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Conserved domains on  [gi|1835908839|ref|WP_168978223|]
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MULTISPECIES: YciK family oxidoreductase [unclassified Citrobacter]

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
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 1-247 0e+00

putative oxoacyl-(acyl carrier protein) reductase; Provisional


:

Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 499.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   1 MHYQPKQDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTCTSEECH 80
Cdd:PRK08945    1 MHYQPKPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLLTATPQNYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  81 QLAQRIAAHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRA 160
Cdd:PRK08945   81 QLADTIEEQFGRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 161 NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMT 240
Cdd:PRK08945  161 NWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRASAFPGEDPQKLKTPEDIMPLYLYLMGDDSRRKNGQS 240


                  ....*..
gi 1835908839 241 FDAQPGR 247
Cdd:PRK08945  241 FDAQPGR 247
 
Name Accession Description Interval E-value
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 1-247 0e+00

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 499.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   1 MHYQPKQDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTCTSEECH 80
Cdd:PRK08945    1 MHYQPKPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLLTATPQNYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  81 QLAQRIAAHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRA 160
Cdd:PRK08945   81 QLADTIEEQFGRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 161 NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMT 240
Cdd:PRK08945  161 NWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRASAFPGEDPQKLKTPEDIMPLYLYLMGDDSRRKNGQS 240


                  ....*..
gi 1835908839 241 FDAQPGR 247
Cdd:PRK08945  241 FDAQPGR 247
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 9-244 8.82e-152

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: 422.37  E-value: 8.82e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTCTSEECHQLAQRIAA 88
Cdd:cd05340     1 LLNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLLTCTSENCQQLAQRIAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05340    81 NYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMTFDAQ 244
Cdd:cd05340   161 KFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMTFDAQ 236
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 8-242 1.27e-68

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: 211.95  E-value: 1.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   8 DLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltcTSEE-CHQLAQRI 86
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA-GGRALAVAADV---TDEAaVEALVAAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGLLGDIcPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:COG1028    78 VAAFGRLDILVNNAGITPPG-PLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED----------PQKLKTPADIMPLYLWLMGDDSRRK 236
Cdd:COG1028   157 ASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEvrealaaripLGRLGTPEEVAAAVLFLASDAASYI 236


                  ....*.
gi 1835908839 237 TGMTFD 242
Cdd:COG1028   237 TGQVLA 242
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 13-211 1.62e-61

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 191.67  E-value: 1.62e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIaDENGTQPQWFTLDLltcTS-EECHQLAQRIAAHFP 91
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKEL-GALGGKALFIQGDV---TDrAQVKALVEQAVERLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:pfam00106  77 RLDILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED 211
Cdd:pfam00106 156 VIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 16-196 2.12e-12

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: 63.66  E-value: 2.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   16 LVTGASDGIGREATQTYARYGA-TVILLGRNEEKLRQVARTIAD--ENGTQPQWFTLDLltCTSEECHQLAQRIAAHFPR 92
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAEleAAGARVTVVACDV--ADRDALAAVLAAIPAVEGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   93 LDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLllksDAGSLVFTSSSVGRQGRANWGAYAtskfAT 172
Cdd:smart00822  82 LTGVIHAAGVLDD-GVLASLTPERFAAVLAPKAAGAWNLHELTADL----PLDFFVLFSSIAGVLGSPGQANYA----AA 152

                          170       180
                   ....*....|....*....|....
gi 1835908839  173 EGMMQVLADEYQNRHLRVNCINPG 196
Cdd:smart00822 153 NAFLDALAEYRRARGLPALSIAWG 176
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 14-206 2.16e-12

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: 64.93  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARY----GATVILLGRNEEKLRQVARTI-ADENGTQPQWFTLDLltcTSEECHQLAQRIAA 88
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIgAERSGLRVVRVSLDL---GAEAGLEQLLKALR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDG-----VLHNAGLLGDICPMSEQnplvWQDVMQVN----VNATFML-TQALLPLLLKSDAGS---LVFTSSSVG 155
Cdd:TIGR01500  79 ELPRPKGlqrllLINNAGTLGDVSKGFVD----LSDSTQVQnywaLNLTSMLcLTSSVLKAFKDSPGLnrtVVNISSLCA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1835908839 156 RQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASA 206
Cdd:TIGR01500 155 IQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQV 205
 
Name Accession Description Interval E-value
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 1-247 0e+00

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 499.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   1 MHYQPKQDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTCTSEECH 80
Cdd:PRK08945    1 MHYQPKPDLLKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEAVYDEIEAAGGPQPAIIPLDLLTATPQNYQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  81 QLAQRIAAHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRA 160
Cdd:PRK08945   81 QLADTIEEQFGRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 161 NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMT 240
Cdd:PRK08945  161 NWGAYAVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAMRASAFPGEDPQKLKTPEDIMPLYLYLMGDDSRRKNGQS 240


                  ....*..
gi 1835908839 241 FDAQPGR 247
Cdd:PRK08945  241 FDAQPGR 247
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 9-244 8.82e-152

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: 422.37  E-value: 8.82e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTCTSEECHQLAQRIAA 88
Cdd:cd05340     1 LLNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLLTCTSENCQQLAQRIAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05340    81 NYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMTFDAQ 244
Cdd:cd05340   161 KFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMTFDAQ 236
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 8-242 1.27e-68

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: 211.95  E-value: 1.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   8 DLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltcTSEE-CHQLAQRI 86
Cdd:COG1028     2 TRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELRAA-GGRALAVAADV---TDEAaVEALVAAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGLLGDIcPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:COG1028    78 VAAFGRLDILVNNAGITPPG-PLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLRGSPGQAAYA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED----------PQKLKTPADIMPLYLWLMGDDSRRK 236
Cdd:COG1028   157 ASKAAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEvrealaaripLGRLGTPEEVAAAVLFLASDAASYI 236


                  ....*.
gi 1835908839 237 TGMTFD 242
Cdd:COG1028   237 TGQVLA 242
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 13-211 1.62e-61

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 191.67  E-value: 1.62e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIaDENGTQPQWFTLDLltcTS-EECHQLAQRIAAHFP 91
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAKEL-GALGGKALFIQGDV---TDrAQVKALVEQAVERLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:pfam00106  77 RLDILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPYPGGSAYSASKAA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED 211
Cdd:pfam00106 156 VIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 15-238 2.64e-58

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: 185.18  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVArtIADENGTQPQWFTLDLltCTSEECHQLAQRIAAHFPRLD 94
Cdd:cd05233     1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA--AIEALGGNAVAVQADV--SDEEDVEALVEEALEEFGRLD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFATEG 174
Cdd:cd05233    77 ILVNNAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835908839 175 MMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED---------PQKLKTPADIMPLYLWLMGDDSRRKTG 238
Cdd:cd05233   156 LTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAekelaaaipLGRLGTPEEVAEAVVFLASDEASYITG 228
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
10-221 4.01e-55

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 177.37  E-value: 4.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:COG0300     3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELR-AAGARVEVVALDV--TDPDAVAALAEAVLAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:COG0300    80 FGPIDVLVNNAGV-GGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASK 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLkTPADI 221
Cdd:COG0300   159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL-SPEEV 209
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 11-224 1.27e-51

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: 168.05  E-value: 1.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIadenGTQPQWFTLDLltcTSEE-CHQLAQRIAAH 89
Cdd:COG4221     4 KGKVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAEL----GGRALAVPLDV---TDEAaVEAAVAAAVAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:COG4221    77 FGRLDVLVNNAGV-ALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPL 224
Cdd:COG4221   156 AAVRGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVFDGDAEAAAAVYEGLEPL 210
PRK08703 PRK08703
SDR family oxidoreductase;
7-238 1.83e-50

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 165.10  E-value: 1.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   7 QDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTCTSEECHQLAQRI 86
Cdd:PRK08703    1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVYDAIVEAGHPEPFAIRFDLMSAEEKEFEQFAATI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFP-RLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY 165
Cdd:PRK08703   81 AEATQgKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHGETPKAYWGGF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 166 ATSKFATEGMMQVLADEYQN-RHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTG 238
Cdd:PRK08703  161 GASKAALNYLCKVAADEWERfGNLRANVLVPGPINSPQRIKSHPGEAKSERKSYGDVLPAFVWWASAESKGRSG 234
PRK12826 PRK12826
SDR family oxidoreductase;
10-242 7.13e-49

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 161.24  E-value: 7.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK12826    4 LEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVEAA-GGKARARQVDV--RDRAALKAAVAAGVED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQ-GRANWGAYATS 168
Cdd:PRK12826   81 FGRLDILVANAGIFPL-TPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRvGYPGLAHYAAS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLK---------TPADIMPLYLWLMGDDSRRKTGM 239
Cdd:PRK12826  160 KAGLVGFTRALALELAARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAaaiplgrlgEPEDIAAAVLFLASDEARYITGQ 239


                  ...
gi 1835908839 240 TFD 242
Cdd:PRK12826  240 TLP 242
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
9-238 1.04e-48

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 160.71  E-value: 1.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIaDENGTQPQWFTLDLltCTSEECHQLAQRIAA 88
Cdd:PRK05653    2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAEL-RAAGGEARVLVFDV--SDEAAVRALIEAAVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK05653   79 AFGALDILVNNAGITRDalLPRMSEED---WDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGNPGQTNYS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM--------RASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTG 238
Cdd:PRK05653  156 AAKAGVIGFTKALALELASRGITVNAVAPGFIDTDMteglpeevKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITG 235
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 9-238 2.31e-44

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 149.69  E-value: 2.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtQPQWFTLDLltcTSEECHQ-LAQRIA 87
Cdd:PRK07478    3 RLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELDQLVAEIRAEGG-EAVALAGDV---RDEAYAKaLVALAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQ-GRANWGAYA 166
Cdd:PRK07478   79 ERFGGLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTaGFPGMAAYA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQ----------KLKTPADIMPLYLWLMGDDSRRK 236
Cdd:PRK07478  159 ASKAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEALafvaglhalkRMAQPEEIAQAALFLASDAASFV 238


                  ..
gi 1835908839 237 TG 238
Cdd:PRK07478  239 TG 240
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 9-240 1.47e-40

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 140.11  E-value: 1.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQRIAA 88
Cdd:PRK12939    4 NLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALEAA-GGRAHAIAADL--ADPASVQRFFDAAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK12939   81 ALGGLDGLVNNAGIT-NSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGAPKLGAYVAS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAfPTEDP----------QKLKTPADIMPLYLWLMGDDSRRKTG 238
Cdd:PRK12939  160 KGAVIGMTRSLARELGGRGITVNAIAPGLTATEATAYV-PADERhayylkgralERLQVPDDVAGAVLFLLSDAARFVTG 238


                  ..
gi 1835908839 239 MT 240
Cdd:PRK12939  239 QL 240
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 19-238 7.96e-40

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: 137.56  E-value: 7.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  19 GASD--GIGREATQTYARYGATVILLGRNEEKLRQVARtIADENGTqpqwftlDLLTC--TSEE-CHQLAQRIAAHFPRL 93
Cdd:pfam13561   1 GAANesGIGWAIARALAEEGAEVVLTDLNEALAKRVEE-LAEELGA-------AVLPCdvTDEEqVEALVAAAVEKFGRL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGLLGDI-CPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSdaGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:pfam13561  73 DILVNNAGFAPKLkGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEG--GSIVNLSSIGAERVVPNYNAYGAAKAAL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835908839 173 EGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPTEDPQK--------LK---TPADIMPLYLWLMGDDSRRKTG 238
Cdd:pfam13561 151 EALTRYLAVELGPRGIRVNAISPGPIKTLA-ASGIPGFDELLaaaearapLGrlgTPEEVANAAAFLASDLASYITG 226
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 13-241 6.25e-39

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: 135.37  E-value: 6.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVArTIADENGTQPQWFTLDLLTctSEECHQLAQRIAAHFPR 92
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETV-EEIKALGGNAAALEADVSD--REAVEALVEKVEAEFGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKF 170
Cdd:cd05333    78 VDILVNNAGITRDnlLMRMSEED---WDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLIGNPGQANYAASKA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 171 ATEGMMQVLADEYQNRHLRVNCINPGGTRTGMraSAFPTEDPQK----------LKTPADIMPLYLWLMGDDSRRKTGMT 240
Cdd:cd05333   155 GVIGFTKSLAKELASRGITVNAVAPGFIDTDM--TDALPEKVKEkilkqiplgrLGTPEEVANAVAFLASDDASYITGQV 232


                  .
gi 1835908839 241 F 241
Cdd:cd05333   233 L 233
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 10-241 4.79e-38

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 133.40  E-value: 4.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKL-RQVARTIADeNGTQPQWFTLDLltCTSEECHQLAQRIAA 88
Cdd:PRK05557    3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGaEALVAEIGA-LGGKALAVQGDV--SDAESVERAVDEAKA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLL--GDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK05557   80 EFGGVDILVNNAGITrdNLLMRMKEED---WDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLMGNPGQANYA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPTEDPQKLKT---------PADIMPLYLWLMGDDSRRKT 237
Cdd:PRK05557  157 ASKAGVIGFTKSLARELASRGITVNAVAPGFIETDM-TDALPEDVKEAILAqiplgrlgqPEEIASAVAFLASDEAAYIT 235


                  ....
gi 1835908839 238 GMTF 241
Cdd:PRK05557  236 GQTL 239
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-238 4.58e-37

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 130.76  E-value: 4.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGR-NEEKLRQVARTIADEnGTQPQWFTLDLLTCtsEECHQLAQRIAA 88
Cdd:PRK12825    4 LMGRVALVTGAARGLGRAIALRLARAGADVVVHYRsDEEAAEELVEAVEAL-GRRAQAVQADVTDK--AALEAAVAAAVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK12825   81 RFGRIDILVNNAGIFED-KPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAGLPGWPGRSNYAAA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLK--------TPADIMPLYLWLMGDDSRRKTG 238
Cdd:PRK12825  160 KAGLVGLTKALARELAEYGITVNMVAPGDIDTDMKEATIEEAREAKDAetplgrsgTPEDIARAVAFLCSDASDYITG 237
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 13-202 1.85e-34

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: 123.88  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRqvarTIADENGTQPQWFTLDLltcTSEE-CHQLAQRIAAHFP 91
Cdd:cd05374     1 KVVLITGCSSGIGLALALALAAQGYRVIATARNPDKLE----SLGELLNDNLEVLELDV---TDEEsIKAAVKEVIERFG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:cd05374    74 RIDVLVNNAGY-GLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAA 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:cd05374   153 LEALSESLRLELAPFGIKVTIIEPGPVRTGF 183
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 10-246 9.29e-34

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: 122.00  E-value: 9.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVIL-LGRNEEKLRQVARTIADeNGTQPQWFTLDLltCTSEECHQLAQRIAA 88
Cdd:cd05362     1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVnYASSKAAAEEVVAEIEA-AGGKAIAVQADV--SDPSQVARLFDAAEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLksDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05362    78 AFGGVDILVNNAGVM-LKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLR--DGGRIINISSSLTAAYTPNYGAYAGS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKT---------PADIMPLYLWLMGDDSRRKTGM 239
Cdd:cd05362   155 KAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYAGKTEEAVEGYAKmsplgrlgePEDIAPVVAFLASPDGRWVNGQ 234


                  ....*..
gi 1835908839 240 TFDAQPG 246
Cdd:cd05362   235 VIRANGG 241
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 10-230 1.17e-33

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: 122.08  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltcTSEECHQ-LAQRIAA 88
Cdd:cd05347     3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIEKE-GVEATAFTCDV---SDEEAIKaAVEAIEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAG--LLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:cd05347    79 DFGKIDILVNNAGiiRRHPAEEFPEAE---WRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGGPPVPAYA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFptEDPQKLKTPADIMPLYLW-----LMG 230
Cdd:cd05347   156 ASKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTEAVV--ADPEFNDDILKRIPAGRWgqpedLVG 222
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 10-240 8.71e-33

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: 119.74  E-value: 8.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:cd05352     6 LKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDV--SSQESVEKTFKQIQKD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGllgdIC---PMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRqgRAN----W 162
Cdd:cd05352    84 FGKIDILIANAG----ITvhkPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGT--IVNrpqpQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFP-TEDPQKLKTPA-------DIMPLYLWLMGDDSR 234
Cdd:cd05352   158 AAYNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKeLRKKWESYIPLkrialpeELVGAYLYLASDASS 237


                  ....*.
gi 1835908839 235 RKTGMT 240
Cdd:cd05352   238 YTTGSD 243
FabG-like PRK07231
SDR family oxidoreductase;
9-240 4.52e-32

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 118.01  E-value: 4.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADenGTQPQWFTLDlltcTSEECHQ--LAQRI 86
Cdd:PRK07231    2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEILA--GGRAIAVAAD----VSDEADVeaAVAAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK07231   76 LERFGSVDILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAGLRPRPGLGWYN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPTEDP-------------QKLKTPADIMPLYLWLMGDDS 233
Cdd:PRK07231  156 ASKGAVITLTKALAAELGPDKIRVNAVAPVVVETGL-LEAFMGEPTpenrakflatiplGRLGTPEDIANAALFLASDEA 234


                  ....*..
gi 1835908839 234 RRKTGMT 240
Cdd:PRK07231  235 SWITGVT 241
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 10-240 4.98e-32

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 117.59  E-value: 4.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKlrqVARTIADENGTQPQWFTLDLLTctSEECHQLAQRIAAH 89
Cdd:PRK12828    5 LQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAP---LSQTLPGVPADALRIGGIDLVD--PQAARRAVDEVNRQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLL--GDIcpmSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK12828   80 FGRLDALVNIAGAFvwGTI---ADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAGPGMGAYAA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTGMT 240
Cdd:PRK12828  157 AKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRADMPDADFSRWVTPEQIAAVIAFLLSDEAQAITGAS 229
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 12-200 6.46e-32

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: 116.97  E-value: 6.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVA---RTIADENGTQPQWFTLDLlTCTsEECHQLAQRIAA 88
Cdd:cd08939     1 GKHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVeeiEAEANASGQKVSYISADL-SDY-EEVEQAFAQAVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGllGDIC-PMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd08939    79 KGGPPDLVVNCAG--ISIPgLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALVGIYGYSAYCP 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:cd08939   157 SKFALRGLAESLRQELKPYNIRVSVVYPPDTDT 189
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 10-241 1.48e-31

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 116.70  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLrqvARTIADENGTQPQWFTLDLLTCtsEECHQLAQRIAAH 89
Cdd:PRK12829    9 LDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAAL---AATAARLPGAKVTATVADVADP--AQVERVFDTAVER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSV-GRQGRANWGAYATS 168
Cdd:PRK12829   84 FGGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVaGRLGYPGRTPYAAS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTG-------------------MRASAFPTEDPQKLKTPADIMPLYLWLM 229
Cdd:PRK12829  164 KWAVVGLVKSLAIELGPLGIRVNAILPGIVRGPrmrrviearaqqlgigldeMEQEYLEKISLGRMVEPEDIAATALFLA 243

                         250
                  ....*....|..
gi 1835908839 230 GDDSRRKTGMTF 241
Cdd:PRK12829  244 SPAARYITGQAI 255
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 9-246 2.05e-31

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 116.21  E-value: 2.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIaDENGTQPQWFTLDLltcTSEE-CHQLAQRIA 87
Cdd:PRK07890    2 LLKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAAEI-DDLGRRALAVPTDI---TDEDqCANLVALAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK07890   78 ERFGRVDALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLRHSQPKYGAYKM 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINP-------------------GGTRTGMRASAFPTEDPQKLKTPADIMPLYLWL 228
Cdd:PRK07890  157 AKGALLAASQSLATELGPQGIRVNSVAPgyiwgdplkgyfrhqagkyGVTVEQIYAETAANSDLKRLPTDDEVASAVLFL 236

                         250
                  ....*....|....*...
gi 1835908839 229 MGDDSRRKTGMTFDAQPG 246
Cdd:PRK07890  237 ASDLARAITGQTLDVNCG 254
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 13-222 6.19e-31

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: 114.26  E-value: 6.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGRE-ATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQRIAAHFP 91
Cdd:cd05324     1 KVALVTGANRGIGFEiVRQLAKSGPGTVILTARDVERGQAAVEKLRAE-GLSVRFHQLDV--TDDASIEAAADFVEEKYG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQgranWGAYATSKFA 171
Cdd:cd05324    78 GLDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSL----TSAYGVSKAA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIM 222
Cdd:cd05324   154 LNALTRILAKELKETGIKVNACCPGWVKTDMGGGKAPKTPEEGAETPVYLA 204
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 10-207 6.64e-31

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: 114.99  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltcTSEECH-QLAQRIAA 88
Cdd:cd05332     1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELGAPSPHVVPLDM---SDLEDAeQVVEEALK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGllgdicpMSEQNPL------VWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQG---R 159
Cdd:cd05332    78 LFGGLDILINNAG-------ISMRSLFhdtsidVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKIGvpfR 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1835908839 160 AnwgAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAF 207
Cdd:cd05332   151 T---AYAASKHALQGFFDSLRAELSEPNISVTVVCPGLIDTNIAMNAL 195
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 10-240 1.02e-29

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: 111.71  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGR-NEEKLRQVARTIADeNGTQPQWFTLDLltCTSEECHQLAQRIAA 88
Cdd:cd05358     1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRsKEDAAEEVVEEIKA-VGGKAIAVQADV--SKEEDVVALFQSAIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDA-GSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd05358    78 EFGTLDILVNNAGLQGD-ASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIkGKIINMSSVHEKIPWPGHVNYAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFptEDPQKLK------------TPADIMPLYLWLMGDDSRR 235
Cdd:cd05358   157 SKGGVKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAW--DDPEQRAdllslipmgrigEPEEIAAAAAWLASDEASY 234


                  ....*
gi 1835908839 236 KTGMT 240
Cdd:cd05358   235 VTGTT 239
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 12-202 4.75e-29

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: 110.39  E-value: 4.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADE-NGTQPQWFTLDLLTCTSeeCHQLAQRIAAHF 90
Cdd:cd05327     1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIKKEtGNAKVEVIQLDLSSLAS--VRQFAEEFLARF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGLLgdICP--MSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRAN------- 161
Cdd:cd05327    79 PRLDILINNAGIM--APPrrLTKDG---FELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDfndldle 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1835908839 162 -------WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:cd05327   154 nnkeyspYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTEL 201
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-238 5.25e-29

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 109.55  E-value: 5.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLG-RNEEKLRQVARTIADENGTqpqwfTLDLLTCTS--EECHQLAQRI 86
Cdd:PRK05565    3 LMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYdINEEAAQELLEEIKEEGGD-----AIAVKADVSseEDVENLVEQI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK05565   78 VEKFGKIDILVNNAGI-SNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCEVLYS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPTEDPQKLK---------TPADIMPLYLWLMGDDSRRKT 237
Cdd:PRK05565  157 ASKGAVNAFTKALAKELAPSGIRVNAVAPGAIDTEM-WSSFSEEDKEGLAeeiplgrlgKPEEIAKVVLFLASDDASYIT 235


                  .
gi 1835908839 238 G 238
Cdd:PRK05565  236 G 236
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 10-242 6.81e-29

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: 109.60  E-value: 6.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLtcTSEECHQLAQRIAAH 89
Cdd:cd05369     1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEISSATGGRAHPIQCDVR--DPEAVEAAVDETLKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGllGD-ICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDA-GSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd05369    79 FGKIDILINNAA--GNfLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHgGSILNISATYAYTGSPFQVHSAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPG--GTRTGMRaSAFPTEDP----------QKLKTPADIMPLYLWLMGDDSRR 235
Cdd:cd05369   157 AKAGVDALTRSLAVEWGPYGIRVNAIAPGpiPTTEGME-RLAPSGKSekkmiervplGRLGTPEEIANLALFLLSDAASY 235


                  ....*....
gi 1835908839 236 KTG--MTFD 242
Cdd:cd05369   236 INGttLVVD 244
PRK09072 PRK09072
SDR family oxidoreductase;
10-220 8.23e-29

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 109.65  E-value: 8.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdeNGTQPQWFTLDLltCTSEECHQLAQRiAAH 89
Cdd:PRK09072    3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLP--YPGRHRWVVADL--TSEAGREAVLAR-ARE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK09072   78 MGGINVLINNAGV-NHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASK 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFpTEDPQKLKTPAD 220
Cdd:PRK09072  157 FALRGFSEALRRELADTGVRVLYLAPRATRTAMNSEAV-QALNRALGNAMD 206
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 10-241 1.16e-28

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 109.04  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdeNGTQPQWFTLDLLTCTSEE---CHQLAQRI 86
Cdd:PRK12827    4 LDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRGRAEADAVA--AGIEAAGGKALGLAFDVRDfaaTRAALDAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGLLGDIcPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSD-AGSLVFTSSSVGRQGRANWGAY 165
Cdd:PRK12827   82 VEEFGRLDILVNNAGIATDA-AFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrGGRIVNIASVAGVRGNRGQVNY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQK------LKTPADIMPLYLWLMGDDSRRKTGM 239
Cdd:PRK12827  161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMADNAAPTEHLLNpvpvqrLGEPDEVAALVAFLVSDAASYVTGQ 240


