPLAGKRGLVVGIANEqsIAWGCARAFRALGAELAVTYLNDkaRPYVEPLAE------ELDAPIflpLDVREPGQL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   74 EELMQTVSSQFdGKLNILVSNV----------GVIRSkptteyTEDDFAFHISSNVEAAYHFSQLSHPLLKASGygSIIF 143
Cdd:PRK07533  76 EAVFARIAEEW-GRLDFLLHSIafapkedlhgRVVDC------SREGFALAMDVSCHSFIRMARLAEPLMTNGG--SLLT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  144 VSSIAGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPlSQSYLEDvsFKkALL----SRTPLGRV 219
Cdd:PRK07533 147 MSYYGAEKVVENYNLMGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKTR-AASGIDD--FD-ALLedaaERAPLRRL 222
                        250       260       270
                 ....*....|....*....|....*....|....
gi 30684202  220 GEPNEVASLVAFLCLPAASYITGQTICVDGGLTV 253
Cdd:PRK07533 223 VDIDDVGAVAAFLASDAARRLTGNTLYIDGGYHI 256
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
13-249 4.98e-12

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: 63.50  E-value: 4.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  13 LVTGGASGIGYAIVEELAGFGARIHVCDISEaklnqslSEWEKKGFQVSGSVCDVasrperEELMQTVSS--QFDGKLNI 90
Cdd:cd05334   5 LVYGGRGALGSAVVQAFKSRGWWVASIDLAE-------NEEADASIIVLDSDSFT------EQAKQVVASvaRLSGKVDA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVS-----NVGVIRSKPTTEYTEDDFAFHISSNVEAayhfSQLSHPLLKasGYGSIIFVSSIAGViSFDAGSI-YGLTKG 164
Cdd:cd05334  72 LICvaggwAGGSAKSKSFVKNWDLMWKQNLWTSFIA----SHLATKHLL--SGGLLVLTGAKAAL-EPTPGMIgYGAAKA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 165 ALIQLAKNLACEW--AKDGIRANAVAPNVINTPLSQSYLEDVSFKkallSRTPlgrvgePNEVASLVAFLCLPAASYITG 242
Cdd:cd05334 145 AVHQLTQSLAAENsgLPAGSTANAILPVTLDTPANRKAMPDADFS----SWTP------LEFIAELILFWASGAARPKSG 214

                ....*..
gi 30684202 243 QTICVDG 249
Cdd:cd05334 215 SLIPVVT 221
PRK08264 PRK08264
SDR family oxidoreductase;
6-198 6.61e-12

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 63.37  E-value: 6.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARihvcdiseaklnqslsewekkgfQVSGSVCDVASRPEREELMQTVssQFD 85
Cdd:PRK08264   3 DIKGKVVLVTGANRGIGRAFVEQLLARGAA-----------------------KVYAAARDPESVTDLGPRVVPL--QLD 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 --------------GKLNILVSNVGVIRSK-PTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGV 150
Cdd:PRK08264  58 vtdpasvaaaaeaaSDVTILVNNAGIFRTGsLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSW 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 30684202  151 ISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQ 198
Cdd:PRK08264 138 VNFPNLGTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDMAA 185
PRK06182 PRK06182
short chain dehydrogenase; Validated
11-195 6.22e-11

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 61.13  E-value: 6.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCdiseAKLNQSLSEWEKKGFQVSGsvCDVASRPEREELMQTVSSQfDGKLNI 90
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQGYTVYGA----ARRVDKMEDLASLGVHPLS--LDVTDEASIKAAVDTIIAE-EGRIDV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:PRK06182  78 LVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALEGFS 157
                        170       180
                 ....*....|....*....|....*
gi 30684202  171 KNLACEWAKDGIRANAVAPNVINTP 195
Cdd:PRK06182 158 DALRLEVAPFGIDVVVIEPGGIKTE 182
PRK05866 PRK05866
SDR family oxidoreductase;
7-196 6.39e-11

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 61.30  E-value: 6.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdG 86
Cdd:PRK05866  38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRI-G 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVG-VIRsKPTTEYTEddfAFHISSNVEAAYHFSQLS-----HPLLKASGYGSIIFVSSiAGVIS-----Fda 155
Cdd:PRK05866 117 GVDILINNAGrSIR-RPLAESLD---RWHDVERTMVLNYYAPLRlirglAPGMLERGDGHIINVAT-WGVLSeasplF-- 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 30684202  156 gSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPL 196
Cdd:PRK05866 190 -SVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPM 229
PRK07109 PRK07109
short chain dehydrogenase; Provisional
11-195 8.29e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 61.09  E-value: 8.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:PRK07109  10 VVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEEL-GPIDT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:PRK07109  89 WVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFT 168
                        170       180
                 ....*....|....*....|....*..
gi 30684202  171 KNLACEWAKDG--IRANAVAPNVINTP 195
Cdd:PRK07109 169 DSLRCELLHDGspVSVTMVQPPAVNTP 195
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
12-196 9.56e-11

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: 59.52  E-value: 9.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAgfgarIHVCDISEAklnqslsewekkGFQVSGSVCDVASRPEREELMQTVssqfdGKLNIL 91
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLS-----AHGHEVITA------------GRSSGDYQVDITDEASIKALFEKV-----GHFDAI 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  92 VSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLkASGyGSIIFVSSIAGVISFDAGSIYGLTKGALIQLAK 171
Cdd:cd11731  59 VSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVRHGLPYL-NDG-GSITLTSGILAQRPIPGGAAAATVNGALEGFVR 136
                       170       180
                ....*....|....*....|....*
gi 30684202 172 NLACEWAkDGIRANAVAPNVINTPL 196
Cdd:cd11731 137 AAAIELP-RGIRINAVSPGVVEESL 160
PRK08703 PRK08703
SDR family oxidoreductase;
6-195 9.76e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 60.33  E-value: 9.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSV-CDV--ASRPEREELMQTVSS 82
Cdd:PRK08703   3 TLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAIrFDLmsAEEKEFEQFAATIAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   83 QFDGKLNILVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:PRK08703  83 ATQGKLDGIVHCAGYFYAlSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGFGA 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 30684202  162 TKGALIQLAKNLACEWAKDG-IRANAVAPNVINTP 195
Cdd:PRK08703 163 SKAALNYLCKVAADEWERFGnLRANVLVPGPINSP 197
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
7-189 1.09e-10

