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Conserved domains on  [gi|1622955129|ref|XP_028707267|]
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dehydrogenase/reductase SDR family member 2, mitochondrial isoform X1 [Macaca mulatta]

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

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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 ...
 27-227 3.99e-91

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 cd08936:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 256  Bit Score: 270.57  E-value: 3.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  27 GIDRKGILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVAT 106
Cdd:cd08936     1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVY 185
Cdd:cd08936    81 AVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRgGGSVVIVSSVAAFHPFPGLGPY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDW 227
Cdd:cd08936   161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALW 202
 
Name Accession Description Interval E-value
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 27-227 3.99e-91

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: 270.57  E-value: 3.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  27 GIDRKGILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVAT 106
Cdd:cd08936     1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVY 185
Cdd:cd08936    81 AVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRgGGSVVIVSSVAAFHPFPGLGPY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDW 227
Cdd:cd08936   161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALW 202
FabG-like PRK07231
SDR family oxidoreductase;
34-228 4.06e-59

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 188.89  E-value: 4.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGlSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07231    3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK07231   82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGLRPRPGLGWYNASKGAV 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWG 228
Cdd:PRK07231  162 ITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMG 197
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 34-222 8.41e-57

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: 182.68  E-value: 8.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:COG1028     4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:COG1028    84 LDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAASKAAV 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:COG1028   163 VGLTRSLALELAPRGIRVNAVAPGPIDTPM 192
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 37-224 2.17e-45

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 151.61  E-value: 2.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:pfam00106  81 LVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSgGRIVNISSVAGLVPYPGGSAYSASKAAVIGF 159

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMTK 188
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 40-123 4.78e-08

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: 51.71  E-value: 4.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129   40 VVTGSTSGIGFAIARRLAQDGA-HVVISSR---KQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83


                   ....*...
gi 1622955129  116 FLVCCAGV 123
Cdd:smart00822  84 GVIHAAGV 91
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 38-217 1.51e-05

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: 45.30  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAHVVISSRK-QQNVDRAAAQLQREGLSVAgIVCH-----VGKAEDR-ERLVATALEH 110
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRsAAAASTLAAELNARRPNSA-VTCQadlsnSATLFSRcEAIIDACFRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 111 CGGIDFLVCCAGV---NPLV----GSTLGTSEQIWDKILNV---NVKSPALLLS-----QLLPYMEKRKGAVTLVSSVAA 175
Cdd:TIGR02685  82 FGRCDVLVNNASAfypTPLLrgdaGEGVGDKKSLEVQVAELfgsNAIAPYFLIKafaqrQAGTRAEQRSTNLSIVNLCDA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622955129 176 Y--FPRMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGV 217
Cdd:TIGR02685 162 MtdQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL 205
 
Name Accession Description Interval E-value
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 27-227 3.99e-91

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: 270.57  E-value: 3.99e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  27 GIDRKGILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVAT 106
Cdd:cd08936     1 GVTRRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVY 185
Cdd:cd08936    81 AVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRgGGSVVIVSSVAAFHPFPGLGPY 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDW 227
Cdd:cd08936   161 NVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTSFSSALW 202
FabG-like PRK07231
SDR family oxidoreductase;
34-228 4.06e-59

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 188.89  E-value: 4.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGlSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07231    3 LEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILAGG-RAIAVAADVSDEADVEAAVAAALERFGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK07231   82 VDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGLRPRPGLGWYNASKGAV 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWG 228
Cdd:PRK07231  162 ITLTKALAAELGPDKIRVNAVAPVVVETGLLEAFMG 197
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 34-222 8.41e-57

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: 182.68  E-value: 8.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:COG1028     4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:COG1028    84 LDILVNNAGITP-PGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAASKAAV 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:COG1028   163 VGLTRSLALELAPRGIRVNAVAPGPIDTPM 192
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 39-224 3.24e-50

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: 165.53  E-value: 3.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDrAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFLV 118
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALA-ELAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 119 CCAGVNPLVGSTLGTSEQiWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALLALTR 197
Cdd:cd05233    80 NNAGIARPGPLEELTDED-WDRVLDVNLTGVFLLTRAALPHMKKQGgGRIVNISSVAGLRPLPGQAAYAASKAALEGLTR 158

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 198 TLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:cd05233   159 SLALELAPYGIRVNAVAPGLVDTPMLA 185
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
34-222 1.21e-47

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 159.26  E-value: 1.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:COG0300    83 IDVLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:COG0300   162 EGFSESLRAELAPTGVRVTAVCPGPVDTPF 191
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 37-224 2.17e-45

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 151.61  E-value: 2.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:pfam00106  81 LVNNAGITG-LGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSgGRIVNISSVAGLVPYPGGSAYSASKAAVIGF 159

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTDMTK 188
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
33-221 1.29e-44

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 151.08  E-value: 1.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  33 ILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK05653   82 ALDILVNNAGITR-DALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMiKARYGRIVNISSVSGVTGNPGQTNYSAAKAG 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK05653  161 VIGFTKALALELASRGITVNAVAPGFIDTD 190
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 37-223 4.54e-44

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: 149.56  E-value: 4.54e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqreGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:COG4221     6 KVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:COG4221    83 LVNNAGVALL-GPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGsGHIVNISSIAGLRPYPGGAVYAATKAAVRGL 161

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:COG4221   162 SESLRAELRPTGIRVTVIEPGAVDTEFL 189
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 36-221 6.44e-40

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: 139.33  E-value: 6.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  36 ERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGvNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALLA 194
Cdd:cd05344    81 ILVNNAG-GPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNVARAGLIG 159

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 195 LTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05344   160 LVKTLSRELAPDGVTVNSVLPGYIDTE 186
PRK07035 PRK07035
SDR family oxidoreductase;
34-223 2.61e-38

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 135.14  E-value: 2.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07035    6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-VSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK07035   86 LDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVnVASVNGVSPGDFQGIYSITKAAV 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PRK07035  166 ISMTKAFAKECAPFGIRVNALLPGLTDTKFA 196
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-221 8.67e-37

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 131.12  E-value: 8.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISsrkqQNVDRAAAQ-----LQREGLSVAGIVCHVGKAEDRERLVATAL 108
Cdd:PRK05565    3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIA----YDINEEAAQelleeIKEEGGDAIAVKADVSSEEDVENLVEQIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 109 EHCGGIDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-VSSVAAYFPRMELGVYNV 187
Cdd:PRK05565   79 EKFGKIDILVNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVnISSIWGLIGASCEVLYSA 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK05565  158 SKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTE 191
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 34-215 4.83e-36

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: 129.05  E-value: 4.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAgivCHVGKAEDRERLVATALEHCGG 113
Cdd:cd05345     3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQ---ADVTKRADVEAMVEAALSKFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-VSSVAAYFPRMELGVYNVSKTAL 192
Cdd:cd05345    80 LDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIInIASTAGLRPRPGLTWYNASKGWV 159

                         170       180
                  ....*....|....*....|...
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVP 215
Cdd:cd05345   160 VTATKAMAVELAPRNIRVNCLCP 182
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 44-221 6.56e-36

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: 128.32  E-value: 6.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  44 STSGIGFAIARRLAQDGAHVVIS---SRKQQNVDRAAAQLqreglSVAGIVCHVGKAEDRERLVATALEHCGGIDFLVCC 120
Cdd:pfam13561   4 NESGIGWAIARALAEEGAEVVLTdlnEALAKRVEELAEEL-----GAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 121 AGV-NPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLALTRTL 199
Cdd:pfam13561  79 AGFaPKLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM-KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYL 157

                         170       180
                  ....*....|....*....|..
gi 1622955129 200 ALELAPKDIRVNCLVPGVIKTD 221
Cdd:pfam13561 158 AVELGPRGIRVNAISPGPIKTL 179
PRK12826 PRK12826
SDR family oxidoreductase;
37-221 1.31e-35

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 128.11  E-value: 1.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK12826    7 RVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLDI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEK-RKGAVTLVSSVAA-YFPRMELGVYNVSKTALLA 194
Cdd:PRK12826   87 LVANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRaGGGRIVLTSSVAGpRVGYPGLAHYAASKAGLVG 165

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 195 LTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK12826  166 FTRALALELAARNITVNSVHPGGVDTP 192
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 34-221 1.90e-35

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 127.62  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE-GLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK05557    3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGAlGGKALAVQGDVSDAESVERAVDEAKAEFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGV---NPLvgstLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK05557   83 GVDILVNNAGItrdNLL----MRMKEEDWDRVIDTNLTGVFNLTKAVARPMmKQRSGRIINISSVVGLMGNPGQANYAAS 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK05557  159 KAGVIGFTKSLARELASRGITVNAVAPGFIETD 191
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 34-248 4.47e-34

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: 124.06  E-value: 4.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVG---KAEDRERLVATALEH 110
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSCLQAGVSEKKILLVVAdltEEEGQDRIISTTLAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 111 CGGIDFLVCCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd05364    81 FGRLDILVNNAGI-LAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVLYYCISKA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKvdwgAGGLCRNRVLPVLSRCQLHH 248
Cdd:cd05364   160 ALDQFTRCTALELAPKGVRVNSVSPGVIVTGFHR----RMGMPEEQYIKFLSRAKETH 213
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 37-221 5.03e-34

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: 123.43  E-value: 5.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVnplvgsT-----LGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd05333    81 LVNNAGI------TrdnllMRMSEEDWDAVINVNLTGVFNVTQAVIRAMiKRRSGRIINISSVVGLIGNPGQANYAASKA 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05333   155 GVIGFTKSLAKELASRGITVNAVAPGFIDTD 185
PRK06181 PRK06181
SDR family oxidoreductase;
37-264 5.17e-33

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 121.62  E-value: 5.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK06181    2 KVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLALT 196
Cdd:PRK06181   82 LVNNAGITMWSRFDELTDLSVFERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALHGFF 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622955129 197 RTLALELAPKDIRVNCLVPGVIKTDFSKVDWGAGG-------LCRNRVLPVLSRCQLHHRGEHRSGRLLLSALRG 264
Cdd:PRK06181  162 DSLRIELADDGVAVTVVCPGFVATDIRKRALDGDGkplgkspMQESKIMSAEECAEAILPAIARRKRLLVMSLRG 236
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 34-228 6.14e-33

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: 120.95  E-value: 6.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNvdrAAAQLQREGLSVAG-IVCH---VGKAEDRERLVATALE 109
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSKED---AAEEVVEEIKAVGGkAIAVqadVSKEEDVVALFQSAIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVNPLVGSTLGTSEQiWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYFPRMELGVYNV 187
Cdd:cd05358    78 EFGTLDILVNNAGLQGDASSHEMTLED-WNKVIDVNLTGQFLCAREAIKRFrkSKIKGKIINMSSVHEKIPWPGHVNYAA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWG 228
Cdd:cd05358   157 SKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWD 197
PRK07326 PRK07326
SDR family oxidoreductase;
34-223 9.73e-33

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 120.12  E-value: 9.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGlSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07326    4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAAFGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:PRK07326   83 LDVLIANAGVG-HFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGAAYNASKFGLV 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PRK07326  162 GFSEAAMLDLRQYGIKVSTIMPGSVATHFN 191
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-221 4.45e-32

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 118.82  E-value: 4.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRK-QQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:PRK12825    7 RVALVTGAARGLGRAIALRLARAGADVVVHYRSdEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRID 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGV---NPLVGstlgTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAyFPRMELGV-YNVSKT 190
Cdd:PRK12825   87 ILVNNAGIfedKPLAD----MSDDEWDEVIDVNLSGVFHLLRAVVPPMrKQRGGRIVNISSVAG-LPGWPGRSnYAAAKA 161

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK12825  162 GLVGLTKALARELAEYGITVNMVAPGDIDTD 192
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 39-227 7.57e-32

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: 117.96  E-value: 7.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVissrkqqNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFLV 118
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVI-------ALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 119 CCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLALTR 197
Cdd:cd05331    74 NCAGV-LRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMkDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLSK 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 198 TLALELAPKDIRVNCLVPGVIKTDFSKVDW 227
Cdd:cd05331   153 CLGLELAPYGVRCNVVSPGSTDTAMQRTLW 182
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 34-225 2.03e-31

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 117.35  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK08213   10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGH 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVN--------PLvgstlgtseQIWDKILNVNVKSpALLLSQLLP--YMEKRK-GAVTLVSSVAA----YFP 178
Cdd:PRK08213   90 VDILVNNAGATwgapaedhPV---------EAWDKVMNLNVRG-LFLLSQAVAkrSMIPRGyGRIINVASVAGlggnPPE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622955129 179 RMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKV 225
Cdd:PRK08213  160 VMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRG 206
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 34-222 6.36e-31

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 115.84  E-value: 6.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK12939    5 LAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTlGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGA--VTLVSSVAAY-FPRmeLGVYNVSKT 190
Cdd:PRK12939   85 LDGLVNNAGITNSKSAT-ELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGriVNLASDTALWgAPK--LGAYVASKG 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK12939  162 AVIGMTRSLARELGGRGITVNAIAPGLTATEA 193
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
34-211 6.81e-31

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 121.49  E-value: 6.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGlSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK08324  420 LAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPD-RALGVACDVTDEAAVQAAFEEAALAFGG 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK--GAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK08324  499 VDIVVSNAGIAI-SGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGlgGSIVFIASKNAVNPGPNFGAYGAAKAA 577

                         170       180
                  ....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVN 211
Cdd:PRK08324  578 ELHLVRQLALELGPDGIRVN 597
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 37-221 7.38e-31

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 115.75  E-value: 7.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVissrkqqNVDRAAaqLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK08220    9 KTVWVTGAAQGIGYAVALAFVEAGAKVI-------GFDQAF--LTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:PRK08220   80 LVNAAGILRM-GATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFrRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSL 158

                         170       180
                  ....*....|....*....|....*.
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08220  159 AKCVGLELAPYGVRCNVVSPGSTDTD 184
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 28-220 2.05e-30

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 114.77  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  28 IDRKGILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqrEGLSVAGIVCHVGKAEDRERLVATA 107
Cdd:PRK12829    3 IDLLKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARL--PGAKVTATVADVADPAQVERVFDTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 108 LEHCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAyfPRMELGV-- 184
Cdd:PRK12829   81 VERFGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLkASGHGGVIIALSSVA--GRLGYPGrt 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 185 -YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK12829  159 pYAASKWAVVGLVKSLAIELGPLGIRVNAILPGIVRG 195
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 37-224 6.21e-30

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: 112.33  E-value: 6.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGA-HVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05324     1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGA-VTLVSSVaayfprmeLGV----YNVSKT 190
Cdd:cd05324    81 ILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGrIVNVSSG--------LGSltsaYGVSKA 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:cd05324   153 ALNALTRILAKELKETGIKVNACCPGWVKTDMGG 186
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 34-222 7.13e-30

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: 112.75  E-value: 7.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS-SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:cd05362     1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNyASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSS--VAAYFPRMelGVYNVSKT 190
Cdd:cd05362    81 GVDILVNNAGVMLK-KPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL-RDGGRIINISSslTAAYTPNY--GAYAGSKA 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:cd05362   157 AVEAFTRVLAKELGGRGITVNAVAPGPVDTDM 188
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 32-218 2.38e-29

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 111.59  E-value: 2.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:PRK07890    1 MLLKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSpALLLSQL-LPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:PRK07890   81 GRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLG-TLRLTQAfTPALAESGGSIVMINSMVLRHSQPKYGAYKMAKG 159

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVI 218
Cdd:PRK07890  160 ALLAASQSLATELGPQGIRVNSVAPGYI 187
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 37-224 4.86e-29

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: 110.78  E-value: 4.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAqlqREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGE---LLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:cd05374    78 LVNNAGYG-LFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMrKQGSGRIVNVSSVAGLVPTPFLGPYCASKAALEAL 156

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:cd05374   157 SESLRLELAPFGIKVTIIEPGPVRTGFAD 185
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 34-224 6.03e-29

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: 110.53  E-value: 6.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd05347     3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:cd05347    83 IDILVNNAGII-RRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGhGKIINICSLLSELGGPPVPAYAASKGGV 161

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:cd05347   162 AGLTKALATEWARHGIQVNAIAPGYFATEMTE 193
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 31-221 1.16e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 110.09  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  31 KGILAERVAVVTGSTSGIGFAIARRLAQDGA-HVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALE 109
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAaGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK--GAVTLVSSVAAYFPRMELGVYNV 187
Cdd:PRK06198   81 AFGRLDALVNAAGL-TDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKaeGTIVNIGSMSAHGGQPFLAAYCA 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK06198  160 SKGALATLTRNAAYALLRNRIRVNGLNIGWMATE 193
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 39-223 2.35e-28

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: 108.36  E-value: 2.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQlQREGlsVAGIVCHVGKAEDRERLVATALEHCGGIDFLV 118
Cdd:cd08929     3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQ-ELEG--VLGLAGDVRDEADVRRAVDAMEEAFGGLDALV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 119 CCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLALTRT 198
Cdd:cd08929    80 NNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEA 159

                         170       180
                  ....*....|....*....|....*
gi 1622955129 199 LALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:cd08929   160 AMLDLREANIRVVNVMPGSVDTGFA 184
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 34-216 3.05e-28

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 108.94  E-value: 3.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqreGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK08265    4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVnpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:PRK08265   81 VDILVNLACT--YLDDGLASSRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSISAKFAQTGRWLYPASKAAIR 158

                         170       180
                  ....*....|....*....|...
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPG 216
Cdd:PRK08265  159 QLTRSMAMDLAPDGIRVNSVSPG 181
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 34-251 5.57e-28

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: 107.92  E-value: 5.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd05329     4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSRSERQELMDTVASHFGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 -IDFLVCCAGVNPLVGSTLGTSEQiWDKILNVNVKSpALLLSQLLPYMEKR--KGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd05329    84 kLNILVNNAGTNIRKEAKDYTEED-YSLIMSTNFEA-AYHLSRLAHPLLKAsgNGNIVFISSVAGVIAVPSGAPYGATKG 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKvdwgagGLCRN--RVLPVLSRCQLHHRGE 251
Cdd:cd05329   162 ALNQLTRSLACEWAKDNIRVNAVAPWVIATPLVE------PVIQQkeNLDKVIERTPLKRFGE 218
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 34-222 6.40e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 107.71  E-value: 6.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07478    4 LNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAY---FPRMelGVYNVSK 189
Cdd:PRK07478   84 LDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGgGSLIFTSTFVGHtagFPGM--AAYAASK 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK07478  162 AGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPM 194
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 34-227 7.07e-28