                  ..
gi 1835908839 240 TF 241
Cdd:PRK12827  241 VI 242
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 15-216 1.79e-28

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: 108.14  E-value: 1.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYAR--YGATVILLGRNEEKLRQVARtiADENGTQPQWFTLDLltCTSEECHQLAQRIAAHFPR 92
Cdd:cd05367     2 IILTGASRGIGRALAEELLKrgSPSVVVLLARSEEPLQELKE--ELRPGLRVTTVKADL--SDAAGVEQLLEAIRKLDGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDA-GSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:cd05367    78 RDLLINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSSGAAVNPFKGWGLYCSSKAA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1835908839 172 TEGMMQVLADEYQNrhLRVNCINPGGTRTGM----RASAFPTEDPQKLK 216
Cdd:cd05367   158 RDMFFRVLAAEEPD--VRVLSYAPGVVDTDMqreiRETSADPETRSRFR 204
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 10-238 2.01e-28

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: 108.24  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIadenGTQPQWFTLDLltcTSEECHQLAQRIA-A 88
Cdd:cd05341     3 LKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAEL----GDAARFFHLDV---TDEDGWTAVVDTArE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05341    76 AFGRLDVLVNNAGIL-TGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLVGDPALAAYNAS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEY--QNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKT---------PADIMPLYLWLMGDDSRRKT 237
Cdd:cd05341   155 KGAVRGLTKSAALECatQGYGIRVNSVHPGYIYTPMTDELLIAQGEMGNYPntpmgragePDEIAYAVVYLASDESSFVT 234


                  .
gi 1835908839 238 G 238
Cdd:cd05341   235 G 235
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 9-247 3.56e-28

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 107.79  E-value: 3.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVIL--LG---RNEEKLRQVARTIADE---NGTQPQWFTLDLltctsEECH 80
Cdd:cd05353     2 RFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndLGgdrKGSGKSSSAADKVVDEikaAGGKAVANYDSV-----EDGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  81 QLAQRIAAHFPRLDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQG 158
Cdd:cd05353    77 KIVKTAIDAFGRVDILVNNAGILRDrsFAKMSEED---WDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAGLYG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 159 RANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGtRTGMRASAFPTEDPQKLKtPADIMPLYLWLMGDDSrRKTG 238
Cdd:cd05353   154 NFGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPAA-GSRMTETVMPEDLFDALK-PEYVAPLVLYLCHESC-EVTG 230


                  ....*....
gi 1835908839 239 MTFDAQPGR 247
Cdd:cd05353   231 GLFEVGAGW 239
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 10-247 4.14e-28

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: 107.50  E-value: 4.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTI--ADENGTQPQWFTLDLltcTSEEC-HQLAQRI 86
Cdd:cd05364     1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSClqAGVSEKKILLVVADL---TEEEGqDRIISTT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGLLGdICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYA 166
Cdd:cd05364    78 LAKFGRLDILVNNAGILA-KGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK-GEIVNVSSVAGGRSFPGVLYYC 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTG-MRASAFPTEDPQKL-------------KTPADIMPLYLWLMGDD 232
Cdd:cd05364   156 ISKAALDQFTRCTALELAPKGVRVNSVSPGVIVTGfHRRMGMPEEQYIKFlsrakethplgrpGTVDEVAEAIAFLASDA 235

                         250
                  ....*....|....*
gi 1835908839 233 SRRKTGMTFDAQPGR 247
Cdd:cd05364   236 SSFITGQLLPVDGGR 250
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 10-238 1.12e-27

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 106.81  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTI-ADENGTQPQWFTLDLltCTSEECHQLAQRIAA 88
Cdd:PRK05875    5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIeALKGAGAVRYEPADV--TDEDQVARAVDAATA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK05875   83 WHGRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAASNTHRWFGAYGVT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAfpTEDPQKLK-----TP-------ADIMPLYLWLMGDDSRRK 236
Cdd:PRK05875  163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVAPI--TESPELSAdyracTPlprvgevEDVANLAMFLLSDAASWI 240


                  ..
gi 1835908839 237 TG 238
Cdd:PRK05875  241 TG 242
PRK08219 PRK08219
SDR family oxidoreductase;
13-202 1.51e-27

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 105.40  E-value: 1.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARyGATVILLGRNEEKLRQVARTIADEngtqpQWFTLDLltcTSEECHQLAqriAAHFPR 92
Cdd:PRK08219    4 PTALITGASRGIGAAIARELAP-THTLLLGGRPAERLDELAAELPGA-----TPFPVDL---TDPEAIAAA---VEQLGR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLlKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:PRK08219   72 LDVLVHNAGVA-DLGPVAESTVDEWRATLEVNVVAPAELTRLLLPAL-RAAHGHVVFINSGAGLRANPGWGSYAASKFAL 149

                         170       180       190
                  ....*....|....*....|....*....|
gi 1835908839 173 EGMMQVLADEyQNRHLRVNCINPGGTRTGM 202
Cdd:PRK08219  150 RALADALREE-EPGNVRVTSVHPGRTDTDM 178
PRK06172 PRK06172
SDR family oxidoreductase;
10-238 2.68e-27

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 105.60  E-value: 2.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIaDENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK06172    5 FSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALI-REAGGEALFVACDV--TRDAEVKALVEQTIAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK06172   82 YGRLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAGLGAAPKMSIYAASK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTeDPQKLK------------TPADIMPLYLWLMGDDSRRKT 237
Cdd:PRK06172  162 HAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRAYEA-DPRKAEfaaamhpvgrigKVEEVASAVLYLCSDGASFTT 240


                  .
gi 1835908839 238 G 238
Cdd:PRK06172  241 G 241
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-221 1.59e-26

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 102.84  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK07666    5 LQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLKAVAEEVE-AYGVKVVIATADV--SDYEEVTAAIEQLKNE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK07666   82 LGSIDILINNAGI-SKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQKGAAVTSAYSASK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTE-DPQKLKTPADI 221
Cdd:PRK07666  161 FGVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTDgNPDKVMQPEDL 213
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 11-238 3.25e-26

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: 102.16  E-value: 3.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTiadengtqPQWFTLDLLTCTSEECHQLAQRIAahf 90
Cdd:cd05368     1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERG--------PGITTRVLDVTDKEQVAALAKEEG--- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 pRLDGVLHNAGL--LGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGR-QGRANWGAYAT 167
Cdd:cd05368    70 -RIDVLFNCAGFvhHGSILDCEDDD---WDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSiKGVPNRFVYST 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM---RASAFPteDPQ-------------KLKTPADIMPLYLWLMGD 231
Cdd:cd05368   146 TKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTPSleeRIQAQP--DPEealkafaarqplgRLATPEEVAALAVYLASD 223


                  ....*..
gi 1835908839 232 DSRRKTG 238
Cdd:cd05368   224 ESAYVTG 230
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 16-240 5.71e-26

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: 101.66  E-value: 5.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVIL-LGRNEEKLRQVARTIAdENGTQPQWFTLDLLTCtsEECHQLAQRIAAHFPRLD 94
Cdd:cd05359     2 LVTGGSRGIGKAIALRLAERGADVVInYRKSKDAAAEVAAEIE-ELGGKAVVVRADVSQP--QDVEEMFAAVKERFGRLD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFATEG 174
Cdd:cd05359    79 VLVSNAAA-GAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835908839 175 MMQVLADEYQNRHLRVNCINPGGTRTGMRASaFPTEDPQK-----------LKTPADIMPLYLWLMGDDSRRKTGMT 240
Cdd:cd05359   158 LVRYLAVELGPRGIRVNAVSPGVIDTDALAH-FPNREDLLeaaaantpagrVGTPQDVADAVGFLCSDAARMITGQT 233
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
10-238 7.34e-26

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 101.80  E-value: 7.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEkLRQVARTIAdENGTQPQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:PRK08226    4 LTGKTALITGALQGIGEGIARVFARHGANLILLDISPE-IEKLADELC-GRGHRCTAVVADVRDPASVA--AAIKRAKEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGL--LGDICPMSEQNplvwQDV-MQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGR----QGRAnw 162
Cdd:PRK08226   80 EGRIDILVNNAGVcrLGSFLDMSDED----RDFhIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDmvadPGET-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 163 gAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQ----------------KLKTPADIMPLYL 226
Cdd:PRK08226  154 -AYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSNPEdpesvltemakaiplrRLADPLEVGELAA 232

                         250
                  ....*....|..
gi 1835908839 227 WLMGDDSRRKTG 238
Cdd:PRK08226  233 FLASDESSYLTG 244
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 10-240 8.09e-26

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: 101.38  E-value: 8.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTqpqwftldLLTC--TSEECHQLAQRIA 87
Cdd:cd05326     2 LDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDIS--------FVHCdvTVEADVRAAVDTA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 -AHFPRLDGVLHNAGLLGDICP-MSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY 165
Cdd:cd05326    74 vARFGRLDIMFNNAGVLGAPCYsILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGLGPHAY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQ-------------KLKTPADIMPLYLWLMGDD 232
Cdd:cd05326   154 TASKHAVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVEDEAieeavrgaanlkgTALRPEDIAAAVLYLASDD 233


                  ....*...
gi 1835908839 233 SRRKTGMT 240
Cdd:cd05326   234 SRYVSGQN 241
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 11-197 1.10e-25

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: 100.87  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTCtsEECHQLAQRIAAHF 90
Cdd:cd08930     1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALEQLKEELTNLYKNRVIALELDITSK--ESIKELIESYLEKF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGL--LGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVG----------RQG 158
Cdd:cd08930    79 GRIDILINNAYPspKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGviapdfriyeNTQ 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1835908839 159 RANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGG 197
Cdd:cd08930   159 MYSPVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGG 197
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-238 1.47e-25

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 104.93  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   5 PKQDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPqwFTLDLltcTSEE-CHQLA 83
Cdd:PRK08324  415 PKPKPLAGKVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGGPDRALG--VACDV---TDEAaVQAAF 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  84 QRIAAHFPRLDGVLHNAGLL--GDICPMSEQnplVWQDVMQVNVNATFMLTQALLPLLLKSDA-GSLVFTSSSVGRQGRA 160
Cdd:PRK08324  490 EEAALAFGGVDIVVSNAGIAisGPIEETSDE---DWRRSFDVNATGHFLVAREAVRIMKAQGLgGSIVFIASKNAVNPGP 566

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 161 NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGG--TRTGM--------RASAF--PTEDPQK-------LK---TP 218
Cdd:PRK08324  567 NFGAYGAAKAAELHLVRQLALELGPDGIRVNGVNPDAvvRGSGIwtgewieaRAAAYglSEEELEEfyrarnlLKrevTP 646

                         250       260
                  ....*....|....*....|
gi 1835908839 219 ADIMPLYLWLMGDDSRRKTG 238
Cdd:PRK08324  647 EDVAEAVVFLASGLLSKTTG 666
PRK07454 PRK07454
SDR family oxidoreductase;
9-200 2.04e-25

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 100.03  E-value: 2.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLlTCTSEECHQLaQRIAA 88
Cdd:PRK07454    3 LNSMPRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRST-GVKAAAYSIDL-SNPEAIAPGI-AELLE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGllgdicpMSEQNPLV------WQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANW 162
Cdd:PRK07454   80 QFGCPDVLINNAG-------MAYTGPLLemplsdWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAARNAFPQW 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK07454  153 GAYCVSKAALAAFTKCLAEEERSHGIRVCTITLGAVNT 190
PRK06181 PRK06181
SDR family oxidoreductase;
12-236 2.10e-25

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 100.44  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltcTSEE-CHQLAQRIAAHF 90
Cdd:PRK06181    1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLASLAQELADH-GGEALVVPTDV---SDAEaCERLIEAAVARF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGL--LGDICPMSEQNplVWQDVMQVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK06181   77 GGIDILVNNAGItmWSRFDELTDLS--VFERVMRVNYLGAVYCTHAALPHLKASR-GQIVVVSSLAGLTGVPTRSGYAAS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAF-----PTEDP----QKLKTPADIMPLYLWLMgddSRRK 236
Cdd:PRK06181  154 KHALHGFFDSLRIELADDGVAVTVVCPGFVATDIRKRALdgdgkPLGKSpmqeSKIMSAEECAEAILPAI---ARRK 227
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 9-247 2.49e-25

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 100.90  E-value: 2.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVIL--LGRN---EEKLRQVARTIADE---NGTQPQWFTLDLLTCTSEEch 80
Cdd:PRK07791    3 LLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVndIGVGldgSASGGSAAQAVVDEivaAGGEAVANGDDIADWDGAA-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  81 QLAQRIAAHFPRLDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATF-MLTQALLPLLLKSDAG-----SLVFTSS 152
Cdd:PRK07791   81 NLVDAAVETFGGLDVLVNNAGILRDrmIANMSEEE---WDAVIAVHLKGHFaTLRHAAAYWRAESKAGravdaRIINTSS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 153 SVGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGtRTGMRASAF------PTEDPQKLKTPADIMPLYL 226
Cdd:PRK07791  158 GAGLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPAA-RTRMTETVFaemmakPEEGEFDAMAPENVSPLVV 236

                         250       260
                  ....*....|....*....|.
gi 1835908839 227 WLMGDDSRRKTGMTFDAQPGR 247
Cdd:PRK07791  237 WLGSAESRDVTGKVFEVEGGK 257
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 10-219 3.13e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 100.12  E-value: 3.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEklrqVARTIADENGTQPQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:PRK06841   13 LSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSED----VAEVAAQLLGGNAKGLVCDVSDSQSVE--AAVAAVISA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG--LLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK06841   87 FGRIDILVNSAGvaLLAPAEDVSEED---WDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVVALERHVAYCA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPG--GTRTGMRASAFPTEDPQKLKTPA 219
Cdd:PRK06841  164 SKAGVVGMTKVLALEWGPYGITVNAISPTvvLTELGKKAWAGEKGERAKKLIPA 217
PRK06138 PRK06138
SDR family oxidoreductase;
10-240 4.38e-25

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 99.46  E-value: 4.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADenGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK06138    3 LAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAIAA--GGRAFARQGDV--GSAEAVEALVDFVAAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGL--LGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK06138   79 WGRLDVLVNNAGFgcGGTVVTTDEAD---WDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGGRGRAAYVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFP-TEDPQKLK-------------TPADIMPLYLWLMGDDS 233
Cdd:PRK06138  156 SKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFArHADPEALRealrarhpmnrfgTAEEVAQAALFLASDES 235


                  ....*..
gi 1835908839 234 RRKTGMT 240
Cdd:PRK06138  236 SFATGTT 242
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 15-219 7.78e-25

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: 98.52  E-value: 7.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTY-ARYGATVILLGRNEEKLRQV-ARTIADENGTQPQwftLDLltctSEECHQLAQRIAAHFP- 91
Cdd:cd05325     1 VLITGASRGIGLELVRQLlARGNNTVIATCRDPSAATELaALGASHSRLHILE---LDV----TDEIAESAEAVAERLGd 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 -RLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGR---QGRANWGAYAT 167
Cdd:cd05325    74 aGLDVLINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSigdNTSGGWYSYRA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrasAFPTEDPQKLKTPA 219
Cdd:cd05325   154 SKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDM---GGPFAKNKGPITPE 202
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 10-203 1.00e-24

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: 98.38  E-value: 1.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpqwFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:cd08934     1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELEAEGGKA---LVLELDVTDEQQVDAAVERTVEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG--LLGdicPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd08934    78 LGRLDILVNNAGimLLG---PVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNA 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMR 203
Cdd:cd08934   155 TKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTELR 190
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 12-238 1.23e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 98.25  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENgtqpqwFTLDLltctseECHQLAQRIAAHFP 91
Cdd:PRK07060    9 GKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCEP------LRLDV------GDDAAIRAALAAAG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAG--LLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKS-DAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK07060   77 AFDGLVNCAGiaSLESALDMTAEG---FDRVMAVNARGAALVARHVARAMIAAgRGGSIVNVSSQAALVGLPDHLAYCAS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFptEDPQK------------LKTPADIMPLYLWLMGDDSRRK 236
Cdd:PRK07060  154 KAALDAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAW--SDPQKsgpmlaaiplgrFAEVDDVAAPILFLLSDAASMV 231


                  ..
gi 1835908839 237 TG 238
Cdd:PRK07060  232 SG 233
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 15-243 1.48e-24

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: 97.93  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLrqvartiaDENGTQPQWFTLDLltCTSEECHQLAQRIAAHFPRLD 94
Cdd:cd05331     1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLL--------LEYGDPLRLTPLDV--ADAAAVREVCSRLLAEHGPID 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLL--GDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:cd05331    71 ALVNCAGVLrpGATDPLSTED---WEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAAL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 173 EGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED-----------------P-QKLKTPADIMPLYLWLMGD--- 231
Cdd:cd05331   148 ASLSKCLGLELAPYGVRCNVVSPGSTDTAMQRTLWHDEDgaaqviagvpeqfrlgiPlGKIAQPADIANAVLFLASDqag 227

                         250
                  ....*....|....*..
gi 1835908839 232 -----DSRRKTGMTFDA 243
Cdd:cd05331   228 hitmhDLVVDGGATLGA 244
PRK07035 PRK07035
SDR family oxidoreductase;
10-224 4.86e-24

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 96.62  E-value: 4.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpqwftlDLLTCTSEECHQLA---QRI 86
Cdd:PRK07035    6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDGCQAVADAIVAAGGKA------EALACHIGEMEQIDalfAHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK07035   80 RERHGRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGVSPGDFQGIYS 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFpTEDPQKLKTPADIMPL 224
Cdd:PRK07035  160 ITKAAVISMTKAFAKECAPFGIRVNALLPGLTDTKF-ASAL-FKNDAILKQALAHIPL 215
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 10-227 5.26e-24

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: 96.78  E-value: 5.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTqPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:cd08942     4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELS-AYGE-CIAIPADL--SSEEGIEALVARVAER 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGL-----LGDIcPMSEqnplvWQDVMQVNVNATFMLTQALLPLLLKS----DAGSLVFTSSSVGRQGRA 160
Cdd:cd08942    80 SDRLDVLVNNAGAtwgapLEAF-PESG-----WDKVMDINVKSVFFLTQALLPLLRAAataeNPARVINIGSIAGIVVSG 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835908839 161 --NWgAYATSKFATEGMMQVLADEYQNRHLRVNCINPGgtRTGMRASAFPTEDPQKLKTPADIMPLYLW 227
Cdd:cd08942   154 leNY-SYGASKAAVHQLTRKLAKELAGEHITVNAIAPG--RFPSKMTAFLLNDPAALEAEEKSIPLGRW 219
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 10-247 8.52e-24

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: 95.92  E-value: 8.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKlrqvARTIADENGTQPQWFTLDLltcTSEECHQLAQRIAAH 89
Cdd:cd05345     3 LEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADG----AERVAADIGEAAIAIQADV---TKRADVEAMVEAALS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 -FPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05345    76 kFGRLDILVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNAS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPTED-PQ------------KLKTPADIMPLYLWLMGDDSRR 235
Cdd:cd05345   156 KGWVVTATKAMAVELAPRNIRVNCLCPVAGETPL-LSMFMGEDtPEnrakfratiplgRLSTPDDIANAALYLASDEASF 234

                         250
                  ....*....|..
gi 1835908839 236 KTGMTFDAQPGR 247
Cdd:cd05345   235 ITGVALEVDGGR 246
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-204 2.09e-23

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 97.98  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGR--NEEKLRQVARTIadeNGTQpqwFTLDLltCTSEECHQLAQRIA 87
Cdd:PRK08261  208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVCLDVpaAGEALAAVANRV---GGTA---LALDI--TAPDAPARIAEHLA 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSS---VGRQGRANw 162
Cdd:PRK08261  280 ERHGGLDIVVHNAGITRDktLANMDEAR---WDSVLAVNLLAPLRITEALLAAGALGDGGRIVGVSSIsgiAGNRGQTN- 355

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1835908839 163 gaYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRA 204
Cdd:PRK08261  356 --YAASKAGVIGLVQALAPLLAERGITINAVAPGFIETQMTA 395
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 7-242 3.06e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 94.69  E-value: 3.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   7 QDLLQGRIILVTGASDGIGREATQTYARYGAT-VILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltCTSEECHQLAQR 85
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKGEAQAAELE-ALGAKAVFVQADL--SDVEDCRRVVAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  86 IAAHFPRLDGvLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDA-GSLVFTSSSVGRQGRANWGA 164
Cdd:PRK06198   78 ADEAFGRLDA-LVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAHGGQPFLAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT---------------GMRASAFPTEDPQKLKTPADIMPLYLWLM 229
Cdd:PRK06198  157 YCASKGALATLTRNAAYALLRNRIRVNGLNIGWMATegedriqrefhgapdDWLEKAAATQPFGRLLDPDEVARAVAFLL 236

                         250
                  ....*....|...
gi 1835908839 230 GDDSRRKTGMTFD 242
Cdd:PRK06198  237 SDESGLMTGSVID 249
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-208 5.21e-23

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 93.87  E-value: 5.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltcTSEE-CHQLAQRIAA 88
Cdd:PRK08217    3 LKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGAL-GTEVRGYAANV---TDEEdVEATFAQIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGD-----------ICPMS-EQnplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGR 156
Cdd:PRK08217   79 DFGQLNGLINNAGILRDgllvkakdgkvTSKMSlEQ----FQSVIDVNLTGVFLCGREAAAKMIESGSKGVIINISSIAR 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 157 QGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFP 208
Cdd:PRK08217  155 AGNMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAAMKP 206
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 10-247 5.70e-23

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: 94.28  E-value: 5.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVIL--LGRNEEKLRQVARTIaDENGTQPQWFTLDLltctSEE--CHQLAQR 85
Cdd:cd05355    24 LKGKKALITGGDSGIGRAVAIAFAREGADVAInyLPEEEDDAEETKKLI-EEEGRKCLLIPGDL----GDEsfCRDLVKE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  86 IAAHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKsdAGSLVFTSSSVGRQGRANWGAY 165
Cdd:cd05355    99 VVKEFGKLDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK--GSSIINTTSVTAYKGSPHLLDY 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED---------PQKLKTPADIMPLYLWLMGDDSRRK 236
Cdd:cd05355   177 AATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKvsefgsqvpMGRAGQPAEVAPAYVFLASQDSSYV 256

                         250
                  ....*....|.
gi 1835908839 237 TGMTFDAQPGR 247
Cdd:cd05355   257 TGQVLHVNGGE 267
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 14-246 5.80e-23

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: 93.79  E-value: 5.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtqpQWFTLDLLTCTSEECHQLAQRIAAHFPRL 93
Cdd:cd05365     1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVAAAIQQAGG---QAIGLECNVTSEQDLEAVVKATVSQFGGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGLLGdicPMSEQNPLVWQD---VMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKF 170
Cdd:cd05365    78 TILVNNAGGGG---PKPFDMPMTEEDfewAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSENKNVRIAAYGSSKA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 171 ATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQK---------LKTPADIMPLYLWLMGDDSRRKTGMTF 241
Cdd:cd05365   155 AVNHMTRNLAFDLGPKGIRVNAVAPGAVKTDALASVLTPEIERAmlkhtplgrLGEPEDIANAALFLCSPASAWVSGQVL 234


                  ....*
gi 1835908839 242 DAQPG 246
Cdd:cd05365   235 TVSGG 239
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 13-221 6.14e-23

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: 93.20  E-value: 6.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADengtqPQWFTLDLLTctSEECHQLAQRIAAHFPR 92
Cdd:cd08932     1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSASGGD-----VEAVPYDARD--PEDARALVDALRDRFGR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLGDIcPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:cd08932    74 IDVLVHNAGIGRPT-TLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFAL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 173 EGMMQVLADEYQNRHLRVNCINPGGTRTGM-----RASAFPtedPQKLKTPADI 221
Cdd:cd08932   153 RALAHALRQEGWDHGVRVSAVCPGFVDTPMaqgltLVGAFP---PEEMIQPKDI 203
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 10-246 6.93e-23

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 93.44  E-value: 6.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRqvarTIADENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK12936    4 LSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLE----ALAAELGERVKIFPANL--SDRDEVKALGQKAEAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK12936   78 LEGVDILVNNAGITKDglFVRMSDED---WDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRA-----------SAFPTedpQKLKTPADIMPLYLWLMGDDSRRK 236
Cdd:PRK12936  155 SKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGklndkqkeaimGAIPM---KRMGTGAEVASAVAYLASSEAAYV 231

                         250
                  ....*....|
gi 1835908839 237 TGMTFDAQPG 246
Cdd:PRK12936  232 TGQTIHVNGG 241
PRK06500 PRK06500
SDR family oxidoreductase;
10-234 8.31e-23

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 93.48  E-value: 8.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEngtqpqwftldLLTCTSE-----ECHQLAQ 84
Cdd:PRK06500    4 LQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGES-----------ALVIRADagdvaAQKALAQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAAHFPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSdaGSLVFTSSSVGRQGRANWGA 164
Cdd:PRK06500   73 ALAEAFGRLDAVFINAG-VAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANP--ASIVLNGSINAHIGMPNSSV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT------GMRASAFP--TEDPQKL------KTPADIMPLYLWLMG 230
Cdd:PRK06500  150 YAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTplygklGLPEATLDavAAQIQALvplgrfGTPEEIAKAVLYLAS 229