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 60.27  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSV-CDV--ASRPEREELMQTVSSQ 83
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIpLDLltATPQNYQQLADTIEEQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   84 FdGKLNILVSNVGVI--RSkPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:PRK08945  90 F-GRLDGVLHNAGLLgeLG-PMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRANWGAYAV 167
                        170       180
                 ....*....|....*....|....*...
gi 30684202  162 TKGALIQLAKNLACEWAKDGIRANAVAP 189
Cdd:PRK08945 168 SKFATEGMMQVLADEYQGTNLRVNCINP 195
PRK07201 PRK07201
SDR family oxidoreductase;
2-182 1.48e-10

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 61.12  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    2 DKRWSLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVS 81
Cdd:PRK07201 364 DLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDIL 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   82 SQFDGkLNILVSNVGviRS-KPTTEYTED---DFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIaGVIS----F 153
Cdd:PRK07201 444 AEHGH-VDYLVNNAG--RSiRRSVENSTDrfhDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSI-GVQTnaprF 519
                        170       180
                 ....*....|....*....|....*....
gi 30684202  154 DAgsiYGLTKGALIQLAKNLACEWAKDGI 182
Cdd:PRK07201 520 SA---YVASKAALDAFSDVAASETLSDGI 545
PRK06179 PRK06179
short chain dehydrogenase; Provisional
11-202 5.68e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 58.38  E-value: 5.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAgfgarihvcdiseaklnqslseweKKGFQVSGSV----------------CDVASRPERE 74
Cdd:PRK06179   6 VALVTGASSGIGRATAEKLA------------------------RAGYRVFGTSrnparaapipgvelleLDVTDDASVQ 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   75 ELMQTVSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFD 154
Cdd:PRK06179  62 AAVDEVIARA-GRIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAP 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 30684202  155 AGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLE 202
Cdd:PRK06179 141 YMALYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPE 188
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
12-199 1.04e-09

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: 56.76  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEwekkgFQVSGSVCDVASRPEREELMQTvssqfDGKLNIL 91
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAE-----VGALARPADVAAELEVWALAQE-----LGPLDLL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  92 VSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGsiIFVSSIAGVISFDAGSIYGLTKGALIQLAK 171
Cdd:cd11730  71 VYAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARL--VFLGAYPELVMLPGLSAYAAAKAALEAYVE 148
                       170       180
                ....*....|....*....|....*...
gi 30684202 172 NLACEWakDGIRANAVAPNVINTPLSQS 199
Cdd:cd11730 149 VARKEV--RGLRLTLVRPPAVDTGLWAP 174
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
11-151 3.14e-09

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: 54.80  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202     11 TALVTGGASGIGYAIVEELAGFGARiHVC-----DISEAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:smart00822   2 TYLITGGLGGLGRALARWLAERGAR-RLVllsrsGPDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVE- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30684202     86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPL-LKAsgygsIIFVSSIAGVI 151
Cdd:smart00822  80 GPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADLpLDF-----FVLFSSIAGVL 141
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
11-195 3.82e-09

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: 55.47  E-value: 3.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSL-SEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFdGKLN 89
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLvDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEI-GPLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  90 ILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGV------ISFDAGsiygltK 163
Cdd:cd05373  80 VLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLrgragfAAFAGA------K 153
                       170       180       190
                ....*....|....*....|....*....|...
gi 30684202 164 GALIQLAKNLACEWAKDGIR-ANAVAPNVINTP 195
Cdd:cd05373 154 FALRALAQSMARELGPKGIHvAHVIIDGGIDTD 186
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
6-250 5.57e-09

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 55.12  E-value: 5.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGAS--GIGYAIVEELAGFGARI---HVCDISE---AKLNQSLSEWEKKGFQvsgsvCDVASRPEREELM 77
Cdd:PRK08594   4 SLEGKTYVVMGVANkrSIAWGIARSLHNAGAKLvftYAGERLEkevRELADTLEGQESLLLP-----CDVTSDEEITACF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   78 QTVSSQfdgklnilvsnVGVI-----------RSKPTTEYTEDDF-AFHISSNVeAAYHFSQLSH---PLLKASGygSII 142
Cdd:PRK08594  79 ETIKEE-----------VGVIhgvahciafanKEDLRGEFLETSRdGFLLAQNI-SAYSLTAVAReakKLMTEGG--SIV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  143 FVSSIAGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDV-SFKKALLSRTPLGRVGE 221
Cdd:PRK08594 145 TLTYLGGERVVQNYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRT-LSAKGVGGFnSILKEIEERAPLRRTTT 223
                        250       260
                 ....*....|....*....|....*....
gi 30684202  222 PNEVASLVAFLCLPAASYITGQTICVDGG 250
Cdd:PRK08594 224 QEEVGDTAAFLFSDLSRGVTGENIHVDSG 252
PRK08017 PRK08017
SDR family oxidoreductase;
11-198 1.35e-08

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 54.32  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIhvcdISEAKLNQSLSEWEKKGFqvSGSVCDVASRPEREELMQTVSSQFDGKLNI 90
Cdd:PRK08017   4 SVLITGCSSGIGLEAALELKRRGYRV----LAACRKPDDVARMNSLGF--TGILLDLDDPESVERAADEVIALTDNRLYG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:PRK08017  78 LFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWS 157
                        170       180
                 ....*....|....*....|....*...
gi 30684202  171 KNLACEWAKDGIRANAVAPNVINTPLSQ 198
Cdd:PRK08017 158 DALRMELRHSGIKVSLIEPGPIRTRFTD 185
PRK09009 PRK09009
SDR family oxidoreductase;
10-227 1.47e-08