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 107.82  E-value: 7.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnVDRAAAQLQREGLsvAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06841   13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSED-VAEVAAQLLGGNA--KGLVCDVSDSQSVEAAVAAVISAFGR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK06841   90 IDILVNSAGVALL-APAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMiAAGGGKIVNLASQAGVVALERHVAYCASKAGV 168

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDW 227
Cdd:PRK06841  169 VGMTKVLALEWGPYGITVNAISPTVVLTELGKKAW 203
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 37-220 7.66e-28

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: 107.34  E-value: 7.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQ----REGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:cd08939     2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEaeanASGQKVSYISADLSDYEEVEQAFAQAVEKGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVN-PLVGSTLgTSEQIwDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd08939    82 PPDLVVNCAGISiPGLFEDL-TAEEF-ERGMDVNYFGSLNVAHAVLPLMkEQRPGHIVFVSSQAALVGIYGYSAYCPSKF 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd08939   160 ALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 39-225 7.73e-28

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: 107.44  E-value: 7.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKqqNVDRA---AAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05359     1 ALVTGGSRGIGKAIALRLAERGADVVINYRK--SKDAAaevAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNPLVgSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKG----AVTLVSSVAAYFPRMELGVynvSKTA 191
Cdd:cd05359    79 VLVSNAAAGAFR-PLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGgrivAISSLGSIRALPNYLAVGT---AKAA 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTDFSKV 225
Cdd:cd05359   155 LEALVRYLAVELGPRGIRVNAVSPGVIDTDALAH 188
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 34-220 1.10e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 107.28  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK12429    2 LKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAG---VNPLVgsTLGTSEqiWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK12429   82 VDILVNNAGiqhVAPIE--DFPTEK--WKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGKAAYVSAK 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK12429  158 HGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 35-221 1.54e-27

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 106.97  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  35 AERVAVVTGSTSGIGFAIARRLAQDGAHVVISS-RKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK12745    1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDrPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLV-GSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKG-------AVTLVSSVAAYFPRMELGVY 185
Cdd:PRK12745   81 IDCLVNNAGVGVKVrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEpeelphrSIVFVSSVNAIMVSPNRGEY 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK12745  161 CISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTD 196
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 38-221 1.83e-27

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: 106.50  E-value: 1.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFL 117
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 118 VCCAGVNPLVGSTLGTSEQIWDKILNVNVKSpALLLSQL-LPYMEKRKGAVTL-VSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:cd05365    81 VNNAGGGGPKPFDMPMTEEDFEWAFKLNLFS-AFRLSQLcAPHMQKAGGGAILnISSMSSENKNVRIAAYGSSKAAVNHM 159

                         170       180
                  ....*....|....*....|....*.
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05365   160 TRNLAFDLGPKGIRVNAVAPGAVKTD 185
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 34-221 4.17e-27

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: 105.65  E-value: 4.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRkqqNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADI---DGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:cd08944    78 LDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARgGGSIVNLSSIAGQSGDPGYGAYGASKAAI 157

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd08944   158 RNLTRTLAAELRHAGIRCNALAPGLIDTP 186
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 37-222 6.29e-27

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: 105.08  E-value: 6.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd05323     1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVN-PLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK----GAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:cd05323    81 LINNAGILdEKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAPQFPVYSASKHG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 192 LLALTRTLALELAPK-DIRVNCLVPGVIKTDF 222
Cdd:cd05323   161 VVGFTRSLADLLEYKtGVRVNAICPGFTNTPL 192
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 34-223 9.48e-27

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: 104.98  E-value: 9.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREG-LSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGaPSPHVVPLDMSDLEDAEQVVEEALKLFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:cd05332    81 GLDILINNAGISMR-SLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLiERSQGSIVVVSSIAGKIGVPFRTAYAASKHA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:cd05332   160 LQGFFDSLRAELSEPNISVTVVCPGLIDTNIA 191
PRK06172 PRK06172
SDR family oxidoreductase;
34-221 1.75e-26

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 104.06  E-value: 1.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06172    5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAY--FPRMELgvYNVSKT 190
Cdd:PRK06172   85 LDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQgGGAIVNTASVAGLgaAPKMSI--YAASKH 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK06172  163 AVIGLTKSAAIEYAKKGIRVNAVCPAVIDTD 193
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 34-223 2.50e-26

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: 103.57  E-value: 2.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE-GLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:cd05352     6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKyGVKTKAYKCDVSSQESVEKTFKQIQKDFG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLVGSTLGTSEQiWDKILNVNVKSpALLLSQL--LPYMEKRKGAVTLVSSVAAY---FPRmELGVYNV 187
Cdd:cd05352    86 KIDILIANAGITVHKPALDYTYEQ-WNKVIDVNLNG-VFNCAQAaaKIFKKQGKGSLIITASMSGTivnRPQ-PQAAYNA 162

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:cd05352   163 SKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLT 198
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 34-221 2.59e-26

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 103.77  E-value: 2.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06113    9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWdkILNVNVKSPaLLLSQL-LPYMEKRKGAVTL-VSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK06113   89 VDILVNNAGGGGPKPFDMPMADFRR--AYELNVFSF-FHLSQLvAPEMEKNGGGVILtITSMAAENKNINMTSYASSKAA 165

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK06113  166 ASHLVRNMAFDLGEKNIRVNGIAPGAILTD 195
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 36-221 2.87e-26

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: 103.70  E-value: 2.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  36 ERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQ-QNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGI 114
Cdd:cd05337     1 RPVAIVTGASRGIGRAIATELAARGFDIAINDLPDdDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNPLV-GSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-------EKRKGAVTLVSSVAAYFPRMELGVYN 186
Cdd:cd05337    81 DCLVNNAGIAVRPrGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMveqpdrfDGPHRSIIFVTSINAYLVSPNRGEYC 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 187 VSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05337   161 ISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTD 195
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 34-221 3.70e-26

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: 103.05  E-value: 3.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGL-SVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGgRAHPIQCDVRDPEAVEAAVDETLKEFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLVGSTlGTSEQIWDKILNVNVKSPALLLSQLLPY-MEKRKGAVtLVSSVAAY----FPRM------E 181
Cdd:cd05369    81 KIDILINNAAGNFLAPAE-SLSPNGFKTVIDIDLNGTFNTTKAVGKRlIEAKHGGS-ILNISATYaytgSPFQvhsaaaK 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622955129 182 LGVYNVSKtallaltrTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05369   159 AGVDALTR--------SLAVEWGPYGIRVNAIAPGPIPTT 190
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 37-220 3.79e-26

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: 103.22  E-value: 3.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQL--QREGLSVAgIVCHVGKAEDRERLVATALEHCGGI 114
Cdd:cd05366     3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEisEAGYNAVA-VGADVTDKDDVEALIDQAVEKFGSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEK--RKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:cd05366    82 DVMVNNAGIAP-ITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKlgHGGKIINASSIAGVQGFPNLGAYSASKFAV 160

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05366   161 RGLTQTAAQELAPKGITVNAYAPGIVKT 188
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 37-226 1.02e-25

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: 101.29  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQReglsVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGD----VEAVPYDARDPEDARALVDALRDRFGRIDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:cd08932    77 LVHNAGIG-RPTTLREGSDAELEAHFSINVIAPAELTRALLPALrEAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRAL 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFSKVD 226
Cdd:cd08932   156 AHALRQEGWDHGVRVSAVCPGFVDTPMAQGL 186
PRK06500 PRK06500
SDR family oxidoreductase;
34-220 1.09e-25

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 101.96  E-value: 1.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqreGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06500    4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAEL---GESALVIRADAGDVAAQKALAQALAEAFGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVnplvgSTLG----TSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK06500   81 LDAVFINAGV-----AKFApledWDEAMFDRSFNTNVKGPYFLIQALLPLL-ANPASIVLNGSINAHIGMPNSSVYAASK 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06500  155 AALLSLAKTLSGELLPRGIRVNAVSPGPVQT 185
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 34-221 2.09e-25

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 100.97  E-value: 2.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS-SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK12937    3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-VSSVAAYFPrmELGVYNVSKTA 191
Cdd:PRK12937   83 RIDVLVNNAGVMPL-GTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGGRIINLsTSVIALPLP--GYGPYAASKAA 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK12937  160 VEGLVHVLANELRGRGITVNAVAPGPVATE 189
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
34-221 2.83e-25

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 100.95  E-value: 2.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS-SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK08063    2 FSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNyARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCA--GVN-PLvgstLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAA--YFPrmELGVYN 186
Cdd:PRK08063   82 RLDVFVNNAasGVLrPA----MELEESHWDWTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSLGSirYLE--NYTTVG 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 187 VSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08063  156 VSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTD 190
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 37-220 3.19e-25

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 100.69  E-value: 3.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd08945     4 EVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGvNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLP---YMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:cd08945    84 LVNNAG-RSGGGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGRIINIASTGGKQGVVHAAPYSASKHGVV 162

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd08945   163 GFTKALGLELARTGITVNAVCPGFVET 189
PRK07063 PRK07063
SDR family oxidoreductase;
34-229 4.12e-25

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 100.51  E-value: 4.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE--GLSVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:PRK07063    5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDvaGARVLAVPADVTDAASVAAAVAAAEEAF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAY------FPrmelgv 184
Cdd:PRK07063   85 GPLDVLVNNAGIN-VFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMvERGRGSIVNIASTHAFkiipgcFP------ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622955129 185 YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWGA 229
Cdd:PRK07063  158 YPVAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNA 202
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 34-218 4.83e-25

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: 100.16  E-value: 4.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVD------------RAAAQLQREGLSVAGIVCHVGKAEDRE 101
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDngsakslpgtieETAEEIEAAGGQALPIVVDVRDEDQVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 102 RLVATALEHCGGIDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRM 180
Cdd:cd05338    81 ALVEATVDQFGRLDILVNNAGAIWL-SLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAgQGHILNISPPLSLRPAR 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622955129 181 ELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVI 218
Cdd:cd05338   160 GDVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTA 197
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 39-220 1.64e-24

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: 98.56  E-value: 1.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFLV 118
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 119 CCAGVNplvGSTLGTSEQIWD--KILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:cd05350    81 INAGVG---KGTSLGDLSFKAfrETIDTNLLGAAAILEAALPQFRAKGrGHLVLISSVAALRGLPGAAAYSASKAALSSL 157

                         170       180
                  ....*....|....*....|....*
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05350   158 AESLRYDVKKRGIRVTVINPGFIDT 182
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 37-222 1.76e-24

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: 98.74  E-value: 1.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREG-LSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05343     7 RVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGyPTLFPYQCDLSNEEQILSMFSAIRTQHQGVD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGV---NPLVGSTlgTSEqiWDKILNVNVKSPALLLSQLLPYMEKRK---GAVTLVSSVAA--YFPRMELGVYNV 187
Cdd:cd05343    87 VCINNAGLarpEPLLSGK--TEG--WKEMFDVNVLALSICTREAYQSMKERNvddGHIININSMSGhrVPPVSVFHFYAA 162

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 188 SKTALLALTRTLALEL--APKDIRVNCLVPGVIKTDF 222
Cdd:cd05343   163 TKHAVTALTEGLRQELreAKTHIRATSISPGLVETEF 199
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 34-220 2.93e-24

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 98.26  E-value: 2.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRK-QQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK08936    5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSdEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLVGSTLGTSEQiWDKILNVNVKSPALLLSQLLPYMEK--RKGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:PRK08936   85 TLDVMINNAGIENAVPSHEMSLED-WNKVINTNLTGAFLGSREAIKYFVEhdIKGNIINMSSVHEQIPWPLFVHYAASKG 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK08936  164 GVKLMTETLAMEYAPKGIRVNNIGPGAINT 193
PRK06138 PRK06138
SDR family oxidoreductase;
34-220 6.44e-24

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 97.14  E-value: 6.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVcHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06138    3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAAGGRAFARQG-DVGSAEAVEALVDFVAARWGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK06138   82 LDVLVNNAGFGCG-GTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGRAAYVASKGAI 160

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06138  161 ASLTRAMALDHATDGIRVNAVAPGTIDT 188
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 41-189 9.59e-24

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: 96.38  E-value: 9.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQReglsVAGIVCHVGKAEDRERLVATALEHCGGIDFLVCC 120
Cdd:COG3967    10 ITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPG----LHTIVLDVADPASIAALAEQVTAEFPDLNVLINN 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622955129 121 AGV--NPLVGSTLGTSEQIwDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-VSSVAAYFPRMELGVYNVSK 189
Cdd:COG3967    86 AGImrAEDLLDEAEDLADA-EREITTNLLGPIRLTAAFLPHLKAQPEAAIVnVSSGLAFVPLAVTPTYSATK 156
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 34-221 9.65e-24

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: 97.14  E-value: 9.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd08935     3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVN-------------PLVGSTLGTSEQIWDKILNVNVKSpALLLSQLL--PYMEKRKGAVTLVSSVAAYFP 178
Cdd:cd08935    83 VDILINGAGGNhpdattdpehyepETEQNFFDLDEEGWEFVFDLNLNG-SFLPSQVFgkDMLEQKGGSIINISSMNAFSP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622955129 179 RMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd08935   162 LTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 32-221 1.22e-23

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 96.56  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRkqqNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:PRK06200    2 GWLHGQVALITGGGSGIGRALVERFLAEGARVAVLER---SAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGV----NPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNV 187
Cdd:PRK06200   79 GKLDCFVGNAGIwdynTSLVDIPAETLDTAFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPGGGGPLYTA 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 188 SKTALLALTRTLALELAPkDIRVNCLVPGVIKTD 221
Cdd:PRK06200  159 SKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTD 191
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 37-221 1.85e-23

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 96.14  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGL--SVAGIVCHVGKAEDRERLVATALEHCGGI 114
Cdd:cd05327     2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKETGnaKVEVIQLDLSSLASVRQFAEEFLARFPRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNPlvgSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGA-VTLVSSVAAYFPRM------------- 180
Cdd:cd05327    82 DILINNAGIMA---PPRRLTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSrIVNVSSIAHRAGPIdfndldlennkey 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 181 -ELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05327   159 sPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTE 200
PRK07774 PRK07774
SDR family oxidoreductase;
34-225 2.78e-23

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 95.58  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07774    4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVnpLVG----STLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRmelGVYNVS 188
Cdd:PRK07774   84 IDYLVNNAAI--YGGmkldLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGgGAIVNQSSTAAWLYS---NFYGLA 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKV 225
Cdd:PRK07774  159 KVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEATRT 195
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-224 3.40e-23

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 94.76  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK07666   85 IDILINNAGISKF-GKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMiERQSGDIINISSTAGQKGAAVTSAYSASKFGV 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:PRK07666  164 LGLTESLMQEVRKHNIRVTALTPSTVATDMAV 195
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 37-225 4.35e-23

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: 94.59  E-value: 4.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCH--VGKAEDRERLvataLEHCGGI 114
Cdd:cd05356     2 TWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAAdfSAGDDIYERI----EKELEGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 D--FLVCCAGVNPLVGSTLG-TSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd05356    78 DigILVNNVGISHSIPEYFLeTPEDELQDIINVNVMATLKMTRLILPGMVKRkKGAIVNISSFAGLIPTPLLATYSASKA 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKV 225
Cdd:cd05356   158 FLDFFSRALYEEYKSQGIDVQSLLPYLVATKMSKI 192
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 34-225 4.94e-23

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 94.82  E-value: 4.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK08085    7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGV---NPLvgstLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK08085   87 IDVLINNAGIqrrHPF----TEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQaGKIINICSMQSELGRDTITPYAASK 162

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKV 225
Cdd:PRK08085  163 GAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKA 198
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 34-220 5.56e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 94.80  E-value: 5.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqrEGLSVAgivCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06057    5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEV--GGLFVP---TDVTDEDAVNALFDTAAETYGS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLV-GSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTlvsSVAAYFPRMELGV----YNV 187
Cdd:PRK06057   80 VDIAFNNAGISPPEdDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMvRQGKGSII---NTASFVAVMGSATsqisYTA 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06057  157 SKGGVLAMSRELGVQFARQGIRVNALCPGPVNT 189
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
37-220 5.62e-23

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 94.79  E-value: 5.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK08643    3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLVGSTLGTSEQIwDKILNVNVKSPALLLSQLLPYMEKRK--GAVTLVSSVAAYFPRMELGVYNVSKTALLA 194
Cdd:PRK08643   83 VVNNAGVAPTTPIETITEEQF-DKVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGVVGNPELAVYSSTKFAVRG 161

                         170       180
                  ....*....|....*....|....*.
gi 1622955129 195 LTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK08643  162 LTQTAARDLASEGITVNAYAPGIVKT 187
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 34-220 5.83e-23

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: 94.37  E-value: 5.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQReglsvAGIVCH--VGKAEDRERLVATALEHC 111
Cdd:cd05341     3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGD-----AARFFHldVTDEDGWTAVVDTAREAF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGVnpLVGSTL--GTSEQiWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:cd05341    78 GRLDVLVNNAGI--LTGGTVetTTLEE-WRRLLDINLTGVFLGTRAVIPPMkEAGGGSIINMSSIEGLVGDPALAAYNAS 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 189 KTALLALTRTLALELAPKD--IRVNCLVPGVIKT 220
Cdd:cd05341   155 KGAVRGLTKSAALECATQGygIRVNSVHPGYIYT 188
PRK09242 PRK09242
SDR family oxidoreductase;
34-251 6.32e-23

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 94.81  E-value: 6.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE--GLSVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:PRK09242    7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEEfpEREVHGLAADVSDDEDRRAILDWVEDHW 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSpALLLSQLL-PYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK09242   87 DGLHILVNNAGGN-IRKAAIDYTEDEWRGIFETNLFS-AFELSRYAhPLLKQHAsSAIVNIGSVSGLTHVRSGAPYGMTK 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKvdwgagGLCRN--RVLPVLSRCQLHHRGE 251
Cdd:PRK09242  165 AALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTS------GPLSDpdYYEQVIERTPMRRVGE 222
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 37-220 8.76e-23