                  ....
gi 1835908839 231 DDSR 234
Cdd:PRK06500  230 DESA 233
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 9-200 9.31e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 93.41  E-value: 9.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltcTSE-ECHQLAQRIA 87
Cdd:PRK12429    1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALQ-KAGGKAIGVAMDV---TDEeAINAGIDYAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK12429   77 ETFGGVDILVNNAG-IQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLVGSAGKAAYVS 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK12429  156 AKHGLIGLTKVVALEGATHGVTVNAICPGYVDT 188
PRK07774 PRK07774
SDR family oxidoreductase;
10-246 9.83e-23

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 93.27  E-value: 9.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpqwFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:PRK07774    4 FDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAEGAERVAKQIVADGGTA---IAVQVDVSDPDSAKAMADATVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGD--ICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSvgrqgrANW---GA 164
Cdd:PRK07774   81 FGGIDYLVNNAAIYGGmkLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSST------AAWlysNF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPG-----GTRT----GMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRR 235
Cdd:PRK07774  155 YGLAKVGLNGLTQQLARELGGMNIRVNAIAPGpidteATRTvtpkEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASW 234

                         250
                  ....*....|.
gi 1835908839 236 KTGMTFDAQPG 246
Cdd:PRK07774  235 ITGQIFNVDGG 245
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 14-215 1.31e-22

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: 92.69  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDlltCTS-EECHQLAQRIAAHFPR 92
Cdd:cd05339     1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKGAEETANNVR-KAGGKVHYYKCD---VSKrEEVYEAAKKIKKEVGD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLGDICPMSEQNPLVwQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:cd05339    77 VTILINNAGVVSGKKLLELPDEEI-EKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLISPAGLADYCASKAAA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835908839 173 EGMMQVLADE---YQNRHLRVNCINPGGTRTGM-------RASAFPTEDPQKL 215
Cdd:cd05339   156 VGFHESLRLElkaYGKPGIKTTLVCPYFINTGMfqgvktpRPLLAPILEPEYV 208
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 10-238 1.66e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 92.70  E-value: 1.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDlltCTSEE-CHQLAQRIAA 88
Cdd:PRK08213   10 LSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLE-ALGIDALWIAAD---VADEAdIERLAEETLE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLL-GdiCPmSEQNPL-VWQDVMQVNVNATFMLTQALLPLL-LKSDAGSLVFTSSSVGRQG----RAN 161
Cdd:PRK08213   86 RFGHVDILVNNAGATwG--AP-AEDHPVeAWDKVMNLNVRGLFLLSQAVAKRSmIPRGYGRIINVASVAGLGGnppeVMD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQ--------KLKTPADIMPLYLWLMGDDS 233
Cdd:PRK08213  163 TIAYNTSKGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLGEDllahtplgRLGDDEDLKGAALLLASDAS 242


                  ....*
gi 1835908839 234 RRKTG 238
Cdd:PRK08213  243 KHITG 247
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 6-240 7.14e-22

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: 91.06  E-value: 7.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   6 KQDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENgtqpqwftldlLTCTSEECH----Q 81
Cdd:cd08936     4 RRDPLANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLQGEG-----------LSVTGTVCHvgkaE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  82 LAQRIAAHFPRLDGVLH----NAGL---LGDICPMSEQnplVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSV 154
Cdd:cd08936    73 DRERLVATAVNLHGGVDilvsNAAVnpfFGNILDSTEE---VWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 155 GRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT----------GMRASAFPTEDPQKLKTPADIMPL 224
Cdd:cd08936   150 AFHPFPGLGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKTsfssalwmdkAVEESMKETLRIRRLGQPEDCAGI 229

                         250
                  ....*....|....*.
gi 1835908839 225 YLWLMGDDSRRKTGMT 240
Cdd:cd08936   230 VSFLCSEDASYITGET 245
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 10-246 7.96e-22

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: 90.63  E-value: 7.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEngtqpqwfTLDLLTCTSEECH--QLAQRIA 87
Cdd:cd08944     1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGG--------ALALRVDVTDEQQvaALFERAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd08944    73 EEFGGLDLLVNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQSGDPGYGAYGA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED---------------PQKLKTPADIMPLYLWLMGDD 232
Cdd:cd08944   153 SKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAKLAGFEgalgpggfhllihqlQGRLGRPEDVAAAVVFLLSDD 232

                         250
                  ....*....|....
gi 1835908839 233 SRRKTGMTFDAQPG 246
Cdd:cd08944   233 ASFITGQVLCVDGG 246
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 10-231 9.67e-22

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 90.71  E-value: 9.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEeklrqvartiADENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK08220    6 FSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAF----------LTQEDYPFATFVLDV--SDAAAVAQVCQRLLAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLD------GVLHnaglLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWG 163
Cdd:PRK08220   74 TGPLDvlvnaaGILR----MGATDSLSDED---WQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHVPRIGMA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED-----------------P-QKLKTPADIMPLY 225
Cdd:PRK08220  147 AYGASKAALTSLAKCVGLELAPYGVRCNVVSPGSTDTDMQRTLWVDEDgeqqviagfpeqfklgiPlGKIARPQEIANAV 226


                  ....*.
gi 1835908839 226 LWLMGD 231
Cdd:PRK08220  227 LFLASD 232
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 10-208 1.20e-21

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 90.73  E-value: 1.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADeNGTQPQWFTLDLltcTSE-ECHQLAQRIAA 88
Cdd:PRK13394    5 LNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGANAVADEINK-AGGKAIGVAMDV---TNEdAVNAGIDKVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSV-GRQGRANWGAYAT 167
Cdd:PRK13394   81 RFGSVDILVSNAG-IQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVhSHEASPLKSAYVT 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFP 208
Cdd:PRK13394  160 AKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQIP 200
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 10-240 2.35e-21

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: 89.45  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARtiaDENGTQPqwFTLDLLTCTSEEchqlaQRIAAH 89
Cdd:cd05351     5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADLDSLVR---ECPGIEP--VCVDLSDWDATE-----EALGSV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPrLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQ-ALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05351    75 GP-VDLLVNNAA-VAILQPFLEVTKEAFDRSFDVNVRAVIHVSQiVARGMIARGVPGSIVNVSSQASQRALTNHTVYCST 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFptEDPQKLKTPADIMPL------------YLWLMGDDSRRK 236
Cdd:cd05351   153 KAALDMLTKVMALELGPHKIRVNSVNPTVVMTDMGRDNW--SDPEKAKKMLNRIPLgkfaevedvvnaILFLLSDKSSMT 230


                  ....
gi 1835908839 237 TGMT 240
Cdd:cd05351   231 TGST 234
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
13-246 2.41e-21

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 89.44  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILlgrNEEKLRQVARTIADENGTQP-QWFTLDLLTCTSEECHQLAQRIAAHFP 91
Cdd:PRK12824    3 KIALVTGAKRGIGSAIARELLNDGYRVIA---TYFSGNDCAKDWFEEYGFTEdQVRLKELDVTDTEECAEALAEIEEEEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK12824   80 PVDILVNNAGITRDsvFKRMSHQE---WNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPTEDPQKLK---------TPADIMPLYLWLMGDDSRRKTGMT 240
Cdd:PRK12824  157 AGMIGFTKALASEGARYGITVNCIAPGYIATPM-VEQMGPEVLQSIVnqipmkrlgTPEEIAAAVAFLVSEAAGFITGET 235


                  ....*.
gi 1835908839 241 FDAQPG 246
Cdd:PRK12824  236 ISINGG 241
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 14-196 2.79e-21

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: 89.26  E-value: 2.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltCTSEECHQLAQRIAAHFPRL 93
Cdd:cd05346     2 TVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAKFPVKVLPLQLDV--SDRESIEAALENLPEEFRDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFATE 173
Cdd:cd05346    80 DILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVR 159

                         170       180
                  ....*....|....*....|...
gi 1835908839 174 GMMQVLADEYQNRHLRVNCINPG 196
Cdd:cd05346   160 QFSLNLRKDLIGTGIRVTNIEPG 182
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 17-208 3.00e-21

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: 88.81  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  17 VTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDlLTCTSEECHQLAQRIAAhfprLD-G 95
Cdd:cd05356     6 VTGATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAAD-FSAGDDIYERIEKELEG----LDiG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  96 VL-HNAGLLGDI-CPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFATE 173
Cdd:cd05356    81 ILvNNVGISHSIpEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1835908839 174 GMMQVLADEYQNRHLRVNCINPGGTRTGM----RASAFP 208
Cdd:cd05356   161 FFSRALYEEYKSQGIDVQSLLPYLVATKMskirKSSLFV 199
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 10-246 4.36e-21

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 89.01  E-value: 4.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGR-NEEKLRQVARTIaDENGTQPQWFTLDLltCTSEECHQLAQRIAA 88
Cdd:PRK08936    5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsDEEEANDVAEEI-KKAGGEAIAVKGDV--TVESDVVNLIQTAVK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLlgDICPMSEQNPLV-WQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQgrANW---GA 164
Cdd:PRK08936   82 EFGTLDVMINNAGI--ENAVPSHEMSLEdWNKVINTNLTGAFLGSREAIKYFVEHDIKGNIINMSSVHEQ--IPWplfVH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFptEDPQKLKT------------PADIMPLYLWLMGDD 232
Cdd:PRK08936  158 YAASKGGVKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEKF--ADPKQRADvesmipmgyigkPEEIAAVAAWLASSE 235

                         250
                  ....*....|....
gi 1835908839 233 SRRKTGMTFDAQPG 246
Cdd:PRK08936  236 ASYVTGITLFADGG 249
PRK07326 PRK07326
SDR family oxidoreductase;
10-229 5.80e-21

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 88.14  E-value: 5.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPqwFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:PRK07326    4 LKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVLG--LAADVRDEADVQ--RAVDAIVAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSdAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK07326   80 FGGLDVLIANAG-VGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRG-GGYIINISSLAGTNFFAGGAAYNASK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKtPADIMPLYLWLM 229
Cdd:PRK07326  158 FGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDAWKIQ-PEDIAQLVLDLL 216
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 12-201 1.41e-20

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: 87.33  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLLTctSEECHQLAQRIAAHFP 91
Cdd:cd05344     1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAASELRAG-GAGVLAVVADLTD--PEDIDRLVEKAGDAFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:cd05344    78 RVDILVNNAGG-PPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVARAG 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRTG 201
Cdd:cd05344   157 LIGLVKTLSRELAPDGVTVNSVLPGYIDTE 186
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 12-207 1.54e-20

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 86.94  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEklrqvartiaDENGTQPQWFTLDLltctseeCHQLAQrIAAHFP 91
Cdd:PRK06550    5 TKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDK----------PDLSGNFHFLQLDL-------SDDLEP-LFDWVP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:PRK06550   67 SVDILCNTAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAAYTASKHA 146

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAF 207
Cdd:PRK06550  147 LAGFTKQLALDYAKDGIQVFGIAPGAVKTPMTAADF 182
PRK05867 PRK05867
SDR family oxidoreductase;
10-238 2.11e-20

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 87.01  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENG---------TQPqwftldlltctsEECH 80
Cdd:PRK05867    7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLADEIGTSGGkvvpvccdvSQH------------QQVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  81 QLAQRIAAHFPRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVgrQGR- 159
Cdd:PRK05867   75 SMLDQVTAELGGIDIAVCNAGII-TVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASM--SGHi 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 160 ----ANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM-------RASAFPTEDPQKLKTPADIMPLYLWL 228
Cdd:PRK05867  152 invpQQVSHYCASKAAVIHLTKAMAVELAPHKIRVNSVSPGYILTELvepyteyQPLWEPKIPLGRLGRPEELAGLYLYL 231

                         250
                  ....*....|
gi 1835908839 229 MGDDSRRKTG 238
Cdd:PRK05867  232 ASEASSYMTG 241
PRK07832 PRK07832
SDR family oxidoreductase;
16-202 2.30e-20

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 87.41  E-value: 2.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltCTSEECHQLAQRIAAHFPRLDG 95
Cdd:PRK07832    4 FVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALGGTVPEHRALDI--SDYDAVAAFAADIHAAHGSMDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  96 VLHNAG--LLGDICPMSEQNplvWQDVMQVN------VNATFMltqalLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK07832   82 VMNIAGisAWGTVDRLTHEQ---WRRMVDVNlmgpihVIETFV-----PPMVAAGRGGHLVNVSSAAGLVALPWHAAYSA 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:PRK07832  154 SKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTPL 188
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 13-238 4.35e-20

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: 85.97  E-value: 4.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVIL-LGRNEEKlrqvARTIADENGTQPQWFTLDLLTctSEECHQLAQRIAAHFP 91
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGARVVVnYYRSTES----AEAVAAEAGERAIAIQADVRD--RDQVQAMIEEAKNHFG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAglLGDICPMSEQNP----LVWQDVM-QVN--VNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGA 164
Cdd:cd05349    75 PVDTIVNNA--LIDFPFDPDQRKtfdtIDWEDYQqQLEgaVKGALNLLQAVLPDFKERGSGRVINIGTNLFQNPVVPYHD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTE--------DP-QKLKTPADIMPLYLWLMGDDSRR 235
Cdd:cd05349   153 YTTAKAALLGFTRNMAKELGPYGITVNMVSGGLLKVTDASAATPKEvfdaiaqtTPlGKVTTPQDIADAVLFFASPWARA 232


                  ...
gi 1835908839 236 KTG 238
Cdd:cd05349   233 VTG 235
PRK06484 PRK06484
short chain dehydrogenase; Validated
 11-204 4.81e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 88.75  E-value: 4.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIadenGTQPQWFTLDLltCTSEECHQLAQRIAAHF 90
Cdd:PRK06484    4 QSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSL----GPDHHALAMDV--SDEAQIREGFEQLHREF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGLLG-DICPMSEQNPLVWQDVMQVNVNATFMLT-QALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK06484   78 GRIDVLVNNAGVTDpTMTATLDTTLEEFARLQAINLTGAYLVArEALRLMIEQGHGAAIVNVASGAGLVALPKRTAYSAS 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRA 204
Cdd:PRK06484  158 KAAVISLTRSLACEWAAKGIRVNAVLPGYVRTQMVA 193
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 10-213 6.11e-20

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: 86.04  E-value: 6.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENgtqPQWFTLDLLTCTS--EECHQLAQRIA 87
Cdd:cd05330     1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEIA---PDAEVLLIKADVSdeAQVEAYVDATV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd05330    78 EQFGRIDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGGIRGVGNQSGYAA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQ 213
Cdd:cd05330   158 AKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKQLGPE 203
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 10-228 9.44e-20

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 85.28  E-value: 9.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtqpQWFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:PRK06113    9 LDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGG---QAFACRCDITSEQELSALADFALSK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLG----DIcPMSEqnpLVWqdVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY 165
Cdd:PRK06113   86 LGKVDILVNNAGGGGpkpfDM-PMAD---FRR--AYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQK---------LKTPADIMPLYLWL 228
Cdd:PRK06113  160 ASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKmlqhtpirrLGQPQDIANAALFL 231
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 15-209 1.07e-19

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: 84.69  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRqvarTIADENGTQPQWFTLDLLTCTSEECHQLAQR-IAAHFPRL 93
Cdd:cd05350     1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLD----ELKAELLNPNPSVEVEILDVTDEERNQLVIAeLEAELGGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGL-----LGDicpmseqnpLVWQD---VMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY 165
Cdd:cd05350    77 DLVIINAGVgkgtsLGD---------LSFKAfreTIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAALRGLPGAAAY 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPT 209
Cdd:cd05350   148 SASKAALSSLAESLRYDVKKRGIRVTVINPGFIDTPLTANMFTM 191
PRK09242 PRK09242
SDR family oxidoreductase;
10-216 1.34e-19

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 84.80  E-value: 1.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQvARTIADENGTQPQWFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:PRK09242    7 LDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQ-ARDELAEEFPEREVHGLAADVSDDEDRRAILDWVEDH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGllGDICPMS-EQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK09242   86 WDGLHILVNNAG--GNIRKAAiDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMT 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTgmRASAFPTEDPQKLK 216
Cdd:PRK09242  164 KAALLQMTRNLAVEWAEDGIRVNAVAPWYIRT--PLTSGPLSDPDYYE 209
PRK06124 PRK06124
SDR family oxidoreductase;
10-223 1.40e-19

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 84.76  E-value: 1.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK06124    9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVAALRAAGGAA-EALAFDI--ADEEAVAAAFARIDAE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK06124   86 HGRLDILVNNVGAR-DRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQVARAGDAVYPAAK 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGgtrtgmrasAFPTEDPQKLKTPADIMP 223
Cdd:PRK06124  165 QGLTGLMRALAAEFGPHGITSNAIAPG---------YFATETNAAMAADPAVGP 209
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 12-201 1.42e-19

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: 84.75  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARtiADENGTQPQWFTLDLltcTSEECHQLA-QRIAAHF 90
Cdd:cd08943     1 GKVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAE--AAQGGPRALGVQCDV---TSEAQVQSAfEQAVLEF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGLL--GDICPMSEQNplvWQDVMQVNVNATFMLTQ-ALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd08943    76 GGLDIVVSNAGIAtsSPIAETSLED---WNRSMDINLTGHFLVSReAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSA 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTG 201
Cdd:cd08943   153 AKAAEAHLARCLALEGGEDGIRVNTVNPDAVFRG 186
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 10-200 3.81e-19

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: 83.65  E-value: 3.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVArTIADENGTQPQWFTLDLLtcTSEECHQLAQRIAAH 89
Cdd:cd05329     4 LEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECL-TEWREKGFKVEGSVCDVS--SRSERQELMDTVASH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 F-PRLDGVLHNAGllGDIC-PMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd05329    81 FgGKLNILVNNAG--TNIRkEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGA 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:cd05329   159 TKGALNQLTRSLACEWAKDNIRVNAVAPWVIAT 191
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 16-247 7.30e-19

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: 82.73  E-value: 7.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVA-RTIADENGTqpQWFTLDLltcTS-EECHQLAQRIAAHFPRL 93
Cdd:cd05323     4 IITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAElQAINPKVKA--TFVQCDV---TSwEQLAAAFKKAIEKFGRV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGLLGDiCPMSEQNPLV--WQDVMQVNVNATFMLTQALLPLLLKS---DAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05323    79 DILINNAGILDE-KSYLFAGKLPppWEKTIDVNLTGVINTTYLALHYMDKNkggKGGVIVNIGSVAGLYPAPQFPVYSAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRH-LRVNCINPGGTRT----GMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSrrKTGMTFDA 243
Cdd:cd05323   158 KHGVVGFTRSLADLLEYKTgVRVNAICPGFTNTpllpDLVAKEAEMLPSAPTQSPEVVAKAIVYLIEDDE--KNGAIWIV 235


                  ....
gi 1835908839 244 QPGR 247
Cdd:cd05323   236 DGGK 239
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 12-240 7.44e-19

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 82.81  E-value: 7.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltCTSEECHQLAQRIAAHFP 91
Cdd:cd05366     2 SKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADV--TDKDDVEALIDQAVEKFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSD-AGSLVFTSSSVGRQGRANWGAYATSKF 170
Cdd:cd05366    80 SFDVMVNNAGI-APITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQGFPNLGAYSASKF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 171 ATEGMMQVLADEYQNRHLRVNCINPGGTRTGM------------------RASAFPTEDPQK-LKTPADIMPLYLWLMGD 231
Cdd:cd05366   159 AVRGLTQTAAQELAPKGITVNAYAPGIVKTEMwdyideevgeiagkpegeGFAEFSSSIPLGrLSEPEDVAGLVSFLASE 238


                  ....*....
gi 1835908839 232 DSRRKTGMT 240
Cdd:cd05366   239 DSDYITGQT 247
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 10-246 1.15e-18

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 82.10  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVIL-LGRNEEKLRQVARTIADENGtqpQWFTLDLLTCTSEECHQLAQRIAA 88
Cdd:PRK12937    3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVnYAGSAAAADELVAEIEAAGG---RAIAVQADVADAAAVTRLFDAAET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAG--LLGDICPMSEQnplVWQDVMQVNVNATFMLTQALLPLLLksDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK12937   80 AFGRIDVLVNNAGvmPLGTIADFDLE---DFDRTIATNLRGAFVVLREAARHLG--QGGRIINLSTSVIALPLPGYGPYA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrasAFPTEDP------------QKLKTPADIMPLYLWLMGDDSR 234
Cdd:PRK12937  155 ASKAAVEGLVHVLANELRGRGITVNAVAPGPVATEL---FFNGKSAeqidqlaglaplERLGTPEEIAAAVAFLAGPDGA 231

                         250
                  ....*....|..
gi 1835908839 235 RKTGMTFDAQPG 246
Cdd:PRK12937  232 WVNGQVLRVNGG 243
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 12-201 1.51e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 82.39  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADengtqpQWFTLDLLTCTSEECHQLAQRIAAHFP 91
Cdd:PRK08263    3 EKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGD------RLLPLALDVTDRAAVFAAVETAVEHFG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAG--LLGDICPMSEQNPlvwQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK08263   77 RLDIVVNNAGygLFGMIEEVTESEA---RAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASK 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTG 201
Cdd:PRK08263  154 WALEGMSEALAQEVAEFGIKVTLVEPGGYSTD 185
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 12-242 1.60e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 82.03  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtqpQWFTLDLLTCTSEECHQLAQRIAAHFP 91
Cdd:PRK07677    1 EKVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIEQFPG---QVLTVQMDVRNPEDVQKMVEQIDEKFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGllGD-ICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDA-GSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK07677   78 RIDALINNAA--GNfICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIkGNIINMVATYAWDAGPGVIHSAAAK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 170 FATEGMMQVLADEYQNRH-LRVNCINPGGT-RTGMRASAFPTEDPQK----------LKTPADIMPLYLWLMGDDSRRKT 237
Cdd:PRK07677  156 AGVLAMTRTLAVEWGRKYgIRVNAIAPGPIeRTGGADKLWESEEAAKrtiqsvplgrLGTPEEIAGLAYFLLSDEAAYIN 235


                  ....*..
gi 1835908839 238 G--MTFD 242
Cdd:PRK07677  236 GtcITMD 242
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 12-217 2.08e-18

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 81.57  E-value: 2.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVArtiadENGTQPQWFTLDLltcTSEECHQLA-QRIAAHF 90
Cdd:cd05371     2 GLVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETVA-----KLGDNCRFVPVDV---TSEKDVKAAlALAKAKF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGllgdICP---------MSEQNPLVWQDVMQVNVNATFMLTQ------ALLPLLLKSDAGSLVFTSSSVG 155
Cdd:cd05371    74 GRLDIVVNCAG----IAVaaktynkkgQQPHSLELFQRVINVNLIGTFNVIRlaagamGKNEPDQGGERGVIINTASVAA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 156 RQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAfptedPQKLKT 217
Cdd:cd05371   150 FEGQIGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAGL-----PEKVRD 206
PRK06128 PRK06128
SDR family oxidoreductase;
2-247 2.42e-18

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 82.21  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   2 HYQPKQD----------LLQGRIILVTGASDGIGREATQTYARYGATVIL--LGRNEEKLRQVARTIADEnGTQPQWFTL 69
Cdd:PRK06128   35 EMQPKPDhgeqsykgfgRLQGRKALITGADSGIGRATAIAFAREGADIALnyLPEEEQDAAEVVQLIQAE-GRKAVALPG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  70 DLltctSEE--CHQLAQRIAAHFPRLDGVLHNAG---LLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLksdA 144
Cdd:PRK06128  114 DL----KDEafCRQLVERAVKELGGLDILVNIAGkqtAVKDIADITTEQ---FDATFKTNVYAMFWLCKAAIPHLP---P 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 145 GSLVFTSSSV-GRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASA---------FPTEDPQK 214
Cdd:PRK06128  184 GASIINTGSIqSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGgqppekipdFGSETPMK 263

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1835908839 215 LK-TPADIMPLYLWLMGDDSRRKTGMTFDAQPGR 247
Cdd:PRK06128  264 RPgQPVEMAPLYVLLASQESSYVTGEVFGVTGGL 297
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 11-205 2.78e-18

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: 81.43  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENgtqpqwFTLDLLTC---TSEECHQLAQRIA 87
Cdd:cd08945     2 DSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELREAG------VEADGRTCdvrSVPEIEALVAAAV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGLL--GDICPMSEQnplVWQDVMQVNVNATFMLTQALLPL--LLKSDAGSLVFTSSSVGRQGRANWG 163
Cdd:cd08945    76 ARYGPIDVLVNNAGRSggGATAELADE---LWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHAA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRAS 205
Cdd:cd08945   153 PYSASKHGVVGFTKALGLELARTGITVNAVCPGFVETPMAAS 194
PRK07201 PRK07201
SDR family oxidoreductase;
10-210 2.78e-18

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 83.85  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK07201  369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIR-AKGGTAHAYTCDL--TDSAAVDHTVKDILAE 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG------------LLGDicpmseqnplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVfTSSSVGRQ 157
Cdd:PRK07201  446 HGHVDYLVNNAGrsirrsvenstdRFHD-----------YERTMAVNYFGAVRLILGLLPHMRERRFGHVV-NVSSIGVQ 513