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 53.91  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEEL-AGF-GARIHvcdiseAKLNQSLSEWEKKGFQ-VSGSVCDvasrperEELMQTVSSQFDg 86
Cdd:PRK09009   1 MNILIVGGSGGIGKAMVKQLlERYpDATVH------ATYRHHKPDFQHDNVQwHALDVTD-------EAEIKQLSEQFT- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVIRSK-----PTTEYTEDDFAFH-ISSNVEA----AYHFSqlshPLLKASgygsiifVSSIAGVISFDAG 156
Cdd:PRK09009  67 QLDWLINCVGMLHTQdkgpeKSLQALDADFFLQnITLNTLPslllAKHFT----PKLKQS-------ESAKFAVISAKVG 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  157 SI----------YGLTKGALIQLAKNLACEWA---KDGIRAnAVAPNVINTPLSQSYLEDVsfkkallsrtPLGRVGEPN 223
Cdd:PRK09009 136 SIsdnrlggwysYRASKAALNMFLKTLSIEWQrslKHGVVL-ALHPGTTDTALSKPFQQNV----------PKGKLFTPE 204

                 ....
gi 30684202  224 EVAS 227
Cdd:PRK09009 205 YVAQ 208
PRK05693 PRK05693
SDR family oxidoreductase;
11-199 2.61e-08

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 53.64  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHvcdiSEAKLNQSLSEWEKKGFQVSGsvCDVASRPEREELMQTVSSQFdGKLNI 90
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVW----ATARKAEDVEALAAAGFTAVQ--LDVNDGAALARLAEELEAEH-GGLDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKaSGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLA 170
Cdd:PRK05693  76 LINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLR-RSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALS 154
                        170       180
                 ....*....|....*....|....*....
gi 30684202  171 KNLACEWAKDGIRANAVAPNVINTPLSQS 199
Cdd:PRK05693 155 DALRLELAPFGVQVMEVQPGAIASQFASN 183
PRK05854 PRK05854
SDR family oxidoreductase;
7-196 3.79e-08

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 53.15  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKK--GFQVSGSVCDVASRPEREELMQTVSSqf 84
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTAvpDAKLSLRALDLSSLASVAALGEQLRA-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 DGK-LNILVSNVGVIRSkPTTEYTEDDFAFHISSNVEAayHFSQLSH--PLLKAsGYGSIIFVSSIA---GVI------- 151
Cdd:PRK05854  90 EGRpIHLLINNAGVMTP-PERQTTADGFELQFGTNHLG--HFALTAHllPLLRA-GRARVTSQSSIAarrGAInwddlnw 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30684202  152 --SFDAGSIYGLTKGALIQLAKNL-----ACEWakdGIRANAVAPNVINTPL 196
Cdd:PRK05854 166 erSYAGMRAYSQSKIAVGLFALELdrrsrAAGW---GITSNLAHPGVAPTNL 214
PRK06914 PRK06914
SDR family oxidoreductase;
11-230 5.76e-08

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 52.33  E-value: 5.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQ-----VSGSVCDVASRPEREELMQTVssqfd 85
Cdd:PRK06914   5 IAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQqnikvQQLDVTDQNSIHNFQLVLKEI----- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK06914  80 GRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSKYA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30684202  166 LIQLAKNLACEWAKDGIRANAVAPNVINTP-------LSQSYLEDVSFKKALLSR------TPLGRVGEPNEVASLVA 230
Cdd:PRK06914 160 LEGFSESLRLELKPFGIDVALIEPGSYNTNiwevgkqLAENQSETTSPYKEYMKKiqkhinSGSDTFGNPIDVANLIV 237
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
7-255 7.26e-08

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 52.13  E-value: 7.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGA--SGIGYAIVEELAGFGARIHVCDISEAkLNQSLSEWEKKGFQVS-----GSVCDVA---------SR 70
Cdd:PRK06300   6 LTGKIAFIAGIGddQGYGWGIAKALAEAGATILVGTWVPI-YKIFSQSLELGKFDASrklsnGSLLTFAkiypmdasfDT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   71 PE------RE-------------ELMQTVSSQFdGKLNILVSNV--GVIRSKPTTEYTEDDFAFHISSnveAAYHF-SQL 128
Cdd:PRK06300  85 PEdvpeeiREnkrykdlsgytisEVAEQVKKDF-GHIDILVHSLanSPEISKPLLETSRKGYLAALST---SSYSFvSLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  129 SH--PLLKASGYG-SIIFVSSIAGVISFDAGsiYGLTKGALIQLAKNLACEWAKD-GIRANAVAPNvintPLSQSYLEDV 204
Cdd:PRK06300 161 SHfgPIMNPGGSTiSLTYLASMRAVPGYGGG--MSSAKAALESDTKVLAWEAGRRwGIRVNTISAG----PLASRAGKAI 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30684202  205 SFKKAL----LSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGGLTVNG 255
Cdd:PRK06300 235 GFIERMvdyyQDWAPLPEPMEAEQVGAAAAFLVSPLASAITGETLYVDHGANVMG 289
PRK07984 PRK07984
enoyl-ACP reductase FabI;
7-253 1.01e-07

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 51.83  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGAS--GIGYAIVEELAGFGARIHVCDISEaKLNQSLSEWEKkgfQVSGSV---CDVASRPEREEL---MQ 78
Cdd:PRK07984   4 LSGKRILVTGVASklSIAYGIAQAMHREGAELAFTYQND-KLKGRVEEFAA---QLGSDIvlpCDVAEDASIDAMfaeLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   79 TVSSQFDGklniLVSNVGVirsKPTTEYTEDDF------AFHISSNVeAAYHFSQLSHPLLKASGYGSIIFVSSIAGV-I 151
Cdd:PRK07984  80 KVWPKFDG----FVHSIGF---APGDQLDGDYVnavtreGFKIAHDI-SSYSFVAMAKACRSMLNPGSALLTLSYLGAeR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  152 SFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDvsFKKALL---SRTPLGRVGEPNEVASL 228
Cdd:PRK07984 152 AIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRT-LAASGIKD--FRKMLAhceAVTPIRRTVTIEDVGNS 228
                        250       260
                 ....*....|....*....|....*
gi 30684202  229 VAFLCLPAASYITGQTICVDGGLTV 253
Cdd:PRK07984 229 AAFLCSDLSAGISGEVVHVDGGFSI 253
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
10-250 1.16e-07