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 93.71  E-value: 8.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIvcHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK12828    8 KVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVPADALRIGGI--DLVDPQAARRAVDEVNRQFGRLDA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVnpLVGSTL--GTSEQiWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:PRK12828   86 LVNIAGA--FVWGTIadGDADT-WDRMYGVNVKTTLNASKAALPALtASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVA 162

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK12828  163 RLTEALAAELLDRGITVNAVLPSIIDT 189
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 35-220 1.13e-22

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: 94.14  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  35 AERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGL-SVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd08933     8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPgSCKFVPCDVTKEEDIKTLISVTVERFGR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:cd08933    88 IDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKGAIT 167

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd08933   168 AMTKALAVDESRYGVRVNCISPGNIWT 194
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 37-221 1.75e-22

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: 93.28  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQ--LQREGLSVAGIVCHVGKAEDRERLVATALEHCGGI 114
Cdd:cd08940     3 KVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAglAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGGV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:cd08940    83 DILVNNAGIQ-HVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANKSAYVAAKHGVV 161

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd08940   162 GLTKVVALETAGTGVTCNAICPGWVLTP 189
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-220 2.63e-22

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 92.86  E-value: 2.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQ-QNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK06077    4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRaEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSpALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK06077   84 VADILVNNAGLG-LFSPFLNVDDKLIDKHISTDFKS-VIYCSQELAKEMREGGAIVNIASVAGIRPAYGLSIYGAMKAAV 161

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 193 LALTRTLALELAPKdIRVNCLVPGVIKT 220
Cdd:PRK06077  162 INLTKYLALELAPK-IRVNAIAPGFVKT 188
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 33-221 3.20e-22

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: 91.98  E-value: 3.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  33 ILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDraaaQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:cd05370     2 KLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLA----EAKKELPNIHTIVLDVGDAESVEALAEALLSEYP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLVGSTLGTSE-QIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd05370    78 NLDILINNAGIQRPIDLRDPASDlDKADTEIDTNLIGPIRLIKAFLPHLKKQpEATIVNVSSGLAFVPMAANPVYCATKA 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05370   158 ALHSYTLALRHQLKDTGVEVVEIVPPAVDTE 188
PRK06398 PRK06398
aldose dehydrogenase; Validated
 34-229 3.24e-22

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 92.59  E-value: 3.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnvdraaaqlqrEGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06398    4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEP-----------SYNDVDYFKVDVSNKEQVIKGIDYVISKYGR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEK-RKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK06398   73 IDILVNNAGIE-SYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKqDKGVIINIASVQSFAVTRNAAAYVTSKHAV 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 193 LALTRTLALELAPKdIRVNCLVPGVIKTDFskVDWGA 229
Cdd:PRK06398  152 LGLTRSIAVDYAPT-IRCVAVCPGSIRTPL--LEWAA 185
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 34-220 4.19e-22

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: 92.13  E-value: 4.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVagIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISF--VHCDVTVEADVRAAVDTAVARFGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGV-NPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEK-RKGAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:cd05326    80 LDIMFNNAGVlGAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPaKKGSIVSVASVAGVVGGLGPHAYTASKHA 159

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05326   160 VLGLTRSAATELGEHGIRVNCVSPYGVAT 188
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 34-216 4.47e-22

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: 92.16  E-value: 4.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAgIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd08942     4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAYGECIA-IPADLSSEEGIEALVARVAERSDR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNplVGSTLGT-SEQIWDKILNVNVKSPALLLSQLLPYMEKRKGA-----VTLVSSVAAYF-PRMELGVYN 186
Cdd:cd08942    83 LDVLVNNAGAT--WGAPLEAfPESGWDKVMDINVKSVFFLTQALLPLLRAAATAenparVINIGSIAGIVvSGLENYSYG 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 187 VSKTALLALTRTLALELAPKDIRVNCLVPG 216
Cdd:cd08942   161 ASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 37-227 6.72e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 91.70  E-value: 6.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVagivcHVGkaedRERLVATALEHCGGIDF 116
Cdd:PRK07060   10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEPLRL-----DVG----DDAAIRAALAAAGAFDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLA 194
Cdd:PRK07060   81 LVNCAGIASL-ESALDMTAEGFDRVMAVNARGAALVARHVARAMiaAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDA 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 195 LTRTLALELAPKDIRVNCLVPGVIKTDFSKVDW 227
Cdd:PRK07060  160 ITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAW 192
PRK09135 PRK09135
pteridine reductase; Provisional
 37-218 8.68e-22

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 91.53  E-value: 8.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRK-QQNVDRAAAQL--QREGlSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK09135    7 KVALITGGARRIGAAIARTLHAAGYRVAIHYHRsAAEADALAAELnaLRPG-SAAALQADLLDPDALPELVAACVAAFGR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGV---NPLvGSTlgtSEQIWDKILNVNVKSPaLLLSQ-LLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK09135   86 LDALVNNASSfypTPL-GSI---TEAQWDDLFASNLKAP-FFLSQaAAPQLRKQRGAIVNITDIHAERPLKGYPVYCAAK 160

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 190 TALLALTRTLALELAPkDIRVNCLVPGVI 218
Cdd:PRK09135  161 AALEMLTRSLALELAP-EVRVNAVAPGAI 188
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 37-236 1.41e-21

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 90.91  E-value: 1.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVaGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd08943     2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAQGGPRAL-GVQCDVTSEAQVQSAFEQAVLEFGGLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK--GAVTLVSSVAAYFPRMELGVYNVSKTALLA 194
Cdd:cd08943    81 VVSNAGIAT-SSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSAAKAAEAH 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 195 LTRTLALELAPKDIRVNCLVPGVIktdFSKVDWGAGGLCRNR 236
Cdd:cd08943   160 LARCLALEGGEDGIRVNTVNPDAV---FRGSKIWEGVWRAAR 198
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 34-221 1.43e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 91.40  E-value: 1.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqrEGLSVAGIVCH----VGKAEDRERLVATALE 109
Cdd:PRK05875    5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEI--EALKGAGAVRYepadVTDEDQVARAVDAATA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKG-AVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK05875   83 WHGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGgSFVGISSIAASNTHRWFGAYGVT 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK05875  163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTD 195
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 23-220 1.51e-21

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 90.89  E-value: 1.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  23 MSSTGIDRKGilaeRVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRER 102
Cdd:PRK07097    1 MSENLFSLKG----KIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 103 LVATALEHCGGIDFLVCCAGV---NPLvgstLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFP 178
Cdd:PRK07097   77 MVSQIEKEVGVIDILVNNAGIikrIPM----LEMSAEDFRQVIDIDLNAPFIVSKAVIPSMiKKGHGKIINICSMMSELG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 179 RMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07097  153 RETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIAT 194
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 37-220 1.58e-21

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: 90.61  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVV---ISSRKQQNVDRaaaqlqreGLSVAGIVCHVGKAEDRERLVATAlehcGG 113
Cdd:cd05368     3 KVALITAAAQGIGRAIALAFAREGANVIatdINEEKLKELER--------GPGITTRVLDVTDKEQVAALAKEE----GR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRM-ELGVYNVSKTA 191
Cdd:cd05368    71 IDVLFNCAGFVH-HGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKdGSIINMSSVASSIKGVpNRFVYSTTKAA 149

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05368   150 VIGLTKSVAADFAQQGIRCNAICPGTVDT 178
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-220 1.73e-21

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 90.95  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQqNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06935   13 LDGKVAIVTGGNTGLGQGYAVALAKAGADIIITTHGT-NWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGV---NPLvgstLGTSEQIWDKILNVNVKSpALLLSQLLP--YMEKRKGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK06935   92 IDILVNNAGTirrAPL----LEYKDEDWNAVMDINLNS-VYHLSQAVAkvMAKQGSGKIINIASMLSFQGGKFVPAYTAS 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06935  167 KHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 37-218 2.00e-21

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: 90.03  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRK-QQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRsEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLA 194
Cdd:cd05357    81 VLVNNASAFY-PTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLaGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEG 159

                         170       180
                  ....*....|....*....|....
gi 1622955129 195 LTRTLALELAPKdIRVNCLVPGVI 218
Cdd:cd05357   160 LTRSAALELAPN-IRVNGIAPGLI 182
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 34-232 3.62e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 90.00  E-value: 3.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqreGLSVAGIVcHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07825    3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAEL---GLVVGGPL-DVTDPASFAAFLDAVEADLGP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPaLLLSQL-LPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK07825   79 IDVLVNNAGVMP-VGPFLDEPDAVTRRILDVNVYGV-ILGSKLaAPRMvPRGRGHVVNVASLAGKIPVPGMATYCASKHA 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWGAGGL 232
Cdd:PRK07825  157 VVGFTDAARLELRGTGVHVSVVLPSFVNTELIAGTGGAKGF 197
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 34-222 3.63e-21

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: 89.52  E-value: 3.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:cd08934    81 LDILVNNAGIM-LLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNkGTIVNISSVAGRVAVRNSAVYNATKFGV 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:cd08934   160 NAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
32-220 4.94e-21

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 89.47  E-value: 4.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:PRK08226    2 GKLTGKTALITGALQGIGEGIARVFARHGANLILLDISPE-IEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGV-YNVSK 189
Cdd:PRK08226   81 GRIDILVNNAGVCRL-GSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMiARKDGRIVMMSSVTGDMVADPGETaYALTK 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK08226  160 AAIVGLTKSLAVEYAQSGIRVNAICPGYVRT 190
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 34-221 5.27e-21

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: 89.33  E-value: 5.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRkqqNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd05348     2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDR---SAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQ----IWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:cd05348    79 LDCFIGNAGIWDYSTSLVDIPEEkldeAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPGGGGPLYTASK 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 190 TALLALTRTLALELAPKdIRVNCLVPGVIKTD 221
Cdd:cd05348   159 HAVVGLVKQLAYELAPH-IRVNGVAPGGMVTD 189
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 38-222 5.35e-21

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


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 89.22  E-value: 5.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFL 117
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 118 VCCAGV---NPLVGStlgTSEQIwDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:cd05339    81 INNAGVvsgKKLLEL---PDEEI-EKTFEVNTLAHFWTTKAFLPDMlERNHGHIVTIASVAGLISPAGLADYCASKAAAV 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 194 ALTRTLALELAP---KDIRVNCLVPGVIKTDF 222
Cdd:cd05339   157 GFHESLRLELKAygkPGIKTTLVCPYFINTGM 188
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 34-221 9.13e-21

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 88.76  E-value: 9.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREG-LSVAGIVCHVGKAEDRERLVATaLEHCG 112
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESnVDVSYIVADLTKREDLERTVKE-LKNIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGvNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK08339   85 EPDIFFFSTG-GPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKGfGRIIYSTSVAIKEPIPNIALSNVVRIS 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08339  164 MAGLVRTLAKELGPKGITVNGIMPGIIRTD 193
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 32-220 1.06e-20

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 88.89  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS--SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALE 109
Cdd:cd05355    22 GKLKGKKALITGGDSGIGRAVAIAFAREGADVAINylPEEEDDAEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:cd05355   102 EFGKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHL-KKGSSIINTTSVTAYKGSPHLLDYAATK 180

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05355   181 GAIVAFTRGLSLQLAEKGIRVNAVAPGPIWT 211
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
34-221 1.10e-20

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 88.55  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRkqqNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07067    4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADI---KPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGV---NPLVGSTlgtsEQIWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK07067   81 IDILFNNAALfdmAPILDIS----RDSYDRLFAVNVKGLFFLMQAVARHMveQGRGGKIINMASQAGRRGEALVSHYCAT 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK07067  157 KAAVISYTQSAALALIRHGINVNAIAPGVVDTP 189
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 34-221 1.15e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 88.42  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqreglsvagIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06523    7 LAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSRPDDLPEGVEF---------VAADLTTAEGCAAVARAVLERLGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGvnplvGST------LGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRME-LGVY 185
Cdd:PRK06523   78 VDILVHVLG-----GSSapaggfAALTDEEWQDELNLNLLAAVRLDRALLPGMiARGSGVIIHVTSIQRRLPLPEsTTAY 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK06523  153 AAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIETE 188
PRK07814 PRK07814
SDR family oxidoreductase;
34-220 1.48e-20

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 88.30  E-value: 1.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAG---VNPLvgstLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK--GAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK07814   88 LDIVVNNVGgtmPNPL----LSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSggGSVINISSTMGRLAGRGFAAYGTA 163

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 189 KTALLALTRTLALELAPKdIRVNCLVPGVIKT 220
Cdd:PRK07814  164 KAALAHYTRLAALDLCPR-IRVNAIAPGSILT 194
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-221 1.75e-20

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 88.09  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK08217    3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGV---NPLVGSTLGT-----SEQIWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYfPRMELG 183
Cdd:PRK08217   83 LNGLINNAGIlrdGLLVKAKDGKvtskmSLEQFQSVIDVNLTGVFLCGREAAAKMieSGSKGVIINISSIARA-GNMGQT 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622955129 184 VYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08217  162 NYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETE 199
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 34-220 1.83e-20

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 88.03  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK13394    5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAG---VNPLVgstlGTSEQIWDKILNVNVKSPALLLSQLLPYMEK--RKGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK13394   85 VDILVSNAGiqiVNPIE----NYSFADWKKMQAIHVDGAFLTTKAALKHMYKddRGGVVIYMGSVHSHEASPLKSAYVTA 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK13394  161 KHGLLGLARVLAKEGAKHNVRSHVVCPGFVRT 192
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 36-220 2.40e-20

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: 87.34  E-value: 2.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  36 ERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQlqreGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05371     2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVAKL----GDNCRFVPVDVTSEKDVKAALALAKAKFGRLD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNPlVGSTLGT------SEQIWDKILNVNV-------KSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMEL 182
Cdd:cd05371    78 IVVNCAGIAV-AAKTYNKkgqqphSLELFQRVINVNLigtfnviRLAAGAMGKNEPDQGGERGVIINTASVAAFEGQIGQ 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622955129 183 GVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05371   157 AAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 34-227 2.54e-20

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: 87.14  E-value: 2.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDraaaQLQREGLSVAGIVCHVGKAEDRERlvatALEHCGG 113
Cdd:cd05351     5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLD----SLVRECPGIEPVCVDLSDWDATEE----ALGSVGP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR--KGAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:cd05351    77 VDLLVNNAAV-AILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARgvPGSIVNVSSQASQRALTNHTVYCSTKAA 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDW 227
Cdd:cd05351   156 LDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNW 191
PRK08589 PRK08589
SDR family oxidoreductase;
32-220 2.84e-20

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 87.91  E-value: 2.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVV---ISSRKQQNVDraaaQLQREGLSVAGIVCHVGKAEDRERLVATAL 108
Cdd:PRK08589    2 KRLENKVAVITGASTGIGQASAIALAQEGAYVLavdIAEAVSETVD----KIKSNGGKAKAYHVDISDEQQVKDFASEIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 109 EHCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK08589   78 EQFGRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSSFSGQAADLYRSGYNAA 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK08589  158 KGAVINFTKSIAIEYGRDGIRANAIAPGTIET 189
PRK07454 PRK07454
SDR family oxidoreductase;
37-220 4.66e-20

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 86.55  E-value: 4.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK07454    7 PRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAY--FPrmELGVYNVSKTALL 193
Cdd:PRK07454   87 LINNAGM-AYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARnaFP--QWGAYCVSKAALA 163

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07454  164 AFTKCLAEEERSHGIRVCTITLGAVNT 190
PRK06484 PRK06484
short chain dehydrogenase; Validated
 37-220 4.67e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.52  E-value: 4.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLsvaGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK06484    6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHH---ALAMDVSDEAQIREGFEQLHREFGRIDV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGV-NPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:PRK06484   83 LVNNAGVtDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMieQGHGAAIVNVASGAGLVALPKRTAYSASKAAVI 162

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06484  163 SLTRSLACEWAAKGIRVNAVLPGYVRT 189
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 39-225 8.25e-20

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: 86.18  E-value: 8.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE-GLSVAGIVCHVGKAEDRERLVATALEHCGGIDFL 117
Cdd:cd05346     3 VLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKfPVKVLPLQLDVSDRESIEAALENLPEEFRDIDIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 118 VCCAGVnplvgsTLGT------SEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd05346    83 VNNAGL------ALGLdpaqeaDLEDWETMIDTNVKGLLNVTRLILPIMIARnQGHIINLGSIAGRYPYAGGNVYCATKA 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKV 225
Cdd:cd05346   157 AVRQFSLNLRKDLIGTGIRVTNIEPGLVETEFSLV 191
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 34-221 1.28e-19

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 85.44  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS-SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK12935    4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVINyNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK12935   84 KVDILVNNAGITR-DRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYItEAEEGRIISISSIIGQAGGFGQTNYSAAKAG 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK12935  163 MLGFTKSLALELAKTNVTVNAICPGFIDTE 192
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 33-220 1.49e-19

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: 84.94  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  33 ILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVC---HVGKAEDRERLVATALE 109
Cdd:cd05340     1 LLNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFIldlLTCTSENCQQLAQRIAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:cd05340    81 NYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYAVS 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05340   161 KFATEGL*QVLADEYQQRNLRVNCINPGGTRT 192
PRK07831 PRK07831
SDR family oxidoreductase;
32-225 1.65e-19

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 85.47  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGST-SGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE-GLS-VAGIVCHVGKAEDRERLVATAL 108
Cdd:PRK07831   13 GLLAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAElGLGrVEAVVCDVTSEAQVDALIDAAV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 109 EHCGGIDFLVCCAGvnpLVGSTL---GTSEQiWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLV--SSVAAYFPRMELG 183
Cdd:PRK07831   93 ERLGRLDVLVNNAG---LGGQTPvvdMTDDE-WSRVLDVTLTGTFRATRAALRYMRARGHGGVIVnnASVLGWRAQHGQA 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622955129 184 VYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDF-SKV 225
Cdd:PRK07831  169 HYAAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFlAKV 211
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
37-220 1.86e-19

