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Conserved domains on  [gi|15833594|ref|NP_312367|]
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3-oxoacyl-[acyl-carrier-protein] reductase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
5-243 3.54e-155

3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well conserved family of proteins closely related to the FabG family, TIGR01830, and possibly equal in function. In all completed genomes with a member of this family, a FabG in TIGR01830 is also found. [Fatty acid and phospholipid metabolism, Biosynthesis]


:

Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 430.48  E-value: 3.54e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:TIGR01831   1 VLVTGASRGIGRAIANQLAADGFNIGVHYHSDAAGAQETLNAIVANGGNGRLLSFDVADRVACREVLEADIAQHGAYYGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:TIGR01831  81 VLNAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMPMIGARQGGRIITLASVSGVMGNRGQVNYSAAKAGLIGAT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833594   165 KALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGML 243
Cdd:TIGR01831 161 KALAIELAKRKITVNCIAPGLIDTGMIAMEESALKEALSMVPMKRMGQPEEVAGLASFLMSDIAGYVTRQVISVNGGML 239
 
Name Accession Description Interval E-value
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
5-243 3.54e-155

3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well conserved family of proteins closely related to the FabG family, TIGR01830, and possibly equal in function. In all completed genomes with a member of this family, a FabG in TIGR01830 is also found. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 430.48  E-value: 3.54e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:TIGR01831   1 VLVTGASRGIGRAIANQLAADGFNIGVHYHSDAAGAQETLNAIVANGGNGRLLSFDVADRVACREVLEADIAQHGAYYGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:TIGR01831  81 VLNAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMPMIGARQGGRIITLASVSGVMGNRGQVNYSAAKAGLIGAT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833594   165 KALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGML 243
Cdd:TIGR01831 161 KALAIELAKRKITVNCIAPGLIDTGMIAMEESALKEALSMVPMKRMGQPEEVAGLASFLMSDIAGYVTRQVISVNGGML 239
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-243 4.07e-129

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 364.87  E-value: 4.07e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKV-VIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQgGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK05653  83 LDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARY-GRIVNISSVSGVTGNPGQTNYSAAKAGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK05653 162 IGFTKALALELASRGITVNAVAPGFIDTDMTEgLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVN 241

                 ....
gi 15833594  240 GGML 243
Cdd:PRK05653 242 GGMY 245
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
3-242 4.28e-108

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: 311.40  E-value: 4.28e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYhRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTD-RSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGgRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd05333  80 ILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSG-RIINISSVVGLIGNPGQANYAASKAGVIG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:cd05333 159 FTKSLAKELASRGITVNAVAPGFIDTDMTDaLPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGG 238

                .
gi 15833594 242 M 242
Cdd:cd05333 239 M 239
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
3-243 1.61e-86

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: 257.02  E-value: 1.61e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYhRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:COG1028   7 KVALVTGGSSGIGRAIARALAAEGARVVITD-RDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:COG1028  86 ILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMR-ERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTGMIE---MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:COG1028 165 LTRSLALELAPRGIRVNAVAPGPIDTPMTRallGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVD 244

                ....
gi 15833594 240 GGML 243
Cdd:COG1028 245 GGLT 248
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
12-242 2.81e-61

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: 192.26  E-value: 2.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    12 KGIGRAIACQLAADGFNIGVHYHRDAtgAQETLNAIVANGGnGRLLSFDVANREQCREVLEHEIAQHGAWYGVVSNAGIA 91
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEA--LAKRVEELAEELG-AAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    92 R--DAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATKALAI 169
Cdd:pfam13561  83 PklKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM---KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAV 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833594   170 ELAKRKITVNCIAPGLIDTGM---IEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLAasgIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
3-156 2.06e-19

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: 82.53  E-value: 2.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594      3 RSVLVTGASKGIGRAIACQLAAdgfnigvHYHR----------DATGAQETLNAIVANGGNGRLLSFDVANREQCREVLE 72
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAE-------RGARrlvllsrsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     73 HEIAQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpcimpMIGARQGGRIITLSSVSGVMGNRGQVN 152
Cdd:smart00822  74 AIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHE-----LTADLPLDFFVLFSSIAGVLGSPGQAN 148

                   ....
gi 15833594    153 YSAA 156
Cdd:smart00822 149 YAAA 152
 
Name Accession Description Interval E-value
fabG_rel TIGR01831
3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well ...
5-243 3.54e-155

3-oxoacyl-(acyl-carrier-protein) reductase, putative; This model represents a small, very well conserved family of proteins closely related to the FabG family, TIGR01830, and possibly equal in function. In all completed genomes with a member of this family, a FabG in TIGR01830 is also found. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273825 [Multi-domain]  Cd Length: 239  Bit Score: 430.48  E-value: 3.54e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:TIGR01831   1 VLVTGASRGIGRAIANQLAADGFNIGVHYHSDAAGAQETLNAIVANGGNGRLLSFDVADRVACREVLEADIAQHGAYYGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:TIGR01831  81 VLNAGIARDAAFPALSEDDWDAVIHTNLDGFYNVIHPCIMPMIGARQGGRIITLASVSGVMGNRGQVNYSAAKAGLIGAT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833594   165 KALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGML 243
Cdd:TIGR01831 161 KALAIELAKRKITVNCIAPGLIDTGMIAMEESALKEALSMVPMKRMGQPEEVAGLASFLMSDIAGYVTRQVISVNGGML 239
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-243 4.07e-129

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 364.87  E-value: 4.07e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK05653   4 QGKTALVTGASRGIGRAIALRLAADGAKV-VIYDSNEEAAEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQgGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK05653  83 LDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARY-GRIVNISSVSGVTGNPGQTNYSAAKAGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK05653 162 IGFTKALALELASRGITVNAVAPGFIDTDMTEgLPEEVKAEILKEIPLGRLGQPEEVANAVAFLASDAASYITGQVIPVN 241

                 ....
gi 15833594  240 GGML 243
Cdd:PRK05653 242 GGMY 245
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
3-242 4.28e-108

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: 311.40  E-value: 4.28e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYhRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEGAKVAVTD-RSEEAAAETVEEIKALGGNAAALEADVSDREAVEALVEKVEAEFGPVD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGgRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd05333  80 ILVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSG-RIINISSVVGLIGNPGQANYAASKAGVIG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:cd05333 159 FTKSLAKELASRGITVNAVAPGFIDTDMTDaLPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLHVNGG 238

                .
gi 15833594 242 M 242
Cdd:cd05333 239 M 239
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-242 6.43e-102

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 296.01  E-value: 6.43e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK12825   5 MGRVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK12825  85 IDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMR-KQRGGRIVNISSVAGLPGWPGRSNYAAAKAGL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEME-ESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK12825 164 VGLTKALARELAEYGITVNMVAPGDIDTDMKEATiEEAREAKDAETPLGRSGTPEDIARAVAFLCSDASDYITGQVIEVT 243

                 ...
gi 15833594  240 GGM 242
Cdd:PRK12825 244 GGV 246
3oxo_ACP_reduc TIGR01830
3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, ...
5-242 4.17e-93

3-oxoacyl-(acyl-carrier-protein) reductase; This model represents 3-oxoacyl-[ACP] reductase, also called 3-ketoacyl-acyl carrier protein reductase, an enzyme of fatty acid biosynthesis. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273824 [Multi-domain]  Cd Length: 239  Bit Score: 273.32  E-value: 4.17e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:TIGR01830   1 ALVTGASRGIGRAIALKLAKEGAKVIITYRSSEEGAEEVVEELKALGVKALGVVLDVSDREDVKAVVEEIEEELGTIDIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGgRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:TIGR01830  81 VNNAGITRDNLLMRMKEEDWDAVIDTNLTGVFNLTQAVLRIMIKQRSG-RIINISSVVGLMGNAGQANYAASKAGVIGFT 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833594   165 KALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:TIGR01830 160 KSLAKELASRNITVNAVAPGFIDTDMTDkLSEKVKKKILSQIPLGRFGQPEEVANAVAFLASDEASYITGQVIHVDGGM 238
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
3-242 1.10e-90

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 267.44  E-value: 1.10e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK05557   6 KVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARqGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK05557  86 ILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQR-SGRIINISSVVGLMGNPGQANYAASKAGVIG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAM-SMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK05557 165 FTKSLARELASRGITVNAVAPGFIETDMTDALPEDVKEAIlAQIPLGRLGQPEEIASAVAFLASDEAAYITGQTLHVNGG 244

                 .
gi 15833594  242 M 242
Cdd:PRK05557 245 M 245
PRK12827 PRK12827
short chain dehydrogenase; Provisional
1-242 7.89e-88

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 260.42  E-value: 7.89e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGV---HYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQ 77
Cdd:PRK12827   5 DSRRVLITGGSGGLGRAIAVRLAADGADVIVldiHPMRGRAEADAVAAGIEAAGGKALGLAFDVRDFAATRAALDAGVEE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 HGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK12827  85 FGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGGRIVNIASVAGVRGNRGQVNYAASK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE---MEESALKEAmsmiPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:PRK12827 165 AGLIGLTKTLANELAPRGITVNAVAPGAINTPMADnaaPTEHLLNPV----PVQRLGEPDEVAALVAFLVSDAASYVTGQ 240

                 ....*...
gi 15833594  235 VISINGGM 242
Cdd:PRK12827 241 VIPVDGGF 248
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
3-243 1.61e-86

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: 257.02  E-value: 1.61e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYhRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:COG1028   7 KVALVTGGSSGIGRAIARALAAEGARVVITD-RDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:COG1028  86 ILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMR-ERGGGRIVNISSIAGLRGSPGQAAYAASKAAVVG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTGMIE---MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:COG1028 165 LTRSLALELAPRGIRVNAVAPGPIDTPMTRallGAEEVREALAARIPLGRLGTPEEVAAAVLFLASDAASYITGQVLAVD 244

                ....
gi 15833594 240 GGML 243
Cdd:COG1028 245 GGLT 248
PRK12826 PRK12826
SDR family oxidoreductase;
1-243 2.11e-83

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 249.06  E-value: 2.11e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK12826   5 EGRVALVTGAARGIGRAIAVRLAADGAEVIVV-DICGDDAAATAELVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARqGGRIITLSSVSGV-MGNRGQVNYSAAKAG 159
Cdd:PRK12826  84 LDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAG-GGRIVLTSSVAGPrVGYPGLAHYAASKAG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK12826 163 LVGFTRALALELAARNITVNSVHPGGVDTPMAGnlGDAQWAEAIAAAIPLGRLGEPEDIAAAVLFLASDEARYITGQTLP 242

                 ....*.
gi 15833594  238 INGGML 243
Cdd:PRK12826 243 VDGGAT 248
AcAcCoA_reduct TIGR01829
acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the ...
3-242 1.40e-74

acetoacetyl-CoA reductase; This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.


Pssm-ID: 273823 [Multi-domain]  Cd Length: 242  Bit Score: 226.55  E-value: 1.40e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:TIGR01829   1 RIALVTGGMGGIGTAICQRLAKDGYRVAANCGPNEERAEAWLQEQGALGFDFRVVEGDVSSFESCKAAVAKVEAELGPVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:TIGR01829  81 VLVNNAGITRDATFKKMTYEQWDAVIDTNLNSVFNVTQPVIDGMR-ERGWGRIINISSVNGQKGQFGQTNYSAAKAGMIG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   163 ATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:TIGR01829 160 FTKALAQEGATKGVTVNTISPGYIATDMVMaMREDVLNSIVAQIPVKRLGRPEEIAAAVAFLASEEAGYITGATLSINGG 239

                  .
gi 15833594   242 M 242
Cdd:TIGR01829 240 L 240
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
1-241 6.55e-73

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 222.33  E-value: 6.55e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWFEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK12824  81 VDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQP-LFAAMCEQGYGRIINISSVNGLKGQFGQTNYSAAKAGM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK12824 160 IGFTKALASEGARYGITVNCIAPGYIATPMVEqMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFITGETISIN 239

                 ..
gi 15833594  240 GG 241
Cdd:PRK12824 240 GG 241
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
5-239 1.33e-68

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: 210.99  E-value: 1.33e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETlnAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELA--AIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:cd05233  79 VNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAA-LPHMKKQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLT 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833594 165 KALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:cd05233 158 RSLALELAPYGIRVNAVAPGLVDTPMLAklGPEEAEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-243 4.15e-67

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 207.39  E-value: 4.15e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK05565   4 MGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQELLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK05565  84 IDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMI-KRKSGVIVNISSIWGLIGASCEVLYSASKGAV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMI----EMEESALKEamsMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVI 236
Cdd:PRK05565 163 NAFTKALAKELAPSGIRVNAVAPGAIDTEMWssfsEEDKEGLAE---EIPLGRLGKPEEIAKVVLFLASDDASYITGQII 239

                 ....*..
gi 15833594  237 SINGGML 243
Cdd:PRK05565 240 TVDGGWT 246
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
12-242 2.81e-61

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: 192.26  E-value: 2.81e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    12 KGIGRAIACQLAADGFNIGVHYHRDAtgAQETLNAIVANGGnGRLLSFDVANREQCREVLEHEIAQHGAWYGVVSNAGIA 91
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEA--LAKRVEELAEELG-AAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    92 R--DAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATKALAI 169
Cdd:pfam13561  83 PklKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLM---KEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAV 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833594   170 ELAKRKITVNCIAPGLIDTGM---IEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:pfam13561 160 ELGPRGIRVNAISPGPIKTLAasgIPGFDELLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
3-243 1.49e-60

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 190.90  E-value: 1.49e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRdatgaQETLNAIVAN-GGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK12936   7 RKALVTGASGGIGEEIARLLHAQGAIVGLHGTR-----VEKLEALAAElGERVKIFPANLSDRDEVKALGQKAEADLEGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK12936  82 DILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMM-RRRYGRIINITSVVGVTGNPGQANYCASKAGMI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEA-MSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISING 240
Cdd:PRK12936 161 GFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLNDKQKEAiMGAIPMKRMGTGAEVASAVAYLASSEAAYVTGQTIHVNG 240

                 ...
gi 15833594  241 GML 243
Cdd:PRK12936 241 GMA 243
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
6-242 2.44e-59

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 187.90  E-value: 2.44e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK12935  10 IVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVNHFGKVDILV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATK 165
Cdd:PRK12935  90 NNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTS-AVLPYITEAEEGRIISISSIIGQAGGFGQTNYSAAKAGMLGFTK 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833594  166 ALAIELAKRKITVNCIAPGLIDTGMI-EMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAgYVTRQVISINGGM 242
Cdd:PRK12935 169 SLALELAKTNVTVNAICPGFIDTEMVaEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRDGA-YITGQQLNINGGL 245
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
5-242 3.10e-56

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: 179.89  E-value: 3.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd05358   6 ALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGTLDIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:cd05358  86 VNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKGKIINMSSVHEKIPWPGHVNYAASKGGVKMMT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 165 KALAIELAKRKITVNCIAPGLIDTGMIEM---EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:cd05358 166 KTLAQEYAPKGIRVNAIAPGAINTPINAEawdDPEQRADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVTGTTLFVDGG 245

                .
gi 15833594 242 M 242
Cdd:cd05358 246 M 246
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
6-241 2.10e-55

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: 177.47  E-value: 2.10e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:cd05362   7 LVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVDILV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATK 165
Cdd:cd05362  87 NNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRL---RDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAFTR 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833594 166 ALAIELAKRKITVNCIAPGLIDTGMIEMEES--ALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:cd05362 164 VLAKELGGRGITVNAVAPGPVDTDMFYAGKTeeAVEGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQVIRANGG 241
PRK12829 PRK12829
short chain dehydrogenase; Provisional
1-241 6.34e-54

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 174.48  E-value: 6.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVhyhrdATGAQETLNAIVANGGNGRLLSF--DVANREQCREVLEHEIAQH 78
Cdd:PRK12829  10 DGLRVLVTGGASGIGRAIAEAFAEAGARVHV-----CDVSEAALAATAARLPGAKVTATvaDVADPAQVERVFDTAVERF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIA-RDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK12829  85 GGLDVLVNNAGIAgPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVAGRLGYPGRTPYAASK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEM------------EESALKEAMSMIPMKRMGQAEEVAGLASYLMS 225
Cdd:PRK12829 165 WAVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRRviearaqqlgigLDEMEQEYLEKISLGRMVEPEDIAATALFLAS 244
                        250
                 ....*....|....*.
gi 15833594  226 DIAGYVTRQVISINGG 241
Cdd:PRK12829 245 PAARYITGQAISVDGN 260
PRK12743 PRK12743
SDR family oxidoreductase;
1-243 2.04e-53

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 172.91  E-value: 2.04e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK12743  81 IDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKE-AMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK12743 161 GGLTKAMALELVEHGILVNAVAPGAIATPMNGMDDSDVKPdSRPGIPLGRPGDTHEIASLVAWLCSEGASYTTGQSLIVD 240

                 ....
gi 15833594  240 GGML 243
Cdd:PRK12743 241 GGFM 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
5-190 2.87e-52

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 167.79  E-value: 2.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     5 VLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVL-VDRSEEKLEAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:pfam00106  82 VNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIK-GSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160
                         170       180
                  ....*....|....*....|....*.
gi 15833594   165 KALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTDM 186
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
1-243 8.43e-51

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: 166.01  E-value: 8.43e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:cd05366   1 MSKVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:cd05366  81 FDVMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 161 IGATKALAIELAKRKITVNCIAPGLIDTGMIE------------MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIA 228
Cdd:cd05366 161 RGLTQTAAQELAPKGITVNAYAPGIVKTEMWDyideevgeiagkPEGEGFAEFSSSIPLGRLSEPEDVAGLVSFLASEDS 240
                       250
                ....*....|....*
gi 15833594 229 GYVTRQVISINGGML 243
Cdd:cd05366 241 DYITGQTILVDGGMV 255
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-217 1.09e-50

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 165.81  E-value: 1.09e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYhRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:COG0300   4 TGKTVLITGASSGIGRALARALAARGARVVLVA-RDAERLEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLARFGP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:COG0300  83 IDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRA-LLPLMRARGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15833594 161 IGATKALAIELAKRKITVNCIAPGLIDTGMIemeesalkEAMSMIPMKRMGQAEEVA 217
Cdd:COG0300 162 EGFSESLRAELAPTGVRVTAVCPGPVDTPFT--------ARAGAPAGRPLLSPEEVA 210
PRK12939 PRK12939
short chain dehydrogenase; Provisional
2-243 3.46e-49

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 161.68  E-value: 3.46e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK12939   7 GKRALVTGAARGLGAAFAEALAEAGATVAFN-DGLAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK12939  86 DGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAAL-PHLRDSGRGRIVNLASDTALWGAPKLGAYVASKGAVI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDTGMIEM--EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK12939 165 GMTRSLARELGGRGITVNAIAPGLTATEATAYvpADERHAYYLKGRALERLQVPDDVAGAVLFLLSDAARFVTGQLLPVN 244

                 ....
gi 15833594  240 GGML 243
Cdd:PRK12939 245 GGFV 248
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
3-242 7.03e-48

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 158.25  E-value: 7.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNI----GVHYHRDAT--GAQETLN-AIVANGGNgrllsfdVANREQCREVLEHEI 75
Cdd:PRK12938   4 RIAYVTGGMGGIGTSICQRLHKDGFKVvagcGPNSPRRVKwlEDQKALGfDFIASEGN-------VGDWDSTKAAFDKVK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   76 AQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSA 155
Cdd:PRK12938  77 AEVGEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMV-ERGWGRIINISSVNGQKGQFGQTNYST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  156 AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:PRK12938 156 AKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMVKaIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFSTGA 235

                 ....*...
gi 15833594  235 VISINGGM 242
Cdd:PRK12938 236 DFSLNGGL 243
PRK07577 PRK07577
SDR family oxidoreductase;
2-241 1.96e-47

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 156.81  E-value: 1.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFN-IGVhyhrdATGAQETLNaivanggnGRLLSFDVANREQCREVLEhEIAQHGA 80
Cdd:PRK07577   3 SRTVLVTGATKGIGLALSLRLANLGHQvIGI-----ARSAIDDFP--------GELFACDLADIEQTAATLA-QINEIHP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGgRIITLSSVSgVMGNRGQVNYSAAKAGI 160
Cdd:PRK07577  69 VDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQG-RIVNICSRA-IFGALDRTSYSAAKSAL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEMEE----SALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVI 236
Cdd:PRK07577 147 VGCTRTWALELAEYGITVNAVAPGPIETELFRQTRpvgsEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQVL 226

                 ....*
gi 15833594  237 SINGG 241
Cdd:PRK07577 227 GVDGG 231
PRK06701 PRK06701
short chain dehydrogenase; Provisional
5-241 1.57e-45

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 153.65  E-value: 1.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIGVHY---HRDAtgaQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK06701  49 ALITGGDSGIGRAVAVLFAKEGADIAIVYldeHEDA---NETKQRVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELGRL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDA-AFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK06701 126 DILVNNAAFQYPQqSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL---KQGSAIINTGSITGYEGNETLIDYSATKGAI 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMI--EMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISI 238
Cdd:PRK06701 203 HAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIpsDFDEEKVSQFGSNTPMQRPGQPEELAPAYVFLASPDSSYITGQMLHV 282

                 ...
gi 15833594  239 NGG 241
Cdd:PRK06701 283 NGG 285
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
3-242 1.94e-45

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: 152.43  E-value: 1.94e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEheiaQHGAWY 82
Cdd:cd05344   2 KVALVTAASSGIGLAIARALAREGARVAI-CARNRENLERAASELRAGGAGVLAVVADLTDPEDIDRLVE----KAGDAF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 G----VVSNAGIARDAAFPALSDDDWDAVIHTNldsFYNVIQPC--IMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:cd05344  77 GrvdiLVNNAGGPPPGPFAELTDEDWLEAFDLK---LLSVIRIVraVLPGMKERGWGRIVNISSLTVKEPEPNLVLSNVA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE------------MEESALKEAMSMIPMKRMGQAEEVAGLASYLM 224
Cdd:cd05344 154 RAGLIGLVKTLSRELAPDGVTVNSVLPGYIDTERVRrllearaekegiSVEEAEKEVASQIPLGRVGKPEELAALIAFLA 233
                       250
                ....*....|....*...
gi 15833594 225 SDIAGYVTRQVISINGGM 242
Cdd:cd05344 234 SEKASYITGQAILVDGGL 251
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
3-241 2.00e-45

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: 152.10  E-value: 2.00e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd05352   9 KVAIVTGGSRGIGLAIARALAEAGADVAIIYNSAPRAEEKAEELAKKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGKID 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQ--VNYSAAKAGI 160
Cdd:cd05352  89 ILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFK-KQGKGSLIITASMSGTIVNRPQpqAAYNASKAAV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAM-SMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:cd05352 168 IHLAKSLAVEWAKYFIRVNSISPGYIDTDLTDFVDKELRKKWeSYIPLKRIALPEELVGAYLYLASDASSYTTGSDLIID 247

                ..
gi 15833594 240 GG 241
Cdd:cd05352 248 GG 249
23BDH TIGR02415
acetoin reductases; One member of this family, as characterized in Klebsiella terrigena, is ...
3-243 2.14e-45

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


Pssm-ID: 131468 [Multi-domain]  Cd Length: 254  Bit Score: 152.22  E-value: 2.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATgAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:TIGR02415   1 KVALVTGGAQGIGKGIAERLAKDGFAVAVADLNEET-AKETAKEINQAGGKAVAYKLDVSDKDQVFSAIDQAAEKFGGFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:TIGR02415  80 VMVNNAGVAPITPILEITEEELKKVYNVNVKGVLFGIQAAARQFKKQGHGGKIINAASIAGHEGNPILSAYSSTKFAVRG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   163 ATKALAIELAKRKITVNCIAPGLIDTGM---IEMEESAL---------KEAMSMIPMKRMGQAEEVAGLASYLMSDIAGY 230
Cdd:TIGR02415 160 LTQTAAQELAPKGITVNAYCPGIVKTPMweeIDEETSEIagkpigegfEEFSSEIALGRPSEPEDVAGLVSFLASEDSDY 239
                         250
                  ....*....|...
gi 15833594   231 VTRQVISINGGML 243
Cdd:TIGR02415 240 ITGQSILVDGGMV 252
FabG-like PRK07231
SDR family oxidoreductase;
3-243 3.05e-45

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 151.52  E-value: 3.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIvanGGNGRLLSF--DVANREQCREVLEHEIAQHGA 80
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFAAEGARVVVT-DRNEEAAERVAAEI---LAGGRAIAVaaDVSDEADVEAAVAAALERFGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIA-RDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARqGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:PRK07231  82 VDILVNNAGTThRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG-GGAIVNVASTAGLRPRPGLGWYNASKGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIE--MEES---ALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLEafMGEPtpeNRAKFLATIPLGRLGTPEDIANAALFLASDEASWITGV 240

                 ....*....
gi 15833594  235 VISINGGML 243
Cdd:PRK07231 241 TLVVDGGRC 249
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-242 4.06e-44

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 148.96  E-value: 4.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK08217   8 IVITGGAQGLGRAMAEYLAQKGAKLAL-IDLNQEKLEEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLNGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAF---------PALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVmGNRGQVNYSA 155
Cdd:PRK08217  87 INNAGILRDGLLvkakdgkvtSKMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSKGVIINISSIARA-GNMGQTNYSA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  156 AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDiaGYVTRQ 234
Cdd:PRK08217 166 SKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMTAaMKPEALERLEKMIPVGRLGEPEEIAHTVRFIIEN--DYVTGR 243

                 ....*...
gi 15833594  235 VISINGGM 242
Cdd:PRK08217 244 VLEIDGGL 251
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-243 4.49e-44

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 153.84  E-value: 4.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFN-IGVhyhrDATGAQETLNAiVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK08261 211 KVALVTGAARGIGAAIAEVLARDGAHvVCL----DVPAAGEALAA-VANRVGGTALALDITAPDAPARIAEHLAERHGGL 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcimpMIGA---RQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:PRK08261 286 DIVVHNAGITRDKTLANMDEARWDSVLAVNLLAPLRITEA----LLAAgalGDGGRIVGVSSISGIAGNRGQTNYAASKA 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEA-MSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK08261 362 GVIGLVQALAPLLAERGITINAVAPGFIETQMTAAIPFATREAgRRMNSLQQGGLPVDVAETIAWLASPASGGVTGNVVR 441

                 ....*.
gi 15833594  238 INGGML 243
Cdd:PRK08261 442 VCGQSL 447
PRK06138 PRK06138
SDR family oxidoreductase;
3-243 2.20e-43