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 51.09  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTA--LVTGGASGIGYAIVEELAGFGARIHVCDISEaklNQSLSEWEKKGfqVSGSVCDVASRPEREELMQTVSSQFDGk 87
Cdd:PRK06483   1 MPApiLITGAGQRIGLALAWHLLAQGQPVIVSYRTH---YPAIDGLRQAG--AQCIQADFSTNAGIMAFIDELKQHTDG- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   88 LNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGS--IIFVSS----------IAgvisfda 155
Cdd:PRK06483  75 LRAIIHNASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHAAsdIIHITDyvvekgsdkhIA------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  156 gsiYGLTKGALIQLAKNLACEWAKDgIRANAVAPNVI--NTPlsqsylEDVSFKKALLSRTPLGRVGEPNEVASLVAFLC 233
Cdd:PRK06483 148 ---YAASKAALDNMTLSFAAKLAPE-VKVNSIAPALIlfNEG------DDAAYRQKALAKSLLKIEPGEEEIIDLVDYLL 217
                        250
                 ....*....|....*..
gi 30684202  234 lpAASYITGQTICVDGG 250
Cdd:PRK06483 218 --TSCYVTGRSLPVDGG 232
PRK08278 PRK08278
SDR family oxidoreductase;
6-189 1.45e-07

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 51.06  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIhvcdISEAK-----------LNQSLSEWEKKGFQVSGSVCDVASRPERE 74
Cdd:PRK08278   3 SLSGKTLFITGASRGIGLAIALRAARDGANI----VIAAKtaephpklpgtIHTAAEEIEAAGGQALPLVGDVRDEDQVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   75 ELMQTVSSQFdGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIfvsSIAGVISFD 154
Cdd:PRK08278  79 AAVAKAVERF-GGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHIL---TLSPPLNLD 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30684202  155 -----AGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAP 189
Cdd:PRK08278 155 pkwfaPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
11-214 1.95e-07

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: 50.92  E-value: 1.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGA-RIHV-CDISEAKLNQSLseWEKKGFQVSGSV----CDVASrpeREELMQTVSSQF 84
Cdd:cd09806   2 VVLITGCSSGIGLHLAVRLASDPSkRFKVyATMRDLKKKGRL--WEAAGALAGGTLetlqLDVCD---SKSVAAAVERVT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  85 DGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:cd09806  77 ERHVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDVYCASKF 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 30684202 165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQSYLEDVSfkKALLSRT 214
Cdd:cd09806 157 ALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSPE--EVLDRTA 204
PRK07775 PRK07775
SDR family oxidoreductase;
11-189 2.40e-07

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 50.52  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELA--GF----GARihvcdiSEAKLNQSLSEWEKKGFQVSGSVCDVASrPEREELMQTVSSQF 84
Cdd:PRK07775  12 PALVAGASSGIGAATAIELAaaGFpvalGAR------RVEKCEELVDKIRADGGEAVAFPLDVTD-PDSVKSFVAQAEEA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   85 DGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK07775  85 LGEIEVLVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKA 164
                        170       180
                 ....*....|....*....|....*
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAP 189
Cdd:PRK07775 165 GLEAMVTNLQMELEGTGVRASIVHP 189
PRK06139 PRK06139
SDR family oxidoreductase;
6-195 3.12e-07

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 50.49  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQVSGSVCDVaSRPEREELMQTVSSQFD 85
Cdd:PRK06139   4 PLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDV-TDADQVKALATQAASFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   86 GKLNILVSNVGVirsKPTTEYTEDDFAFH---ISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLT 162
Cdd:PRK06139  83 GRIDVWVNNVGV---GAVGRFEETPIEAHeqvIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYSAS 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 30684202  163 KGALIQLAKNLACEWAKD-GIRANAVAPNVINTP 195
Cdd:PRK06139 160 KFGLRGFSEALRGELADHpDIHVCDVYPAFMDTP 193
PRK07024 PRK07024
SDR family oxidoreductase;
10-198 3.28e-07

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 49.93  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELAGFGARIHVCdiseAKLNQSLSEW-----EKKGFQVSGS-VCDVASrpereelMQTVSSQ 83
Cdd:PRK07024   3 LKVFITGASSGIGQALAREYARQGATLGLV----ARRTDALQAFaarlpKAARVSVYAAdVRDADA-------LAAAAAD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   84 F---DGKLNILVSNVGVirSKPT-TEYTEDDFAFH--ISSNVEAAYH-FSQLSHPLlKASGYGSIIFVSSIAGVISFDAG 156
Cdd:PRK07024  72 FiaaHGLPDVVIANAGI--SVGTlTEEREDLAVFRevMDTNYFGMVAtFQPFIAPM-RAARRGTLVGIASVAGVRGLPGA 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30684202  157 SIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSQ 198
Cdd:PRK07024 149 GAYSASKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPMTA 190
PRK05884 PRK05884
SDR family oxidoreductase;
10-250 4.64e-07

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 49.42  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLnqslsEWEKKGFQVSGSVCDVASRPEREElmqtVSSQFDGKLN 89
Cdd:PRK05884   1 VEVLVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDL-----EVAAKELDVDAIVCDNTDPASLEE----ARGLFPHHLD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVsNVgvirskPTTEYTEDDFAFHISSNVEAAYHfSQLSHPLLKA------------SGyGSIIFVSSIagviSFDAGS 157
Cdd:PRK05884  72 TIV-NV------PAPSWDAGDPRTYSLADTANAWR-NALDATVLSAvltvqsvgdhlrSG-GSIISVVPE----NPPAGS 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  158 IYGLTKGALIQLAKNLACEWAKDGIRANAVAPNvinTPLSQSYledvsfkkALLSRTPLGRVGEpneVASLVAFLCLPAA 237
Cdd:PRK05884 139 AEAAIKAALSNWTAGQAAVFGTRGITINAVACG---RSVQPGY--------DGLSRTPPPVAAE---IARLALFLTTPAA 204
                        250
                 ....*....|...
gi 30684202  238 SYITGQTICVDGG 250
Cdd:PRK05884 205 RHITGQTLHVSHG 217
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
65-253 4.91e-07