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 84.82  E-value: 1.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKqqNVDRAAAQLQREGLSVAGI---VCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK12824    3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFS--GNDCAKDWFEEYGFTEDQVrlkELDVTDTEECAEALAEIEEEEGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK12824   81 VDILVNNAGITR-DSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMcEQGYGRIINISSVNGLKGQFGQTNYSAAKAGM 159

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK12824  160 IGFTKALASEGARYGITVNCIAPGYIAT 187
PRK05867 PRK05867
SDR family oxidoreductase;
34-222 2.68e-19

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 84.70  E-value: 2.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYFPRM--ELGVYNVSK 189
Cdd:PRK05867   87 IDIAVCNAGIIT-VTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMvkQGQGGVIINTASMSGHIINVpqQVSHYCASK 165

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK05867  166 AAVIHLTKAMAVELAPHKIRVNSVSPGYILTEL 198
PRK06194 PRK06194
hypothetical protein; Provisional
 34-189 4.05e-19

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 84.68  E-value: 4.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06194    4 FAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-------EKRKGAVTLVSSVAAYFPRMELGVYN 186
Cdd:PRK06194   84 VHLLFNNAGVGA-GGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMlaaaekdPAYEGHIVNTASMAGLLAPPAMGIYN 162


                  ...
gi 1622955129 187 VSK 189
Cdd:PRK06194  163 VSK 165
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 34-218 4.14e-19

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 84.29  E-value: 4.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVissrkqqNVDRAAAQLQREGLSVagIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06171    7 LQGKIIIVTGGSSGIGLAIVKELLANGANVV-------NADIHGGDGQHENYQF--VPTDVSSAEEVNHTVAEIIEKFGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVN-P--LV-----GSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-VSSVAAYFPRMELGV 184
Cdd:PRK06171   78 IDGLVNNAGINiPrlLVdekdpAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVnMSSEAGLEGSEGQSC 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 185 YNVSKTALLALTRTLALELAPKDIRVNCLVPGVI 218
Cdd:PRK06171  158 YAATKAALNSFTRSWAKELGKHNIRVVGVAPGIL 191
PRK12743 PRK12743
SDR family oxidoreductase;
37-220 4.60e-19

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 83.93  E-value: 4.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVIS-SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQQGFDIGITwHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRID 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNplVGST-LGTSEQIWDKILNVNVKSPALLLSQLLPYMEK--RKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK12743   83 VLVNNAGAM--TKAPfLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKqgQGGRIINITSVHEHTPLPGASAYTAAKHAL 160

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK12743  161 GGLTKAMALELVEHGILVNAVAPGAIAT 188
PRK06124 PRK06124
SDR family oxidoreductase;
34-221 2.55e-18

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 82.07  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06124    9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGV---NPLVGSTLGTSEQiwdkILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK06124   89 LDILVNNVGArdrRPLAELDDAAIRA----LLETDLVAPILLSRLAAQRMKRQGyGRIIAITSIAGQVARAGDAVYPAAK 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK06124  165 QGLTGLMRALAAEFGPHGITSNAIAPGYFATE 196
PRK07062 PRK07062
SDR family oxidoreductase;
34-220 2.57e-18

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 82.40  E-value: 2.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE--GLSVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:PRK07062    6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKfpGARLLAARCDVLDEADVAAFAAAVEARF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGVNPLvgSTLG-TSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMEL------- 182
Cdd:PRK07062   86 GGVDMLVNNAGQGRV--STFAdTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSLLALQPEPHMvatsaar 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622955129 183 -GVYNVSKtallaltrTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07062  164 aGLLNLVK--------SLATELAPKGVRVNSILLGLVES 194
PRK08628 PRK08628
SDR family oxidoreductase;
34-215 2.70e-18

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 81.93  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNvDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK08628    5 LKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPD-DEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGstLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:PRK08628   84 IDGLVNNAGVNDGVG--LEAGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQL 161

                         170       180
                  ....*....|....*....|..
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVP 215
Cdd:PRK08628  162 ALTREWAVALAKDGVRVNAVIP 183
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 34-221 4.98e-18

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 81.30  E-value: 4.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVI----SSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALE 109
Cdd:PRK12827    4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVldihPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVNPLVGSTLGTSEQiWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYFPRMELGVYNV 187
Cdd:PRK12827   84 EFGRLDILVNNAGIATDAAFAELSIEE-WDDVIDVNLDGFFNVTQAALPPMirARRGGRIVNIASVAGVRGNRGQVNYAA 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK12827  163 SKAGLIGLTKTLANELAPRGITVNAVAPGAINTP 196
PRK07856 PRK07856
SDR family oxidoreductase;
34-223 7.05e-18

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 80.75  E-value: 7.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDraaaqlqrEGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07856    4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPETV--------DGRPAEFHAADVRDPDQVAALVDAIVERHGR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVgSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK--GAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK07856   76 LDVLVNNAGGSPYA-LAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPggGSIVNIGSVSGRRPSPGTAAYGAAKAG 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 192 LLALTRTLALELAPKdIRVNCLVPGVIKTDFS 223
Cdd:PRK07856  155 LLNLTRSLAVEWAPK-VRVNAVVVGLVRTEQS 185
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 34-221 7.84e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 81.55  E-value: 7.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQrEGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK05872    7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELG-GDDRVLTVVADVTDLAAMQAAAEEAVERFGG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:PRK05872   86 IDVVVANAGIASG-GSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMAAYCASKAGVE 164

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK05872  165 AFANALRLEVAHHGVTVGSAYLSWIDTD 192
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 37-220 8.19e-18

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 81.16  E-value: 8.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK05876    7 RGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLA 194
Cdd:PRK05876   87 VFSNAGI-VVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLleQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVG 165

                         170       180
                  ....*....|....*....|....*.
gi 1622955129 195 LTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK05876  166 LAETLAREVTADGIGVSVLCPMVVET 191
PRK08278 PRK08278
SDR family oxidoreductase;
34-215 8.32e-18

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 81.10  E-value: 8.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQ-------NVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVAT 106
Cdd:PRK08278    4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEphpklpgTIHTAAEEIEAAGGQALPLVGDVRDEDQVAAAVAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVNPLVGsTLGTSEQIWDKILNVNVKSpALLLSQL-LPYMEKRKGA--VTL---VSSVAAYFPRm 180
Cdd:PRK08278   84 AVERFGGIDICVNNASAINLTG-TEDTPMKRFDLMQQINVRG-TFLVSQAcLPHLKKSENPhiLTLsppLNLDPKWFAP- 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 181 eLGVYNVSKTALLALTRTLALELAPKDIRVNCLVP 215
Cdd:PRK08278  161 -HTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 33-223 1.27e-17

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 80.12  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  33 ILAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS-SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERL---VATAL 108
Cdd:PRK12747    1 MLKGKVALVTGASRGIGRAIAKRLANDGALVAIHyGNRKEEAEETVYEIQSNGGSAFSIGANLESLHGVEALyssLDNEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 109 EHCGG---IDFLVCCAGVNPlvGSTL-GTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTlVSSVAAYFPRMELGV 184
Cdd:PRK12747   81 QNRTGstkFDILINNAGIGP--GAFIeETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSRIIN-ISSAATRISLPDFIA 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622955129 185 YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PRK12747  158 YSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMN 196
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 37-220 1.28e-17

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: 79.93  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnvdRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd09761     2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEE---RGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGV-NPLVGSTLGTSEqiWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:cd09761    79 LVNNAARgSKGILSSLLLEE--WDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVAL 156

                         170       180
                  ....*....|....*....|....*
gi 1622955129 196 TRTLALELAPkDIRVNCLVPGVIKT 220
Cdd:cd09761   157 THALAMSLGP-DIRVNCISPGWINT 180
PRK07074 PRK07074
SDR family oxidoreductase;
37-220 1.50e-17

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 79.81  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGlsVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK07074    3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDAR--FVPVACDLTDAASLAAALANAAAERGPVDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLVgSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSV---AAyfprmeLG--VYNVSKT 190
Cdd:PRK07074   81 LVANAGAARAA-SLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRsRGAVVNIGSVngmAA------LGhpAYSAAKA 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07074  154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKT 183
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 34-221 2.15e-17

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 79.94  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK08277    8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVN--------------PLVGSTLGTSEQIWDKILNVNvkspalLLSQLLPYM-------EKRKGAVTLVSS 172
Cdd:PRK08277   88 CDILINGAGGNhpkattdnefheliEPTKTFFDLDEEGFEFVFDLN------LLGTLLPTQvfakdmvGRKGGNIINISS 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622955129 173 VAAYFPRMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08277  162 MNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
PRK12746 PRK12746
SDR family oxidoreductase;
34-223 2.54e-17

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 79.31  E-value: 2.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS-SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATaLEH-- 110
Cdd:PRK12746    4 LDGKVALVTGASRGIGRAIAMRLANDGALVAIHyGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQ-LKNel 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 111 -----CGGIDFLVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSVAAYFPRMELGVY 185
Cdd:PRK12746   83 qirvgTSEIDILVNNAGIGTQ-GTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLL-RAEGRVINISSAEVRLGFTGSIAY 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PRK12746  161 GLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDIN 198
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 36-219 3.07e-17

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: 78.92  E-value: 3.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  36 ERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLS-VAGIVCHVGKAEDRERLVATALEHCGGI 114
Cdd:cd08930     2 DKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNrVIALELDITSKESIKELIESYLEKFGRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNPLVGSTLGT--SEQIWDKILNVNVKSpALLLSQ-LLPYMEKR-KGAVTLVSSVAAYF-PRMEL------- 182
Cdd:cd08930    82 DILINNAYPSPKVWGSRFEefPYEQWNEVLNVNLGG-AFLCSQaFIKLFKKQgKGSIINIASIYGVIaPDFRIyentqmy 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622955129 183 --GVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIK 219
Cdd:cd08930   161 spVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIL 199
PRK05650 PRK05650
SDR family oxidoreductase;
40-220 3.51e-17

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 79.31  E-value: 3.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFLVC 119
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 120 CAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALLALTRT 198
Cdd:PRK05650   84 NAGVAS-GGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSET 162

                         170       180
                  ....*....|....*....|..
gi 1622955129 199 LALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK05650  163 LLVELADDEIGVHVVCPSFFQT 184
PRK08219 PRK08219
SDR family oxidoreductase;
37-221 3.67e-17

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 78.44  E-value: 3.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDgAHVVISSRKQQNVDRAAAQLQREGLSVAGIVchvgkaedRERLVATALEHCGGIDF 116
Cdd:PRK08219    4 PTALITGASRGIGAAIARELAPT-HTLLLGGRPAERLDELAAELPGATPFPVDLT--------DPEAIAAAVEQLGRLDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLALT 196
Cdd:PRK08219   75 LVHNAGVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALA 153

                         170       180
                  ....*....|....*....|....*
gi 1622955129 197 RTLALELAPKdIRVNCLVPGVIKTD 221
Cdd:PRK08219  154 DALREEEPGN-VRVTSVHPGRTDTD 177
PRK07985 PRK07985
SDR family oxidoreductase;
32-220 5.08e-17

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 79.27  E-value: 5.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS--SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALE 109
Cdd:PRK07985   45 GRLKDRKALVTGGDSGIGRAAAIAYAREGADVAISylPVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHK 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTlVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK07985  125 ALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGASIIT-TSSIQAYQPSPHLLDYAATK 203

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07985  204 AAILNYSRGLAKQVAEKGIRVNIVAPGPIWT 234
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 32-216 8.10e-17

(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: 77.75  E-value: 8.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS----SRKQQNVDRAAAQLQREGLSVAGivchvGKA-------EDR 100
Cdd:cd05353     1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVNdlggDRKGSGKSSSAADKVVDEIKAAG-----GKAvanydsvEDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 101 ERLVATALEHCGGIDFLVCCAGVnpLV-GSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFP 178
Cdd:cd05353    76 EKIVKTAIDAFGRVDILVNNAGI--LRdRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYG 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622955129 179 RMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPG 216
Cdd:cd05353   154 NFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 35-216 1.21e-16

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 77.29  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  35 AERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGI 114
Cdd:PRK12823    7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSEL-VHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLvccagVNPlVGSTLG-------TSEQIWDKILnvnvKS--PALLLSQ-LLPYM-EKRKGAVTLVSSVAAYfprmelG 183
Cdd:PRK12823   86 DVL-----INN-VGGTIWakpfeeyEEEQIEAEIR----RSlfPTLWCCRaVLPHMlAQGGGAIVNVSSIATR------G 149

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 184 VYNV----SKTALLALTRTLALELAPKDIRVNCLVPG 216
Cdd:PRK12823  150 INRVpysaAKGGVNALTASLAFEYAEHGIRVNAVAPG 186
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 37-232 1.23e-16

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 76.93  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVissrkqqNVDRAAAQLQREGLsvagivcHVGKAEDRERLvATALEHCGGIDF 116
Cdd:PRK06550    6 KTVLITGAASGIGLAQARAFLAQGAQVY-------GVDKQDKPDLSGNF-------HFLQLDLSDDL-EPLFDWVPSVDI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-VSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:PRK06550   71 LCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIInMCSIASFVAGGGGAAYTASKHALAGF 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFSKVDWGAGGL 232
Cdd:PRK06550  151 TKQLALDYAKDGIQVFGIAPGAVKTPMTAADFEPGGL 187
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 37-225 1.62e-16

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 76.73  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRkqQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVNYY--RSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGV----NPLVGSTLGTSE-QIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd05349    79 IVNNALIdfpfDPDQRKTFDTIDwEDYQQQLEGAVKGALNLLQAVLPDFKERGsGRVINIGTNLFQNPVVPYHDYTTAKA 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIK-TDFSKV 225
Cdd:cd05349   159 ALLGFTRNMAKELGPYGITVNMVSGGLLKvTDASAA 194
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 34-218 1.75e-16

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 76.92  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07576    7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPrMELGVYNV-SKTAL 192
Cdd:PRK07576   87 IDVLVSGAAGN-FPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVP-MPMQAHVCaAKAGV 164

                         170       180
                  ....*....|....*....|....*.
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVI 218
Cdd:PRK07576  165 DMLTRTLALEWGPEGIRVNSIVPGPI 190
PRK07201 PRK07201
SDR family oxidoreductase;
29-174 2.19e-16

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 78.84  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  29 DRKGILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATAL 108
Cdd:PRK07201  364 DLRGPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDIL 443

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622955129 109 EHCGGIDFLVCCAGvNPLVGSTLGTSEQIWD--KILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVA 174
Cdd:PRK07201  444 AEHGHVDYLVNNAG-RSIRRSVENSTDRFHDyeRTMAVNYFGAVRLILGLLPHMrERRFGHVVNVSSIG 511
PRK05855 PRK05855
SDR family oxidoreductase;
37-221 2.51e-16

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 78.48  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK05855  316 KLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDI 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNpLVGSTLGTSEQIWDKILNVN---VKSPALLLSQllpYMEKRK--GAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK05855  396 VVNNAGIG-MAGGFLDTSAEDWDRVLDVNlwgVIHGCRLFGR---QMVERGtgGHIVNVASAAAYAPSRSLPAYATSKAA 471

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK05855  472 VLMLSECLRAELAAAGIGVTAICPGFVDTN 501
PRK07069 PRK07069
short chain dehydrogenase; Validated
 39-220 7.26e-16

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 75.13  E-value: 7.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNV-DRAAAQLQRE-GLSVAGIVCHVGKAEDR-ERLVATALEHCGGID 115
Cdd:PRK07069    2 AFITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGlDAFAAEINAAhGEGVAFAAVQDVTDEAQwQALLAQAADAMGGLS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVnplvgSTLGTSEQI----WDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:PRK07069   82 VLVNNAGV-----GSFGAIEQIeldeWRRVMAINVESIFLGCKHALPYLrASQPASIVNISSVAAFKAEPDYTAYNASKA 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 191 ALLALTRTLALELAPK--DIRVNCLVPGVIKT 220
Cdd:PRK07069  157 AVASLTKSIALDCARRglDVRCNSIHPTFIRT 188
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 34-220 1.34e-15

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 74.18  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqreGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK12936    4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAEL---GERVKIFPANLSDRDEVKALGQKAEADLEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLL-PYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK12936   81 VDILVNNAGITK-DGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRYGRIINITSVVGVTGNPGQANYCASKAGM 159

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK12936  160 IGFSKSLAQEIATRNVTVNCVAPGFIES 187
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 37-222 1.71e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 74.55  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnvdRAAAQLQreglsVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK06179    5 KVALVTGASSGIGRATAEKLARAGYRVFGTSRNPA---RAAPIPG-----VELLELDVTDDASVQAAVDEVIARAGRIDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNpLVGSTLGTS-EQIwDKILNVNVKSPALLLSQLLPYMEK-RKGAVTLVSSVAAYFPRMELGVYNVSKTALLA 194
Cdd:PRK06179   77 LVNNAGVG-LAGAAEESSiAQA-QALFDTNVFGILRMTRAVLPHMRAqGSGRIINISSVLGFLPAPYMALYAASKHAVEG 154

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 195 LTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK06179  155 YSESLDHEVRQFGIRVSLVEPAYTKTNF 182
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 34-221 2.08e-15

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: 73.81  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSrkqQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIAD---INLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAG---VNPLVGSTlgtsEQIWDKILNVNVKSPALLLSQLLPYM--EKRKGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:cd05363    78 IDILVNNAAlfdLAPIVDIT----RESYDRLFAINVSGTLFMMQAVARAMiaQGRGGKIINMASQAGRRGEALVGVYCAT 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05363   154 KAAVISLTQSAGLNLIRHGINVNAIAPGVVDGE 186
PRK06114 PRK06114
SDR family oxidoreductase;
34-220 2.46e-15

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 73.66  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQN-VDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK06114    6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLVGSTLGTSEQiWDKILNVNVKspALLLS---QLLPYMEKRKGAVTLVSSVAAYFPRMEL--GVYNV 187
Cdd:PRK06114   86 ALTLAVNAAGIANANPAEEMEEEQ-WQTVMDINLT--GVFLScqaEARAMLENGGGSIVNIASMSGIIVNRGLlqAHYNA 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06114  163 SKAGVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
PRK09072 PRK09072
SDR family oxidoreductase;
34-222 3.88e-15