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 146.84  E-value: 2.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVAnGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK06138   6 RVAIVTGAGSGIGRATAKLFAREGARVVV-ADRDAEAAERVAAAIAA-GGRAFARQGDVGSAEAVEALVDFVAARWGRLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK06138  84 VLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAI-PIMQRQGGGSIVNTASQLALAGGRGRAAYVASKGAIAS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEM------EESALKEAMSMI-PMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:PRK06138 163 LTRAMALDHATDGIRVNAVAPGTIDTPYFRRifarhaDPEALREALRARhPMNRFGTAEEVAQAALFLASDESSFATGTT 242

                 ....*...
gi 15833594  236 ISINGGML 243
Cdd:PRK06138 243 LVVDGGWL 250
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
6-243 2.62e-43

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: 146.73  E-value: 2.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:cd05347   9 LVTGASRGIGFGIASGLAEAGANI-VINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDILV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATK 165
Cdd:cd05347  88 NNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMI-KQGHGKIINICSLLSELGGPPVPAYAASKGGVAGLTK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 166 ALAIELAKRKITVNCIAPGLIDTGMIE---MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:cd05347 167 ALATEWARHGIQVNAIAPGYFATEMTEavvADPEFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQIIFVDGGW 246

                .
gi 15833594 243 L 243
Cdd:cd05347 247 L 247
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
3-217 4.09e-43

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 145.71  E-value: 4.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIvanGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:COG4221   6 KVALITGASSGIGAATARALAAAGARVVL-AARRAERLEALAAEL---GGRALAVPLDVTDEAAVEAAVAAAVAEFGRLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:COG4221  82 VLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTR-AALPAMRARGSGHIVNISSIAGLRPYPGGAVYAATKAAVRG 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPMKRMGQAEEVA 217
Cdd:COG4221 161 LSESLRAELRPTGIRVTVIEPGAVDTEFLDsVFDGDAEAAAAVYEGLEPLTPEDVA 216
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
5-241 4.70e-43

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: 145.96  E-value: 4.70e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAAEIEELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:cd05359  81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQ-AAKLMRERGGGRIVAISSLGSIRALPNYLAVGTAKAALEALV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 165 KALAIELAKRKITVNCIAPGLIDTGMIEM---EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:cd05359 160 RYLAVELGPRGIRVNAVSPGVIDTDALAHfpnREDLLEAAAANTPAGRVGTPQDVADAVGFLCSDAARMITGQTLVVDGG 239
PRK12937 PRK12937
short chain dehydrogenase; Provisional
2-242 5.98e-43

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 145.66  E-value: 5.98e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK12937   5 NKVAIVTGASRGIGAAIARRLAADGFAVAVNYAGSAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK12937  85 DVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHL---GQGGRIINLSTSVIALPLPGYGPYAASKAAVE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDTGM-IEMEESALKEAMS-MIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK12937 162 GLVHVLANELRGRGITVNAVAPGPVATELfFNGKSAEQIDQLAgLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQVLRVN 241

                 ...
gi 15833594  240 GGM 242
Cdd:PRK12937 242 GGF 244
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
3-242 1.55e-42

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 144.87  E-value: 1.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK08936   8 KVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFGTLD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK08936  88 VMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIKGNIINMSSVHEQIPWPLFVHYAASKGGVKL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGmIEMEESALKE----AMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISI 238
Cdd:PRK08936 168 MTETLAMEYAPKGIRVNNIGPGAINTP-INAEKFADPKqradVESMIPMGYIGKPEEIAAVAAWLASSEASYVTGITLFA 246

                 ....
gi 15833594  239 NGGM 242
Cdd:PRK08936 247 DGGM 250
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
6-241 1.71e-42

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 144.94  E-value: 1.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIgVHYHRDATgAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK08226  10 LITGALQGIGEGIARVFARHGANL-ILLDISPE-IEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDILV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVM-GNRGQVNYSAAKAGIIGAT 164
Cdd:PRK08226  88 NNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMI-ARKDGRIVMMSSVTGDMvADPGETAYALTKAAIVGLT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAPGLIDTGMIEM---------EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:PRK08226 167 KSLAVEYAQSGIRVNAICPGYVRTPMAESiarqsnpedPESVLTEMAKAIPLRRLADPLEVGELAAFLASDESSYLTGTQ 246

                 ....*.
gi 15833594  236 ISINGG 241
Cdd:PRK08226 247 NVIDGG 252
PRK09730 PRK09730
SDR family oxidoreductase;
6-241 5.18e-42

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 143.45  E-value: 5.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK09730   5 LVTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAALV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIA-RDAAFPALSDDDWDAVIHTNLDSFYNVIQPCI--MPMIGARQGGRIITLSSVSGVMGNRGQ-VNYSAAKAGII 161
Cdd:PRK09730  85 NNAGILfTQCTVENLTAERINRVLSTNVTGYFLCCREAVkrMALKHGGSGGAIVNVSSAASRLGAPGEyVDYAASKGAID 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDTGMIEM--EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK09730 165 TLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASggEPGRVDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYVTGSFIDLA 244

                 ..
gi 15833594  240 GG 241
Cdd:PRK09730 245 GG 246
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
3-242 1.32e-41

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: 142.22  E-value: 1.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIgvhyhrDATGAQETLNAIVANGGNGRLLSFDVANREQcrevLEHEIAQHGAWY 82
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREGANV------IATDINEEKLKELERGPGITTRVLDVTDKEQ----VAALAKEEGRID 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVM-GNRGQVNYSAAKAGII 161
Cdd:cd05368  73 VLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKML-ARKDGSIINMSSVASSIkGVPNRFVYSTTKAAVI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 162 GATKALAIELAKRKITVNCIAPGLIDTGMIEME-------ESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:cd05368 152 GLTKSVAADFAQQGIRCNAICPGTVDTPSLEERiqaqpdpEEALKAFAARQPLGRLATPEEVAALAVYLASDESAYVTGT 231

                ....*...
gi 15833594 235 VISINGGM 242
Cdd:cd05368 232 AVVIDGGW 239
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
1-242 1.62e-41

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 142.17  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATgAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK08643   1 MSKVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEET-AQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK08643  80 LNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGGKIINATSQAGVVGNPELAVYSSTKFAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEM------------EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIA 228
Cdd:PRK08643 160 RGLTQTAARDLASEGITVNAYAPGIVKTPMMFDiahqvgenagkpDEWGMEQFAKDITLGRLSEPEDVANCVSFLAGPDS 239
                        250
                 ....*....|....
gi 15833594  229 GYVTRQVISINGGM 242
Cdd:PRK08643 240 DYITGQTIIVDGGM 253
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
1-241 1.13e-40

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: 140.27  E-value: 1.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQ-ETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHG 79
Cdd:cd08940   1 KGKVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEaVRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMiGARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:cd08940  81 GVDILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHM-KKQGWGRIINIASVHGLVASANKSAYVAAKHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIEM------------EESALKEAMS-MIPMKRMGQAEEVAGLASYLMSD 226
Cdd:cd08940 160 VVGLTKVVALETAGTGVTCNAICPGWVLTPLVEKqisalaqkngvpQEQAARELLLeKQPSKQFVTPEQLGDTAVFLASD 239
                       250
                ....*....|....*
gi 15833594 227 IAGYVTRQVISINGG 241
Cdd:cd08940 240 AASQITGTAVSVDGG 254
PRK06114 PRK06114
SDR family oxidoreductase;
6-241 1.24e-40

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 139.92  E-value: 1.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK06114  12 FVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHIEAAGRRAIQIAADVTSKADLRAAVARTEAELGALTLAV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRG--QVNYSAAKAGIIGA 163
Cdd:PRK06114  92 NAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAML-ENGGGSIVNIASMSGIIVNRGllQAHYNASKAGVIHL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  164 TKALAIELAKRKITVNCIAPGLIDTGMIEMEESA--LKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK06114 171 SKSLAMEWVGRGIRVNSISPGYTATPMNTRPEMVhqTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAASFCTGVDLLVDGG 250
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
3-241 1.78e-40

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: 140.12  E-value: 1.78e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHY---HRDAtgAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHG 79
Cdd:cd05355  27 KKALITGGDSGIGRAVAIAFAREGADVAINYlpeEEDD--AEETKKLIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFG 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGVVSNAGIARDA-AFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:cd05355 105 KLDILVNNAAYQHPQeSIEDITTEQLEKTFRTNIFSMFYLTKAALPHL---KKGSSIINTTSVTAYKGSPHLLDYAATKG 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 159 GIIGATKALAIELAKRKITVNCIAPGLIDTGMI--EMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVI 236
Cdd:cd05355 182 AIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIpsSFPEEKVSEFGSQVPMGRAGQPAEVAPAYVFLASQDSSYVTGQVL 261

                ....*
gi 15833594 237 SINGG 241
Cdd:cd05355 262 HVNGG 266
PRK06124 PRK06124
SDR family oxidoreductase;
3-243 1.84e-40

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 139.46  E-value: 1.84e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK06124  12 QVALVTGSARGLGFEIARALAGAGAHVLVN-GRNAATLEAAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGiARD-AAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigARQG-GRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK06124  91 ILVNNVG-ARDrRPLAELDDAAIRALLETDLVAPILLSRLAAQRM--KRQGyGRIIAITSIAGQVARAGDAVYPAAKQGL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPG--LIDTGMIEMEESALKEAMSM-IPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK06124 168 TGLMRALAAEFGPHGITSNAIAPGyfATETNAAMAADPAVGPWLAQrTPLGRWGRPEEIAGAAVFLASPAASYVNGHVLA 247

                 ....*.
gi 15833594  238 INGGML 243
Cdd:PRK06124 248 VDGGYS 253
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
3-242 2.66e-40

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: 138.87  E-value: 2.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGnGRLLSF--DVANREQCREVLEHEIAQHGA 80
Cdd:cd05369   4 KVAFITGGGTGIGKAIAKAFAELGASVAI-AGRKPEVLEAAAEEISSATG-GRAHPIqcDVRDPEAVEAAVDETLKEFGK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:cd05369  82 IDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAGV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 161 IGATKALAIELAKRKITVNCIAPGLIDT--GMIEMEESALKE--AMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVI 236
Cdd:cd05369 162 DALTRSLAVEWGPYGIRVNAIAPGPIPTteGMERLAPSGKSEkkMIERVPLGRLGTPEEIANLALFLLSDAASYINGTTL 241

                ....*.
gi 15833594 237 SINGGM 242
Cdd:cd05369 242 VVDGGQ 247
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
3-243 3.51e-40

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: 138.74  E-value: 3.51e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAadGFNIGVHY-HRDATGAQETLNAIVANGGNGRLLSFDVANREQcREVLEHEIAQH--G 79
Cdd:cd05329   7 KTALVTGGTKGIGYAIVEELA--GLGAEVYTcARNQKELDECLTEWREKGFKVEGSVCDVSSRSE-RQELMDTVASHfgG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:cd05329  84 KLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSR-LAHPLLKASGNGNIVFISSVAGVIAVPSGAPYGATKGA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIEM---EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVI 236
Cdd:cd05329 163 LNQLTRSLACEWAKDNIRVNAVAPWVIATPLVEPviqQKENLDKVIERTPLKRFGEPEEVAALVAFLCMPAASYITGQII 242

                ....*..
gi 15833594 237 SINGGML 243
Cdd:cd05329 243 AVDGGLT 249
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
3-241 4.93e-40

(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: 138.22  E-value: 4.93e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVH--------YHRDATGAQETLNAIVANGGNGRLLSFDVANREQcreVLEHE 74
Cdd:cd05353   6 RVVLVTGAGGGLGRAYALAFAERGAKVVVNdlggdrkgSGKSSSAADKVVDEIKAAGGKAVANYDSVEDGEK---IVKTA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  75 IAQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYS 154
Cdd:cd05353  83 IDAFGRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRA-AWPYMRKQKFGRIINTSSAAGLYGNFGQANYS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 155 AAKAGIIGATKALAIELAKRKITVNCIAPglidTGMIEMEESALKEamsmiPMKRMGQAEEVAGLASYLMSDiAGYVTRQ 234
Cdd:cd05353 162 AAKLGLLGLSNTLAIEGAKYNITCNTIAP----AAGSRMTETVMPE-----DLFDALKPEYVAPLVLYLCHE-SCEVTGG 231

                ....*..
gi 15833594 235 VISINGG 241
Cdd:cd05353 232 LFEVGAG 238
PRK06172 PRK06172
SDR family oxidoreductase;
6-241 6.21e-40

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 137.96  E-value: 6.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK06172  11 LVTGGAAGIGRATALAFAREGAKV-VVADRDAAGGEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAAYGRLDYAF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDA-AFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:PRK06172  90 NNAGIEIEQgRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLML-AQGGGAIVNTASVAGLGAAPKMSIYAASKHAVIGLT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAPGLIDTGMI----EMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISING 240
Cdd:PRK06172 169 KSAAIEYAKKGIRVNAVCPAVIDTDMFrrayEADPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGASFTTGHALMVDG 248

                 .
gi 15833594  241 G 241
Cdd:PRK06172 249 G 249
PRK06484 PRK06484
short chain dehydrogenase; Validated
2-241 1.52e-39

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 143.07  E-value: 1.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIvanGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK06484   5 SRVVLVTGAAGGIGRAACQRFARAGDQV-VVADRNVERARERADSL---GPDHHALAMDVSDEAQIREGFEQLHREFGRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPAL--SDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:PRK06484  81 DVLVNNAGVTDPTMTATLdtTLEEFARLQAINLTGAYLVAREALRLMIEQGHGAAIVNVASGAGLVALPKRTAYSASKAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALK----EAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:PRK06484 161 VISLTRSLACEWAAKGIRVNAVLPGYVRTQMVAELERAGKldpsAVRSRIPLGRLGRPEEIAEAVFFLASDQASYITGST 240

                 ....*.
gi 15833594  236 ISINGG 241
Cdd:PRK06484 241 LVVDGG 246
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
3-241 2.81e-39

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 136.55  E-value: 2.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKEGAKVVIA-DLNDEAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK12429  84 ILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAA-LPIMKAQGGGRIINMASVHGLVGSAGKAAYVSAKHGLIG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEM------------EESALKEAM-SMIPMKRMGQAEEVAGLASYLMSDIAG 229
Cdd:PRK12429 163 LTKVVALEGATHGVTVNAICPGYVDTPLVRKqipdlakergisEEEVLEDVLlPLVPQKRFTTVEEIADYALFLASFAAK 242
                        250
                 ....*....|..
gi 15833594  230 YVTRQVISINGG 241
Cdd:PRK12429 243 GVTGQAWVVDGG 254
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
2-242 1.34e-38

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: 134.97  E-value: 1.34e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   2 SRSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:cd08945   3 SEVALVTGATSGIGLAIARRLGKEGLRVFV-CARGEEGLATTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCI-MPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:cd08945  82 DVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLkAGGMLERGTGRIINIASTGGKQGVVHAAPYSASKHGV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEM------------EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIA 228
Cdd:cd08945 162 VGFTKALGLELARTGITVNAVCPGFVETPMAASvrehyadiwevsTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGA 241
                       250
                ....*....|....
gi 15833594 229 GYVTRQVISINGGM 242
Cdd:cd08945 242 AAVTAQALNVCGGL 255
PRK07060 PRK07060
short chain dehydrogenase; Provisional
3-243 4.50e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 132.92  E-value: 4.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDAtGAQETLNAIVANGGngrlLSFDVANREQCREVLeheiAQHGAWY 82
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARV-VAAARNA-AALDRLAGETGCEP----LRLDVGDDAAIRAAL----AAAGAFD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK07060  80 GLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKAALDA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEM---EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK07060 160 ITRVLCVELGPHGIRVNSVNPTVTLTPMAAEawsDPQKSGPMLAAIPLGRFAEVDDVAAPILFLLSDAASMVSGVSLPVD 239

                 ....
gi 15833594  240 GGML 243
Cdd:PRK07060 240 GGYT 243
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
6-243 4.66e-38

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: 133.36  E-value: 4.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:cd05337   5 IVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAEVLAAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCLV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  86 SNAGIA--RDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMI---GARQG--GRIITLSSVSGVMG--NRGQvnYSAA 156
Cdd:cd05337  85 NNAGIAvrPRGDLLDLTEDSFDRLIAINLRGPFFLTQAVARRMVeqpDRFDGphRSIIFVTSINAYLVspNRGE--YCIS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMS--MIPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:cd05337 163 KAGLSMATRLLAYRLADEGIAVHEIRPGLIHTDMTAPVKEKYDELIAagLVPIRRWGQPEDIAKAVRTLASGLLPYSTGQ 242

                ....*....
gi 15833594 235 VISINGGML 243
Cdd:cd05337 243 PINIDGGLS 251
PRK06841 PRK06841
short chain dehydrogenase; Provisional
3-241 4.77e-38

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 133.25  E-value: 4.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQEtlnAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK06841  16 KVAVVTGGASGIGHAIAELFAAKGARVAL-LDRSEDVAEV---AAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRID 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK06841  92 ILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMI-AAGGGKIVNLASQAGVVALERHVAYCASKAGVVG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTgmiEMEESA----LKEAM-SMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK06841 171 MTKVLALEWGPYGITVNAISPTVVLT---ELGKKAwageKGERAkKLIPAGRFAYPEEIAAAALFLASDAAAMITGENLV 247

                 ....
gi 15833594  238 INGG 241
Cdd:PRK06841 248 IDGG 251
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
3-241 1.09e-37

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 132.26  E-value: 1.09e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIG-VHYHRDatGAQETLNAIVANGGNGRLLSF--DVANREQCREVLEHEIAQHG 79
Cdd:cd05330   4 KVVLITGGGSGLGLATAVRLAKEGAKLSlVDLNEE--GLEAAKAALLEIAPDAEVLLIkaDVSDEAQVEAYVDATVEQFG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGVVSNAGI-ARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:cd05330  82 RIDGFFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEK-VLKVMREQGSGMIVNTASVGGIRGVGNQSGYAAAKH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 159 GIIGATKALAIELAKRKITVNCIAPGLIDTGMIEME---------ESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAG 229
Cdd:cd05330 161 GVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSlkqlgpenpEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAG 240
                       250
                ....*....|..
gi 15833594 230 YVTRQVISINGG 241
Cdd:cd05330 241 YVNAAVVPIDGG 252
PRK09242 PRK09242
SDR family oxidoreductase;
3-243 1.23e-37

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 132.18  E-value: 1.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRL--LSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK09242  10 QTALITGASKGIGLAIAREFLGLGADV-LIVARDADALAQARDELAEEFPEREVhgLAADVSDDEDRRAILDWVEDHWDG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK09242  89 LHILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSR-YAHPLLKQHASSAIVNIGSVSGLTHVRSGAPYGMTKAAL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIE---MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK09242 168 LQMTRNLAVEWAEDGIRVNAVAPWYIRTPLTSgplSDPDYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAASYITGQCIA 247

                 ....*.
gi 15833594  238 INGGML 243
Cdd:PRK09242 248 VDGGFL 253
PRK07063 PRK07063
SDR family oxidoreductase;
5-241 1.69e-37

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 132.10  E-value: 1.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLL--SFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07063  10 ALVTGAAQGIGAAIARAFAREGAAVAL-ADLDAALAERAAAAIARDVAGARVLavPADVTDAASVAAAVAAAEEAFGPLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK07063  89 VLVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMV-ERGRGSIVNIASTHAFKIIPGCFPYPVAKHGLLG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEM-------EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:PRK07063 168 LTRALGIEYAARNVRVNAIAPGYIETQLTEDwwnaqpdPAAARAETLALQPMKRIGRPEEVAMTAVFLASDEAPFINATC 247

                 ....*.
gi 15833594  236 ISINGG 241
Cdd:PRK07063 248 ITIDGG 253
PRK12828 PRK12828
short chain dehydrogenase; Provisional
3-243 2.45e-37

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 131.07  E-value: 2.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGngRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARV-ALIGRGAAPLSQTLPGVPADAL--RIGGIDLVDPQAARRAVDEVNRQFGRLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK12828  85 ALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALT-ASGGGRIVNIGAGAALKAGPGMGAYAAAKAGVAR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEmeesalkEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:PRK12828 164 LTEALAAELLDRGITVNAVLPSIIDTPPNR-------ADMPDADFSRWVTPEQIAAVIAFLLSDEAQAITGASIPVDGGV 236

                 .
gi 15833594  243 L 243
Cdd:PRK12828 237 A 237
PRK07774 PRK07774
SDR family oxidoreductase;
2-241 2.60e-37

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 131.02  E-value: 2.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK07774   6 DKVAIVTGAAGGIGQAYAEALAREGASVVVA-DINAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSD---DDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGnrgQVNYSAAKA 158
Cdd:PRK07774  85 DYLVNNAAIYGGMKLDLLITvpwDYYKKFMSVNLDGALVCTR-AVYKHMAKRGGGAIVNQSSTAAWLY---SNFYGLAKV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDT--GMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVI 236
Cdd:PRK07774 161 GLNGLTQQLARELGGMNIRVNAIAPGPIDTeaTRTVTPKEFVADMVKGIPLSRMGTPEDLVGMCLFLLSDEASWITGQIF 240

                 ....*
gi 15833594  237 SINGG 241
Cdd:PRK07774 241 NVDGG 245
PRK07035 PRK07035
SDR family oxidoreductase;
6-243 7.74e-37

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 130.14  E-value: 7.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK07035  12 LVTGASRGIGEAIAKLLAQQGAHVIVS-SRKLDGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLDILV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAgiARDAAFPALSDDD---WDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK07035  91 NNA--AANPYFGHILDTDlgaFQKTVDVNIRGYFFMSVEA-GKLMKEQGGGSIVNVASVNGVSPGDFQGIYSITKAAVIS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK07035 168 MTKAFAKECAPFGIRVNALLPGLTDTkfaSALFKNDAILKQALAHIPLRRHAEPSEMAGAVLYLASDASSYTTGECLNVD 247

                 ....
gi 15833594  240 GGML 243
Cdd:PRK07035 248 GGYL 251
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-243 8.81e-37

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 130.24  E-value: 8.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVHYHrdATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK06935  19 IVTGGNTGLGQGYAVALAKAGADIIITTH--GTNWDETRRLIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDILV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigARQG-GRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:PRK06935  97 NNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVM--AKQGsGKIINIASMLSFQGGKFVPAYTASKHGVAGLT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAPGLI---DTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK06935 175 KAFANELAAYNIQVNAIAPGYIktaNTAPIRADKNRNDEILKRIPAGRWGEPDDLMGAAVFLASRASDYVNGHILAVDGG 254

                 ..
gi 15833594  242 ML 243
Cdd:PRK06935 255 WL 256
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
5-242 2.85e-36

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: 128.34  E-value: 2.85e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQetlNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd05349   3 VLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAE---AVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNA-------GIARDAaFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:cd05349  80 VNNAlidfpfdPDQRKT-FDTIDWEDYQQQLEGAVKGALNLLQAVL-PDFKERGSGRVINIGTNLFQNPVVPYHDYTTAK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 158 AGIIGATKALAIELAKRKITVNCIAPGLID-TGMIEMEESALKEAMSMI-PMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:cd05349 158 AALLGFTRNMAKELGPYGITVNMVSGGLLKvTDASAATPKEVFDAIAQTtPLGKVTTPQDIADAVLFFASPWARAVTGQN 237

                ....*..
gi 15833594 236 ISINGGM 242
Cdd:cd05349 238 LVVDGGL 244
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
5-241 8.93e-36

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: 127.22  E-value: 8.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIvanGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd08944   6 AIVTGAGAGIGAACAARLAREGARVVVA-DIDGGAAQAVVAQI---AGGALALRVDVTDEQQVAALFERAVEEFGGLDLL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDA-AFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGA 163
Cdd:cd08944  82 VNNAGAMHLTpAIIDTDLAVWDQTMAINLRGTFLCCRHAA-PRMIARGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 164 TKALAIELAKRKITVNCIAPGLIDTGMIE----MEESALKE--AMSMIPMK--RMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:cd08944 161 TRTLAAELRHAGIRCNALAPGLIDTPLLLaklaGFEGALGPggFHLLIHQLqgRLGRPEDVAAAVVFLLSDDASFITGQV 240

                ....*.
gi 15833594 236 ISINGG 241
Cdd:cd08944 241 LCVDGG 246
PRK05867 PRK05867
SDR family oxidoreductase;
3-241 1.21e-35

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 127.07  E-value: 1.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK05867  10 KRALITGASTGIGKRVALAYVEAGAQVAIA-ARHLDALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQV--NYSAAKAGI 160
Cdd:PRK05867  89 IAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASMSGHIINVPQQvsHYCASKAAV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISING 240
Cdd:PRK05867 169 IHLTKAMAVELAPHKIRVNSVSPGYILTELVEPYTEYQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYMTGSDIVIDG 248

                 .
gi 15833594  241 G 241
Cdd:PRK05867 249 G 249
PRK07677 PRK07677
short chain dehydrogenase; Provisional
5-241 3.17e-35

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 125.95  E-value: 3.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK07677   4 VIITGGSSGMGKAMAKRFAEEGANV-VITGRTKEKLEEAKLEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDAL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAgiARDAAFPA--LSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK07677  83 INNA--AGNFICPAedLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIKGNIINMVATYAWDAGPGVIHSAAAKAGVLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKR-KITVNCIAPGLID-TGMIE---MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK07677 161 MTRTLAVEWGRKyGIRVNAIAPGPIErTGGADklwESEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAYINGTCIT 240

                 ....
gi 15833594  238 INGG 241
Cdd:PRK07677 241 MDGG 244
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-243 1.40e-34

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 124.30  E-value: 1.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEELAATQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIA--RDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQG-----GRIITLSSVSGVMG--NRGQv 151
Cdd:PRK12745  81 IDCLVNNAGVGvkVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMLAQPEPeelphRSIVFVSSVNAIMVspNRGE- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  152 nYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIemeeSALKE------AMSMIPMKRMGQAEEVAGLASYLMS 225
Cdd:PRK12745 160 -YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDMT----APVTAkydaliAKGLVPMPRWGEPEDVARAVAALAS 234
                        250
                 ....*....|....*...
gi 15833594  226 DIAGYVTRQVISINGGML 243
Cdd:PRK12745 235 GDLPYSTGQAIHVDGGLS 252
PRK06398 PRK06398
aldose dehydrogenase; Validated
5-243 1.46e-34

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 124.17  E-value: 1.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADG---FNIGVHYHRDAtgaqetlnaivanggNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK06398   9 AIVTGGSQGIGKAVVNRLKEEGsnvINFDIKEPSYN---------------DVDYFKVDVSNKEQVIKGIDYVISKYGRI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARqGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK06398  74 DILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD-KGVIINIASVQSFAVTRNAAAYVTSKHAVL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKrKITVNCIAPGLIDTGMIEME------------ESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAG 229
Cdd:PRK06398 153 GLTRSIAVDYAP-TIRCVAVCPGSIRTPLLEWAaelevgkdpehvERKIREWGEMHPMKRVGKPEEVAYVVAFLASDLAS 231
                        250
                 ....*....|....
gi 15833594  230 YVTRQVISINGGML 243
Cdd:PRK06398 232 FITGECVTVDGGLR 245
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
3-242 1.69e-34

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 124.29  E-value: 1.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALGEAGARV-VLSARKAEELEEAAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAafPALSD--DDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNR----GQVNYSAA 156
Cdd:PRK08213  92 ILVNNAGATWGA--PAEDHpvEAWDKVMNLNVRGLFLLSQAVAKRSMIPRGYGRIINVASVAGLGGNPpevmDTIAYNTS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAM-SMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:PRK08213 170 KGAVINFTRALAAEWGPHGIRVNAIAPGFFPTKMTRGTLERLGEDLlAHTPLGRLGDDEDLKGAALLLASDASKHITGQI 249

                 ....*..
gi 15833594  236 ISINGGM 242
Cdd:PRK08213 250 LAVDGGV 256
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
3-241 2.08e-34

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


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 123.68  E-value: 2.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGR---LLSFDVANREQCREVLEHEIAQHG 79
Cdd:cd05364   4 KVAIITGSSSGIGAGTAILFARLGARLALT-GRDAERLEETRQSCLQAGVSEKkilLVVADLTEEEGQDRIISTTLAKFG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARqgGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:cd05364  83 RLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTK--GEIVNVSSVAGGRSFPGVLYYCISKAA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 160 IIGATKALAIELAKRKITVNCIAPGLIDTGM---IEMEESA----LKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVT 232
Cdd:cd05364 161 LDQFTRCTALELAPKGVRVNSVSPGVIVTGFhrrMGMPEEQyikfLSRAKETHPLGRPGTVDEVAEAIAFLASDASSFIT 240

                ....*....
gi 15833594 233 RQVISINGG 241
Cdd:cd05364 241 GQLLPVDGG 249
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-241 2.90e-34

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 123.36  E-value: 2.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQEtlnaiVANGGnGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKE-----LREKG-VFTIKCDVGNRDQVKKSKEVVEKEFGRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLD-SFYNVIQpcIMPMIGARQGGRIITLSSVSGV-MGNRGQVNYSAAKAG 159
Cdd:PRK06463  81 DVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNgAIYTTYE--FLPLLKLSKNGAIVNIASNAGIgTAAEGTTFYAITKAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDTGMI-----EMEESALKEAM-SMIPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:PRK06463 159 IIILTRRLAFELGKYGIRVNAVAPGWVETDMTlsgksQEEAEKLRELFrNKTVLKTTGKPEDIANIVLFLASDDARYITG 238

                 ....*...
gi 15833594  234 QVISINGG 241
Cdd:PRK06463 239 QVIVADGG 246
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
3-241 3.57e-34

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: 122.39  E-value: 3.57e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd05357  81 VLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAF-ARRLAGSRNGSIINIIDAMTDRPLTGYFAYCMSKAALEG 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833594 163 ATKALAIELAKRkITVNCIAPGLIDTGMiEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDiaGYVTRQVISINGG 241
Cdd:cd05357 160 LTRSAALELAPN-IRVNGIAPGLILLPE-DMDAEYRENALRKVPLKRRPSAEEIADAVIFLLDS--NYITGQIIKVDGG 234
PRK07069 PRK07069
short chain dehydrogenase; Validated
6-242 3.98e-34

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 122.90  E-value: 3.98e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSF--DVANREQCREVLEHEIAQHGAWYG 83
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDAFAAEINAAHGEGVAFAAvqDVTDEAQWQALLAQAADAMGGLSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   84 VVSNAGIARDAAFPALSDDDWDAVIHTNLDSfynVIQPC--IMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK07069  83 LVNNAGVGSFGAIEQIELDEWRRVMAINVES---IFLGCkhALPYLRASQPASIVNISSVAAFKAEPDYTAYNASKAAVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKRKITVNC--IAPGLIDTGMIEM------EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:PRK07069 160 SLTKSIALDCARRGLDVRCnsIHPTFIRTGIVDPifqrlgEEEATRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVTG 239

                 ....*....
gi 15833594  234 QVISINGGM 242
Cdd:PRK07069 240 AELVIDGGI 248
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-241 4.32e-34

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 122.38  E-value: 4.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFN-IGVHYHrDATGAQETLNAIVANggngrlLSFDVAnreqcrevlehEIAQHG 79
Cdd:PRK06550   4 MTKTVLITGAASGIGLAQARAFLAQGAQvYGVDKQ-DKPDLSGNFHFLQLD------LSDDLE-----------PLFDWV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 AWYGVVSN-AGIArDAAFPAL--SDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:PRK06550  66 PSVDILCNtAGIL-DDYKPLLdtSLEEWQHIFDTNLTSTFLLTRA-YLPQMLERKSGIIINMCSIASFVAGGGGAAYTAS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGM--IEMEESAL-KEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:PRK06550 144 KHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPMtaADFEPGGLaDWVARETPIKRWAEPEEVAELTLFLASGKADYMQG 223

                 ....*...
gi 15833594  234 QVISINGG 241
Cdd:PRK06550 224 TIVPIDGG 231
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
5-241 1.21e-33

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: 121.72  E-value: 1.21e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQetlnaIVAN-GGNGRLLSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:cd05341   8 AIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQA-----AAAElGDAARFFHLDVTDEDGWTAVVDTAREAFGRLDV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGArQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGA 163
Cdd:cd05341  83 LVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEA-GGGSIINMSSIEGLVGDPALAAYNASKGAVRGL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 164 TKALAIELAKRK--ITVNCIAPGLIDTGMIE--MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:cd05341 162 TKSAALECATQGygIRVNSVHPGYIYTPMTDelLIAQGEMGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVTGSELVVD 241

                ..
gi 15833594 240 GG 241
Cdd:cd05341 242 GG 243
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-242 2.81e-33

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 120.96  E-value: 2.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIvanGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK08642   4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADEL---GDRAIALQADVTDREQVQAMFATATEHFGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WY-GVVSNA-------GIARDaAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSvsgvmgNRGQV- 151
Cdd:PRK08642  81 PItTVVNNAladfsfdGDARK-KADDITWEDFQQQLEGSVKGALNTIQAALPGMR-EQGFGRIINIGT------NLFQNp 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  152 -----NYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTgmieMEESAL--KEAMSMI----PMKRMGQAEEVAGLA 220
Cdd:PRK08642 153 vvpyhDYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT----TDASAAtpDEVFDLIaattPLRKVTTPQEFADAV 228
                        250       260
                 ....*....|....*....|..
gi 15833594  221 SYLMSDIAGYVTRQVISINGGM 242
Cdd:PRK08642 229 LFFASPWARAVTGQNLVVDGGL 250
PRK07791 PRK07791
short chain dehydrogenase; Provisional
3-243 3.16e-33

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 121.32  E-value: 3.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFN-----IGVHYHRDATG---AQETLNAIVANGGNGRLLSFDVANREQCREVLEHE 74
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEGARvvvndIGVGLDGSASGgsaAQAVVDEIVAAGGEAVANGDDIADWDGAANLVDAA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   75 IAQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYnviqpCIMPMIGARQGG----------RIITLSSVSGV 144
Cdd:PRK07791  87 VETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHF-----ATLRHAAAYWRAeskagravdaRIINTSSGAGL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  145 MGNRGQVNYSAAKAGIIGATKALAIELAKRKITVNCIAP----GLIDTGMIEMEESALKEAM-SMIPmkrmgqaEEVAGL 219
Cdd:PRK07791 162 QGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPaartRMTETVFAEMMAKPEEGEFdAMAP-------ENVSPL 234
                        250       260
                 ....*....|....*....|....
gi 15833594  220 ASYLMSDIAGYVTRQVISINGGML 243
Cdd:PRK07791 235 VVWLGSAESRDVTGKVFEVEGGKI 258
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-241 4.67e-33

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 120.21  E-value: 4.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK06077   9 VVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKRAEEMNETLKMVKENGGEGIGVLADVSTREGCETLAKATIDRYGVADIL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:PRK06077  89 VNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEM---REGGAIVNIASVAGIRPAYGLSIYGAMKAAVINLT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRkITVNCIAPGLIDTGMIE-------MEESALKEAMSMipMKRMGQAEEVAGLASYLMSDIAgyVTRQVIS 237
Cdd:PRK06077 166 KYLALELAPK-IRVNAIAPGFVKTKLGEslfkvlgMSEKEFAEKFTL--MGKILDPEEVAEFVAAILKIES--ITGQVFV 240

                 ....
gi 15833594  238 INGG 241
Cdd:PRK06077 241 LDSG 244
PRK08589 PRK08589
SDR family oxidoreductase;
2-243 6.61e-33

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 120.27  E-value: 6.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNigVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK08589   6 NKVAVITGASTGIGQASAIALAQEGAY--VLAVDIAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAA----FPAlsdDDWDAVIHTNLDSFYNVIQPCIMPMIgaRQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK08589  84 DVLFNNAGVDNAAGriheYPV---DVFDKIMAVDMRGTFLMTKMLLPLMM--EQGGSIINTSSFSGQAADLYRSGYNAAK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMI--------EMEESALKEAMS-MIPMKRMGQAEEVAGLASYLMSDIA 228
Cdd:PRK08589 159 GAVINFTKSIAIEYGRDGIRANAIAPGTIETPLVdkltgtseDEAGKTFRENQKwMTPLGRLGKPEEVAKLVVFLASDDS 238
                        250
                 ....*....|....*
gi 15833594  229 GYVTRQVISINGGML 243
Cdd:PRK08589 239 SFITGETIRIDGGVM 253
PRK08628 PRK08628
SDR family oxidoreductase;
5-241 6.76e-33

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 120.06  E-value: 6.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGfNIGVHYHRDATGAqETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK08628  10 VIVTGGASGIGAAISLRLAEEG-AIPVIFGRSAPDD-EFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPAlSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGrIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:PRK08628  88 VNNAGVNDGVGLEA-GREAFVASLERNLIHYYVMAHYCL-PHLKASRGA-IVNISSKTALTGQGGTSGYAAAKGAQLALT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAPGLIDTGMIEM-------EESALKEAMSMIPM-KRMGQAEEVAGLASYLMSDIAGYVTRQVI 236
Cdd:PRK08628 165 REWAVALAKDGVRVNAVIPAEVMTPLYENwiatfddPEAKLAAITAKIPLgHRMTTAEEIADTAVFLLSERSSHTTGQWL 244

                 ....*
gi 15833594  237 SINGG 241
Cdd:PRK08628 245 FVDGG 249
PRK06947 PRK06947
SDR family oxidoreductase;
1-241 9.68e-33

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 119.14  E-value: 9.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSVGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIArdAAFPALSDDDWD---AVIHTNLDSFYNVIQPCIMPMIGAR--QGGRIITLSSVSGVMGNRGQ-VNYS 154
Cdd:PRK06947  81 LDALVNNAGIV--APSMPLADMDAArlrRMFDTNVLGAYLCAREAARRLSTDRggRGGAIVNVSSIASRLGSPNEyVDYA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  155 AAKAGIIGATKALAIELAKRKITVNCIAPGLIDTgmiEMEESALKEAM-----SMIPMKRMGQAEEVAGLASYLMSDIAG 229
Cdd:PRK06947 159 GSKGAVDTLTLGLAKELGPHGVRVNAVRPGLIET---EIHASGGQPGRaarlgAQTPLGRAGEADEVAETIVWLLSDAAS 235
                        250
                 ....*....|..
gi 15833594  230 YVTRQVISINGG 241
Cdd:PRK06947 236 YVTGALLDVGGG 247
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
6-241 1.45e-32

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: 118.65  E-value: 1.45e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIvanGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:cd05345   9 IVTGAGSGFGEGIARRFAQEGARVVI-ADINADGAERVAADI---GEAAIAIQADVTKRADVEAMVEAALSKFGRLDILV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  86 SNAGIA-RDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:cd05345  85 NNAGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQ-ALVPHMEEQGGGVIINIASTAGLRPRPGLTWYNASKGWVVTAT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 165 KALAIELAKRKITVNCIAPGLIDTGMIEM-----EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:cd05345 164 KAMAVELAPRNIRVNCLCPVAGETPLLSMfmgedTPENRAKFRATIPLGRLSTPDDIANAALYLASDEASFITGVALEVD 243

                ..
gi 15833594 240 GG 241
Cdd:cd05345 244 GG 245
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
6-242 2.14e-32

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: 118.41  E-value: 2.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:cd08936  14 LVTASTDGIGLAIARRLAQDGAHVVVS-SRKQQNVDRAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVNLHGGVDILV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  86 SNAgiARDAAFPALSD---DDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd08936  93 SNA--AVNPFFGNILDsteEVWDKILDVNVKATALMTK-AVVPEMEKRGGGSVVIVSSVAAFHPFPGLGPYNVSKTALLG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTG---MIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:cd08936 170 LTKNLAPELAPRNIRVNCLAPGLIKTSfssALWMDKAVEESMKETLRIRRLGQPEDCAGIVSFLCSEDASYITGETVVVG 249

                ...
gi 15833594 240 GGM 242
Cdd:cd08936 250 GGT 252
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
3-242 2.17e-32

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 118.72  E-value: 2.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07523  11 RRALVTGSSQGIGYALAEGLAQAGAEV-ILNGRDPAKLAAAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK07523  90 ILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIA-RGAGKIINIASVQSALARPGIAPYTATKGAVGN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGM-----IEMEESALKEAMSmiPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK07523 169 LTKGMATDWAKHGLQCNAIAPGYFDTPLnaalvADPEFSAWLEKRT--PAGRWGKVEELVGACVFLASDASSFVNGHVLY 246

                 ....*
gi 15833594  238 INGGM 242
Cdd:PRK07523 247 VDGGI 251
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
1-241 2.44e-32

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: 118.21  E-value: 2.44e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   1 MSRSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRL-LSFDVANREQCREVLEHEIAQHG 79
Cdd:cd08930   1 EDKIILITGAAGLIGKAFCKALLSAGARL-ILADINAPALEQLKEELTNLYKNRVIaLELDITSKESIKELIESYLEKFG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGVVSNAGI---ARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigARQG-GRIITLSSVSGVMG----NRGQ- 150
Cdd:cd08930  80 RIDILINNAYPspkVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLF--KKQGkGSIINIASIYGVIApdfrIYENt 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 151 -----VNYSAAKAGIIGATKALAIELAKRKITVNCIAPGlidtGMIEMEESALKEAMS-MIPMKRMGQAEEVAGLASYLM 224
Cdd:cd08930 158 qmyspVEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG----GILNNQPSEFLEKYTkKCPLKRMLNPEDLRGAIIFLL 233
                       250
                ....*....|....*..
gi 15833594 225 SDIAGYVTRQVISINGG 241
Cdd:cd08930 234 SDASSYVTGQNLVIDGG 250
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-242 4.21e-32

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 119.12  E-value: 4.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAqHGAWY 82
Cdd:PRK07792  13 KVAVVTGAAAGLGRAEALGLARLGATVVVNDVASALDASDVLDEIRAAGAKAVAVAGDISQRATADELVATAVG-LGGLD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIM------PMIGARQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:PRK07792  92 IVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAywrakaKAAGGPVYGRIVNTSSEAGLVGPVGQANYGAA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPgLIDTGMIE--MEESALKEAMSMIPMkrmgQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:PRK07792 172 KAGITALTLSAARALGRYGVRANAICP-RARTAMTAdvFGDAPDVEAGGIDPL----SPEHVVPLVQFLASPAAAEVNGQ 246

                 ....*...
gi 15833594  235 VISINGGM 242
Cdd:PRK07792 247 VFIVYGPM 254
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
1-241 7.05e-32

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 117.13  E-value: 7.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSV-LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEhEIAQH- 78
Cdd:PRK08063   2 FSGKVaLVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEETAEEIEALGRKALAVKANVGDVEKIKEMFA-QIDEEf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVmgnRGQVNYSA--- 155
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEA-AKLMEKVGGGKIISLSSLGSI---RYLENYTTvgv 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  156 AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEM---EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVT 232
Cdd:PRK08063 157 SKAALEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHfpnREELLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIR 236

                 ....*....
gi 15833594  233 RQVISINGG 241
Cdd:PRK08063 237 GQTIIVDGG 245
PRK06128 PRK06128
SDR family oxidoreductase;
3-243 1.52e-31

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 117.27  E-value: 1.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHY-HRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK06128  56 RKALITGADSGIGRATAIAFAREGADIALNYlPEEEQDAAEVVQLIQAEGRKAVALPGDLKDEAFCRQLVERAVKELGGL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAG--IAR-DAAfpALSDDDWDAVIHTNLDSFYNVIQPCImPMIGArqGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:PRK06128 136 DILVNIAGkqTAVkDIA--DITTEQFDATFKTNVYAMFWLCKAAI-PHLPP--GASIINTGSIQSYQPSPTLLDYASTKA 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDTGMIE---MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:PRK06128 211 AIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPsggQPPEKIPDFGSETPMKRPGQPVEMAPLYVLLASQESSYVTGEV 290

                 ....*...
gi 15833594  236 ISINGGML 243
Cdd:PRK06128 291 FGVTGGLL 298
PRK07074 PRK07074
SDR family oxidoreductase;
1-243 2.08e-31

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 116.02  E-value: 2.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGfNIGVHYHRDAtgaqETLNAIVANGGNGRLLSF--DVANREQCREVLEHEIAQH 78
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAG-DRVLALDIDA----AALAAFADALGDARFVPVacDLTDAASLAAALANAAAER 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGvMGNRGQVNYSAAKA 158
Cdd:PRK07074  76 GPVDVLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGML-KRSRGAVVNIGSVNG-MAALGHPAYSAAKA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESA----LKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:PRK07074 154 GLIHYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARVAAnpqvFEELKKWYPLQDFATPDDVANAVLFLASPAARAITGV 233

                 ....*....
gi 15833594  235 VISINGGML 243
Cdd:PRK07074 234 CLPVDGGLT 242
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-241 3.17e-31

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 115.56  E-value: 3.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASK--GIGRAIACQLAADGFNIGVHYHR--DAT---GAQETLNAIVA-----NGGNGRLLSFDVANREQCR 68
Cdd:PRK12748   4 MKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYWSpyDKTmpwGMHDKEPVLLKeeiesYGVRCEHMEIDLSQPYAPN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   69 EVLEHEIAQHGAWYGVVSNAGIArdaafpalSDDDWDAVIHTNLDSFY--NVIQPCIMPMIGARQ-----GGRIITLSS- 140
Cdd:PRK12748  84 RVFYAVSERLGDPSILINNAAYS--------THTRLEELTAEQLDKHYavNVRATMLLSSAFAKQydgkaGGRIINLTSg 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  141 -VSGVMgnRGQVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMieMEESALKEAMSMIPMKRMGQAEEVAGL 219
Cdd:PRK12748 156 qSLGPM--PDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGW--ITEELKHHLVPKFPQGRVGEPVDAARL 231
                        250       260
                 ....*....|....*....|..
gi 15833594  220 ASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK12748 232 IAFLVSEEAKWITGQVIHSEGG 253
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
1-241 4.60e-31

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 115.13  E-value: 4.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSF--DVANREQCREVLEHEIAQH 78
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAV-ADINSEKAANVAQEINAEYGEGMAYGFgaDATSEQSVLALSRGVDEIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:PRK12384  80 GRVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPG-LIDTGMIE-----------MEESALKEA-MSMIPMKRMGQAEEVAGLASYLMS 225
Cdd:PRK12384 160 GGVGLTQSLALDLAEYGITVHSLMLGnLLKSPMFQsllpqyakklgIKPDEVEQYyIDKVPLKRGCDYQDVLNMLLFYAS 239
                        250
                 ....*....|....*.
gi 15833594  226 DIAGYVTRQVISINGG 241
Cdd:PRK12384 240 PKASYCTGQSINVTGG 255
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
3-190 5.84e-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: 113.87  E-value: 5.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGPGTVILTARDVERGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDD-WDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMgnrgQVNYSAAKAGII 161
Cdd:cd05324  81 ILVNNAGIAFKGFDDSTPTREqARETMKTNFFGTVDVTQ-ALLPLLKKSPAGRIVNVSSGLGSL----TSAYGVSKAALN 155
                       170       180
                ....*....|....*....|....*....
gi 15833594 162 GATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:cd05324 156 ALTRILAKELKETGIKVNACCPGWVKTDM 184
PRK07478 PRK07478
short chain dehydrogenase; Provisional
3-241 6.60e-31

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 114.64  E-value: 6.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDAtGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07478   7 KVAIITGASSGIGRAAAKLFAREGAKVVVGARRQA-ELDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAA-FPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGV-MGNRGQVNYSAAKAGI 160
Cdd:PRK07478  86 IAFNNAGTLGEMGpVAEMSLEGWRETLATNLTSAFLGAKHQIPAML-ARGGGSLIFTSTFVGHtAGFPGMAAYAASKAGL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEM---EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK07478 165 IGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAmgdTPEALAFVAGLHALKRMAQPEEIAQAALFLASDAASFVTGTALL 244

                 ....
gi 15833594  238 INGG 241
Cdd:PRK07478 245 VDGG 248
PRK09135 PRK09135
pteridine reductase; Provisional
1-241 1.68e-30

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 113.48  E-value: 1.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQE---TLNAIVANggNGRLLSFDVANREQCREVLEHEIAQ 77
Cdd:PRK09135   5 SAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADAlaaELNALRPG--SAAALQADLLDPDALPELVAACVAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 HGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK09135  83 FGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQ-AAAPQL-RKQRGAIVNITDIHAERPLKGYPVYCAAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKrKITVNCIAPGLI-----DTGMIEMEESALkeaMSMIPMKRMGQAEEVAGLASYLMSDiAGYVT 232
Cdd:PRK09135 161 AALEMLTRSLALELAP-EVRVNAVAPGAIlwpedGNSFDEEARQAI---LARTPLKRIGTPEDIAEAVRFLLAD-ASFIT 235

                 ....*....
gi 15833594  233 RQVISINGG 241
Cdd:PRK09135 236 GQILAVDGG 244
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
3-241 2.72e-30

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 113.18  E-value: 2.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgvhYHRDatgaqetlnaIVANGGNGRLLSF---DVANREQCREVLEHEIAQHG 79
Cdd:PRK06171  10 KIIIVTGGSSGIGLAIVKELLANGANV---VNAD----------IHGGDGQHENYQFvptDVSSAEEVNHTVAEIIEKFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 AWYGVVSNAGIAR-----DAAFPA----LSDDDWDAVIHTNLDSFYNVIQPCIMPMIGaRQGGRIITLSSVSGVMGNRGQ 150
Cdd:PRK06171  77 RIDGLVNNAGINIprllvDEKDPAgkyeLNEAAFDKMFNINQKGVFLMSQAVARQMVK-QHDGVIVNMSSEAGLEGSEGQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  151 VNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLID-TGM--IEMEE----------SALKE---AMSMIPMKRMGQAE 214
Cdd:PRK06171 156 SCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEaTGLrtPEYEEalaytrgitvEQLRAgytKTSTIPLGRSGKLS 235
                        250       260
                 ....*....|....*....|....*..
gi 15833594  215 EVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK06171 236 EVADLVCYLLSDRASYITGVTTNIAGG 262
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
5-241 3.42e-30

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: 112.66  E-value: 3.42e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASV-VIADLKSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFP-ALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGA 163
Cdd:cd05365  81 VNNAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLC-APHMQKAGGGAILNISSMSSENKNVRIAAYGSSKAAVNHM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 164 TKALAIELAKRKITVNCIAPGLIDTGMI------EMEESALKEAmsmiPMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:cd05365 160 TRNLAFDLGPKGIRVNAVAPGAVKTDALasvltpEIERAMLKHT----PLGRLGEPEDIANAALFLCSPASAWVSGQVLT 235

                ....
gi 15833594 238 INGG 241
Cdd:cd05365 236 VSGG 239
PRK06123 PRK06123
SDR family oxidoreductase;
1-241 4.76e-30

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 112.18  E-value: 4.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGI-ARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMiGARQGGR---IITLSSVSGVMGNRGQ-VNYSA 155
Cdd:PRK06123  81 LDALVNNAGIlEAQMRLEQMDAARLTRIFATNVVGSFLCAREAVKRM-STRHGGRggaIVNVSSMAARLGSPGEyIDYAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  156 AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEM--EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:PRK06123 160 SKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASggEPGRVDRVKAGIPMGRGGTAEEVARAILWLLSDEASYTTG 239

                 ....*...
gi 15833594  234 QVISINGG 241
Cdd:PRK06123 240 TFIDVSGG 247
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-241 6.65e-30

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 112.19  E-value: 6.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGAS--KGIGRAIACQLAADGFNI----GVHYHRDAT-GAQETLNA-----IVANGGNGRLLSFDVANREQCREVLEH 73
Cdd:PRK12859  10 VVTGVSrlDGIGAAICKELAEAGADIfftyWTAYDKEMPwGVDQDEQIqlqeeLLKNGVKVSSMELDLTQNDAPKELLNK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   74 EIAQHGAWYGVVSNAGIARDAAFPALSDDDWDAviHTNLdsfyNVIQPCIMP-----MIGARQGGRIITLSSVSGVMGNR 148
Cdd:PRK12859  90 VTEQLGYPHILVNNAAYSTNNDFSNLTAEELDK--HYMV----NVRATTLLSsqfarGFDKKSGGRIINMTSGQFQGPMV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  149 GQVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMieMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIA 228
Cdd:PRK12859 164 GELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGW--MTEEIKQGLLPMFPFGRIGEPKDAARLIKFLASEEA 241
                        250
                 ....*....|...
gi 15833594  229 GYVTRQVISINGG 241
Cdd:PRK12859 242 EWITGQIIHSEGG 254
PRK07856 PRK07856
SDR family oxidoreductase;
3-241 7.80e-30

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 111.56  E-value: 7.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATgaqetlnaiVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07856   7 RVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAPE---------TVDGRPAEFHAADVRDPDQVAALVDAIVERHGRLD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDA----AFPALSDddwdAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:PRK07856  78 VLVNNAGGSPYAlaaeASPRFHE----KIVELNLLAPLLVAQAANAVMQQQPGGGSIVNIGSVSGRRPSPGTAAYGAAKA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKrKITVNCIAPGLIDTGMIEM---EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:PRK07856 154 GLLNLTRSLAVEWAP-KVRVNAVVVGLVRTEQSELhygDAEGIAAVAATVPLGRLATPADIAWACLFLASDLASYVSGAN 232

                 ....*.
gi 15833594  236 ISINGG 241
Cdd:PRK07856 233 LEVHGG 238
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
5-241 1.44e-29

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: 111.02  E-value: 1.44e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgvhyhrdaTGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATV--------IALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDAL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:cd05331  73 VNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQA-VAPHMKDRRTGAIVTVASNAAHVPRISMAAYGASKAALASLS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 165 KALAIELAKRKITVNCIAPGLIDTGMIEM-------EESALK---EAMSM-IPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:cd05331 152 KCLGLELAPYGVRCNVVSPGSTDTAMQRTlwhdedgAAQVIAgvpEQFRLgIPLGKIAQPADIANAVLFLASDQAGHITM 231

                ....*...
gi 15833594 234 QVISINGG 241
Cdd:cd05331 232 HDLVVDGG 239
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
3-192 2.20e-29

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


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 110.40  E-value: 2.20e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNigVHyhrdATG-AQETL-NAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYR--VI----ATArNPDKLeSLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:cd05374  75 IDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAF-LPLMRKQGSGRIVNVSSVAGLVPTPFLGPYCASKAAL 153
                       170       180       190
                ....*....|....*....|....*....|..
gi 15833594 161 IGATKALAIELAKRKITVNCIAPGLIDTGMIE 192
Cdd:cd05374 154 EALSESLRLELAPFGIKVTIIEPGPVRTGFAD 185
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
6-242 2.28e-29

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: 110.62  E-value: 2.28e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQetlnaiVANGGNGRLLSF---DVANREQCREVLEHEIAQHGAWY 82
Cdd:cd05326   8 IITGGASGIGEATARLFAKHGARVVIADIDDDAGQA------VAAELGDPDISFvhcDVTVEADVRAAVDTAVARFGRLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPAL--SDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGrIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:cd05326  82 IMFNNAGVLGAPCYSILetSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGS-IVSVASVAGVVGGLGPHAYTASKHAV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 161 IGATKALAIELAKRKITVNCIAPGLIDTGMI----EMEESALKEAM--SMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:cd05326 161 LGLTRSAATELGEHGIRVNCVSPYGVATPLLtagfGVEDEAIEEAVrgAANLKGTALRPEDIAAAVLYLASDDSRYVSGQ 240

                ....*...
gi 15833594 235 VISINGGM 242
Cdd:cd05326 241 NLVVDGGL 248
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
3-243 2.68e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 110.23  E-value: 2.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK08085  10 KNILITGSAQGIGFLLATGLAEYGAEIIIN-DITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK08085  89 VLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMV-KRQAGKIINICSMQSELGRDTITPYAASKGAVKM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKEAMSM-IPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK08085 168 LTRGMCVELARHNIQVNGIAPGYFKTEMTKalVEDEAFTAWLCKrTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVD 247

                 ....
gi 15833594  240 GGML 243
Cdd:PRK08085 248 GGML 251
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-217 2.80e-29

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 109.78  E-value: 2.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07666   8 KNALITGAGRGIGRAVAIALAKEGVNVGL-LARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSID 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK07666  87 ILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMI-ERQSGDIINISSTAGQKGAAVTSAYSASKFGVLG 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMiemeesALKEAMSMIPMKRMGQAEEVA 217
Cdd:PRK07666 166 LTESLMQEVRKHNIRVTALTPSTVATDM------AVDLGLTDGNPDKVMQPEDLA 214
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
3-243 3.17e-29

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: 110.63  E-value: 3.17e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd08935   6 KVAVITGGTGVLGGAMARALAQAGAKVAA-LGRNQEKGDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAA--------------FPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGArQGGRIITLSSVSGVMGNR 148
Cdd:cd08935  85 ILINGAGGNHPDAttdpehyepeteqnFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLEQ-KGGSIINISSMNAFSPLT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 149 GQVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTG-----MIEMEESALKEAMSMI---PMKRMGQAEEVAGLA 220
Cdd:cd08935 164 KVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPqnrklLINPDGSYTDRSNKILgrtPMGRFGKPEELLGAL 243
                       250       260
                ....*....|....*....|....
gi 15833594 221 SYLMSDIA-GYVTRQVISINGGML 243
Cdd:cd08935 244 LFLASEKAsSFVTGVVIPVDGGFS 267
PRK07326 PRK07326
SDR family oxidoreductase;
1-225 3.56e-29

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 109.72  E-value: 3.56e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVaNGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK07326   5 KGKVALITGGSKGIGFAIAEALLAEGYKVAI-TARDQKELEEAAAELN-NKGNVLGLAADVRDEADVQRAVDAIVAAFGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK07326  83 LDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPAL--KRGGGYIINISSLAGTNFFAGGAAYNASKFGL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESALKEamsmipmkrmgQAEEVAGLASYLMS 225
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPGSVAThfnGHTPSEKDAWKI-----------QPEDIAQLVLDLLK 217
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
5-192 4.72e-29

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: 109.34  E-value: 4.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRdaTGAQETLNAIVANGGNG-RLLSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARR--TDRLDELKAELLNPNPSvEVEILDVTDEERNQLVIAELEAELGGLDL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGA 163
Cdd:cd05350  79 VIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEA-ALPQFRAKGRGHLVLISSVAALRGLPGAAAYSASKAALSSL 157
                       170       180
                ....*....|....*....|....*....
gi 15833594 164 TKALAIELAKRKITVNCIAPGLIDTGMIE 192
Cdd:cd05350 158 AESLRYDVKKRGIRVTVINPGFIDTPLTA 186
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
5-192 6.30e-29

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: 109.25  E-value: 6.30e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd05339   2 VLITGGGSGIGRLLALEFAKRGAKV-VILDINEKGAEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:cd05339  81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDML-ERNHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 15833594 165 KALAIELA---KRKITVNCIAPGLIDTGMIE 192
Cdd:cd05339 160 ESLRLELKaygKPGIKTTLVCPYFINTGMFQ 190
PRK12746 PRK12746
SDR family oxidoreductase;
3-241 1.15e-28

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 108.97  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELQIRV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 G------VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIgaRQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:PRK12746  87 GtseidiLVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQ-TLPLL--RAEGRVINISSAEVRLGFTGSIAYGLS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKE-AMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:PRK12746 164 KGALNTMTLPLAKHLGERGITVNTIMPGYTKTDINAklLDDPEIRNfATNSSVFGRIGQVEDIADAVAFLASSDSRWVTG 243

                 ....*...
gi 15833594  234 QVISINGG 241
Cdd:PRK12746 244 QIIDVSGG 251
PRK07832 PRK07832
SDR family oxidoreductase;
3-192 1.17e-28

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 108.98  E-value: 1.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGN-GRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAEL-FLTDRDADGLAQTVADARALGGTvPEHRALDISDYDAVAAFAADIHAAHGSM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK07832  80 DVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLR 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDTGMIE 192
Cdd:PRK07832 160 GLSEVLRFDLARHGIGVSVVVPGAVKTPLVN 190
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
3-241 1.89e-28

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 108.19  E-value: 1.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIvanGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07067   7 KVALLTGAASGIGEAVAERYLAEGARVVI-ADIKPARARLAALEI---GPAAIAVSLDVTRQDSIDRIVAAAVERFGGID 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK07067  83 ILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGRGGKIINMASQAGRRGEALVSHYCATKAAVIS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEMEESAL------------KEAMSMIPMKRMGQAEEVAGLASYLMSDIAGY 230
Cdd:PRK07067 163 YTQSAALALIRHGINVNAIAPGVVDTPMWDQVDALFaryenrppgekkRLVGEAVPLGRMGVPDDLTGMALFLASADADY 242
                        250
                 ....*....|.
gi 15833594  231 VTRQVISINGG 241
Cdd:PRK07067 243 IVAQTYNVDGG 253
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-243 2.48e-28

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 108.04  E-value: 2.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNI-GVHYhrdaTGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK08993  14 VVTGCDTGLGQGMALGLAEAGCDIvGINI----VEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHIDIL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:PRK08993  90 VNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAPGLI---DTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK08993 170 RLMANEWAKHNINVNAIAPGYMatnNTQQLRADEQRSAEILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYTIAVDGG 249

                 ..
gi 15833594  242 ML 243
Cdd:PRK08993 250 WL 251
PRK06500 PRK06500
SDR family oxidoreductase;
1-242 2.66e-28

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 107.73  E-value: 2.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSR----SVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATG---AQETLnaivanGGNGRLLSFDVANREQCREvLEH 73
Cdd:PRK06500   1 MSRlqgkTALITGGTSGIGLETARQFLAEGARVAI-TGRDPASleaARAEL------GESALVIRADAGDVAAQKA-LAQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   74 EIAQHGAWYGVV-SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGarQGGRIITLSSVSGVMGNRGQVN 152
Cdd:PRK06500  73 ALAEAFGRLDAVfINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQ-ALLPLLA--NPASIVLNGSINAHIGMPNSSV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  153 YSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESALKEAM----SMIPMKRMGQAEEVAGLASYLMS 225
Cdd:PRK06500 150 YAASKAALLSLAKTLSGELLPRGIRVNAVSPGPVQTplyGKLGLPEATLDAVAaqiqALVPLGRFGTPEEIAKAVLYLAS 229
                        250
                 ....*....|....*..
gi 15833594  226 DIAGYVTRQVISINGGM 242
Cdd:PRK06500 230 DESAFIVGSEIIVDGGM 246
PRK12742 PRK12742
SDR family oxidoreductase;
2-241 4.92e-28

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 106.77  E-value: 4.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVHYhrdaTGAQETLNAIVANGGnGRLLSFDVANREQCREVleheIAQHGAW 81
Cdd:PRK12742   6 GKKVLVLGGSRGIGAAIVRRFVTDGANVRFTY----AGSKDAAERLAQETG-ATAVQTDSADRDAVIDV----VRKSGAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNViqpcimPMIGARQ---GGRIITLSSVSG-VMGNRGQVNYSAAK 157
Cdd:PRK12742  77 DILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHA------SVEAARQmpeGGRIIIIGSVNGdRMPVAGMAAYAASK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMiEMEESALKEAM-SMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVI 236
Cdd:PRK12742 151 SALQGMARGLARDFGPRGITINVVQPGPIDTDA-NPANGPMKDMMhSFMAIKRHGRPEEVAGMVAWLAGPEASFVTGAMH 229

                 ....*
gi 15833594  237 SINGG 241
Cdd:PRK12742 230 TIDGA 234
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
5-239 5.36e-28

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 106.57  E-value: 5.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVA----NGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:cd08939   4 VLITGGSSGIGKALAKELVKEGANVII-VARSESKLEEAVEEIEAeanaSGQKVSYISADLSDYEEVEQAFAQAVEKGGP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:cd08939  83 PDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVL-PLMKEQRPGHIVFVSSQAALVGIYGYSAYCPSKFAL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 161 IGATKALAIELAKRKITVNCIAPGLIDTGMIEMEE-------SALKEAMSMIPmkrmgqAEEVaglASYLMSDI-AGYVT 232
Cdd:cd08939 162 RGLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENktkpeetKAIEGSSGPIT------PEEA---ARIIVKGLdRGYDD 232

                ....*..
gi 15833594 233 RQVISIN 239
Cdd:cd08939 233 VFTDFIG 239
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
3-243 5.79e-28

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: 106.84  E-value: 5.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGaQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd08937   5 KVVVVTGAAQGIGRGVAERLAGEGARV-LLVDRSELV-HEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAA-FPALSDDDWDAVIHTNLdsfYNVIQPC--IMPMIGARQGGRIITLSSVSGVMGNRgqVNYSAAKAG 159
Cdd:cd08937  83 VLINNVGGTIWAKpYEHYEEEQIEAEIRRSL---FPTLWCCraVLPHMLERQQGVIVNVSSIATRGIYR--IPYSAAKGG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 160 IIGATKALAIELAKRKITVNCIAPGLIDT-------GMIEMEESA-------LKEAMSMIPMKRMGQAEEVAGLASYLMS 225
Cdd:cd08937 158 VNALTASLAFEHARDGIRVNAVAPGGTEApprkiprNAAPMSEQEkvwyqriVDQTLDSSLMGRYGTIDEQVRAILFLAS 237
                       250
                ....*....|....*...
gi 15833594 226 DIAGYVTRQVISINGGML 243
Cdd:cd08937 238 DEASYITGTVLPVGGGDL 255
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
6-243 8.04e-28

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 106.53  E-value: 8.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNI-GVHYHrdatGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK12481  12 IITGCNTGLGQGMAIGLAKAGADIvGVGVA----EAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:PRK12481  88 INNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGGKIINIASMLSFQGGIRVPSYTASKSAVMGLT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAPGLI---DTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK12481 168 RALATELSQYNINVNAIAPGYMatdNTAALRADTARNEAILERIPASRWGTPDDLAGPAIFLSSSASDYVTGYTLAVDGG 247

                 ..
gi 15833594  242 ML 243
Cdd:PRK12481 248 WL 249
PRK08267 PRK08267
SDR family oxidoreductase;
3-217 9.16e-28

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 106.56  E-value: 9.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIvaNGGNGRLLSFDVANREQCREVLeheiAQHGAWY 82
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGA-YDINEAGLAALAAEL--GAGNAWTGALDVTDRAAWDAAL----ADFAAAT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 G-----VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK08267  75 GgrldvLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAA-LPYLKATPGARVINTSSASAIYGQPGLAVYSATK 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMsmipMKRMG---QAEEVA 217
Cdd:PRK08267 154 FAVRGLTEALDLEWRRHGIRVADVMPLFVDTAMLDGTSNEVDAGS----TKRLGvrlTPEDVA 212
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
3-226 1.02e-27

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 105.85  E-value: 1.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVAnGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELQAINP-KVKATFVQCDVTSWEQLAAAFKKAIEKFGRVD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIA--RDAAFPALSDDDWDAVIHTNLDSFYNVIQPCI--MPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:cd05323  80 ILINNAGILdeKSYLFAGKLPPPWEKTIDVNLTGVINTTYLALhyMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASKH 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833594 159 GIIGATKALAIEL-AKRKITVNCIAPGLIDTGMIEMEESALKEAMSMIPMKRMgqaEEVAGLASYLMSD 226
Cdd:cd05323 160 GVVGFTRSLADLLeYKTGVRVNAICPGFTNTPLLPDLVAKEAEMLPSAPTQSP---EVVAKAIVYLIED 225
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-241 1.09e-27

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 110.71  E-value: 1.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETlNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK08324 425 ALVTGAAGGIGKATAKRLAAEGACV-VLADLDEEAAEAA-AAELGGPDRALGVACDVTDEAAVQAAFEEAALAFGGVDIV 502
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:PRK08324 503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGGSIVFIASKNAVNPGPNFGAYGAAKAAELHLV 582
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAP-------GLIDTGMIE-------MEESALkEAMSMIPM--KRMGQAEEVAGLASYLMSDIA 228
Cdd:PRK08324 583 RQLALELGPDGIRVNGVNPdavvrgsGIWTGEWIEaraaaygLSEEEL-EEFYRARNllKREVTPEDVAEAVVFLASGLL 661
                        250
                 ....*....|...
gi 15833594  229 GYVTRQVISINGG 241
Cdd:PRK08324 662 SKTTGAIITVDGG 674
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
3-243 1.49e-27

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: 105.63  E-value: 1.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRdatgAQETLNAIVANGGNGRLLSFDVANREQCREVLeheiAQHGAWY 82
Cdd:cd05351   8 KRALVTGAGKGIGRATVKALAKAGARV-VAVSR----TQADLDSLVRECPGIEPVCVDLSDWDATEEAL----GSVGPVD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd05351  79 LLVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSM---IPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:cd05351 159 LTKVMALELGPHKIRVNSVNPTVVMTDMGRDNWSDPEKAKKMlnrIPLGKFAEVEDVVNAILFLLSDKSSMTTGSTLPVD 238

                ....
gi 15833594 240 GGML 243
Cdd:cd05351 239 GGFL 242
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
3-241 3.31e-27

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 104.98  E-value: 3.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDaTGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVAIADLNQ-DGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK13394  87 ILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEM------------EESALKEAMS-MIPMKRMGQAEEVAGLASYLMSDIAG 229
Cdd:PRK13394 167 LARVLAKEGAKHNVRSHVVCPGFVRTPLVDKqipeqakelgisEEEVVKKVMLgKTVDGVFTTVEDVAQTVLFLSSFPSA 246
                        250
                 ....*....|..
gi 15833594  230 YVTRQVISINGG 241
Cdd:PRK13394 247 ALTGQSFVVSHG 258
PRK07576 PRK07576
short chain dehydrogenase; Provisional
3-241 1.10e-26

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 103.88  E-value: 1.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07576  10 KNVVVVGGTSGINLGIAQAFARAGANVAV-ASRSQEKVDAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGiardAAFPA----LSDDDWDAVIHTNLDSFYNVIQPCIMPMigARQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:PRK07576  89 VLVSGAA----GNFPApaagMSANGFKTVVDIDLLGTFNVLKAAYPLL--RRPGASIIQISAPQAFVPMPMQAHVCAAKA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLID--TGM-----IEMEESALKEAmsmIPMKRMGQAEEVAGLASYLMSDIAGYV 231
Cdd:PRK07576 163 GVDMLTRTLALEWGPEGIRVNSIVPGPIAgtEGMarlapSPELQAAVAQS---VPLKRNGTKQDIANAALFLASDMASYI 239
                        250
                 ....*....|
gi 15833594  232 TRQVISINGG 241
Cdd:PRK07576 240 TGVVLPVDGG 249
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
3-226 1.24e-26

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: 102.44  E-value: 1.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYhRDatgaQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGL-RN----PEDLAALSASGGDVEAVPYDARDPEDARALVDALRDRFGRID 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd08932  76 VLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRAL-LPALREAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRA 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTGMieMEESALKEAmsmIPMKRMGQAEEVAGLASYLMSD 226
Cdd:cd08932 155 LAHALRQEGWDHGVRVSAVCPGFVDTPM--AQGLTLVGA---FPPEEMIQPKDIANLVRMVIEL 213
PRK05650 PRK05650
SDR family oxidoreductase;
5-235 1.41e-26

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 103.58  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGaQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALADVNEEGG-EETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPALSDDDWDAVIHTNLdsfYNVIQPC--IMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK05650  82 VNNAGVASGGFFEELSLEDWDWQIAINL---MGVVKGCkaFLPLFKRQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMiemeesaLKEAMSMIP-MKRMgqaeeVAGL---ASYLMSDIAGYVTRQV 235
Cdd:PRK05650 159 LSETLLVELADDEIGVHVVCPSFFQTNL-------LDSFRGPNPaMKAQ-----VGKLlekSPITAADIADYIYQQV 223
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
3-241 1.49e-26

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: 102.94  E-value: 1.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANG-------------GNGRLLSfDVANREQCRE 69
Cdd:cd08942   7 KIVLVTGGSRGIGRMIAQGFLEAGARVIIS-ARKAEACADAAEELSAYGeciaipadlsseeGIEALVA-RVAERSDRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  70 VLeheiaqhgawygvVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMI----GARQGGRIITLSSVSGVM 145
Cdd:cd08942  85 VL-------------VNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQA-LLPLLraaaTAENPARVINIGSIAGIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 146 GNRGQV-NYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEM---EESALKEAMSMIPMKRMGQAEEVAGLAS 221
Cdd:cd08942 151 VSGLENySYGASKAAVHQLTRKLAKELAGEHITVNAIAPGRFPSKMTAFllnDPAALEAEEKSIPLGRWGRPEDMAGLAI 230
                       250       260
                ....*....|....*....|
gi 15833594 222 YLMSDIAGYVTRQVISINGG 241
Cdd:cd08942 231 MLASRAGAYLTGAVIPVDGG 250
PRK06949 PRK06949
SDR family oxidoreductase;
3-242 2.53e-26

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 102.53  E-value: 2.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLAQAGAKV-VLASRRVERLKELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMI-------GARQGGRIITLSSVSG--VMGNRGQvnY 153
Cdd:PRK06949  89 ILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKRMIarakgagNTKPGGRIINIASVAGlrVLPQIGL--Y 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  154 SAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYV 231
Cdd:PRK06949 167 CMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHhhWETEQGQKLVSMLPRKRVGKPEDLDGLLLLLAADESQFI 246
                        250
                 ....*....|.
gi 15833594  232 TRQVISINGGM 242
Cdd:PRK06949 247 NGAIISADDGF 257
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
3-189 4.92e-26

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: 101.04  E-value: 4.92e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQEtlnAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd08929   1 KAALVTGASRGIGEATARLLHAEGYRVGI-CARDEARLAA---AAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd08929  77 ALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALL-RRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLG 155
                       170       180
                ....*....|....*....|....*..
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTG 189
Cdd:cd08929 156 LSEAAMLDLREANIRVVNVMPGSVDTG 182
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
6-241 5.57e-26

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 101.85  E-value: 5.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVHYHRdATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK06113  15 IITGAGAGIGKEIAITFATAGASVVVSDIN-ADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGKVDILV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDAAFPaLSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATK 165
Cdd:PRK06113  94 NNAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVA-PEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  166 ALAIELAKRKITVNCIAPGLIDTGMI------EMEESALKEAmsmiPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISIN 239
Cdd:PRK06113 172 NMAFDLGEKNIRVNGIAPGAILTDALksvitpEIEQKMLQHT----PIRRLGQPQDIANAALFLCSPAASWVSGQILTVS 247

                 ..
gi 15833594  240 GG 241
Cdd:PRK06113 248 GG 249
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
6-243 6.35e-26

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 101.68  E-value: 6.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK07097  14 LITGASYGIGFAIAKAYAKAGATI-VFNDINQELVDKGLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDILV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATK 165
Cdd:PRK07097  93 NNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMI-KKGHGKIINICSMMSELGRETVSAYAAAKGGLKMLTK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  166 ALAIELAKRKITVNCIAPGLIDTGmiemEESALKEA-------------MSMIPMKRMGQAEEVAGLASYLMSDIAGYVT 232
Cdd:PRK07097 172 NIASEYGEANIQCNGIGPGYIATP----QTAPLRELqadgsrhpfdqfiIAKTPAARWGDPEDLAGPAVFLASDASNFVN 247
                        250
                 ....*....|.
gi 15833594  233 RQVISINGGML 243
Cdd:PRK07097 248 GHILYVDGGIL 258
PRK07985 PRK07985
SDR family oxidoreductase;
3-241 7.64e-26

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 102.38  E-value: 7.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGG-NGRLLSFDVANREQCREvLEHEiaQHGAW 81
Cdd:PRK07985  50 RKALVTGGDSGIGRAAAIAYAREGADVAISYLPVEEEDAQDVKKIIEECGrKAVLLPGDLSDEKFARS-LVHE--AHKAL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIA-RDAAFPALSD---DDWDAVIHTNLDSFYNVIQPCImPMIGArqGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK07985 127 GGLDIMALVAgKQVAIPDIADltsEQFQKTFAINVFALFWLTQEAI-PLLPK--GASIITTSSIQAYQPSPHLLDYAATK 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMI---EMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:PRK07985 204 AAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQisgGQTQDKIPQFGQQTPMKRAGQPAELAPVYVYLASQESSYVTAE 283

                 ....*..
gi 15833594  235 VISINGG 241
Cdd:PRK07985 284 VHGVCGG 290
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
5-241 8.76e-26

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 101.11  E-value: 8.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFN-IGVhyhrdatgaqeTLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:PRK08220  11 VWVTGAAQGIGYAVALAFVEAGAKvIGF-----------DQAFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   84 VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGA 163
Cdd:PRK08220  80 LVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAV-MPQFRRQRSGAIVTVGSNAAHVPRIGMAAYGASKAALTSL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  164 TKALAIELAKRKITVNCIAPGLIDTgmiEMEESALKEAMSM--------------IPMKRMGQAEEVAGLASYLMSDIAG 229
Cdd:PRK08220 159 AKCVGLELAPYGVRCNVVSPGSTDT---DMQRTLWVDEDGEqqviagfpeqfklgIPLGKIARPQEIANAVLFLASDLAS 235
                        250
                 ....*....|..
gi 15833594  230 YVTRQVISINGG 241
Cdd:PRK08220 236 HITLQDIVVDGG 247
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
3-242 9.28e-26

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: 100.73  E-value: 9.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETlnaiVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFA----EAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRID 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd09761  78 VLVNNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELI--KNKGRIINIASTRAFQSEPDSEAYAASKGGLVA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 163 ATKALAIELAkRKITVNCIAPGLIDTGMIEMEESA--LKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISING 240
Cdd:cd09761 156 LTHALAMSLG-PDIRVNCISPGWINTTEQQEFTAAplTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDG 234

                ..
gi 15833594 241 GM 242
Cdd:cd09761 235 GM 236
PRK07814 PRK07814
SDR family oxidoreductase;
6-242 1.35e-25

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 101.01  E-value: 1.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK07814  14 VVTGAGRGLGAAIALAFAEAGADV-LIAARTESQLDEVAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDIVV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATK 165
Cdd:PRK07814  93 NNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGGGSVINISSTMGRLAGRGFAAYGTAKAALAHYTR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  166 ALAIELAKRkITVNCIAPGLIDTGMIE--MEESALKEAM-SMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:PRK07814 173 LAALDLCPR-IRVNAIAPGSILTSALEvvAANDELRAPMeKATPLRRLGDPEDIAAAAVYLASPAGSYLTGKTLEVDGGL 251
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
5-241 1.78e-25

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 100.74  E-value: 1.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK08277  13 AVITGGGGVLGGAMAKELARAGAKVAI-LDRNQEKAEAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPCDIL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAG---------------IARDAAFPALSDDDWDAVIHTNldsFYNVIQPCIM---PMIGaRQGGRIITLSSVSGVMG 146
Cdd:PRK08277  92 INGAGgnhpkattdnefhelIEPTKTFFDLDEEGFEFVFDLN---LLGTLLPTQVfakDMVG-RKGGNIINISSMNAFTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  147 NRGQVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTgmiEMEESAL-----------KEAMSMIPMKRMGQAEE 215
Cdd:PRK08277 168 LTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT---EQNRALLfnedgslteraNKILAHTPMGRFGKPEE 244
                        250       260
                 ....*....|....*....|....*..
gi 15833594  216 VAGLASYLMSDIA-GYVTRQVISINGG 241
Cdd:PRK08277 245 LLGTLLWLADEKAsSFVTGVVLPVDGG 271
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
3-241 2.10e-25

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: 100.06  E-value: 2.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQEtlnaiVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:cd05371   3 LVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSPGETV-----AKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIA---------RDAAFPAlsdDDWDAVIHTNLDSFYNVIQpCIMPMIGARQG------GRIITLSSVSGVMGN 147
Cdd:cd05371  78 IVVNCAGIAvaaktynkkGQQPHSL---ELFQRVINVNLIGTFNVIR-LAAGAMGKNEPdqggerGVIINTASVAAFEGQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 148 RGQVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE-MEESALKEAMSMIPM-KRMGQAEEVAGLASYLMS 225
Cdd:cd05371 154 IGQAAYSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLLAgLPEKVRDFLAKQVPFpSRLGDPAEYAHLVQHIIE 233
                       250
                ....*....|....*.
gi 15833594 226 DiaGYVTRQVISINGG 241
Cdd:cd05371 234 N--PYLNGEVIRLDGA 247
PRK12747 PRK12747
short chain dehydrogenase; Provisional
3-241 2.13e-25

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 100.15  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANR---EQCREVLEHEIAQHG 79
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETVYEIQSNGGSAFSIGANLESLhgvEALYSSLDNELQNRT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 A---WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:PRK12747  85 GstkFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRL---RDNSRIINISSAATRISLPDFIAYSMT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKE-AMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:PRK12747 162 KGAINTMTFTLAKQLGARGITVNAILPGFIKTDMNAelLSDPMMKQyATTISAFNRLGEVEDIADTAAFLASPDSRWVTG 241

                 ....*...
gi 15833594  234 QVISINGG 241
Cdd:PRK12747 242 QLIDVSGG 249
PRK06057 PRK06057
short chain dehydrogenase; Provisional
3-242 2.26e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 100.19  E-value: 2.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQetlnaiVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK06057   8 RVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKA------AADEVGGLFVPTDVTDEDAVNALFDTAAETYGSVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIA--RDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGN-RGQVNYSAAKAG 159
Cdd:PRK06057  82 IAFNNAGISppEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMV-RQGKGSIINTASFVAVMGSaTSQISYTASKGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIEM------EESALKeaMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:PRK06057 161 VLAMSRELGVQFARQGIRVNALCPGPVNTPLLQElfakdpERAARR--LVHVPMGRFAEPEEIAAAVAFLASDDASFITA 238

                 ....*....
gi 15833594  234 QVISINGGM 242
Cdd:PRK06057 239 STFLVDGGI 247
PRK05875 PRK05875
short chain dehydrogenase; Provisional
3-241 7.25e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 99.11  E-value: 7.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNI---GVHYHRDATGAQEtlnaIVANGGNG--RLLSFDVANREQCREVLEHEIAQ 77
Cdd:PRK05875   8 RTYLVTGGGSGIGKGVAAGLVAAGAAVmivGRNPDKLAAAAEE----IEALKGAGavRYEPADVTDEDQVARAVDAATAW 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 HGAWYGVVSNAGIARD-AAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGArQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:PRK05875  84 HGRLHGVVHCAGGSETiGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRG-GGGSFVGISSIAASNTHRWFGAYGVT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKEAMSM-IPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:PRK05875 163 KSAVDHLMKLAADELGPSWVRVNSIRPGLIRTDLVApiTESPELSADYRAcTPLPRVGEVEDVANLAMFLLSDAASWITG 242

                 ....*...
gi 15833594  234 QVISINGG 241
Cdd:PRK05875 243 QVINVDGG 250
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
6-222 8.44e-25

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: 8.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGASKGIGRAIACQLAADGFNIGVHYHRdATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:cd08934   7 LVTGASSGIGEATARALAAEGAAVAIAARR-VDRLEALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDILV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  86 SNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATK 165
Cdd:cd08934  86 NNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTH-AALPHHLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSE 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15833594 166 ALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSM--IPMKRMGQAEEVAGLASY 222
Cdd:cd08934 165 GLRQEVTERGVRVVVIEPGTVDTELRDHITHTITKEAYEerISTIRKLQAEDIAAAVRY 223
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
5-239 1.21e-24

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: 97.74  E-value: 1.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVH-YHRDATGAQETLNAIVaNGGNGRLLSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:cd05367   2 IILTGASRGIGRALAEELLKRGSPSVVVlLARSEEPLQELKEELR-PGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGIARD--AAFPAlSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:cd05367  81 LINNAGSLGPvsKIEFI-DLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAARD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 162 GATKALAIELakRKITVNCIAPGLIDTGMIE--MEESALKEAMSMIP-MKRMGQ---AEEVAG-LASYLMSDIagYVTRQ 234
Cdd:cd05367 160 MFFRVLAAEE--PDVRVLSYAPGVVDTDMQReiRETSADPETRSRFRsLKEKGElldPEQSAEkLANLLEKDK--FESGA 235

                ....*
gi 15833594 235 VISIN 239
Cdd:cd05367 236 HVDYY 240
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
1-241 1.29e-24

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: 98.31  E-value: 1.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVAN-GGNGRLLSFDVANREQCrEVLEHEIAQHg 79
Cdd:cd05322   1 MNQVAVVIGGGQTLGEFLCHGLAEAGYDVAV-ADINSENAEKVADEINAEyGEKAYGFGADATNEQSV-IALSKGVDEI- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 awYG----VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSA 155
Cdd:cd05322  78 --FKrvdlLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIQGRIIQINSKSGKVGSKHNSGYSA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 156 AKAGIIGATKALAIELAKRKITVNCIAPG-LIDTGMIE-----------MEESALKEA-MSMIPMKRMGQAEEVAGLASY 222
Cdd:cd05322 156 AKFGGVGLTQSLALDLAEHGITVNSLMLGnLLKSPMFQsllpqyakklgIKESEVEQYyIDKVPLKRGCDYQDVLNMLLF 235
                       250
                ....*....|....*....
gi 15833594 223 LMSDIAGYVTRQVISINGG 241
Cdd:cd05322 236 YASPKASYCTGQSINITGG 254
PRK05855 PRK05855
SDR family oxidoreductase;
5-191 1.78e-24

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 101.21  E-value: 1.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFAREGAEV-VASDIDEAAAERTAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIV 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPALSDDDWDAVIHTNLdsfYNVIQPCIM---PMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK05855 397 VNNAGIGMAGGFLDTSAEDWDRVLDVNL---WGVIHGCRLfgrQMVERGTGGHIVNVASAAAYAPSRSLPAYATSKAAVL 473
                        170       180       190
                 ....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDTGMI 191
Cdd:PRK05855 474 MLSECLRAELAAAGIGVTAICPGFVDTNIV 503
PRK06484 PRK06484
short chain dehydrogenase; Validated
2-243 1.97e-24

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 101.08  E-value: 1.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIvanGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK06484 269 PRVVAITGGARGIGRAVADRFAAAGDRLLI-IDRDAEGAKKLAEAL---GDEHLSVQADITDEAAVESAFAQIQARWGRL 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIArDAAFPAL--SDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:PRK06484 345 DVLVNNAGIA-EVFKPSLeqSAEDFTRVYDVNLSGAFACARAAARLM---SQGGVIVNLGSIASLLALPPRNAYCASKAA 420
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDT-GMIEMEESALKEAMSM---IPMKRMGQAEEVAGLASYLMSDIAGYVTRQV 235
Cdd:PRK06484 421 VTMLSRSLACEWAPAGIRVNTVAPGYIETpAVLALKASGRADFDSIrrrIPLGRLGDPEEVAEAIAFLASPAASYVNGAT 500

                 ....*...
gi 15833594  236 ISINGGML 243
Cdd:PRK06484 501 LTVDGGWT 508
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
5-241 2.64e-24

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 97.22  E-value: 2.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANG-GNGRLLSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:cd08933  12 VIVTGGSRGIGRGIVRAFVENGAKV-VFCARGEAAGQALESELNRAGpGSCKFVPCDVTKEEDIKTLISVTVERFGRIDC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGIARDAAFP-ALSDDDWDAVIHTNLDSFYnVIQPCIMPMIGARQGGrIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:cd08933  91 LVNNAGWHPPHQTTdETSAQEFRDLLNLNLISYF-LASKYALPHLRKSQGN-IINLSSLVGSIGQKQAAPYVATKGAITA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 163 ATKALAIELAKRKITVNCIAPGLIDTGMIEM-------EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDiAGYVTRQV 235
Cdd:cd08933 169 MTKALAVDESRYGVRVNCISPGNIWTPLWEElaaqtpdTLATIKEGELAQLLGRMGTEAESGLAALFLAAE-ATFCTGID 247

                ....*.
gi 15833594 236 ISINGG 241
Cdd:cd08933 248 LLLSGG 253
PRK07024 PRK07024
SDR family oxidoreductase;
1-190 2.92e-24

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 97.31  E-value: 2.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRdaTGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK07024   1 MPLKVFITGASSGIGQALAREYARQGATLGLVARR--TDALQAFAARLPKAARVSVYAADVRDADALAAAAADFIAAHGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIAR--DAAFPAlsddDWDA---VIHTNLDSFYNVIQPCIMPMIGARQGgRIITLSSVSGVMGNRGQVNYSA 155
Cdd:PRK07024  79 PDVVIANAGISVgtLTEERE----DLAVfreVMDTNYFGMVATFQPFIAPMRAARRG-TLVGIASVAGVRGLPGAGAYSA 153
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15833594  156 AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:PRK07024 154 SKAAAIKYLESLRVELRPAGVRVVTIAPGYIRTPM 188
PRK09134 PRK09134
SDR family oxidoreductase;
3-241 3.63e-24

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 96.92  E-value: 3.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK09134  10 RAALVTGAARRIGRAIALDLAAHGFDVAVHYNRSRDEAEALAAEIRALGRRAVALQADLADEAEVRALVARASAALGPIT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSfynviqPCIMPMIGARQggriiTLSSVSGVMGNR----------GQVN 152
Cdd:PRK09134  90 LLVNNASLFEYDSAASFTRASWDRHMATNLRA------PFVLAQAFARA-----LPADARGLVVNMidqrvwnlnpDFLS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  153 YSAAKAGIIGATKALAIELAKRkITVNCIAPGLIDTGmIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSdiAGYVT 232
Cdd:PRK09134 159 YTLSKAALWTATRTLAQALAPR-IRVNAIGPGPTLPS-GRQSPEDFARQHAATPLGRGSTPEEIAAAVRYLLD--APSVT 234

                 ....*....
gi 15833594  233 RQVISINGG 241
Cdd:PRK09134 235 GQMIAVDGG 243
PRK07831 PRK07831
SDR family oxidoreductase;
3-238 6.45e-24

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 96.26  E-value: 6.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGAS-KGIGRAIACQLAADGFNIGV---HYHRDAtgaqETLNAIVANGGNGRLLSF--DVANREQCREVLEHEIA 76
Cdd:PRK07831  18 KVVLVTAAAgTGIGSATARRALEEGARVVIsdiHERRLG----ETADELAAELGLGRVEAVvcDVTSEAQVDALIDAAVE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   77 QHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:PRK07831  94 RLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVNNASVLGWRAQHGQAHYAAA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE-------MEESALKEAMSmipmkRMGQAEEVAGLASYLMSDIAG 229
Cdd:PRK07831 174 KAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAkvtsaelLDELAAREAFG-----RAAEPWEVANVIAFLASDYSS 248

                 ....*....
gi 15833594  230 YVTRQVISI 238
Cdd:PRK07831 249 YLTGEVVSV 257
PRK05717 PRK05717
SDR family oxidoreductase;
3-242 9.80e-24

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 95.73  E-value: 9.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQetlnAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSK----VAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIA--RDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGArQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK05717  87 ALVCNAAIAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHC-APYLRA-HNGAIVNLASTRARQSEPDTEAYAASKGGL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  161 IGATKALAIELAKrKITVNCIAPGLIDT-GMIEMEESALKEA-MSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISI 238
Cdd:PRK05717 165 LALTHALAISLGP-EIRVNAVSPGWIDArDPSQRRAEPLSEAdHAQHPAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFVV 243

                 ....
gi 15833594  239 NGGM 242
Cdd:PRK05717 244 DGGM 247
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
3-202 1.83e-23

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: 94.44  E-value: 1.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIvaNGGNGRLLSFDVANREQcrevLEHEIAQHGAWY 82
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGWFVGL-YDIDEDGLAALAAEL--GAENVVAGALDVTDRAA----WAAALADFAAAT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 G-----VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:cd08931  74 GgrldaLFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAAL-PYLKATPGARVINTASSSAIYGQPDLAVYSATK 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15833594 158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEM--EESALKEAM 202
Cdd:cd08931 153 FAVRGLTEALDVEWARHGIRVADVWPWFVDTPILTKgeTGAAPKKGL 199
PRK07062 PRK07062
SDR family oxidoreductase;
3-241 2.31e-23

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 95.11  E-value: 2.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLL--SFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK07062   9 RVAVVTGGSSGIGLATVELLLEAGASVAI-CGRDEERLASAEARLREKFPGARLLaaRCDVLDEADVAAFAAAVEARFGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNldsFYNVIQP--CIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:PRK07062  88 VDMLVNNAGQGRVSTFADTTDDAWRDELELK---YFSVINPtrAFLPLLRASAAASIVCVNSLLALQPEPHMVATSAARA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKE-----------AMSMIPMKRMGQAEEVAGLASYLMS 225
Cdd:PRK07062 165 GLLNLVKSLATELAPKGVRVNSILLGLVESGQWRrrYEARADPGqsweawtaalaRKKGIPLGRLGRPDEAARALFFLAS 244
                        250
                 ....*....|....*.
gi 15833594  226 DIAGYVTRQVISINGG 241
Cdd:PRK07062 245 PLSSYTTGSHIDVSGG 260
SDR_subfam_2 TIGR04504
SDR family mycofactocin-dependent oxidoreductase; Members of this protein subfamily are ...
3-242 2.41e-23

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: 94.70  E-value: 2.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     3 RSVLVTGASKGIGRAIACQLAADGFNI----------GVHYhRDATGAQetLNAIVAN-GGNGRLLSFDVANREQCREVL 71
Cdd:TIGR04504   2 RVALVTGAARGIGAATVRRLAADGWRVvavdlcaddpAVGY-PLATRAE--LDAVAAAcPDQVLPVIADVRDPAALAAAV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    72 EHEIAQHGAWYGVVSNAG-IARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQ--GGRIITLSSVSGVMGNR 148
Cdd:TIGR04504  79 ALAVERWGRLDAAVAAAGvIAGGRPLWETTDAELDLLLDVNLRGVWNLARAAVPAMLARPDprGGRFVAVASAAATRGLP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   149 GQVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMieMEESA----LKEAMSMIPMKRMGQ---AEEVAGLAS 221
Cdd:TIGR04504 159 HLAAYCAAKHAVVGLVRGLAADLGGTGVTANAVSPGSTRTAM--LAATArlygLTDVEEFAGHQLLGRllePEEVAAAVA 236
                         250       260
                  ....*....|....*....|.
gi 15833594   222 YLMSDIAGYVTRQVISINGGM 242
Cdd:TIGR04504 237 WLCSPASSAVTGSVVHADGGF 257
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
3-188 2.92e-23

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: 94.38  E-value: 2.92e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGV---HYHRDATG--------AQETLNAIVANGGNGRLLSFDVANREQCREVL 71
Cdd:cd05338   4 KVAFVTGASRGIGRAIALRLAKAGATVVVaakTASEGDNGsakslpgtIEETAEEIEAAGGQALPIVVDVRDEDQVRALV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  72 EHEIAQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQV 151
Cdd:cd05338  84 EATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAA-LPHMVKAGQGHILNISPPLSLRPARGDV 162
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15833594 152 NYSAAKAGIIGATKALAIELAKRKITVNCIAPG-LIDT 188
Cdd:cd05338 163 AYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPStAIET 200
PRK07890 PRK07890
short chain dehydrogenase; Provisional
5-241 3.61e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 94.25  E-value: 3.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK07890   8 VVVSGVGPGLGRTLAVRAARAGADV-VLAARTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDAL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAgiARDAAFPALSD---DDWDAVIHTNLDSFYNVIQPCIMPMigARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK07890  87 VNNA--FRVPSMKPLADadfAHWRAVIELNVLGTLRLTQAFTPAL--AESGGSIVMINSMVLRHSQPKYGAYKMAKGALL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLI--DT--GMIEM--------EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAG 229
Cdd:PRK07890 163 AASQSLATELGPQGIRVNSVAPGYIwgDPlkGYFRHqagkygvtVEQIYAETAANSDLKRLPTDDEVASAVLFLASDLAR 242
                        250
                 ....*....|..
gi 15833594  230 YVTRQVISINGG 241
Cdd:PRK07890 243 AITGQTLDVNCG 254
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
3-241 1.30e-22

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: 92.68  E-value: 1.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGV---HYHRDATGAQETlnaivanGGNGRLLSFDVANREQCREVLEHEIAQHG 79
Cdd:cd05363   4 KTALITGSARGIGRAFAQAYVREGARVAIadiNLEAARATAAEI-------GPAACAISLDVTDQASIDRCVAALVDRWG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:cd05363  77 SIDILVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGGKIINMASQAGRRGEALVGVYCATKAA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESAL------------KEAMSMIPMKRMGQAEEVAGLASYLMSDI 227
Cdd:cd05363 157 VISLTQSAGLNLIRHGINVNAIAPGVVDGEHWDGVDAKFaryenrprgekkRLVGEAVPFGRMGRAEDLTGMAIFLASTD 236
                       250
                ....*....|....
gi 15833594 228 AGYVTRQVISINGG 241
Cdd:cd05363 237 ADYIVAQTYNVDGG 250
PRK06198 PRK06198
short chain dehydrogenase; Provisional
3-236 3.20e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 91.61  E-value: 3.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK06198   7 KVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKGEAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK06198  87 ALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEGTIVNIGSMSAHGGQPFLAAYCASKGALAT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDT-GMIEM-------EESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQ 234
Cdd:PRK06198 167 LTRNAAYALLRNRIRVNGLNIGWMATeGEDRIqrefhgaPDDWLEKAAATQPFGRLLDPDEVARAVAFLLSDESGLMTGS 246

                 ..
gi 15833594  235 VI 236
Cdd:PRK06198 247 VI 248
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
5-241 9.39e-22

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 90.14  E-value: 9.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQeTLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd08943   4 ALVTGGASGIGLAIAKRLAAEGAAV-VVADIDPEIAE-KVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:cd08943  82 VSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 165 KALAIELAKRKITVNCIAP-----GLIDTGMIEMEESALKEAMSM------IPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:cd08943 162 RCLALEGGEDGIRVNTVNPdavfrGSKIWEGVWRAARAKAYGLLEeeyrtrNLLKREVLPEDVAEAVVAMASEDFGKTTG 241

                ....*...
gi 15833594 234 QVISINGG 241
Cdd:cd08943 242 AIVTVDGG 249
PRK06523 PRK06523
short chain dehydrogenase; Provisional
3-243 1.33e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 89.96  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVAnggngrllsfDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK06523  10 KRALVTGGTKGIGAATVARLLEAGARVVTTARSRPDDLPEGVEFVAA----------DLTTAEGCAAVARAVLERLGGVD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAA--FPALSDDDWDAVIHTNLdsFYNV-IQPCIMPMIGARQGGRIITLSSVSGVMGNRGQ-VNYSAAKA 158
Cdd:PRK06523  80 ILVHVLGGSSAPAggFAALTDEEWQDELNLNL--LAAVrLDRALLPGMIARGSGVIIHVTSIQRRLPLPEStTAYAAAKA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDT-GMIEM-----------EESALKEAMSM---IPMKRMGQAEEVAGLASYL 223
Cdd:PRK06523 158 ALSTYSKSLSKEVAPKGVRVNTVSPGWIETeAAVALaerlaeaagtdYEGAKQIIMDSlggIPLGRPAEPEEVAELIAFL 237
                        250       260
                 ....*....|....*....|
gi 15833594  224 MSDIAGYVTRQVISINGGML 243
Cdd:PRK06523 238 ASDRAASITGTEYVIDGGTV 257
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
5-217 2.04e-21

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: 89.57  E-value: 2.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRdatgaQETLNAIV---ANGGNGR--LLSFDVANREQCREVLEHEIAQHG 79
Cdd:cd05332   6 VIITGASSGIGEELAYHLARLGARLVLSARR-----EERLEEVKsecLELGAPSphVVPLDMSDLEDAEQVVEEALKLFG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNldsFYNVIQP--CIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:cd05332  81 GLDILINNAGISMRSLFHDTSIDVDRKIMEVN---YFGPVALtkAALPHLIERSQGSIVVVSSIAGKIGVPFRTAYAASK 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833594 158 AGIIGATKALAIELAKRKITVNCIAPGLIDTgmiEMEESALKEAMSMIPMKRMGQ-----AEEVA 217
Cdd:cd05332 158 HALQGFFDSLRAELSEPNISVTVVCPGLIDT---NIAMNALSGDGSMSAKMDDTTangmsPEECA 219
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
3-241 3.04e-21

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 89.23  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRdATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK12823   9 KVVVVTGAAQGIGRGVALRAAAEGARV-VLVDR-SELVHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRID 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIA-RDAAFPALSDDDWDAVIHTnldSFYNVIQPC--IMPMIGARQGGRIITLSSVS--GVmgNRgqVNYSAAK 157
Cdd:PRK12823  87 VLINNVGGTiWAKPFEEYEEEQIEAEIRR---SLFPTLWCCraVLPHMLAQGGGAIVNVSSIAtrGI--NR--VPYSAAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDT----------GMIEMEESALKEAMSMI----PMKRMGQAEEVAGLASYL 223
Cdd:PRK12823 160 GGVNALTASLAFEYAEHGIRVNAVAPGGTEApprrvprnaaPQSEQEKAWYQQIVDQTldssLMKRYGTIDEQVAAILFL 239
                        250
                 ....*....|....*...
gi 15833594  224 MSDIAGYVTRQVISINGG 241
Cdd:PRK12823 240 ASDEASYITGTVLPVGGG 257
PRK07825 PRK07825
short chain dehydrogenase; Provisional
3-191 6.20e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 88.46  E-value: 6.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFN--IGvhyHRDATGAQETLNAIvangGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALGARvaIG---DLDEALAKETAAEL----GLVVGGPLDVTDPASFAAFLDAVEADLGP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFpalsDDDWDAVIHTNLD-SFYNVIQPC--IMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK07825  79 IDVLVNNAGVMPVGPF----LDEPDAVTRRILDvNVYGVILGSklAAPRMVPRGRGHVVNVASLAGKIPVPGMATYCASK 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMI 191
Cdd:PRK07825 155 HAVVGFTDAARLELRGTGVHVSVVLPSFVNTELI 188
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
5-197 9.72e-21

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 87.35  E-value: 9.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQEtLNAIVANGGNGRLLSFDVANREQcrEVLEhEIAQHGAWYG- 83
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNTVIATCRDPSAATE-LAALGASHSRLHILELDVTDEIA--ESAE-AVAERLGDAGl 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 --VVSNAGIAR-DAAFPALSDDDWDAVIHTNldsfynVIQPCIM-----PMIGARQGGRIITLSSVSGVMGNR---GQVN 152
Cdd:cd05325  77 dvLINNAGILHsYGPASEVDSEDLLEVFQVN------VLGPLLLtqaflPLLLKGARAKIINISSRVGSIGDNtsgGWYS 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15833594 153 YSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGM----------IEMEESA 197
Cdd:cd05325 151 YRASKAALNMLTKSLAVELKRDGITVVSLHPGWVRTDMggpfaknkgpITPEESV 205
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
5-188 9.78e-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: 87.72  E-value: 9.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRL-LSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKL-ILTGRRAERLQELADELGAKFPVKVLpLQLDVSDRESIEAALENLPEEFRDIDI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGIARDAAfPALSDD--DWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:cd05346  82 LVNNAGLALGLD-PAQEADleDWETMIDTNVKGLLNVTR-LILPIMIARNQGHIINLGSIAGRYPYAGGNVYCATKAAVR 159
                       170       180
                ....*....|....*....|....*..
gi 15833594 162 GATKALAIELAKRKITVNCIAPGLIDT 188
Cdd:cd05346 160 QFSLNLRKDLIGTGIRVTNIEPGLVET 186
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
3-190 1.44e-20

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: 86.86  E-value: 1.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDV--ANREQCREVLEHEIAQHGA 80
Cdd:cd05340   5 RIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVADHINEEGGRQPQWFILDLltCTSENCQQLAQRIAVNYPR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARD-AAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:cd05340  85 LDGVLHNAGLLGDvCPLSEQNPQVWQDV*QVNVNATFMLTQAL-LPLLLKSDAGSLVFTSSSVGRQGRANWGAYAVSKFA 163
                       170       180       190
                ....*....|....*....|....*....|.
gi 15833594 160 IIGATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:cd05340 164 TEGL*QVLADEYQQRNLRVNCINPGGTRTAM 194
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
6-242 1.92e-20

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: 87.29  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     6 LVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQ---ETLNAivANGGNGRLLSFDVANR----EQCREVLEHEIAQH 78
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAAStlaAELNA--RRPNSAVTCQADLSNSatlfSRCEAIIDACFRAF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    79 GAWYGVVSNAgiardAAF---PALSDDDWDAV-----IHTNLDSFY--NVIQPCIMPMIGAR--------QGGRIITLSS 140
Cdd:TIGR02685  83 GRCDVLVNNA-----SAFyptPLLRGDAGEGVgdkksLEVQVAELFgsNAIAPYFLIKAFAQrqagtraeQRSTNLSIVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   141 VSGVMGNR---GQVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLiDTGMIEMEESALKEAMSMIPM-KRMGQAEEV 216
Cdd:TIGR02685 158 LCDAMTDQpllGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGL-SLLPDAMPFEVQEDYRRKVPLgQREASAEQI 236
                         250       260
                  ....*....|....*....|....*.
gi 15833594   217 AGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:TIGR02685 237 ADVVIFLVSPKAKYITGTCIKVDGGL 262
PRK07454 PRK07454
SDR family oxidoreductase;
1-188 2.12e-20

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 86.55  E-value: 2.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK07454   5 SMPRALITGASSGIGKATALAFAKAGWDL-ALVARSQDALEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK07454  84 PDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCS-AVLPGMRARGGGLIINVSSIAARNAFPQWGAYCVSKAAL 162
                        170       180
                 ....*....|....*....|....*...
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDT 188
Cdd:PRK07454 163 AAFTKCLAEEERSHGIRVCTITLGAVNT 190
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
5-190 2.13e-20

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: 86.50  E-value: 2.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDatgaQETLNAIVAN-----GGNGRLLSFDVANREQCREVLEHEIAqhG 79
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAKRGFNV-ILISRT----QEKLDAVAKEieekyGVETKTIAADFSAGDDIYERIEKELE--G 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWYGV-VSNAGIARD--AAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGN-RGQVnYSA 155
Cdd:cd05356  77 LDIGIlVNNVGISHSipEYFLETPEDELQDIINVNVMATLKMTR-LILPGMVKRKKGAIVNISSFAGLIPTpLLAT-YSA 154
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15833594 156 AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:cd05356 155 SKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATKM 189
PRK09072 PRK09072
SDR family oxidoreductase;
2-217 9.40e-20

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 84.99  E-value: 9.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDAtGAQETLNAIVANGGNGRLLSFDVANrEQCREVLEHEIAQHGAW 81
Cdd:PRK09072   5 DKRVLLTGASGGIGQALAEALAAAGARLLLV-GRNA-EKLEALAARLPYPGRHRWVVADLTS-EAGREAVLARAREMGGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK09072  82 NVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTR-ALLPLLRAQPSAMVVNVGSTFGSIGYPGYASYCASKFALR 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSmipmKRMGQAEEVA 217
Cdd:PRK09072 161 GFSEALRRELADTGVRVLYLAPRATRTAMNSEAVQALNRALG----NAMDDPEDVA 212
PRK06181 PRK06181
SDR family oxidoreductase;
5-188 1.37e-19

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 84.64  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK06181   4 VIITGASEGIGRALAVRLARAGAQL-VLAARNETRLASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPALSDDDW-DAVIHTN-LDSFYnviqpCI---MPMIGARQGgRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:PRK06181  83 VNNAGITMWSRFDELTDLSVfERVMRVNyLGAVY-----CThaaLPHLKASRG-QIVVVSSLAGLTGVPTRSGYAASKHA 156
                        170       180
                 ....*....|....*....|....*....
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDT 188
Cdd:PRK06181 157 LHGFFDSLRIELADDGVAVTVVCPGFVAT 185
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
3-156 2.06e-19

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: 82.53  E-value: 2.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594      3 RSVLVTGASKGIGRAIACQLAAdgfnigvHYHR----------DATGAQETLNAIVANGGNGRLLSFDVANREQCREVLE 72
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAE-------RGARrlvllsrsgpDAPGAAALLAELEAAGARVTVVACDVADRDALAAVLA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     73 HEIAQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpcimpMIGARQGGRIITLSSVSGVMGNRGQVN 152
Cdd:smart00822  74 AIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHE-----LTADLPLDFFVLFSSIAGVLGSPGQAN 148

                   ....
gi 15833594    153 YSAA 156
Cdd:smart00822 149 YAAA 152
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
5-224 2.48e-19

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: 82.56  E-value: 2.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADG-FNIGVHYHRDAtgaqetlnaivanggngrllsfdvanreqcrevleheiaqhgawyg 83
Cdd:cd02266   1 VLVTGGSGGIGGAIARWLASRGsPKVLVVSRRDV---------------------------------------------- 34
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGA 163
Cdd:cd02266  35 VVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLE-AARELMKAKRLGRFILISSVAGLFGAPGLGGYAASKAALDGL 113
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833594 164 TKALAIELAKRKITVNCIAPGLI-DTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLM 224
Cdd:cd02266 114 AQQWASEGWGNGLPATAVACGTWaGSGMAKGPVAPEEILGNRRHGVRTMPPEEVARALLNAL 175
PRK08265 PRK08265
short chain dehydrogenase; Provisional
6-241 3.25e-19

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 83.52  E-value: 3.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIvanGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVV 85
Cdd:PRK08265  10 IVTGGATLIGAAVARALVAAGARVAI-VDIDADNGAAVAASL---GERARFIATDITDDAAIERAVATVVARFGRVDILV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   86 SNAGIARDAAFPAlSDDDWDAVIHTNLDSFYNVIQPCIMPMigARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGATK 165
Cdd:PRK08265  86 NLACTYLDDGLAS-SRADWLAALDVNLVSAAMLAQAAHPHL--ARGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLTR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  166 ALAIELAKRKITVNCIAPG-----LIDTGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISING 240
Cdd:PRK08265 163 SMAMDLAPDGIRVNSVSPGwtwsrVMDELSGGDRAKADRVAAPFHLLGRVGDPEEVAQVVAFLCSDAASFVTGADYAVDG 242

                 .
gi 15833594  241 G 241
Cdd:PRK08265 243 G 243
PRK09186 PRK09186
flagellin modification protein A; Provisional
5-241 6.96e-19

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 82.73  E-value: 6.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNgRLLSF---DVANREQCREVLEHEIAQHGAW 81
Cdd:PRK09186   7 ILITGAGGLIGSALVKAILEAGGIV-IAADIDKEALNELLESLGKEFKS-KKLSLvelDITDQESLEEFLSKSAEKYGKI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNA---GIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQ-------- 150
Cdd:PRK09186  85 DGAVNCAyprNKDYGKKFFDVSLDDFNENLSLHLGSSFLFSQQFAKYFK-KQGGGNLVNISSIYGVVAPKFEiyegtsmt 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  151 --VNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSmipMKRMGQAEEVAGLASYLMSDIA 228
Cdd:PRK09186 164 spVEYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGGILDNQPEAFLNAYKKCCN---GKGMLDPDDICGTLVFLLSDQS 240
                        250
                 ....*....|...
gi 15833594  229 GYVTRQVISINGG 241
Cdd:PRK09186 241 KYITGQNIIVDDG 253
PRK12744 PRK12744
SDR family oxidoreductase;
3-241 1.12e-18

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 82.09  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFN-IGVHYHRDAT--GAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHG 79
Cdd:PRK12744   9 KVVLIAGGAKNLGGLIARDLAAQGAKaVAIHYNSAASkaDAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLssVSGVMG--NRGQVNYSAAK 157
Cdd:PRK12744  89 RPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHL---NDNGKIVTL--VTSLLGafTPFYSAYAGSK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESA-----LKEAMSMIPMKRMG--QAEEVAGLASYLMSDiAGY 230
Cdd:PRK12744 164 APVEHFTRAASKEFGARGISVTAVGPGPMDTPFFYPQEGAeavayHKTAAALSPFSKTGltDIEDIVPFIRFLVTD-GWW 242
                        250
                 ....*....|.
gi 15833594  231 VTRQVISINGG 241
Cdd:PRK12744 243 ITGQTILINGG 253
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
3-242 7.61e-18

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 80.00  E-value: 7.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLN----AIVANGGngrllsfDVANREQCREVLEHEIAQH 78
Cdd:PRK06200   7 QVALITGGGSGIGRALVERFLAEGARVAV-LERSAEKLASLRQrfgdHVLVVEG-------DVTSYADNQRAVDQTVDAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGI----ARDAAFPALS-DDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSsVSGVMGNRGQVNY 153
Cdd:PRK06200  79 GKLDCFVGNAGIwdynTSLVDIPAETlDTAFDEIFNVNVKGYLLGAKAAL-PALKASGGSMIFTLS-NSSFYPGGGGPLY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  154 SAAKAGIIGATKALAIELAKrKITVNCIAPGLIDTGM-----IEMEESALK-------EAMSMIPMKRMGQAEEVAGLAS 221
Cdd:PRK06200 157 TASKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTDLrgpasLGQGETSISdspgladMIAAITPLQFAPQPEDHTGPYV 235
                        250       260
                 ....*....|....*....|..
gi 15833594  222 YLMSD-IAGYVTRQVISINGGM 242
Cdd:PRK06200 236 LLASRrNSRALTGVVINADGGL 257
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
3-204 1.19e-17

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: 79.43  E-value: 1.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNigvHYHRDAT----GAQETLNAIV--ANGGNGRLLSFDVANRE---QCRE-VLE 72
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLASDPSK---RFKVYATmrdlKKKGRLWEAAgaLAGGTLETLQLDVCDSKsvaAAVErVTE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  73 HEIAQhgawygVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVN 152
Cdd:cd09806  78 RHVDV------LVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQA-FLPDMKRRGSGRILVTSSVGGLQGLPFNDV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15833594 153 YSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTgmiEMEESALKEAMSM 204
Cdd:cd09806 151 YCASKFALEGLCESLAVQLLPFNVHLSLIECGPVHT---AFMEKVLGSPEEV 199
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-241 1.32e-17

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 79.03  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQEtLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK05786   6 KKVAIIGVSEGLGYAVAYFALKEGAQV-CINSRNENKLKR-MKKTLSKYGNIHYVVGDVSSTESARNVIEKAAKVLNAID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDddWDAVIHTNLDSFYNVIQpCIMPMIgaRQGGRIITLSSVSGV-MGNRGQVNYSAAKAGII 161
Cdd:PRK05786  84 GLVVTVGGYVEDTVEEFSG--LEEMLTNHIKIPLYAVN-ASLRFL--KEGSSIVLVSSMSGIyKASPDQLSYAVAKAGLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDtGMIEMEESALKeamsmipMKRMGQA----EEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK05786 159 KAVEILASELLGRGIRVNGIAPTTIS-GDFEPERNWKK-------LRKLGDDmappEDFAKVIIWLLTDEADWVDGVVIP 230

                 ....
gi 15833594  238 INGG 241
Cdd:PRK05786 231 VDGG 234
PRK08263 PRK08263
short chain dehydrogenase; Provisional
1-189 2.26e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 78.93  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDAtgaqETLNAIVANGGNGRL-LSFDVANREQCREVLEHEIAQHG 79
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRV-VATARDT----ATLADLAEKYGDRLLpLALDVTDRAAVFAAVETAVEHFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:PRK08263  77 RLDIVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQ-AVLPYLREQRSGHIIQISSIGGISAFPMSGIYHASKWA 155
                        170       180       190
                 ....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDTG 189
Cdd:PRK08263 156 LEGMSEALAQEVAEFGIKVTLVEPGGYSTD 185
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
4-242 2.28e-17

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: 78.55  E-value: 2.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   4 SVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETlnaIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:cd05348   6 VALITGGGSGLGRALVERFVAEGAKVAV-LDRSAEKVAEL---RADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGI-ARDAAFPALS----DDDWDAVIHTNLDSFYNVIQPCiMPMIGARQGGRIITLSsVSGVMGNRGQVNYSAAKA 158
Cdd:cd05348  82 FIGNAGIwDYSTSLVDIPeeklDEAFDELFHINVKGYILGAKAA-LPALYATEGSVIFTVS-NAGFYPGGGGPLYTASKH 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 159 GIIGATKALAIELAKrKITVNCIAPGLIDT--------GMIEMEESA--LKEAM-SMIPMKRMGQAEEVAGLASYLMS-D 226
Cdd:cd05348 160 AVVGLVKQLAYELAP-HIRVNGVAPGGMVTdlrgpaslGQGETSISTppLDDMLkSILPLGFAPEPEDYTGAYVFLASrG 238
                       250
                ....*....|....*.
gi 15833594 227 IAGYVTRQVISINGGM 242
Cdd:cd05348 239 DNRPATGTVINYDGGM 254
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
5-188 5.70e-17

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: 77.04  E-value: 5.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAKVVL-AARSAEALHELAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDTW 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFPALSDDDWDAVIHTN-LDSFYNVIQPciMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGA 163
Cdd:cd05360  82 VNNAGVAVFGRFEDVTPEEFRRVFDVNyLGHVYGTLAA--LPHLRRRGGGALINVGSLLGYRSAPLQAAYSASKHAVRGF 159
                       170       180
                ....*....|....*....|....*..
gi 15833594 164 TKALAIELAK--RKITVNCIAPGLIDT 188
Cdd:cd05360 160 TESLRAELAHdgAPISVTLVQPTAMNT 186
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
3-208 5.76e-17

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: 76.96  E-value: 5.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVhyhrdaTG-AQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:cd05370   6 NTVLITGGTSGIGLALARKFLEAGNTVII------TGrREERLAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  82 YGVVSNAGIARDAAFPALSD--DDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:cd05370  80 DILINNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIK-AFLPHLKKQPEATIVNVSSGLAFVPMAANPVYCATKAA 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15833594 160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSMIPMK 208
Cdd:cd05370 159 LHSYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKMPLD 207
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
3-198 7.85e-17

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: 77.26  E-value: 7.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGNGR--LLSFDVANREQCREVLEHEIAQHGA 80
Cdd:cd05327   2 KVVVITGANSGIGKETARELAKRGAHVIIA-CRNEEKGEEAAAEIKKETGNAKveVIQLDLSSLASVRQFAEEFLARFPR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARDAAfpALSDDDWDAVIHTN-LDSFY--NVIQPCIMpmigARQGGRIITLSSVSGVMGNRGQVN----- 152
Cdd:cd05327  81 LDILINNAGIMAPPR--RLTKDGFELQFAVNyLGHFLltNLLLPVLK----ASAPSRIVNVSSIAHRAGPIDFNDldlen 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15833594 153 ---------YSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESAL 198
Cdd:cd05327 155 nkeyspykaYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSFF 209
PRK08416 PRK08416
enoyl-ACP reductase;
1-241 9.74e-17

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 77.12  E-value: 9.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGG-NGRLLSFDVANREQCREVLEHEIAQHG 79
Cdd:PRK08416   7 KGKTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEANKIAEDLEQKYGiKAKAYPLNILEPETYKELFKKIDEDFD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 AWYGVVSNAGIARDAA------FPALSDDDWDAVIHTNLDSFYNVIQPCI--MPMIGarqGGRIITLSSVsgvmGNRGQV 151
Cdd:PRK08416  87 RVDFFISNAIISGRAVvggytkFMRLKPKGLNNIYTATVNAFVVGAQEAAkrMEKVG---GGSIISLSST----GNLVYI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  152 -NYSA---AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEM-----EESALKEAMSmiPMKRMGQAEEVAGLASY 222
Cdd:PRK08416 160 eNYAGhgtSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAftnyeEVKAKTEELS--PLNRMGQPEDLAGACLF 237
                        250
                 ....*....|....*....
gi 15833594  223 LMSDIAGYVTRQVISINGG 241
Cdd:PRK08416 238 LCSEKASWLTGQTIVVDGG 256
PRK06482 PRK06482
SDR family oxidoreductase;
1-189 2.57e-16

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 75.92  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRdaTGAQETLNAivANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:PRK06482   1 MSKTWFITGASSGFGRGMTERLLARGDRVAATVRR--PDALDDLKA--RYGDRLWVLQLDVTDSAAVRAVVDRAFAALGR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK06482  77 IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAAL-PHLRRQGGGRIVQVSSEGGQIAYPGFSLYHATKWGI 155
                        170       180
                 ....*....|....*....|....*....
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTG 189
Cdd:PRK06482 156 EGFVEAVAQEVAPFGIEFTIVEPGPARTN 184
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
5-204 2.68e-16

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: 76.16  E-value: 2.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNI--GVhYHRDATGAQEtLNAIvaNGGNGRLLSFDVANREQCREVLEH---EIAQHG 79
Cdd:cd09805   3 VLITGCDSGFGNLLAKKLDSLGFTVlaGC-LTKNGPGAKE-LRRV--CSDRLRTLQLDVTKPEQIKRAAQWvkeHVGEKG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  80 AWyGVVSNAGIArdaAFPALSD----DDWDAVIHTNLDSFYNVIQpCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSA 155
Cdd:cd09805  79 LW-GLVNNAGIL---GFGGDEEllpmDDYRKCMEVNLFGTVEVTK-AFLPLL-RRAKGRVVNVSSMGGRVPFPAGGAYCA 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15833594 156 AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSM 204
Cdd:cd09805 153 SKAAVEAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKKL 201
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
3-225 5.34e-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: 5.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRdATGAQETLNAIVANGGNGRLLSF--DVANREQCREVLEHEIAQHGA 80
Cdd:cd05343   7 RVALVTGASVGIGAAVARALVQHGMKV-VGCAR-RVDKIEALAAECQSAGYPTLFPYqcDLSNEEQILSMFSAIRTQHQG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARDAAFPALSDDDWDAVIHTnldsfyNVIQPCI--------MPMIGARQgGRIITLSSVSG---VMGNRG 149
Cdd:cd05343  85 VDVCINNAGLARPEPLLSGKTEGWKEMFDV------NVLALSIctreayqsMKERNVDD-GHIININSMSGhrvPPVSVF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 150 QVnYSAAKAGIIGATKALAIEL--AKRKITVNCIAPGLIDTGMIEM--EESALKEAMSMIPMKRMgQAEEVAGLASYLMS 225
Cdd:cd05343 158 HF-YAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKlhDNDPEKAAATYESIPCL-KPEDVANAVLYVLS 235
PRK08251 PRK08251
SDR family oxidoreductase;
1-192 5.60e-16

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 74.59  E-value: 5.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRdaTGAQETLNA-IVANGGNGRLL--SFDVANREQCREVLEHEIAQ 77
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKGRDLALCARR--TDRLEELKAeLLARYPGIKVAvaALDVNDHDQVFEVFAEFRDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 HGAWYGVVSNAGIARDAAfpaLSDDDWDAVIHTNLDSFYNVIQPC--IMPMIGARQGGRIITLSSVSGVMGNRGQVN-YS 154
Cdd:PRK08251  79 LGGLDRVIVNAGIGKGAR---LGTGKFWANKATAETNFVAALAQCeaAMEIFREQGSGHLVLISSVSAVRGLPGVKAaYA 155
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15833594  155 AAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE 192
Cdd:PRK08251 156 ASKAGVASLGEGLRAELAKTPIKVSTIEPGYIRSEMNA 193
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
5-190 1.15e-15

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: 73.66  E-value: 1.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVhyhrdaTG-AQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:COG3967   8 ILITGGTSGIGLALAKRLHARGNTVII------TGrREEKLEEAAAANPGLHTIVLDVADPASIAALAEQVTAEFPDLNV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGIAR--DAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:COG3967  82 LINNAGIMRaeDLLDEAEDLADAEREITTNLLGPIRLTAAFL-PHLKAQPEAAIVNVSSGLAFVPLAVTPTYSATKAALH 160
                       170       180
                ....*....|....*....|....*....
gi 15833594 162 GATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:COG3967 161 SYTQSLRHQLKDTSVKVIELAPPAVDTDL 189
PRK07041 PRK07041
SDR family oxidoreductase;
6-241 1.56e-15

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 73.15  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIGVhyhrdATGAQETLNAIVA---NGGNGRLLSFDVANREQCREVLeheiAQHGAWY 82
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTI-----ASRSRDRLAAAARalgGGAPVRTAALDITDEAAVDAFF----AEAGPFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPmigarQGGriiTLSSVSGVMGNR---GQVNYSAAKAG 159
Cdd:PRK07041  72 HVVITAADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAARIA-----PGG---SLTFVSGFAAVRpsaSGVLQGAINAA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAkrKITVNCIAPGLIDT----GMIEMEESALKEAMSM-IPMKRMGQAEEVAGLASYLMSDiaGYVTRQ 234
Cdd:PRK07041 144 LEALARGLALELA--PVRVNTVSPGLVDTplwsKLAGDAREAMFAAAAErLPARRVGQPEDVANAILFLAAN--GFTTGS 219

                 ....*..
gi 15833594  235 VISINGG 241
Cdd:PRK07041 220 TVLVDGG 226
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
4-158 1.77e-15

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: 71.82  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     4 SVLVTGASKGIGRAIACQLAADGF-NIGVHYHRDATG--AQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA 80
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGArHLVLLSRSAAPRpdAQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    81 WYGVVSNAGIARDAAFPALSDDDWDAVI---------------HTNLDSFynviqpcimpmigarqggriITLSSVSGVM 145
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLapkvtgtwnlheatpDEPLDFF--------------------VLFSSIAGLL 141
                         170
                  ....*....|...
gi 15833594   146 GNRGQVNYSAAKA 158
Cdd:pfam08659 142 GSPGQANYAAANA 154
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
6-242 1.87e-15

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: 73.13  E-value: 1.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGA--SKGIGRAIACQLAADGFNIGVHYHRDAtgAQETLNAIVANGGNGRLLSFDVANREQCREVLEhEIAQH-GAWY 82
Cdd:COG0623   9 LITGVanDRSIAWGIAKALHEEGAELAFTYQGEA--LKKRVEPLAEELGSALVLPCDVTDDEQIDALFD-EIKEKwGKLD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVV-SnagIA---RDAAFPALSDDDWDAVIHTnLD----SFYNVIQPCiMPMIgaRQGGRIITLSSVS--------GVMG 146
Cdd:COG0623  86 FLVhS---IAfapKEELGGRFLDTSREGFLLA-MDisaySLVALAKAA-EPLM--NEGGSIVTLTYLGaervvpnyNVMG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 147 nrgqvnysAAKAGIIGATKALAIELAKRKITVNCIAPGLIDT-------GMIEMeesaLKEAMSMIPMKRMGQAEEVAGL 219
Cdd:COG0623 159 --------VAKAALEASVRYLAADLGPKGIRVNAISAGPIKTlaasgipGFDKL----LDYAEERAPLGRNVTIEEVGNA 226
                       250       260
                ....*....|....*....|...
gi 15833594 220 ASYLMSDIAGYVTRQVISINGGM 242
Cdd:COG0623 227 AAFLLSDLASGITGEIIYVDGGY 249
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
3-231 2.49e-15

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: 74.34  E-value: 2.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAAdgfnigvHYHR---------DATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEh 73
Cdd:cd05274 151 GTYLITGGLGGLGLLVARWLAA-------RGARhlvllsrrgPAPRAAARAALLRAGGARVSVVRCDVTDPAALAALLA- 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  74 EIAQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMpmigaRQGGRIITLSSVSGVMGNRGQVNY 153
Cdd:cd05274 223 ELAAGGPLAGVIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPD-----LPLDFFVLFSSVAALLGGAGQAAY 297
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 154 SAAKAgiigATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALK--EAMSMIPMKRmgqAEEVAGLASYLMSDIAGYV 231
Cdd:cd05274 298 AAANA----FLDALAAQRRRRGLPATSVQWGAWAGGGMAAAAALRArlARSGLGPLAP---AEALEALEALLASDAPQAV 370
PRK08264 PRK08264
SDR family oxidoreductase;
3-190 3.37e-15

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 72.23  E-value: 3.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLaadgfnigvhYHRDAT----GAQETlnAIVANGGNGRL-LSFDVANREQCREVLEH---- 73
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQL----------LARGAAkvyaAARDP--ESVTDLGPRVVpLQLDVTDPASVAAAAEAasdv 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   74 EIaqhgawygVVSNAGIARDAAFPALSD-DDWDAVIHTNldsFYNVIQPC--IMPMIGARQGGRIITLSSVSGVMGNRGQ 150
Cdd:PRK08264  75 TI--------LVNNAGIFRTGSLLLEGDeDALRAEMETN---YFGPLAMAraFAPVLAANGGGAIVNVLSVLSWVNFPNL 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15833594  151 VNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:PRK08264 144 GTYSASKAAAWSLTQALRAELAPQGTRVLGVHPGPIDTDM 183
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
2-220 3.90e-15

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 72.48  E-value: 3.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   2 SRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEhEIAQH--- 78
Cdd:cd09763   3 GKIALVTGASRGIGRGIALQLGEAGATVYITGRTILPQLPGTAEEIEARGGKCIPVRCDHSDDDEVEALFE-RVAREqqg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  79 -------GAWyGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFY--NVIQPCIMPMIGArqgGRIITLSSVSGVMgNRG 149
Cdd:cd09763  82 rldilvnNAY-AAVQLILVGVAKPFWEEPPTIWDDINNVGLRAHYacSVYAAPLMVKAGK---GLIVIISSTGGLE-YLF 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833594 150 QVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE--MEESALKEAMSMIPMKRMGQAEEVAGLA 220
Cdd:cd09763 157 NVAYGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLemPEDDEGSWHAKERDAFLNGETTEYSGRC 229
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
6-156 4.64e-15

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: 73.56  E-value: 4.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGASKGIGRAIACQLAADgFNIGVH------YHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHG 79
Cdd:cd08953 209 LVTGGAGGIGRALARALARR-YGARLVllgrspLPPEEEWKAQTLAALEALGARVLYISADVTDAAAVRRLLEKVRERYG 287
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833594  80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpcimpMIGARQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:cd08953 288 AIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQ-----ALADEPLDFFVLFSSVSAFFGGAGQADYAAA 359
PRK06125 PRK06125
short chain dehydrogenase; Provisional
2-242 6.19e-15

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 72.00  E-value: 6.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGfnigVHYH---RDATGAQETLNAIVANGGNG-RLLSFDVANREQCREVLeheiAQ 77
Cdd:PRK06125   7 GKRVLITGASKGIGAAAAEAFAAEG----CHLHlvaRDADALEALAADLRAAHGVDvAVHALDLSSPEAREQLA----AE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 HGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIItlsSVSGVMGNRGQVNY---S 154
Cdd:PRK06125  79 AGDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTR-LAYPRMKARGSGVIV---NVIGAAGENPDADYicgS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  155 AAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEM-----------EESALKEAMSMIPMKRMGQAEEVAGLASYL 223
Cdd:PRK06125 155 AGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTllkgraraelgDESRWQELLAGLPLGRPATPEEVADLVAFL 234
                        250
                 ....*....|....*....
gi 15833594  224 MSDIAGYVTRQVISINGGM 242
Cdd:PRK06125 235 ASPRSGYTSGTVVTVDGGI 253
PRK05876 PRK05876
short chain dehydrogenase; Provisional
3-195 6.45e-15

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 72.30  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK05876   7 RGAVITGGASGIGLATGTEFARRGARV-VLGDVDKPGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIG 162
Cdd:PRK05876  86 VVFSNAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVG 165
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15833594  163 ATKALAIELAKRKITVNCIAPGLIDTGMIEMEE 195
Cdd:PRK05876 166 LAETLAREVTADGIGVSVLCPMVVETNLVANSE 198
PRK06182 PRK06182
short chain dehydrogenase; Validated
2-189 1.57e-14

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 71.14  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVhyhrdATGAQETLNAIVANGgnGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK06182   3 KKVALVTGASSGIGKATARRLAAQGYTVYG-----AARRVDKMEDLASLG--VHPLSLDVTDEASIKAAVDTIIAEEGRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:PRK06182  76 DVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQ-LVLPHMRAQRSGRIINISSMGGKIYTPLGAWYHATKFALE 154
                        170       180
                 ....*....|....*....|....*...
gi 15833594  162 GATKALAIELAKRKITVNCIAPGLIDTG 189
Cdd:PRK06182 155 GFSDALRLEVAPFGIDVVVIEPGGIKTE 182
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
3-243 1.94e-14

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: 70.30  E-value: 1.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyhrDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEiaqhGAWY 82
Cdd:cd05361   2 SIALVTHARHFAGPASAEALTEDGYTVVCH---DASFADAAERQAFESENPGTKALSEQKPEELVDAVLQAG----GAID 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GVVSNAGIARDaaFPALsDDDWDAVIHTNLDSFynVIQPCIM-----PMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:cd05361  75 VLVSNDYIPRP--MNPI-DGTSEADIRQAFEAL--SIFPFALlqaaiAQMKKAGGGSIIFITSAVPKKPLAYNSLYGPAR 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 158 AGIIGATKALAIELAKRKITVNCIAPGLID------TGMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYV 231
Cdd:cd05361 150 AAAVALAESLAKELSRDNILVYAIGPNFFNsptyfpTSDWENNPELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPI 229
                       250
                ....*....|..
gi 15833594 232 TRQVISINGGML 243
Cdd:cd05361 230 TGQFFAFAGGYL 241
PRK07775 PRK07775
SDR family oxidoreductase;
3-190 7.81e-14

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 69.01  E-value: 7.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHYHRdATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07775  11 RPALVAGASSGIGAATAIELAAAGFPVALGARR-VEKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGiarDAAFPAL---SDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:PRK07775  90 VLVSGAG---DTYFGKLheiSTEQFESQVQIHLVGANRLATAVLPGMI-ERRRGDLIFVGSDVALRQRPHMGAYGAAKAG 165
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:PRK07775 166 LEAMVTNLQMELEGTGVRASIVHPGPTLTGM 196
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
3-241 1.01e-13

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 68.59  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGAS--KGIGRAIACQLAADGFNIGVHYHRDATGAQET-LNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHG 79
Cdd:PRK07370   7 KKALVTGIAnnRSIAWGIAQQLHAAGAELGITYLPDEKGRFEKkVRELTEPLNPSLFLPCDVQDDAQIEETFETIKQKWG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 AWYGVVSNAGIAR----DAAFPALSDDDWdaviHTNLD-SFYNVIQPCIMPMIGARQGGRIITLSSVSGVmgnRGQVNYS 154
Cdd:PRK07370  87 KLDILVHCLAFAGkeelIGDFSATSREGF----ARALEiSAYSLAPLCKAAKPLMSEGGSIVTLTYLGGV---RAIPNYN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  155 ---AAKAGIIGATKALAIELAKRKITVNCIAPGLIDTgmieMEESALKEAMSMI-------PMKRMGQAEEVAGLASYLM 224
Cdd:PRK07370 160 vmgVAKAALEASVRYLAAELGPKNIRVNAISAGPIRT----LASSAVGGILDMIhhveekaPLRRTVTQTEVGNTAAFLL 235
                        250
                 ....*....|....*..
gi 15833594  225 SDIAGYVTRQVISINGG 241
Cdd:PRK07370 236 SDLASGITGQTIYVDAG 252
PRK08339 PRK08339
short chain dehydrogenase; Provisional
3-243 1.02e-13

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 68.73  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGG-NGRLLSFDVANREQCREVLEhEIAQHGAW 81
Cdd:PRK08339   9 KLAFTTASSKGIGFGVARVLARAGADV-ILLSRNEENLKKAREKIKSESNvDVSYIVADLTKREDLERTVK-ELKNIGEP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAFPALSDDDWDAVIHTNL-DSFYnvIQPCIMPMIGARQGGRIITLSSVS--GVMGNRGQVNysAAKA 158
Cdd:PRK08339  87 DIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLyPAVY--LTRALVPAMERKGFGRIIYSTSVAikEPIPNIALSN--VVRI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDTG-MIEME-----------ESALKEAMSMIPMKRMGQAEEVAGLASYLMSD 226
Cdd:PRK08339 163 SMAGLVRTLAKELGPKGITVNGIMPGIIRTDrVIQLAqdrakregksvEEALQEYAKPIPLGRLGEPEEIGYLVAFLASD 242
                        250
                 ....*....|....*..
gi 15833594  227 IAGYVTRQVISINGGML 243
Cdd:PRK08339 243 LGSYINGAMIPVDGGRL 259
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
3-201 1.26e-13

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 68.17  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADgfniGVHYHRDATGAQETLNAIvANGGNGRLLSF-----DVANREQCREVLEHEIAQ 77
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEK----GTHVISISRTENKELTKL-AEQYNSNLTFHsldlqDVHELETNFNEILSSIQE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 H--GAWYgVVSNAGIAR--DAAFPALSDDdwdavIHTNLDsfYNVIQPCI-----MPMIGARQGG-RIITLSSVSGVMGN 147
Cdd:PRK06924  77 DnvSSIH-LINNAGMVApiKPIEKAESEE-----LITNVH--LNLLAPMIltstfMKHTKDWKVDkRVINISSGAAKNPY 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15833594  148 RGQVNYSAAKAGIIGATKALAIELAKRKITVNCIA--PGLIDTGMIEMEESALKEA 201
Cdd:PRK06924 149 FGWSAYCSSKAGLDMFTQTVATEQEEEEYPVKIVAfsPGVMDTNMQAQIRSSSKED 204
PRK07109 PRK07109
short chain dehydrogenase; Provisional
2-188 1.66e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 68.79  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHG-- 79
Cdd:PRK07109   8 RQVVVITGASAGVGRATARAFARRGAKVVL-LARGEEGLEALAAEIRAAGGEALAVVADVADAEAVQAAADRAEEELGpi 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 -AWygvVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSvsgVMGNRG---QVNYSA 155
Cdd:PRK07109  87 dTW---VNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMR-PRDRGAIIQVGS---ALAYRSiplQSAYCA 159
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15833594  156 AKAGIIGATKALAIEL--AKRKITVNCIAPGLIDT 188
Cdd:PRK07109 160 AKHAIRGFTDSLRCELlhDGSPVSVTMVQPPAVNT 194
PRK07201 PRK07201
SDR family oxidoreductase;
3-191 2.01e-13

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 69.21  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVAEAGATV-FLVARNGEALDELVAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVD 450
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAG--IARDAafpALSDD---DWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVsGVMGNRGQVN-YSAA 156
Cdd:PRK07201 451 YLVNNAGrsIRRSV---ENSTDrfhDYERTMAVNYFGAVRLILGLLPHMR-ERRFGHVVNVSSI-GVQTNAPRFSaYVAS 525
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMI 191
Cdd:PRK07201 526 KAALDAFSDVAASETLSDGITFTTIHMPLVRTPMI 560
PLN02253 PLN02253
xanthoxin dehydrogenase
1-241 3.18e-13

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 67.54  E-value: 3.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGaQETLNAIvanGGNGRLLSF--DVANREQCREVLEHEIAQH 78
Cdd:PLN02253  17 LGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLG-QNVCDSL---GGEPNVCFFhcDVTVEDDVSRAVDFTVDKF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARdaafPALSD------DDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGrIITLSSVSGVMGNRGQVN 152
Cdd:PLN02253  93 GTLDIMVNNAGLTG----PPCPDirnvelSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGS-IVSLCSVASAIGGLGPHA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  153 YSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMI-------EMEESALKEAMSMIPMKRMGQ-----AEEVAGLA 220
Cdd:PLN02253 168 YTGSKHAVLGLTRSVAAELGKHGIRVNCVSPYAVPTALAlahlpedERTEDALAGFRAFAGKNANLKgveltVDDVANAV 247
                        250       260
                 ....*....|....*....|.
gi 15833594  221 SYLMSDIAGYVTRQVISINGG 241
Cdd:PLN02253 248 LFLASDEARYISGLNLMIDGG 268
PRK06180 PRK06180
short chain dehydrogenase; Provisional
1-184 3.21e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 67.25  E-value: 3.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGfnigvhyHRDATGA--QETLNAIVA-NGGNGRLLSFDVANREQCREVLEHEIAQ 77
Cdd:PRK06180   3 SMKTWLITGVSSGFGRALAQAALAAG-------HRVVGTVrsEAARADFEAlHPDRALARLLDVTDFDAIDAVVADAEAT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 HGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK06180  76 FGPIDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTK-AVLPGMRARRRGHIVNITSMGGLITMPGIGYYCGSK 154
                        170       180
                 ....*....|....*....|....*..
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPG 184
Cdd:PRK06180 155 FALEGISESLAKEVAPFGIHVTAVEPG 181
PRK06179 PRK06179
short chain dehydrogenase; Provisional
2-190 1.48e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 65.31  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNI--GVhyhRDATGAQeTLNAIvanggngRLLSFDVANREQCREVLEHEIAQHG 79
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLARAGYRVfgTS---RNPARAA-PIPGV-------ELLELDVTDDASVQAAVDEVIARAG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   80 AWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGV-----MGnrgqvNYS 154
Cdd:PRK06179  73 RIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTR-AVLPHMRAQGSGRIINISSVLGFlpapyMA-----LYA 146
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15833594  155 AAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:PRK06179 147 ASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK06914 PRK06914
SDR family oxidoreductase;
1-188 1.58e-12

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 65.43  E-value: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSV-LVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRL--LSFDVANREQCREVLEhEIAQ 77
Cdd:PRK06914   1 MNKKIaIVTGASSGFGLLTTLELAKKGYLV-IATMRNPEKQENLLSQATQLNLQQNIkvQQLDVTDQNSIHNFQL-VLKE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 HGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK06914  79 IGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQ-AVLPYMRKQKSGKIINISSISGRVGFPGLSPYVSSK 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDT 188
Cdd:PRK06914 158 YALEGFSESLRLELKPFGIDVALIEPGSYNT 188
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
6-242 1.90e-12

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: 64.91  E-value: 1.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   6 LVTGAS--KGIGRAIACQLAADGFNIGVHYHRDATG--AQETLNAIvanGGNGRLLSFDVANREQCREVLEhEIAQH-GA 80
Cdd:cd05372   5 LITGIAndRSIAWGIAKALHEAGAELAFTYQPEALRkrVEKLAERL---GESALVLPCDVSNDEEIKELFA-EVKKDwGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIA-RDAA---FPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGArqGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:cd05372  81 LDGLVHSIAFApKVQLkgpFLDTSRKGFLKALDISAYSLVSLAKAA-LPIMNP--GGSIVTLSYLGSERVVPGYNVMGVA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 157 KAGIIGATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTR 233
Cdd:cd05372 158 KAALESSVRYLAYELGRKGIRVNAISAGPIKTlaaSGITGFDKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSDLSSGITG 237

                ....*....
gi 15833594 234 QVISINGGM 242
Cdd:cd05372 238 EIIYVDGGY 246
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
5-197 1.93e-12

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: 64.74  E-value: 1.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFN---IGVhyhRDATGAQEtLNAivANGGNGRLLSFDVAN-------REQCREVlehE 74
Cdd:cd05354   6 VLVTGANRGIGKAFVESLLAHGAKkvyAAV---RDPGSAAH-LVA--KYGDKVVPLRLDVTDpesikaaAAQAKDV---D 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  75 IaqhgawygVVSNAGIARDAAfpALSDDDWDAV---IHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQV 151
Cdd:cd05354  77 V--------VINNAGVLKPAT--LLEEGALEALkqeMDVNVFGLLRLAQ-AFAPVLKANGGGAIVNLNSVASLKNFPAMG 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15833594 152 NYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGM---IEMEESA 197
Cdd:cd05354 146 TYSASKSAAYSLTQGLRAELAAQGTLVLSVHPGPIDTRMaagAGGPKES 194
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
3-190 5.99e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 63.35  E-value: 5.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVHyHRDATGAQETLNAIVANGGN-GRLLSFDV--ANREQCREvLEHEIAQH- 78
Cdd:PRK08945  13 RIILVTGAGDGIGREAALTYARHGATVILL-GRTEEKLEAVYDEIEAAGGPqPAIIPLDLltATPQNYQQ-LADTIEEQf 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARD-AAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRII-TLSSVsgvmGNRGQVN---Y 153
Cdd:PRK08945  91 GRLDGVLHNAGLLGElGPMEQQDPEVWQDVMQVNVNATFMLTQ-ALLPLLLKSPAASLVfTSSSV----GRQGRANwgaY 165
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15833594  154 SAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:PRK08945 166 AVSKFATEGMMQVLADEYQGTNLRVNCINPGGTRTAM 202
PRK05872 PRK05872
short chain dehydrogenase; Provisional
3-191 6.05e-12

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 63.84  E-value: 6.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhyhrdaTG-AQETLNAIVANGGNGRL---LSFDVANREQCREVLEHEIAQH 78
Cdd:PRK05872  10 KVVVVTGAARGIGAELARRLHARGAKLAL------VDlEEAELAALAAELGGDDRvltVVADVTDLAAMQAAAEEAVERF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARqgGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:PRK05872  84 GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR--GYVLQVSSLAAFAAAPGMAAYCASKA 161
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDTGMI 191
Cdd:PRK05872 162 GVEAFANALRLEVAHHGVTVGSAYLSWIDTDLV 194
PRK05693 PRK05693
SDR family oxidoreductase;
4-206 8.50e-12

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 63.27  E-value: 8.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    4 SVLVTGASKGIGRAIACQLAADGFNIGVHYHRDatgaqETLNAIVANGGNGRLLsfDVANREQCREVLEHEIAQHGAWYG 83
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKA-----EDVEALAAAGFTAVQL--DVNDGAALARLAEELEAEHGGLDV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   84 VVSNAGIardAAFPALSDDDWDAV---IHTNLDSFYNVIQpCIMPMIGaRQGGRIITLSSVSGVMGNRGQVNYSAAKAGI 160
Cdd:PRK05693  76 LINNAGY---GAMGPLLDGGVEAMrrqFETNVFAVVGVTR-ALFPLLR-RSRGLVVNIGSVSGVLVTPFAGAYCASKAAV 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 15833594  161 IGATKALAIELAKRKITVNCIAPGLIDTgmiEMEESALKEAMSMIP 206
Cdd:PRK05693 151 HALSDALRLELAPFGVQVMEVQPGAIAS---QFASNASREAEQLLA 193
PRK08017 PRK08017
SDR family oxidoreductase;
1-192 1.18e-11

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 62.80  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVhyhrdATGAQETLNAIVANGGNGRLLSFDVAnreqcrEVLEHEIAQ--- 77
Cdd:PRK08017   1 MQKSVLITGCSSGIGLEAALELKRRGYRVLA-----ACRKPDDVARMNSLGFTGILLDLDDP------ESVERAADEvia 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   78 --HGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSA 155
Cdd:PRK08017  70 ltDNRLYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTM-LLLPAMLPHGEGRIVMTSSVMGLISTPGRGAYAA 148
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15833594  156 AKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIE 192
Cdd:PRK08017 149 SKYALEAWSDALRMELRHSGIKVSLIEPGPIRTRFTD 185
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
5-217 2.87e-11

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 60.67  E-value: 2.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgvhyhrdatgaqetlnaiVANGGNGRLLSFDVANREQCREVLEheiaQHGAWYGV 84
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEV------------------ITAGRSSGDYQVDITDEASIKALFE----KVGHFDAI 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpcimpmIGA---RQGGRIITLSSVSGVMGNRGQVNYSAAKAGII 161
Cdd:cd11731  59 VSTAGDAEFAPLAELTDADFQRGLNSKLLGQINLVR------HGLpylNDGGSITLTSGILAQRPIPGGAAAATVNGALE 132
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15833594 162 GATKALAIELAKRkITVNCIAPGLIDTGMIEMeesalkeaMSMIPMKRMGQAEEVA 217
Cdd:cd11731 133 GFVRAAAIELPRG-IRINAVSPGVVEESLEAY--------GDFFPGFEPVPAEDVA 179
PRK08219 PRK08219
SDR family oxidoreductase;
1-190 2.87e-11

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 61.10  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADgfnigvhyHRDATGA--QETLNAIVANGGNGRLLSFDVANREQcrevLEHEIAQH 78
Cdd:PRK08219   2 ERPTALITGASRGIGAAIARELAPT--------HTLLLGGrpAERLDELAAELPGATPFPVDLTDPEA----IAAAVEQL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARDAAFPALSDDDWdaviHTNLDsfYNVIQPC-----IMPMIGARQgGRIITLSSVSGVMGNRGQVNY 153
Cdd:PRK08219  70 GRLDVLVHNAGVADLGPVAESTVDEW----RATLE--VNVVAPAeltrlLLPALRAAH-GHVVFINSGAGLRANPGWGSY 142
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15833594  154 SAAKAGIIGATKALAIELAKrKITVNCIAPGLIDTGM 190
Cdd:PRK08219 143 AASKFALRALADALREEEPG-NVRVTSVHPGRTDTDM 178
PRK06139 PRK06139
SDR family oxidoreductase;
3-188 1.15e-10

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 60.50  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGA-- 80
Cdd:PRK06139   8 AVVVITGASSGIGQATAEAFARRGARL-VLAARDEEALQAVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGGRid 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 -WygvVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAG 159
Cdd:PRK06139  87 vW---VNNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAAL-PIFKKQGHGIFINMISLGGFAAQPYAAAYSASKFG 162
                        170       180       190
                 ....*....|....*....|....*....|
gi 15833594  160 IIGATKALAIELAK-RKITVNCIAPGLIDT 188
Cdd:PRK06139 163 LRGFSEALRGELADhPDIHVCDVYPAFMDT 192
PRK05993 PRK05993
SDR family oxidoreductase;
1-201 1.44e-10

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 59.66  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDatgaqETLNAIVANGGNGRLLSFdvaNREQCREVLEHEIAQ--H 78
Cdd:PRK05993   3 MKRSILITGCSSGIGAYCARALQSDGWRVFATCRKE-----EDVAALEAEGLEAFQLDY---AEPESIAALVAQVLElsG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPcIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:PRK05993  75 GRLDALFNNGAYGQPGAVEDLPTEALRAQFEANFFGWHDLTRR-VIPVMRKQGQGRIVQCSSILGLVPMKYRGAYNASKF 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15833594  159 GIIGATKALAIELAKRKITVNCIAPGLIDTGM-----------IEMEESALKEA 201
Cdd:PRK05993 154 AIEGLSLTLRMELQGSGIHVSLIEPGPIETRFranalaafkrwIDIENSVHRAA 207
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
5-203 1.95e-10

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: 58.69  E-value: 1.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETlnaivANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGv 84
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLL-SGRDAGALAGL-----AAEVGALARPADVAAELEVWALAQELGPLDLLVYA- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  85 vsnAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGArqGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGAT 164
Cdd:cd11730  74 ---AGAILGKPLARTKPAAWRRILDANLTGAALVLKHA-LALLAA--GARLVFLGAYPELVMLPGLSAYAAAKAALEAYV 147
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15833594 165 KALAIELAKRKITVncIAPGLIDTGMIEMEESALKEAMS 203
Cdd:cd11730 148 EVARKEVRGLRLTL--VRPPAVDTGLWAPPGRLPKGALS 184
PRK06101 PRK06101
SDR family oxidoreductase;
4-221 2.59e-10

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 58.73  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    4 SVLVTGASKGIGRAIACQLAADGFNIgvhyhrDATGA-QETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWy 82
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQGWQV------IACGRnQSVLDELHTQSANIFTLAFDVTDHPGTKAALSQLPFIPELW- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 gvVSNAGiarDAAFpaLSDDDWDA-----VIHTNLDSFYNVIQPCiMPMIgaRQGGRIITLSSV-SGVMGNRGQVnYSAA 156
Cdd:PRK06101  76 --IFNAG---DCEY--MDDGKVDAtlmarVFNVNVLGVANCIEGI-QPHL--SCGHRVVIVGSIaSELALPRAEA-YGAS 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESalkeAMSMIPMKRMGQAEEVAGLAS 221
Cdd:PRK06101 145 KAAVAYFARTLQLDLRPKGIEVVTVFPGFVATPLTDKNTF----AMPMIITVEQASQEIRAQLAR 205
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
5-186 3.45e-10

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 58.23  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIgvhyhrDATG-AQETLNAIVAN-GGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKV------IATGrRQERLQELKDElGDNLYIAQLDVRNRAAIEEMLASLPAEWRNID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIA--RDAAFPAlSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGvmgnrgqvNYSAAKAGI 160
Cdd:PRK10538  77 VLVNNAGLAlgLEPAHKA-SVEDWETMIDTNNKGLVYMTR-AVLPGMVERNHGHIINIGSTAG--------SWPYAGGNV 146
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15833594  161 IGATKA--------LAIELAKRKITVNCIAPGLI 186
Cdd:PRK10538 147 YGATKAfvrqfslnLRTDLHGTAVRVTDIEPGLV 180
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
6-190 1.37e-09

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: 56.84  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594     6 LVTGASKGIGRAIACQLAADGFNIG---VHYHRDATGAQETLNAIVA--NGGNGRLLSFDVANrEQCREVLEHEIAQHGA 80
Cdd:TIGR01500   4 LVTGASRGFGRTIAQELAKCLKSPGsvlVLSARNDEALRQLKAEIGAerSGLRVVRVSLDLGA-EAGLEQLLKALRELPR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    81 WYG-----VVSNAGIARDAA--FPALSD-----DDWdaviHTNLDSFYnVIQPCIMPMIGARQGGR--IITLSSVSGVMG 146
Cdd:TIGR01500  83 PKGlqrllLINNAGTLGDVSkgFVDLSDstqvqNYW----ALNLTSML-CLTSSVLKAFKDSPGLNrtVVNISSLCAIQP 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 15833594   147 NRGQVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGM 190
Cdd:TIGR01500 158 FKGWALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTDM 201
KR_3_FAS_SDR_x cd08956
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ...
5-158 1.74e-09

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); 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 consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis 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. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187659 [Multi-domain]  Cd Length: 448  Bit Score: 57.28  E-value: 1.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGfniGVhYH--------RDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIA 76
Cdd:cd08956 196 VLITGGTGTLGALLARHLVTEH---GV-RHlllvsrrgPDAPGAAELVAELAALGAEVTVAACDVADRAALAALLAAVPA 271
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  77 QHgAWYGVVSNAGIARDAAFPALSDDDWDAVI---------------HTNLDSFynviqpcimpmigarqggriITLSSV 141
Cdd:cd08956 272 DH-PLTAVVHAAGVLDDGVLTSLTPERLDAVLrpkvdaawhlheltrDLDLAAF--------------------VLFSSA 330
                       170
                ....*....|....*..
gi 15833594 142 SGVMGNRGQVNYSAAKA 158
Cdd:cd08956 331 AGVLGSPGQANYAAANA 347
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
131-241 2.20e-09

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 56.28  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  131 QGGRIITLSSVSG--------VMGnrgqvnysAAKAGIIGATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESALK 199
Cdd:PRK08594 139 EGGSIVTLTYLGGervvqnynVMG--------VAKASLEASVKYLANDLGKDGIRVNAISAGPIRTlsaKGVGGFNSILK 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15833594  200 EAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK08594 211 EIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSG 252
PRK06953 PRK06953
SDR family oxidoreductase;
2-190 2.28e-09

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 55.85  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQEtLNAIVAnggngRLLSFDVANREQcrevleheIAQHGAW 81
Cdd:PRK06953   1 MKTVLIVGASRGIGREFVRQYRADGWRV-IATARDAAALAA-LQALGA-----EALALDVADPAS--------VAGLAWK 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YG------VVSNAGI--ARDAAFPALSDDDWDAVIHTNLDSFYNVIqPCIMPMIGARqGGRIITLSS----VSGVMGNRG 149
Cdd:PRK06953  66 LDgealdaAVYVAGVygPRTEGVEPITREDFDAVMHTNVLGPMQLL-PILLPLVEAA-GGVLAVLSSrmgsIGDATGTTG 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15833594  150 QVnYSAAKAGIIGATKALAIElaKRKITVNCIAPGLIDTGM 190
Cdd:PRK06953 144 WL-YRASKAALNDALRAASLQ--ARHATCIALHPGWVRTDM 181
PRK08278 PRK08278
SDR family oxidoreductase;
3-194 3.43e-09

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 55.68  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNI--------------GVHYhrdaTGAQEtlnaIVANGGNGRLLSFDVANREQCR 68
Cdd:PRK08278   7 KTLFITGASRGIGLAIALRAARDGANIviaaktaephpklpGTIH----TAAEE----IEAAGGQALPLVGDVRDEDQVA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   69 EVLEHEIAQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLS-SVSgvMGN 147
Cdd:PRK08278  79 AAVAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACL-PHLKKSENPHILTLSpPLN--LDP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15833594  148 R---GQVNYSAAKAGIIGATKALAIELAKRKITVNCIAP-GLIDTGMIEME 194
Cdd:PRK08278 156 KwfaPHTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWPrTTIATAAVRNL 206
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
5-214 4.71e-09

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 56.08  E-value: 4.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLL--SFDVANREQCREVLEHEiaqhGAWY 82
Cdd:COG3347 428 ALVTGGAGGIGRATAARLAAEGAAV-VVADLDGEAAEAAAAELGGGYGADAVDatDVDVTAEAAVAAAFGFA----GLDI 502
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  83 GV----VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKA 158
Cdd:COG3347 503 GGsdigVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVSKNAAAAAYGAAAAATAKA 582
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15833594 159 GIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAMSMIPMKRMGQAE 214
Cdd:COG3347 583 AAQHLLRALAAEGGANGINANRVNPDAVLDGSAIWASAARAERAAAYGIGNLLLEE 638
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
5-242 7.22e-09

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: 54.81  E-value: 7.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFN-IGV-----HYHRDaTGAQETLNAIVAnggngrllsfDVANREQcrevleheiaqh 78
Cdd:cd05328   2 IVITGAASGIGAATAELLEDAGHTvIGIdlreaDVIAD-LSTPEGRAAAIA----------DVLARCS------------ 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  79 GAWYGVVSNAGIARDAAFpalsdddwDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNR---------- 148
Cdd:cd05328  59 GVLDGLVNCAGVGGTTVA--------GLVLKVNYFGLRALME-ALLPRLRKGHGPAAVVVSSIAGAGWAQdklelakala 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594 149 -----------------GQVNYSAAKAGIIGATKALAIE-LAKRKITVNCIAPGLIDTGMIEMEESAL--KEAMSMI--P 206
Cdd:cd05328 130 agtearavalaehagqpGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPILQAFLQDPrgGESVDAFvtP 209
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15833594 207 MKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:cd05328 210 MGRRAEPDEIAPVIAFLASDAASWINGANLFVDGGL 245
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
3-241 8.97e-09

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 54.59  E-value: 8.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTG--ASKGIGRAIACQLAADGFNIGVHYHRDATgaQETLNAIVANGGNGRLLSFDVANREQCREVLEhEIAQHga 80
Cdd:PRK08690   7 KKILITGmiSERSIAYGIAKACREQGAELAFTYVVDKL--EERVRKMAAELDSELVFRCDVASDDEINQVFA-DLGKH-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVvsnAGIARDAAFP---ALSDDDWDAVIHTNLDSFYNV-------IQPCIMPMIGARQGGrIITLSSVSGVmgnRGQ 150
Cdd:PRK08690  82 WDGL---DGLVHSIGFApkeALSGDFLDSISREAFNTAHEIsayslpaLAKAARPMMRGRNSA-IVALSYLGAV---RAI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  151 VNYSA---AKAGIIGATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLM 224
Cdd:PRK08690 155 PNYNVmgmAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTlaaSGIADFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLL 234
                        250
                 ....*....|....*..
gi 15833594  225 SDIAGYVTRQVISINGG 241
Cdd:PRK08690 235 SDLSSGITGEITYVDGG 251
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
3-188 1.04e-08

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: 54.39  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLS--FDVANREQCREVLEHEIAQHGA 80
Cdd:cd09807   2 KTVIITGANTGIGKETARELARRGARV-IMACRDMAKCEEAAAEIRRDTLNHEVIVrhLDLASLKSIRAFAAEFLAEEDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARdaaFP-ALSDDDWD---AVIH------TNLdsfynviqpcIMPMIGARQGGRIITLSSVSGVMG---- 146
Cdd:cd09807  81 LDVLINNAGVMR---CPySKTEDGFEmqfGVNHlghfllTNL----------LLDLLKKSAPSRIVNVSSLAHKAGkinf 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15833594 147 ---------NRGqVNYSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDT 188
Cdd:cd09807 148 ddlnseksyNTG-FAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRT 197
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
1-241 1.48e-08

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 53.40  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNIGVHY--HRDATGAQETLNAIvanggngrLLSFDVANREQCREVLEHEIAQH 78
Cdd:PRK06483   1 MPAPILITGAGQRIGLALAWHLLAQGQPVIVSYrtHYPAIDGLRQAGAQ--------CIQADFSTNAGIMAFIDELKQHT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIGARQGGR-IITLSSVSGVMGNRGQVNYSAAK 157
Cdd:PRK06483  73 DGLRAIIHNASDWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLRGHGHAASdIIHITDYVVEKGSDKHIAYAASK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  158 AGIIGATKALAIELAKrKITVNCIAPGLI---DTGMIEMEESALKEAMsmipMKRMGQAEEVAGLASYLMSdiAGYVTRQ 234
Cdd:PRK06483 153 AALDNMTLSFAAKLAP-EVKVNSIAPALIlfnEGDDAAYRQKALAKSL----LKIEPGEEEIIDLVDYLLT--SCYVTGR 225

                 ....*..
gi 15833594  235 VISINGG 241
Cdd:PRK06483 226 SLPVDGG 232
PRK09291 PRK09291
SDR family oxidoreductase;
1-189 1.64e-08

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 53.46  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASKGIGRAIACQLAADGFNI--GVHYHRDATGAQEtlnAIVANGGNGRLLSFDVANreqcrevlEHEIAQH 78
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGHNViaGVQIAPQVTALRA---EAARRGLALRVEKLDLTD--------AIDRAQA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAW-YGV-VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCIMPMIgARQGGRIITLSSVSGVMGNRGQVNYSAA 156
Cdd:PRK09291  70 AEWdVDVlLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMV-ARGKGKVVFTSSMAGLITGPFTGAYCAS 148
                        170       180       190
                 ....*....|....*....|....*....|...
gi 15833594  157 KAGIIGATKALAIELAKRKITVNCIAPGLIDTG 189
Cdd:PRK09291 149 KHALEAIAEAMHAELKPFGIQVATVNPGPYLTG 181
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
4-202 1.69e-08

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: 53.54  E-value: 1.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   4 SVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYG 83
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREAKLEALLVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  84 VVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNYSAAKAGIIGA 163
Cdd:cd05373  81 LVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAR-EAAKRMLARGRGTIIFTGATASLRGRAGFAAFAGAKFALRAL 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15833594 164 TKALAIELAKRKITV-NCIAPGLIDTGMI-----EMEESALKEAM 202
Cdd:cd05373 160 AQSMARELGPKGIHVaHVIIDGGIDTDFIrerfpKRDERKEEDGI 204
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
171-243 1.92e-08

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 53.47  E-value: 1.92e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833594  171 LAKRKITVNCIAPGLIDTGMIEMEESALKEAM---SMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGML 243
Cdd:PRK12428 156 FGARGIRVNCVAPGPVFTPILGDFRSMLGQERvdsDAKRMGRPATADEQAAVLVFLCSDAARWINGVNLPVDGGLA 231
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
3-193 2.31e-08

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 53.22  E-value: 2.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   3 RSVLVTGASKGIGRAIACQLAADGFNI--------------GVHYhrdaTGAQEtlnaIVANGGNGRLLSFDVANREQCR 68
Cdd:cd09762   4 KTLFITGASRGIGKAIALKAARDGANVviaaktaephpklpGTIY----TAAEE----IEAAGGKALPCIVDIRDEDQVR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  69 EVLEHEIAQHGAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQPCImPMIGARQGGRIITLSSVSGV--MG 146
Cdd:cd09762  76 AAVEKAVEKFGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACL-PYLKKSKNPHILNLSPPLNLnpKW 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15833594 147 NRGQVNYSAAKAGIIGATKALAIELAKRKITVNCIAP-GLIDTGMIEM 193
Cdd:cd09762 155 FKNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWPrTAIATAAMNM 202
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
2-190 1.59e-07

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 50.40  E-value: 1.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   2 SRSVLVTGASKGIGRAIACQLAADGFNIGVhyhRDATGAQETLNAIVANGGNGRLlsfdvanrEQCREVLEHEIAQHGAW 81
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWVAS---IDLAENEEADASIIVLDSDSFT--------EQAKQVVASVARLSGKV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  82 YGVVSNAGiarDAAFPALSDDD----WDAVIHTNLDSFYNVIQPCIMPMigaRQGGRIITLSSVSGVMGNRGQVNYSAAK 157
Cdd:cd05334  70 DALICVAG---GWAGGSAKSKSfvknWDLMWKQNLWTSFIASHLATKHL---LSGGLLVLTGAKAALEPTPGMIGYGAAK 143
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15833594 158 AGIIGATKALAIEL--AKRKITVNCIAPGLIDTGM 190
Cdd:cd05334 144 AAVHQLTQSLAAENsgLPAGSTANAILPVTLDTPA 178
PRK07806 PRK07806
SDR family oxidoreductase;
2-140 2.05e-07

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 50.49  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    2 SRSVLVTGASKGIGRAIACQLAADGFNIGVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:PRK07806   6 GKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQKAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGL 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15833594   82 YGVVSNagiardAAFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIGArqGGRIITLSS 140
Cdd:PRK07806  86 DALVLN------ASGGMESGMDEDYAMRLNRDAQRNLARAA-LPLMPA--GSRVVFVTS 135
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
12-241 2.37e-07

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 50.51  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   12 KGIGRAIACQLAADGFNIGVHYHRDATgaQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVVSNAGIA 91
Cdd:PRK08415  17 KSIAYGIAKACFEQGAELAFTYLNEAL--KKRVEPIAQELGSDYVYELDVSKPEHFKSLAESLKKDLGKIDFIVHSVAFA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   92 -RDA---AFPALSDDDWDAVIHTNLDSFYNVIQPCiMPMIgaRQGGRIITLSSVSGVmgnRGQVNYS---AAKAGIIGAT 164
Cdd:PRK08415  95 pKEAlegSFLETSKEAFNIAMEISVYSLIELTRAL-LPLL--NDGASVLTLSYLGGV---KYVPHYNvmgVAKAALESSV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAPGLIDT----GMIEMEEsALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISING 240
Cdd:PRK08415 169 RYLAVDLGKKGIRVNAISAGPIKTlaasGIGDFRM-ILKWNEINAPLKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVDA 247

                 .
gi 15833594  241 G 241
Cdd:PRK08415 248 G 248
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
4-158 3.03e-07

beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (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 oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase 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 consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses 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-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses 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 the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187658 [Multi-domain]  Cd Length: 376  Bit Score: 50.36  E-value: 3.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   4 SVLVTGASKGIGRAIACQLAADGFNIGVHYHRDA--TGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAW 81
Cdd:cd08955 151 TYLITGGLGGLGLLVAEWLVERGARHLVLTGRRApsAAARQAIAALEEAGAEVVVLAADVSDRDALAAALAQIRASLPPL 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  82 YGVVSNAGIARDAAFPALSDDDWDAVI---------------HTNLDSFynviqpcimpmigarqggriITLSSVSGVMG 146
Cdd:cd08955 231 RGVIHAAGVLDDGVLANQDWERFRKVLapkvqgawnlhqltqDLPLDFF--------------------VLFSSVASLLG 290
                       170
                ....*....|..
gi 15833594 147 NRGQVNYSAAKA 158
Cdd:cd08955 291 SPGQANYAAANA 302
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
108-241 3.85e-07

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 49.62  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  108 IHTNLDSFYNVIQ-PCIMPMIGARQ-------GGRIITLSSVSG--------VMGnrgqvnysAAKAGIIGATKALAIEL 171
Cdd:PRK06603 107 VDTSLENFHNSLHiSCYSLLELSRSaealmhdGGSIVTLTYYGAekvipnynVMG--------VAKAALEASVKYLANDM 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833594  172 AKRKITVNCIAPGLIDT---GMIEMEESALKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK06603 179 GENNIRVNAISAGPIKTlasSAIGDFSTMLKSHAATAPLKRNTTQEDVGGAAVYLFSELSKGVTGEIHYVDCG 251
PRK05866 PRK05866
SDR family oxidoreductase;
5-191 5.97e-07

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 49.35  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGV 84
Cdd:PRK05866  43 ILLTGASSGIGEAAAEQFARRGATV-VAVARREDLLDAVADRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDIL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAG--IARDAafpALSDDDWDAVIHTNLDSFYNVIQPC--IMPMIGARQGGRIITLSS---VSGVMGNRGQvnYSAAK 157
Cdd:PRK05866 122 INNAGrsIRRPL---AESLDRWHDVERTMVLNYYAPLRLIrgLAPGMLERGDGHIINVATwgvLSEASPLFSV--YNASK 196
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15833594  158 AGIIGATKALAIELAKRKITVNCIAPGLIDTGMI 191
Cdd:PRK05866 197 AALSAVSRVIETEWGDRGVHSTTLYYPLVATPMI 230
PRK06940 PRK06940
short chain dehydrogenase; Provisional
1-241 8.00e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 48.86  E-value: 8.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    1 MSRSVLVTGASkGIGRAIACQLAAdGFNIGVHYHRDATgAQETLNAIVANGGNGRLLSFDVANREQCREVLEhEIAQHGA 80
Cdd:PRK06940   1 MKEVVVVIGAG-GIGQAIARRVGA-GKKVLLADYNEEN-LEAAAKTLREAGFDVSTQEVDVSSRESVKALAA-TAQTLGP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   81 WYGVVSNAGIARDAAFPA--LSDDDWD-AVIhtnLDSFYNVIQPcimpmigarqGGRIITLSSVSGVM------------ 145
Cdd:PRK06940  77 VTGLVHTAGVSPSQASPEaiLKVDLYGtALV---LEEFGKVIAP----------GGAGVVIASQSGHRlpaltaeqeral 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  146 -------------GNRGQVN-----YSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESALKEAM--SMI 205
Cdd:PRK06940 144 attpteellslpfLQPDAIEdslhaYQIAKRANALRVMAEAVKWGERGARINSISPGIISTPLAQDELNGPRGDGyrNMF 223
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 15833594  206 ---PMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK06940 224 aksPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGG 262
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
5-158 1.04e-06

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


Pssm-ID: 187655 [Multi-domain]  Cd Length: 480  Bit Score: 49.09  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGfnigvHYHR--------DATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEhEIA 76
Cdd:cd08952 233 VLVTGGTGALGAHVARWLARRG-----AEHLvltsrrgpDAPGAAELVAELTALGARVTVAACDVADRDALAALLA-ALP 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  77 QHGAWYGVVSNAGIARDAAFPALSDDDWDAVI---------------HTNLDSFynviqpcimpmigarqggriITLSSV 141
Cdd:cd08952 307 AGHPLTAVVHAAGVLDDGPLDDLTPERLAEVLrakvagarhldeltrDRDLDAF--------------------VLFSSI 366
                       170
                ....*....|....*..
gi 15833594 142 SGVMGNRGQVNYSAAKA 158
Cdd:cd08952 367 AGVWGSGGQGAYAAANA 383
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
132-241 1.09e-06

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 48.18  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  132 GGRIITLSsvsgVMGN-RGQVNYSA---AKAGIIGATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESALKEAMSM 204
Cdd:PRK06079 136 GASIVTLT----YFGSeRAIPNYNVmgiAKAALESSVRYLARDLGKKGIRVNAISAGAVKTlavTGIKGHKDLLKESDSR 211
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15833594  205 IPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK06079 212 TVDGVGVTIEEVGNTAAFLLSDLSTGVTGDIIYVDKG 248
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
130-242 1.10e-06

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 48.40  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  130 RQGGRIITLSSVS--------GVMGnrgqvnysAAKAGIIGATKALAIELAKRKITVNCIAPGLIDT----GMIEMEEsA 197
Cdd:PRK07533 139 TNGGSLLTMSYYGaekvvenyNLMG--------PVKAALESSVRYLAAELGPKGIRVHAISPGPLKTraasGIDDFDA-L 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15833594  198 LKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGGM 242
Cdd:PRK07533 210 LEDAAERAPLRRLVDIDDVGAVAAFLASDAARRLTGNTLYIDGGY 254
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
5-149 1.65e-06

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 48.05  E-value: 1.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   5 VLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQEtlnaiVANGGNGRLLSFDVANREQCREVLE------HEIAQH 78
Cdd:COG0451   2 ILVTGGAGFIGSHLARRLLARGHEV-VGLDRSPPGAAN-----LAALPGVEFVRGDLRDPEALAAALAgvdavvHLAAPA 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833594  79 GAWYgvvsnagiardaafpalsdDDWDAVIHTNLDSFYNVIQpcimpmiGARQGG--RIITLSSvSGVMGNRG 149
Cdd:COG0451  76 GVGE-------------------EDPDETLEVNVEGTLNLLE-------AARAAGvkRFVYASS-SSVYGDGE 121
PRK07102 PRK07102
SDR family oxidoreductase;
4-217 1.75e-06

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 47.61  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    4 SVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNG-RLLSFDVANreqcrevleheIAQHGAWY 82
Cdd:PRK07102   3 KILIIGATSDIARACARRYAAAGARLYL-AARDVERLERLADDLRARGAVAvSTHELDILD-----------TASHAAFL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAGIARDAAFPALSDD-----DWDA---VIHTNldsFYNVIQPC--IMPMIGARQGGRIITLSSVSgvmGNRG-QV 151
Cdd:PRK07102  71 DSLPALPDIVLIAVGTLGDQaaceaDPALalrEFRTN---FEGPIALLtlLANRFEARGSGTIVGISSVA---GDRGrAS 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833594  152 N--YSAAKAGIIGATKALAIELAKRKITVNCIAPGLIDTGMIEmeesALKeamsmIPMKRMGQAEEVA 217
Cdd:PRK07102 145 NyvYGSAKAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTPMTA----GLK-----LPGPLTAQPEEVA 203
PRK07578 PRK07578
short chain dehydrogenase; Provisional
5-238 1.79e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 47.12  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADgfnigvhyhrdatgaqetlNAIVANGGNGRLLSFDVANREQCREVLEheiaQHGAWYGV 84
Cdd:PRK07578   3 ILVIGASGTIGRAVVAELSKR-------------------HEVITAGRSSGDVQVDITDPASIRALFE----KVGKVDAV 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 VSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpcimpmIG---ARQGGRiITLssVSGVMGN---RGQVNYSAAKA 158
Cdd:PRK07578  60 VSAAGKVHFAPLAEMTDEDFNVGLQSKLMGQVNLVL------IGqhyLNDGGS-FTL--TSGILSDepiPGGASAATVNG 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  159 GIIGATKALAIELaKRKITVNCIAPGLIdtgmiemEESALKEAMSM-----IPMKRMGQAeevaglasYLMSdIAGYVTR 233
Cdd:PRK07578 131 ALEGFVKAAALEL-PRGIRINVVSPTVL-------TESLEKYGPFFpgfepVPAARVALA--------YVRS-VEGAQTG 193

                 ....*
gi 15833594  234 QVISI 238
Cdd:PRK07578 194 EVYKV 198
PRK08340 PRK08340
SDR family oxidoreductase;
5-242 2.26e-06

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 47.49  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    5 VLVTGASKGIGRAIACQLAADGFN--IGVHYHRDATGAQETLNAIvangGNGRLLSFDVANREQCREVLEHEIAQHGAWY 82
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARvvISSRNEENLEKALKELKEY----GEVYAVKADLSDKDDLKNLVKEAWELLGGID 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   83 GVVSNAG-------IARDAAFpalsdDDW--DAVIHTNLDSFYNVIqpCIMPMIGARQGGRIITLSSVSGVMGNRGQVNY 153
Cdd:PRK08340  79 ALVWNAGnvrcepcMLHEAGY-----SDWleAALLHLVAPGYLTTL--LIQAWLEKKMKGVLVYLSSVSVKEPMPPLVLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  154 SAAKAGIIGATKALAIELAKRKITVNCIAPGLIDT--------------GMIeMEESALKEAMSMIPMKRMGQAEEVAGL 219
Cdd:PRK08340 152 DVTRAGLVQLAKGVSRTYGGKGIRAYTVLLGSFDTpgarenlariaeerGVS-FEETWEREVLERTPLKRTGRWEELGSL 230
                        250       260
                 ....*....|....*....|...
gi 15833594  220 ASYLMSDIAGYVTRQVISINGGM 242
Cdd:PRK08340 231 IAFLLSENAEYMLGSTIVFDGAM 253
PLN02780 PLN02780
ketoreductase/ oxidoreductase
6-198 2.90e-06

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 47.17  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGGNGRLLSFDVANREQCRE-VLEHEIAQHGAWYGV 84
Cdd:PLN02780  57 LVTGPTDGIGKGFAFQLARKGLNL-VLVARNPDKLKDVSDSIQSKYSKTQIKTVVVDFSGDIDEgVKRIKETIEGLDVGV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   85 -VSNAGIARDAA--FPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGARQGGRIITLSSVSGVM--GNRGQVNYSAAKAG 159
Cdd:PLN02780 136 lINNVGVSYPYArfFHEVDEELLKNLIKVNVEGTTKVTQ-AVLPGMLKRKKGAIINIGSGAAIVipSDPLYAVYAATKAY 214
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15833594  160 IIGATKALAIELAKRKITVNCIAPGLIDTGMIEMEESAL 198
Cdd:PLN02780 215 IDQFSRCLYVEYKKSGIDVQCQVPLYVATKMASIRRSSF 253
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
14-241 1.82e-05

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 44.74  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   14 IGRAIACQLAADGFNIGVHYHRDATGAQetLNAIVANGGNGRLLSFDVANREQCREVLEHEIAQHGAWYGVVSNAGIARD 93
Cdd:PRK06505  21 IAWGIAKQLAAQGAELAFTYQGEALGKR--VKPLAESLGSDFVLPCDVEDIASVDAVFEALEKKWGKLDFVVHAIGFSDK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   94 AAFPAL----SDDDWDAVIHTNLDSFYNVIQPC--IMPmigarQGGRIITLSSVSGVmgnRGQVNYSA---AKAGIIGAT 164
Cdd:PRK06505  99 NELKGRyadtTRENFSRTMVISCFSFTEIAKRAakLMP-----DGGSMLTLTYGGST---RVMPNYNVmgvAKAALEASV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  165 KALAIELAKRKITVNCIAPGLIDTgmieMEESALKEAMSMI-------PMKRMGQAEEVAGLASYLMSDIAGYVTRQVIS 237
Cdd:PRK06505 171 RYLAADYGPQGIRVNAISAGPVRT----LAGAGIGDARAIFsyqqrnsPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHF 246

                 ....
gi 15833594  238 INGG 241
Cdd:PRK06505 247 VDSG 250
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
124-241 2.35e-05

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 44.43  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  124 MPMIGARqgGRIITLSSVSGVmgnRGQVNYSA---AKAGIIGATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESA 197
Cdd:PRK06997 132 LPMLSDD--ASLLTLSYLGAE---RVVPNYNTmglAKASLEASVRYLAVSLGPKGIRANGISAGPIKTlaaSGIKDFGKI 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15833594  198 LKEAMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK06997 207 LDFVESNAPLRRNVTIEEVGNVAAFLLSDLASGVTGEITHVDSG 250
PRK08703 PRK08703
SDR family oxidoreductase;
3-52 2.47e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 44.15  E-value: 2.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIgVHYHRDATGAQETLNAIVANGG 52
Cdd:PRK08703   7 KTILVTGASQGLGEQVAKAYAAAGATV-ILVARHQKKLEKVYDAIVEAGH 55
PRK06194 PRK06194
hypothetical protein; Provisional
3-194 3.96e-05

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 43.85  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    3 RSVLVTGASKGIGRAIACQLAADGFNIGVhyhrdATGAQETLNAIVA--NGGNGRLLSF--DVANREQCREVLEHEIAQH 78
Cdd:PRK06194   7 KVAVITGAASGFGLAFARIGAALGMKLVL-----ADVQQDALDRAVAelRAQGAEVLGVrtDVSDAAQVEALADAALERF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   79 GAWYGVVSNAGIARDAAFPALSDDDWDAVIHTNLDSFYNVIQpCIMPMIGAR------QGGRIITLSSVSGVMGNRGQVN 152
Cdd:PRK06194  82 GAVHLLFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVR-AFTPLMLAAaekdpaYEGHIVNTASMAGLLAPPAMGI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15833594  153 YSAAKAGIIGATKAL--AIELAKRKITVNCIAPGLIDTGMIEME 194
Cdd:PRK06194 161 YNVSKHAVVSLTETLyqDLSLVTDQVGASVLCPYFVPTGIWQSE 204
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
1-190 7.87e-05

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: 42.86  E-value: 7.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   1 MSRsVLVTGASKGIGRAIACQLAADGFNIGVHyhrdATGAQETLNAIVANGGNGRLLSFDVANREQCREvLEHEIAQHGA 80
Cdd:cd08951   7 MKR-IFITGSSDGLGLAAARTLLHQGHEVVLH----ARSQKRAADAKAACPGAAGVLIGDLSSLAETRK-LADQVNAIGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  81 WYGVVSNAGIARDaAFPALSDDDWDAVIhtnldsFYNVIQPCIMPMIgARQGGRIITLSS---------VSGVM-GNRGQ 150
Cdd:cd08951  81 FDAVIHNAGILSG-PNRKTPDTGIPAMV------AVNVLAPYVLTAL-IRRPKRLIYLSSgmhrggnasLDDIDwFNRGE 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15833594 151 VN---YSAAKAGIIgatkALAIELAKR--KITVNCIAPGLIDTGM 190
Cdd:cd08951 153 NDspaYSDSKLHVL----TLAAAVARRwkDVSSNAVHPGWVPTKM 193
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
132-241 9.05e-05

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 42.82  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  132 GGRIITLSSVSG--------VMGnrgqvnysAAKAGIIGATKALAIELAKRKITVNCIAPGLIDT---GMIEMEESALKE 200
Cdd:PRK08159 141 GGSILTLTYYGAekvmphynVMG--------VAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTlaaSGIGDFRYILKW 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 15833594  201 AMSMIPMKRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK08159 213 NEYNAPLRRTVTIEEVGDSALYLLSDLSRGVTGEVHHVDSG 253
PRK07023 PRK07023
SDR family oxidoreductase;
6-226 1.16e-04

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 42.31  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594    6 LVTGASKGIGRAIACQLAADGFN-IGVHYHRD---ATGAQETLNAIVANGGNGRLLSFDVANREQCREVLEHEIaqhgaw 81
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAvLGVARSRHpslAAAAGERLAEVELDLSDAAAAAAWLAGDLLAAFVDGASR------ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   82 YGVVSNAGIARDAAfPALSDDDWDAVIHTNLdsfyNVIQPCIMP--MIGARQGG---RIITLSSVSGVMGNRGQVNYSAA 156
Cdd:PRK07023  79 VLLINNAGTVEPIG-PLATLDAAAIARAVGL----NVAAPLMLTaaLAQAASDAaerRILHISSGAARNAYAGWSVYCAT 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833594  157 KAGIIGATKALAIElAKRKITVNCIAPGLIDTGMIEMEESALKEAMSM----IPMKRMGQ---AEEVAG-LASYLMSD 226
Cdd:PRK07023 154 KAALDHHARAVALD-ANRALRIVSLAPGVVDTGMQATIRATDEERFPMrerfRELKASGAlstPEDAARrLIAYLLSD 230
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
2-140 1.28e-04

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


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 42.20  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594   2 SRSVLVTGASKGIGRAIACQLAADGFNIGVhYHRDATGAQETLNAIVANGGNGRLLS--FDVANREQCREVLEHEIAQHG 79
Cdd:cd09808   1 GRSFLITGANSGIGKAAALAIAKRGGTVHM-VCRNQTRAEEARKEIETESGNQNIFLhiVDMSDPKQVWEFVEEFKEEGK 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833594  80 AWYGVVSNAGIARDAAfpALSDDDWDAVIHTNLDSFYnVIQPCIMPMIGARQGGRIITLSS 140
Cdd:cd09808  80 KLHVLINNAGCMVNKR--ELTEDGLEKNFATNTLGTY-ILTTHLIPVLEKEEDPRVITVSS 137
PRK07984 PRK07984
enoyl-ACP reductase FabI;
138-241 1.02e-03

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 39.50  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833594  138 LSSVSGVMGNRGQVNYSA---AKAGIIGATKALAIELAKRKITVNCIAPGLIDTgmieMEESALKEAMSMI-------PM 207
Cdd:PRK07984 141 LLTLSYLGAERAIPNYNVmglAKASLEANVRYMANAMGPEGVRVNAISAGPIRT----LAASGIKDFRKMLahceavtPI 216
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15833594  208 KRMGQAEEVAGLASYLMSDIAGYVTRQVISINGG 241
Cdd:PRK07984 217 RRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGG 250
 
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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