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 49.43  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   65 CDVASRPEREELMQTVSSQFDGkLNILVSNVGVirskPTTEYTEDDF-------AFHISSNVeAAYHFSQLSH---PLLk 134
Cdd:PRK06997  63 CDVASDEQIDALFASLGQHWDG-LDGLVHSIGF----APREAIAGDFldglsreNFRIAHDI-SAYSFPALAKaalPML- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  135 aSGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDVSFK-KALLSR 213
Cdd:PRK06997 136 -SDDASLLTLSYLGAERVVPNYNTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKT-LAASGIKDFGKIlDFVESN 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30684202  214 TPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGGLTV 253
Cdd:PRK06997 214 APLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSGFNA 253
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
112-255 5.72e-07

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 49.17  E-value: 5.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  112 AFHISsnveaAYHFSQLSHPLLKASGYGSiifvsSIAGViSFDAG---SIY---GLTKGALIQLAKNLACEWAKDGIRAN 185
Cdd:PRK07889 116 ALHVS-----AYSLKSLAKALLPLMNEGG-----SIVGL-DFDATvawPAYdwmGVAKAALESTNRYLARDLGPRGIRVN 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30684202  186 AVAPNVINTPLSQSYLEDVSFKKALLSRTPLG-RVGEPNEVASLVAFLC---LPAasyITGQTICVDGGLTVNG 255
Cdd:PRK07889 185 LVAAGPIRTLAAKAIPGFELLEEGWDERAPLGwDVKDPTPVARAVVALLsdwFPA---TTGEIVHVDGGAHAMG 255
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
9-238 6.87e-07

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 49.13  E-value: 6.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKgfqvSGS------VCDVASRPEREELMQTVSS 82
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETE----SGNqniflhIVDMSDPKQVWEFVEEFKE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  83 QFDgKLNILVSNVGVIRSKptTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSiAGVI----------- 151
Cdd:cd09808  77 EGK-KLHVLINNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSS-GGMLvqklntnnlqs 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202 152 ---SFDAGSIYGLTKGALIQLAKnlacEWAKD--GIRANAVAPNVINTPLSQSYLEDV--SFKKALLSrtplgrvgePNE 224
Cdd:cd09808 153 ertAFDGTMVYAQNKRQQVIMTE----QWAKKhpEIHFSVMHPGWADTPAVRNSMPDFhaRFKDRLRS---------EEQ 219
                       250
                ....*....|....
gi 30684202 225 VASLVAFLCLPAAS 238
Cdd:cd09808 220 GADTVVWLALSSAA 233
PRK06101 PRK06101
SDR family oxidoreductase;
11-197 1.05e-06

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 48.33  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAklnqSLSEWEKKGFQVSGSVCDVASRPEREELMqtvsSQFDGKLNI 90
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQS----VLDELHTQSANIFTLAFDVTDHPGTKAAL----SQLPFIPEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   91 LVSNVGvirskpTTEYTEDD------FAFHISSNVEAAYHFSQLSHPLLKaSGYgSIIFVSSIAGVISFDAGSIYGLTKG 164
Cdd:PRK06101  75 WIFNAG------DCEYMDDGkvdatlMARVFNVNVLGVANCIEGIQPHLS-CGH-RVVIVGSIASELALPRAEAYGASKA 146
                        170       180       190
                 ....*....|....*....|....*....|...
gi 30684202  165 ALIQLAKNLACEWAKDGIRANAVAPNVINTPLS 197
Cdd:PRK06101 147 AVAYFARTLQLDLRPKGIEVVTVFPGFVATPLT 179
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
10-192 1.23e-06

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 48.21  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELAGFGARIhvcdISEAKLNQSLSEWEKK-GFQVSGSVCDVASRPEREELMQTVSSQFDgKL 88
Cdd:PRK10538   1 MIVLVTGATAGFGECITRRFIQQGHKV----IATGRRQERLQELKDElGDNLYIAQLDVRNRAAIEEMLASLPAEWR-NI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGV-IRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALI 167
Cdd:PRK10538  76 DVLVNNAGLaLGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVR 155
                        170       180
                 ....*....|....*....|....*
gi 30684202  168 QLAKNLACEWAKDGIRANAVAPNVI 192
Cdd:PRK10538 156 QFSLNLRTDLHGTAVRVTDIEPGLV 180
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
7-189 1.89e-06

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: 47.83  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   7 LKGMTALVTGGASGIGYAIVEELAGFGARIHV-CDISEA--KLNQSL----SEWEKKGFQVSGSVCDVASRPEREELMQT 79
Cdd:cd09762   1 LAGKTLFITGASRGIGKAIALKAARDGANVVIaAKTAEPhpKLPGTIytaaEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  80 VSSQFDGkLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGV--ISFDAGS 157
Cdd:cd09762  81 AVEKFGG-IDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNPHILNLSPPLNLnpKWFKNHT 159
                       170       180       190
                ....*....|....*....|....*....|..
gi 30684202 158 IYGLTKGALIQLAKNLACEWAKDGIRANAVAP 189
Cdd:cd09762 160 AYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK09291 PRK09291
SDR family oxidoreductase;
11-194 2.40e-06