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 73.44  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLsVAGIVCHVGKAEDRERLVATALEHcGG 113
Cdd:PRK09072    3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGR-HRWVVADLTSEAGREAVLARAREM-GG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIwDKILNVNVKSPALLLSQLLPYMEK-RKGAVTLVSSV--AAYFPrmelG--VYNVS 188
Cdd:PRK09072   81 INVLINNAGVNHFALLEDQDPEAI-ERLLALNLTAPMQLTRALLPLLRAqPSAMVVNVGSTfgSIGYP----GyaSYCAS 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK09072  156 KFALRGFSEALRRELADTGVRVLYLAPRATRTAM 189
PRK05866 PRK05866
SDR family oxidoreductase;
19-189 3.88e-15

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 73.62  E-value: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  19 LSVRMSSTGIDRKGilaERVaVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAE 98
Cdd:PRK05866   27 LINRPPRQPVDLTG---KRI-LLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAMAVPCDLSDLD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  99 DRERLVATALEHCGGIDFLVCCAGVNplVGSTLGTSEQIW---DKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVA 174
Cdd:PRK05866  103 AVDALVADVEKRIGGVDILINNAGRS--IRRPLAESLDRWhdvERTMVLNYYAPLRLIRGLAPGMlERGDGHIINVATWG 180

                         170
                  ....*....|....*.
gi 1622955129 175 AYFPRMEL-GVYNVSK 189
Cdd:PRK05866  181 VLSEASPLfSVYNASK 196
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-221 4.51e-15

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 73.02  E-value: 4.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVisSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK12481    6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIV--GVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK--GAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK12481   84 IDILINNAGI-IRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGngGKIINIASMLSFQGGIRVPSYTASKSA 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK12481  163 VMGLTRALATELSQYNINVNAIAPGYMATD 192
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-221 5.79e-15

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 74.49  E-value: 5.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVIssrkqqnVDRAAAQlqrEGLS-VAGIV------CHVGKAEDRERLVAT 106
Cdd:PRK08261  208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVC-------LDVPAAG---EALAaVANRVggtalaLDITAPDAPARIAEH 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVnpLVGSTLG-TSEQIWDKILNVNVKSP-----ALLLSQLLPymekRKGAVTLVSSVAayfprm 180
Cdd:PRK08261  278 LAERHGGLDIVVHNAGI--TRDKTLAnMDEARWDSVLAVNLLAPlriteALLAAGALG----DGGRIVGVSSIS------ 345

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622955129 181 elGV--------YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08261  346 --GIagnrgqtnYAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQ 392
PRK06182 PRK06182
short chain dehydrogenase; Validated
 37-222 7.01e-15

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 72.69  E-value: 7.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKqqnVDRAAAqlqregLSVAGIVC---HVGKAEDRERLVATALEHCGG 113
Cdd:PRK06182    4 KVALVTGASSGIGKATARRLAAQGYTVYGAARR---VDKMED------LASLGVHPlslDVTDEASIKAAVDTIIAEEGR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGvnplVGStLGTSEQI----WDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAA--YFPrmeLGV-Y 185
Cdd:PRK06182   75 IDVLVNNAG----YGS-YGAIEDVpideARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGkiYTP---LGAwY 146

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK06182  147 HATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTEW 183
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 34-220 1.53e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 71.72  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07523    8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVN---PLVgstlGTSEQIWDKILNVNVKSpALLLSQLL--PYMEKRKGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK07523   88 IDILVNNAGMQfrtPLE----DFPADAFERLLRTNISS-VFYVGQAVarHMIARGAGKIINIASVQSALARPGIAPYTAT 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07523  163 KGAVGNLTKGMATDWAKHGLQCNAIAPGYFDT 194
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 34-123 2.17e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 71.88  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK07109    6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGP 85

                          90
                  ....*....|
gi 1622955129 114 IDFLVCCAGV 123
Cdd:PRK07109   86 IDTWVNNAMV 95
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 37-222 2.29e-14

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: 70.49  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd05360     1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:cd05360    81 WVNNAGVA-VFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGgGALINVGSLLGYRSAPLQAAYSASKHAVRGF 159

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 196 TRTLALELAP--KDIRVNCLVPGVIKTDF 222
Cdd:cd05360   160 TESLRAELAHdgAPISVTLVQPTAMNTPF 188
PRK06484 PRK06484
short chain dehydrogenase; Validated
 24-220 2.47e-14

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 72.57  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  24 SSTGIDRKGILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEdreRL 103
Cdd:PRK06484  257 STAQAPSPLAESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVE---SA 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 104 VATALEHCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKrKGAVTLVSSVAAYFPRMELG 183
Cdd:PRK06484  334 FAQIQARWGRLDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQ-GGVIVNLGSIASLLALPPRN 412

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 184 VYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06484  413 AYCASKAAVTMLSRSLACEWAPAGIRVNTVAPGYIET 449
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-222 3.25e-14

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 70.18  E-value: 3.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGlSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYG-NIHYVVGDVSSTESARNVIEKAAKVLNA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGvnplvGSTLGTSEQI--WDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSV-AAYFPRMELGVYNVSKT 190
Cdd:PRK05786   82 IDGLVVTVG-----GYVEDTVEEFsgLEEMLTNHIKIPLYAVNASLRFL-KEGSSIVLVSSMsGIYKASPDQLSYAVAKA 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK05786  156 GLAKAVEILASELLGRGIRVNGIAPTTISGDF 187
PRK06949 PRK06949
SDR family oxidoreductase;
34-227 3.28e-14

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 70.56  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06949    7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGA--------VTLVSSVAAYFPRMELGV 184
Cdd:PRK06949   87 IDILVNNSGVST-TQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIARaKGAgntkpggrIINIASVAGLRVLPQIGL 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622955129 185 YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDW 227
Cdd:PRK06949  166 YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHW 208
PRK08340 PRK08340
SDR family oxidoreductase;
40-189 3.42e-14

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 70.60  E-value: 3.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGlSVAGIVCHVGKAEDRERLVATALEHCGGIDFLVC 119
Cdd:PRK08340    4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYG-EVYAVKADLSDKDDLKNLVKEAWELLGGIDALVW 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622955129 120 CAG---VNPLVGSTLGTSEqiWDKILNVNVKSPALLLSQLLP-YME-KRKGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK08340   83 NAGnvrCEPCMLHEAGYSD--WLEAALLHLVAPGYLTTLLIQaWLEkKMKGVLVYLSSVSVKEPMPPLVLADVTR 155
PRK05717 PRK05717
SDR family oxidoreductase;
37-220 5.80e-14

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 69.92  E-value: 5.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAgivCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK05717   11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIA---MDVADEAQVAAGVAEVLGQFGRLDA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLVGSTLGTSE-QIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:PRK05717   88 LVCNAAIADPHNTTLESLSlAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAASKGGLLAL 167

                         170       180
                  ....*....|....*....|....*
gi 1622955129 196 TRTLALELAPkDIRVNCLVPGVIKT 220
Cdd:PRK05717  168 THALAISLGP-EIRVNAVSPGWIDA 191
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 34-166 8.25e-14

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: 69.40  E-value: 8.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQ-------NVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVAT 106
Cdd:cd09762     1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgTIYTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVNPLVGsTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGA 166
Cdd:cd09762    81 AVEKFGGIDILVNNASAISLTG-TLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKSKNP 139
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 39-224 1.01e-13

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: 68.86  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVI-SSRKQQnvdrAAAQLQREGLSVAGIVCHVGKAEDRERLVATALE---HCGGI 114
Cdd:cd05325     1 VLITGASRGIGLELVRQLLARGNNTVIaTCRDPS----AATELAALGASHSRLHILELDVTDEIAESAEAVAerlGDAGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEK-RKGAVTLVSSVAAYFPRMELG---VYNVSKT 190
Cdd:cd05325    77 DVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKgARAKIINISSRVGSIGDNTSGgwySYRASKA 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:cd05325   157 ALNMLTKSLAVELKRDGITVVSLHPGWVRTDMGG 190
PRK06128 PRK06128
SDR family oxidoreductase;
32-220 1.16e-13

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 69.50  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS--SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALE 109
Cdd:PRK06128   51 GRLQGRKALITGADSGIGRATAIAFAREGADIALNylPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK06128  131 ELGGLDILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL-PPGASIINTGSIQSYQPSPTLLDYASTK 209

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06128  210 AAIVAFTKALAKQVAEKGIRVNAVAPGPVWT 240
PRK08264 PRK08264
SDR family oxidoreductase;
34-221 1.50e-13

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 68.38  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARR-LAQDGAHVVISSRkqqNVDRAAAQLQReglsVAGIVCHVGKAEDrerlVATALEHCG 112
Cdd:PRK08264    4 IKGKVVLVTGANRGIGRAFVEQlLARGAAKVYAAAR---DPESVTDLGPR----VVPLQLDVTDPAS----VAAAAEAAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK08264   73 DVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANgGGAIVNVLSVLSWVNFPNLGTYSASKAA 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08264  153 AWSLTQALRAELAPQGTRVLGVHPGPIDTD 182
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 34-231 1.55e-13

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 70.33  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLsvAGIVCHVGKAEDRERLVATALEHC-- 111
Cdd:COG3347   423 LAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYG--ADAVDATDVDVTAEAAVAAAFGFAgl 500

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 --GGIDFLVCCAGvnpLVGSTLGTSEQIWDKILNVNVKSPAL-LLSQLLPYMEKRKG----AVTLVSSVAAYFPRmELGV 184
Cdd:COG3347   501 diGGSDIGVANAG---IASSSPEEETRLSFWLNNFAHLSTGQfLVARAAFQGTGGQGlggsSVFAVSKNAAAAAY-GAAA 576

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622955129 185 YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWGAGG 231
Cdd:COG3347   577 AATAKAAAQHLLRALAAEGGANGINANRVNPDAVLDGSAIWASAARA 623
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-220 1.76e-13

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 68.56  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGST--SGIGFAIARRLAQDGAHVVISSRKQQNVD-----------RAAAQLQREGLSVAGIVCHVGKAEDR 100
Cdd:PRK12748    3 LMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTmpwgmhdkepvLLKEEIESYGVRCEHMEIDLSQPYAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 101 ERLVATALEHCGGIDFLV---CCAGVNPLvgSTLgTSEQIwDKILNVNVKSPaLLLSQLLP--YMEKRKGAVTLVSSVAA 175
Cdd:PRK12748   83 NRVFYAVSERLGDPSILInnaAYSTHTRL--EEL-TAEQL-DKHYAVNVRAT-MLLSSAFAkqYDGKAGGRIINLTSGQS 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622955129 176 YFP-RMELGvYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK12748  158 LGPmPDELA-YAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT 202
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 32-220 3.22e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 68.14  E-value: 3.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISS-RKQQNVDRAAAQLQREG---LSVAGivcHVGKAEDRERLVATA 107
Cdd:PRK06701   42 GKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYlDEHEDANETKQRVEKEGvkcLLIPG---DVSDEAFCKDAVEET 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 108 LEHCGGIDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSVAAYFPRMELGVYNV 187
Cdd:PRK06701  119 VRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQGSAIINTGSITGYEGNETLIDYSA 197

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06701  198 TKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWT 230
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 40-179 5.12e-13

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: 67.13  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGAHVVissrkqqNVDRaaaqlqREglsvAGIVCHVGKAEDRERLVATALEHCGG-IDFLV 118
Cdd:cd05328     3 VITGAASGIGAATAELLEDAGHTVI-------GIDL------RE----ADVIADLSTPEGRAAAIADVLARCSGvLDGLV 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622955129 119 CCAGVNPLVGStlgtseqiwDKILNVNVKSPALLLSQLLPYMEKRKG-AVTLVSSVAAYFPR 179
Cdd:cd05328    66 NCAGVGGTTVA---------GLVLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAGAGWA 118
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 36-216 5.62e-13

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 66.98  E-value: 5.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  36 ERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE-GLSVA-GIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK12384    2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEyGEGMAyGFGADATSEQSVLALSRGVDEIFGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGV---NPLVGSTLGTseqiWDKILNVNVKSPALLLSQLLPYMEKR--KGAVTLVSSVAAYFPRMELGVYNVS 188
Cdd:PRK12384   82 VDLLVYNAGIakaAFITDFQLGD----FDRSLQVNLVGYFLCAREFSRLMIRDgiQGRIIQINSKSGKVGSKHNSGYSAA 157

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPG 216
Cdd:PRK12384  158 KFGGVGLTQSLALDLAEYGITVHSLMLG 185
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 37-230 9.81e-13

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: 66.40  E-value: 9.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd08937     5 KVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSEL-VHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAG----VNPLVGSTLGTSEQIWDKILnvnvkSPALLLSQ-LLPYMEKRK-GAVTLVSSVAAyfpRMELGV-YNVSK 189
Cdd:cd08937    84 LINNVGgtiwAKPYEHYEEEQIEAEIRRSL-----FPTLWCCRaVLPHMLERQqGVIVNVSSIAT---RGIYRIpYSAAK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWGAG 230
Cdd:cd08937   156 GGVNALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAA 196
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 41-223 9.93e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 66.48  E-value: 9.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQnvDRAAAQLQREGLSVAgIVCHVGKAEDRERLVATALEHCGGIDFLVCC 120
Cdd:PRK06180    9 ITGVSSGFGRALAQAALAAGHRVVGTVRSEA--ARADFEALHPDRALA-RLLDVTDFDAIDAVVADAEATFGPIDVLVNN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 121 AGVnplvgSTLGTSEQIWD----KILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAY--FPRMelGVYNVSKTALL 193
Cdd:PRK06180   86 AGY-----GHEGAIEESPLaemrRQFEVNVFGAVAMTKAVLPGMrARRRGHIVNITSMGGLitMPGI--GYYCGSKFALE 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PRK06180  159 GISESLAKEVAPFGIHVTAVEPGSFRTDWA 188
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 34-221 1.28e-12

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: 66.32  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQ--LQREGLSVAgIVCHVGKAEDRERLVA-TALEH 110
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEeiEARGGKCIP-VRCDHSDDDEVEALFErVAREQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 111 CGGIDFLVCCA-GVNPLVGSTLG-----TSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGV 184
Cdd:cd09763    80 QGRLDILVNNAyAAVQLILVGVAkpfweEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEYLFNVA 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 185 YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd09763   160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTE 196
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 32-220 1.29e-12

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: 65.82  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTG--STSGIGFAIARRLAQDGAHVVISS---RKQQNVDRAAAQLQREGLsvagIVCHVGKAEDRERLVAT 106
Cdd:COG0623     1 GLLKGKRGLITGvaNDRSIAWGIAKALHEEGAELAFTYqgeALKKRVEPLAEELGSALV----LPCDVTDDEQIDALFDE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCC---AGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLvSSVAA--YFPrme 181
Cdd:COG0623    77 IKEKWGKLDFLVHSiafAPKEELGGRFLDTSREGFLLAMDISAYSLVALAKAAEPLMNEGGSIVTL-TYLGAerVVP--- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 182 lgVYN---VSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:COG0623   153 --NYNvmgVAKAALEASVRYLAADLGPKGIRVNAISAGPIKT 192
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 30-220 1.31e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 66.05  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  30 RKGILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIV-CHVGKA--EDRERLVAT 106
Cdd:PRK08945    6 KPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIpLDLLTAtpQNYQQLADT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVnplvgstLGT-------SEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFP 178
Cdd:PRK08945   86 IEEQFGRLDGVLHNAGL-------LGElgpmeqqDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSSVGRQG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 179 RMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK08945  159 RANWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRT 200
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 37-230 1.90e-12

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: 65.56  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGA---HVVISSR---KQQNVDRAAAQLQREGLSVAGI-VCHvgkaedrERLVATALE 109
Cdd:cd09806     1 TVVLITGCSSGIGLHLAVRLASDPSkrfKVYATMRdlkKKGRLWEAAGALAGGTLETLQLdVCD-------SKSVAAAVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGG--IDFLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYN 186
Cdd:cd09806    74 RVTErhVDVLVCNAGVG-LLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLPFNDVYC 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622955129 187 VSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWGAG 230
Cdd:cd09806   153 ASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVLGSP 196
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 37-144 2.63e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 65.08  E-value: 2.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:PRK07677    2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81

                          90       100
                  ....*....|....*....|....*...
gi 1622955129 117 LVCCAGVNPLVgSTLGTSEQIWDKILNV 144
Cdd:PRK07677   82 LINNAAGNFIC-PAEDLSVNGWNSVIDI 108
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 32-223 2.89e-12

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 65.19  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNvdrAAAQLQREGlsVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:PRK06463    3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN---EAKELREKG--VFTIKCDVGNRDQVKKSKEVVEKEF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGVNPLVgSTLGTSEQIWDKILNVNVKSPALLLSQLLPYME-KRKGAVTLVSSVAAYFPRME-LGVYNVSK 189
Cdd:PRK06463   78 GRVDVLVNNAGIMYLM-PFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKlSKNGAIVNIASNAGIGTAAEgTTFYAITK 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PRK06463  157 AGIIILTRRLAFELGKYGIRVNAVAPGWVETDMT 190
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 38-221 3.65e-12

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: 64.61  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAH--VVISSRKQQNVDRAAAQLQrEGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05367     1 VIILTGASRGIGRALAEELLKRGSPsvVVLLARSEEPLQELKEELR-PGLRVTTVKADLSDAAGVEQLLEAIRKLDGERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR--KGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:cd05367    80 LLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRglKKTVVNVSSGAAVNPFKGWGLYCSSKAARD 159

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 194 ALTRTLALELapKDIRVNCLVPGVIKTD 221
Cdd:cd05367   160 MFFRVLAAEE--PDVRVLSYAPGVVDTD 185
PRK07806 PRK07806
SDR family oxidoreductase;
32-177 4.19e-12

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 64.36  E-value: 4.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSR-KQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEH 110
Cdd:PRK07806    2 GDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRqKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622955129 111 CGGIDFLVccagVNPLVGSTLGTSEqiwDKILNVNVKSPALLLSQLLPYMEKrKGAVTLVSSVAAYF 177
Cdd:PRK07806   82 FGGLDALV----LNASGGMESGMDE---DYAMRLNRDAQRNLARAALPLMPA-GSRVVFVTSHQAHF 140
PRK05693 PRK05693
SDR family oxidoreductase;
38-224 4.46e-12