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 158 GRA-NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRAsafPTE 210
Cdd:PRK07201  514 TNApRFSAYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMIA---PTK 564
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-247 3.12e-18

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 80.98  E-value: 3.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATV-ILLGRNEEKLRQVartiaDENGTqpqwFTLDLLTCTSEECHQLAQRIAA 88
Cdd:PRK06463    5 FKGKVALITGGTRGIGRAIAEAFLREGAKVaVLYNSAENEAKEL-----REKGV----FTIKCDVGNRDQVKKSKEVVEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGrQGRANWGA--YA 166
Cdd:PRK06463   76 EFGRVDVLVNNAGIM-YLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAG-IGTAAEGTtfYA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLK-------------TPADIMPLYLWLMGDDS 233
Cdd:PRK06463  154 ITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDMTLSGKSQEEAEKLRelfrnktvlkttgKPEDIANIVLFLASDDA 233

                         250
                  ....*....|....
gi 1835908839 234 RRKTGMTFDAQPGR 247
Cdd:PRK06463  234 RYITGQVIVADGGR 247
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 10-134 4.92e-18

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: 80.21  E-value: 4.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGRE-ATQTYARyGATVILLGRNEEKLRQVARTIadengtqPQWFTLDLLTCTSEECHQLAQRIAA 88
Cdd:COG3967     3 LTGNTILITGGTSGIGLAlAKRLHAR-GNTVIITGRREEKLEEAAAAN-------PGLHTIVLDVADPASIAALAEQVTA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1835908839  89 HFPRLDGVLHNAGLLGDICPMSEQNPL-VWQDVMQVNVNATFMLTQA 134
Cdd:COG3967    75 EFPDLNVLINNAGIMRAEDLLDEAEDLaDAEREITTNLLGPIRLTAA 121
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 11-212 4.98e-18

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: 80.66  E-value: 4.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltcTSEE-CHQLAQRIAAH 89
Cdd:cd08933     8 ADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKFVPCDV---TKEEdIKTLISVTVER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:cd08933    85 FGRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQ-GNIINLSSLVGSIGQKQAAPYVATK 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGM-RASAFPTEDP 212
Cdd:cd08933   164 GAITAMTKALAVDESRYGVRVNCISPGNIWTPLwEELAAQTPDT 207
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 10-215 6.53e-18

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 80.05  E-value: 6.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILlgrNEEKLRQVARTIADENGTQP-QWFTLDLLTCTSEECHQLAQRIAA 88
Cdd:PRK12935    4 LNGKVAIVTGGAKGIGKAITVALAQEGAKVVI---NYNSSKEAAENLVNELGKEGhDVYAVQADVSKVEDANRLVEEAVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGDICpMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK12935   81 HFGKVDILVNNAGITRDRT-FKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRAsAFPTEDPQKL 215
Cdd:PRK12935  160 KAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMVA-EVPEEVRQKI 205
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
10-196 8.25e-18

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 80.07  E-value: 8.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIadenGTQPQWFTLDlLTCTSEECHQLAQrIAAH 89
Cdd:PRK07067    4 LQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEI----GPAAIAVSLD-VTRQDSIDRIVAA-AVER 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLL-LKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK07067   78 FGGIDILFNNAALF-DMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMvEQGRGGKIINMASQAGRRGEALVSHYCAT 156

                         170       180
                  ....*....|....*....|....*...
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPG 196
Cdd:PRK07067  157 KAAVISYTQSAALALIRHGINVNAIAPG 184
PRK08589 PRK08589
SDR family oxidoreductase;
10-246 9.05e-18

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 80.21  E-value: 9.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNeEKLRQVARTIADeNGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK08589    4 LENKVAVITGASTGIGQASAIALAQEGAYVLAVDIA-EAVSETVDKIKS-NGGKAKAYHVDI--SDEQQVKDFASEIKEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKsDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK08589   80 FGRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME-QGGSIINTSSFSGQAADLYRSGYNAAK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPG-----------GTRTGMRASAFptEDPQK-------LKTPADIMPLYLWLMGD 231
Cdd:PRK08589  159 GAVINFTKSIAIEYGRDGIRANAIAPGtietplvdkltGTSEDEAGKTF--RENQKwmtplgrLGKPEEVAKLVVFLASD 236

                         250
                  ....*....|....*
gi 1835908839 232 DSRRKTGMTFDAQPG 246
Cdd:PRK08589  237 DSSFITGETIRIDGG 251
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 12-240 1.10e-17

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: 79.80  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLG-RNEEKLRQVARTIADENGTQPQWFTLDlLTCtSEECHQLAQRIAAHF 90
Cdd:cd08940     2 GKVALVTGSTSGIGLGIARALAAAGANIVLNGfGDAAEIEAVRAGLAAKHGVKVLYHGAD-LSK-PAAIEDMVAYAQRQF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKF 170
Cdd:cd08940    80 GGVDILVNNAG-IQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLVASANKSAYVAAKH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 171 ATEGMMQVLADEYQNRHLRVNCINPGGTRT--------------------GMRASAFPTEDPQKLKTPADIMPLYLWLMG 230
Cdd:cd08940   159 GVVGLTKVVALETAGTGVTCNAICPGWVLTplvekqisalaqkngvpqeqAARELLLEKQPSKQFVTPEQLGDTAVFLAS 238

                         250
                  ....*....|
gi 1835908839 231 DDSRRKTGMT 240
Cdd:cd08940   239 DAASQITGTA 248
PRK07985 PRK07985
SDR family oxidoreductase;
10-233 1.67e-17

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 79.65  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVIL--LGRNEEKLRQVARTIaDENGTQPQWFTLDLltctSEE--CHQLAQR 85
Cdd:PRK07985   47 LKDRKALVTGGDSGIGRAAAIAYAREGADVAIsyLPVEEEDAQDVKKII-EECGRKAVLLPGDL----SDEkfARSLVHE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  86 IAAHFPRLDGVLHNAG---LLGDICPM-SEQnplvWQDVMQVNVNATFMLTQALLPLLLKsdAGSLVFTSSSVGRQGRAN 161
Cdd:PRK07985  122 AHKALGGLDIMALVAGkqvAIPDIADLtSEQ----FQKTFAINVFALFWLTQEAIPLLPK--GASIITTSSIQAYQPSPH 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED--PQ--------KLKTPADIMPLYLWLMGD 231
Cdd:PRK07985  196 LLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDkiPQfgqqtpmkRAGQPAELAPVYVYLASQ 275


                  ..
gi 1835908839 232 DS 233
Cdd:PRK07985  276 ES 277
PRK07814 PRK07814
SDR family oxidoreductase;
10-246 1.88e-17

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 79.05  E-value: 1.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLLtcTSEECHQLAQRIAAH 89
Cdd:PRK07814    8 LDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEVAEQIRAA-GRRAHVVAADLA--HPEATAGLAGQAVEA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLK-SDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK07814   85 FGRLDIVVNNVGGTMP-NPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEhSGGGSVINISSTMGRLAGRGFAAYGTA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRhLRVNCINPGGTRTG----------MRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTG 238
Cdd:PRK07814  164 KAALAHYTRLAALDLCPR-IRVNAIAPGSILTSalevvaandeLRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLTG 242


                  ....*...
gi 1835908839 239 MTFDAQPG 246
Cdd:PRK07814  243 KTLEVDGG 250
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 16-221 2.12e-17

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: 78.32  E-value: 2.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARtiADENGTQPqwftldlLTCTSEECHQLAQRIAAH---FPR 92
Cdd:cd08929     4 LVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAA--QELEGVLG-------LAGDVRDEADVRRAVDAMeeaFGG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLlGDICPMSEQNPLVW-QDVMQVNVNATFMLTQALLPLLLKSdAGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:cd08929    75 LDALVNNAGV-GVMKPVEELTPEEWrLVLDTNLTGAFYCIHKAAPALLRRG-GGTIVNVGSLAGKNAFKGGAAYNASKFG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASafPTEDPQKLKtPADI 221
Cdd:cd08929   153 LLGLSEAAMLDLREANIRVVNVMPGSVDTGFAGS--PEGQAWKLA-PEDV 199
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
1-200 3.27e-17

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 78.24  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   1 MHYQPKQDLLQGRIILVTGASDGIGREATQTYARYGATVIL--LGRNEEKLRQvartIADENGTQPQWFTLDLltCTSEE 78
Cdd:PRK06935    4 DKFSMDFFSLDGKVAIVTGGNTGLGQGYAVALAKAGADIIIttHGTNWDETRR----LIEKEGRKVTFVQVDL--TKPES 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  79 CHQLAQRIAAHFPRLDGVLHNAGllgdicpMSEQNPLV------WQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSS 152
Cdd:PRK06935   78 AEKVVKEALEEFGKIDILVNNAG-------TIRRAPLLeykdedWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIAS 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1835908839 153 SVGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK06935  151 MLSFQGGKFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 14-228 3.64e-17

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: 77.81  E-value: 3.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltcTSE-ECHQLAQRIAAHFPR 92
Cdd:cd05373     1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDA---RDEdEVIALFDLIEEEIGP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:cd05373    78 LEVLVYNAGA-NVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFAL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835908839 173 EGMMQVLADEYQNRHLRV-NCINPGGTRTGMRASAFPTEDPQKLK----TPADIMPLYLWL 228
Cdd:cd05373   157 RALAQSMARELGPKGIHVaHVIIDGGIDTDFIRERFPKRDERKEEdgilDPDAIAEAYWQL 217
PRK06114 PRK06114
SDR family oxidoreductase;
10-202 5.25e-17

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 77.90  E-value: 5.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEK-LRQVARTIADENGTQPQwftldlLTCTSEECHQLAQRIA- 87
Cdd:PRK06114    6 LDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAETAEHIEAAGRRAIQ------IAADVTSKADLRAAVAr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 --AHFPRLDGVLHNAGLLGDIcPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVG---RQGrANW 162
Cdd:PRK06114   80 teAELGALTLAVNAAGIANAN-PAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGiivNRG-LLQ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:PRK06114  158 AHYNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPM 197
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 13-196 7.03e-17

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: 76.93  E-value: 7.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEklrQVARTIADE-NGTQPQWFTL--DLltCTSEECHQLAQRIAAH 89
Cdd:cd05357     1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSE---AEAQRLKDElNALRNSAVLVqaDL--SDFAACADLVAAAFRA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG--LLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:cd05357    76 FGRCDVLVNNASafYPTPLGQGSEDA---WAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTDRPLTGYFAYCM 152

                         170       180
                  ....*....|....*....|....*....
gi 1835908839 168 SKFATEGMMQVLADEYQNRhLRVNCINPG 196
Cdd:cd05357   153 SKAALEGLTRSAALELAPN-IRVNGIAPG 180
PRK06484 PRK06484
short chain dehydrogenase; Validated
 12-200 8.55e-17

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 79.12  E-value: 8.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTqpqwFTLDLLTCTSEEchQLAQRIAAHFP 91
Cdd:PRK06484  269 PRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLS----VQADITDEAAVE--SAFAQIQARWG 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKsdAGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:PRK06484  343 RLDVLVNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQ--GGVIVNLGSIASLLALPPRNAYCASKAA 420

                         170       180
                  ....*....|....*....|....*....
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK06484  421 VTMLSRSLACEWAPAGIRVNTVAPGYIET 449
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 10-202 9.90e-17

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 77.10  E-value: 9.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK08085    7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQE-GIKAHAAPFNV--THKQEVEAAIEHIEKD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLL--GDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK08085   84 IGPIDVLINNAGIQrrHPFTEFPEQE---WNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDTITPYAA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1835908839 168 SKFA----TEGMMQVLAdeyqnRH-LRVNCINPGGTRTGM 202
Cdd:PRK08085  161 SKGAvkmlTRGMCVELA-----RHnIQVNGIAPGYFKTEM 195
PRK07856 PRK07856
SDR family oxidoreductase;
10-238 1.02e-16

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 76.90  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEklrqvartiADENGTQPQWFTLDLLtcTSEECHQLAQRIAAH 89
Cdd:PRK07856    4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAP---------ETVDGRPAEFHAADVR--DPDQVAALVDAIVER 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDIcPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDA-GSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK07856   73 HGRLDVLVNNAGGSPYA-LAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPGgGSIVNIGSVSGRRPSPGTAAYGAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRhLRVNCINPGGTRTGmrASAFPTEDPQ------------KLKTPADIMPLYLWLMGDDSRRK 236
Cdd:PRK07856  152 KAGLLNLTRSLAVEWAPK-VRVNAVVVGLVRTE--QSELHYGDAEgiaavaatvplgRLATPADIAWACLFLASDLASYV 228


                  ..
gi 1835908839 237 TG 238
Cdd:PRK07856  229 SG 230
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 10-196 1.05e-16

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: 77.11  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIaDENGTQPQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:cd08935     3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEI-TALGGRAIALAADVLDRASLE--RAREEIVAQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 F----------------PRLDGVLHNAGLLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSS 153
Cdd:cd08935    80 FgtvdilingaggnhpdATTDPEHYEPETEQNFFDLDEEG---WEFVFDLNLNGSFLPSQVFGKDMLEQKGGSIINISSM 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1835908839 154 VGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPG 196
Cdd:cd08935   157 NAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPG 199
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 10-243 1.32e-16

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: 76.62  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARtiadENGTQPQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:cd05348     2 LKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRA----DFGDAVVGVEGDVRSLADNE--RAVARCVER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGL------LGDICPmsEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWG 163
Cdd:cd05348    76 FGKLDCFIGNAGIwdystsLVDIPE--EKLDEAFDELFHINVKGYILGAKAALPALYATE-GSVIFTVSNAGFYPGGGGP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNrHLRVNCINPGGTRT-----------GMRASAFPTED------P-QKLKTPADIMPLY 225
Cdd:cd05348   153 LYTASKHAVVGLVKQLAYELAP-HIRVNGVAPGGMVTdlrgpaslgqgETSISTPPLDDmlksilPlGFAPEPEDYTGAY 231

                         250       260
                  ....*....|....*....|.
gi 1835908839 226 LWLMG-DDSRRKTG--MTFDA 243
Cdd:cd05348   232 VFLASrGDNRPATGtvINYDG 252
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-246 1.68e-16

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 76.27  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGAS--DGIGREATQTYARYGATVIL-----------LGRNEEKLRQVARTIADeNGTQPQWFTLDLltCTS 76
Cdd:PRK12748    3 LMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFtywspydktmpWGMHDKEPVLLKEEIES-YGVRCEHMEIDL--SQP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  77 EECHQLAQRIAAHFPRLDGVLHNAGllgdicpMSEQNPLVWQDVMQ------VNVNATFMLTQALLPLLLKSDAGSLVFT 150
Cdd:PRK12748   80 YAPNRVFYAVSERLGDPSILINNAA-------YSTHTRLEELTAEQldkhyaVNVRATMLLSSAFAKQYDGKAGGRIINL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 151 SSSVGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTG------MRA--SAFPTedpQKLKTPADIM 222
Cdd:PRK12748  153 TSGQSLGPMPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGwiteelKHHlvPKFPQ---GRVGEPVDAA 229

                         250       260
                  ....*....|....*....|....
gi 1835908839 223 PLYLWLMGDDSRRKTGMTFDAQPG 246
Cdd:PRK12748  230 RLIAFLVSEEAKWITGQVIHSEGG 253
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 10-196 1.77e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 76.64  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltcTSEE-CHQLAQRIAA 88
Cdd:PRK07097    8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYR-ELGIEAHGYVCDV---TDEDgVQAMVSQIEK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGDIcPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK07097   84 EVGVIDILVNNAGIIKRI-PMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSELGRETVSAYAAA 162

                         170       180
                  ....*....|....*....|....*...
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPG 196
Cdd:PRK07097  163 KGGLKMLTKNIASEYGEANIQCNGIGPG 190
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 15-221 2.37e-16

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: 75.57  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENG-TQPqwftLDLlTCTSEECHQLAQRIAAHFPRL 93
Cdd:cd08931     3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGAENVvAGA----LDV-TDRAAWAAALADFAAATGGRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGLL--GdicpMSEQNPLVWQDVMqVNVNATFMLTQALLPL-LLKSDAGSLVF-TSSSVGRQGRANWGAYATSK 169
Cdd:cd08931    78 DALFNNAGVGrgG----PFEDVPLAAHDRM-VDINVKGVLNGAYAALpYLKATPGARVInTASSSAIYGQPDLAVYSATK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRT----GMRASAFPTEDPQKLKTPADI 221
Cdd:cd08931   153 FAVRGLTEALDVEWARHGIRVADVWPWFVDTpiltKGETGAAPKKGLGRVLPVSDV 208
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
12-240 2.70e-16

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 75.92  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtqpQWFTLDLLTCTSEECHQLAQRIAAHFP 91
Cdd:PRK08643    2 SKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAAADKLSKDGG---KAIAVKADVSDRDQVFAAVRQVVDTFG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSD-AGSLVFTSSSVGRQGRANWGAYATSKF 170
Cdd:PRK08643   79 DLNVVVNNAG-VAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhGGKIINATSQAGVVGNPELAVYSSTKF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 171 ATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRAS-------------AFPTEDPQK------LKTPADIMPLYLWLMGD 231
Cdd:PRK08643  158 AVRGLTQTAARDLASEGITVNAYAPGIVKTPMMFDiahqvgenagkpdEWGMEQFAKditlgrLSEPEDVANCVSFLAGP 237


                  ....*....
gi 1835908839 232 DSRRKTGMT 240
Cdd:PRK08643  238 DSDYITGQT 246
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 10-203 3.74e-16

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 75.38  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADengtqpqwftlDLLT----CTSEECHQLA-Q 84
Cdd:PRK06200    4 LHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGD-----------HVLVvegdVTSYADNQRAvD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAAHFPRLDGVLHNAGL------LGDICPmsEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSdAGSLVFTSSS----V 154
Cdd:PRK06200   73 QTVDAFGKLDCFVGNAGIwdyntsLVDIPA--ETLDTAFDEIFNVNVKGYLLGAKAALPALKAS-GGSMIFTLSNssfyP 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1835908839 155 GRQGRanwgAYATSKFATEGMMQVLADEYQNrHLRVNCINPGGTRTGMR 203
Cdd:PRK06200  150 GGGGP----LYTASKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTDLR 193
PRK06947 PRK06947
SDR family oxidoreductase;
13-247 4.01e-16

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 75.23  E-value: 4.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATV-ILLGRNEEKLRQVARTIADENGTqpqwfTLDLLTCTSEECHQLA--QRIAAH 89
Cdd:PRK06947    3 KVVLITGASRGIGRATAVLAAARGWSVgINYARDAAAAEETADAVRAAGGR-----ACVVAGDVANEADVIAmfDAVQSA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKS---DAGSLVFTSSSVGRQGRAN-WGAY 165
Cdd:PRK06947   78 FGRLDALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrggRGGAIVNVSSIASRLGSPNeYVDY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKL---------KTPADIMPLYLWLMGDDSRRK 236
Cdd:PRK06947  158 AGSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRAARLgaqtplgraGEADEVAETIVWLLSDAASYV 237

                         250
                  ....*....|.
gi 1835908839 237 TGMTFDAQPGR 247
Cdd:PRK06947  238 TGALLDVGGGR 248
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 10-223 5.25e-16

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 74.86  E-value: 5.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtqPQWFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:cd05343     4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALAAECQSAGY--PTLFPYQCDLSNEEQILSMFSAIRTQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQAL--LPLLLKSDAGSLVFTSSSVGR--QGRANWGAY 165
Cdd:cd05343    82 HQGVDVCINNAG-LARPEPLLSGKTEGWKEMFDVNVLALSICTREAyqSMKERNVDDGHIININSMSGHrvPPVSVFHFY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 166 ATSKFATEGMMQVLADEYQ--NRHLRVNCINPGGTRTGMrASAFPTEDPQKLKTPADIMP 223
Cdd:cd05343   161 AATKHAVTALTEGLRQELReaKTHIRATSISPGLVETEF-AFKLHDNDPEKAAATYESIP 219
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 10-212 6.05e-16

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: 74.37  E-value: 6.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGrneeklrqvARTIA------DENGTQPQWFTLDLLTCTSeechqlA 83
Cdd:cd05354     1 IKDKTVLVTGANRGIGKAFVESLLAHGAKKVYAA---------VRDPGsaahlvAKYGDKVVPLRLDVTDPES------I 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  84 QRIAAHFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWG 163
Cdd:cd05354    66 KAAAAQAKDVDVVINNAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVASLKNFPAMG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASA-FPTEDP 212
Cdd:cd05354   146 TYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAgGPKESP 195
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 10-200 6.52e-16

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 74.70  E-value: 6.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltCTSEECHQLAQRIAAh 89
Cdd:PRK06125    5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVHALDL--SSPEAREQLAAEAGD- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 fprLDGVLHNAGLL--GDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK06125   82 ---IDILVNNAGAIpgGGLDDVDDAA---WRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGENPDADYICGSA 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK06125  156 GNAALMAFTRALGGKSLDDGVRVVGVNPGPVAT 188
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 10-205 6.79e-16

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 74.80  E-value: 6.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpqwFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:PRK07523    8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQGLSA---HALAFDVTDHDAVRAAIDAFEAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGllgdicpMSEQNPL------VWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWG 163
Cdd:PRK07523   85 IGPIDILVNNAG-------MQFRTPLedfpadAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSALARPGIA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRAS 205
Cdd:PRK07523  158 PYTATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAA 199
PRK07074 PRK07074
SDR family oxidoreductase;
13-238 9.32e-16

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 74.42  E-value: 9.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpqwFTLDLltcTSEE--CHQLAQRIAAHF 90
Cdd:PRK07074    3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFVP---VACDL---TDAAslAAALANAAAERG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PrLDGVLHNAGLLGDICpMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSvgrQGRANWG--AYATS 168
Cdd:PRK07074   77 P-VDVLVANAGAARAAS-LHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSV---NGMAALGhpAYSAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM---RASAFPT--ED-----P-QKLKTPADIMPLYLWLMGDDSRRKT 237
Cdd:PRK07074  152 KAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAweaRVAANPQvfEElkkwyPlQDFATPDDVANAVLFLASPAARAIT 231


                  .
gi 1835908839 238 G 238
Cdd:PRK07074  232 G 232
PRK09135 PRK09135
pteridine reductase; Provisional
 11-233 1.07e-15

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 74.19  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEklrQVARTIADE-NGTQPQWFTL---DLLTCtsEECHQLAQRI 86
Cdd:PRK09135    5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSA---AEADALAAElNALRPGSAAAlqaDLLDP--DALPELVAAC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGL-----LGDIcpmSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSdAGSLVFTSSSVGRQGRAN 161
Cdd:PRK09135   80 VAAFGRLDALVNNASSfyptpLGSI---TEAQ---WDDLFASNLKAPFFLSQAAAPQLRKQ-RGAIVNITDIHAERPLKG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNrHLRVNCINPGgtrtgmrASAFPTEDP----------------QKLKTPADIMPLY 225
Cdd:PRK09135  153 YPVYCAAKAALEMLTRSLALELAP-EVRVNAVAPG-------AILWPEDGNsfdeearqailartplKRIGTPEDIAEAV 224


                  ....*...
gi 1835908839 226 LWLMGDDS 233
Cdd:PRK09135  225 RFLLADAS 232
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 10-196 1.54e-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: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKlrqvARTIADENGTQPQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:cd05363     1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEA----ARATAAEIGPAACAISLDVTDQASID--RCVAALVDR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPL-LLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05363    75 WGSIDILVNNAALF-DLAPIVDITRESYDRLFAINVSGTLFMMQAVARAmIAQGRGGKIINMASQAGRRGEALVGVYCAT 153

                         170       180
                  ....*....|....*....|....*...
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPG 196
Cdd:cd05363   154 KAAVISLTQSAGLNLIRHGINVNAIAPG 181
PRK07063 PRK07063
SDR family oxidoreductase;
10-213 1.63e-15

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 73.93  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADE-NGTQPQWFTLDLltCTSEECHQLAQRIAA 88
Cdd:PRK07063    5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERAAAAIARDvAGARVLAVPADV--TDAASVAAAVAAAEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGL--LGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK07063   83 AFGPLDVLVNNAGInvFADPLAMTDED---WRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAFKIIPGCFPYP 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRAS---AFPteDPQ 213
Cdd:PRK07063  160 VAKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDwwnAQP--DPA 207
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
10-232 2.96e-15

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 72.98  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNE-----EKLRQVARTIADengtqpqwFTLDLLTCtsEECHQLAQ 84
Cdd:PRK08993    8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDIVGINIVEptetiEQVTALGRRFLS--------LTADLRKI--DGIPALLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAAHFPRLDGVLHNAGLL--GDICPMSEQNplvWQDVMQVNVNATFMLTQALLPL-LLKSDAGSLVFTSSSVGRQGRAN 161
Cdd:PRK08993   78 RAVAEFGHIDILVNNAGLIrrEDAIEFSEKD---WDDVMNLNIKSVFFMSQAAAKHfIAQGNGGKIINIASMLSFQGGIR 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAfpTEDPQKLKTPADIMPLYLWLMGDD 232
Cdd:PRK08993  155 VPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMATNNTQQL--RADEQRSAEILDRIPAGRWGLPSD 223
PLN02253 PLN02253
xanthoxin dehydrogenase
 5-238 3.25e-15

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 73.32  E-value: 3.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   5 PKQDLLqGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpqWFTLDLltcTSEECHQLAQ 84
Cdd:PLN02253   12 PSQRLL-GKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVC--FFHCDV---TVEDDVSRAV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAA-HFPRLDGVLHNAGLLGDICPMSEQNPLV-WQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANW 162
Cdd:PLN02253   86 DFTVdKFGTLDIMVNNAGLTGPPCPDIRNVELSeFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGLGP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFP----TEDPQK-----------LK----TPADIMP 223
Cdd:PLN02253  166 HAYTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALALAHLPederTEDALAgfrafagknanLKgvelTVDDVAN 245

                         250
                  ....*....|....*
gi 1835908839 224 LYLWLMGDDSRRKTG 238
Cdd:PLN02253  246 AVLFLASDEARYISG 260
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 13-200 3.48e-15

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: 72.42  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltCTSEECHQLAQRIAAHFPR 92
Cdd:cd05360     1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVR-ELGGEAIAVVADV--ADAAQVERAADTAVERFGR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:cd05360    78 IDTWVNNAG-VAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAV 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1835908839 173 EGMMQVLADEYQ--NRHLRVNCINPGGTRT 200
Cdd:cd05360   157 RGFTESLRAELAhdGAPISVTLVQPTAMNT 186
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 10-222 3.70e-15

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 72.43  E-value: 3.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEE--------KLRQVARTIADE---NGTQPQWFTLDLLtcTSEE 78
Cdd:cd05338     1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASegdngsakSLPGTIEETAEEieaAGGQALPIVVDVR--DEDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  79 CHQLAQRIAAHFPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRqg 158
Cdd:cd05338    79 VRALVEATVDQFGRLDILVNNAG-AIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLSL-- 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835908839 159 RANWG--AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIM 222
Cdd:cd05338   156 RPARGdvAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTAIETPAATELSGGSDPARARSPEIL 221
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-248 3.99e-15

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 72.49  E-value: 3.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENgtQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK05786    3 LKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKYG--NIHYVVGDV--SSTESARNVIEKAAKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDG-VLHNAGLLGDicPMSEQNPLvwQDVMQVNVNATFMLTQALLPLLLKsdaGSLVFTSSSVGRQGRA--NWGAYA 166
Cdd:PRK05786   79 LNAIDGlVVTVGGYVED--TVEEFSGL--EEMLTNHIKIPLYAVNASLRFLKE---GSSIVLVSSMSGIYKAspDQLSYA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGgtrtGMRASAFPTEDPQKLKT-------PADIMPLYLWLMGDDSRRKTGM 239
Cdd:PRK05786  152 VAKAGLAKAVEILASELLGRGIRVNGIAPT----TISGDFEPERNWKKLRKlgddmapPEDFAKVIIWLLTDEADWVDGV 227


                  ....*....
gi 1835908839 240 TFDAQPGRK 248
Cdd:PRK05786  228 VIPVDGGAR 236
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 10-240 5.23e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 72.76  E-value: 5.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPqwftldLLTC--TSEE--CHQLAQR 85
Cdd:PRK06701   44 LKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDANETKQRVEKEGVKC------LLIPgdVSDEafCKDAVEE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  86 IAAHFPRLDGVLHNAGL------LGDIcpMSEQnplvWQDVMQVNVNATFMLTQALLPLLLKSDAgsLVFTSSSVGRQGR 159
Cdd:PRK06701  118 TVRELGRLDILVNNAAFqypqqsLEDI--TAEQ----LDKTFKTNIYSYFHMTKAALPHLKQGSA--IINTGSITGYEGN 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 160 ANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQK------LKTPA---DIMPLYLWLMG 230
Cdd:PRK06701  190 ETLIDYSATKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEKVSQfgsntpMQRPGqpeELAPAYVFLAS 269

                         250
                  ....*....|
gi 1835908839 231 DDSRRKTGMT 240
Cdd:PRK06701  270 PDSSYITGQM 279
PRK06123 PRK06123
SDR family oxidoreductase;
13-247 5.38e-15

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 72.12  E-value: 5.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYG-ATVILLGRNEEKLRQVARTIADENGTqpqwfTLDLLTCTSEECH--QLAQRIAAH 89
Cdd:PRK06123    3 KVMIITGASRGIGAATALLAAERGyAVCLNYLRNRDAAEAVVQAIRRQGGE-----ALAVAADVADEADvlRLFEAVDRE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAG---SLVFTSSSVGRQGRAN-WGAY 165
Cdd:PRK06123   78 LGRLDALVNNAGILEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGrggAIVNVSSMAARLGSPGeYIDY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLK---------TPADIMPLYLWLMGDDSRRK 236
Cdd:PRK06123  158 AASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGRVDRVKagipmgrggTAEEVARAILWLLSDEASYT 237

                         250
                  ....*....|.
gi 1835908839 237 TGMTFDAQPGR 247
Cdd:PRK06123  238 TGTFIDVSGGR 248
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 11-214 6.06e-15

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 72.28  E-value: 6.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNeEKLRQVARTIADeNGTQPQWFTLDLLtcTSEECHQLAQRIAAHF 90
Cdd:PRK12823    7 AGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRS-ELVHEVAAELRA-AGGEALALTADLE--TYAGAQAAMAAAVEAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGllGDIC--PMSEQNPlvwqDVMQVNVNATFMLT----QALLPLLLKSDAGSLVFTSSSVGRQgrANWGA 164
Cdd:PRK12823   83 GRIDVLINNVG--GTIWakPFEEYEE----EQIEAEIRRSLFPTlwccRAVLPHMLAQGGGAIVNVSSIATRG--INRVP 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPGGT----RTGMRASAFPTEDPQK 214
Cdd:PRK12823  155 YSAAKGGVNALTASLAFEYAEHGIRVNAVAPGGTeappRRVPRNAAPQSEQEKA 208
PRK09291 PRK09291
SDR family oxidoreductase;
15-224 7.00e-15

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 71.95  E-value: 7.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVaRTIADENGTQPQWFTLDLLtctseeCHQLAQRIAAHFPrlD 94
Cdd:PRK09291    5 ILITGAGSGFGREVALRLARKGHNVIAGVQIAPQVTAL-RAEAARRGLALRVEKLDLT------DAIDRAQAAEWDV--D 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGL-----LGDIcPMSeqnpLVwQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK09291   76 VLLNNAGIgeagaVVDI-PVE----LV-RELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITGPFTGAYCASK 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTG----MRASAFPTEDPQK-LKTPADIMPL 224
Cdd:PRK09291  150 HALEAIAEAMHAELKPFGIQVATVNPGPYLTGfndtMAETPKRWYDPARnFTDPEDLAFP 209
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 15-249 7.41e-15

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: 72.14  E-value: 7.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTqpqwFTLDLltCTSEECHQLAQRIAAhFPRLD 94
Cdd:cd08951    10 IFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGV----LIGDL--SSLAETRKLADQVNA-IGRFD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLLGDicPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLlksdagSLVFTSSSVGRQGRA-----NWG------ 163
Cdd:cd08951    83 AVIHNAGILSG--PNRKTPDTGIPAMVAVNVLAPYVLTALIRRPK------RLIYLSSGMHRGGNAslddiDWFnrgend 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 164 --AYATSKFATEGMMQVLADEYQNrhLRVNCINPGGTRTGMR-ASAfptedPQKLKtpaDIMPLYLWL-MGDDSRRKT-G 238
Cdd:cd08951   155 spAYSDSKLHVLTLAAAVARRWKD--VSSNAVHPGWVPTKMGgAGA-----PDDLE---QGHLTQVWLaESDDPQALTsG 224

                         250
                  ....*....|.
gi 1835908839 239 MTFDAQPGRKP 249
Cdd:cd08951   225 GYFYHRRLQEP 235
PRK06398 PRK06398
aldose dehydrogenase; Validated
 10-216 8.97e-15

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 71.79  E-value: 8.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEeklrqvartiadengtqPQWFTLDLLTC---TSEECHQLAQRI 86
Cdd:PRK06398    4 LKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKE-----------------PSYNDVDYFKVdvsNKEQVIKGIDYV 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGL--LGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGA 164
Cdd:PRK06398   67 ISKYGRIDILVNNAGIesYGAIHAVEEDE---WDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFAVTRNAAA 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRhLRVNCINPGGTRTGMRASAFPTE---DPQKLK 216
Cdd:PRK06398  144 YVTSKHAVLGLTRSIAVDYAPT-IRCVAVCPGSIRTPLLEWAAELEvgkDPEHVE 197
PRK09730 PRK09730
SDR family oxidoreductase;
14-247 1.33e-14

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 71.03  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVIL-LGRNEEKLRQVARTIADENGtqpQWFTLDLLTCTSEECHQLAQRIAAHFPR 92
Cdd:PRK09730    3 IALVTGGSRGIGRATALLLAQEGYTVAVnYQQNLHAAQEVVNLITQAGG---KAFVLQADISDENQVVAMFTAIDQHDEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGS---LVFTSSSVGRQGR-ANWGAYATS 168
Cdd:PRK09730   80 LAALVNNAGILFTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSggaIVNVSSAASRLGApGEYVDYAAS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRA------------SAFPTedpQKLKTPADIMPLYLWLMGDDSRRK 236
Cdd:PRK09730  160 KGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHAsggepgrvdrvkSNIPM---QRGGQPEEVAQAIVWLLSDKASYV 236

                         250
                  ....*....|.
gi 1835908839 237 TGMTFDAQPGR 247
Cdd:PRK09730  237 TGSFIDLAGGK 247
PRK12746 PRK12746
SDR family oxidoreductase;
10-246 1.44e-14

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 71.22  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATV-ILLGRNEEKLRQVARTIADENGT----QPQWFTLDLLTCTSEEC-HQLA 83
Cdd:PRK12746    4 LDGKVALVTGASRGIGRAIAMRLANDGALVaIHYGRNKQAADETIREIESNGGKafliEADLNSIDGVKKLVEQLkNELQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  84 QRIAAhfPRLDGVLHNAGL--LGDICPMSEQnplVWQDVMQVNVNATFMLTQALLPLLLKSdaGSLVFTSSSVGRQGRAN 161
Cdd:PRK12746   84 IRVGT--SEIDILVNNAGIgtQGTIENTTEE---IFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLGFTG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFptEDPQ------------KLKTPADIMPLYLWLM 229
Cdd:PRK12746  157 SIAYGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAKLL--DDPEirnfatnssvfgRIGQVEDIADAVAFLA 234

                         250
                  ....*....|....*..
gi 1835908839 230 GDDSRRKTGMTFDAQPG 246
Cdd:PRK12746  235 SSDSRWVTGQIIDVSGG 251
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 13-232 1.59e-14

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: 70.95  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATV-ILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltcTSEECHQ-LAQRIAAHF 90
Cdd:cd05337     2 PVAIVTGASRGIGRAIATELAARGFDIaINDLPDDDQATEVVAEVLAA-GRRAIYFQADI---GELSDHEaLLDQAWEDF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGL----LGDICPMSEQNplvWQDVMQVNVNATFMLTQA------LLPLLLKSDAGSLVFTSSSVGRQGRA 160
Cdd:cd05337    78 GRLDCLVNNAGIavrpRGDLLDLTEDS---FDRLIAINLRGPFFLTQAvarrmvEQPDRFDGPHRSIIFVTSINAYLVSP 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 161 NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQklkTPADIMPLYLWLMGDD 232
Cdd:cd05337   155 NRGEYCISKAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDEL---IAAGLVPIRRWGQPED 223
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 4-206 1.68e-14

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 72.64  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   4 QPKQDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtqpqwfTLDLLTCTSEECHQLA 83
Cdd:COG3347   417 MPKPKPLAGRVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYG------ADAVDATDVDVTAEAA 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  84 QRIAAHFPRLD--GVLHNAGLLGDICPMS--EQNPLVWQDVMQVNVNATFMLTQALLPLLLKS-DAGSLVFTSSSVGRQG 158
Cdd:COG3347   491 VAAAFGFAGLDigGSDIGVANAGIASSSPeeETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQgLGGSSVFAVSKNAAAA 570

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1835908839 159 RANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASA 206
Cdd:COG3347   571 AYGAAAAATAKAAAQHLLRALAAEGGANGINANRVNPDAVLDGSAIWA 618
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 10-198 2.20e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 70.81  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVartiADENGTQPQWFTLDLltcTSEEchQLAQ---RI 86
Cdd:PRK08265    4 LAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAV----AASLGERARFIATDI---TDDA--AIERavaTV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGLLGDICPMSEQNPlvWQDVMQVNVNATFMLTQAlLPLLLKSDAGSLV-FTS--SSVGRQGRAnwg 163
Cdd:PRK08265   75 VARFGRVDILVNLACTYLDDGLASSRAD--WLAALDVNLVSAAMLAQA-AHPHLARGGGAIVnFTSisAKFAQTGRW--- 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGT 198
Cdd:PRK08265  149 LYPASKAAIRQLTRSMAMDLAPDGIRVNSVSPGWT 183
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 15-202 2.36e-14

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: 70.77  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVI-----LLGRNEEKLRQVartiadengTQPQWFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:cd09805     3 VLITGCDSGFGNLLAKKLDSLGFTVLagcltKNGPGAKELRRV---------CSDRLRTLQLDVTKPEQIKRAAQWVKEH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPR--LDGVLHNAGLLG-----DICPMSeqnplVWQDVMQVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANW 162
Cdd:cd09805    74 VGEkgLWGLVNNAGILGfggdeELLPMD-----DYRKCMEVNLFGTVEVTKAFLPLLRRAK-GRVVNVSSMGGRVPFPAG 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:cd09805   148 GAYCASKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGI 187
PRK07577 PRK07577
SDR family oxidoreductase;
13-238 3.13e-14

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 69.76  E-value: 3.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNeeklrqvarTIADengtqpqwFTLDLLTCTSEECHQLAQ---RIAAH 89
Cdd:PRK07577    4 RTVLVTGATKGIGLALSLRLANLGHQVIGIARS---------AIDD--------FPGELFACDLADIEQTAAtlaQINEI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPrLDGVLHNAGL-----LGDIcpmsEQNPLvwQDVMQVNVNATFMLTQALLPLLLKSDAGSLVfTSSSVGRQGRANWGA 164
Cdd:PRK07577   67 HP-VDAIVNNVGIalpqpLGKI----DLAAL--QDVYDLNVRAAVQVTQAFLEGMKLREQGRIV-NICSRAIFGALDRTS 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFP-----------TEDPQKLKTPADIMPLYLWLMGDDS 233
Cdd:PRK07577  139 YSAAKSALVGCTRTWALELAEYGITVNAVAPGPIETELFRQTRPvgseeekrvlaSIPMRRLGTPEEVAAAIAFLLSDDA 218


                  ....*
gi 1835908839 234 RRKTG 238
Cdd:PRK07577  219 GFITG 223
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 14-238 3.47e-14

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: 69.83  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEeklrqvartiADengtqpqwFTLDLLTCTSEEcHQLAQRIAAHFPRL 93
Cdd:cd05328     1 TIVITGAASGIGAATAELLEDAGHTVIGIDLRE----------AD--------VIADLSTPEGRA-AAIADVLARCSGVL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGLLGdicpmseqnPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRAN------------ 161
Cdd:cd05328    62 DGLVNCAGVGG---------TTVAGLVLKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGAGWAQDklelakalaagt 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 162 ---------------WGAYATSKFA-TEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTE--------DPQKLK- 216
Cdd:cd05328   133 earavalaehagqpgYLAYAGSKEAlTVWTRRRAATWLYGAGVRVNTVAPGPVETPILQAFLQDPrggesvdaFVTPMGr 212

                         250       260
                  ....*....|....*....|....
gi 1835908839 217 --TPADIMPLYLWLMGDDSRRKTG 238
Cdd:cd05328   213 raEPDEIAPVIAFLASDAASWING 236
PRK08267 PRK08267
SDR family oxidoreductase;
15-223 4.52e-14

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 69.58  E-value: 4.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQwftLDLlTCTSEECHQLAQRIAAHFPRLD 94
Cdd:PRK08267    4 IFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAWTGA---LDV-TDRAAWDAALADFAAATGGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSdAGSLVF-TSSSVGRQGRANWGAYATSKFATE 173
Cdd:PRK08267   80 VLFNNAGILRG-GPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKAT-PGARVInTSSASAIYGQPGLAVYSATKFAVR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1835908839 174 GMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKT-PADIMP 223
Cdd:PRK08267  158 GLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGSTKRlGVRLTP 208
PRK07069 PRK07069
short chain dehydrogenase; Validated
 16-238 5.56e-14

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 69.35  E-value: 5.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEK-LRQVARTIADENGTQPQW-FTLDLltcTSEECHQ-LAQRIAAHFPR 92
Cdd:PRK07069    3 FITGAAGGLGRAIARRMAEQGAKVFLTDINDAAgLDAFAAEINAAHGEGVAFaAVQDV---TDEAQWQaLLAQAADAMGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:PRK07069   80 LSVLVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 173 EGMMQVLADEYQNRHLRVNC--INPGGTRTGMRASAFPT----EDPQKLK---------TPADIMPLYLWLMGDDSRRKT 237
Cdd:PRK07069  159 ASLTKSIALDCARRGLDVRCnsIHPTFIRTGIVDPIFQRlgeeEATRKLArgvplgrlgEPDDVAHAVLYLASDESRFVT 238


                  .
gi 1835908839 238 G 238
Cdd:PRK07069  239 G 239
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 10-220 8.10e-14

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: 68.49  E-value: 8.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARtiadENGTQPqwfTLDLLTCTSEECHQLAQRIAAH 89
Cdd:cd05370     3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKK----ELPNIH---TIVLDVGDAESVEALAEALLSE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDICPMSEQNPL-VWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05370    76 YPNLDILINNAGIQRPIDLRDPASDLdKADTEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCAT 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPAD 220
Cdd:cd05370   156 KAALHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKMPLD 207
PRK07062 PRK07062
SDR family oxidoreductase;
10-193 8.63e-14

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 68.91  E-value: 8.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtQPQWFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:PRK07062    6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLREKFP-GARLLAARCDVLDEADVAAFAAAVEAR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK07062   85 FGGVDMLVNNAG-QGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAAR 163

                         170       180
                  ....*....|....*....|....
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCI 193
Cdd:PRK07062  164 AGLLNLVKSLATELAPKGVRVNSI 187
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 12-238 9.46e-14

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 68.12  E-value: 9.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEeklrqVARtiADENgtqpqwFTLDLLTCTSEECHQLAQRIAAHFP 91
Cdd:cd05334     1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAE-----NEE--ADAS------IIVLDSDSFTEQAKQVVASVARLSG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLL--GDIcpmSEQNPL-VWQDVMQVNVNATFMLTQALLPLLLKsdAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:cd05334    68 KVDALICVAGGWagGSA---KSKSFVkNWDLMWKQNLWTSFIASHLATKHLLS--GGLLVLTGAKAALEPTPGMIGYGAA 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 169 KFATEGMMQVLADEyqNRHL----RVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMPLYLWLMGDDSRRKTG 238
Cdd:cd05334   143 KAAVHQLTQSLAAE--NSGLpagsTANAILPVTLDTPANRKAMPDADFSSWTPLEFIAELILFWASGAARPKSG 214
PRK06914 PRK06914
SDR family oxidoreductase;
12-200 1.60e-13

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 68.51  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQP-QWFTLDLltcTSEECHQLAQRIAAHF 90
Cdd:PRK06914    3 KKIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEKQENLLSQATQLNLQQNiKVQQLDV---TDQNSIHNFQLVLKEI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAG-----LLGDIcPMSEqnplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY 165
Cdd:PRK06914   80 GRIDLLVNNAGyanggFVEEI-PVEE-----YRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRVGFPGLSPY 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK06914  154 VSSKYALEGFSESLRLELKPFGIDVALIEPGSYNT 188
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
13-246 2.38e-13

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 67.73  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVIL-LGRNE-------EKLRQVARTIADENGTQPQWftldlltctsEECHQLAQ 84
Cdd:PRK12938    4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAgCGPNSprrvkwlEDQKALGFDFIASEGNVGDW----------DSTKAAFD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAAHFPRLDGVLHNAGLLGDIC--PMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANW 162
Cdd:PRK12938   74 KVKAEVGEIDVLVNNAGITRDVVfrKMTRED---WTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQKGQFGQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFP--------TEDPQKLKTPADIMPLYLWLMGDDSR 234
Cdd:PRK12938  151 TNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKAIRPdvlekivaTIPVRRLGSPDEIGSIVAWLASEESG 230

                         250
                  ....*....|..
gi 1835908839 235 RKTGMTFDAQPG 246
Cdd:PRK12938  231 FSTGADFSLNGG 242
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 10-241 2.59e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 67.45  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVArtiADENGTqpqWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK06057    5 LAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAA---DEVGGL---FVPTDV--TDEDAVNALFDTAAET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGllgdICPMSEQNPL-----VWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWG- 163
Cdd:PRK06057   77 YGSVDIAFNNAG----ISPPEDDSILntgldAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQi 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFpTEDPQKLK------------TPADIMPLYLWLMGD 231
Cdd:PRK06057  153 SYTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELF-AKDPERAArrlvhvpmgrfaEPEEIAAAVAFLASD 231

                         250
                  ....*....|
gi 1835908839 232 DSRRKTGMTF 241
Cdd:PRK06057  232 DASFITASTF 241
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 12-200 3.39e-13

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 67.49  E-value: 3.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtQPQWFTLDLLTCTSEECHQLAQRIAAHFP 91
Cdd:cd09807     1 GKTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAEIRRDTL-NHEVIVRHLDLASLKSIRAFAAEFLAEED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLLgdICPMSeqnplVWQD--VMQVNVN--ATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWG---- 163
Cdd:cd09807    80 RLDVLINNAGVM--RCPYS-----KTEDgfEMQFGVNhlGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINFDdlns 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1835908839 164 --------AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:cd09807   153 eksyntgfAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK08416 PRK08416
enoyl-ACP reductase;
10-241 3.57e-13

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 67.10  E-value: 3.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVIL-LGRNEEKLRQVARTIADENGTQPQWFTLDLLTctSEECHQLAQRIAA 88
Cdd:PRK08416    6 MKGKTLVISGGTRGIGKAIVYEFAQSGVNIAFtYNSNVEEANKIAEDLEQKYGIKAKAYPLNILE--PETYKELFKKIDE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNA-----GLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWG 163
Cdd:PRK08416   84 DFDRVDFFISNAiisgrAVVGGYTKFMRLKPKGLNNIYTATVNAFVVGAQEAAKRMEKVGGGSIISLSSTGNLVYIENYA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT-GMRasAFPTEDPQKLKT-----------PADIMPLYLWLMGD 231
Cdd:PRK08416  164 GHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTdALK--AFTNYEEVKAKTeelsplnrmgqPEDLAGACLFLCSE 241

                         250
                  ....*....|
gi 1835908839 232 DSRRKTGMTF 241
Cdd:PRK08416  242 KASWLTGQTI 251
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 10-129 3.71e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 67.69  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtqpqWFTLDLLTCTSEECHQLAQRIAAH 89
Cdd:PRK05872    7 LAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGGDDR----VLTVVADVTDLAAMQAAAEEAVER 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1835908839  90 FPRLDGVLHNAGLL--GdicPMSEQNPLVWQDVMQVNVNATF 129
Cdd:PRK05872   83 FGGIDVVVANAGIAsgG---SVAQVDPDAFRRVIDVNLLGVF 121
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 10-207 5.17e-13

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 66.96  E-value: 5.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVIllgrneeklrqvartIADENGTQPQWFTLDLLTC--TS-EECHQLAQRI 86
Cdd:PRK06171    7 LQGKIIIVTGGSSGIGLAIVKELLANGANVV---------------NADIHGGDGQHENYQFVPTdvSSaEEVNHTVAEI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAG-----LLGDI---CPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQG 158
Cdd:PRK06171   72 IEKFGRIDGLVNNAGiniprLLVDEkdpAGKYELNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAGLEG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835908839 159 RANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPG-GTRTGMRASAF 207
Cdd:PRK06171  152 SEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGiLEATGLRTPEY 201
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
9-222 5.25e-13

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 66.67  E-value: 5.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGA-TVILLGRNEEKLRQVARTIaDENGTQPQWFTLDLLTCtsEECHQLAQRIA 87
Cdd:PRK08063    1 VFSGKVALVTGSSRGIGKAIALRLAEEGYdIAVNYARSRKAAEETAEEI-EALGRKALAVKANVGDV--EKIKEMFAQID 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNA--GLLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVfTSSSVGrQGRA--NWG 163
Cdd:PRK08063   78 EEFGRLDVFVNNAasGVLRPAMELEESH---WDWTMNINAKALLFCAQEAAKLMEKVGGGKII-SLSSLG-SIRYleNYT 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPT-----EDPQKlKTPADIM 222
Cdd:PRK08063  153 TVGVSKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDA-LKHFPNreellEDARA-KTPAGRM 214
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
10-196 1.20e-12

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 65.70  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNE--EKLRQVARTiadenGTQPQWFTLDLLTctSEECHQLAQRIA 87
Cdd:PRK12481    6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAEapETQAQVEAL-----GRKFHFITADLIQ--QKDIDSIVSQAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGLL--GDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKS-DAGSLVFTSSSVGRQGRANWGA 164
Cdd:PRK12481   79 EVMGHIDILINNAGIIrrQDLLEFGNKD---WDDVININQKTVFFLSQAVAKQFVKQgNGGKIINIASMLSFQGGIRVPS 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPG 196
Cdd:PRK12481  156 YTASKSAVMGLTRALATELSQYNINVNAIAPG 187
PRK06949 PRK06949
SDR family oxidoreductase;
10-246 1.83e-12

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 65.17  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpQWFTLDLLTctseecHQLAQRIAAH 89
Cdd:PRK06949    7 LEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLKELRAEIEAEGGAA-HVVSLDVTD------YQSIKAAVAH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPR----LDGVLHNAGL-----LGDICPMSeqnplvWQDVMQVNVNATF---------MLTQALLPLLLKSdAGSLVFTS 151
Cdd:PRK06949   80 AETeagtIDILVNNSGVsttqkLVDVTPAD------FDFVFDTNTRGAFfvaqevakrMIARAKGAGNTKP-GGRIINIA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 152 SSVGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKT---------PADIM 222
Cdd:PRK06949  153 SVAGLRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQGQKLVSmlprkrvgkPEDLD 232

                         250       260
                  ....*....|....*....|....
gi 1835908839 223 PLYLWLMGDDSRRKTGMTFDAQPG 246
Cdd:PRK06949  233 GLLLLLAADESQFINGAIISADDG 256
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 16-196 2.12e-12

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: 63.66  E-value: 2.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   16 LVTGASDGIGREATQTYARYGA-TVILLGRNEEKLRQVARTIAD--ENGTQPQWFTLDLltCTSEECHQLAQRIAAHFPR 92
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGArRLVLLSRSGPDAPGAAALLAEleAAGARVTVVACDV--ADRDALAAVLAAIPAVEGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   93 LDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLllksDAGSLVFTSSSVGRQGRANWGAYAtskfAT 172
Cdd:smart00822  82 LTGVIHAAGVLDD-GVLASLTPERFAAVLAPKAAGAWNLHELTADL----PLDFFVLFSSIAGVLGSPGQANYA----AA 152

                          170       180
                   ....*....|....*....|....
gi 1835908839  173 EGMMQVLADEYQNRHLRVNCINPG 196
Cdd:smart00822 153 NAFLDALAEYRRARGLPALSIAWG 176
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 14-206 2.16e-12

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: 64.93  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARY----GATVILLGRNEEKLRQVARTI-ADENGTQPQWFTLDLltcTSEECHQLAQRIAA 88
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKClkspGSVLVLSARNDEALRQLKAEIgAERSGLRVVRVSLDL---GAEAGLEQLLKALR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDG-----VLHNAGLLGDICPMSEQnplvWQDVMQVN----VNATFML-TQALLPLLLKSDAGS---LVFTSSSVG 155
Cdd:TIGR01500  79 ELPRPKGlqrllLINNAGTLGDVSKGFVD----LSDSTQVQnywaLNLTSMLcLTSSVLKAFKDSPGLnrtVVNISSLCA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1835908839 156 RQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASA 206
Cdd:TIGR01500 155 IQPFKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDMQQQV 205
PRK08278 PRK08278
SDR family oxidoreductase;
10-241 2.87e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 64.92  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEE---KLR----QVARTIaDENGTQPQWFTLDLltcTSEEchQL 82
Cdd:PRK08278    4 LSGKTLFITGASRGIGLAIALRAARDGANIVIAAKTAEphpKLPgtihTAAEEI-EAAGGQALPLVGDV---RDED--QV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  83 AQRIAA---HFPRLDGVLHNAG---LLGdicpmSEQNPLVWQDVM-QVNVNATFMLTQALLPLLLKSDAGSLVFTSS--S 153
Cdd:PRK08278   78 AAAVAKaveRFGGIDICVNNASainLTG-----TEDTPMKRFDLMqQINVRGTFLVSQACLPHLKKSENPHILTLSPplN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 154 VGRQGRANWGAYATSKFateGM-MQVL--ADEYQNRHLRVNCINPggtRTGMRASA---FP--TEDPQKLKTPaDIMP-L 224
Cdd:PRK08278  153 LDPKWFAPHTAYTMAKY---GMsLCTLglAEEFRDDGIAVNALWP---RTTIATAAvrnLLggDEAMRRSRTP-EIMAdA 225

                         250
                  ....*....|....*..
gi 1835908839 225 YLWLMGDDSRRKTGMTF 241
Cdd:PRK08278  226 AYEILSRPAREFTGNFL 242
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 10-223 3.27e-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: 64.39  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEE-KLRQVARTIADENGTQPQwftldlLTCTS---EECHQLAQR 85
Cdd:cd09763     1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTILpQLPGTAEEIEARGGKCIP------VRCDHsddDEVEALFER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  86 IAAHFP-RLDGVLHNA------GLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQG 158
Cdd:cd09763    75 VAREQQgRLDILVNNAyaavqlILVGVAKPFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAGKGLIVIISSTGGLEY 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835908839 159 RANWgAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLKTPADIMP 223
Cdd:cd09763   155 LFNV-AYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHAKERDAFL 218
PRK05717 PRK05717
SDR family oxidoreductase;
12-241 3.47e-12

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 64.53  E-value: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEngtqpQWF-TLDLltcTSEEchQLAQRIA--- 87
Cdd:PRK05717   10 GRVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGEN-----AWFiAMDV---ADEA--QVAAGVAevl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGLLGDICPMSEQNPLV-WQDVMQVNVNATfMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK05717   80 GQFGRLDALVCNAAIADPHNTTLESLSLAhWNRVLAVNLTGP-MLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 167 TSKFATEGMMQVLADEYqNRHLRVNCINPG--GTRTGMRASAFPTEDPQKLKTPA-------DIMPLYLWLMGDDSRRKT 237
Cdd:PRK05717  159 ASKGGLLALTHALAISL-GPEIRVNAVSPGwiDARDPSQRRAEPLSEADHAQHPAgrvgtveDVAAMVAWLLSRQAGFVT 237


                  ....
gi 1835908839 238 GMTF 241
Cdd:PRK05717  238 GQEF 241
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 10-196 5.17e-12

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 64.15  E-value: 5.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:PRK08277    8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIK-AAGGEALAVKADVLDKESLE--QARQQILED 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG---------LLGDICPMSEQN-----PLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVG 155
Cdd:PRK08277   85 FGPCDILINGAGgnhpkattdNEFHELIEPTKTffdldEEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMNA 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1835908839 156 RQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPG 196
Cdd:PRK08277  165 FTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPG 205
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 92-206 5.62e-12

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: 62.53  E-value: 5.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:cd02266    31 RRDVVVHNAAI-LDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAA 109

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1835908839 172 TEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASA 206
Cdd:cd02266   110 LDGLAQQWASEGWGNGLPATAVACGTWAGSGMAKG 144
PRK07831 PRK07831
SDR family oxidoreductase;
3-195 5.96e-12

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 63.90  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   3 YQPKQDLLQGRIILVTGASD-GIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPqwftLDLLTC--TSEEC 79
Cdd:PRK07831    8 YVPGHGLLAGKVVLVTAAAGtGIGSATARRALEEGARVVISDIHERRLGETADELAAELGLGR----VEAVVCdvTSEAQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  80 HQ-LAQRIAAHFPRLDGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSV-GRQ 157
Cdd:PRK07831   84 VDaLIDAAVERLGRLDVLVNNAGLGGQ-TPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVNNASVlGWR 162

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1835908839 158 GRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINP 195
Cdd:PRK07831  163 AQHGQAHYAAAKAGVMALTRCSALEAAEYGVRINAVAP 200
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 13-204 6.83e-12

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 63.44  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKlrQVARTIAD--ENGTQPQWFTLDLltCTSEECHQLAQRIAAHF 90
Cdd:PRK12745    3 PVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDE--ELAATQQElrALGVEVIFFPADV--ADLSAHEAMLDAAQAAW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGL----LGDICPMSEQNplvWQDVMQVNVNATFMLTQA------LLPLLLKSDAGSLVFTSSSVGRQGRA 160
Cdd:PRK12745   79 GRIDCLVNNAGVgvkvRGDLLDLTPES---FDRVLAINLRGPFFLTQAvakrmlAQPEPEELPHRSIVFVSSVNAIMVSP 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1835908839 161 NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRA 204
Cdd:PRK12745  156 NRGEYCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMTA 199
PRK12742 PRK12742
SDR family oxidoreductase;
10-238 8.65e-12

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 62.85  E-value: 8.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEeklRQVARTIADENGTQPqwFTLDlltctSEECHQLAQRIAAh 89
Cdd:PRK12742    4 FTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGS---KDAAERLAQETGATA--VQTD-----SADRDAVIDVVRK- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG--LLGDicPMsEQNPLVWQDVMQVNVNATFMltQALLPLLLKSDAGSLVFTSSSVG-RQGRANWGAYA 166
Cdd:PRK12742   73 SGALDILVVNAGiaVFGD--AL-ELDADDIDRLFKINIHAPYH--ASVEAARQMPEGGRIIIIGSVNGdRMPVAGMAAYA 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835908839 167 TSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTED----PQKLK---TPADIMPLYLWLMGDDSRRKTG 238
Cdd:PRK12742  148 ASKSALQGMARGLARDFGPRGITINVVQPGPIDTDANPANGPMKDmmhsFMAIKrhgRPEEVAGMVAWLAGPEASFVTG 226
PRK08628 PRK08628
SDR family oxidoreductase;
8-224 8.91e-12

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 63.05  E-value: 8.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   8 DL-LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdeNGTQPQWFTLDLltCTSEECHQLAQRI 86
Cdd:PRK08628    2 DLnLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSAPDDEFAEELRA--LQPRAEFVQVDL--TDDAQCRDAVEQT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGL---LGdicpmSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWG 163
Cdd:PRK08628   78 VAKFGRIDGLVNNAGVndgVG-----LEAGREAFVASLERNLIHYYVMAHYCLPHLKASR-GAIVNISSKTALTGQGGTS 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPT-EDPQ-KLKTPADIMPL 224
Cdd:PRK08628  152 GYAAAKGAQLALTREWAVALAKDGVRVNAVIPAEVMTPLYENWIATfDDPEaKLAAITAKIPL 214
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 10-174 1.37e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 63.40  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLLtcTSEECHQLAQRIAAH 89
Cdd:PRK07109    6 IGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAAEIRAA-GGEALAVVADVA--DAEAVQAAADRAEEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK07109   83 LGPIDTWVNNAM-VTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAYRSIPLQSAYCAAK 161


                  ....*
gi 1835908839 170 FATEG 174
Cdd:PRK07109  162 HAIRG 166
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 13-219 1.54e-11

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 62.48  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIG--------REATQTYARYgATVILLGRnEEKLRQVARTIADENGTqpqwfTLDLLTCTSEECHQLAQ 84
Cdd:cd09806     1 TVVLITGCSSGIGlhlavrlaSDPSKRFKVY-ATMRDLKK-KGRLWEAAGALAGGTLE-----TLQLDVCDSKSVAAAVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAAHfpRLDGVLHNAGLlGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGA 164
Cdd:cd09806    74 RVTER--HVDVLVCNAGV-GLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGGLQGLPFNDV 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFptEDPQKLKTPA 219
Cdd:cd09806   151 YCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHTAFMEKVL--GSPEEVLDRT 203
PRK07024 PRK07024
SDR family oxidoreductase;
14-202 1.66e-11

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 62.25  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdeNGTQPQWFTLDLltCTSEECHQLAQRIAAHFPRL 93
Cdd:PRK07024    4 KVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLP--KAARVSVYAADV--RDADALAAAAADFIAAHGLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGL-LGDICPMSEQNPlVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:PRK07024   80 DVVIANAGIsVGTLTEEREDLA-VFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAA 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1835908839 173 EGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:PRK07024  159 IKYLESLRVELRPAGVRVVTIAPGYIRTPM 188
PRK07775 PRK07775
SDR family oxidoreductase;
13-202 2.11e-11

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 62.46  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltcTSEECHQ--LAQRIAAHF 90
Cdd:PRK07775   11 RPALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIR-ADGGEAVAFPLDV---TDPDSVKsfVAQAEEALG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PrLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKF 170
Cdd:PRK07775   87 E-IEVLVSGAGDT-YFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALRQRPHMGAYGAAKA 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1835908839 171 ATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:PRK07775  165 GLEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 10-221 2.99e-11

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 61.88  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENG-----TQPQWFTlDLLTctseechqlaq 84
Cdd:PRK07825    3 LRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELGLVVGgpldvTDPASFA-AFLD----------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAAHFPRLDGVLHNAGL--LGdicPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANW 162
Cdd:PRK07825   71 AVEADLGPIDVLVNNAGVmpVG---PFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKIPVPGM 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPTEDPQKLKTPADI 221
Cdd:PRK07825  148 ATYCASKHAVVGFTDAARLELRGTGVHVSVVLPSFVNTEL-IAGTGGAKGFKNVEPEDV 205
PRK08017 PRK08017
SDR family oxidoreductase;
13-200 3.09e-11

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 61.64  E-value: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEklrQVARTiaDENGTQPqwFTLDLLTCTSEEcHQLAQRIAAHFPR 92
Cdd:PRK08017    3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPD---DVARM--NSLGFTG--ILLDLDDPESVE-RAADEVIALTDNR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAG--LLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKF 170
Cdd:PRK08017   75 LYGLFNNAGfgVYGPLSTISRQQ---MEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAASKY 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1835908839 171 ATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK08017  152 ALEAWSDALRMELRHSGIKVSLIEPGPIRT 181
PRK07102 PRK07102
SDR family oxidoreductase;
15-221 3.12e-11

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 61.48  E-value: 3.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTCTS-----EECHqlaqriaah 89
Cdd:PRK07102    4 ILIIGATSDIARACARRYAAAGARLYLAARDVERLERLADDLRARGAVAVSTHELDILDTAShaaflDSLP--------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 fPRLDGVLHNAGLLGD--ICpmsEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK07102   75 -ALPDIVLIAVGTLGDqaAC---EADPALALREFRTNFEGPIALLTLLANRFEARGSGTIVGISSVAGDRGRASNYVYGS 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRAsAFPTedPQKL-KTPADI 221
Cdd:PRK07102  151 AKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTA-GLKL--PGPLtAQPEEV 202
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 8-195 4.30e-11

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 61.51  E-value: 4.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   8 DLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVArtiadeNGTQPQWFTLDLLTCTS---EECHQLAQ 84
Cdd:PRK05876    2 DGFPGRGAVITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAV------NHLRAEGFDVHGVMCDVrhrEEVTHLAD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAAHFPRLDGVLHNAGLL--GDICPMSEQNplvWQDVMQVNVNATFMLTQA-LLPLLLKSDAGSLVFTSSSVGRQGRAN 161
Cdd:PRK05876   76 EAFRLLGHVDVVFSNAGIVvgGPIVEMTHDD---WRWVIDVDLWGSIHTVEAfLPRLLEQGTGGHVVFTASFAGLVPNAG 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINP 195
Cdd:PRK05876  153 LGAYGVAKYGVVGLAETLAREVTADGIGVSVLCP 186
PRK06196 PRK06196
oxidoreductase; Provisional
 10-202 5.03e-11

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 61.62  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIadeNGTqpQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:PRK06196   24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI---DGV--EVVMLDLADLESVR--AFAERFLDS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGdiCPMSEQNPlVWQdvMQVNVN--ATFMLTQaLLPLLLKSDAGSLVFTSSSVG------------ 155
Cdd:PRK06196   97 GRRIDILINNAGVMA--CPETRVGD-GWE--AQFATNhlGHFALVN-LLWPALAAGAGARVVALSSAGhrrspirwddph 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1835908839 156 -RQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:PRK06196  171 fTRGYDKWLAYGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPL 218
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 12-196 5.98e-11

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 60.82  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGT-QPQWFTLDLltCTSEECHQLAQRIAAHF 90
Cdd:PRK12384    2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANVAQEINAEYGEgMAYGFGADA--TSEQSVLALSRGVDEIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGLLgDICPMSEQNPLVWQDVMQVNVNATFMLT-QALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK12384   80 GRVDLLVYNAGIA-KAAFITDFQLGDFDRSLQVNLVGYFLCArEFSRLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAK 158

                         170       180
                  ....*....|....*....|....*..
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPG 196
Cdd:PRK12384  159 FGGVGLTQSLALDLAEYGITVHSLMLG 185
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 12-241 6.42e-11

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 60.67  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIadenGTQPQWFTLDLLTCTSEEchQLAQRIAAHFP 91
Cdd:cd09761     1 GKVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAE----GPNLFFVHGDVADETLVK--FVVYAMLEKLG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQGRANWGAYATSKFA 171
Cdd:cd09761    75 RIDVLVNNAA-RGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIASTRAFQSEPDSEAYAASKGG 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835908839 172 TEGMMQVLADEYqNRHLRVNCINPG--GTRTGMRASAFPTEDPQ-------KLKTPADIMPLYLWLMGDDSRRKTGMTF 241
Cdd:cd09761   153 LVALTHALAMSL-GPDIRVNCISPGwiNTTEQQEFTAAPLTQEDhaqhpagRVGTPKDIANLVLFLCQQDAGFITGETF 230
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 16-221 8.62e-11

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: 59.84  E-value: 8.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADengtqpqwftldlLTCTSEECHQLAQRIAAH-FPRLD 94
Cdd:cd11730     2 LILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGA-------------LARPADVAAELEVWALAQeLGPLD 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAG-LLGDicPMSEQNPLVWQDVMQVNV-NATFMLTQAllpLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:cd11730    69 LLVYAAGaILGK--PLARTKPAAWRRILDANLtGAALVLKHA---LALLAAGARLVFLGAYPELVMLPGLSAYAAAKAAL 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1835908839 173 EGMMQVLADEYQNRHLRVncINPGGTRTGMRASafPTEDPQKLKTPADI 221
Cdd:cd11730   144 EAYVEVARKEVRGLRLTL--VRPPAVDTGLWAP--PGRLPKGALSPEDV 188
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 10-200 8.75e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 60.30  E-value: 8.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILlgrneeklrqVARTIADENGTQPQWFTLDLLtcTSEECHQLAQRIAAH 89
Cdd:PRK06523    7 LAGKRALVTGGTKGIGAATVARLLEAGARVVT----------TARSRPDDLPEGVEFVAADLT--TAEGCAAVARAVLER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG----LLGDICPMSEQnplVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSvgrQGR----AN 161
Cdd:PRK06523   75 LGGVDILVHVLGgssaPAGGFAALTDE---EWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSI---QRRlplpES 148

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK06523  149 TTAYAAAKAALSTYSKSLSKEVAPKGVRVNTVSPGWIET 187
PRK08264 PRK08264
SDR family oxidoreductase;
10-221 9.02e-11

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 59.90  E-value: 9.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGRE-ATQTYARyGATVILLGrneekLRQVARTIADENGTQPqwFTLDLLTCTSeechqlAQRIAA 88
Cdd:PRK08264    4 IKGKVVLVTGANRGIGRAfVEQLLAR-GAAKVYAA-----ARDPESVTDLGPRVVP--LQLDVTDPAS------VAAAAE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATS 168
Cdd:PRK08264   70 AASDVTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNFPNLGTYSAS 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835908839 169 KFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrASAFPTEDPqklkTPADI 221
Cdd:PRK08264  150 KAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM-AAGLDAPKA----SPADV 197
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 11-196 9.92e-11

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: 60.17  E-value: 9.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltcTSE-ECHQLAQRIAAH 89
Cdd:cd05322     1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEYGEKAYGFGADA---TNEqSVIALSKGVDEI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGL----------LGDicpmseqnplvWQDVMQVNVNATFMLT-QALLPLLLKSDAGSLVFTSSSVGRQG 158
Cdd:cd05322    78 FKRVDLLVYSAGIaksakitdfeLGD-----------FDRSLQVNLVGYFLCArEFSKLMIRDGIQGRIIQINSKSGKVG 146

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1835908839 159 RANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPG 196
Cdd:cd05322   147 SKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLG 184
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 12-206 1.24e-10

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 60.84  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYAR-YGATVILLGR-----NEEKLRQVARTIAdENGTQPQWFTLDLltCTSEECHQLAQR 85
Cdd:cd08953   205 GGVYLVTGGAGGIGRALARALARrYGARLVLLGRsplppEEEWKAQTLAALE-ALGARVLYISADV--TDAAAVRRLLEK 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  86 IAAHFPRLDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKsdagSLVFTSSSVGRQGRANWG 163
Cdd:cd08953   282 VRERYGAIDGVIHAAGVLRDalLAQKTAED---FEAVLAPKVDGLLNLAQALADEPLD----FFVLFSSVSAFFGGAGQA 354

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1835908839 164 AYAtskfATEGMMQVLADEYQNRHL--RVNCIN-PGGTRTGMRASA 206
Cdd:cd08953   355 DYA----AANAFLDAFAAYLRQRGPqgRVLSINwPAWREGGMAADL 396
PRK07023 PRK07023
SDR family oxidoreductase;
16-220 1.31e-10

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 59.64  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEKlrqvarTIADENGTQPQWFTLDLlTCTSEECHQLAQRIAAHFPR-LD 94
Cdd:PRK07023    5 IVTGHSRGLGAALAEQLLQPGIAVLGVARSRHP------SLAAAAGERLAEVELDL-SDAAAAAAWLAGDLLAAFVDgAS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVL--HNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:PRK07023   78 RVLliNNAGTVEPIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 173 EGMMQVLADEyQNRHLRVNCINPGGTRTGMRA-------SAFPT-------EDPQKLKTPAD 220
Cdd:PRK07023  158 DHHARAVALD-ANRALRIVSLAPGVVDTGMQAtiratdeERFPMrerfrelKASGALSTPED 218
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
 16-206 1.44e-10

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: 60.48  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGAT-VILLGRNEEKLRQVARTIADE-NGTQPQWFTLDLltCTSEECHQLAQRIAAHFPrL 93
Cdd:cd05274   154 LITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARAALLRaGGARVSVVRCDV--TDPAALAALLAELAAGGP-L 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGLLGDiCPMSEQNPLVWQDVMQVNVNATFMLTQAllplLLKSDAGSLVFTSSSVGRQGRANWGAYAtskfATE 173
Cdd:cd05274   231 AGVIHAAGVLRD-ALLAELTPAAFAAVLAAKVAGALNLHEL----TPDLPLDFFVLFSSVAALLGGAGQAAYA----AAN 301

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835908839 174 GMMQVLADEYQNRHLRVNCINPGGTRTGMRASA 206
Cdd:cd05274   302 AFLDALAAQRRRRGLPATSVQWGAWAGGGMAAA 334
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-207 2.08e-10

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 59.80  E-value: 2.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILlgrNEEKLRQVARTIADE-----------NGTQPQWFTLDLLTctsee 78
Cdd:PRK07792   10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVV---NDVASALDASDVLDEiraagakavavAGDISQRATADELV----- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  79 chqlaqRIAAHFPRLDGVLHNAGLLGD--ICPMSEQNplvWQDVMQVNVNATFMLTQ-ALLPLLLKSDA------GSLVF 149
Cdd:PRK07792   82 ------ATAVGLGGLDIVVNNAGITRDrmLFNMSDEE---WDAVIAVHLRGHFLLTRnAAAYWRAKAKAaggpvyGRIVN 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835908839 150 TSSSVGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGtRTGMRASAF 207
Cdd:PRK07792  153 TSSEAGLVGPVGQANYGAAKAGITALTLSAARALGRYGVRANAICPRA-RTAMTADVF 209
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
15-198 2.80e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 59.22  E-value: 2.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEngtqpqWFTLDLLTctseechqlAQRIAAHFPRLD 94
Cdd:COG0451     2 ILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVE------FVRGDLRD---------PEALAAALAGVD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLLGDicpmSEQNPlvwQDVMQVNVNATFMLTQAllplLLKSDAGSLVFTSSS--VGRQGR--------ANWGA 164
Cdd:COG0451    67 AVVHLAAPAGV----GEEDP---DETLEVNVEGTLNLLEA----ARAAGVKRFVYASSSsvYGDGEGpidedtplRPVSP 135

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1835908839 165 YATSKFATEGMMQVLADEYQnrhLRVNCINPGGT 198
Cdd:COG0451   136 YGASKLAAELLARAYARRYG---LPVTILRPGNV 166
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 11-212 2.98e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 59.15  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKlrqvartiadenGTQPQWFTLDLLTCTSEE-CHQLAQRIAAH 89
Cdd:PRK06179    3 NSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPAR------------AAPIPGVELLELDVTDDAsVQAAVDEVIAR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK06179   71 AGRIDVLVNNAG-VGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFLPAPYMALYAASK 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1835908839 170 FATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDP 212
Cdd:PRK06179  150 HAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPDSP 192
PRK05855 PRK05855
SDR family oxidoreductase;
12-213 3.02e-10

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 59.99  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQRIAAHFP 91
Cdd:PRK05855  315 GKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAERTAELIRAA-GAVAHAYRVDV--SDADAMEAFAEWVRAEHG 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAG--LLGDICPMSEQNplvWQDVMQVNVN---------ATFMLTQALlplllksdAGSLVFTSSSVGRQGRA 160
Cdd:PRK05855  392 VPDIVVNNAGigMAGGFLDTSAED---WDRVLDVNLWgvihgcrlfGRQMVERGT--------GGHIVNVASAAAYAPSR 460

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 161 NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTG-MRASAFPTEDPQ 213
Cdd:PRK05855  461 SLPAYATSKAAVLMLSECLRAELAAAGIGVTAICPGFVDTNiVATTRFAGADAE 514
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-241 3.28e-10

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 58.58  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRN-----EEKLRQVartiaDENGTQPQWFTLDLltCTSEECHQLAQ 84
Cdd:PRK06077    4 LKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKraeemNETLKMV-----KENGGEGIGVLADV--STREGCETLAK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 RIAAHFPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLlkSDAGSLVFTSSSVGRQGRANWGA 164
Cdd:PRK06077   77 ATIDRYGVADILVNNAG-LGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM--REGGAIVNIASVAGIRPAYGLSI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 165 YATSKFATEGMMQVLADEYQNRhLRVNCINPGGTRTGMRASAFP----TEDP--------QKLKTPADIMPLYLWLMGDD 232
Cdd:PRK06077  154 YGAMKAAVINLTKYLALELAPK-IRVNAIAPGFVKTKLGESLFKvlgmSEKEfaekftlmGKILDPEEVAEFVAAILKIE 232


                  ....*....
gi 1835908839 233 SrrKTGMTF 241
Cdd:PRK06077  233 S--ITGQVF 239
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 9-246 4.48e-10

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 58.16  E-value: 4.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATV-ILLGRNEEKLRQVARTIaDENGTQPQWFTLDLLTCTSEEC------HQ 81
Cdd:PRK12747    1 MLKGKVALVTGASRGIGRAIAKRLANDGALVaIHYGNRKEEAEETVYEI-QSNGGSAFSIGANLESLHGVEAlyssldNE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  82 LAQRIAAhfPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLlkSDAGSLVFTSSSVGRQGRAN 161
Cdd:PRK12747   80 LQNRTGS--TKFDILINNAG-IGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL--RDNSRIINISSAATRISLPD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFptEDP------------QKLKTPADIMPLYLWLM 229
Cdd:PRK12747  155 FIAYSMTKGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAELL--SDPmmkqyattisafNRLGEVEDIADTAAFLA 232

                         250
                  ....*....|....*..
gi 1835908839 230 GDDSRRKTGMTFDAQPG 246
Cdd:PRK12747  233 SPDSRWVTGQLIDVSGG 249
PRK05866 PRK05866
SDR family oxidoreductase;
10-211 4.59e-10

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 58.60  E-value: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQ---PQWFTlDLltctsEECHQLAQRI 86
Cdd:PRK05866   38 LTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVADRITRAGGDAmavPCDLS-DL-----DAVDALVADV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAGllgdicpMSEQNPLV-----WQDV---MQVNVNATFMLTQALLPLLLKSDAGSLVFTSS-SVGRQ 157
Cdd:PRK05866  112 EKRIGGVDILINNAG-------RSIRRPLAesldrWHDVertMVLNYYAPLRLIRGLAPGMLERGDGHIINVATwGVLSE 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 158 GRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRAsafPTED 211
Cdd:PRK05866  185 ASPLFSVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIA---PTKA 235
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 16-194 9.18e-10

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: 56.42  E-value: 9.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGA-TVILLGRNEEKLRQVARTIAD--ENGTQpqwftLDLLTCTSEECHQLAQRIA---AH 89
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGArHLVLLSRSAAPRPDAQALIAEleARGVE-----VVVVACDVSDPDAVAALLAeikAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLLGDIcPMSEQNPLVWQDVMQVNVNATFMLTQAllplLLKSDAGSLVFTSSSVGRQGRANWGAYAtsk 169
Cdd:pfam08659  79 GPPIRGVIHAAGVLRDA-LLENMTDEDWRRVLAPKVTGTWNLHEA----TPDEPLDFFVLFSSIAGLLGSPGQANYA--- 150

                         170       180
                  ....*....|....*....|....*
gi 1835908839 170 fATEGMMQVLADEYQNRHLRVNCIN 194
Cdd:pfam08659 151 -AANAFLDALAEYRRSQGLPATSIN 174
PRK06182 PRK06182
short chain dehydrogenase; Validated
 11-201 9.54e-10

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 57.66  E-value: 9.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVArtiadENGTQPqwFTLDLltcTSEE-CHQLAQRIAAH 89
Cdd:PRK06182    2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLA-----SLGVHP--LSLDV---TDEAsIKAAVDTIIAE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG--LLGDI--CPMSEQnplvwQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGR--QGRANWg 163
Cdd:PRK06182   72 EGRIDVLVNNAGygSYGAIedVPIDEA-----RRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKiyTPLGAW- 145

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1835908839 164 aYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTG 201
Cdd:PRK06182  146 -YHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIKTE 182
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 15-196 9.94e-10

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 57.25  E-value: 9.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNE----EKLRQVARTI--ADengtqpqwFTldlltcTSEECHQLAQRIAA 88
Cdd:PRK06483    5 ILITGAGQRIGLALAWHLLAQGQPVIVSYRTHypaiDGLRQAGAQCiqAD--------FS------TNAGIMAFIDELKQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 HFPRLDGVLHNAGL-LGDICPMSEQNplVWQDVMQVNVNATFMLTQALLPLLLKSD--AGSLVFTSSSVGRQGRANWGAY 165
Cdd:PRK06483   71 HTDGLRAIIHNASDwLAEKPGAPLAD--VLARMMQIHVNAPYLLNLALEDLLRGHGhaASDIIHITDYVVEKGSDKHIAY 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1835908839 166 ATSKFATEGMMQVLADEYQNrHLRVNCINPG 196
Cdd:PRK06483  149 AASKAALDNMTLSFAAKLAP-EVKVNSIAPA 178
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-238 1.22e-09

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 57.02  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILlgrNEEKLRQVARTIADENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK08642    3 ISEQTVLVTGGSRGLGAAIARAFAREGARVVV---NYHQSEDAAEALADELGDRAIALQADV--TDREQVQAMFATATEH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPR-LDGVLHNAglLGDIC--PMSEQNP--LVWQDVMQV---NVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRAN 161
Cdd:PRK08642   78 FGKpITTVVNNA--LADFSfdGDARKKAddITWEDFQQQlegSVKGALNTIQAALPGMREQGFGRIINIGTNLFQNPVVP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTE--------DP-QKLKTPADIMPLYLWLMGDD 232
Cdd:PRK08642  156 YHDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRTTDASAATPDEvfdliaatTPlRKVTTPQEFADAVLFFASPW 235


                  ....*.
gi 1835908839 233 SRRKTG 238
Cdd:PRK08642  236 ARAVTG 241
PRK06139 PRK06139
SDR family oxidoreductase;
10-208 1.38e-09

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 57.42  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:PRK06139    5 LHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRAL-GAEVLVVPTDV--TDADQVKALATQAASF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGL--LGDIcpmsEQNPL-VWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYA 166
Cdd:PRK06139   82 GGRIDVWVNNVGVgaVGRF----EETPIeAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFAAQPYAAAYS 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835908839 167 TSKFATEGMMQVLADEYQN-RHLRVNCINP----------GGTRTGMRASAFP 208
Cdd:PRK06139  158 ASKFGLRGFSEALRGELADhPDIHVCDVYPafmdtpgfrhGANYTGRRLTPPP 210
PRK09186 PRK09186
flagellin modification protein A; Provisional
 9-238 2.23e-09

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 56.15  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQP-QWFTLDLltCTSEECHQLAQRIA 87
Cdd:PRK09186    1 MLKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGKEFKSKKlSLVELDI--TDQESLEEFLSKSA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAgllgdiCPMSEQNPLVWQDV----MQVNVN----ATFMLTQALLPLLLKSDAGSLVFTSSSVG---- 155
Cdd:PRK09186   79 EKYGKIDGAVNCA------YPRNKDYGKKFFDVslddFNENLSlhlgSSFLFSQQFAKYFKKQGGGNLVNISSIYGvvap 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 156 ----RQGRANWGA--YATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMrasafPTEDPQKLKT---------PAD 220
Cdd:PRK09186  153 kfeiYEGTSMTSPveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQ-----PEAFLNAYKKccngkgmldPDD 227

                         250
                  ....*....|....*...
gi 1835908839 221 IMPLYLWLMGDDSRRKTG 238
Cdd:PRK09186  228 ICGTLVFLLSDQSKYITG 245
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 14-228 2.48e-09

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 55.92  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLrqvaRTIADENGTQPQWFTLDLLTCTSEEchQLAQRIAAHFPRL 93
Cdd:PRK10538    2 IVLVTGATAGFGECITRRFIQQGHKVIATGRRQERL----QELKDELGDNLYIAQLDVRNRAAIE--EMLASLPAEWRNI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAY-ATSKFAT 172
Cdd:PRK10538   76 DVLVNNAGLALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYgATKAFVR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835908839 173 EGMMQVLADeYQNRHLRVNCINPG---GTR------TGMRASAFPTEDPQKLKTPADIMPLYLWL 228
Cdd:PRK10538  156 QFSLNLRTD-LHGTAVRVTDIEPGlvgGTEfsnvrfKGDDGKAEKTYQNTVALTPEDVSEAVWWV 219
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 10-203 2.60e-09

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: 56.00  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNeEKLRQVARTIAdENGTQPQWFTLDLltctseECHQLAQRIAAH 89
Cdd:cd08937     2 FEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRS-ELVHEVLAEIL-AAGDAAHVHTADL------ETYAGAQGVVRA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 ----FPRLDGVLHNAGllGDIC--PMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGraNWG 163
Cdd:cd08937    74 averFGRVDVLINNVG--GTIWakPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGI--YRI 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMR 203
Cdd:cd08937   150 PYSAAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAPPR 189
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 10-238 4.50e-09

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 55.56  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGAS--DGIGREATQTYARYGATV-----------ILLGRNEEKLRQVARTIaDENGTQPQWFTLDLltcTS 76
Cdd:PRK12859    4 LKNKVAVVTGVSrlDGIGAAICKELAEAGADIfftywtaydkeMPWGVDQDEQIQLQEEL-LKNGVKVSSMELDL---TQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  77 EEC-HQLAQRIAAHFPRLDGVLHNAGllgdicpMSEQNPLVWQDVMQ------VNVNATFMLTQALLPLLLKSDAGSLVF 149
Cdd:PRK12859   80 NDApKELLNKVTEQLGYPHILVNNAA-------YSTNNDFSNLTAEEldkhymVNVRATTLLSSQFARGFDKKSGGRIIN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 150 TSSSVGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTG-----MRASAFPTEDPQKLKTPADIMPL 224
Cdd:PRK12859  153 MTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGwmteeIKQGLLPMFPFGRIGEPKDAARL 232

                         250
                  ....*....|....
gi 1835908839 225 YLWLMGDDSRRKTG 238
Cdd:PRK12859  233 IKFLASEEAEWITG 246
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
 12-238 5.63e-09

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


Pssm-ID: 275297 [Multi-domain]  Cd Length: 259  Bit Score: 55.02  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRneeklrqvartIADENGTQPQWFTLDLLTCTSEECHQLAQRIAA--- 88
Cdd:TIGR04504   1 GRVALVTGAARGIGAATVRRLAADGWRVVAVDL-----------CADDPAVGYPLATRAELDAVAAACPDQVLPVIAdvr 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 --------------HFPRLDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDA---GSLVFTS 151
Cdd:TIGR04504  70 dpaalaaavalaveRWGRLDAAVAAAGVIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARPDprgGRFVAVA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 152 SSVGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM-RASA----------FPTEDPQ-KLKTPA 219
Cdd:TIGR04504 150 SAAATRGLPHLAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAMlAATArlygltdveeFAGHQLLgRLLEPE 229

                         250
                  ....*....|....*....
gi 1835908839 220 DIMPLYLWLMGDDSRRKTG 238
Cdd:TIGR04504 230 EVAAAVAWLCSPASSAVTG 248
PRK12743 PRK12743
SDR family oxidoreductase;
13-202 6.77e-09

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 55.04  E-value: 6.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATV-ILLGRNEEKLRQVARTIAdENGTQPQWFTLDLltCTSEECHQLAQRIAAHFP 91
Cdd:PRK12743    3 QVAIVTASDSGIGKACALLLAQQGFDIgITWHSDEEGAKETAEEVR-SHGVRAEIRQLDL--SDLPEGAQALDKLIQRLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGR-QGRANWGAYATSKF 170
Cdd:PRK12743   80 RIDVLVNNAG-AMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGGRIINITSVHEhTPLPGASAYTAAKH 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1835908839 171 ATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:PRK12743  159 ALGGLTKAMALELVEHGILVNAVAPGAIATPM 190
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
13-204 6.87e-09

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 54.69  E-value: 6.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQvarTIADENGTQPQWFTLDLltctsEECHQLAQRIAAHFPR 92
Cdd:PRK06924    2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENKELT---KLAEQYNSNLTFHSLDL-----QDVHELETNFNEILSS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LD----GVLH---NAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQaLLPLLLKSDAGSL--VFTSSSVGRQGRANWG 163
Cdd:PRK06924   74 IQednvSSIHlinNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTS-TFMKHTKDWKVDKrvINISSGAAKNPYFGWS 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1835908839 164 AYATSKFATEGMMQVLADEYQNRHLRVNCIN--PGGTRTGMRA 204
Cdd:PRK06924  153 AYCSSKAGLDMFTQTVATEQEEEEYPVKIVAfsPGVMDTNMQA 195
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 4-211 7.43e-09

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 55.26  E-value: 7.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   4 QPKQDLLQ-GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENG-TQPQWFTLDLltctSEECHQ 81
Cdd:PLN02780   44 RPAKNLKKyGSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKYSkTQIKTVVVDF----SGDIDE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  82 LAQRIAAHFPRLD-GVLHNAglLGDICPMS----EQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGR 156
Cdd:PLN02780  120 GVKRIKETIEGLDvGVLINN--VGVSYPYArffhEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAI 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 157 QGRAN--WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM---RASAF--PTED 211
Cdd:PLN02780  198 VIPSDplYAVYAATKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVATKMasiRRSSFlvPSSD 259
PRK06194 PRK06194
hypothetical protein; Provisional
 8-205 8.52e-09

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 55.02  E-value: 8.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   8 DLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQRIA 87
Cdd:PRK06194    2 KDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQ-GAEVLGVRTDV--SDAAQVEALADAAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATF---------MLTQALLPLllkSDAGSLVFTSSSVGRQG 158
Cdd:PRK06194   79 ERFGAVHLLFNNAG-VGAGGLVWENSLADWEWVLGVNLWGVIhgvraftplMLAAAEKDP---AYEGHIVNTASMAGLLA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1835908839 159 RANWGAYATSKFA----TEGMMQVLADEYQNRHLRVNCinPGGTRTGMRAS 205
Cdd:PRK06194  155 PPAMGIYNVSKHAvvslTETLYQDLSLVTDQVGASVLC--PYFVPTGIWQS 203
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 10-200 1.59e-08

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 54.09  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLltcTSEECHQLAQRIAAH 89
Cdd:PRK08339    6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSESNVDVSYIVADL---TKREDLERTVKELKN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG--LLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYAT 167
Cdd:PRK08339   83 IGEPDIFFFSTGgpKPGYFMEMSMED---WEGAVKLLLYPAVYLTRALVPAMERKGFGRIIYSTSVAIKEPIPNIALSNV 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835908839 168 SKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK08339  160 VRISMAGLVRTLAKELGPKGITVNGIMPGIIRT 192
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 10-238 1.91e-08

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 53.81  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:PRK07576    7 FAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQAGPEG-LGVSADVRDYAAVE--AAFAQIADE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLhnAGLLGDI-CPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSdAGSLVFTS---SSVGRQGRANWGAy 165
Cdd:PRK07576   84 FGPIDVLV--SGAAGNFpAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRP-GASIIQISapqAFVPMPMQAHVCA- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 166 atSKFATEGMMQVLADEYQNRHLRVNCINPG---GTRtGMRASAFPTEDPQKLK---------TPADIMPLYLWLMGDDS 233
Cdd:PRK07576  160 --AKAGVDMLTRTLALEWGPEGIRVNSIVPGpiaGTE-GMARLAPSPELQAAVAqsvplkrngTKQDIANAALFLASDMA 236


                  ....*
gi 1835908839 234 RRKTG 238
Cdd:PRK07576  237 SYITG 241
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 11-200 3.26e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 53.00  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQvartIADENGTQPQWFTLDLltcTSEEchQLA---QRIA 87
Cdd:PRK06180    3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARAD----FEALHPDRALARLLDV---TDFD--AIDavvADAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  88 AHFPRLDGVLHNA--GLLGDIcpmsEQNPLvwqDVM----QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRAN 161
Cdd:PRK06180   74 ATFGPIDVLVNNAgyGHEGAI----EESPL---AEMrrqfEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLITMPG 146

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK06180  147 IGYYCGSKFALEGISESLAKEVAPFGIHVTAVEPGSFRT 185
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 12-156 6.51e-08

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 52.21  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADE-NGTQPQWFTLDLLTCTSeeCHQLAQRIAAHF 90
Cdd:cd09809     1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAVSRILEEwHKARVEAMTLDLASLRS--VQRFAEAFKAKN 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835908839  91 PRLDGVLHNAGLLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGR 156
Cdd:cd09809    79 SPLHVLVCNAAVFALPWTLTEDG---LETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSESHR 141
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 15-212 9.34e-08

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: 51.04  E-value: 9.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGR----------NEEKLRQVARTIAdengtqpqwfTLDLLTCTSEECHqlaq 84
Cdd:cd11731     1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRssgdyqvditDEASIKALFEKVG----------HFDAIVSTAGDAE---- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  85 riAAHFPRLDgvlhnagllgdicpmSEQNPLVWQDVM--QVNVnatfmltqALLPLLLKSDAGSLVFTSSSVGRQGRANW 162
Cdd:cd11731    67 --FAPLAELT---------------DADFQRGLNSKLlgQINL--------VRHGLPYLNDGGSITLTSGILAQRPIPGG 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQnRHLRVNCINPGGTRTGMRA--SAFPTEDP 212
Cdd:cd11731   122 AAAATVNGALEGFVRAAAIELP-RGIRINAVSPGVVEESLEAygDFFPGFEP 172
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 5-103 1.63e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 51.18  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   5 PKQDllqGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQ-VARTIADENGTQPQWFTLDLLTCTSeeCHQLA 83
Cdd:PRK06197   12 PDQS---GRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAaAARITAATPGADVTLQELDLTSLAS--VRAAA 86

                          90       100
                  ....*....|....*....|
gi 1835908839  84 QRIAAHFPRLDGVLHNAGLL 103
Cdd:PRK06197   87 DALRAAYPRIDLLINNAGVM 106
PRK05993 PRK05993
SDR family oxidoreductase;
13-206 2.07e-07

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 50.80  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEklrQVARTIADENGTqpqwFTLDLltCTSEECHQLAQRIAAHFP- 91
Cdd:PRK05993    5 RSILITGCSSGIGAYCARALQSDGWRVFATCRKEE---DVAALEAEGLEA----FQLDY--AEPESIAALVAQVLELSGg 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHN-----AGLLGDIcP---MSEQ---NPLVWQDvmqvnvnatfmLTQALLPLLLKSDAGSLVFTSSSVGRQGRA 160
Cdd:PRK05993   76 RLDALFNNgaygqPGAVEDL-PteaLRAQfeaNFFGWHD-----------LTRRVIPVMRKQGQGRIVQCSSILGLVPMK 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1835908839 161 NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASA 206
Cdd:PRK05993  144 YRGAYNASKFAIEGLSLTLRMELQGSGIHVSLIEPGPIETRFRANA 189
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 8-206 3.14e-07

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: 50.02  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   8 DLLQGRIILVTG-ASD-----GIGREAtqtyARYGATVILLGRNEeKLRQVARTIADENGTQPqwftldLLTC--TSEE- 78
Cdd:COG0623     1 GLLKGKRGLITGvANDrsiawGIAKAL----HEEGAELAFTYQGE-ALKKRVEPLAEELGSAL------VLPCdvTDDEq 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  79 CHQLAQRIAAHFPRLDGVLHNAGLlgdiCPMSE-QNPLV---WQDVMQ-VNVNA-TFM-LTQALLPLLlkSDAGSLVfTS 151
Cdd:COG0623    70 IDALFDEIKEKWGKLDFLVHSIAF----APKEElGGRFLdtsREGFLLaMDISAySLVaLAKAAEPLM--NEGGSIV-TL 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835908839 152 SSVGRQgRA--NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTgmRASA 206
Cdd:COG0623   143 TYLGAE-RVvpNYNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKT--LAAS 196
PRK07806 PRK07806
SDR family oxidoreductase;
7-100 4.69e-07

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 49.33  E-value: 4.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   7 QDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRN-EEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQR 85
Cdd:PRK07806    1 MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkAPRANKVVAEIEAA-GGRASAVGADL--TDEESVAALMDT 77

                          90
                  ....*....|....*
gi 1835908839  86 IAAHFPRLDGVLHNA 100
Cdd:PRK07806   78 AREEFGGLDALVLNA 92
PRK06482 PRK06482
SDR family oxidoreductase;
16-220 8.74e-07

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 48.96  E-value: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEngtqpqwFTLDLLTCT-SEECHQLAQRIAAHFPRLD 94
Cdd:PRK06482    6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDR-------LWVLQLDVTdSAAVRAVVDRAFAALGRID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAG--LLGdicPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:PRK06482   79 VVVSNAGygLFG---AAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGI 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1835908839 173 EGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPTEDPQKLK-TPAD 220
Cdd:PRK06482  156 EGFVEAVAQEVAPFGIEFTIVEPGPARTNFGAGLDRGAPLDAYDdTPVG 204
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 14-202 1.05e-06

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: 48.54  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIG-----REATQTYARYGATVILLGRNEEKLRQVARTIA---DENGTQPQWFTLDLLTCTSEEchQLAQR 85
Cdd:cd08941     3 VVLVTGANSGLGlaiceRLLAEDDENPELTLILACRNLQRAEAACRALLashPDARVVFDYVLVDLSNMVSVF--AAAKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  86 IAAHFPRLDGVLHNAGL--------LGDICpMSEQNPL---------------------VWQD----VMQVNVNATFMLT 132
Cdd:cd08941    81 LKKRYPRLDYLYLNAGImpnpgidwIGAIK-EVLTNPLfavtnptykiqaegllsqgdkATEDglgeVFQTNVFGHYYLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 133 QALLPLLLKSDAGS-LVFTSSSVGR---------QGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:cd08941   160 RELEPLLCRSDGGSqIIWTSSLNASpkyfslediQHLKGPAPYSSSKYLVDLLSLALNRKFNKLGVYSYVVHPGICTTNL 239
PRK08177 PRK08177
SDR family oxidoreductase;
13-202 1.30e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 48.10  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEK---LRQVArtiadengtQPQWFTLDLLTCTSEEchQLAQRIAAH 89
Cdd:PRK08177    2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQdtaLQALP---------GVHIEKLDMNDPASLD--QLLQRLQGQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 fpRLDGVLHNAGLLG-DICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKsDAGSLVFTSS---SVGRQGRANWGAY 165
Cdd:PRK08177   71 --RFDLLFVNAGISGpAHQSAADATAAEIGQLFLTNAIAPIRLARRLLGQVRP-GQGVLAFMSSqlgSVELPDGGEMPLY 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1835908839 166 ATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:PRK08177  148 KASKAALNSMTRSFVAELGEPTLTVLSMHPGWVKTDM 184
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
 12-228 1.97e-06

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 47.59  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWF-TLDLltCTSEECHQLAQRIAAHF 90
Cdd:cd09808     1 GRSFLITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEARKEIETESGNQNIFLhIVDM--SDPKQVWEFVEEFKEEG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGLLGDICPMSEQNplvWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKF 170
Cdd:cd09808    79 KKLHVLINNAGCMVNKRELTEDG---LEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSSGGMLVQKLNTNNLQSERT 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 171 ATEGMMQ---------VLADEYQNRH--LRVNCINPGGTRTGMRASAFP---TEDPQKLKTPADIMPLYLWL 228
Cdd:cd09808   156 AFDGTMVyaqnkrqqvIMTEQWAKKHpeIHFSVMHPGWADTPAVRNSMPdfhARFKDRLRSEEQGADTVVWL 227
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
8-200 3.13e-06

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 47.02  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   8 DLLQGRIILVTGASD--GIGREATQTYARYGATVILLGRNEEKLRQVARTIADEngtqpqwftLDLLTC--TSEECHQLA 83
Cdd:PRK06079    3 GILSGKKIVVMGVANkrSIAWGCAQAIKDQGATVIYTYQNDRMKKSLQKLVDEE---------DLLVECdvASDESIERA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  84 -QRIAAHFPRLDGVLH------NAGLLGDICPMSEQNPLVWQDVmqvnvNATFMLTQALLPLLLKSDAGSLVfTSSSVGR 156
Cdd:PRK06079   74 fATIKERVGKIDGIVHaiayakKEELGGNVTDTSRDGYALAQDI-----SAYSLIAVAKYARPLLNPGASIV-TLTYFGS 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1835908839 157 QgRA--NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK06079  148 E-RAipNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKT 192
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
 92-234 3.72e-06

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


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 46.14  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  92 RLDGVLHNAGLLGDICpmSEQNPLVWqdvMQVNVNATFMLTQAllplLLKSDAGSLVFTSSSVGrQGRANWG-------- 163
Cdd:cd08946    30 RLDVVVHLAALVGVPA--SWDNPDED---FETNVVGTLNLLEA----ARKAGVKRFVYASSASV-YGSPEGLpeeeetpp 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835908839 164 ----AYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFPtedPQKLKTPADIMPLYLWLMGDDSR 234
Cdd:cd08946   100 rplsPYGVSKLAAEHLLRSYGESYGLPVVILRLANVYGPGQRPRLDGVV---NDFIRRALEGKPLTVFGGGNQTR 171
PRK05693 PRK05693
SDR family oxidoreductase;
14-206 5.70e-06

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 46.32  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVArtiadengtQPQWFTLDLLTCTSEECHQLAQRIAAHFPRL 93
Cdd:PRK05693    3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALA---------AAGFTAVQLDVNDGAALARLAEELEAEHGGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSdAGSLVFTSSSVGRQGRANWGAYATSKFATE 173
Cdd:PRK05693   74 DVLINNAG-YGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRS-RGLVVNIGSVSGVLVTPFAGAYCASKAAVH 151

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835908839 174 GMMQVLADEYQNRHLRVNCINPGGTRTGMRASA 206
Cdd:PRK05693  152 ALSDALRLELAPFGVQVMEVQPGAIASQFASNA 184
PRK06953 PRK06953
SDR family oxidoreductase;
13-202 5.72e-06

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 45.83  E-value: 5.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAdengtqpQWFTLDLltCTSEECHQLAQRIAAHfpR 92
Cdd:PRK06953    2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALAALQALGA-------EALALDV--ADPASVAGLAWKLDGE--A 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLGdicPMSEQNPLVWQD----VMQVNVNAtFMLTQALLPLLLKSDAGSLVFTSSSVGR----QGRANWgA 164
Cdd:PRK06953   71 LDAAVYVAGVYG---PRTEGVEPITREdfdaVMHTNVLG-PMQLLPILLPLVEAAGGVLAVLSSRMGSigdaTGTTGW-L 145

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1835908839 165 YATSKFATEgmMQVLADEYQNRHLRVNCINPGGTRTGM 202
Cdd:PRK06953  146 YRASKAALN--DALRAASLQARHATCIALHPGWVRTDM 181
PRK08251 PRK08251
SDR family oxidoreductase;
15-206 5.86e-06

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 46.08  E-value: 5.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADEN-GTQPQWFTLDLltCTSEECHQLAQRIAAHFPRL 93
Cdd:PRK08251    5 ILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARYpGIKVAVAALDV--NDHDQVFEVFAEFRDELGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGlLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQG-RANWGAYATSKFAT 172
Cdd:PRK08251   83 DRVIVNAG-IGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGlPGVKAAYAASKAGV 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1835908839 173 EGMMQVLADEYQNRHLRVNCINPGGTRTGMRASA 206
Cdd:PRK08251  162 ASLGEGLRAELAKTPIKVSTIEPGYIRSEMNAKA 195
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 13-211 1.56e-05

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 44.87  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  13 RIILVTGASDGIGREATQTYARYGATVILlgrNEEKLRQVARTIADENgTQPQwftldLLTCTSEECHQLAQRIAAHFPR 92
Cdd:cd05361     2 SIALVTHARHFAGPASAEALTEDGYTVVC---HDASFADAAERQAFES-ENPG-----TKALSEQKPEELVDAVLQAGGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLGDICPMSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFAT 172
Cdd:cd05361    73 IDVLVSNDYIPRPMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPARAAA 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1835908839 173 EGMMQVLADEYQNRHLRVNCINPGGTRTgmrASAFPTED 211
Cdd:cd05361   153 VALAESLAKELSRDNILVYAIGPNFFNS---PTYFPTSD 188
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 11-58 2.68e-05

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 44.64  E-value: 2.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1835908839  11 QGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARtIAD 58
Cdd:PRK13771  162 KGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSK-YAD 208
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
9-101 2.96e-05

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 44.16  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   9 LLQGRIILVTG----ASdgIGREATQTYARYGATVIL--LGRneeKLRQVARtIADENGTQPQWFTLDLltcTSEEcH-- 80
Cdd:PRK07889    4 LLEGKRILVTGvitdSS--IAFHVARVAQEQGAEVVLtgFGR---ALRLTER-IAKRLPEPAPVLELDV---TNEE-Hla 73

                          90       100
                  ....*....|....*....|.
gi 1835908839  81 QLAQRIAAHFPRLDGVLHNAG 101
Cdd:PRK07889   74 SLADRVREHVDGLDGVVHSIG 94
PRK09009 PRK09009
SDR family oxidoreductase;
15-219 3.27e-05

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 43.90  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIG----REATQTY--ARYGATVillgrneeklrqvARTIADENGTQPQWFTLDLltCTSEECHQLAQRiaa 88
Cdd:PRK09009    3 ILIVGGSGGIGkamvKQLLERYpdATVHATY-------------RHHKPDFQHDNVQWHALDV--TDEAEIKQLSEQ--- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  89 hFPRLDGVLHNAGLL--GDICP---MSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVG-----RQG 158
Cdd:PRK09009   65 -FTQLDWLINCVGMLhtQDKGPeksLQALDADFFLQNITLNTLPSLLLAKHFTPKLKQSESAKFAVISAKVGsisdnRLG 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835908839 159 raNWGAYATSKFATEGMMQVLADEYQN--RHLRVNCINPGGTRTGMRAsAFPTEDPQ-KLKTPA 219
Cdd:PRK09009  144 --GWYSYRASKAALNMFLKTLSIEWQRslKHGVVLALHPGTTDTALSK-PFQQNVPKgKLFTPE 204
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 12-200 3.66e-05

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: 43.72  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASD--GIGREATQTYARYGATVILLGRNEeKLRQVARTIADENGTQPQWFTLDLltCTSEECHQLAQRIAAH 89
Cdd:cd05372     1 GKRILITGIANdrSIAWGIAKALHEAGAELAFTYQPE-ALRKRVEKLAERLGESALVLPCDV--SNDEEIKELFAEVKKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAGLlgdiCPMSE-QNPLV------WQDVMQVNVNATFMLTQALLPLLlkSDAGSLVFTSSSVGRQGRANW 162
Cdd:cd05372    78 WGKLDGLVHSIAF----APKVQlKGPFLdtsrkgFLKALDISAYSLVSLAKAALPIM--NPGGSIVTLSYLGSERVVPGY 151

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1835908839 163 GAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:cd05372   152 NVMGVAKAALESSVRYLAYELGRKGIRVNAISAGPIKT 189
KR_fFAS_like_SDR_c_like cd08928
ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c) ...
 15-208 3.91e-05

ketoacyl reductase (KR) domain of fungal-type fatty acid synthase (fFAS)-like, classical (c)-like SDRs; KR domain of FAS, including the fungal-type multidomain FAS alpha chain, and the single domain daunorubicin C-13 ketoreductase. Fungal-type FAS is a heterododecameric FAS composed of alpha and beta multifunctional polypeptide chains. The KR, an SDR family member is located centrally in the alpha chain. KR catalyzes the NADP-dependent reduction of ketoacyl-ACP to hydroxyacyl-ACP. KR shares the critical active site Tyr of the classical SDR and has partial identity of the active site tetrad, but the upstream Asn is replaced in KR by Met. As in other SDRs, there is a glycine rich NAD(P)-binding motif, but the pattern found in KR does not match the classical SDRs, and is not strictly conserved within this group. Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Single domain daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187633 [Multi-domain]  Cd Length: 248  Bit Score: 43.82  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDG-IGREATQTYARYGATVILLGRNEEklRQVARTIADENGTQP-QWFTLDLLTCTSEECHQLAQRIAAHFPR 92
Cdd:cd08928     1 VLITGAGDGsIGAEVLQGLLNGGAKVYVTTSRFS--RQVTKYYQDIYAACGaAGSVLIVVPFNQGSKQDVEALAIGIYDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  93 LDGVLHNAGLLGDICPMSEQNpLVWQDVMQVNVNATFMLTQALLPLLlksdagSLVFTSSSVGRQGRA------------ 160
Cdd:cd08928    79 VNGLGWDLDLYGPFAAIPETG-IEIPAIDSKSEVAHRIMLTNLLRPK------GLVKIQKQLRGQETRpaqvilpfspnh 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1835908839 161 ----NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGMRASAFP 208
Cdd:cd08928   152 gtfgDDGAYSESKLHLETLFNRWASESWGNDLTVCGAHIGWTRGTLGGEAAP 203
PRK06940 PRK06940
short chain dehydrogenase; Provisional
 14-241 4.21e-05

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 43.85  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASdGIGreatQTYAR---YGATVILLGRNEEKLRQVARTIADEnGTQPQWFTLDLltCTSEECHQLAQRiAAHF 90
Cdd:PRK06940    4 VVVVIGAG-GIG----QAIARrvgAGKKVLLADYNEENLEAAAKTLREA-GFDVSTQEVDV--SSRESVKALAAT-AQTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  91 PRLDGVLHNAGLlgdiCPmsEQNPLvwQDVMQVNVNATFMLTQALLPLLLKSDAGsLVFTSSSVGR-------QGRA--- 160
Cdd:PRK06940   75 GPVTGLVHTAGV----SP--SQASP--EAILKVDLYGTALVLEEFGKVIAPGGAG-VVIASQSGHRlpaltaeQERAlat 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 161 -------------------NWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPG------------GTR-TGMRA--SA 206
Cdd:PRK06940  146 tpteellslpflqpdaiedSLHAYQIAKRANALRVMAEAVKWGERGARINSISPGiistplaqdelnGPRgDGYRNmfAK 225

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1835908839 207 FPTEDPqklKTPADIMPLYLWLMGDDSRRKTGMTF 241
Cdd:PRK06940  226 SPAGRP---GTPDEIAALAEFLMGPRGSFITGSDF 257
PRK10675 PRK10675
UDP-galactose-4-epimerase; Provisional
 14-223 4.65e-05

UDP-galactose-4-epimerase; Provisional


Pssm-ID: 182639 [Multi-domain]  Cd Length: 338  Bit Score: 44.03  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPQWFTLDLLTctseecHQLAQRIAAHFPrL 93
Cdd:PRK10675    2 RVLVTGGSGYIGSHTCVQLLQNGHDVVILDNLCNSKRSVLPVIERLGGKHPTFVEGDIRN------EALLTEILHDHA-I 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  94 DGVLHNAGL--LGDicpmSEQNPLVWQDvmqVNVNATFMLTQALLPLLLKsdagSLVFTSSSV--GRQGRANW------- 162
Cdd:PRK10675   75 DTVIHFAGLkaVGE----SVQKPLEYYD---NNVNGTLRLISAMRAANVK----NLIFSSSATvyGDQPKIPYvesfptg 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 163 ---GAYATSKFATEgmmQVLAD------EYQNRHLRVncINPggtrTGMRASAFPTEDPQKLktPADIMP 223
Cdd:PRK10675  144 tpqSPYGKSKLMVE---QILTDlqkaqpDWSIALLRY--FNP----VGAHPSGDMGEDPQGI--PNNLMP 202
PRK07041 PRK07041
SDR family oxidoreductase;
16-196 6.54e-05

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 43.10  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIadENGTQPQWFTLDLltcTSEEchQLAQRIAAHfPRLDG 95
Cdd:PRK07041    1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARAL--GGGAPVRTAALDI---TDEA--AVDAFFAEA-GPFDH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  96 VLHNA-----GLLGDIcpmseqnPLV-WQDVMQVNVNATFMLTQALLPlllkSDAGSLVFTSSSVGRQGRANWGAYATSK 169
Cdd:PRK07041   73 VVITAadtpgGPVRAL-------PLAaAQAAMDSKFWGAYRVARAARI----APGGSLTFVSGFAAVRPSASGVLQGAIN 141

                         170       180
                  ....*....|....*....|....*..
gi 1835908839 170 FATEGMMQVLADEYQNrhLRVNCINPG 196
Cdd:PRK07041  142 AALEALARGLALELAP--VRVNTVSPG 166
PRK06101 PRK06101
SDR family oxidoreductase;
15-55 9.61e-05

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 42.55  E-value: 9.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVART 55
Cdd:PRK06101    4 VLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHTQ 44
PRK05650 PRK05650
SDR family oxidoreductase;
15-212 1.18e-04

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 42.34  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGtqpQWFTLDLLTCTSEECHQLAQRIAAHFPRLD 94
Cdd:PRK05650    3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLKLLREAGG---DGFYQRCDVRDYSQLTALAQACEEKWGGID 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLL--GDIcpmSEQNPLVWQDVMQVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRANWGAYATSKFA- 171
Cdd:PRK05650   80 VIVNNAGVAsgGFF---EELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGv 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1835908839 172 ---TEGMMQVLADeyQNRHLRVNCinPGGTRTGMrASAFPTEDP 212
Cdd:PRK05650  157 valSETLLVELAD--DEIGVHVVC--PSFFQTNL-LDSFRGPNP 195
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
 16-236 1.32e-04

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: 42.22  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  16 LVTGASDGIGREATQTYARYGATVILLGRNEEklrQVARTIADE-NGTQPQWFTL---DLLTCTS--EECHQLAQRIAAH 89
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRSA---AAASTLAAElNARRPNSAVTcqaDLSNSATlfSRCEAIIDACFRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  90 FPRLDGVLHNAG-------LLGDIC-PMSEQNPLVWQ--DVMQVNVNATFMLT------QALLPLLLKSDAGSLVFTSSS 153
Cdd:TIGR02685  82 FGRCDVLVNNASafyptplLRGDAGeGVGDKKSLEVQvaELFGSNAIAPYFLIkafaqrQAGTRAEQRSTNLSIVNLCDA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 154 VGRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGgtrtgmrASAFPTEDPQKLKtpadimplylwlmgDDS 233
Cdd:TIGR02685 162 MTDQPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPG-------LSLLPDAMPFEVQ--------------EDY 220


                  ...
gi 1835908839 234 RRK 236
Cdd:TIGR02685 221 RRK 223
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 15-102 1.55e-04

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: 42.12  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGA-TVILLGRNEEKLRQVARtiadENGTQPQWFT---LDLLTCTSeeCHQLAQRIAAHF 90
Cdd:cd09810     4 VVITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQ----EVGMPKDSYSvlhCDLASLDS--VRQFVDNFRRTG 77

                          90
                  ....*....|..
gi 1835908839  91 PRLDGVLHNAGL 102
Cdd:cd09810    78 RPLDALVCNAAV 89
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 10-59 1.82e-04

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 41.97  E-value: 1.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADE 59
Cdd:cd08270   131 LLGRRVLVTGASGGVGRFAVQLAALAGAHVVAVVGSPARAEGLRELGAAE 180
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 15-125 2.22e-04

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


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 40.85  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKlrqvARTIADENGTQPQWFTLDlltctseechqLAQRIAAhFPRLD 94
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKR----LSKEDQEPVAVVEGDLRD-----------LDSLSDA-VQGVD 64

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1835908839  95 GVLHNAGLLGDICPMSEQNPlvwqdVMQVNV 125
Cdd:cd05226    65 VVIHLAGAPRDTRDFCEVDV-----EGTRNV 90
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 12-58 2.75e-04

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 41.53  E-value: 2.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIAD 58
Cdd:cd08259   163 GDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELGAD 209
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 10-62 2.83e-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: 40.84  E-value: 2.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGT 62
Cdd:cd01078    26 LKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRARFGE 78
PRK06720 PRK06720
hypothetical protein; Provisional
 10-102 3.29e-04

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 40.34  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQpqwftldLLTCTSEECHQLAQRI--- 86
Cdd:PRK06720   14 LAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESGQATVEEITNLGGEA-------LFVSYDMEKQGDWQRVisi 86

                          90
                  ....*....|....*..
gi 1835908839  87 -AAHFPRLDGVLHNAGL 102
Cdd:PRK06720   87 tLNAFSRIDMLFQNAGL 103
PRK12744 PRK12744
SDR family oxidoreductase;
10-231 3.80e-04

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 40.88  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVA-RTIAD--ENGTQPQWFTLDLltCTSEECHQLAQRI 86
Cdd:PRK12744    6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKAVAIHYNSAASKADAeETVAAvkAAGAKAVAFQADL--TTAAAVEKLFDDA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  87 AAHFPRLDGVLHNAG--LLGDICPMSEQNplvwQDVMqVNVN---ATFMLTQALLPLllkSDAGSLVFTSSSVGRQGRAN 161
Cdd:PRK12744   84 KAAFGRPDIAINTVGkvLKKPIVEISEAE----YDEM-FAVNsksAFFFIKEAGRHL---NDNGKIVTLVTSLLGAFTPF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839 162 WGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRTGM--------------RASAFPTEDPQKLKTPADIMPLYLW 227
Cdd:PRK12744  156 YSAYAGSKAPVEHFTRAASKEFGARGISVTAVGPGPMDTPFfypqegaeavayhkTAAALSPFSKTGLTDIEDIVPFIRF 235


                  ....
gi 1835908839 228 LMGD 231
Cdd:PRK12744  236 LVTD 239
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 12-59 5.12e-04

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 40.64  E-value: 5.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADE 59
Cdd:cd08253   145 GETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGAELVRQAGADA 192
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 15-195 6.33e-04

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 40.41  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEklRQVARTIADENGtQPQWFTLDlltctseechqlaqriaahFPRLD 94
Cdd:cd05232     2 VLVTGANGFIGRALVDKLLSRGEEVRIAVRNAE--NAEPSVVLAELP-DIDSFTDL-------------------FLGVD 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLLGDicpMSEQNPLVWQDVMQVNVNATFMLTQAllplLLKSDAGSLVFTSS-------SVGRQGRANW----- 162
Cdd:cd05232    60 AVVHLAARVHV---MNDQGADPLSDYRKVNTELTRRLARA----AARQGVKRFVFLSSvkvngegTVGAPFDETDppapq 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1835908839 163 GAYATSKFATEgmmQVLADEYQNRHLRVNCINP 195
Cdd:cd05232   133 DAYGRSKLEAE---RALLELGASDGMEVVILRP 162
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
 12-128 6.84e-04

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


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 40.29  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGA-TVILLGRNEEKLRQVARTIAdENGTQPQWFTLDLLTCTSEechqlAQRIAAHF 90
Cdd:cd05237     2 GKTILVTGGAGSIGSELVRQILKFGPkKLIVFDRDENKLHELVRELR-SRFPHDKLRFIIGDVRDKE-----RLRRAFKE 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1835908839  91 PRLDGVLHNAGLlgDICPMSEQNPLvwqDVMQVNVNAT 128
Cdd:cd05237    76 RGPDIVFHAAAL--KHVPSMEDNPE---EAIKTNVLGT 108
PRK08340 PRK08340
SDR family oxidoreductase;
15-152 8.27e-04

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 39.79  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENGTQPqwFTLDLltCTSEECHQLAQRIAAHFPRLD 94
Cdd:PRK08340    3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEVYA--VKADL--SDKDDLKNLVKEAWELLGGID 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835908839  95 GVLHNAGLLG-DICPMSEQNPLVWQDVMQVNVNA----TFMLTQALLPLLLKsdaGSLVFTSS 152
Cdd:PRK08340   79 ALVWNAGNVRcEPCMLHEAGYSDWLEAALLHLVApgylTTLLIQAWLEKKMK---GVLVYLSS 138
PRK05854 PRK05854
SDR family oxidoreductase;
10-48 1.17e-03

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 39.66  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEK 48
Cdd:PRK05854   12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRAK 50
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 12-66 1.19e-03

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 39.55  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835908839  12 GRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADE--NGTQPQW 66
Cdd:cd08266   167 GETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYviDYRKEDF 223
PRK08862 PRK08862
SDR family oxidoreductase;
14-88 1.28e-03

SDR family oxidoreductase;


Pssm-ID: 236342 [Multi-domain]  Cd Length: 227  Bit Score: 38.94  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835908839  14 IILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQvartiadengtqpqwftldlltcTSEECHQLAQRIAA 88
Cdd:PRK08862    7 IILITSAGSVLGRTISCHFARLGATLILCDQDQSALKD-----------------------TYEQCSALTDNVYS 58
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 8-66 1.95e-03

Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 38.89  E-value: 1.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835908839   8 DLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADE--NGTQPQW 66
Cdd:cd08244   139 TLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGGPAKTALVRALGADVavDYTRPDW 199
PRK08303 PRK08303
short chain dehydrogenase; Provisional
 5-118 2.72e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 38.44  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839   5 PKQDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRN-EEKLRQVAR--TI------ADENGTQPQWFTLDLLtcT 75
Cdd:PRK08303    1 PMMKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRStRARRSEYDRpeTIeetaelVTAAGGRGIAVQVDHL--V 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1835908839  76 SEECHQLAQRIAAHFPRLDgVLHNagllgDIC---PMSEQNPLVWQ 118
Cdd:PRK08303   79 PEQVRALVERIDREQGRLD-ILVN-----DIWggeKLFEWGKPVWE 118
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 8-51 2.80e-03

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 38.31  E-value: 2.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1835908839   8 DLLQGRIILVTGASDGIGREATQtYARY-GATVILL--GRNEEKLRQ 51
Cdd:cd05289   141 GLKAGQTVLIHGAAGGVGSFAVQ-LAKArGARVIATasAANADFLRS 186
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 15-54 3.42e-03

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: 37.52  E-value: 3.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVAR 54
Cdd:COG0702     2 ILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAA 41
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-54 3.94e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 37.96  E-value: 3.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1835908839   6 KQDLLQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKlRQVAR 54
Cdd:cd08268   139 LAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEK-RDALL 186
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
15-101 6.19e-03

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 37.52  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIADENgtqpqwftLDLLTCTSEEchqlAQRIAAHFPRLD 94
Cdd:COG3268     8 IVVYGATGYTGRLVAEYLARRGLRPALAGRNAAKLEAVAAELGAAD--------LPLRVADLDD----PASLAALLAGTR 75


                  ....*..
gi 1835908839  95 GVLHNAG 101
Cdd:COG3268    76 VVLNTVG 82
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 15-184 7.76e-03

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 36.89  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRneekLRQVARTIADENGTqpqWFTLDLltCTSEECHQLAQRIaahfpRLD 94
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDR----LTSASNTARLADLR---FVEGDL--TDRDALEKLLADV-----RPD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  95 GVLHNAGLLGDicPMSEQNPLvwqDVMQVNVNATFMLTQAllplLLKSDAGSLVFTSSS-----VGRQGRANW------- 162
Cdd:pfam01370  67 AVIHLAAVGGV--GASIEDPE---DFIEANVLGTLNLLEA----ARKAGVKRFLFASSSevygdGAEIPQEETtltgpla 137

                         170       180
                  ....*....|....*....|....
gi 1835908839 163 --GAYATSKFATEGMMQVLADEYQ 184
Cdd:pfam01370 138 pnSPYAAAKLAGEWLVLAYAAAYG 161
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
10-200 8.58e-03

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 36.62  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  10 LQGRIILVTGASD------GIGREATQTYARYGATVIL--LGRNEEKLRQVARTIadengtQPQWFtLDLLTCTSEECHQ 81
Cdd:PRK07370    4 LTGKKALVTGIANnrsiawGIAQQLHAAGAELGITYLPdeKGRFEKKVRELTEPL------NPSLF-LPCDVQDDAQIEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835908839  82 LAQRIAAHFPRLDGVLH------NAGLLGDICPMSEQNPLVWQDVmqvnvnATFMLTQ-ALLPLLLKSDAGSLVFTSSSV 154
Cdd:PRK07370   77 TFETIKQKWGKLDILVHclafagKEELIGDFSATSREGFARALEI------SAYSLAPlCKAAKPLMSEGGSIVTLTYLG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1835908839 155 GRQGRANWGAYATSKFATEGMMQVLADEYQNRHLRVNCINPGGTRT 200
Cdd:PRK07370  151 GVRAIPNYNVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRT 196
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 10-50 8.75e-03

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 36.98  E-value: 8.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1835908839  10 LQGRIILVTGASDGIGREATQTYARYGATVILLGRNEEKLR 50
Cdd:PRK07424  176 LKGKTVAVTGASGTLGQALLKELHQQGAKVVALTSNSDKIT 216
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
 15-57 9.66e-03

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. 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: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 36.82  E-value: 9.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1835908839  15 ILVTGASDGIGREATQTYARYGATVILLGRNEEKLRQVARTIA 57
Cdd:cd05242     2 IVITGGTGFIGRALTRRLTAAGHEVVVLSRRPGKAEGLAEVIT 44
 
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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