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 47.30  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELA--GF----GARI--HVCDISEaklnqslsEWEKKGFQVSGSVCDVASRPEREelmQTVSS 82
Cdd:PRK09291   4 TILITGAGSGFGREVALRLArkGHnviaGVQIapQVTALRA--------EAARRGLALRVEKLDLTDAIDRA---QAAEW 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   83 QFDgklnILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLT 162
Cdd:PRK09291  73 DVD----VLLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCAS 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 30684202  163 KGALIQLAKNLACEWAKDGIRANAVAPNVINT 194
Cdd:PRK09291 149 KHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK06180 PRK06180
short chain dehydrogenase; Provisional
11-189 2.50e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 47.60  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIhvcdISEAKLNQSLSEWEK-KGFQVSGSVCDVASRPEREELMQTVSSQFdGKLN 89
Cdd:PRK06180   6 TWLITGVSSGFGRALAQAALAAGHRV----VGTVRSEAARADFEAlHPDRALARLLDVTDFDAIDAVVADAEATF-GPID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   90 ILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGLTKGALIQL 169
Cdd:PRK06180  81 VLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSKFALEGI 160
                        170       180
                 ....*....|....*....|
gi 30684202  170 AKNLACEWAKDGIRANAVAP 189
Cdd:PRK06180 161 SESLAKEVAPFGIHVTAVEP 180
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
12-205 2.62e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 47.37  E-value: 2.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   12 ALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGF-QVSgsvCDVASRPEREELMQTVSSQF--DGKL 88
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSNLtFHS---LDLQDVHELETNFNEILSSIqeDNVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NI-LVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKA-SGYGSIIFVSSIAGVISFDAGSIYGLTKGA 165
Cdd:PRK06924  81 SIhLINNAGMVAPiKPIEKAESEELITNVHLNLLAPMILTSTFMKHTKDwKVDKRVINISSGAAKNPYFGWSAYCSSKAG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 30684202  166 LIQLAKNLACEWAK--DGIRANAVAPNVINTPLsQSYLEDVS 205
Cdd:PRK06924 161 LDMFTQTVATEQEEeeYPVKIVAFSPGVMDTNM-QAQIRSSS 201
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
7-255 3.51e-06

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 47.08  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGA--SGIGYAIVEELAGFGARIHV------CDISEAKL------------NQSLSEWEK-----KGFQVS 61
Cdd:PLN02730   7 LRGKRAFIAGVAddNGYGWAIAKALAAAGAEILVgtwvpaLNIFETSLrrgkfdesrklpDGSLMEITKvypldAVFDTP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   62 GSVCDVASRPER---------EELMQTVSSQFdGKLNILVSNV--GVIRSKPTTEYTEDDFAFHIS----SNVEAAYHFS 126
Cdd:PLN02730  87 EDVPEDVKTNKRyagssnwtvQEVAESVKADF-GSIDILVHSLanGPEVTKPLLETSRKGYLAAISassySFVSLLQHFG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  127 QLSHPllkasgYGSIIFVSSIAG--VISFDAGSIYGlTKGALIQLAKNLACEWA-KDGIRANAVAPNvintPLSQSYLED 203
Cdd:PLN02730 166 PIMNP------GGASISLTYIASerIIPGYGGGMSS-AKAALESDTRVLAFEAGrKYKIRVNTISAG----PLGSRAAKA 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30684202  204 VSFKKAL----LSRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGGLTVNG 255
Cdd:PLN02730 235 IGFIDDMieysYANAPLQKELTADEVGNAAAFLASPLASAITGATIYVDNGLNAMG 290
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
65-250 3.86e-06

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 47.02  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   65 CDVASRPEREELMQTVSSQFdGKLNILVSNVGVirSKPT------TEYTEDDFAfhISSNVeAAYHF---SQLSHPLLKA 135
Cdd:PRK06079  62 CDVASDESIERAFATIKERV-GKIDGIVHAIAY--AKKEelggnvTDTSRDGYA--LAQDI-SAYSLiavAKYARPLLNP 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  136 SGygSIIFVSSIAGVISFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDvsfKKALL---- 211
Cdd:PRK06079 136 GA--SIVTLTYFGSERAIPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKT-LAVTGIKG---HKDLLkesd 209
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 30684202  212 SRTPLGRVGEPNEVASLVAFLCLPAASYITGQTICVDGG 250
Cdd:PRK06079 210 SRTVDGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK07023 PRK07023
SDR family oxidoreductase;
10-194 7.36e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 45.77  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEEL-------------------AGFGARI--HVCDISEAklnQSLSEWekkgfqVSGSVCDVA 68
Cdd:PRK07023   2 VRAIVTGHSRGLGAALAEQLlqpgiavlgvarsrhpslaAAAGERLaeVELDLSDA---AAAAAW------LAGDLLAAF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   69 SRPEREELmqtvssqfdgklniLVSNVGVIRS-KPTTEYTEDDFAFHISSNVEAAYhfsQLSHPLLKASGYGS---IIFV 144
Cdd:PRK07023  73 VDGASRVL--------------LINNAGTVEPiGPLATLDAAAIARAVGLNVAAPL---MLTAALAQAASDAAerrILHI 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 30684202  145 SSIAGVISFDAGSIYGLTKGALIQLAKNLACEwAKDGIRANAVAPNVINT 194
Cdd:PRK07023 136 SSGAARNAYAGWSVYCATKAALDHHARAVALD-ANRALRIVSLAPGVVDT 184
PRK07806 PRK07806
SDR family oxidoreductase;
6-146 1.44e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 45.10  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    6 SLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEA-KLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQF 84
Cdd:PRK07806   3 DLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKApRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEF 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684202   85 dGKLNILVSNV-GVIRSKptteyTEDDFAFHIssNVEAAYHFSQLSHPLLKASgyGSIIFVSS 146
Cdd:PRK07806  83 -GGLDALVLNAsGGMESG-----MDEDYAMRL--NRDAQRNLARAALPLMPAG--SRVVFVTS 135
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
13-151 1.53e-05

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: 45.44  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  13 LVTGGASGIGYAIVEELA-GFGARIHV------CDISEAKLnQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVSSQFd 85
Cdd:cd08953 209 LVTGGAGGIGRALARALArRYGARLVLlgrsplPPEEEWKA-QTLAALEALGARVLYISADVTDAAAVRRLLEKVRERY- 286
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30684202  86 GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQlshpLLKASGYGSIIFVSSIAGVI 151
Cdd:cd08953 287 GAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQ----ALADEPLDFFVLFSSVSAFF 348
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
7-255 2.07e-05