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 64.81  E-value: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVdraaAQLQREGLsvAGIVCHVGKAEDRERLVATALEHCGGIDFL 117
Cdd:PRK05693    3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDV----EALAAAGF--TAVQLDVNDGAALARLAEELEAEHGGLDVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 118 VCCAGVNPLvGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLALTR 197
Cdd:PRK05693   77 INNAGYGAM-GPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSD 155

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 198 TLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:PRK05693  156 ALRLELAPFGVQVMEVQPGAIASQFAS 182
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 39-220 6.44e-12

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: 62.98  E-value: 6.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQ--QNVDraaaqlqreglsvagivchvgkAEDRERLVAtALEHCGGIDF 116
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSgdYQVD----------------------ITDEASIKA-LFEKVGHFDA 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNPLVGSTLGTSEQiWDKILNVNVKSPALLLSQLLPYMEKRkGAVTLVSSVAAYFPRMELGVYNVSKTALLALT 196
Cdd:cd11731    58 IVSTAGDAEFAPLAELTDAD-FQRGLNSKLLGQINLVRHGLPYLNDG-GSITLTSGILAQRPIPGGAAAATVNGALEGFV 135

                         170       180
                  ....*....|....*....|....
gi 1622955129 197 RTLALELaPKDIRVNCLVPGVIKT 220
Cdd:cd11731   136 RAAAIEL-PRGIRINAVSPGVVEE 158
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 37-221 1.09e-11

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: 63.19  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGA-HVVISSRKQQNVDRAAAQLQreglsvAGIVCHVGKAEDRERLVATAlEHCGGID 115
Cdd:cd05354     4 KTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYG------DKVVPLRLDVTDPESIKAAA-AQAKDVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEK-RKGAVTLVSSVAAY--FPRMelGVYNVSKTAL 192
Cdd:cd05354    77 VVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKAnGGGAIVNLNSVASLknFPAM--GTYSASKSAA 154

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd05354   155 YSLTQGLRAELAAQGTLVLSVHPGPIDTR 183
PRK05993 PRK05993
SDR family oxidoreductase;
35-222 1.35e-11

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 63.51  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  35 AERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRaaaqLQREGLSVagIVCHVGKAEDRERLVATALEHCGG- 113
Cdd:PRK05993    3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAA----LEAEGLEA--FQLDYAEPESIAALVAQVLELSGGr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLV-----CCAG-VNPLvgSTLGTSEQiwdkiLNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYN 186
Cdd:PRK05993   77 LDALFnngayGQPGaVEDL--PTEALRAQ-----FEANFFGWHDLTRRVIPVMRKQGqGRIVQCSSILGLVPMKYRGAYN 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 187 VSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK05993  150 ASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRF 185
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 41-225 1.86e-11

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 62.85  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqreGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFLVCC 120
Cdd:PRK10538    5 VTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDEL---GDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 121 AGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLALTRTL 199
Cdd:PRK10538   82 AGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMvERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNL 161

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 200 ALELAPKDIRVNCLVPGVIK-TDFSKV 225
Cdd:PRK10538  162 RTDLHGTAVRVTDIEPGLVGgTEFSNV 188
PRK09291 PRK09291
SDR family oxidoreductase;
41-222 2.26e-11

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 62.71  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERlvatALEHcgGIDFLVCC 120
Cdd:PRK09291    7 ITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTALRAEAARRGLALRVEKLDLTDAIDRAQ----AAEW--DVDVLLNN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 121 AGVnplvgstlGTSEQIWD-------KILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:PRK09291   81 AGI--------GEAGAVVDipvelvrELFETNVFGPLELTQGFVRKMvARGKGKVVFTSSMAGLITGPFTGAYCASKHAL 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK09291  153 EAIAEAMHAELKPFGIQVATVNPGPYLTGF 182
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 36-220 2.62e-11

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: 62.54  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  36 ERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQR--EGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:cd05330     3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiaPDAEVLLIKADVSDEAQVEAYVDATVEQFGR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNVSKTAL 192
Cdd:cd05330    83 IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQSGYAAAKHGV 162

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05330   163 VGLTRNSAVEYGQYGIRINAIAPGAILT 190
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
34-224 3.03e-11

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 61.95  E-value: 3.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVI-----SSRKQQNVDRAAAQlqreGLSVAGIVCHVGKAEDRERLVATAL 108
Cdd:PRK12938    1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpnSPRRVKWLEDQKAL----GFDFIASEGNVGDWDSTKAAFDKVK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 109 EHCGGIDFLVCCAGVNPLVGSTLGTSEQiWDKILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELGVYNV 187
Cdd:PRK12938   77 AEVGEIDVLVNNAGITRDVVFRKMTRED-WTAVIDTNLTSLFNVTKQVIDGMVERGwGRIINISSVNGQKGQFGQTNYST 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:PRK12938  156 AKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVK 192
PRK12744 PRK12744
SDR family oxidoreductase;
34-222 3.54e-11

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 62.06  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVI----SSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALE 109
Cdd:PRK12744    6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAihynSAASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGvNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSS-VAAYFPRMelGVYNVS 188
Cdd:PRK12744   86 AFGRPDIAINTVG-KVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDNGKIVTLVTSlLGAFTPFY--SAYAGS 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:PRK12744  163 KAPVEHFTRAASKEFGARGISVTAVGPGPMDTPF 196
PRK07775 PRK07775
SDR family oxidoreductase;
35-220 4.04e-11

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 62.08  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  35 AERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGI 114
Cdd:PRK07775    9 DRRPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGvNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:PRK07775   89 EVLVSGAG-DTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMiERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLE 167

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07775  168 AMVTNLQMELEGTGVRASIVHPGPTLT 194
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 39-220 4.20e-11

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: 61.83  E-value: 4.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTG--STSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF 116
Cdd:cd05372     4 ILITGiaNDRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLAERLGESALVLPCDVSNDEEIKELFAEVKKDWGKLDG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVNP---LVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLvSSVAA--YFPrmELGVYNVSKTA 191
Cdd:cd05372    84 LVHSIAFAPkvqLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNPGGSIVTL-SYLGSerVVP--GYNVMGVAKAA 160

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd05372   161 LESSVRYLAYELGRKGIRVNAISAGPIKT 189
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 37-241 4.70e-11

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: 61.44  E-value: 4.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVI--SSRKQqnvdraAAQLQREGLSVAGIVCHvgKAEDRERLVATALEHCGGI 114
Cdd:cd05361     2 SIALVTHARHFAGPASAEALTEDGYTVVChdASFAD------AAERQAFESENPGTKAL--SEQKPEELVDAVLQAGGAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGA-VTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:cd05361    74 DVLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGsIIFITSAVPKKPLAYNSLYGPARAAAV 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622955129 194 ALTRTLALELAPKDIRVNCLVPGVIKTD--FSKVDWGAGGLCRNRVLPVL 241
Cdd:cd05361   154 ALAESLAKELSRDNILVYAIGPNFFNSPtyFPTSDWENNPELRERVKRDV 203
PRK07832 PRK07832
SDR family oxidoreductase;
39-220 5.66e-11

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 61.60  E-value: 5.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAgiVCHVGKAEDRERLVATALE-HC--GGID 115
Cdd:PRK07832    3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVP--EHRALDISDYDAVAAFAADiHAahGSMD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVnplvgSTLGTSEQI----WDKILNVNVKSPALLLSQLLPYMEK--RKGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK07832   81 VVMNIAGI-----SAWGTVDRLtheqWRRMVDVNLMGPIHVIETFVPPMVAagRGGHLVNVSSAAGLVALPWHAAYSASK 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07832  156 FGLRGLSEVLRFDLARHGIGVSVVVPGAVKT 186
PRK08267 PRK08267
SDR family oxidoreductase;
41-221 7.08e-11

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 61.11  E-value: 7.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLsVAGIVCHVGKAEDRERLVATALEHCGGIDFLVCC 120
Cdd:PRK08267    6 ITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNA-WTGALDVTDRAAWDAALADFAAATGGRLDVLFNN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 121 AGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-VSSVAAYFPRMELGVYNVSKTALLALTRTL 199
Cdd:PRK08267   85 AGI-LRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVInTSSASAIYGQPGLAVYSATKFAVRGLTEAL 163

                         170       180
                  ....*....|....*....|..
gi 1622955129 200 ALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08267  164 DLEWRRHGIRVADVMPLFVDTA 185
PRK08703 PRK08703
SDR family oxidoreductase;
34-220 9.23e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 60.72  E-value: 9.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREG-LSVAGIVCHVGKAEDRE--RLVAT-ALE 109
Cdd:PRK08703    4 LSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGhPEPFAIRFDLMSAEEKEfeQFAATiAEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAG----VNPLVGSTLGTseqiWDKILNVNVKSPALLLSQLLPYMEKRKGA-VTLVSSVAAYFPRMELGV 184
Cdd:PRK08703   84 TQGKLDGIVHCAGyfyaLSPLDFQTVAE----WVNQYRINTVAPMGLTRALFPLLKQSPDAsVIFVGESHGETPKAYWGG 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 185 YNVSKTALLALTRTLALELAP-KDIRVNCLVPGVIKT 220
Cdd:PRK08703  160 FGASKAALNYLCKVAADEWERfGNLRANVLVPGPINS 196
PRK06123 PRK06123
SDR family oxidoreductase;
35-221 1.08e-10

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 60.56  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  35 AERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRK-QQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06123    1 MRKVMIITGASRGIGAATALLAAERGYAVCLNYLRnRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRK----GAVTLVSSVAAyfprmELGV----- 184
Cdd:PRK06123   81 LDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHggrgGAIVNVSSMAA-----RLGSpgeyi 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622955129 185 -YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK06123  156 dYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTE 193
PLN02253 PLN02253
xanthoxin dehydrogenase
 23-223 1.58e-10

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 60.22  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  23 MSSTGIDRKGILAER----VAVVTGSTSGIGFAIARRLAQDGAHVVISsrkqqNVDRAAAQLQREGL----SVAGIVCHV 94
Cdd:PLN02253    1 MATASSSASSLPSQRllgkVALVTGGATGIGESIVRLFHKHGAKVCIV-----DLQDDLGQNVCDSLggepNVCFFHCDV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  95 GKAEDRERLVATALEHCGGIDFLVCCAGV-NPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSS 172
Cdd:PLN02253   76 TVEDDVSRAVDFTVDKFGTLDIMVNNAGLtGPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMiPLKKGSIVSLCS 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622955129 173 VAAYFPRMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PLN02253  156 VASAIGGLGPHAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALA 206
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
34-221 2.27e-10

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 59.50  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVV---ISSRKQqnvdrAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEH 110
Cdd:PRK08993    8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVginIVEPTE-----TIEQVTALGRRFLSLTADLRKIDGIPALLERAVAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 111 CGGIDFLVCCAGVnPLVGSTLGTSEQIWDKILNVNVKSpALLLSQLLP--YMEKRKGAVTL-VSSVAAYFPRMELGVYNV 187
Cdd:PRK08993   83 FGHIDILVNNAGL-IRREDAIEFSEKDWDDVMNLNIKS-VFFMSQAAAkhFIAQGNGGKIInIASMLSFQGGIRVPSYTA 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622955129 188 SKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08993  161 SKSGVMGVTRLMANEWAKHNINVNAIAPGYMATN 194
PRK12742 PRK12742
SDR family oxidoreductase;
37-226 2.59e-10

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 59.39  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNvdrAAAQLQREGLSVAGIVchvgKAEDRERLVATALEHcGGIDF 116
Cdd:PRK12742    7 KKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKD---AAERLAQETGATAVQT----DSADRDAVIDVVRKS-GALDI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSVAA-YFPRMELGVYNVSKTALLAL 195
Cdd:PRK12742   79 LVVNAGI-AVFGDALELDADDIDRLFKINIHAPYHASVEAARQM-PEGGRIIIIGSVNGdRMPVAGMAAYAASKSALQGM 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFSKVD 226
Cdd:PRK12742  157 ARGLARDFGPRGITINVVQPGPIDTDANPAN 187
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 34-169 3.94e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 58.90  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqrEGLSVAGIVCHV---GKAEDRERLVATAleh 110
Cdd:PRK06125    5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADL--RAAHGVDVAVHAldlSSPEAREQLAAEA--- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622955129 111 cGGIDFLVCCAGVNPlVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL 169
Cdd:PRK06125   80 -GDIDILVNNAGAIP-GGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIV 136
PRK07041 PRK07041
SDR family oxidoreductase;
40-220 4.41e-10

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 58.51  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQrEGLSVAGIVCHVGKAEDRERLVATAlehcGGIDFLVC 119
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALG-GGAPVRTAALDITDEAAVDAFFAEA----GPFDHVVI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 120 CAGVN---PLVGSTLGTSEQIWD-KILNvnvkspALLLSQlLPYMEKRkGAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:PRK07041   76 TAADTpggPVRALPLAAAQAAMDsKFWG------AYRVAR-AARIAPG-GSLTFVSGFAAVRPSASGVLQGAINAALEAL 147

                         170       180
                  ....*....|....*....|....*
gi 1622955129 196 TRTLALELAPkdIRVNCLVPGVIKT 220
Cdd:PRK07041  148 ARGLALELAP--VRVNTVSPGLVDT 170
PRK09730 PRK09730
SDR family oxidoreductase;
38-221 4.58e-10

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 58.71  E-value: 4.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAHVVISSrkQQNVDRA---AAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGI 114
Cdd:PRK09730    3 IALVTGGSRGIGRATALLLAQEGYTVAVNY--QQNLHAAqevVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVnPLVGSTLG--TSEQIwDKILNVNVKSPALLLSQLLPYMEKRKG----AVTLVSSVAAyfprmELGV---- 184
Cdd:PRK09730   81 AALVNNAGI-LFTQCTVEnlTAERI-NRVLSTNVTGYFLCCREAVKRMALKHGgsggAIVNVSSAAS-----RLGApgey 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622955129 185 --YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK09730  154 vdYAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTE 192
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 32-215 6.84e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 58.53  E-value: 6.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTGSTSGIGFAIARRLAQDGAHVVIS----SRKQQNVDRAAAQlqregLSVAGIVCHVGKA---------- 97
Cdd:PRK07791    2 GLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNdigvGLDGSASGGSAAQ-----AVVDEIVAAGGEAvangddiadw 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  98 EDRERLVATALEHCGGIDFLVCCAGVnpLVGSTL-GTSEQIWDKILNVNVKSPALLLSQLLPYM-------EKRKGAVTL 169
Cdd:PRK07791   77 DGAANLVDAAVETFGGLDVLVNNAGI--LRDRMIaNMSEEEWDAVIAVHLKGHFATLRHAAAYWraeskagRAVDARIIN 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622955129 170 VSSVAAYFPRMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVP 215
Cdd:PRK07791  155 TSSGAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAP 200
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 41-221 7.04e-10

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: 57.85  E-value: 7.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGlsvagivCHVGKAE--DRERLVATALEHC----GGI 114
Cdd:cd08931     5 ITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAEN-------VVAGALDvtDRAAWAAALADFAaatgGRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVnplvgSTLGTSEQI----WDKILNVNVKSPALLLSQLLPYMEKRKGA-VTLVSSVAAYFPRMELGVYNVSK 189
Cdd:cd08931    78 DALFNNAGV-----GRGGPFEDVplaaHDRMVDINVKGVLNGAYAALPYLKATPGArVINTASSSAIYGQPDLAVYSATK 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd08931   153 FAVRGLTEALDVEWARHGIRVADVWPWFVDTP 184
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 38-222 1.53e-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: 57.01  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQR--EGLSVAgIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRdaGGSAKA-VPTDARDEDEVIALFDLIEEEIGPLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGAVTLVSSVAAYFPRMELGVYNVSKTALLA 194
Cdd:cd05373    80 VLVYNAGAN-VWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARgRGTIIFTGATASLRGRAGFAAFAGAKFALRA 158

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 195 LTRTLALELAPKDIRV-NCLVPGVIKTDF 222
Cdd:cd05373   159 LAQSMARELGPKGIHVaHVIIDGGIDTDF 187
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 36-223 1.93e-09

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 56.97  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  36 ERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVChvgkaeDRE---RLVATALEHCG 112
Cdd:PRK08263    3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVT------DRAavfAAVETAVEHFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 GIDFLVCCAGvNPLVGSTLGTSEQIWDKILNVNVKSpALLLSQ-LLPYM-EKRKGAVTLVSSVAAY--FPRMelGVYNVS 188
Cdd:PRK08263   77 RLDIVVNNAG-YGLFGMIEEVTESEARAQIDTNFFG-ALWVTQaVLPYLrEQRSGHIIQISSIGGIsaFPMS--GIYHAS 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PRK08263  153 KWALEGMSEALAQEVAEFGIKVTLVEPGGYSTDWA 187
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-225 1.98e-09

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 57.02  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNvdrAAAQLQRE-GLSVAGIVCHVGKAEDRERLVATALEHCG 112
Cdd:PRK08642    3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSED---AAEALADElGDRAIALQADVTDREQVQAMFATATEHFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 113 -GIDFLVCCAGV----NPLVGSTLGTSEqiWD---KILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVAAYFPRMELG 183
Cdd:PRK08642   80 kPITTVVNNALAdfsfDGDARKKADDIT--WEdfqQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNLFQNPVVPYH 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622955129 184 VYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIK-TDFSKV 225
Cdd:PRK08642  158 DYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRtTDASAA 200
PRK07102 PRK07102
SDR family oxidoreductase;
41-174 2.83e-09

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 56.09  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQ-REGLSVAgivCHVGKAEDRERLvATALEHCGGIDFLVC 119
Cdd:PRK07102    6 IIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRaRGAVAVS---THELDILDTASH-AAFLDSLPALPDIVL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622955129 120 CAgvnplVGsTLGT---SEQIWD---KILNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSVA 174
Cdd:PRK07102   82 IA-----VG-TLGDqaaCEADPAlalREFRTNFEGPIALLTLLANRFEARGsGTIVGISSVA 137
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 39-222 4.03e-09