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 44.73  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    7 LKGMTALVTGGAS--GIGYAIVEELAGFGArihvcDISEAKLNQSLSEWEKKGFQVSGS----VCDVASRPEREELMQTV 80
Cdd:PRK08415   3 MKGKKGLIVGVANnkSIAYGIAKACFEQGA-----ELAFTYLNEALKKRVEPIAQELGSdyvyELDVSKPEHFKSLAESL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   81 SSQFdGKLNILVSNVGVirskPTTEYTEDDF------AFHISSNVeAAYHFSQLSH---PLLKASGygSIIFVSSIAGVI 151
Cdd:PRK08415  78 KKDL-GKIDFIVHSVAF----APKEALEGSFletskeAFNIAMEI-SVYSLIELTRallPLLNDGA--SVLTLSYLGGVK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  152 SFDAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDVSFK-KALLSRTPLGRVGEPNEVASLVA 230
Cdd:PRK08415 150 YVPHYNVMGVAKAALESSVRYLAVDLGKKGIRVNAISAGPIKT-LAASGIGDFRMIlKWNEINAPLKKNVSIEEVGNSGM 228
                        250       260
                 ....*....|....*....|....*
gi 30684202  231 FLCLPAASYITGQTICVDGGLTVNG 255
Cdd:PRK08415 229 YLLSDLSSGVTGEIHYVDAGYNIMG 253
PRK06482 PRK06482
SDR family oxidoreductase;
1-189 2.12e-05

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 44.72  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDKRWslkgmtaLVTGGASGIGYAIVEELAGFGARIhvcdISEAKLNQSLSEW-EKKGFQVSGSVCDVAsrpEREELMQT 79
Cdd:PRK06482   1 MSKTW-------FITGASSGFGRGMTERLLARGDRV----AATVRRPDALDDLkARYGDRLWVLQLDVT---DSAAVRAV 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   80 VSSQFD--GKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGS 157
Cdd:PRK06482  67 VDRAFAalGRIDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFS 146
                        170       180       190
                 ....*....|....*....|....*....|..
gi 30684202  158 IYGLTKGALIQLAKNLACEWAKDGIRANAVAP 189
Cdd:PRK06482 147 LYHATKWGIEGFVEAVAQEVAPFGIEFTIVEP 178
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
9-200 2.53e-05

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 44.51  E-value: 2.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   9 GMTALVTGGASGIGYAIVEELAGFGAR-IHVC---DISEAKLNQSLSEWEKKgfQVSGSVCDVAS----RPEREELMQTV 80
Cdd:cd09809   1 GKVIIITGANSGIGFETARSFALHGAHvILACrnmSRASAAVSRILEEWHKA--RVEAMTLDLASlrsvQRFAEAFKAKN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  81 SSqfdgkLNILVSNVGVIrSKPTTeYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIA----------GV 150
Cdd:cd09809  79 SP-----LHVLVCNAAVF-ALPWT-LTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSEShrftdlpdscGN 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30684202 151 ISFDAGS----------IYGLTKGALIQLAKNLACEWAKDGIRANAVAP-NVINTPLSQSY 200
Cdd:cd09809 152 LDFSLLSppkkkywsmlAYNRAKLCNILFSNELHRRLSPRGITSNSLHPgNMMYSSIHRNW 212
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
8-66 4.20e-05

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 43.76  E-value: 4.20e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684202   8 KGMTALVTGGASGIGYAIVEELAGFGAR-IHVCDISEAKLNQSLSEWEKKGFQVS-----GSVCD 66
Cdd:cd05237   1 KGKTILVTGGAGSIGSELVRQILKFGPKkLIVFDRDENKLHELVRELRSRFPHDKlrfiiGDVRD 65
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
11-151 5.49e-05

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


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 42.55  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    11 TALVTGGASGIGYAIVEELAGFGAR-IHVCDISEAKLNQS---LSEWEKKGFQVSGSVCDVASRpereELMQTVSSQFDG 86
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAqalIAELEARGVEVVVVACDVSDP----DAVAALLAEIKA 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30684202    87 KLNIL---VSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHfsqlshpLLKASGYGSI---IFVSSIAGVI 151
Cdd:pfam08659  78 EGPPIrgvIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWN-------LHEATPDEPLdffVLFSSIAGLL 141
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
11-192 7.37e-05

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 43.04  E-value: 7.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  11 TALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLnqslsEWEKKGFQVSGSVCDVASRPEREELMQtvssQFDgklnI 90
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGA-----ANLAALPGVEFVRGDLRDPEALAAALA----GVD----A 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  91 LVSNVGVIRSkptteyTEDDFAFHISSNVEAAYHfsqlshpLL---KASGYGSIIFVSSIA------GVIS----FDAGS 157
Cdd:COG0451  68 VVHLAAPAGV------GEEDPDETLEVNVEGTLN-------LLeaaRAAGVKRFVYASSSSvygdgeGPIDedtpLRPVS 134
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30684202 158 IYGLTKGALIQLAKNLAcewAKDGIRANAV-APNVI 192
Cdd:COG0451 135 PYGASKLAAELLARAYA---RRYGLPVTILrPGNVY 167
PRK07578 PRK07578
short chain dehydrogenase; Provisional
10-193 2.60e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 40.95  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   10 MTALVTGGASGIGYAIVEELAGFGARIHVcdiseaklnqslsewekkGFQvSGSV-CDVASRPEREELMQTVssqfdGKL 88
Cdd:PRK07578   1 MKILVIGASGTIGRAVVAELSKRHEVITA------------------GRS-SGDVqVDITDPASIRALFEKV-----GKV 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASgyGSIIFVSSIAGVISFDAGSIYGLTKGALIQ 168
Cdd:PRK07578  57 DAVVSAAGKVHFAPLAEMTDEDFNVGLQSKLMGQVNLVLIGQHYLNDG--GSFTLTSGILSDEPIPGGASAATVNGALEG 134
                        170       180
                 ....*....|....*....|....*
gi 30684202  169 LAKNLACEwAKDGIRANAVAPNVIN 193
Cdd:PRK07578 135 FVKAAALE-LPRGIRINVVSPTVLT 158
PRK07102 PRK07102
SDR family oxidoreductase;
9-227 3.48e-04