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 54.83  E-value: 4.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGA-HVVISSRKqqnvdraaaqlqreglsvagivchvgkaedrerlvatalehcggiDFL 117
Cdd:cd02266     1 VLVTGGSGGIGGAIARWLASRGSpKVLVVSRR---------------------------------------------DVV 35

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 118 VCCAGVnPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYM-EKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLALT 196
Cdd:cd02266    36 VHNAAI-LDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMkAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGLA 114

                         170       180
                  ....*....|....*....|....*.
gi 1622955129 197 RTLALELAPKDIRVNCLVPGVIKTDF 222
Cdd:cd02266   115 QQWASEGWGNGLPATAVACGTWAGSG 140
PRK06196 PRK06196
oxidoreductase; Provisional
 27-123 6.07e-09

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 55.84  E-value: 6.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  27 GIDRKGilaeRVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLqrEGLSVAGIvcHVGKAEDRERLVAT 106
Cdd:PRK06196   21 GHDLSG----KTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI--DGVEVVML--DLADLESVRAFAER 92

                          90
                  ....*....|....*..
gi 1622955129 107 ALEHCGGIDFLVCCAGV 123
Cdd:PRK06196   93 FLDSGRRIDILINNAGV 109
PRK08017 PRK08017
SDR family oxidoreductase;
40-223 1.30e-08

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 54.32  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAaaqlqrEGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFLVC 119
Cdd:PRK08017    6 LITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARM------NSLGFTGILLDLDDPESVERAADEVIALTDNRLYGLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 120 CAGVNPLVGSTLGTSEQIWDKILNVNV----KSPALLLSQLLPYMEKRkgaVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:PRK08017   80 NNAGFGVYGPLSTISRQQMEQQFSTNFfgthQLTMLLLPAMLPHGEGR---IVMTSSVMGLISTPGRGAYAASKYALEAW 156

                         170       180
                  ....*....|....*....|....*...
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFS 223
Cdd:PRK08017  157 SDALRMELRHSGIKVSLIEPGPIRTRFT 184
PRK07024 PRK07024
SDR family oxidoreductase;
40-220 1.97e-08

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 53.78  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQreglsvAGIVCHVGKAE--DRERLVATA---LEHCGGI 114
Cdd:PRK07024    6 FITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLP------KAARVSVYAADvrDADALAAAAadfIAAHGLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNplVGSTLGTSEQI--WDKILNVNVKSpalLLSQLLPYME--KRKGAVTLV--SSVAAYFPRMELGVYNVS 188
Cdd:PRK07024   80 DVVIANAGIS--VGTLTEEREDLavFREVMDTNYFG---MVATFQPFIApmRAARRGTLVgiASVAGVRGLPGAGAYSAS 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07024  155 KAAAIKYLESLRVELRPAGVRVVTIAPGYIRT 186
PRK07577 PRK07577
SDR family oxidoreductase;
37-238 1.98e-08

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 53.58  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnvDRAAAQLqreglsvagIVCHVGKAEDRERLVATALEHcGGIDF 116
Cdd:PRK07577    4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARSAI--DDFPGEL---------FACDLADIEQTAATLAQINEI-HPVDA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGV---NPLVGSTLGTSEQIWDkiLNVNVkspALLLSQ-LLPYME-KRKGAVTLVSSVAAyFPRMELGVYNVSKTA 191
Cdd:PRK07577   72 IVNNVGIalpQPLGKIDLAALQDVYD--LNVRA---AVQVTQaFLEGMKlREQGRIVNICSRAI-FGALDRTSYSAAKSA 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTDFSKVDWGAGGLCRNRVL 238
Cdd:PRK07577  146 LVGCTRTWALELAEYGITVNAVAPGPIETELFRQTRPVGSEEEKRVL 192
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-216 2.64e-08

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 53.64  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGST--SGIGFAIARRLAQDGAHVVIS-------SRKQQNVDRAAAQLQRE----GLSVAGIVCHVGKAEDR 100
Cdd:PRK12859    4 LKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTywtaydkEMPWGVDQDEQIQLQEEllknGVKVSSMELDLTQNDAP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 101 ERLVATALEHCGGIDFLV--CCAGVNpLVGSTLgTSEQIwDKILNVNVKSPALLLSQLLPYMEKRKGAvTLVSSVAAYFP 178
Cdd:PRK12859   84 KELLNKVTEQLGYPHILVnnAAYSTN-NDFSNL-TAEEL-DKHYMVNVRATTLLSSQFARGFDKKSGG-RIINMTSGQFQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622955129 179 RMELG--VYNVSKTALLALTRTLALELAPKDIRVNCLVPG 216
Cdd:PRK12859  160 GPMVGelAYAATKGAIDALTSSLAAEVAHLGITVNAINPG 199
PRK09134 PRK09134
SDR family oxidoreductase;
35-216 2.68e-08

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 53.39  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  35 AERVAVVTGSTSGIGFAIARRLAQDGAHVVI-SSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK09134    8 APRAALVTGAARRIGRAIALDLAAHGFDVAVhYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAALGP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVnpLVGSTLGT-SEQIWDKILNVNVKSPALL---LSQLLPymEKRKGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK09134   88 ITLLVNNASL--FEYDSAASfTRASWDRHMATNLRAPFVLaqaFARALP--ADARGLVVNMIDQRVWNLNPDFLSYTLSK 163

                         170       180
                  ....*....|....*....|....*..
gi 1622955129 190 TALLALTRTLALELAPKdIRVNCLVPG 216
Cdd:PRK09134  164 AALWTATRTLAQALAPR-IRVNAIGPG 189
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 38-220 3.20e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 53.48  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGStSGIGFAIARRLAQdGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHcGGIDFL 117
Cdd:PRK06940    4 VVVVIGA-GGIGQAIARRVGA-GKKVLLADYNEENLEAAAKTLREAGFDVSTQEVDVSSRESVKALAATAQTL-GPVTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 118 VCCAGVNPLVGSTlgtseqiwDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRM----------------- 180
Cdd:PRK06940   81 VHTAGVSPSQASP--------EAILKVDLYGTALVLEEFGKVIAPGGAGVVIASQSGHRLPALtaeqeralattpteell 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622955129 181 ------------ELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06940  153 slpflqpdaiedSLHAYQIAKRANALRVMAEAVKWGERGARINSISPGIIST 204
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 37-83 3.51e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 53.49  E-value: 3.51e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE 83
Cdd:PRK06197   17 RVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAAARITAA 63
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 40-123 4.78e-08

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: 51.71  E-value: 4.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129   40 VVTGSTSGIGFAIARRLAQDGA-HVVISSR---KQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLSRsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83


                   ....*...
gi 1622955129  116 FLVCCAGV 123
Cdd:smart00822  84 GVIHAAGV 91
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 41-220 8.73e-08

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 52.28  E-value: 8.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVvISSRKQQNVDrAAAQLQR---EGLSVagIVCHVGKAEDRERLVATALEHCG--GID 115
Cdd:cd09805     5 ITGCDSGFGNLLAKKLDSLGFTV-LAGCLTKNGP-GAKELRRvcsDRLRT--LQLDVTKPEQIKRAAQWVKEHVGekGLW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMELGVYNVSKTALLAL 195
Cdd:cd09805    81 GLVNNAGILGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                         170       180
                  ....*....|....*....|....*
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:cd09805   161 SDSLRRELQPWGVKVSIIEPGNFKT 185
PRK05854 PRK05854
SDR family oxidoreductase;
34-83 1.38e-07

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 51.61  E-value: 1.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE 83
Cdd:PRK05854   12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIRTA 61
PRK06914 PRK06914
SDR family oxidoreductase;
37-221 1.47e-07

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 51.56  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSR---KQQNVDRAAAQLQREGlSVAGIVCHVGKAEDRERLVATALEHcGG 113
Cdd:PRK06914    4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRnpeKQENLLSQATQLNLQQ-NIKVQQLDVTDQNSIHNFQLVLKEI-GR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IDFLVCCAGVnpLVGstlGTSEQI----WDKILNVNVKSPALLLSQLLPYMEKRKGA-VTLVSSVAAY--FPrmELGVYN 186
Cdd:PRK06914   82 IDLLVNNAGY--ANG---GFVEEIpveeYRKQFETNVFGAISVTQAVLPYMRKQKSGkIINISSISGRvgFP--GLSPYV 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 187 VSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK06914  155 SSKYALEGFSESLRLELKPFGIDVALIEPGSYNTN 189
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 40-175 1.59e-07

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: 50.25  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGA-HVVISSRKQQNVDRAAA---QLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLSRSAAPRPDAQAliaELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622955129 116 FLVCCAGV---NPLVGSTLGTseqiWDKILNVNVKSpALLLSQLLPYMEKRkgAVTLVSSVAA 175
Cdd:pfam08659  84 GVIHAAGVlrdALLENMTDED----WRRVLAPKVTG-TWNLHEATPDEPLD--FFVLFSSIAG 139
PRK06947 PRK06947
SDR family oxidoreductase;
37-221 1.80e-07

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 50.96  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVIS-SRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVGINyARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGV----NPLVGSTLGTSEQIWDkilnVNVKSPALLLSQLLPYMEK----RKGAVTLVSSVAAYF--PRmELGVY 185
Cdd:PRK06947   83 ALVNNAGIvapsMPLADMDAARLRRMFD----TNVLGAYLCAREAARRLSTdrggRGGAIVNVSSIASRLgsPN-EYVDY 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK06947  158 AGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETE 193
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 37-220 2.25e-07

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: 50.40  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVissrkqqNVDRAAAQLQREGLSVAGIVCHVgkaEDRERLVATALEHCGGIDF 116
Cdd:cd05334     2 RVVLVYGGRGALGSAVVQAFKSRGWWVA-------SIDLAENEEADASIIVLDSDSFT---EQAKQVVASVARLSGKVDA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGvnPLVGSTL--GTSEQIWDKILNVNVKSpALLLSQL-LPYMEKrKGAVTLVSSVAAYFPRMELGVYNVSKTALL 193
Cdd:cd05334    72 LICVAG--GWAGGSAksKSFVKNWDLMWKQNLWT-SFIASHLaTKHLLS-GGLLVLTGAKAALEPTPGMIGYGAAKAAVH 147

                         170       180
                  ....*....|....*....|....*....
gi 1622955129 194 ALTRTLALEL--APKDIRVNCLVPGVIKT 220
Cdd:cd05334   148 QLTQSLAAENsgLPAGSTANAILPVTLDT 176
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 38-178 2.98e-07

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 51.21  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQD-GAHVVISSR-----KQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:cd08953   207 VYLVTGGAGGIGRALARALARRyGARLVLLGRsplppEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERY 286

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622955129 112 GGIDFLVCCAGVNPlvGSTLGT-SEQIWDKILNVNVKSpALLLSQLLPYMEKRkgAVTLVSSVAAYFP 178
Cdd:cd08953   287 GAIDGVIHAAGVLR--DALLAQkTAEDFEAVLAPKVDG-LLNLAQALADEPLD--FFVLFSSVSAFFG 349
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 39-123 6.00e-07

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 49.82  E-value: 6.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGA-HVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFL 117
Cdd:cd09810     4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDAL 83


                  ....*.
gi 1622955129 118 VCCAGV 123
Cdd:cd09810    84 VCNAAV 89
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
34-220 8.56e-07

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 48.94  E-value: 8.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTG--STSGIGFAIARRLAQDGAHVVIS------SRKQQNVDRAAAQLQREGLsvagIVCHVGKAEDRERLVA 105
Cdd:PRK07370    4 LTGKKALVTGiaNNRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVRELTEPLNPSLF----LPCDVQDDAQIEETFE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 106 TALEHCGGIDFLVCC---AGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-----VSSVAAYf 177
Cdd:PRK07370   80 TIKQKWGKLDILVHClafAGKEELIGDFSATSREGFARALEISAYSLAPLCKAAKPLMSEGGSIVTLtylggVRAIPNY- 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622955129 178 prmelGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07370  159 -----NVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRT 196
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
40-176 1.49e-06

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 48.44  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAqlqreglsVAGIVCHVGKAEDRERLvataLEHCGGIDFLVC 119
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAA--------LPGVEFVRGDLRDPEAL----AAALAGVDAVVH 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622955129 120 CAGVnplvgstLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRkgaVTLVSSVAAY 176
Cdd:COG0451    71 LAAP-------AGVGEEDPDETLEVNVEGTLNLLEAARAAGVKR---FVYASSSSVY 117
PRK06139 PRK06139
SDR family oxidoreductase;
30-123 1.81e-06

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 48.56  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  30 RKGILAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALE 109
Cdd:PRK06139    1 MMGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAAS 80

                          90
                  ....*....|....
gi 1622955129 110 HCGGIDFLVCCAGV 123
Cdd:PRK06139   81 FGGRIDVWVNNVGV 94
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 37-83 2.45e-06

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: 47.98  E-value: 2.45e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE 83
Cdd:cd09809     2 KVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEE 48
PRK06482 PRK06482
SDR family oxidoreductase;
41-240 4.16e-06

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 47.03  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQlQREGLSVAgiVCHVGKAEDRERLVATALEHCGGIDFLVCC 120
Cdd:PRK06482    7 ITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKAR-YGDRLWVL--QLDVTDSAAVRAVVDRAFAALGRIDVVVSN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 121 AGVNpLVGSTLG-TSEQIWDKIlNVNVKSPALLLSQLLPYMEKRKGA-VTLVSSV---AAYfPRMelGVYNVSKTALLAL 195
Cdd:PRK06482   84 AGYG-LFGAAEElSDAQIRRQI-DTNLIGSIQVIRAALPHLRRQGGGrIVQVSSEggqIAY-PGF--SLYHATKWGIEGF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622955129 196 TRTLALELAPKDIRVNCLVPGVIKTDFSKvdwgagGLCRNRVLPV 240
Cdd:PRK06482  159 VEAVAQEVAPFGIEFTIVEPGPARTNFGA------GLDRGAPLDA 197
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 34-152 7.40e-06

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 46.70  E-value: 7.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISS-RKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEhCG 112
Cdd:PRK07792   10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDvASALDASDVLDEIRAAGAKAVAVAGDISQRATADELVATAVG-LG 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 113 GIDFLVCCAGV--NPLVGStlgTSEQIWDKILNVNVKSPALL 152
Cdd:PRK07792   89 GLDIVVNNAGItrDRMLFN---MSDEEWDAVIAVHLRGHFLL 127
PRK06953 PRK06953
SDR family oxidoreductase;
37-172 7.51e-06

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 45.83  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAqLQREGLSV----AGIVCHVGKAEDRERLvatalehcg 112
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQA-LGAEALALdvadPASVAGLAWKLDGEAL--------- 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622955129 113 giDFLVCCAGV-NPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSS 172
Cdd:PRK06953   72 --DAAVYVAGVyGPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVLAVLSS 130
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 37-216 1.03e-05

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: 45.92  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE-GLSVAGIVCHVGKAEDRERLVATALEHCGGID 115
Cdd:cd05322     3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEyGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGV---NPLVGSTLGTseqiWDKILNVNVKSPALLLSQLLPYMEKR--KGAVTLVSSVAAYFPRMELGVYNVSKT 190
Cdd:cd05322    83 LLVYSAGIaksAKITDFELGD----FDRSLQVNLVGYFLCAREFSKLMIRDgiQGRIIQINSKSGKVGSKHNSGYSAAKF 158

                         170       180
                  ....*....|....*....|....*.
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLVPG 216
Cdd:cd05322   159 GGVGLTQSLALDLAEHGITVNSLMLG 184
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
37-225 1.13e-05

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 45.83  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLS-VAGIVCHVGKAED--RERLVATALEHCGG 113
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEQYNSNLTfHSLDLQDVHELETnfNEILSSIQEDNVSS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 114 IdFLVCCAG-VNPLVGSTLGTSEQIwDKILNVNVKSPALLLSQLLPYMEKRKGAVTLV--SSVAAYFPRMELGVYNVSKT 190
Cdd:PRK06924   82 I-HLINNAGmVAPIKPIEKAESEEL-ITNVHLNLLAPMILTSTFMKHTKDWKVDKRVIniSSGAAKNPYFGWSAYCSSKA 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622955129 191 ALLALTRTLALELAPKDIRVNCLV--PGVIKTDFSKV 225
Cdd:PRK06924  160 GLDMFTQTVATEQEEEEYPVKIVAfsPGVMDTNMQAQ 196
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
48-220 1.29e-05

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 45.50  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  48 IGFAIARRLAQDGAHVVI---SSRKQQNVDRAAAQLQREGLsvagIVCHVGKAEDRERLVATALEHCGGIDFLVCCAGVN 124
Cdd:PRK08415   19 IAYGIAKACFEQGAELAFtylNEALKKRVEPIAQELGSDYV----YELDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 125 P---LVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTL-----VSSVAAYfprmelGVYNVSKTALLALT 196
Cdd:PRK08415   95 PkeaLEGSFLETSKEAFNIAMEISVYSLIELTRALLPLLNDGASVLTLsylggVKYVPHY------NVMGVAKAALESSV 168

                         170       180
                  ....*....|....*....|....
gi 1622955129 197 RTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK08415  169 RYLAVDLGKKGIRVNAISAGPIKT 192
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 38-217 1.51e-05

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: 45.30  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAHVVISSRK-QQNVDRAAAQLQREGLSVAgIVCH-----VGKAEDR-ERLVATALEH 110
Cdd:TIGR02685   3 AAVVTGAAKRIGSSIAVALHQEGYRVVLHYHRsAAAASTLAAELNARRPNSA-VTCQadlsnSATLFSRcEAIIDACFRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 111 CGGIDFLVCCAGV---NPLV----GSTLGTSEQIWDKILNV---NVKSPALLLS-----QLLPYMEKRKGAVTLVSSVAA 175
Cdd:TIGR02685  82 FGRCDVLVNNASAfypTPLLrgdaGEGVGDKKSLEVQVAELfgsNAIAPYFLIKafaqrQAGTRAEQRSTNLSIVNLCDA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622955129 176 Y--FPRMELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGV 217
Cdd:TIGR02685 162 MtdQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL 205
PRK06720 PRK06720
hypothetical protein; Provisional
 34-123 1.80e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 44.19  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGG 113
Cdd:PRK06720   14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEALFVSYDMEKQGDWQRVISITLNAFSR 93

                          90
                  ....*....|
gi 1622955129 114 IDFLVCCAGV 123
Cdd:PRK06720   94 IDMLFQNAGL 103
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
32-220 1.84e-05

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 44.93  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTG--STSGIGFAIARrLAQD-GAHVVISS--RKQQNVDRAAAQLQREGlsvAGIVCHVGKAEDRERLVAT 106
Cdd:PRK07889    3 GLLEGKRILVTGviTDSSIAFHVAR-VAQEqGAEVVLTGfgRALRLTERIAKRLPEPA---PVLELDVTNEEHLASLADR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVNPlvGSTLGTS--EQIWD---KILNVNVKSPALLLSQLLPYMeKRKGAVtlvssVAAYF-PRM 180
Cdd:PRK07889   79 VREHVDGLDGVVHSIGFAP--QSALGGNflDAPWEdvaTALHVSAYSLKSLAKALLPLM-NEGGSI-----VGLDFdATV 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622955129 181 ELGVYN---VSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK07889  151 AWPAYDwmgVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRT 193
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 40-125 3.01e-05

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 44.07  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGAHVVISSRkqqNVDRAAAqlqregLSVAGIVCHVGKAEDRERLVAtALEhcgGIDFLVC 119
Cdd:COG0702     3 LVTGATGFIGRRVVRALLARGHPVRALVR---DPEKAAA------LAAAGVEVVQGDLDDPESLAA-ALA---GVDAVFL 69


                  ....*.
gi 1622955129 120 CAGVNP 125
Cdd:COG0702    70 LVPSGP 75
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
32-220 3.25e-05

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 44.33  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTG--STSGIGFAIARRLAQDGAHVVISsrkQQNvDRAAAQLQREGL-SVAGIVCHVGKAEDRERLVATAL 108
Cdd:PRK06079    3 GILSGKKIVVMGvaNKRSIAWGCAQAIKDQGATVIYT---YQN-DRMKKSLQKLVDeEDLLVECDVASDESIERAFATIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 109 EHCGGIDFLV---CCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLvssvaAYFPRmELGV- 184
Cdd:PRK06079   79 ERVGKIDGIVhaiAYAKKEELGGNVTDTSRDGYALAQDISAYSLIAVAKYARPLLNPGASIVTL-----TYFGS-ERAIp 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622955129 185 -YNV---SKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06079  153 nYNVmgiAKAALESSVRYLARDLGKKGIRVNAISAGAVKT 192
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 39-225 4.29e-05

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 44.09  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGID--F 116
Cdd:PLN02780   56 ALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSGDIDEGVKRIKETIEGLDvgV 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 LVCCAGVN-PLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKR-KGA-VTLVSSVAAYFPRMEL-GVYNVSKTAL 192
Cdd:PLN02780  136 LINNVGVSyPYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRkKGAiINIGSGAAIVIPSDPLyAVYAATKAYI 215

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622955129 193 LALTRTLALELAPKDIRVNCLVPGVIKTDFSKV 225
Cdd:PLN02780  216 DQFSRCLYVEYKKSGIDVQCQVPLYVATKMASI 248
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 37-221 5.27e-05

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: 43.61  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDR--ERLVATALEHCGGI 114
Cdd:cd09807     2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTLNHEVIVRHLDLASLKsiRAFAAEFLAEEDRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 115 DFLVCCAGVNPLVGStlgTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGA-VTLVSSVAAYF------------PRME 181
Cdd:cd09807    82 DVLINNAGVMRCPYS---KTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSrIVNVSSLAHKAgkinfddlnsekSYNT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622955129 182 LGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:cd09807   159 GFAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTE 198
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 40-123 7.89e-05

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


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 43.53  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGA-HVVISSRKQQN--VDRAAAQLQREGLSVAGIVCHVGKAEDRERLVAtALEHCGGIDF 116
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGArHLVLLSRRGPAprAAARAALLRAGGARVSVVRCDVTDPAALAALLA-ELAAGGPLAG 232


                  ....*..
gi 1622955129 117 LVCCAGV 123
Cdd:cd05274   233 VIHAAGV 239
PRK08251 PRK08251
SDR family oxidoreductase;
30-221 8.36e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 43.00  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  30 RKGILaervavVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE--GLSVAGIVCHVGKAEDRERLVATA 107
Cdd:PRK08251    2 RQKIL------ITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 108 LEHCGGIDFLVCCAGVNPlvGSTLGTSE-QIWDKILNVNVKSpalLLSQLLPYME----KRKGAVTLVSSVAAY--FPRm 180
Cdd:PRK08251   76 RDELGGLDRVIVNAGIGK--GARLGTGKfWANKATAETNFVA---ALAQCEAAMEifreQGSGHLVLISSVSAVrgLPG- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622955129 181 ELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08251  150 VKAAYAASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSE 190
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
34-238 1.17e-04

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 42.79  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTG--STSGIGFAIARRLAQDGAHVVISSRKQ---QNVDRAAAQLQREGLSVagIVCHVGKAEDRERLVATAL 108
Cdd:PRK08594    5 LEGKTYVVMGvaNKRSIAWGIARSLHNAGAKLVFTYAGErleKEVRELADTLEGQESLL--LPCDVTSDEEITACFETIK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 109 EHCGGIDFLVCC---AGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLV-----SSVAAYfprm 180
Cdd:PRK08594   83 EEVGVIHGVAHCiafANKEDLRGEFLETSRDGFLLAQNISAYSLTAVAREAKKLMTEGGSIVTLTylggeRVVQNY---- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622955129 181 elGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTDFSKvdwGAGGLcrNRVL 238
Cdd:PRK08594  159 --NVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRTLSAK---GVGGF--NSIL 209
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
32-225 1.50e-04

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 42.26  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTG--STSGIGFAIARRLAQDGAHVV---ISSRKQQNVDRAAAQLQREGLsvagIVCHVGKAEDRERLVAT 106
Cdd:PRK08690    2 GFLQGKKILITGmiSERSIAYGIAKACREQGAELAftyVVDKLEERVRKMAAELDSELV----FRCDVASDDEINQVFAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGVNP---LVGSTLGT-SEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYFPRMEL 182
Cdd:PRK08690   78 LGKHWDGLDGLVHSIGFAPkeaLSGDFLDSiSREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAVRAIPNY 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622955129 183 GVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT-------DFSKV 225
Cdd:PRK08690  158 NVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTlaasgiaDFGKL 207
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
32-220 2.28e-04

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 41.66  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTG--STSGIGFAIARRLAQDGAHVVISSRK---QQNVDRAAAQLqreGLSVAGiVCHVGKAEDRERLVAT 106
Cdd:PRK08159    6 GLMAGKRGLILGvaNNRSIAWGIAKACRAAGAELAFTYQGdalKKRVEPLAAEL---GAFVAG-HCDVTDEASIDAVFET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 107 ALEHCGGIDFLVCCAGV---NPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVA-AYFPRMEl 182
Cdd:PRK08159   82 LEKKWGKLDFVVHAIGFsdkDELTGRYVDTSRDNFTMTMDISVYSFTAVAQRAEKLMTDGGSILTLTYYGAeKVMPHYN- 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622955129 183 gVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK08159  161 -VMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKT 197
PRK09186 PRK09186
flagellin modification protein A; Provisional
 34-219 2.55e-04

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 41.51  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVAGIV--CHVGKAEDRERLVATALEHC 111
Cdd:PRK09186    2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKLSLveLDITDQESLEEFLSKSAEKY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAgvNPLvGSTLGTS--EQIWDKI---LNVNVKSPALLLSQLLPYMEKRK-GAVTLVSSV-AAYFPRMEL-- 182
Cdd:PRK09186   82 GKIDGAVNCA--YPR-NKDYGKKffDVSLDDFnenLSLHLGSSFLFSQQFAKYFKKQGgGNLVNISSIyGVVAPKFEIye 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622955129 183 GV-------YNVSKTALLALTRTLALELAPKDIRVNCLVPGVIK 219
Cdd:PRK09186  159 GTsmtspveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGIL 202
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
 41-112 3.33e-04

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs 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: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 41.57  E-value: 3.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKqqnvDRAAAQLQREGLSVagivcHVGKAEDRERLVATALE-----HCG 112
Cdd:cd05262     5 VTGATGFIGSAVVRELVAAGHEVVGLARS----DAGAAKLEAAGAQV-----HRGDLEDLDILRKAAAEadaviHLA 72
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 41-158 3.50e-04

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 41.32  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  41 VTGSTSGIGFAIARRLAQDGAHVVISSRKQQnvdRAAAqLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFLVCC 120
Cdd:cd08951    12 ITGSSDGLGLAAARTLLHQGHEVVLHARSQK---RAAD-AKAACPGAAGVLIGDLSSLAETRKLADQVNAIGRFDAVIHN 87

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622955129 121 AGVnpLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLP 158
Cdd:cd08951    88 AGI--LSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRR 123
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 38-221 3.83e-04

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


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 41.05  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQ----DGAHVVISSRKQQNVDRAAAQL--QREGLSVAGIVCHVGKAEDRERLVATALEHC 111
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKclksPGSVLVLSARNDEALRQLKAEIgaERSGLRVVRVSLDLGAEAGLEQLLKALRELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 112 GGIDFLVCCAGVNplvGSTLGTSEQIWDKILN---------VNVKSPALLLSQLLPYMEKRKGA-VTLV--SSVAAYFPR 179
Cdd:TIGR01500  82 RPKGLQRLLLINN---AGTLGDVSKGFVDLSDstqvqnywaLNLTSMLCLTSSVLKAFKDSPGLnRTVVniSSLCAIQPF 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622955129 180 MELGVYNVSKTALLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:TIGR01500 159 KGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTD 200
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 39-253 4.37e-04

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: 40.58  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQnvdrAAAQLQREGLSVAgivchVGKAEDRERLVATALEHCGGIDFLV 118
Cdd:cd11730     1 ALILGATGGIGRALARALAGRGWRLLLSGRDAG----ALAGLAAEVGALA-----RPADVAAELEVWALAQELGPLDLLV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 119 CCAGvNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLvssvAAYFPRME---LGVYNVSKTALLAL 195
Cdd:cd11730    72 YAAG-AILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFL----GAYPELVMlpgLSAYAAAKAALEAY 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622955129 196 TRTLALELapKDIRVNCLVPGVIKTDFskvdWGA-GGLCRNRVLP--VLSRCQLHHRGEHR 253
Cdd:cd11730   147 VEVARKEV--RGLRLTLVRPPAVDTGL----WAPpGRLPKGALSPedVAAAILEAHQGEPQ 201
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 34-83 5.66e-04

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 40.07  E-value: 5.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622955129  34 LAERVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQRE 83
Cdd:cd01078    26 LKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRAR 75
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
43-224 6.94e-04

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


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 40.08  E-value: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  43 GSTSGIGFAIARR-LAQDGAHVVISSRKQQ-NVDRAAAQLQREGL-SVAGIVCHVGKAEDRERLVATALEHcGGIDFLVC 119
Cdd:PRK07904   15 GGTSEIGLAICERyLKNAPARVVLAALPDDpRRDAAVAQMKAAGAsSVEVIDFDALDTDSHPKVIDAAFAG-GDVDVAIV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 120 CAGvnplvgsTLGTSEQIWD------KILNVNVKSP---ALLLSQllpYMEKR-KGAVTLVSSVAAYFPRMELGVYNVSK 189
Cdd:PRK07904   94 AFG-------LLGDAEELWQnqrkavQIAEINYTAAvsvGVLLGE---KMRAQgFGQIIAMSSVAGERVRRSNFVYGSTK 163

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622955129 190 TALLALTRTLALELAPKDIRVNCLVPGVIKTDFSK 224
Cdd:PRK07904  164 AGLDGFYLGLGEALREYGVRVLVVRPGQVRTRMSA 198
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 38-80 7.31e-04

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 40.45  E-value: 7.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQ-----DGAHVVISSRKQQNVDRAAAQL 80
Cdd:cd08941     3 VVLVTGANSGLGLAICERLLAeddenPELTLILACRNLQRAEAACRAL 50
PRK07023 PRK07023
SDR family oxidoreductase;
39-221 7.48e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 40.00  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  39 AVVTGSTSGIGFAIARRLAQDGAHVVISSRKqqnvdRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDF-- 116
Cdd:PRK07023    4 AIVTGHSRGLGAALAEQLLQPGIAVLGVARS-----RHPSLAAAAGERLAEVELDLSDAAAAAAWLAGDLLAAFVDGAsr 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 117 --LVCCAGVNPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEK---RKgaVTLVSSVAAYFPRMELGVYNVSKTA 191
Cdd:PRK07023   79 vlLINNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDaaeRR--ILHISSGAARNAYAGWSVYCATKAA 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALElAPKDIRVNCLVPGVIKTD 221
Cdd:PRK07023  157 LDHHARAVALD-ANRALRIVSLAPGVVDTG 185
PLN00015 PLN00015
protochlorophyllide reductase
 40-123 1.35e-03

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 39.69  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQDGA-HVVISSRKQQNVDRAAAQLQREGLSVAGIVCHVGKAEDRERLVATALEHCGGIDFLV 118
Cdd:PLN00015    1 IITGASSGLGLATAKALAETGKwHVVMACRDFLKAERAAKSAGMPKDSYTVMHLDLASLDSVRQFVDNFRRSGRPLDVLV 80


                  ....*
gi 1622955129 119 CCAGV 123
Cdd:PLN00015   81 CNAAV 85
KR_fFAS_SDR_c_like cd08950
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS), classical (c)-like ...
 35-83 1.73e-03

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


Pssm-ID: 187653 [Multi-domain]  Cd Length: 259  Bit Score: 39.10  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622955129  35 AERVAVVTGSTSG-IGFAIARRLAQDGAHVVI-SSRKQQNVDRAAAQLQRE 83
Cdd:cd08950     6 AGKVALVTGAGPGsIGAEVVAGLLAGGATVIVtTSRFSHERTAFFQKLYRK 56
PRK06101 PRK06101
SDR family oxidoreductase;
38-220 1.82e-03

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 39.08  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  38 VAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQreglSVAGIVCHVGKAEDRERLVA-------TALEH 110
Cdd:PRK06101    3 AVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHTQSA----NIFTLAFDVTDHPGTKAALSqlpfipeLWIFN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 111 CGGIDFLVccagvNPLVGSTLgtseqiWDKILNVNVKSPALLLSQLLPYMEkRKGAVTLVSSVAAYF--PRMElgVYNVS 188
Cdd:PRK06101   79 AGDCEYMD-----DGKVDATL------MARVFNVNVLGVANCIEGIQPHLS-CGHRVVIVGSIASELalPRAE--AYGAS 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622955129 189 KTALLALTRTLALELAPKDIRVNCLVPGVIKT 220
Cdd:PRK06101  145 KAAVAYFARTLQLDLRPKGIEVVTVFPGFVAT 176
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 37-122 3.30e-03

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs 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: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 37.99  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVtGSTSGIGFAIARRLAQDGAHVVISSRKQqnvdRAAAQLQREGLSVAgivchVGKAEDRERLVATalehCGGIDF 116
Cdd:cd05243     1 KVLVV-GATGKVGRHVVRELLDRGYQVRALVRDP----SQAEKLEAAGAEVV-----VGDLTDAESLAAA----LEGIDA 66


                  ....*.
gi 1622955129 117 LVCCAG 122
Cdd:cd05243    67 VISAAG 72
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
48-80 4.91e-03

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 37.46  E-value: 4.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622955129  48 IGFAIARRLAQDGAHVVISSRKQQNVDRAAAQL 80
Cdd:COG2085     9 IGSALARRLAAAGHEVVIGSRDPEKAAALAAEL 41
PRK08177 PRK08177
SDR family oxidoreductase;
37-221 5.61e-03

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 37.32  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  37 RVAVVTGSTSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAAQLQREGLSVagivchvgKAEDRERLVATALEHCGG-ID 115
Cdd:PRK08177    2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEKL--------DMNDPASLDQLLQRLQGQrFD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 116 FLVCCAGV-NPLVGSTLGTSEQIWDKILNVNVKSPALLLSQLLPYMEKRKGAVTLVSSVAAYF---PRMELGVYNVSKTA 191
Cdd:PRK08177   74 LLFVNAGIsGPAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVelpDGGEMPLYKASKAA 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622955129 192 LLALTRTLALELAPKDIRVNCLVPGVIKTD 221
Cdd:PRK08177  154 LNSMTRSFVAELGEPTLTVLSMHPGWVKTD 183
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
32-225 7.09e-03

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 37.11  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  32 GILAERVAVVTG--STSGIGFAIARRLAQDGAHVVISSRKQQNVDRAAaQLQREGLSVAGIVCHVGKAEDRERLVATALE 109
Cdd:PRK06997    2 GFLAGKRILITGllSNRSIAYGIAKACKREGAELAFTYVGDRFKDRIT-EFAAEFGSDLVFPCDVASDEQIDALFASLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129 110 HCGGIDFLVCCAGVNP---LVGSTL-GTSEQIWDKILNVNVKSPALLLSQLLPYMeKRKGAVTLVSSVAAYFPRMELGVY 185
Cdd:PRK06997   81 HWDGLDGLVHSIGFAPreaIAGDFLdGLSRENFRIAHDISAYSFPALAKAALPML-SDDASLLTLSYLGAERVVPNYNTM 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622955129 186 NVSKTALLALTRTLALELAPKDIRVNCLVPGVIKT-------DFSKV 225
Cdd:PRK06997  160 GLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaasgikDFGKI 206
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
 40-118 7.31e-03

NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs; NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. 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. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs 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: 187561 [Multi-domain]  Cd Length: 242  Bit Score: 37.25  E-value: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622955129  40 VVTGSTSGIGFAIARRLAQD-GAHVVISSRkqqNVDRAAAQ-LQREGLSVagivcHVGKAEDRERLvATALEHCGGIdFL 117
Cdd:cd05251     2 LVFGATGKQGGSVVRALLKDpGFKVRALTR---DPSSPAAKaLAAPGVEV-----VQGDLDDPESL-EAALKGVYGV-FL 71


                  .
gi 1622955129 118 V 118
Cdd:cd05251    72 V 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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