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 41.06  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQ-VSGSVCDVASRPEREELMQTVSSQFDgk 87
Cdd:PRK07102   1 MKKILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVaVSTHELDILDTASHAAFLDSLPALPD-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   88 lnILVSNVGVIrskPTTEYTEDDF--AFHI-SSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGvisfDAGS----IYG 160
Cdd:PRK07102  79 --IVLIAVGTL---GDQAACEADPalALREfRTNFEGPIALLTLLANRFEARGSGTIVGISSVAG----DRGRasnyVYG 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30684202  161 LTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLSqsylEDVSFKKALlsrtplgrVGEPNEVAS 227
Cdd:PRK07102 150 SAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMT----AGLKLPGPL--------TAQPEEVAK 204
PLN02780 PLN02780
ketoreductase/ oxidoreductase
9-197 3.68e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 41.00  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    9 GMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQ-SLSEWEKKG-FQVSGSVCDVASrpEREELMQTVSSQFDG 86
Cdd:PLN02780  53 GSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDvSDSIQSKYSkTQIKTVVVDFSG--DIDEGVKRIKETIEG 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 -KLNILVSNVGVirSKPTTEYteddfaFH----------ISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVI--SF 153
Cdd:PLN02780 131 lDVGVLINNVGV--SYPYARF------FHevdeellknlIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVipSD 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 30684202  154 DAGSIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTPLS 197
Cdd:PLN02780 203 PLYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMA 246
PRK05993 PRK05993
SDR family oxidoreductase;
11-194 8.83e-04

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 40.01  E-value: 8.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIhvcdISEAKLNQSLSEWEKKG---FQVSgsvcdvASRPER-EELMQTVSSQFDG 86
Cdd:PRK05993   6 SILITGCSSGIGAYCARALQSDGWRV----FATCRKEEDVAALEAEGleaFQLD------YAEPESiAALVAQVLELSGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSN-----VGVIRSKPTTEYTEddfafHISSNVEAAYHFSQLSHPLLKASGYGSIIFVSSIAGVISFDAGSIYGL 161
Cdd:PRK05993  76 RLDALFNNgaygqPGAVEDLPTEALRA-----QFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNA 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 30684202  162 TKGALIQLAKNLACEWAKDGIRANAVAPNVINT 194
Cdd:PRK05993 151 SKFAIEGLSLTLRMELQGSGIHVSLIEPGPIET 183
PRK08862 PRK08862
SDR family oxidoreductase;
1-194 1.06e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 39.32  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202    1 MDkrwsLKGMTALVTGGASGIGYAIVEELAGFGARIHVCDISEAKLNQSLSEWEKKGFQV-SGSVCDvASRPEREELMQT 79
Cdd:PRK08862   1 MD----IKSSIILITSAGSVLGRTISCHFARLGATLILCDQDQSALKDTYEQCSALTDNVySFQLKD-FSQESIRHLFDA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   80 VSSQFDGKLNILVSN-VGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQLS-HPLLKASGYGSII------FVSSIAGVI 151
Cdd:PRK08862  76 IEQQFNRAPDVLVNNwTSSPLPSLFDEQPSESFIQQLSSLASTLFTYGQVAaERMRKRNKKGVIVnvishdDHQDLTGVE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 30684202  152 SFDAgSIYGLTKgaliqlaknlacEWAKD----GIRANAVAPNVINT 194
Cdd:PRK08862 156 SSNA-LVSGFTH------------SWAKEltpfNIRVGGVVPSIFSA 189
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
157-255 1.18e-03

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 39.61  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  157 SIYGLTKGALIQLAKNLACEWAKDGIRANAVAPNVINTpLSQSYLEDVS-FKKALLSRTPLGRVGEPNEVASLVAFLCLP 235
Cdd:PRK06603 158 NVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKT-LASSAIGDFStMLKSHAATAPLKRNTTQEDVGGAAVYLFSE 236
                         90       100
                 ....*....|....*....|
gi 30684202  236 AASYITGQTICVDGGLTVNG 255
Cdd:PRK06603 237 LSKGVTGEIHYVDCGYNIMG 256
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
4-150 1.40e-03

ketoreductase (KR), subgroup 1, 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 KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding 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: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 39.46  E-value: 1.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   4 RWSLKGmTALVTGGASGIGYAIVEELAGFGARiHVCDIS--------EAKLnqsLSEWEKKGFQVSGSVCDVASRPEREE 75
Cdd:cd08952 226 PWRPRG-TVLVTGGTGALGAHVARWLARRGAE-HLVLTSrrgpdapgAAEL---VAELTALGARVTVAACDVADRDALAA 300
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30684202  76 LMQTVSSqfDGKLNILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFSQL--SHPLlkasgygsIIFV--SSIAGV 150
Cdd:cd08952 301 LLAALPA--GHPLTAVVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDELtrDRDL--------DAFVlfSSIAGV 369
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
13-151 5.44e-03

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: 37.75  E-value: 5.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202  13 LVTGGASGIGYAIVEELAGFGARiHVCDIS----EAKLNQSLSEWEKKGFQVSGSVCDVASRPEREELMQTVssQFDGKL 88
Cdd:cd05274 154 LITGGLGGLGLLVARWLAARGAR-HLVLLSrrgpAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLAEL--AAGGPL 230
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684202  89 NILVSNVGVIRSKPTTEYTEDDFAFHISSNVEAAYHFsqlsHPLLKASGYGSIIFVSSIAGVI 151
Cdd:cd05274 231 AGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNL----HELTPDLPLDFFVLFSSVAALL 289
PRK06953 PRK06953
SDR family oxidoreductase;
11-166 8.83e-03

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 36.59  E-value: 8.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   11 TALVTGGASGIGYAIVEELAGFGARIhvcdISEAKLNQSLSEWEKKGFQVsgSVCDVAsRPEreelmqTVSS---QFDG- 86
Cdd:PRK06953   3 TVLIVGASRGIGREFVRQYRADGWRV----IATARDAAALAALQALGAEA--LALDVA-DPA------SVAGlawKLDGe 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684202   87 KLNILVSNVGVI--RSKPTTEYTEDDFAFHISSNVEAAYHFSQLSHPLLKASGyGSIIFVSS----IAGVISfDAGSIYG 160
Cdd:PRK06953  70 ALDAAVYVAGVYgpRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAG-GVLAVLSSrmgsIGDATG-TTGWLYR 147

                 ....*.
gi 30684202  161 LTKGAL 166
Cdd:PRK06953 148 ASKAAL 153
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure