NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|658549427|ref|WP_029741836|]
View 

MULTISPECIES: SDR family oxidoreductase [Enterobacter]

Protein Classification

SDR family oxidoreductase( domain architecture ID 11482279)

SDR family NAD(P)-dependent oxidoreductase is a short-chain dehydrogenase (SDR) family protein similar to Sinorhizobium meliloti 3-ketoacyl-ACP reductase or Clostridium absonum 7-alpha- hydroxysteroid dehydrogenase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK06500 PRK06500
SDR family oxidoreductase;
1-249 5.68e-160

SDR family oxidoreductase;


:

Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 443.24  E-value: 5.68e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK06500   1 MSRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK06500  81 LDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNGSINAHIGMPNSSVYAASKAALLSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:PRK06500 161 AKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVGSEI 240

                 ....*....
gi 658549427 241 LVDGGMGSL 249
Cdd:PRK06500 241 IVDGGMSNL 249
 
Name Accession Description Interval E-value
PRK06500 PRK06500
SDR family oxidoreductase;
1-249 5.68e-160

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 443.24  E-value: 5.68e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK06500   1 MSRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK06500  81 LDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNGSINAHIGMPNSSVYAASKAALLSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:PRK06500 161 AKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVGSEI 240

                 ....*....
gi 658549427 241 LVDGGMGSL 249
Cdd:PRK06500 241 IVDGGMSNL 249
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
1-246 2.98e-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: 256.64  E-value: 2.98e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:COG1028    1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:COG1028   81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMreRGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:COG1028  161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEE----VREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236
                        250
                 ....*....|.
gi 658549427 236 VGTELLVDGGM 246
Cdd:COG1028  237 TGQVLAVDGGL 247
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
16-246 7.94e-73

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: 221.92  E-value: 7.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   16 SGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD-KAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG--DVT 92
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEElGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGfaPKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   93 HAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAELLPRG 172
Cdd:pfam13561  86 KGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRG 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658549427  173 IRVNGLSPGPVETPAFTKTGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGGM 246
Cdd:pfam13561 166 IRVNAISPGPIKTLAASGIPGFDE----LLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
10-243 1.36e-69

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: 213.68  E-value: 1.36e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERI--LGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLN 87
Cdd:cd05233    2 LVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIeaLGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  88 AGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLS 165
Cdd:cd05233   82 AGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMkkQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658549427 166 AELLPRGIRVNGLSPGPVETPAFTKTGLSDealnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVD 243
Cdd:cd05233  162 LELAPYGIRVNAVAPGLVDTPMLAKLGPEE-----AEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
10-170 4.06e-18

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: 79.06  E-value: 4.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427    10 LITGGTSGIGLATAQAFIAEGAR-VAVTGRNP------DTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrLVLLSRSGpdapgaAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427    83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLlnNPSSVILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:smart00822  84 GVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADL--PLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAE 161

                   ....*...
gi 658549427   163 TLSAELLP 170
Cdd:smart00822 162 YRRARGLP 169
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
10-246 2.27e-16

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 76.12  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-------AERilGDKAWVIPTDAGDIASQKALAETLA----ARW 78
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAAStlaaelnARR--PNSAVTCQADLSNSATLFSRCEAIIdacfRAF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   79 PRLDAVFLNAGDVTHAPLeaWQEDAWD-------------RLMGINLKGPFFLIQALLPLL---------NNPSSVILCG 136
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPL--LRGDAGEgvgdkkslevqvaELFGSNAIAPYFLIKAFAQRQagtraeqrsTNLSIVNLCD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  137 SVSARiGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPG----PVETPAFTKTglsdealnammaEIIKLVPLG 212
Cdd:TIGR02685 161 AMTDQ-PLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGlsllPDAMPFEVQE------------DYRRKVPLG 227
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 658549427  213 -RMGSTTELAKAALYLASDESSYTVGTELLVDGGM 246
Cdd:TIGR02685 228 qREASAEQIADVVIFLVSPKAKYITGTCIKVDGGL 262
 
Name Accession Description Interval E-value
PRK06500 PRK06500
SDR family oxidoreductase;
1-249 5.68e-160

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 443.24  E-value: 5.68e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK06500   1 MSRLQGKTALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK06500  81 LDAVFINAGVAKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPASIVLNGSINAHIGMPNSSVYAASKAALLSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:PRK06500 161 AKTLSGELLPRGIRVNAVSPGPVQTPLYGKLGLPEATLDAVAAQIQALVPLGRFGTPEEIAKAVLYLASDESAFIVGSEI 240

                 ....*....
gi 658549427 241 LVDGGMGSL 249
Cdd:PRK06500 241 IVDGGMSNL 249
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
1-246 2.98e-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: 256.64  E-value: 2.98e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:COG1028    1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALEAAAAELraaGGRALAVAADVTDEAAVEALVAAAVAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:COG1028   81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMreRGGGRIVNISSIAGLRGSPGQAAYAASKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:COG1028  161 AVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEE----VREALAARIPLGRLGTPEEVAAAVLFLASDAASYI 236
                        250
                 ....*....|.
gi 658549427 236 VGTELLVDGGM 246
Cdd:COG1028  237 TGQVLAVDGGL 247
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
16-246 7.94e-73

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: 221.92  E-value: 7.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   16 SGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD-KAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG--DVT 92
Cdd:pfam13561   6 SGIGWAIARALAEEGAEVVLTDLNEALAKRVEELAEElGAAVLPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGfaPKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   93 HAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAELLPRG 172
Cdd:pfam13561  86 KGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVELGPRG 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658549427  173 IRVNGLSPGPVETPAFTKTGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGGM 246
Cdd:pfam13561 166 IRVNAISPGPIKTLAASGIPGFDE----LLAAAEARAPLGRLGTPEEVANAAAFLASDLASYITGQVLYVDGGY 235
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
10-243 1.36e-69

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: 213.68  E-value: 1.36e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERI--LGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLN 87
Cdd:cd05233    2 LVTGASSGIGRAIARRLAREGAKVVLADRNEEALAELAAIeaLGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  88 AGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLS 165
Cdd:cd05233   82 AGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMkkQGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRSLA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658549427 166 AELLPRGIRVNGLSPGPVETPAFTKTGLSDealnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVD 243
Cdd:cd05233  162 LELAPYGIRVNAVAPGLVDTPMLAKLGPEE-----AEKELAAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVIPVD 234
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
3-246 3.00e-62

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 195.38  E-value: 3.00e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERI--LGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEAlAAELraAGGEARVLVFDVSDEAAVRALIEAAVEAFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK05653  82 ALDILVNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMikARYGRIVNISSVSGVTGNPGQTNYSAAKAGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAftktglsDEALNAMM-AEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK05653 162 IGFTKALALELASRGITVNAVAPGFIDTDM-------TEGLPEEVkAEILKEIPLGRLGQPEEVANAVAFLASDAASYIT 234
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:PRK05653 235 GQVIPVNGGM 244
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
10-242 1.95e-61

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: 193.09  E-value: 1.95e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:COG4221    9 LITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRLDVLVNNAG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAE 167
Cdd:COG4221   89 VALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMraRGSGHIVNISSIAGLRPYPGGAVYAATKAAVRGLSESLRAE 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658549427 168 LLPRGIRVNGLSPGPVETPaftktgLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVgTELLV 242
Cdd:COG4221  169 LRPTGIRVTVIEPGAVDTE------FLDSVFDGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPAHVNV-NELVL 236
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
4-246 5.45e-60

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 189.63  E-value: 5.45e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA--ERI--LGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK05557   3 LEGKVALVTGASRGIGRAIAERLAAQGANVVINYASSEAGAEAlvAEIgaLGGKALAVQGDVSDAESVERAVDEAKAEFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK05557  83 GVDILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMmkQRSGRIINISSVVGLMGNPGQANYAASKAGV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFTKtgLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVG 237
Cdd:PRK05557 163 IGFTKSLARELASRGITVNAVAPGFIETDMTDA--LPED----VKEAILAQIPLGRLGQPEEIASAVAFLASDEAAYITG 236

                 ....*....
gi 658549427 238 TELLVDGGM 246
Cdd:PRK05557 237 QTLHVNGGM 245
FabG-like PRK07231
SDR family oxidoreductase;
3-246 3.01e-58

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 185.42  E-value: 3.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERI-LGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK07231   2 RLEGKVAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERvAAEIlAGGRAIAVAADVSDEADVEAAVAAALERFGS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGdVTHA--PLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:PRK07231  82 VDILVNNAG-TTHRngPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMrgEGGGAIVNVASTAGLRPRPGLGWYNASKGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKtgLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK07231 161 VITLTKALAAELGPDKIRVNAVAPVVVETGLLEA--FMGEPTPENRAKFLATIPLGRLGTPEDIANAALFLASDEASWIT 238
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:PRK07231 239 GVTLVVDGGR 248
PRK12826 PRK12826
SDR family oxidoreductase;
1-246 4.87e-58

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 184.73  E-value: 4.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK12826   1 TRDLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAATAELVeaaGGKARARQVDVRDRAALKAAVAAGVED 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARI-GLPTSSVYAASK 154
Cdd:PRK12826  81 FGRLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALirAGGGRIVLTSSVAGPRvGYPGLAHYAASK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAFtkTGLSDEALNAMMAeiiKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK12826 161 AGLVGFTRALALELAARNITVNSVHPGGVDTPMA--GNLGDAQWAEAIA---AAIPLGRLGEPEDIAAAVLFLASDEARY 235
                        250
                 ....*....|..
gi 658549427 235 TVGTELLVDGGM 246
Cdd:PRK12826 236 ITGQTLPVDGGA 247
PRK12829 PRK12829
short chain dehydrogenase; Provisional
1-245 4.97e-55

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 177.56  E-value: 4.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK12829   6 LKPLDGLRVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAAtAARLPGAKVTATVADVADPAQVERVFDTAVERFG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVT-HAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:PRK12829  86 GLDVLVNNAGIAGpTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLkasGHGGVIIALSSVAGRLGYPGRTPYAASKW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFT-----KTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASD 230
Cdd:PRK12829 166 AVVGLVKSLAIELGPLGIRVNAILPGIVRGPRMRrvieaRAQQLGIGLDEMEQEYLEKISLGRMVEPEDIAATALFLASP 245
                        250
                 ....*....|....*
gi 658549427 231 ESSYTVGTELLVDGG 245
Cdd:PRK12829 246 AARYITGQAISVDGN 260
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
3-204 9.40e-55

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 176.21  E-value: 9.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:COG0300    2 SLTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELraaGARVEVVALDVTDPDAVAALAEAVLARFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:COG0300   82 PIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMraRGRGRIVNVSSVAGLRGLPGMAAYAASKAAL 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPaFTKTGLSDEALNAMMAE 204
Cdd:COG0300  162 EGFSESLRAELAPTGVRVTAVCPGPVDTP-FTARAGAPAGRPLLSPE 207
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
7-247 2.50e-54

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: 175.04  E-value: 2.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERI---LGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:cd05333    1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEikaLGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:cd05333   81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMikRRSGRIINISSVVGLIGNPGQANYAASKAGVIGFT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 162 RTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELL 241
Cdd:cd05333  161 KSLAKELASRGITVNAVAPG------FIDTDMTDALPEKVKEKILKQIPLGRLGTPEEVANAVAFLASDDASYITGQVLH 234

                 ....*.
gi 658549427 242 VDGGMG 247
Cdd:cd05333  235 VNGGMY 240
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
2-245 1.47e-53

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: 174.02  E-value: 1.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVT---GRNPDT-----LAEAErilGDKAWVIPTDAGDIASQKALAET 73
Cdd:cd05355   22 GKLKGKKALITGGDSGIGRAVAIAFAREGADVAINylpEEEDDAeetkkLIEEE---GRKCLLIPGDLGDESFCRDLVKE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  74 LAARWPRLDAVFLNAGD-VTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAA 152
Cdd:cd05355   99 VVKEFGKLDILVNNAAYqHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKKGSSIINTTSVTAYKGSPHLLDYAA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnamMAEIIKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:cd05355  179 TKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEK-----VSEFGSQVPMGRAGQPAEVAPAYVFLASQDS 253
                        250
                 ....*....|...
gi 658549427 233 SYTVGTELLVDGG 245
Cdd:cd05355  254 SYVTGQVLHVNGG 266
PRK06138 PRK06138
SDR family oxidoreductase;
2-245 2.68e-53

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 172.64  E-value: 2.68e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE--AERILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERvaAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK06138  81 RLDVLVNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMqrQGGGSIVNTASQLALAGGRGRAAYVASKGAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVG 237
Cdd:PRK06138 161 ASLTRAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEALREALRARHPMNRFGTAEEVAQAALFLASDESSFATG 240

                 ....*...
gi 658549427 238 TELLVDGG 245
Cdd:PRK06138 241 TTLVVDGG 248
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-245 5.49e-53

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 172.13  E-value: 5.49e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK07067   1 MMRLQGKVALLTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK07067  81 IDILFNNAALFDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMveqGRGGKIINMASQAGRRGEALVSHYCATKAAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFtktglsdEALNAMMA------------EIIKLVPLGRMGSTTELAKAAL 225
Cdd:PRK07067 161 ISYTQSAALALIRHGINVNAIAPGVVDTPMW-------DQVDALFAryenrppgekkrLVGEAVPLGRMGVPDDLTGMAL 233
                        250       260
                 ....*....|....*....|
gi 658549427 226 YLASDESSYTVGTELLVDGG 245
Cdd:PRK07067 234 FLASADADYIVAQTYNVDGG 253
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
7-190 1.37e-52

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 168.95  E-value: 1.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427    7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLEAVAkelGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS--SVILCGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSggRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160
                         170       180
                  ....*....|....*....|....*....
gi 658549427  162 RTLSAELLPRGIRVNGLSPGPVETPAFTK 190
Cdd:pfam00106 161 RSLALELAPHGIRVNAVAPGGVDTDMTKE 189
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-247 1.42e-52

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 170.82  E-value: 1.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRN----PDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK12825   1 MGSLMGRVALVTGAARGLGRAIALRLARAGADVVVHYRSdeeaAEELVEAVEALGRRAQAVQADVTDKAALEAAVAAAVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  77 RWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK12825  81 RFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMrkQRGGRIVNISSVAGLPGWPGRSNYAAAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAftKTGLSDEALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK12825 161 AGLVGLTKALARELAEYGITVNMVAPGDIDTDM--KEATIEEAREAKDAET----PLGRSGTPEDIARAVAFLCSDASDY 234
                        250
                 ....*....|...
gi 658549427 235 TVGTELLVDGGMG 247
Cdd:PRK12825 235 ITGQVIEVTGGVD 247
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
4-245 1.89e-51

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: 167.97  E-value: 1.89e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL------GDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:cd05364    1 LSGKVAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEETRQSClqagvsEKKILLVVADLTEEEGQDRIISTTLAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:cd05364   81 FGRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPhLIKTKGEIVNVSSVAGGRSFPGVLYYCISKAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:cd05364  161 LDQFTRCTALELAPKGVRVNSVSPGVIVTGFHRRMGMPEEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASDASSFIT 240

                 ....*....
gi 658549427 237 GTELLVDGG 245
Cdd:cd05364  241 GQLLPVDGG 249
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
7-246 1.27e-50

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: 165.34  E-value: 1.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGdkawvIPTDAGDIASQKALaETLAARWPRLDAVFL 86
Cdd:cd05368    3 KVALITAAAQGIGRAIALAFAREGANVIATDINEEKLKELERGPG-----ITTRVLDVTDKEQV-AALAKEEGRIDVLFN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARI-GLPTSSVYAASKAALLSLART 163
Cdd:cd05368   77 CAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPkmLARKDGSIINMSSVASSIkGVPNRFVYSTTKAAVIGLTKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 164 LSAELLPRGIRVNGLSPGPVETPAFTK----TGLSDEALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSYTVGTE 239
Cdd:cd05368  157 VAADFAQQGIRCNAICPGTVDTPSLEEriqaQPDPEEALKAFAARQ----PLGRLATPEEVAALAVYLASDESAYVTGTA 232

                 ....*..
gi 658549427 240 LLVDGGM 246
Cdd:cd05368  233 VVIDGGW 239
PRK06841 PRK06841
short chain dehydrogenase; Provisional
3-245 3.27e-50

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 164.83  E-value: 3.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRID 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK06841  92 ILVNSAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRhmIAAGGGKIVNLASQAGVVALERHVAYCASKAGVVGM 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETpAFTKTGLSDEALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:PRK06841 172 TKVLALEWGPYGITVNAISPTVVLT-ELGKKAWAGEKGERAKKLI----PAGRFAYPEEIAAAALFLASDAAAMITGENL 246

                 ....*
gi 658549427 241 LVDGG 245
Cdd:PRK06841 247 VIDGG 251
PRK07856 PRK07856
SDR family oxidoreductase;
4-245 1.06e-49

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 163.57  E-value: 1.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDtlaeaERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:PRK07856   4 LTGRVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRAP-----ETVDGRPAEFHAADVRDPDQVAALVDAIVERHGRLDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS---SVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK07856  79 LVNNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQPgggSIVNIGSVSGRRPSPGTAAYGAAKAGLLNL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRgIRVNGLSPGPVETPAFTKTGLSDEALNAMMAeiikLVPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:PRK07856 159 TRSLAVEWAPK-VRVNAVVVGLVRTEQSELHYGDAEGIAAVAA----TVPLGRLATPADIAWACLFLASDLASYVSGANL 233

                 ....*
gi 658549427 241 LVDGG 245
Cdd:PRK07856 234 EVHGG 238
PRK07478 PRK07478
short chain dehydrogenase; Provisional
1-245 3.66e-49

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 162.02  E-value: 3.66e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNP---DTLAEAERILGDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK07478   1 MMRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQaelDQLVAEIRAEGGEAVALAGDVRDEAYAKALVALAVER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDV-THAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGS-VSARIGLPTSSVYAAS 153
Cdd:PRK07478  81 FGGLDIAFNNAGTLgEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMlaRGGGSLIFTSTfVGHTAGFPGMAAYAAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 154 KAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALnammAEIIKLVPLGRMGSTTELAKAALYLASDESS 233
Cdd:PRK07478 161 KAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTPMGRAMGDTPEAL----AFVAGLHALKRMAQPEEIAQAALFLASDAAS 236
                        250
                 ....*....|..
gi 658549427 234 YTVGTELLVDGG 245
Cdd:PRK07478 237 FVTGTALLVDGG 248
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
3-248 7.27e-49

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: 161.34  E-value: 7.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVT-GRNPDTLAEAERILGD-----KAWVIptdagDIASQKALAETLA- 75
Cdd:cd05352    5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIyNSAPRAEEKAEELAKKygvktKAYKC-----DVSSQESVEKTFKq 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 --ARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARI-GLP-TSSV 149
Cdd:cd05352   80 iqKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFkkQGKGSLIITASMSGTIvNRPqPQAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 150 YAASKAALLSLARTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLAS 229
Cdd:cd05352  160 YNASKAAVIHLAKSLAVEWAKYFIRVNSISPG------YIDTDLTDFVDKELRKKWESYIPLKRIALPEELVGAYLYLAS 233
                        250
                 ....*....|....*....
gi 658549427 230 DESSYTVGTELLVDGGMGS 248
Cdd:cd05352  234 DASSYTTGSDLIIDGGYTC 252
PRK06172 PRK06172
SDR family oxidoreductase;
1-245 8.96e-49

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 161.07  E-value: 8.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK06172   2 SMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGEETVALIreaGGEALFVACDVTRDAEVKALVEQTIAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAG-DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK06172  82 YGRLDYAFNNAGiEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMlaQGGGAIVNTASVAGLGAAPKMSIYAASK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKtglSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK06172 162 HAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRR---AYEADPRKAEFAAAMHPVGRIGKVEEVASAVLYLCSDGASF 238
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:PRK06172 239 TTGHALMVDGG 249
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
4-245 5.77e-48

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: 158.80  E-value: 5.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD--KAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:cd08942    4 VAGKIVLVTGGSRGIGRMIAQGFLEAGARVIISARKAEACADAAEELSAygECIAIPADLSSEEGIEALVARVAERSDRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL------NNPSSVILCGSVSARIGLPTSS-VYAASK 154
Cdd:cd08942   84 DVLVNNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLraaataENPARVINIGSIAGIVVSGLENySYGASK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETpAFTKTGLSDEalnAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:cd08942  164 AAVHQLTRKLAKELAGEHITVNAIAPGRFPS-KMTAFLLNDP---AALEAEEKSIPLGRWGRPEDMAGLAIMLASRAGAY 239
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:cd08942  240 LTGAVIPVDGG 250
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
2-245 1.04e-47

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: 158.32  E-value: 1.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:cd05341    1 NRLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNP--SSVILCGSVSARIGLPTSSVYAASKAALLS 159
Cdd:cd05341   81 DVLVNNAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAggGSIINMSSIEGLVGDPALAAYNASKGAVRG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPR--GIRVNGLSPGPVETPaftktgLSDEALNAMMA-EIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:cd05341  161 LTKSAALECATQgyGIRVNSVHPGYIYTP------MTDELLIAQGEmGNYPNTPMGRAGEPDEIAYAVVYLASDESSFVT 234

                 ....*....
gi 658549427 237 GTELLVDGG 245
Cdd:cd05341  235 GSELVVDGG 243
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
2-245 1.16e-47

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: 157.94  E-value: 1.16e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:cd05345    1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGdVTH--APLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVIL----CGSVSARIGLptsSVYAASK 154
Cdd:cd05345   81 DILVNNAG-ITHrnKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPhMEEQGGGVIIniasTAGLRPRPGL---TWYNASK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEAlnAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:cd05345  157 GWVVTATKAMAVELAPRNIRVNCLCPVAGETPLLSMFMGEDTP--ENRAKFRATIPLGRLSTPDDIANAALYLASDEASF 234
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:cd05345  235 ITGVALEVDGG 245
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
6-246 1.24e-47

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: 158.21  E-value: 1.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   6 DKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:cd05344    1 GKVALVTAASSGIGLAIARALAREGARVAICARNRENLERAAselRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS--SVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:cd05344   81 ILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwgRIVNISSLTVKEPEPNLVLSNVARAGLIGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKL-----VPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:cd05344  161 VKTLSRELAPDGVTVNSVLPGYIDTERVRRLLEARAEKEGISVEEAEKevasqIPLGRVGKPEELAALIAFLASEKASYI 240
                        250
                 ....*....|.
gi 658549427 236 VGTELLVDGGM 246
Cdd:cd05344  241 TGQAILVDGGL 251
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
4-246 2.51e-47

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: 157.36  E-value: 2.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL----GDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:cd05369    1 LKGKVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLEAAAEEIssatGGRAHPIQCDVRDPEAVEAAVDETLKEFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:cd05369   81 KIDILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLieaKHGGSILNISATYAYTGSPFQVHSAAAKAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVE-TPAFTKTGLSDEAlnamMAEIIKLVPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:cd05369  161 VDALTRSLAVEWGPYGIRVNAIAPGPIPtTEGMERLAPSGKS----EKKMIERVPLGRLGTPEEIANLALFLLSDAASYI 236
                        250
                 ....*....|.
gi 658549427 236 VGTELLVDGGM 246
Cdd:cd05369  237 NGTTLVVDGGQ 247
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
4-246 2.55e-47

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: 157.13  E-value: 2.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:cd05347    3 LKGKVALVTGASRGIGFGIASGLAEAGANIVINSRNEEKAEEAQQLIekeGVEATAFTCDVSDEEAIKAAVEAIEEDFGK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:cd05347   83 IDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMikQGHGKIINICSLLSELGGPPVPAYAASKGGVA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPaFTKTGLSDEALNAmmaEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:cd05347  163 GLTKALATEWARHGIQVNAIAPGYFATE-MTEAVVADPEFND---DILKRIPAGRWGQPEDLVGAAVFLASDASDYVNGQ 238

                 ....*...
gi 658549427 239 ELLVDGGM 246
Cdd:cd05347  239 IIFVDGGW 246
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
4-246 4.33e-47

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: 156.77  E-value: 4.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRN----PDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:cd05358    1 LKGKVALVTGASSGIGKAIAIRLATAGANVVVNYRSkedaAEEVVEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILC-GSVSARIGLPTSSVYAASKAA 156
Cdd:cd05358   81 TLDILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFrkSKIKGKIINmSSVHEKIPWPGHVNYAASKGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALnammAEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:cd05358  161 VKMMTKTLAQEYAPKGIRVNAIAPGAINTPINAEAWDDPEQR----ADLLSLIPMGRIGEPEEIAAAAAWLASDEASYVT 236
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:cd05358  237 GTTLFVDGGM 246
PRK06701 PRK06701
short chain dehydrogenase; Provisional
2-247 1.48e-46

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 156.35  E-value: 1.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLA-------EAErilGDKAWVIPTDAGDIA-SQKALAET 73
Cdd:PRK06701  42 GKLKGKVALITGGDSGIGRAVAVLFAKEGADIAIVYLDEHEDAnetkqrvEKE---GVKCLLIPGDVSDEAfCKDAVEET 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  74 LAArWPRLDAVFLNAGDVTHA-PLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAA 152
Cdd:PRK06701 119 VRE-LGRLDILVNNAAFQYPQqSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGSAIINTGSITGYEGNETLIDYSA 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnamMAEIIKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:PRK06701 198 TKGAIHAFTRSLAQSLVQKGIRVNAVAPGPIWTPLIPSDFDEEK-----VSQFGSNTPMQRPGQPEELAPAYVFLASPDS 272
                        250
                 ....*....|....*
gi 658549427 233 SYTVGTELLVDGGMG 247
Cdd:PRK06701 273 SYITGQMLHVNGGVI 287
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-246 2.55e-46

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 154.61  E-value: 2.55e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE--AERI--LGDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQelLEEIkeEGGDAIAVKADVSSEEDVENLVEQIVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVIL-CGSVSARIGLPTSSVYAASKA 155
Cdd:PRK05565  81 FGKIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPyMIKRKSGVIVnISSIWGLIGASCEVLYSASKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKtgLSDEALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:PRK05565 161 AVNAFTKALAKELAPSGIRVNAVAPGAIDTEMWSS--FSEEDKEGLAEEI----PLGRLGKPEEIAKVVLFLASDDASYI 234
                        250
                 ....*....|.
gi 658549427 236 VGTELLVDGGM 246
Cdd:PRK05565 235 TGQIITVDGGW 245
PRK08589 PRK08589
SDR family oxidoreductase;
1-245 2.98e-46

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 155.32  E-value: 2.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERI--LGDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK08589   1 MKRLENKVAVITGASTGIGQASAIALAQEGAYVLAVDIAEAVSETVDKIksNGGKAKAYHVDISDEQQVKDFASEIKEQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAG-DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPL-LNNPSSVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:PRK08589  81 GRVDVLFNNAGvDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLmMEQGGSIINTSSFSGQAADLYRSGYNAAKGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVETPAFTK-TGLSDEALNAMMAEIIKLV-PLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK08589 161 VINFTKSIAIEYGRDGIRANAIAPGTIETPLVDKlTGTSEDEAGKTFRENQKWMtPLGRLGKPEEVAKLVVFLASDDSSF 240
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:PRK08589 241 ITGETIRIDGG 251
PRK09242 PRK09242
SDR family oxidoreductase;
1-246 3.19e-45

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 152.21  E-value: 3.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL-----GDKAWVIPTDAGDIASQKALAETLA 75
Cdd:PRK09242   4 RWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeefpEREVHGLAADVSDDEDRRAILDWVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAG-DVTHAPLEaWQEDAWDRLMGINLKGPFFLIQALLPLLNN--PSSVILCGSVSARIGLPTSSVYAA 152
Cdd:PRK09242  84 DHWDGLHILVNNAGgNIRKAAID-YTEDEWRGIFETNLFSAFELSRYAHPLLKQhaSSAIVNIGSVSGLTHVRSGAPYGM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETPaFTKTGLSDEalnAMMAEIIKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:PRK09242 163 TKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTP-LTSGPLSDP---DYYEQVIERTPMRRVGEPEEVAAAVAFLCMPAA 238
                        250
                 ....*....|....
gi 658549427 233 SYTVGTELLVDGGM 246
Cdd:PRK09242 239 SYITGQCIAVDGGF 252
PRK12939 PRK12939
short chain dehydrogenase; Provisional
1-246 5.21e-45

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 151.28  E-value: 5.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK12939   2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELAAALeaaGGRAHAIAADLADPASVQRFFDAAAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKA 155
Cdd:PRK12939  82 LGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRgrIVNLASDTALWGAPKLGAYVASKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFtKTGLSDEAlnamMAEIIKLVPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:PRK12939 162 AVIGMTRSLARELGGRGITVNAIAPGLTATEAT-AYVPADER----HAYYLKGRALERLQVPDDVAGAVLFLLSDAARFV 236
                        250
                 ....*....|.
gi 658549427 236 VGTELLVDGGM 246
Cdd:PRK12939 237 TGQLLPVNGGF 247
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
1-246 1.44e-44

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: 150.29  E-value: 1.44e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIAS---QKALAETLAAR 77
Cdd:cd05329    1 RWNLEGKTALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKGFKVEGSVCDVSSrseRQELMDTVASH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 W-PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:cd05329   81 FgGKLNILVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLkaSGNGNIVFISSVAGVIAVPSGAPYGATK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPaFTKTGLSD-EALNAmmaeIIKLVPLGRMGSTTELAKAALYLASDESS 233
Cdd:cd05329  161 GALNQLTRSLACEWAKDNIRVNAVAPWVIATP-LVEPVIQQkENLDK----VIERTPLKRFGEPEEVAALVAFLCMPAAS 235
                        250
                 ....*....|...
gi 658549427 234 YTVGTELLVDGGM 246
Cdd:cd05329  236 YITGQIIAVDGGL 248
PRK06198 PRK06198
short chain dehydrogenase; Provisional
1-232 5.09e-44

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 149.00  E-value: 5.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGAR-VAVTGRNPDT---LAEAERILGDKAWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERGAAgLVICGRNAEKgeaQAAELEALGAKAVFVQADLSDVEDCRRVVAAADE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  77 RWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAAS 153
Cdd:PRK06198  81 AFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMrrrKAEGTIVNIGSMSAHGGQPFLAAYCAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 154 KAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKT-----GLSDEALNAMMAEiiklVPLGRMGSTTELAKAALYLA 228
Cdd:PRK06198 161 KGALATLTRNAAYALLRNRIRVNGLNIGWMATEGEDRIqrefhGAPDDWLEKAAAT----QPFGRLLDPDEVARAVAFLL 236

                 ....
gi 658549427 229 SDES 232
Cdd:PRK06198 237 SDES 240
PRK06057 PRK06057
short chain dehydrogenase; Provisional
1-248 1.02e-43

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 147.95  E-value: 1.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGdkAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK06057   2 SQRLAGRVAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVG--GLFVPTDVTDEDAVNALFDTAAETYGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAG--DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSV-YAASKA 155
Cdd:PRK06057  80 VDIAFNNAGisPPEDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPhmVRQGKGSIINTASFVAVMGSATSQIsYTASKG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:PRK06057 160 GVLAMSRELGVQFARQGIRVNALCPGPVNTPLLQELFAKDP---ERAARRLVHVPMGRFAEPEEIAAAVAFLASDDASFI 236
                        250
                 ....*....|...
gi 658549427 236 VGTELLVDGGMGS 248
Cdd:PRK06057 237 TASTFLVDGGISG 249
PRK07063 PRK07063
SDR family oxidoreductase;
1-249 4.00e-43

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 146.73  E-value: 4.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-----AERILGDKAWVIPTDAGDIASQKALAETLA 75
Cdd:PRK07063   2 MNRLAGKVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAERaaaaiARDVAGARVLAVPADVTDAASVAAAVAAAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAG-DVTHAPLEAWQEDaWDRLMGINLKGPFFLIQALLP-LLNNPSSVIL-CGSVSARIGLPTSSVYAA 152
Cdd:PRK07063  82 EAFGPLDVLVNNAGiNVFADPLAMTDED-WRRCFAVDLDGAWNGCRAVLPgMVERGRGSIVnIASTHAFKIIPGCFPYPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:PRK07063 161 AKHGLLGLTRALGIEYAARNVRVNAIAPGYIETQLTEDWWNAQPDPAAARAETLALQPMKRIGRPEEVAMTAVFLASDEA 240
                        250
                 ....*....|....*..
gi 658549427 233 SYTVGTELLVDGGMGSL 249
Cdd:PRK07063 241 PFINATCITIDGGRSVL 257
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
4-245 5.46e-43

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 145.88  E-value: 5.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE--AERI--LGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:cd05362    1 LAGKVALVTGASRGIGRAIAKRLARDGASVVVNYASSKAAAEevVAEIeaAGGKAIAVQADVSDPSQVARLFDAAEKAFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLS 159
Cdd:cd05362   81 GVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGRIINISSSLTAAYTPNYGAYAGSKAAVEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETPAFTkTGLSDEALnammAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTE 239
Cdd:cd05362  161 FTRVLAKELGGRGITVNAVAPGPVDTDMFY-AGKTEEAV----EGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNGQV 235

                 ....*.
gi 658549427 240 LLVDGG 245
Cdd:cd05362  236 IRANGG 241
PRK12827 PRK12827
short chain dehydrogenase; Provisional
1-246 3.22e-42

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 144.09  E-value: 3.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDT-LAEAERIL------GDKAWVIPTDAGDIASQKALAET 73
Cdd:PRK12827   1 MASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRgRAEADAVAagieaaGGKALGLAFDVRDFAATRAALDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  74 LAARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP---LLNNPSSVILCGSVSARIGLPTSSVY 150
Cdd:PRK12827  81 GVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPpmiRARRGGRIVNIASVAGVRGNRGQVNY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 151 AASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAftktglsdeALNAMMAE-IIKLVPLGRMGSTTELAKAALYLAS 229
Cdd:PRK12827 161 AASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPM---------ADNAAPTEhLLNPVPVQRLGEPDEVAALVAFLVS 231
                        250
                 ....*....|....*..
gi 658549427 230 DESSYTVGTELLVDGGM 246
Cdd:PRK12827 232 DAASYVTGQVIPVDGGF 248
PRK06484 PRK06484
short chain dehydrogenase; Validated
11-245 8.34e-42

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 149.23  E-value: 8.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  11 ITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAGD 90
Cdd:PRK06484 274 ITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDVLVNNAGI 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  91 V-THAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAELL 169
Cdd:PRK06484 354 AeVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLACEWA 433
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549427 170 PRGIRVNGLSPGPVETPAFTKTGLSDEalnAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGG 245
Cdd:PRK06484 434 PAGIRVNTVAPGYIETPAVLALKASGR---ADFDSIRRRIPLGRLGDPEEVAEAIAFLASPAASYVNGATLTVDGG 506
PRK06484 PRK06484
short chain dehydrogenase; Validated
7-245 9.05e-42

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 149.23  E-value: 9.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:PRK06484   6 RVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRIDVLVN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAG--DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNP---SSVILCGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:PRK06484  86 NAGvtDPTMTATLDTTLEEFARLQAINLTGAYLVAREALRLMIEQghgAAIVNVASGAGLVALPKRTAYSASKAAVISLT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 162 RTLSAELLPRGIRVNGLSPGPVETP---AFTKTGLSDEALnammaeIIKLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK06484 166 RSLACEWAAKGIRVNAVLPGYVRTQmvaELERAGKLDPSA------VRSRIPLGRLGRPEEIAEAVFFLASDQASYITGS 239

                 ....*..
gi 658549427 239 ELLVDGG 245
Cdd:PRK06484 240 TLVVDGG 246
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
4-245 1.36e-41

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 142.24  E-value: 1.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:cd08944    1 LEGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAP-LEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNP--SSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:cd08944   81 LVNNAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARggGSIVNLSSIAGQSGDPGYGAYGASKAAIRNL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAF-TKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTE 239
Cdd:cd08944  161 TRTLAAELRHAGIRCNALAPGLIDTPLLlAKLAGFEGALGPGGFHLLIHQLQGRLGRPEDVAAAVVFLLSDDASFITGQV 240

                 ....*.
gi 658549427 240 LLVDGG 245
Cdd:cd08944  241 LCVDGG 246
PRK07035 PRK07035
SDR family oxidoreductase;
4-246 1.83e-41

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 142.08  E-value: 1.83e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPD---TLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK07035   6 LTGKIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDgcqAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAG-DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK07035  86 LDILVNNAAaNPYFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMkeQGGGSIVNVASVNGVSPGDFQGIYSITKAAV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETP---AFTKTglsDEALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK07035 166 ISMTKAFAKECAPFGIRVNALLPGLTDTKfasALFKN---DAILKQALAHI----PLRRHAEPSEMAGAVLYLASDASSY 238
                        250
                 ....*....|..
gi 658549427 235 TVGTELLVDGGM 246
Cdd:PRK07035 239 TTGECLNVDGGY 250
PRK09135 PRK09135
pteridine reductase; Provisional
1-245 2.35e-41

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 141.99  E-value: 2.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-----ERILGDKAWVIPTDAGDIASQKALAETLA 75
Cdd:PRK09135   1 MMTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSAAEADAlaaelNALRPGSAAALQADLLDPDALPELVAACV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLN-NPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK09135  81 AAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRkQRGAIVNITDIHAERPLKGYPVYCAAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRgIRVNGLSPGPVETPAFTKTgLSDEAlnamMAEIIKLVPLGRMGSTTELAKAALYLAsDESSY 234
Cdd:PRK09135 161 AALEMLTRSLALELAPE-VRVNAVAPGAILWPEDGNS-FDEEA----RQAILARTPLKRIGTPEDIAEAVRFLL-ADASF 233
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:PRK09135 234 ITGQILAVDGG 244
PRK07576 PRK07576
short chain dehydrogenase; Provisional
1-245 2.91e-41

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 142.02  E-value: 2.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD---KAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK07576   4 MFDFAGKNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEKVDAAVAQLQQagpEGLGVSADVRDYAAVEAAFAQIADE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILcgSVSAR---IGLPTSSVYAASK 154
Cdd:PRK07576  84 FGPIDVLVSGAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASII--QISAPqafVPMPMQAHVCAAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVE-TPAFTKTGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESS 233
Cdd:PRK07576 162 AGVDMLTRTLALEWGPEGIRVNSIVPGPIAgTEGMARLAPSPE----LQAAVAQSVPLKRNGTKQDIANAALFLASDMAS 237
                        250
                 ....*....|..
gi 658549427 234 YTVGTELLVDGG 245
Cdd:PRK07576 238 YITGVVLPVDGG 249
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
10-245 3.05e-41

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: 141.34  E-value: 3.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPD-----TLAEAERiLGDKAWVIPTDAGDIASQKALAETLAARWPRLDAV 84
Cdd:cd05359    2 LVTGGSRGIGKAIALRLAERGADVVINYRKSKdaaaeVAAEIEE-LGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 FLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:cd05359   81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMreRGGGRIVAISSLGSIRALPNYLAVGTAKAALEALVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 163 TLSAELLPRGIRVNGLSPGPVETPAFTK----TGLSDEALNAMmaeiiklvPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:cd05359  161 YLAVELGPRGIRVNAVSPGVIDTDALAHfpnrEDLLEAAAANT--------PAGRVGTPQDVADAVGFLCSDAARMITGQ 232

                 ....*..
gi 658549427 239 ELLVDGG 245
Cdd:cd05359  233 TLVVDGG 239
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
3-246 3.19e-41

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 141.62  E-value: 3.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK08213   9 DLSGKTALVTGGSRGLGLQIAEALGEAGARVVLSARKAEELEEAAAHLealGIDALWIAADVADEADIERLAEETLERFG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNP---SSVILCGSVSARIGLPTSSV----YAA 152
Cdd:PRK08213  89 HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPrgyGRIINVASVAGLGGNPPEVMdtiaYNT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:PRK08213 169 SKGAVINFTRALAAEWGPHGIRVNAIAPG------FFPTKMTRGTLERLGEDLLAHTPLGRLGDDEDLKGAALLLASDAS 242
                        250
                 ....*....|....
gi 658549427 233 SYTVGTELLVDGGM 246
Cdd:PRK08213 243 KHITGQILAVDGGV 256
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
3-246 1.96e-40

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: 139.51  E-value: 1.96e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD-KAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:cd05326    1 RLDGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDpDISFVHCDVTVEADVRAAVDTAVARFGRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHAP--LEAWQEDAWDRLMGINLKGPFFLIQ----ALLPllNNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:cd05326   81 DIMFNNAGVLGAPCysILETSLEEFERVLDVNVYGAFLGTKhaarVMIP--AKKGSIVSVASVAGVVGGLGPHAYTASKH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTK-TGLSDEALNAMMAEIIKlvPLGRMGSTTELAKAALYLASDESSY 234
Cdd:cd05326  159 AVLGLTRSAATELGEHGIRVNCVSPYGVATPLLTAgFGVEDEAIEEAVRGAAN--LKGTALRPEDIAAAVLYLASDDSRY 236
                        250
                 ....*....|..
gi 658549427 235 TVGTELLVDGGM 246
Cdd:cd05326  237 VSGQNLVVDGGL 248
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
3-245 2.32e-40

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 139.64  E-value: 2.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK12429   1 MLKGKVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAAAAAEALqkaGGKAIGVAMDVTDEEAINAGIDYAVETFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK12429  81 GVDILVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMkaQGGGRIINMASVHGLVGSAGKAAYVSAKHGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETP-------AFTKT-GLS-DEALNAMMAEiikLVPLGRMGSTTELAKAALYLA 228
Cdd:PRK12429 161 IGLTKVVALEGATHGVTVNAICPGYVDTPlvrkqipDLAKErGISeEEVLEDVLLP---LVPQKRFTTVEEIADYALFLA 237
                        250
                 ....*....|....*..
gi 658549427 229 SDESSYTVGTELLVDGG 245
Cdd:PRK12429 238 SFAAKGVTGQAWVVDGG 254
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
4-245 9.74e-40

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: 137.75  E-value: 9.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:cd05363    1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:cd05363   81 LVNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMiaqGRGGKIINMASQAGRRGEALVGVYCATKAAVISL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAFtktglsdEALNAMMAE------------IIKLVPLGRMGSTTELAKAALYLA 228
Cdd:cd05363  161 TQSAGLNLIRHGINVNAIAPGVVDGEHW-------DGVDAKFARyenrprgekkrlVGEAVPFGRMGRAEDLTGMAIFLA 233
                        250
                 ....*....|....*..
gi 658549427 229 SDESSYTVGTELLVDGG 245
Cdd:cd05363  234 STDADYIVAQTYNVDGG 250
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
4-246 1.21e-39

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 137.94  E-value: 1.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGR----NPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK08936   5 LEGKVVVITGGSTGLGRAMAVRFGKEKAKVVINYRsdeeEANDVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:PRK08936  85 TLDVMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFvehDIKGNIINMSSVHEQIPWPLFVHYAASKGG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTgLSDEALNAmmaEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK08936 165 VKLMTETLAMEYAPKGIRVNNIGPGAINTPINAEK-FADPKQRA---DVESMIPMGYIGKPEEIAAVAAWLASSEASYVT 240
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:PRK08936 241 GITLFADGGM 250
PRK07062 PRK07062
SDR family oxidoreductase;
4-247 1.44e-39

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 137.48  E-value: 1.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL-----GDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK07062   6 LEGRVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLrekfpGARLLAARCDVLDEADVAAFAAAVEARF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLN-NPSSVILC-GSVSARIGLPTSSVYAASKAA 156
Cdd:PRK07062  86 GGVDMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRaSAAASIVCvNSLLALQPEPHMVATSAARAG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVETPA----FTKTGLSDEALNAMMAEII--KLVPLGRMGSTTELAKAALYLASD 230
Cdd:PRK07062 166 LLNLVKSLATELAPKGVRVNSILLGLVESGQwrrrYEARADPGQSWEAWTAALArkKGIPLGRLGRPDEAARALFFLASP 245
                        250
                 ....*....|....*..
gi 658549427 231 ESSYTVGTELLVDGGMG 247
Cdd:PRK07062 246 LSSYTTGSHIDVSGGFA 262
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
1-247 1.96e-39

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 137.39  E-value: 1.96e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK06200   1 MGWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTH-APLEAWQED----AWDRLMGINLKGPFFLIQALLP-LLNNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK06200  81 LDCFVGNAGIWDYnTSLVDIPAEtldtAFDEIFNVNVKGYLLGAKAALPaLKASGGSMIFTLSNSSFYPGGGGPLYTASK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRgIRVNGLSPGPVETP--AFTKTGLSDEALNAM--MAEIIK-LVPLGRMGSTTELAKAALYLAS 229
Cdd:PRK06200 161 HAVVGLVRQLAYELAPK-IRVNGVAPGGTVTDlrGPASLGQGETSISDSpgLADMIAaITPLQFAPQPEDHTGPYVLLAS 239
                        250
                 ....*....|....*....
gi 658549427 230 DE-SSYTVGTELLVDGGMG 247
Cdd:PRK06200 240 RRnSRALTGVVINADGGLG 258
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
7-240 9.56e-39

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: 134.41  E-value: 9.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERiLGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:cd08932    1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSA-SGGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:cd08932   80 NAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSgrVVFLNSLSGKRVLAGNAGYSASKFALRALAHAL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549427 165 SAELLPRGIRVNGLSPGPVETPAFTKTGLsdealnammaeiIKLVPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:cd08932  160 RQEGWDHGVRVSAVCPGFVDTPMAQGLTL------------VGAFPPEEMIQPKDIANLVRMVIELPENITSVAVL 223
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
10-197 1.21e-38

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: 134.67  E-value: 1.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:cd05374    4 LITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNNAG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL-NNPSSVIL-CGSVSARIGLPTSSVYAASKAALLSLARTLSAE 167
Cdd:cd05374   84 YGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMrKQGSGRIVnVSSVAGLVPTPFLGPYCASKAALEALSESLRLE 163
                        170       180       190
                 ....*....|....*....|....*....|
gi 658549427 168 LLPRGIRVNGLSPGPVETPAFTKTGLSDEA 197
Cdd:cd05374  164 LAPFGIKVTIIEPGPVRTGFADNAAGSALE 193
PRK07774 PRK07774
SDR family oxidoreductase;
1-245 1.56e-38

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 134.49  E-value: 1.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDtLAE--AERILGD--KAWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK07774   1 MGRFDDKVAIVTGAAGGIGQAYAEALAREGASVVVADINAE-GAErvAKQIVADggTAIAVQVDVSDPDSAKAMADATVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  77 RWPRLDAVFLNAGDVTHAPLEA-----WqeDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPtSSVYA 151
Cdd:PRK07774  80 AFGGIDYLVNNAAIYGGMKLDLlitvpW--DYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLY-SNFYG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 152 ASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAfTKTGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDE 231
Cdd:PRK07774 157 LAKVGLNGLTQQLARELGGMNIRVNAIAPGPIDTEA-TRTVTPKE----FVADMVKGIPLSRMGTPEDLVGMCLFLLSDE 231
                        250
                 ....*....|....
gi 658549427 232 SSYTVGTELLVDGG 245
Cdd:PRK07774 232 ASWITGQIFNVDGG 245
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
7-246 2.14e-38

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: 134.43  E-value: 2.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPD-TLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:cd05366    3 KVAIITGAAQGIGRAIAERLAADGFNIVLADLNLEeAAKSTIQEIseaGYNAVAVGADVTDKDDVEALIDQAVEKFGSFD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPL---LNNPSSVILCGSVSARIGLPTSSVYAASKAALLS 159
Cdd:cd05366   83 VMVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQfkkLGHGGKIINASSIAGVQGFPNLGAYSASKFAVRG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETP-------AFTKTGLSDEALNamMAEIIKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:cd05366  163 LTQTAAQELAPKGITVNAYAPGIVKTEmwdyideEVGEIAGKPEGEG--FAEFSSSIPLGRLSEPEDVAGLVSFLASEDS 240
                        250
                 ....*....|....
gi 658549427 233 SYTVGTELLVDGGM 246
Cdd:cd05366  241 DYITGQTILVDGGM 254
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
3-247 5.22e-38

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: 133.25  E-value: 5.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:cd05348    1 WLKGEVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAG------DVTHAPLEAWqEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:cd05348   81 CFIGNAGiwdystSLVDIPEEKL-DEAFDELFHINVKGYILGAKAALPaLYATEGSVIFTVSNAGFYPGGGGPLYTASKH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRgIRVNGLSPGPVETPAFTKTGLSDEALNAMM---AEIIK-LVPLGRMGSTTELAKAALYLASDE 231
Cdd:cd05348  160 AVVGLVKQLAYELAPH-IRVNGVAPGGMVTDLRGPASLGQGETSISTpplDDMLKsILPLGFAPEPEDYTGAYVFLASRG 238
                        250
                 ....*....|....*..
gi 658549427 232 SSYTV-GTELLVDGGMG 247
Cdd:cd05348  239 DNRPAtGTVINYDGGMG 255
PRK08628 PRK08628
SDR family oxidoreductase;
3-245 7.91e-38

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 132.78  E-value: 7.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNP--DTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK08628   4 NLKDKVVIVTGGASGIGAAISLRLAEEGAIPVIFGRSApdDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGiNLKGPFFLIQALLPLLNNPSSVIL-CGSVSARIGLPTSSVYAASKAALLS 159
Cdd:PRK08628  84 IDGLVNNAGVNDGVGLEAGREAFVASLER-NLIHYYVMAHYCLPHLKASRGAIVnISSKTALTGQGGTSGYAAAKGAQLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETPAFTK--TGLSDEAlnAMMAEIIKLVPLG-RMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK08628 163 LTREWAVALAKDGVRVNAVIPAEVMTPLYENwiATFDDPE--AKLAAITAKIPLGhRMTTAEEIADTAVFLLSERSSHTT 240

                 ....*....
gi 658549427 237 GTELLVDGG 245
Cdd:PRK08628 241 GQWLFVDGG 249
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
7-245 1.08e-37

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: 132.02  E-value: 1.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDtlAEAERI------LGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:cd05357    1 AVALVTGAAKRIGRAIAEALAAEGYRVVVHYNRSE--AEAQRLkdelnaLRNSAVLVQADLSDFAACADLVAAAFRAFGR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVI-LCGSVSARiGLPTSSVYAASKAAL 157
Cdd:cd05357   79 CDVLVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLagSRNGSIInIIDAMTDR-PLTGYFAYCMSKAAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRgIRVNGLSPGPvetpaftkTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASdeSSYTVG 237
Cdd:cd05357  158 EGLTRSAALELAPN-IRVNGIAPGL--------ILLPEDMDAEYRENALRKVPLKRRPSAEEIADAVIFLLD--SNYITG 226

                 ....*...
gi 658549427 238 TELLVDGG 245
Cdd:cd05357  227 QIIKVDGG 234
PRK12828 PRK12828
short chain dehydrogenase; Provisional
1-245 1.64e-37

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 131.46  E-value: 1.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK12828   2 EHSLQGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTlPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK12828  82 RLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALtaSGGGRIVNIGAGAALKAGPGMGAYAAAKAGV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFTKtglsdealnAMMAEIiklvpLGRMGSTTELAKAALYLASDESSYTVG 237
Cdd:PRK12828 162 ARLTEALAAELLDRGITVNAVLPSIIDTPPNRA---------DMPDAD-----FSRWVTPEQIAAVIAFLLSDEAQAITG 227

                 ....*...
gi 658549427 238 TELLVDGG 245
Cdd:PRK12828 228 ASIPVDGG 235
PRK08265 PRK08265
short chain dehydrogenase; Provisional
1-249 1.70e-37

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 132.05  E-value: 1.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK08265   1 MIGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDaWDRLMGINLKGPFFLIQALLPLLNNPSSVIL-CGSVSARIGLPTSSVYAASKAALLS 159
Cdd:PRK08265  81 VDILVNLACTYLDDGLASSRAD-WLAALDVNLVSAAMLAQAAHPHLARGGGAIVnFTSISAKFAQTGRWLYPASKAAIRQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETPAF-TKTGLSDEALNAMMAEiikLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK08265 160 LTRSMAMDLAPDGIRVNSVSPGWTWSRVMdELSGGDRAKADRVAAP---FHLLGRVGDPEEVAQVVAFLCSDAASFVTGA 236
                        250
                 ....*....|.
gi 658549427 239 ELLVDGGMGSL 249
Cdd:PRK08265 237 DYAVDGGYSAL 247
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-245 1.82e-37

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 131.83  E-value: 1.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGdkAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKG--VFTIKCDVGNRDQVKKSKEVVEKEFGRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS-VILCGSVSARIGLPT--SSVYAASKAALL 158
Cdd:PRK06463  81 DVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNgAIVNIASNAGIGTAAegTTFYAITKAGII 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPaFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK06463 161 ILTRRLAFELGKYGIRVNAVAPGWVETD-MTLSGKSQEEAEKLRELFRNKTVLKTTGKPEDIANIVLFLASDDARYITGQ 239

                 ....*..
gi 658549427 239 ELLVDGG 245
Cdd:PRK06463 240 VIVADGG 246
PRK07677 PRK07677
short chain dehydrogenase; Provisional
7-245 7.29e-37

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 130.18  E-value: 7.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEAKLEIeqfPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVS----ARIGLPTSsvyAASKAAL 157
Cdd:PRK07677  82 LINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKywIEKGIKGNIINMVATyawdAGPGVIHS---AAAKAGV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPR-GIRVNGLSPGPVEtpaftKTGLSDEAL--NAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK07677 159 LAMTRTLAVEWGRKyGIRVNAIAPGPIE-----RTGGADKLWesEEAAKRTIQSVPLGRLGTPEEIAGLAYFLLSDEAAY 233
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:PRK07677 234 INGTCITMDGG 244
PRK07041 PRK07041
SDR family oxidoreductase;
10-245 1.53e-36

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 129.00  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIpTDAGDIASQKALaETLAARWPRLDAVFLNAG 89
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGGAPVR-TAALDITDEAAV-DAFFAEAGPFDHVVITAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQAllPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAELL 169
Cdd:PRK07041  79 DTPGGPVRALPLAAAQAAMDSKFWGAYRVARA--ARIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLALELA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549427 170 PrgIRVNGLSPGPVETPAFtkTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLAsdESSYTVGTELLVDGG 245
Cdd:PRK07041 157 P--VRVNTVSPGLVDTPLW--SKLAGDAREAMFAAAAERLPARRVGQPEDVANAILFLA--ANGFTTGSTVLVDGG 226
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
1-245 1.82e-36

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 129.54  E-value: 1.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL--GDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK08226   1 MGKLTGKTALITGALQGIGEGIARVFARHGANLILLDISPEIEKLADELCgrGHRCTAVVADVRDPASVAAAIKRAKEKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARI-GLPTSSVYAASKA 155
Cdd:PRK08226  81 GRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPemIARKDGRIVMMSSVTGDMvADPGETAYALTKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGL-SD-EALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESS 233
Cdd:PRK08226 161 AIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARqSNpEDPESVLTEMAKAIPLRRLADPLEVGELAAFLASDESS 240
                        250
                 ....*....|..
gi 658549427 234 YTVGTELLVDGG 245
Cdd:PRK08226 241 YLTGTQNVIDGG 252
PRK06114 PRK06114
SDR family oxidoreductase;
3-245 2.74e-36

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 128.75  E-value: 2.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDT-LAE-AERI--LGDKAWVIptdAGDIASQKALAETLA--- 75
Cdd:PRK06114   5 DLDGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDgLAEtAEHIeaAGRRAIQI---AADVTSKADLRAAVArte 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDaVFLNAGDVTHA-PLEAWQEDAWDRLMGINLKGPFFLIQA--LLPLLNNPSSVILCGSVSARI---GLpTSSV 149
Cdd:PRK06114  82 AELGALT-LAVNAAGIANAnPAEEMEEEQWQTVMDINLTGVFLSCQAeaRAMLENGGGSIVNIASMSGIIvnrGL-LQAH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 150 YAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKtglsdealnAMMAEIIKLV----PLGRMGSTTELAKAAL 225
Cdd:PRK06114 160 YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPMNTR---------PEMVHQTKLFeeqtPMQRMAKVDEMVGPAV 230
                        250       260
                 ....*....|....*....|
gi 658549427 226 YLASDESSYTVGTELLVDGG 245
Cdd:PRK06114 231 FLLSDAASFCTGVDLLVDGG 250
PRK06523 PRK06523
short chain dehydrogenase; Provisional
3-246 2.88e-36

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 128.87  E-value: 2.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRN-PDTLAEAerilgdkAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAGARVVTTARSrPDDLPEG-------VEFVAADLTTAEGCAAVARAVLERLGGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVThAPL---EAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSV-YAASKA 155
Cdd:PRK06523  79 DILVHVLGGSS-APAggfAALTDEEWQDELNLNLLAAVRLDRALLPGMiaRGSGVIIHVTSIQRRLPLPESTTaYAAAKA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFT--------KTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYL 227
Cdd:PRK06523 158 ALSTYSKSLSKEVAPKGVRVNTVSPGWIETEAAValaerlaeAAGTDYEGAKQIIMDSLGGIPLGRPAEPEEVAELIAFL 237
                        250
                 ....*....|....*....
gi 658549427 228 ASDESSYTVGTELLVDGGM 246
Cdd:PRK06523 238 ASDRAASITGTEYVIDGGT 256
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
4-246 2.93e-36

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: 128.60  E-value: 2.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITG--GTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILG--DKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:COG0623    3 LKGKRGLITGvaNDRSIAWGIAKALHEEGAELAFTYQGEALKKRVEPLAEelGSALVLPCDVTDDEQIDALFDEIKEKWG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFlnagdvtH----APLEAwqedawdrlmginLKGPF-------FLI-------------QALLPLLNNPSSVILC 135
Cdd:COG0623   83 KLDFLV-------HsiafAPKEE-------------LGGRFldtsregFLLamdisayslvalaKAAEPLMNEGGSIVTL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 136 GSVSARIGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFtkTGLSDeaLNAMMAEIIKLVPLGRMG 215
Cdd:COG0623  143 TYLGAERVVPNYNVMGVAKAALEASVRYLAADLGPKGIRVNAISAGPIKTLAA--SGIPG--FDKLLDYAEERAPLGRNV 218
                        250       260       270
                 ....*....|....*....|....*....|.
gi 658549427 216 STTELAKAALYLASDESSYTVGTELLVDGGM 246
Cdd:COG0623  219 TIEEVGNAAAFLLSDLASGITGEIIYVDGGY 249
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
7-246 5.67e-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: 127.96  E-value: 5.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVF 85
Cdd:cd05349    1 QVVLVTGASRGLGAAIARSFAREGARVVVNYYRSTESAEAvAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNA-------GDVTHAPLEAWQEDAWDRLMGiNLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAA 156
Cdd:cd05349   81 NNAlidfpfdPDQRKTFDTIDWEDYQQQLEG-AVKGALNLLQAVLPDFKERGSgrVINIGTNLFQNPVVPYHDYTTAKAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVETpaftkTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:cd05349  160 LLGFTRNMAKELGPYGITVNMVSGGLLKV-----TDASAATPKEVFDAIAQTTPLGKVTTPQDIADAVLFFASPWARAVT 234
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:cd05349  235 GQNLVVDGGL 244
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
3-245 8.82e-36

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 127.53  E-value: 8.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE--AERI--LGDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK08063   1 VFSGKVALVTGSSRGIGKAIALRLAEEGYDIAVNYARSRKAAEetAEEIeaLGRKALAVKANVGDVEKIKEMFAQIDEEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:PRK08063  81 GRLDVFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMekVGGGKIISLSSLGSIRYLENYTTVGVSKAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK08063 161 LEALTRYLAVELAPKGIAVNAVSGGAVDTDALKHFPNREE----LLEDARAKTPAGRMVEPEDVANAVLFLCSPEADMIR 236

                 ....*....
gi 658549427 237 GTELLVDGG 245
Cdd:PRK08063 237 GQTIIVDGG 245
PRK07060 PRK07060
short chain dehydrogenase; Provisional
1-246 1.17e-35

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 127.14  E-value: 1.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKawVIPTDAGDIASQKALAetlaARWPR 80
Cdd:PRK07060   4 AFDFSGKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCE--PLRLDVGDDAAIRAAL----AAAGA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK07060  78 FDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMiaaGRGGSIVNVSSQAALVGLPDHLAYCASKAAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSYTVG 237
Cdd:PRK07060 158 DAITRVLCVELGPHGIRVNSVNPTVTLTPMAAEAWSDPQKSGPMLAAI----PLGRFAEVDDVAAPILFLLSDAASMVSG 233

                 ....*....
gi 658549427 238 TELLVDGGM 246
Cdd:PRK07060 234 VSLPVDGGY 242
PRK12937 PRK12937
short chain dehydrogenase; Provisional
4-246 1.29e-35

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 126.78  E-value: 1.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVT----GRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK12937   3 LSNKVAIVTGASRGIGAAIARRLAADGFAVAVNyagsAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLS 159
Cdd:PRK12937  83 RIDVLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGGRIINLSTSVIALPLPGYGPYAASKAAVEG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETPAFTKtGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTE 239
Cdd:PRK12937 163 LVHVLANELRGRGITVNAVAPGPVATELFFN-GKSAE----QIDQLAGLAPLERLGTPEEIAAAVAFLAGPDGAWVNGQV 237

                 ....*..
gi 658549427 240 LLVDGGM 246
Cdd:PRK12937 238 LRVNGGF 244
PRK07069 PRK07069
short chain dehydrogenase; Validated
10-246 2.73e-35

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 126.36  E-value: 2.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE--AERILGDK----AWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFLTDINDAAGLDafAAEINAAHgegvAFAAVQDVTDEAQWQALLAQAADAMGGLSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:PRK07069  83 LVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLraSQPASIVNISSVAAFKAEPDYTAYNASKAAVASLT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 162 RTLSAELLPRG--IRVNGLSPGPVETPAF--TKTGLSDEALnamMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVG 237
Cdd:PRK07069 163 KSIALDCARRGldVRCNSIHPTFIRTGIVdpIFQRLGEEEA---TRKLARGVPLGRLGEPDDVAHAVLYLASDESRFVTG 239

                 ....*....
gi 658549427 238 TELLVDGGM 246
Cdd:PRK07069 240 AELVIDGGI 248
PRK07985 PRK07985
SDR family oxidoreductase;
2-245 2.76e-35

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 127.42  E-value: 2.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTgRNPDTLAEAERI------LGDKAWVIPTDAGDIASQKALAETLA 75
Cdd:PRK07985  45 GRLKDRKALVTGGDSGIGRAAAIAYAREGADVAIS-YLPVEEEDAQDVkkiieeCGRKAVLLPGDLSDEKFARSLVHEAH 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAGDVTHAP-LEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK07985 124 KALGGLDIMALVAGKQVAIPdIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGASIITTSSIQAYQPSPHLLDYAATK 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALnammAEIIKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK07985 204 AAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKI----PQFGQQTPMKRAGQPAELAPVYVYLASQESSY 279
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:PRK07985 280 VTAEVHGVCGG 290
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
3-208 3.64e-35

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: 125.66  E-value: 3.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAwVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:COG3967    2 KLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAANPGLH-TIVLDVADPASIAALAEQVTAEFPDLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGdVTHAplEAWQEDAWD-----RLMGINLKGPFFLIQALLPLL-NNPSSVILC-GSVSARIGLPTSSVYAASKA 155
Cdd:COG3967   81 VLINNAG-IMRA--EDLLDEAEDladaeREITTNLLGPIRLTAAFLPHLkAQPEAAIVNvSSGLAFVPLAVTPTYSATKA 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEA--LNAMMAEIIKL 208
Cdd:COG3967  158 ALHSYTQSLRHQLKDTSVKVIELAPPAVDTDLTGGQGGDPRAmpLDEFADEVMAG 212
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
1-245 3.79e-35

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 125.77  E-value: 3.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAeaerilGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK08220   3 AMDFSGKTVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAFLTQE------DYPFATFVLDVSDAAAVAQVCQRLLAETGP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDaVFLNAGDVTH-APLEAWQEDAWDRLMGINLKGPFFLIQALLPLL-NNPSSVILC-GSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK08220  77 LD-VLVNAAGILRmGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFrRQRSGAIVTvGSNAAHVPRIGMAAYGASKAAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETP---AFTKTGLSDEALNAMMAEIIKL-VPLGRMGSTTELAKAALYLASDESS 233
Cdd:PRK08220 156 TSLAKCVGLELAPYGVRCNVVSPGSTDTDmqrTLWVDEDGEQQVIAGFPEQFKLgIPLGKIARPQEIANAVLFLASDLAS 235
                        250
                 ....*....|..
gi 658549427 234 YTVGTELLVDGG 245
Cdd:PRK08220 236 HITLQDIVVDGG 247
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
4-245 4.52e-35

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 125.89  E-value: 4.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLaeaeriLGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:PRK06171   7 LQGKIIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDG------QHENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAG--------DVT--HAPLEAwQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVILcgSVSARIGLPTS---SV 149
Cdd:PRK06171  81 LVNNAGiniprllvDEKdpAGKYEL-NEAAFDKMFNINQKGVFLMSQAVARqMVKQHDGVIV--NMSSEAGLEGSegqSC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 150 YAASKAALLSLARTLSAELLPRGIRVNGLSPGPVE-----TP------AFTKtGLSDEALNAMMAEiIKLVPLGRMGSTT 218
Cdd:PRK06171 158 YAATKAALNSFTRSWAKELGKHNIRVVGVAPGILEatglrTPeyeealAYTR-GITVEQLRAGYTK-TSTIPLGRSGKLS 235
                        250       260
                 ....*....|....*....|....*..
gi 658549427 219 ELAKAALYLASDESSYTVGTELLVDGG 245
Cdd:PRK06171 236 EVADLVCYLLSDRASYITGVTTNIAGG 262
PRK06128 PRK06128
SDR family oxidoreductase;
1-247 7.40e-35

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 126.51  E-value: 7.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTgRNPDTLAEAERIL------GDKAWVIPTDAGDIASQKALAETL 74
Cdd:PRK06128  50 FGRLQGRKALITGADSGIGRATAIAFAREGADIALN-YLPEEEQDAAEVVqliqaeGRKAVALPGDLKDEAFCRQLVERA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  75 AARWPRLDAVFLNAG-DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAAS 153
Cdd:PRK06128 129 VKELGGLDILVNIAGkQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLPPGASIINTGSIQSYQPSPTLLDYAST 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 154 KAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEiiklVPLGRMGSTTELAKAALYLASDESS 233
Cdd:PRK06128 209 KAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPLQPSGGQPPEKIPDFGSE----TPMKRPGQPVEMAPLYVLLASQESS 284
                        250
                 ....*....|....
gi 658549427 234 YTVGTELLVDGGMG 247
Cdd:PRK06128 285 YVTGEVFGVTGGLL 298
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
7-245 1.16e-34

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: 124.87  E-value: 1.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL-----GDKAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:cd08940    3 KVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAEIEAVRAGlaakhGVKVLYHGADLSKPAAIEDMVAYAQRQFGGV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGdVTH-APLEAWQEDAWDRLMGINLKGPFFLIQALLPLLN--NPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:cd08940   83 DILVNNAG-IQHvAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKkqGWGRIINIASVHGLVASANKSAYVAAKHGVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETP---------AFTKTGLSDEALNAMMAEiikLVPLGRMGSTTELAKAALYLAS 229
Cdd:cd08940  162 GLTKVVALETAGTGVTCNAICPGWVLTPlvekqisalAQKNGVPQEQAARELLLE---KQPSKQFVTPEQLGDTAVFLAS 238
                        250
                 ....*....|....*.
gi 658549427 230 DESSYTVGTELLVDGG 245
Cdd:cd08940  239 DAASQITGTAVSVDGG 254
PRK06398 PRK06398
aldose dehydrogenase; Validated
1-249 2.04e-34

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 124.17  E-value: 2.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKawvipTDAGDIasqKALAETLAARWPR 80
Cdd:PRK06398   1 DLGLKDKVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKEPSYNDVDYFKVDV-----SNKEQV---IKGIDYVISKYGR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK06398  73 IDILVNNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPymLKQDKGVIINIASVQSFAVTRNAAAYVTSKHAVL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRgIRVNGLSPGPVETP-----AFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESS 233
Cdd:PRK06398 153 GLTRSIAVDYAPT-IRCVAVCPGSIRTPllewaAELEVGKDPEHVERKIREWGEMHPMKRVGKPEEVAYVVAFLASDLAS 231
                        250
                 ....*....|....*.
gi 658549427 234 YTVGTELLVDGGMGSL 249
Cdd:PRK06398 232 FITGECVTVDGGLRAL 247
PRK07326 PRK07326
SDR family oxidoreductase;
1-186 9.36e-34

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 121.66  E-value: 9.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWV--IPTDAGDIASQKALAETLAARW 78
Cdd:PRK07326   1 MMSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEEAAAELNNKGNVlgLAADVRDEADVQRAVDAIVAAF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL-NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK07326  81 GGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALkRGGGYIINISSLAGTNFFAGGAAYNASKFGL 160
                        170       180
                 ....*....|....*....|....*....
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK07326 161 VGFSEAAMLDLRQYGIKVSTIMPGSVATH 189
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
4-245 1.12e-33

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: 121.81  E-value: 1.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLaeaERILGDKAWVIPTdAGDIASQKALAETLAARWPrLDA 83
Cdd:cd05351    5 FAGKRALVTGAGKGIGRATVKALAKAGARVVAVSRTQADL---DSLVRECPGIEPV-CVDLSDWDATEEALGSVGP-VDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNN---PSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:cd05351   80 LVNNAAVAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIArgvPGSIVNVSSQASQRALTNHTVYCSTKAALDML 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETpAFTKTGLSDEALNAMMAEIIklvPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:cd05351  160 TKVMALELGPHKIRVNSVNPTVVMT-DMGRDNWSDPEKAKKMLNRI---PLGKFAEVEDVVNAILFLLSDKSSMTTGSTL 235

                 ....*
gi 658549427 241 LVDGG 245
Cdd:cd05351  236 PVDGG 240
PRK06124 PRK06124
SDR family oxidoreductase;
4-246 1.28e-33

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 122.13  E-value: 1.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK06124   9 LAGQVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLEAAVaalRAAGGAAEALAFDIADEEAVAAAFARIDAEHGR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK06124  89 LDILVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYgrIIAITSIAGQVARAGDAVYPAAKQGLT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPAfTKTGLSDEALNAMMAeiiKLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK06124 169 GLMRALAAEFGPHGITSNAIAPGYFATET-NAAMAADPAVGPWLA---QRTPLGRWGRPEEIAGAAVFLASPAASYVNGH 244

                 ....*...
gi 658549427 239 ELLVDGGM 246
Cdd:PRK06124 245 VLAVDGGY 252
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
10-245 1.32e-33

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 128.04  E-value: 1.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILG--DKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLN 87
Cdd:PRK08324 426 LVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGgpDRALGVACDVTDEAAVQAAFEEAALAFGGVDIVVSN 505
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  88 AGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:PRK08324 506 AGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMkaqGLGGSIVFIASKNAVNPGPNFGAYGAAKAAELHLVRQL 585
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 165 SAELLPRGIRVNGLSPGPVetpaFTKTGLSDEALNAMMAEIIKLVP------------LGRMGSTTELAKAALYLASDES 232
Cdd:PRK08324 586 ALELGPDGIRVNGVNPDAV----VRGSGIWTGEWIEARAAAYGLSEeeleefyrarnlLKREVTPEDVAEAVVFLASGLL 661
                        250
                 ....*....|...
gi 658549427 233 SYTVGTELLVDGG 245
Cdd:PRK08324 662 SKTTGAIITVDGG 674
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
1-246 2.76e-33

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 120.79  E-value: 2.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK12936   1 MFDLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALL-PLLNNP-SSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK12936  81 VDILVNNAGITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELThPMMRRRyGRIINITSVVGVTGNPGQANYCASKAGMI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPAFTKtgLSDEALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK12936 161 GFSKSLAQEIATRNVTVNCVAPGFIESAMTGK--LNDKQKEAIMGAI----PMKRMGTGAEVASAVAYLASSEAAYVTGQ 234

                 ....*...
gi 658549427 239 ELLVDGGM 246
Cdd:PRK12936 235 TIHVNGGM 242
PRK07890 PRK07890
short chain dehydrogenase; Provisional
4-245 4.82e-33

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 120.45  E-value: 4.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK07890   3 LKGKVVVVSGVGPGLGRTLAVRAARAGADVVLAARTAERLDEVAaeiDDLGRRALAVPTDITDEDQCANLVALALERFGR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDV-THAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS-SVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK07890  83 VDALVNNAFRVpSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGgSIVMINSMVLRHSQPKYGAYKMAKGALL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPG-----PVET---PAFTKTGLSDEALNAMMAEIIklvPLGRMGSTTELAKAALYLASD 230
Cdd:PRK07890 163 AASQSLATELGPQGIRVNSVAPGyiwgdPLKGyfrHQAGKYGVTVEQIYAETAANS---DLKRLPTDDEVASAVLFLASD 239
                        250
                 ....*....|....*
gi 658549427 231 ESSYTVGTELLVDGG 245
Cdd:PRK07890 240 LARAITGQTLDVNCG 254
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
10-210 5.02e-33

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: 120.05  E-value: 5.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWV-------IPTDAGD-IASQKALAEtlAARWPRL 81
Cdd:cd08939    5 LITGGSSGIGKALAKELVKEGANVIIVARSESKLEEAVEEIEAEANAsgqkvsyISADLSDyEEVEQAFAQ--AVEKGGP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 -DAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:cd08939   83 pDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMkeQRPGHIVFVSSQAALVGIYGYSAYCPSKFALR 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVP 210
Cdd:cd08939  163 GLAESLRQELKPYNIRVSVVYPPDTDTPGFEEENKTKPEETKAIEGSSGPIT 214
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
10-246 5.44e-33

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: 120.26  E-value: 5.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVT-GRNPD----TLAEAERiLGDKAWVIPTDAGDIASQKALAETLAARWPRLDAV 84
Cdd:cd05337    5 IVTGASRGIGRAIATELAARGFDIAINdLPDDDqateVVAEVLA-AGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 FLNAGdVTHAP----LEAwQEDAWDRLMGINLKGPFFLIQAL-LPLLNNPS-------SVILCGSVSARIGLPTSSVYAA 152
Cdd:cd05337   84 VNNAG-IAVRPrgdlLDL-TEDSFDRLIAINLRGPFFLTQAVaRRMVEQPDrfdgphrSIIFVTSINAYLVSPNRGEYCI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETpafTKTGLSDEALNAMMAEiiKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:cd05337  162 SKAGLSMATRLLAYRLADEGIAVHEIRPGLIHT---DMTAPVKEKYDELIAA--GLVPIRRWGQPEDIAKAVRTLASGLL 236
                        250
                 ....*....|....
gi 658549427 233 SYTVGTELLVDGGM 246
Cdd:cd05337  237 PYSTGQPINIDGGL 250
PRK05867 PRK05867
SDR family oxidoreductase;
4-245 7.34e-33

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 120.14  E-value: 7.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL---AEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK05867   7 LHGKRALITGASTGIGKRVALAYVEAGAQVAIAARHLDALeklADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS---SVILCGSVSARI-GLPTS-SVYAASKA 155
Cdd:PRK05867  87 IDIAVCNAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGqggVIINTASMSGHIiNVPQQvSHYCASKA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFtktglsdEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:PRK05867 167 AVIHLTKAMAVELAPHKIRVNSVSPGYILTELV-------EPYTEYQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYM 239
                        250
                 ....*....|
gi 658549427 236 VGTELLVDGG 245
Cdd:PRK05867 240 TGSDIVIDGG 249
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
4-202 2.20e-32

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: 117.79  E-value: 2.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD-KAWVIptDAGDIASQKALAETLAARWPRLD 82
Cdd:cd05370    3 LTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPNiHTIVL--DVGDAESVEALAEALLSEYPNLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQE--DAWDRLMGINLKGPFFLIQALLP-LLNNPSSVIL-CGSVSARIGLPTSSVYAASKAALL 158
Cdd:cd05370   81 ILINNAGIQRPIDLRDPASdlDKADTEIDTNLIGPIRLIKAFLPhLKKQPEATIVnVSSGLAFVPMAANPVYCATKAALH 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMM 202
Cdd:cd05370  161 SYTLALRHQLKDTGVEVVEIVPPAVDTELHEERRNPDGGTPRKM 204
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-246 2.48e-32

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 118.67  E-value: 2.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERI--LGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAIVDYNEETAQAaADKLskDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPL---LNNPSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK08643  83 VVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAfkkLGHGGKIINATSQAGVVGNPELAVYSSTKFAVRGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAFTKTG--LSDEALNAM---MAEIIKLVPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:PRK08643 163 TQTAARDLASEGITVNAYAPGIVKTPMMFDIAhqVGENAGKPDewgMEQFAKDITLGRLSEPEDVANCVSFLAGPDSDYI 242
                        250
                 ....*....|.
gi 658549427 236 VGTELLVDGGM 246
Cdd:PRK08643 243 TGQTIIVDGGM 253
PRK09072 PRK09072
SDR family oxidoreductase;
3-225 3.64e-32

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 118.12  E-value: 3.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAgDIASQKALAETL--AARWPR 80
Cdd:PRK09072   2 DLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRHRWVVA-DLTSEAGREAVLarAREMGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK09072  81 INVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSamVVNVGSTFGSIGYPGYASYCASKFALR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPvetpafTKTGLSDEALNAMMAEiiklvpLG-RMGSTTELAKAAL 225
Cdd:PRK09072 161 GFSEALRRELADTGVRVLYLAPRA------TRTAMNSEAVQALNRA------LGnAMDDPEDVAAAVL 216
PRK06125 PRK06125
short chain dehydrogenase; Provisional
3-248 3.91e-32

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 118.22  E-value: 3.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWV-IPTDAGDIASQKALAEtLAARWPRL 81
Cdd:PRK06125   4 HLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVdVAVHALDLSSPEAREQ-LAAEAGDI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSvilcGSVSARIGLPTSSV---Y---AASKA 155
Cdd:PRK06125  83 DILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGS----GVIVNVIGAAGENPdadYicgSAGNA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTK-------TGLSDEalnAMMAEIIKLVPLGRMGSTTELAKAALYLA 228
Cdd:PRK06125 159 ALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTllkgrarAELGDE---SRWQELLAGLPLGRPATPEEVADLVAFLA 235
                        250       260
                 ....*....|....*....|
gi 658549427 229 SDESSYTVGTELLVDGGMGS 248
Cdd:PRK06125 236 SPRSGYTSGTVVTVDGGISA 255
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
5-245 5.34e-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: 117.44  E-value: 5.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   5 TDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL--AEAERILGDKAWVIPTDAgDIASQKALA---ETLAARWP 79
Cdd:cd08930    1 EDKIILITGAAGLIGKAFCKALLSAGARLILADINAPALeqLKEELTNLYKNRVIALEL-DITSKESIKeliESYLEKFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAG---DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGS---VSA---RI---GLP 145
Cdd:cd08930   80 RIDILINNAYpspKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFkkQGKGSIINIASiygVIApdfRIyenTQM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 146 TSSV-YAASKAALLSLARTLSAELLPRGIRVNGLSPGPV---ETPAFTKtglsdealnammaEIIKLVPLGRMGSTTELA 221
Cdd:cd08930  160 YSPVeYSVIKAGIIHLTKYLAKYYADTGIRVNAISPGGIlnnQPSEFLE-------------KYTKKCPLKRMLNPEDLR 226
                        250       260
                 ....*....|....*....|....
gi 658549427 222 KAALYLASDESSYTVGTELLVDGG 245
Cdd:cd08930  227 GAIIFLLSDASSYVTGQNLVIDGG 250
PRK07814 PRK07814
SDR family oxidoreductase;
3-246 5.59e-32

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 117.96  E-value: 5.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERI--LGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK07814   7 RLDDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLDEvAEQIraAGRRAHVVAADLAHPEATAGLAGQAVEAFG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS---SVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:PRK07814  87 RLDIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSgggSVINISSTMGRLAGRGFAAYGTAKAA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRgIRVNGLSPGPVETPAFTKTGLSDEalnaMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK07814 167 LAHYTRLAALDLCPR-IRVNAIAPGSILTSALEVVAANDE----LRAPMEKATPLRRLGDPEDIAAAAVYLASPAGSYLT 241
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:PRK07814 242 GKTLEVDGGL 251
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-246 7.06e-32

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 117.37  E-value: 7.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPD-----TLAEAERiLGDKAWVIPTDAGDIASQKALAETLAARWPRLDAV 84
Cdd:PRK12745   6 LVTGGRRGIGLGIARALAAAGFDLAINDRPDDeelaaTQQELRA-LGVEVIFFPADVADLSAHEAMLDAAQAAWGRIDCL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 FLNAG--DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALL--------PLLNNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK12745  85 VNNAGvgVKVRGDLLDLTPESFDRVLAINLRGPFFLTQAVAkrmlaqpePEELPHRSIVFVSSVNAIMVSPNRGEYCISK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAftkTGLSDEALNAMMAEiiKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK12745 165 AGLSMAAQLFAARLAEEGIGVYEVRPGLIKTDM---TAPVTAKYDALIAK--GLVPMPRWGEPEDVARAVAALASGDLPY 239
                        250
                 ....*....|..
gi 658549427 235 TVGTELLVDGGM 246
Cdd:PRK12745 240 STGQAIHVDGGL 251
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
7-246 1.13e-31

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: 116.52  E-value: 1.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:cd09761    2 KVAIVTGGGHGIGKQICLDFLEAGDKVVFADIDEERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLS 165
Cdd:cd09761   82 NAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDeLIKNKGRIINIASTRAFQSEPDSEAYAASKGGLVALTHALA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 166 AELLPRgIRVNGLSPGPVETpaftkTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGG 245
Cdd:cd09761  162 MSLGPD-IRVNCISPGWINT-----TEQQEFTAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFITGETFIVDGG 235

                 .
gi 658549427 246 M 246
Cdd:cd09761  236 M 236
PRK12743 PRK12743
SDR family oxidoreductase;
5-246 2.17e-31

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 116.29  E-value: 2.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   5 TDKYTLITGGTSGIGLATAQAFIAEGARVAVT----GRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK12743   1 MAQVAIVTASDSGIGKACALLLAQQGFDIGITwhsdEEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQ-ALLPLLN--NPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK12743  81 IDVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQiAARHMVKqgQGGRIINITSVHEHTPLPGASAYTAAKHAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAftkTGLSDE-ALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK12743 161 GGLTKAMALELVEHGILVNAVAPGAIATPM---NGMDDSdVKPDSRPGI----PLGRPGDTHEIASLVAWLCSEGASYTT 233
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:PRK12743 234 GQSLIVDGGF 243
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
4-248 2.22e-31

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: 116.10  E-value: 2.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL-GDKAWVIPT--DAGDIASQKALAETLAARWPR 80
Cdd:cd08936    8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVDRAVATLqGEGLSVTGTvcHVGKAEDRERLVATAVNLHGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAG---------DVThapleawqEDAWDRLMGINLKGPFFLIQALLPLLNNPS--SVILCGSVSARIGLPTSSV 149
Cdd:cd08936   88 VDILVSNAAvnpffgnilDST--------EEVWDKILDVNVKATALMTKAVVPEMEKRGggSVVIVSSVAAFHPFPGLGP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 150 YAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETpAFTKTGLSDEALNAMMAEIIKlvpLGRMGSTTELAKAALYLAS 229
Cdd:cd08936  160 YNVSKTALLGLTKNLAPELAPRNIRVNCLAPGLIKT-SFSSALWMDKAVEESMKETLR---IRRLGQPEDCAGIVSFLCS 235
                        250
                 ....*....|....*....
gi 658549427 230 DESSYTVGTELLVDGGMGS 248
Cdd:cd08936  236 EDASYITGETVVVGGGTPS 254
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
4-245 2.88e-31

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: 115.70  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD-----KAWVIPTDAGDIASQKALAETLAARW 78
Cdd:cd05330    1 FKDKVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAG-DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKA 155
Cdd:cd05330   81 GRIDGFFNNAGiEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSgmIVNTASVGGIRGVGNQSGYAAAKH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKT--GLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESS 233
Cdd:cd05330  161 GVVGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSlkQLGPENPEEAGEEFVSVNPMKRFGEPEEVAAVVAFLLSDDAG 240
                        250
                 ....*....|..
gi 658549427 234 YTVGTELLVDGG 245
Cdd:cd05330  241 YVNAAVVPIDGG 252
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
10-245 3.75e-31

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: 115.26  E-value: 3.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAerilGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:cd05331    2 IVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEY----GDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNN--PSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAE 167
Cdd:cd05331   78 VLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDrrTGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 168 LLPRGIRVNGLSPGPVETpAFTKTGLSDEALNAMM----AEIIKL-VPLGRMGSTTELAKAALYLASDESSYTVGTELLV 242
Cdd:cd05331  158 LAPYGVRCNVVSPGSTDT-AMQRTLWHDEDGAAQViagvPEQFRLgIPLGKIAQPADIANAVLFLASDQAGHITMHDLVV 236

                 ...
gi 658549427 243 DGG 245
Cdd:cd05331  237 DGG 239
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
10-185 3.88e-31

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: 115.07  E-value: 3.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD----KAWVIPTDAGDIASQKALAETLAARWPRLDAVF 85
Cdd:cd05346    4 LITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELGAkfpvKVLPLQLDVSDRESIEAALENLPEEFRDIDILV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAGDVTH-APLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:cd05346   84 NNAGLALGlDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMiaRNQGHIINLGSIAGRYPYAGGNVYCATKAAVRQFSL 163
                        170       180
                 ....*....|....*....|...
gi 658549427 163 TLSAELLPRGIRVNGLSPGPVET 185
Cdd:cd05346  164 NLRKDLIGTGIRVTNIEPGLVET 186
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
3-245 4.49e-31

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 115.22  E-value: 4.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVT--GRNPD-TLAEAERiLGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK06935  12 SLDGKVAIVTGGNTGLGQGYAVALAKAGADIIITthGTNWDeTRRLIEK-EGRKVTFVQVDLTKPESAEKVVKEALEEFG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK06935  91 KIDILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSgkIINIASMLSFQGGKFVPAYTASKHGV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETpAFTKTGLSDEALNAmmaEIIKLVPLGRMGSTTELAKAALYLASDESSYTVG 237
Cdd:PRK06935 171 AGLTKAFANELAAYNIQVNAIAPGYIKT-ANTAPIRADKNRND---EILKRIPAGRWGEPDDLMGAAVFLASRASDYVNG 246

                 ....*...
gi 658549427 238 TELLVDGG 245
Cdd:PRK06935 247 HILAVDGG 254
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
4-248 6.95e-31

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: 115.25  E-value: 6.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNP---DTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:cd08935    3 LKNKVAVITGGTGVLGGAMARALAQAGAKVAALGRNQekgDKVAKEITALGGRAIALAADVLDRASLERAREEIVAQFGT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAG--------DVTHAPLEAWQ------EDAWDRLMGINLKGPFFLIQALL-PLLNNPS-SVILCGSVSARIGL 144
Cdd:cd08935   83 VDILINGAGgnhpdattDPEHYEPETEQnffdldEEGWEFVFDLNLNGSFLPSQVFGkDMLEQKGgSIINISSMNAFSPL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 145 PTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDE-ALNAMMAEIIKLVPLGRMGSTTELAKA 223
Cdd:cd08935  163 TKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQNRKLLINPDgSYTDRSNKILGRTPMGRFGKPEELLGA 242
                        250       260
                 ....*....|....*....|....*.
gi 658549427 224 ALYLASDE-SSYTVGTELLVDGGMGS 248
Cdd:cd08935  243 LLFLASEKaSSFVTGVVIPVDGGFSA 268
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
4-185 1.01e-30

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 114.22  E-value: 1.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERIL---GDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:cd05332    1 LQGKVVIITGASSGIGEELAYHLARLGARLVLSARREERLEEvKSECLelgAPSPHVVPLDMSDLEDAEQVVEEALKLFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPleaWQEDAWD---RLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:cd05332   81 GLDILINNAGISMRSL---FHDTSIDvdrKIMEVNYFGPVALTKAALPHLieRSQGSIVVVSSIAGKIGVPFRTAYAASK 157
                        170       180       190
                 ....*....|....*....|....*....|.
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:cd05332  158 HALQGFFDSLRAELSEPNISVTVVCPGLIDT 188
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
4-246 2.00e-30

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 113.71  E-value: 2.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDK---AWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK07523   8 LTGRRALVTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAAAESLKGQglsAHALAFDVTDHDAVRAAIDAFEAEIGP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK07523  88 IDILVNNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMiaRGAGKIINIASVQSALARPGIAPYTATKGAVG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPaFTKTGLSDEALNAMMAeiiKLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK07523 168 NLTKGMATDWAKHGLQCNAIAPGYFDTP-LNAALVADPEFSAWLE---KRTPAGRWGKVEELVGACVFLASDASSFVNGH 243

                 ....*...
gi 658549427 239 ELLVDGGM 246
Cdd:PRK07523 244 VLYVDGGI 251
PRK05717 PRK05717
SDR family oxidoreductase;
7-246 3.36e-30

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 113.06  E-value: 3.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAG--DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLN-NPSSVILCGSVSARIGLPTSSVYAASKAALLSLART 163
Cdd:PRK05717  91 NAAiaDPHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRaHNGAIVNLASTRARQSEPDTEAYAASKGGLLALTHA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 164 LSAELLPRgIRVNGLSPGPVET--PAFTKTGLSDEALNAMMaeiiklvPLGRMGSTTELAKAALYLASDESSYTVGTELL 241
Cdd:PRK05717 171 LAISLGPE-IRVNAVSPGWIDArdPSQRRAEPLSEADHAQH-------PAGRVGTVEDVAAMVAWLLSRQAGFVTGQEFV 242

                 ....*
gi 658549427 242 VDGGM 246
Cdd:PRK05717 243 VDGGM 247
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
4-226 3.78e-30

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: 112.63  E-value: 3.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:cd08934    1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALADELeaeGGKALVLELDVTDEQQVDAAVERTVEALGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:cd08934   81 LDILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPhhLLRNKGTIVNISSVAGRVAVRNSAVYNATKFGVN 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPafTKTGLSDEALNAMMAEII-KLVPLgrmgSTTELAKAALY 226
Cdd:cd08934  161 AFSEGLRQEVTERGVRVVVIEPGTVDTE--LRDHITHTITKEAYEERIsTIRKL----QAEDIAAAVRY 223
PRK12742 PRK12742
SDR family oxidoreductase;
1-248 6.12e-30

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 111.77  E-value: 6.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVT-GRNPDTLAEAERILGDKAwvIPTDAGDIasqKALAETLAARWP 79
Cdd:PRK12742   1 MGAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTyAGSKDAAERLAQETGATA--VQTDSADR---DAVIDVVRKSGA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 rLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSA-RIGLPTSSVYAASKAALL 158
Cdd:PRK12742  76 -LDILVVNAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPEGGRIIIIGSVNGdRMPVAGMAAYAASKSALQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAeiIKlvplgRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK12742 155 GMARGLARDFGPRGITINVVQPGPIDTDANPANGPMKDMMHSFMA--IK-----RHGRPEEVAGMVAWLAGPEASFVTGA 227
                        250
                 ....*....|
gi 658549427 239 ELLVDGGMGS 248
Cdd:PRK12742 228 MHTIDGAFGA 237
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
3-245 9.42e-30

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: 111.86  E-value: 9.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDK----AWVIPTDAGDIASQKALAETLAARW 78
Cdd:cd08933    6 RYADKVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAgpgsCKFVPCDVTKEEDIKTLISVTVERF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGdvtHAPLEAWQEDA----WDRLMGINLKGPFFLIQALLPLL-NNPSSVILCGSVSARIGLPTSSVYAAS 153
Cdd:cd08933   86 GRIDCLVNNAG---WHPPHQTTDETsaqeFRDLLNLNLISYFLASKYALPHLrKSQGNIINLSSLVGSIGQKQAAPYVAT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 154 KAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASdESS 233
Cdd:cd08933  163 KGAITAMTKALAVDESRYGVRVNCISPGNIWTPLWEELAAQTPDTLATIKEGELAQLLGRMGTEAESGLAALFLAA-EAT 241
                        250
                 ....*....|..
gi 658549427 234 YTVGTELLVDGG 245
Cdd:cd08933  242 FCTGIDLLLSGG 253
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-245 1.13e-29

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 111.21  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAErilgdkawvIPTDAGDIASQkalAETLAARWPRLDA 83
Cdd:PRK06550   3 FMTKTVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLSGN---------FHFLQLDLSDD---LEPLFDWVPSVDI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDV-THAPLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVI--LCgSVSARIGLPTSSVYAASKAALLS 159
Cdd:PRK06550  71 LCNTAGILdDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPqMLERKSGIIinMC-SIASFVAGGGGAAYTASKHALAG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETPaftkTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTE 239
Cdd:PRK06550 150 FTKQLALDYAKDGIQVFGIAPGAVKTP----MTAADFEPGGLADWVARETPIKRWAEPEEVAELTLFLASGKADYMQGTI 225

                 ....*.
gi 658549427 240 LLVDGG 245
Cdd:PRK06550 226 VPIDGG 231
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
2-245 1.60e-29

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 110.62  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGD--KAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK05786   1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKRMKKTLSKygNIHYVVGDVSSTESARNVIEKAAKVLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEdaWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVS-ARIGLPTSSVYAASKAALL 158
Cdd:PRK05786  81 AIDGLVVTVGGYVEDTVEEFSG--LEEMLTNHIKIPLYAVNASLRFLKEGSSIVLVSSMSgIYKASPDQLSYAVAKAGLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGpvetpaftktglsdealnAMMAEII------KLVPLGR-MGSTTELAKAALYLASDE 231
Cdd:PRK05786 159 KAVEILASELLGRGIRVNGIAPT------------------TISGDFEpernwkKLRKLGDdMAPPEDFAKVIIWLLTDE 220
                        250
                 ....*....|....
gi 658549427 232 SSYTVGTELLVDGG 245
Cdd:PRK05786 221 ADWVDGVVIPVDGG 234
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
10-245 1.88e-29

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: 110.84  E-value: 1.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTlAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:cd05371    6 VVTGGASGLGLATVERLLAQGAKVVILDLPNSP-GETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIVVNCAG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 ------------DVTHaPLEAWQedawdRLMGINLKGPFFLIQALLPLL--NNPSS------VILCGSVSARIGLPTSSV 149
Cdd:cd05371   85 iavaaktynkkgQQPH-SLELFQ-----RVINVNLIGTFNVIRLAAGAMgkNEPDQggergvIINTASVAAFEGQIGQAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 150 YAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFtkTGLSDEALNAMMAEIIklvPLGRMGSTTELAKAALYLAs 229
Cdd:cd05371  159 YSASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDTPLL--AGLPEKVRDFLAKQVP---FPSRLGDPAEYAHLVQHII- 232
                        250
                 ....*....|....*.
gi 658549427 230 dESSYTVGTELLVDGG 245
Cdd:cd05371  233 -ENPYLNGEVIRLDGA 247
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
7-245 2.84e-29

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: 110.08  E-value: 2.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE--RILGD-KAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:cd05323    1 KVAIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAElqAINPKvKATFVQCDVTSWEQLAAAFKKAIEKFGRVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAG-DVTHAPLEAWQEDA-WDRLMGINLKGPFFLIQALLPLL-----NNPSSVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:cd05323   81 LINNAGiLDEKSYLFAGKLPPpWEKTIDVNLTGVINTTYLALHYMdknkgGKGGVIVNIGSVAGLYPAPQFPVYSASKHG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPR-GIRVNGLSPGPVETPAFTktglSDEALNAMMAEIIKLVPlgrmgsTTELAKAALYLASDESSYt 235
Cdd:cd05323  161 VVGFTRSLADLLEYKtGVRVNAICPGFTNTPLLP----DLVAKEAEMLPSAPTQS------PEVVAKAIVYLIEDDEKN- 229
                        250
                 ....*....|
gi 658549427 236 vGTELLVDGG 245
Cdd:cd05323  230 -GAIWIVDGG 238
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
4-246 4.69e-29

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 109.84  E-value: 4.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNP---DTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAeraELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK08085  87 IDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMvkRQAGKIINICSMQSELGRDTITPYAASKGAVK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPaFTKTGLSDEALNAMMAeiiKLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK08085 167 MLTRGMCVELARHNIQVNGIAPGYFKTE-MTKALVEDEAFTAWLC---KRTPAARWGDPQELIGAAVFLSSKASDFVNGH 242

                 ....*...
gi 658549427 239 ELLVDGGM 246
Cdd:PRK08085 243 LLFVDGGM 250
PRK12746 PRK12746
SDR family oxidoreductase;
1-245 4.76e-29

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 110.12  E-value: 4.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAV-TGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK12746   1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIhYGRNKQAADETIREIesnGGKAFLIEADLNSIDGVKKLVEQLKN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  77 RW------PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVY 150
Cdd:PRK12746  81 ELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAEGRVINISSAEVRLGFTGSIAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 151 AASKAALLSLARTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEALNAmmAEIIKLVP----LGRMGSTTELAKAALY 226
Cdd:PRK12746 161 GLSKGALNTMTLPLAKHLGERGITVNTIMPG------YTKTDINAKLLDD--PEIRNFATnssvFGRIGQVEDIADAVAF 232
                        250
                 ....*....|....*....
gi 658549427 227 LASDESSYTVGTELLVDGG 245
Cdd:PRK12746 233 LASSDSRWVTGQIIDVSGG 251
PRK06181 PRK06181
SDR family oxidoreductase;
6-200 4.90e-29

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 110.07  E-value: 4.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   6 DKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNP---DTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGAQLVLAARNEtrlASLAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAW-DRLMGINLKGPFFLIQALLP-LLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK06181  81 ILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPhLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALHGF 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEALNA 200
Cdd:PRK06181 161 FDSLRIELADDGVAVTVVCPG------FVATDIRKRALDG 194
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
7-245 5.22e-29

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 109.47  E-value: 5.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLA----EAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAkdwfEEYGFTEDQVRLKELDVTDTEECAEALAEIEEEEGPVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK12824  83 ILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYgrIINISSVNGLKGQFGQTNYSAAKAGMIGF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAFTKTGlsDEALNAMMAEIiklvPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:PRK12824 163 TKALASEGARYGITVNCIAPGYIATPMVEQMG--PEVLQSIVNQI----PMKRLGTPEEIAAAVAFLVSEAAGFITGETI 236

                 ....*
gi 658549427 241 LVDGG 245
Cdd:PRK12824 237 SINGG 241
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
6-232 1.34e-28

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: 109.24  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   6 DKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL-----GDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:cd05327    1 GKVVVITGANSGIGKETARELAKRGAHVIIACRNEEKGEEAAAEIkketgNAKVEVIQLDLSSLASVRQFAEEFLARFPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAwqEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIG-----LPTSS----- 148
Cdd:cd05327   81 LDILINNAGIMAPPRRLT--KDGFELQFAVNYLGHFLLTNLLLPVLkaSAPSRIVNVSSIAHRAGpidfnDLDLEnnkey 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 149 ----VYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGlsdeaLNAMMAeiiKLVPLGRMGSTTELAKAA 224
Cdd:cd05327  159 spykAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNG-----SFFLLY---KLLRPFLKKSPEQGAQTA 230

                 ....*...
gi 658549427 225 LYLASDES 232
Cdd:cd05327  231 LYAATSPE 238
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-246 2.30e-28

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 108.25  E-value: 2.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERILGDKAWVIPTDAGDIASQKALAETLAARWPR- 80
Cdd:PRK08642   2 QISEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEAlADELGDRAIALQADVTDREQVQAMFATATEHFGKp 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNA-------GDVTHAPLEAWQEDAWDRLMGiNLKGPFFLIQALLPLLNNPSSvilcGSVsarIGLPTSSV---- 149
Cdd:PRK08642  82 ITTVVNNAladfsfdGDARKKADDITWEDFQQQLEG-SVKGALNTIQAALPGMREQGF----GRI---INIGTNLFqnpv 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 150 -----YAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETpaftkTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAA 224
Cdd:PRK08642 154 vpyhdYTTAKAALLGLTRNLAAELGPYGITVNMVSGGLLRT-----TDASAATPDEVFDLIAATTPLRKVTTPQEFADAV 228
                        250       260
                 ....*....|....*....|..
gi 658549427 225 LYLASDESSYTVGTELLVDGGM 246
Cdd:PRK08642 229 LFFASPWARAVTGQNLVVDGGL 250
PRK07577 PRK07577
SDR family oxidoreductase;
4-249 2.70e-28

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 107.51  E-value: 2.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAwviptDAGDIASqkALAETLAARwpRLDA 83
Cdd:PRK07577   1 MSSRTVLVTGATKGIGLALSLRLANLGHQVIGIARSAIDDFPGELFACDLA-----DIEQTAA--TLAQINEIH--PVDA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:PRK07577  72 IVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEgMKLREQGRIVNICSRAIFGALDRTSYSAAKSALVGCTR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 163 TLSAELLPRGIRVNGLSPGPVETPAFTKT---GLSDEalnammAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTE 239
Cdd:PRK07577 152 TWALELAEYGITVNAVAPGPIETELFRQTrpvGSEEE------KRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFITGQV 225
                        250
                 ....*....|
gi 658549427 240 LLVDGGmGSL 249
Cdd:PRK07577 226 LGVDGG-GSL 234
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
3-245 4.14e-28

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 107.63  E-value: 4.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDT---LAEAERILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK06113   8 RLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAanhVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDaWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK06113  88 KVDILVNNAGGGGPKPFDMPMAD-FRRAYELNVFSFFHLSQLVAPEMekNGGGVILTITSMAAENKNINMTSYASSKAAA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFtKTGLSDEALNAMMaeiiKLVPLGRMGSTTELAKAALYLASDESSYTVG 237
Cdd:PRK06113 167 SHLVRNMAFDLGEKNIRVNGIAPGAILTDAL-KSVITPEIEQKML----QHTPIRRLGQPQDIANAALFLCSPAASWVSG 241

                 ....*...
gi 658549427 238 TELLVDGG 245
Cdd:PRK06113 242 QILTVSGG 249
PRK08267 PRK08267
SDR family oxidoreductase;
10-239 6.61e-28

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 106.95  E-value: 6.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDK-AWVIPTDAGDIAS-QKALAETLAARWPRLDAVFLN 87
Cdd:PRK08267   5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGnAWTGALDVTDRAAwDAALADFAAATGGRLDVLFNN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  88 AGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL-NNPSSVIL-CGSVSARIGLPTSSVYAASKAALLSLARTLS 165
Cdd:PRK08267  85 AGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLkATPGARVInTSSASAIYGQPGLAVYSATKFAVRGLTEALD 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658549427 166 AELLPRGIRVNGLSPGPVETPaftktgLSDEALNAMMAEIIKlvplgRMG---STTELAKAAL--YLASDESSYTVGTE 239
Cdd:PRK08267 165 LEWRRHGIRVADVMPLFVDTA------MLDGTSNEVDAGSTK-----RLGvrlTPEDVAEAVWaaVQHPTRLHWPVGKQ 232
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
4-207 9.00e-28

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


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 105.95  E-value: 9.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGA-RVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLaarwPRLD 82
Cdd:cd05354    1 IKDKTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQA----KDVD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVT-HAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLS 159
Cdd:cd05354   77 VVINNAGVLKpATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLkaNGGGAIVNLNSVASLKNFPAMGTYSASKSAAYS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIK 207
Cdd:cd05354  157 LTQGLRAELAAQGTLVLSVHPGPIDTRMAAGAGGPKESPETVAEAVLK 204
PRK05650 PRK05650
SDR family oxidoreductase;
10-208 1.35e-27

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 106.66  E-value: 1.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:PRK05650   4 MITGAASGLGRAIALRWAREGWRLALADVNEEGGEETLkllREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:PRK05650  84 NAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFkrQKSGRIVNIASMAGLMQGPAMSSYNVAKAGVVALSETL 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 658549427 165 SAELLPRGIRVNglspgpVETPAFTKTGLSDEA---LNAMMAEIIKL 208
Cdd:PRK05650 164 LVELADDEIGVH------VVCPSFFQTNLLDSFrgpNPAMKAQVGKL 204
PRK05872 PRK05872
short chain dehydrogenase; Provisional
1-203 2.94e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 106.21  E-value: 2.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILG--DKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK05872   4 MTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGgdDRVLTVVADVTDLAAMQAAAEEAVERF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK05872  84 GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPaLIERRGYVLQVSSLAAFAAAPGMAAYCASKAGV 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMA 203
Cdd:PRK05872 164 EAFANALRLEVAHHGVTVGSAYLSWIDTDLVRDADADLPAFRELRA 209
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
10-246 3.33e-27

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: 104.97  E-value: 3.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITG--GTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERI---LGDKAWVIPTDAGDIASQKALAETLAARWPRLDAv 84
Cdd:cd05372    5 LITGiaNDRSIAWGIAKALHEAGAELAFTYQPEALRKRVEKLaerLGESALVLPCDVSNDEEIKELFAEVKKDWGKLDG- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 flnagdVTHAPLEAWQEDAWDRLMGINLKGpfFLI-------------QALLPLLNNPSSVILCGSVSARIGLPTSSVYA 151
Cdd:cd05372   84 ------LVHSIAFAPKVQLKGPFLDTSRKG--FLKaldisayslvslaKAALPIMNPGGSIVTLSYLGSERVVPGYNVMG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 152 ASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAftKTGLSDeaLNAMMAEIIKLVPLGRMGSTTELAKAALYLASDE 231
Cdd:cd05372  156 VAKAALESSVRYLAYELGRKGIRVNAISAGPIKTLA--ASGITG--FDKMLEYSEQRAPLGRNVTAEEVGNTAAFLLSDL 231
                        250
                 ....*....|....*
gi 658549427 232 SSYTVGTELLVDGGM 246
Cdd:cd05372  232 SSGITGEIIYVDGGY 246
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
10-245 4.81e-27

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: 104.40  E-value: 4.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA--ERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLN 87
Cdd:cd08943    5 LVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVaeAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIVVSN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  88 AGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:cd08943   85 AGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMksqGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLARCL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 165 SAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNA----MMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTEL 240
Cdd:cd08943  165 ALEGGEDGIRVNTVNPDAVFRGSKIWEGVWRAARAKayglLEEEYRTRNLLKREVLPEDVAEAVVAMASEDFGKTTGAIV 244

                 ....*
gi 658549427 241 LVDGG 245
Cdd:cd08943  245 TVDGG 249
PRK06947 PRK06947
SDR family oxidoreductase;
7-245 5.75e-27

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 104.50  E-value: 5.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRN-----PDTLAEAERIlGDKAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINYARdaaaaEETADAVRAA-GGRACVVAGDVANEADVIAMFDAVQSAFGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHA-PLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNP-----SSVILCGSVSARIGLPTSSV-YAASK 154
Cdd:PRK06947  82 DALVNNAGIVAPSmPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrggrgGAIVNVSSIASRLGSPNEYVdYAGSK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEAlnammAEIIKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK06947 162 GAVDTLTLGLAKELGPHGVRVNAVRPGLIETEIHASGGQPGRA-----ARLGAQTPLGRAGEADEVAETIVWLLSDAASY 236
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:PRK06947 237 VTGALLDVGGG 247
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
11-190 6.27e-27

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: 104.00  E-value: 6.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  11 ITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLN 87
Cdd:cd05360    5 ITGASSGIGRATALAFAERGAKVVLAARSAEALHELAREVrelGGEAIAVVADVADAAQVERAADTAVERFGRIDTWVNN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  88 AGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLN--NPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLS 165
Cdd:cd05360   85 AGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRrrGGGALINVGSLLGYRSAPLQAAYSASKHAVRGFTESLR 164
                        170       180
                 ....*....|....*....|....*..
gi 658549427 166 AELLPRG--IRVNGLSPGPVETPAFTK 190
Cdd:cd05360  165 AELAHDGapISVTLVQPTAMNTPFFGH 191
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
4-191 8.21e-27

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: 103.81  E-value: 8.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA----ERILGDKAWVIPTDAGDIASQ--KALAETLAAR 77
Cdd:cd05340    2 LNDRIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRQVadhiNEEGGRQPQWFILDLLTCTSEncQQLAQRIAVN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNA---GDVThaPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLN--NPSSVILCGSVSARIGLPTSSVYAA 152
Cdd:cd05340   82 YPRLDGVLHNAgllGDVC--PLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLksDAGSLVFTSSSVGRQGRANWGAYAV 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKT 191
Cdd:cd05340  160 SKFATEGL*QVLADEYQQRNLRVNCINPGGTRTAMRASA 198
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
1-245 1.03e-26

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 103.82  E-value: 1.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL-AEAERI--LGDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK13394   2 MSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADLNQDGAnAVADEInkAGGKAIGVAMDVTNEDAVNAGIDKVAER 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK13394  82 FGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMykdDRGGVVIYMGSVHSHEASPLKSAYVTAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKT--------GLSDEALNAMMaeIIKLVPLGRMGSTTELAKAALY 226
Cdd:PRK13394 162 HGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLVDKQipeqakelGISEEEVVKKV--MLGKTVDGVFTTVEDVAQTVLF 239
                        250
                 ....*....|....*....
gi 658549427 227 LASDESSYTVGTELLVDGG 245
Cdd:PRK13394 240 LSSFPSAALTGQSFVVSHG 258
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
10-186 1.49e-26

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: 102.79  E-value: 1.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE--AERILGDK-AWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:cd05350    2 LITGASSGIGRALAREFAKAGYNVALAARRTDRLDElkAELLNPNPsVEVEILDVTDEERNQLVIAELEAELGGLDLVII 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:cd05350   82 NAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRghLVLISSVAALRGLPGAAAYSASKAALSSLAESL 161
                        170       180
                 ....*....|....*....|..
gi 658549427 165 SAELLPRGIRVNGLSPGPVETP 186
Cdd:cd05350  162 RYDVKKRGIRVTVINPGFIDTP 183
PRK08264 PRK08264
SDR family oxidoreductase;
6-186 2.33e-26

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 102.27  E-value: 2.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   6 DKYTLITGGTSGIGLATAQAFIAEGAR-VAVTGRNPDTLAEaeriLGDKAWVIPTDAGDIASQKALAETLaarwPRLDAV 84
Cdd:PRK08264   6 GKVVLVTGANRGIGRAFVEQLLARGAAkVYAAARDPESVTD----LGPRVVPLQLDVTDPASVAAAAEAA----SDVTIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 FLNAG-DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL-NNPSSVIL-CGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:PRK08264  78 VNNAGiFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLaANGGGAIVnVLSVLSWVNFPNLGTYSASKAAAWSLT 157
                        170       180
                 ....*....|....*....|....*
gi 658549427 162 RTLSAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK08264 158 QALRAELAPQGTRVLGVHPGPIDTD 182
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
7-185 2.82e-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: 101.82  E-value: 2.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:cd08929    1 KAALVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFL-IQALLPLLNNPSSVIL-CGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:cd08929   81 NAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCiHKAAPALLRRGGGTIVnVGSLAGKNAFKGGAAYNASKFGLLGLSEAA 160
                        170       180
                 ....*....|....*....|.
gi 658549427 165 SAELLPRGIRVNGLSPGPVET 185
Cdd:cd08929  161 MLDLREANIRVVNVMPGSVDT 181
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
1-246 3.41e-26

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 102.39  E-value: 3.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERILGDK---AWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENlVNELGKEghdVYAVQADVSKVEDANRLVEEAVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  77 RWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK12935  81 HFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEgrIISISSIIGQAGGFGQTNYSAAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDeSSY 234
Cdd:PRK12935 161 AGMLGFTKSLALELAKTNVTVNAICPG------FIDTEMVAEVPEEVRQKIVAKIPKKRFGQADEIAKGVVYLCRD-GAY 233
                        250
                 ....*....|..
gi 658549427 235 TVGTELLVDGGM 246
Cdd:PRK12935 234 ITGQQLNINGGL 245
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
4-246 8.63e-26

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 101.68  E-value: 8.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL---AEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK07097   8 LKGKIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVdkgLAAYRELGIEAHGYVCDVTDEDGVQAMVSQIEKEVGV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK07097  88 IDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMikKGHGKIINICSMMSELGRETVSAYAAAKGGLK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETP--AFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK07097 168 MLTKNIASEYGEANIQCNGIGPGYIATPqtAPLRELQADGSRHPFDQFIIAKTPAARWGDPEDLAGPAVFLASDASNFVN 247
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:PRK07097 248 GHILYVDGGI 257
PRK07074 PRK07074
SDR family oxidoreductase;
5-246 1.02e-25

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 101.38  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   5 TDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWV-IPTDAGDIAS-QKALAETLAARWPrLD 82
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDARFVpVACDLTDAASlAAALANAAAERGP-VD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVS--ARIGLPTssvYAASKAALL 158
Cdd:PRK07074  80 VLVANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEgmLKRSRGAVVNIGSVNgmAALGHPA---YSAAKAGLI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGlsdEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK07074 157 HYTKLLAVEYGRFGIRANAVAPGTVKTQAWEARV---AANPQVFEELKKWYPLQDFATPDDVANAVLFLASPAARAITGV 233

                 ....*...
gi 658549427 239 ELLVDGGM 246
Cdd:PRK07074 234 CLPVDGGL 241
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
7-185 1.44e-25

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: 100.00  E-value: 1.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGA-RVAVTGRNPDT-LAEAERIL--GDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:cd05324    1 KVALVTGANRGIGFEIVRQLAKSGPgTVILTARDVERgQAAVEKLRaeGLSVRFHQLDVTDDASIEAAADFVEEKYGGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDV--THAPLEAWQEdAWDRLMGINLKGPFFLIQALLPLLNNPSS--VIlcgSVSARIGLPTSSvYAASKAALL 158
Cdd:cd05324   81 ILVNNAGIAfkGFDDSTPTRE-QARETMKTNFFGTVDVTQALLPLLKKSPAgrIV---NVSSGLGSLTSA-YGVSKAALN 155
                        170       180
                 ....*....|....*....|....*..
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:cd05324  156 ALTRILAKELKETGIKVNACCPGWVKT 182
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
4-181 3.49e-25

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 99.56  E-value: 3.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLA----EAERILGDKAWVIPTDAGDIASQ--KALAETLAAR 77
Cdd:PRK08945  10 LKDRIILVTGAGDGIGREAALTYARHGATVILLGRTEEKLEavydEIEAAGGPQPAIIPLDLLTATPQnyQQLADTIEEQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNA---GDVThaPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNpssvilcgSVSARIGLPTSSV----- 149
Cdd:PRK08945  90 FGRLDGVLHNAgllGELG--PMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLK--------SPAASLVFTSSSVgrqgr 159
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 658549427 150 -----YAASKAALLSLARTLSAELLPRGIRVNGLSPG 181
Cdd:PRK08945 160 anwgaYAVSKFATEGMMQVLADEYQGTNLRVNCINPG 196
PRK05875 PRK05875
short chain dehydrogenase; Provisional
4-247 4.37e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 99.88  E-value: 4.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERI--LGDKAWVI--PTDAGDIASQKALAETLAARW 78
Cdd:PRK05875   5 FQDRTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAaEEIeaLKGAGAVRyePADVTDEDQVARAVDAATAWH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNA-GDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQ--ALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:PRK05875  85 GRLHGVVHCAgGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKhaARELVRGGGGSFVGISSIAASNTHRWFGAYGVTKS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEALN--AMMAEIIKLVPLGRMGSTTELAKAALYLASDESS 233
Cdd:PRK05875 165 AVDHLMKLAADELGPSWVRVNSIRPG------LIRTDLVAPITEspELSADYRACTPLPRVGEVEDVANLAMFLLSDAAS 238
                        250
                 ....*....|....
gi 658549427 234 YTVGTELLVDGGMG 247
Cdd:PRK05875 239 WITGQVINVDGGHM 252
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
3-245 6.29e-25

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: 99.14  E-value: 6.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL--GDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:cd08937    1 RFEGKVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSELVHEVLAEILaaGDAAHVHTADLETYAGAQGVVRAAVERFGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHA-PLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVIL-CGSVSARIGLPTSsvYAASKAAL 157
Cdd:cd08937   81 VDVLINNVGGTIWAkPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPhMLERQQGVIVnVSSIATRGIYRIP--YSAAKGGV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNA-------MMAEIIKLVPLGRMGSTTELAKAALYLASD 230
Cdd:cd08937  159 NALTASLAFEHARDGIRVNAVAPGGTEAPPRKIPRNAAPMSEQekvwyqrIVDQTLDSSLMGRYGTIDEQVRAILFLASD 238
                        250
                 ....*....|....*
gi 658549427 231 ESSYTVGTELLVDGG 245
Cdd:cd08937  239 EASYITGTVLPVGGG 253
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-195 1.15e-24

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 97.84  E-value: 1.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL-AEAERI--LGDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK07666   2 AQSLQGKNALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLkAVAEEVeaYGVKVVIATADVSDYEEVTAAIEQLKNE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:PRK07666  82 LGSIDILINNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMieRQSGDIINISSTAGQKGAAVTSAYSASKF 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSD 195
Cdd:PRK07666 162 GVLGLTESLMQEVRKHNIRVTALTPSTVATDMAVDLGLTD 201
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
10-248 2.11e-24

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: 97.61  E-value: 2.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL---GDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:cd08945    7 LVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATTVKELreaGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVLVN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP---LLNNPSS-VILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:cd08945   87 NAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKaggMLERGTGrIINIASTGGKQGVVHAAPYSASKHGVVGFTK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 163 TLSAELLPRGIRVNGLSPGPVETPAFTK-----TGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVG 237
Cdd:cd08945  167 ALGLELARTGITVNAVCPGFVETPMAASvrehyADIWEVSTEEAFDRITARVPLGRYVTPEEVAGMVAYLIGDGAAAVTA 246
                        250
                 ....*....|.
gi 658549427 238 TELLVDGGMGS 248
Cdd:cd08945  247 QALNVCGGLGN 257
PRK12747 PRK12747
short chain dehydrogenase; Provisional
4-245 2.50e-24

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 97.45  E-value: 2.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE----RILGDKAWVIPTDAGDIASQKALAETLAARW- 78
Cdd:PRK12747   2 LKGKVALVTGASRGIGRAIAKRLANDGALVAIHYGNRKEEAEETvyeiQSNGGSAFSIGANLESLHGVEALYSSLDNELq 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 -----PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAAS 153
Cdd:PRK12747  82 nrtgsTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNSRIINISSAATRISLPDFIAYSMT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 154 KAALLSLARTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEAL-NAMMAEIIKLVP-LGRMGSTTELAKAALYLASDE 231
Cdd:PRK12747 162 KGAINTMTFTLAKQLGARGITVNAILPG------FIKTDMNAELLsDPMMKQYATTISaFNRLGEVEDIADTAAFLASPD 235
                        250
                 ....*....|....
gi 658549427 232 SSYTVGTELLVDGG 245
Cdd:PRK12747 236 SRWVTGQLIDVSGG 249
PRK06101 PRK06101
SDR family oxidoreductase;
10-186 3.63e-24

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 96.86  E-value: 3.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEaeriLGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:PRK06101   5 LITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDE----LHTQSANIFTLAFDVTDHPGTKAALSQLPFIPELWIFNAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 D-------VTHAPLEAwqedawdRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:PRK06101  81 DceymddgKVDATLMA-------RVFNVNVLGVANCIEGIQPHLSCGHRVVIVGSIASELALPRAEAYGASKAAVAYFAR 153
                        170       180
                 ....*....|....*....|....
gi 658549427 163 TLSAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK06101 154 TLQLDLRPKGIEVVTVFPGFVATP 177
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
3-246 4.54e-24

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 96.57  E-value: 4.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVaecGALGTEVRGYAANVTDEEDVEATFAQIAEDFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAG---D-----------VTHAPLEAWQEdawdrLMGINLKGPFFLIQ--ALLPLLNNPSSVILCGSVSARIG 143
Cdd:PRK08217  82 QLNGLINNAGilrDgllvkakdgkvTSKMSLEQFQS-----VIDVNLTGVFLCGReaAAKMIESGSKGVIINISSIARAG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 144 LPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETpAFTKtGLSDEALNAMmaeiIKLVPLGRMGSTTELAKA 223
Cdd:PRK08217 157 NMGQTNYSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIET-EMTA-AMKPEALERL----EKMIPVGRLGEPEEIAHT 230
                        250       260
                 ....*....|....*....|...
gi 658549427 224 ALYLAsdESSYTVGTELLVDGGM 246
Cdd:PRK08217 231 VRFII--ENDYVTGRVLEIDGGL 251
PRK07454 PRK07454
SDR family oxidoreductase;
10-186 5.42e-24

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 96.18  E-value: 5.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPD---TLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:PRK07454  10 LITGASSGIGKATALAFAKAGWDLALVARSQDaleALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQFGCPDVLIN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:PRK07454  90 NAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMraRGGGLIINVSSIAARNAFPQWGAYCVSKAALAAFTKCL 169
                        170       180
                 ....*....|....*....|..
gi 658549427 165 SAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK07454 170 AEEERSHGIRVCTITLGAVNTP 191
PRK06123 PRK06123
SDR family oxidoreductase;
6-245 6.53e-24

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 96.39  E-value: 6.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   6 DKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE----RILGDKAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:PRK06123   2 RKVMIITGASRGIGAATALLAAERGYAVCLNYLRNRDAAEAVvqaiRRQGGEALAVAADVADEADVLRLFEAVDRELGRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDV-THAPLEAWQEDAWDRLMGINLKGPFFL----IQALLPLLNNPSSVIL-CGSVSARIGLPTSSV-YAASK 154
Cdd:PRK06123  82 DALVNNAGILeAQMRLEQMDAARLTRIFATNVVGSFLCareaVKRMSTRHGGRGGAIVnVSSMAARLGSPGEYIdYAASK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnamMAEIIKLVPLGRMGSTTELAKAALYLASDESSY 234
Cdd:PRK06123 162 GAIDTMTIGLAKEVAAEGIRVNAVRPGVIYTEIHASGGEPGR-----VDRVKAGIPMGRGGTAEEVARAILWLLSDEASY 236
                        250
                 ....*....|.
gi 658549427 235 TVGTELLVDGG 245
Cdd:PRK06123 237 TTGTFIDVSGG 247
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
10-245 9.40e-24

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: 95.71  E-value: 9.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPD---TLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:cd05365    3 IVTGGAAGIGKAIAGTLAKAGASVVIADLKSEgaeAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILVN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLE-AWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVIL-CGSVSARIGLPTSSVYAASKAALLSLART 163
Cdd:cd05365   83 NAGGGGPKPFDmPMTEEDFEWAFKLNLFSAFRLSQLCAPhMQKAGGGAILnISSMSSENKNVRIAAYGSSKAAVNHMTRN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 164 LSAELLPRGIRVNGLSPGPVETPAFtKTGLSDEALNAMMAEiiklVPLGRMGSTTELAKAALYLASDESSYTVGTELLVD 243
Cdd:cd05365  163 LAFDLGPKGIRVNAVAPGAVKTDAL-ASVLTPEIERAMLKH----TPLGRLGEPEDIANAALFLCSPASAWVSGQVLTVS 237

                 ..
gi 658549427 244 GG 245
Cdd:cd05365  238 GG 239
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
10-188 9.87e-24

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: 95.39  E-value: 9.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL---AEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:cd05339    3 LITGGGSGIGRLLALEFAKRGAKVVILDINEKGAeetANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILIN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVILC-GSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:cd05339   83 NAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPdMLERNHGHIVTiASVAGLISPAGLADYCASKAAAVGFHESL 162
                        170       180
                 ....*....|....*....|....*..
gi 658549427 165 SAELLP---RGIRVNGLSPGPVETPAF 188
Cdd:cd05339  163 RLELKAygkPGIKTTLVCPYFINTGMF 189
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
7-191 1.09e-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: 95.21  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILG-DKAWVIPTDAGD-IASQKALAETLAARWPRLDAV 84
Cdd:cd08931    1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGaENVVAGALDVTDrAAWAAALADFAAATGGRLDAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 FLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNP--SSVILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:cd08931   81 FNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATpgARVINTASSSAIYGQPDLAVYSATKFAVRGLTE 160
                        170       180
                 ....*....|....*....|....*....
gi 658549427 163 TLSAELLPRGIRVNGLSPGPVETPAFTKT 191
Cdd:cd08931  161 ALDVEWARHGIRVADVWPWFVDTPILTKG 189
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
10-243 1.31e-23

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: 94.19  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNpdtlaeaeriLGDkawvIPTDAGDIASQKALAETLAArwprLDAVFLNAG 89
Cdd:cd11731    2 IVIGATGTIGLAVAQLLSAHGHEVITAGRS----------SGD----YQVDITDEASIKALFEKVGH----FDAIVSTAG 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRlmGINLK--GPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAE 167
Cdd:cd11731   64 DAEFAPLAELTDADFQR--GLNSKllGQINLVRHGLPYLNDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIE 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549427 168 lLPRGIRVNGLSPGPVETPAftktglsdEALNAMMAEIIKlvplgrmGSTTELAKAalYLASDESSYTvGTELLVD 243
Cdd:cd11731  142 -LPRGIRINAVSPGVVEESL--------EAYGDFFPGFEP-------VPAEDVAKA--YVRSVEGAFT-GQVLHVD 198
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
5-245 1.63e-23

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 95.49  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   5 TDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERILG----DKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK12384   1 MNQVAVVIGGGQTLGAFLCHGLAEEGYRVAVADINSEKAANvAQEINAeygeGMAYGFGADATSEQSVLALSRGVDEIFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:PRK12384  81 RVDLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMirdGIQGRIIQINSKSGKVGSKHNSGYSAAKFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGP-VETPAF--------TKTGLSDEALNAMMaeiIKLVPLGRMGSTTELAKAALYL 227
Cdd:PRK12384 161 GVGLTQSLALDLAEYGITVHSLMLGNlLKSPMFqsllpqyaKKLGIKPDEVEQYY---IDKVPLKRGCDYQDVLNMLLFY 237
                        250
                 ....*....|....*...
gi 658549427 228 ASDESSYTVGTELLVDGG 245
Cdd:PRK12384 238 ASPKASYCTGQSINVTGG 255
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
10-185 1.64e-23

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: 94.67  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEG-ARVAVTGRNPDTLAEAERILGDKAWV--IPTDAGD--IASQKALAETLAARwpRLDAV 84
Cdd:cd05325    2 LITGASRGIGLELVRQLLARGnNTVIATCRDPSAATELAALGASHSRLhiLELDVTDeiAESAEAVAERLGDA--GLDVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 FLNAGDVTHAPLEAWQ-EDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILcGSVSARIG------LPTSSVYAASKAAL 157
Cdd:cd05325   80 INNAGILHSYGPASEVdSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKI-INISSRVGsigdntSGGWYSYRASKAAL 158
                        170       180
                 ....*....|....*....|....*...
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:cd05325  159 NMLTKSLAVELKRDGITVVSLHPGWVRT 186
PLN02253 PLN02253
xanthoxin dehydrogenase
3-245 2.09e-23

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 95.66  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDaGDIASQKALAETL---AARWP 79
Cdd:PLN02253  15 RLLGKVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLGQNVCDSLGGEPNVCFFH-CDVTVEDDVSRAVdftVDKFG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGdVTHAP---LEAWQEDAWDRLMGINLKGPFFLIQ--ALLPLLNNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PLN02253  94 TLDIMVNNAG-LTGPPcpdIRNVELSEFEKVFDVNVKGVFLGMKhaARIMIPLKKGSIVSLCSVASAIGGLGPHAYTGSK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVET----PAFTKTGLSDEALNAMMAEIIKLVPL-GRMGSTTELAKAALYLAS 229
Cdd:PLN02253 173 HAVLGLTRSVAAELGKHGIRVNCVSPYAVPTalalAHLPEDERTEDALAGFRAFAGKNANLkGVELTVDDVANAVLFLAS 252
                        250
                 ....*....|....*.
gi 658549427 230 DESSYTVGTELLVDGG 245
Cdd:PLN02253 253 DEARYISGLNLMIDGG 268
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
10-186 4.53e-23

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 93.89  E-value: 4.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEG--ARVAVTGRNPDTLAEAERIL--GDKAWVIPTDAGDIASQKALAETLAARWPRLDAVF 85
Cdd:cd05367    3 ILTGASRGIGRALAEELLKRGspSVVVLLARSEEPLQELKEELrpGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAGDV-THAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS---VILCGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:cd05367   83 NNAGSLgPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkktVVNVSSGAAVNPFKGWGLYCSSKAARDMFF 162
                        170       180
                 ....*....|....*....|....*
gi 658549427 162 RTLSAELlpRGIRVNGLSPGPVETP 186
Cdd:cd05367  163 RVLAAEE--PDVRVLSYAPGVVDTD 185
PRK08263 PRK08263
short chain dehydrogenase; Provisional
5-185 4.98e-23

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 94.33  E-value: 4.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   5 TDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAV 84
Cdd:PRK08263   2 MEKVWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 FLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:PRK08263  82 VNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSghIIQISSIGGISAFPMSGIYHASKWALEGMSE 161
                        170       180
                 ....*....|....*....|...
gi 658549427 163 TLSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK08263 162 ALAQEVAEFGIKVTLVEPGGYST 184
PRK07832 PRK07832
SDR family oxidoreductase;
7-186 9.60e-23

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 93.57  E-value: 9.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERILGDKAWVIPTDAGDIASQ---KALAETLAARWPRLD 82
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQtVADARALGGTVPEHRALDISDYdavAAFAADIHAAHGSMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP----------LLNNPSSVILcgsvsarIGLPTSSVYAA 152
Cdd:PRK07832  81 VVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpmvaagrgghLVNVSSAAGL-------VALPWHAAYSA 153
                        170       180       190
                 ....*....|....*....|....*....|....
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK07832 154 SKFGLRGLSEVLRFDLARHGIGVSVVVPGAVKTP 187
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
10-249 1.40e-22

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: 92.56  E-value: 1.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPdtlAEAERILGDKAWViptdagdiasQKALAETLAARWPRLDAVFLNAG 89
Cdd:cd05328    3 VITGAASGIGAATAELLEDAGHTVIGIDLRE---ADVIADLSTPEGR----------AAAIADVLARCSGVLDGLVNCAG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLeawqedawDRLMGINLKGPFFLIQALLPLL----------------------NNPSSVILCGSVSARI----- 142
Cdd:cd05328   70 VGGTTVA--------GLVLKVNYFGLRALMEALLPRLrkghgpaavvvssiagagwaqdKLELAKALAAGTEARAvalae 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 143 --GLPTSSVYAASKAALLSLARTLSAE-LLPRGIRVNGLSPGPVETP---AFTKTGLSDEALNAMMAeiiklvPLGRMGS 216
Cdd:cd05328  142 haGQPGYLAYAGSKEALTVWTRRRAATwLYGAGVRVNTVAPGPVETPilqAFLQDPRGGESVDAFVT------PMGRRAE 215
                        250       260       270
                 ....*....|....*....|....*....|...
gi 658549427 217 TTELAKAALYLASDESSYTVGTELLVDGGMGSL 249
Cdd:cd05328  216 PDEIAPVIAFLASDAASWINGANLFVDGGLDAS 248
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
9-192 1.58e-22

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: 91.43  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   9 TLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAwvIPTDAGDIASQKALAETLaarwPRLDAVFLNA 88
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALA--RPADVAAELEVWALAQEL----GPLDLLVYAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  89 GDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAEL 168
Cdd:cd11730   75 GAILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKEV 154
                        170       180
                 ....*....|....*....|....
gi 658549427 169 lpRGIRVNGLSPGPVETPAFTKTG 192
Cdd:cd11730  155 --RGLRLTLVRPPAVDTGLWAPPG 176
PRK07109 PRK07109
short chain dehydrogenase; Provisional
1-188 2.70e-22

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 93.45  E-value: 2.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK07109   3 LKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEALAaeiRAAGGEALAVVADVADAEAVQAAADRAEEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:PRK07109  83 LGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMrpRDRGAIIQVGSALAYRSIPLQSAYCAAKH 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 658549427 156 ALLSLARTLSAELLPRG--IRVNGLSPGPVETPAF 188
Cdd:PRK07109 163 AIRGFTDSLRCELLHDGspVSVTMVQPPAVNTPQF 197
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
4-245 2.73e-22

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 92.27  E-value: 2.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL---AEAERILGDKAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:PRK08277   8 LKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAeavVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAG---------DVTHAPLEAWQ------EDAWDRLMGINLKGPFFLIQALL-PLLNNPSSVIL-CGSVSARIG 143
Cdd:PRK08277  88 CDILINGAGgnhpkattdNEFHELIEPTKtffdldEEGFEFVFDLNLLGTLLPTQVFAkDMVGRKGGNIInISSMNAFTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 144 LPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETpAFTKTGLSDE--ALNAMMAEIIKLVPLGRMGSTTELA 221
Cdd:PRK08277 168 LTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLT-EQNRALLFNEdgSLTERANKILAHTPMGRFGKPEELL 246
                        250       260
                 ....*....|....*....|....*
gi 658549427 222 KAALYLASDE-SSYTVGTELLVDGG 245
Cdd:PRK08277 247 GTLLWLADEKaSSFVTGVVLPVDGG 271
PRK09730 PRK09730
SDR family oxidoreductase;
7-245 3.77e-22

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 91.45  E-value: 3.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVT-GRNPDTLAEA-ERI--LGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNyQQNLHAAQEVvNLItqAGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDV-THAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL-----NNPSSVILCGSVSARIGLPTSSV-YAASKA 155
Cdd:PRK09730  82 ALVNNAGILfTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMalkhgGSGGAIVNVSSAASRLGAPGEYVdYAASKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnamMAEIIKLVPLGRMGSTTELAKAALYLASDESSYT 235
Cdd:PRK09730 162 AIDTLTTGLSLEVAAQGIRVNCVRPGFIYTEMHASGGEPGR-----VDRVKSNIPMQRGGQPEEVAQAIVWLLSDKASYV 236
                        250
                 ....*....|
gi 658549427 236 VGTELLVDGG 245
Cdd:PRK09730 237 TGSFIDLAGG 246
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-245 6.76e-22

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 90.73  E-value: 6.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRN--PDTLAEAErILGDKAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:PRK12481   6 LNGKVAIITGCNTGLGQGMAIGLAKAGADIVGVGVAeaPETQAQVE-ALGRKFHFITADLIQQKDIDSIVSQAVEVMGHI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK12481  85 DILINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFvkqGNGGKIINIASMLSFQGGIRVPSYTASKSAVM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETPAfTKTGLSDEALNAmmaEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGT 238
Cdd:PRK12481 165 GLTRALATELSQYNINVNAIAPGYMATDN-TAALRADTARNE---AILERIPASRWGTPDDLAGPAIFLSSSASDYVTGY 240

                 ....*..
gi 658549427 239 ELLVDGG 245
Cdd:PRK12481 241 TLAVDGG 247
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
10-245 7.08e-22

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 90.38  E-value: 7.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGdkAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:PRK06483   6 LITGAGQRIGLALAWHLLAQGQPVIVSYRTHYPAIDGLRQAG--AQCIQADFSTNAGIMAFIDELKQHTDGLRAIIHNAS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL----NNPSSVI-LCGSVSARiGLPTSSVYAASKAALLSLARTL 164
Cdd:PRK06483  84 DWLAEKPGAPLADVLARMMQIHVNAPYLLNLALEDLLrghgHAASDIIhITDYVVEK-GSDKHIAYAASKAALDNMTLSF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 165 SAELLPRgIRVNGLSPG-----PVETPAFTKTGLSDEAL--NAMMAEIIKLVplgrmgsttelakaaLYLAsdESSYTVG 237
Cdd:PRK06483 163 AAKLAPE-VKVNSIAPAlilfnEGDDAAYRQKALAKSLLkiEPGEEEIIDLV---------------DYLL--TSCYVTG 224

                 ....*...
gi 658549427 238 TELLVDGG 245
Cdd:PRK06483 225 RSLPVDGG 232
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
4-198 7.17e-22

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: 90.53  E-value: 7.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGR---------NPDTL------AEAERILGDKAWVIPTDAGDIASQK 68
Cdd:cd05338    1 LSGKVAFVTGASRGIGRAIALRLAKAGATVVVAAKtasegdngsAKSLPgtieetAEEIEAAGGQALPIVVDVRDEDQVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  69 ALAETLAARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVIL-CGSVSARIGLPT 146
Cdd:cd05338   81 ALVEATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPhMVKAGQGHILnISPPLSLRPARG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 658549427 147 SSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGP-VETPAFTK-TGLSDEAL 198
Cdd:cd05338  161 DVAYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPSTaIETPAATElSGGSDPAR 214
PRK08219 PRK08219
SDR family oxidoreductase;
9-186 9.25e-22

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 89.99  E-value: 9.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   9 TLITGGTSGIGLATAQAfIAEGARVAVTGRNPDTLAE-AERILGDKAWViptdaGDIASQKALAETLAaRWPRLDAVFLN 87
Cdd:PRK08219   6 ALITGASRGIGAAIARE-LAPTHTLLLGGRPAERLDElAAELPGATPFP-----VDLTDPEAIAAAVE-QLGRLDVLVHN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  88 AGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS-SVILCGSVSARIGLPTSSVYAASKAALLSLARTLSA 166
Cdd:PRK08219  79 AGVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHgHVVFINSGAGLRANPGWGSYAASKFALRALADALRE 158
                        170       180
                 ....*....|....*....|
gi 658549427 167 ElLPRGIRVNGLSPGPVETP 186
Cdd:PRK08219 159 E-EPGNVRVTSVHPGRTDTD 177
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
1-245 9.89e-22

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 90.77  E-value: 9.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNP--DTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK12823   3 NQRFAGKVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSElvHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHA-PLEAWQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSSVILCGSVSAriglpTSSV----YAA 152
Cdd:PRK12823  83 GRIDVLINNVGGTIWAkPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPhMLAQGGGAIVNVSSIA-----TRGInrvpYSA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFT---KTGLSDEALNAMMAEIIKLV----PLGRMGSTTELAKAAL 225
Cdd:PRK12823 158 AKGGVNALTASLAFEYAEHGIRVNAVAPGGTEAPPRRvprNAAPQSEQEKAWYQQIVDQTldssLMKRYGTIDEQVAAIL 237
                        250       260
                 ....*....|....*....|
gi 658549427 226 YLASDESSYTVGTELLVDGG 245
Cdd:PRK12823 238 FLASDEASYITGTVLPVGGG 257
PRK07831 PRK07831
SDR family oxidoreductase;
2-237 1.49e-21

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 90.09  E-value: 1.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGT-SGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIL-----GDKAWVIPTDAGDIASQKALAETLA 75
Cdd:PRK07831  13 GLLAGKVVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELaaelgLGRVEAVVCDVTSEAQVDALIDAAV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVIL-CGSVSARIGLPTSSVYAA 152
Cdd:PRK07831  93 ERLGRLDVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMraRGHGGVIVnNASVLGWRAQHGQAHYAA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGlSDEALnammAEIIKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:PRK07831 173 AKAGVMALTRCSALEAAEYGVRINAVAPSIAMHPFLAKVT-SAELL----DELAAREAFGRAAEPWEVANVIAFLASDYS 247

                 ....*
gi 658549427 233 SYTVG 237
Cdd:PRK07831 248 SYLTG 252
PRK05866 PRK05866
SDR family oxidoreductase;
3-191 1.59e-21

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 90.57  E-value: 1.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERIL--GDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAvADRITraGGDAMAVPCDLSDLDAVDALVADVEKRIG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAwQEDAW---DRLMGINLKGPFFLIQALLP---------LLNNPSSVILCGSVsariglPTS 147
Cdd:PRK05866 117 GVDILINNAGRSIRRPLAE-SLDRWhdvERTMVLNYYAPLRLIRGLAPgmlergdghIINVATWGVLSEAS------PLF 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 658549427 148 SVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKT 191
Cdd:PRK05866 190 SVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMIAPT 233
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
7-245 5.91e-21

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: 88.68  E-value: 5.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPD----TLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:cd05322    3 QVAVVIGGGQTLGEFLCHGLAEAGYDVAVADINSEnaekVADEINAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAALLS 159
Cdd:cd05322   83 LLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMirdGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGP-VETPAF--------TKTGLSDEALNAMMaeiIKLVPLGRMGSTTELAKAALYLASD 230
Cdd:cd05322  163 LTQSLALDLAEHGITVNSLMLGNlLKSPMFqsllpqyaKKLGIKESEVEQYY---IDKVPLKRGCDYQDVLNMLLFYASP 239
                        250
                 ....*....|....*
gi 658549427 231 ESSYTVGTELLVDGG 245
Cdd:cd05322  240 KASYCTGQSINITGG 254
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
4-246 8.92e-21

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 87.76  E-value: 8.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVaVTGRNPDT-----LAEAERILGDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK12938   1 MSQRIAYVTGGMGGIGTSICQRLHKDGFKV-VAGCGPNSprrvkWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS--SVILCGSVSARIGLPTSSVYAASKAA 156
Cdd:PRK12938  80 GEIDVLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGwgRIINISSVNGQKGQFGQTNYSTAKAG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGpvetpaFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTV 236
Cdd:PRK12938 160 IHGFTMSLAQEVATKGVTVNTVSPG------YIGTDMVKAIRPDVLEKIVATIPVRRLGSPDEIGSIVAWLASEESGFST 233
                        250
                 ....*....|
gi 658549427 237 GTELLVDGGM 246
Cdd:PRK12938 234 GADFSLNGGL 243
PRK07201 PRK07201
SDR family oxidoreductase;
2-206 1.04e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 90.78  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK07201 367 GPLVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVaeiRAKGGTAHAYTCDLTDSAAVDHTVKDILAEH 446
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHAPLEAWQEDAWD--RLMGINLKGPFFLIQALLPLLN--------NPSSVilcgSVSARIglPTSS 148
Cdd:PRK07201 447 GHVDYLVNNAGRSIRRSVENSTDRFHDyeRTMAVNYFGAVRLILGLLPHMRerrfghvvNVSSI----GVQTNA--PRFS 520
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658549427 149 VYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTG-------LSDEALNAMMAEII 206
Cdd:PRK07201 521 AYVASKAALDAFSDVAASETLSDGITFTTIHMPLVRTPMIAPTKrynnvptISPEEAADMVVRAI 585
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-245 2.05e-20

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 87.05  E-value: 2.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGT--SGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAE--------- 72
Cdd:PRK12748   3 LMKKIALVTGASrlNGIGAAVCRRLAAKGIDIFFTYWSPYDKTMPWGMHDKEPVLLKEEIESYGVRCEHMEidlsqpyap 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  73 -----TLAARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLP 145
Cdd:PRK12748  83 nrvfyAVSERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVNVRATMLLSSAFAKQYDGKAGgrIINLTSGQSLGPMP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 146 TSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPvetpafTKTGLSDEALnamMAEIIKLVPLGRMGSTTELAKAAL 225
Cdd:PRK12748 163 DELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGP------TDTGWITEEL---KHHLVPKFPQGRVGEPVDAARLIA 233
                        250       260
                 ....*....|....*....|
gi 658549427 226 YLASDESSYTVGTELLVDGG 245
Cdd:PRK12748 234 FLVSEEAKWITGQVIHSEGG 253
PRK05693 PRK05693
SDR family oxidoreductase;
10-185 2.22e-20

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 87.15  E-value: 2.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERIlGDKAwvIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:PRK05693   5 LITGCSSGIGRALADAFKAAGYEVWATARKAEDVEALAAA-GFTA--VQLDVNDGAALARLAEELEAEHGGLDVLINNAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVIL-CGSVSARIGLPTSSVYAASKAALLSLARTLSAEL 168
Cdd:PRK05693  82 YGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVnIGSVSGVLVTPFAGAYCASKAAVHALSDALRLEL 161
                        170
                 ....*....|....*..
gi 658549427 169 LPRGIRVNGLSPGPVET 185
Cdd:PRK05693 162 APFGVQVMEVQPGAIAS 178
PRK07825 PRK07825
short chain dehydrogenase; Provisional
3-194 2.45e-20

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 86.92  E-value: 2.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGdKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:PRK07825   2 DLRGKVVAITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG-LVVGGPLDVTDPASFAAFLDAVEADLGPID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK07825  81 VLVNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPrmVPRGRGHVVNVASLAGKIPVPGMATYCASKHAVVGF 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 658549427 161 ARTLSAELLPRGIRVNglspgpVETPAFTKTGLS 194
Cdd:PRK07825 161 TDAARLELRGTGVHVS------VVLPSFVNTELI 188
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
7-195 2.88e-20

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: 86.75  E-value: 2.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGAR---VAVTGRN---PDTLAEAER-ILGDKAWVIPTDAGDIASQKALAETLAARwp 79
Cdd:cd09806    1 TVVLITGCSSGIGLHLAVRLASDPSKrfkVYATMRDlkkKGRLWEAAGaLAGGTLETLQLDVCDSKSVAAAVERVTER-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:cd09806   79 HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSgrILVTSSVGGLQGLPFNDVYCASKFAL 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETpAFTKTGLSD 195
Cdd:cd09806  159 EGLCESLAVQLLPFNVHLSLIECGPVHT-AFMEKVLGS 195
PRK07024 PRK07024
SDR family oxidoreductase;
11-186 3.81e-20

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 86.14  E-value: 3.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  11 ITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE--AERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNA 88
Cdd:PRK07024   7 ITGASSGIGQALAREYARQGATLGLVARRTDALQAfaARLPKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIANA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  89 GdVTHAPLEAWQED--AWDRLMGINLKGPFFLIQALLPLLNNPSSVILCG--SVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:PRK07024  87 G-ISVGTLTEEREDlaVFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGiaSVAGVRGLPGAGAYSASKAAAIKYLESL 165
                        170       180
                 ....*....|....*....|..
gi 658549427 165 SAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK07024 166 RVELRPAGVRVVTIAPGYIRTP 187
PRK06914 PRK06914
SDR family oxidoreductase;
7-190 3.87e-20

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 86.62  E-value: 3.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPD---TLAE--AERILGDKAWVIPTDAGDIASQKALAETLAaRWPRL 81
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRNPEkqeNLLSqaTQLNLQQNIKVQQLDVTDQNSIHNFQLVLK-EIGRI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLS 159
Cdd:PRK06914  83 DLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSgkIINISSISGRVGFPGLSPYVSSKYALEG 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETPAFTK 190
Cdd:PRK06914 163 FSESLRLELKPFGIDVALIEPGSYNTNIWEV 193
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
2-235 5.01e-20

(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: 85.84  E-value: 5.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAV------------TGRNPDTLAEAERILGDKAWvipTDAGDIASQKA 69
Cdd:cd05353    1 LRFDGRVVLVTGAGGGLGRAYALAFAERGAKVVVndlggdrkgsgkSSSAADKVVDEIKAAGGKAV---ANYDSVEDGEK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  70 LAETLAARWPRLDAVFLNAG---DVTHAPLEawqEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGL 144
Cdd:cd05353   78 IVKTAIDAFGRVDILVNNAGilrDRSFAKMS---EEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFgrIINTSSAAGLYGN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 145 PTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGpVETpAFTKTGLSDEALNAMMAEiiKLVPLgrmgsttelakaA 224
Cdd:cd05353  155 FGQANYSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA-AGS-RMTETVMPEDLFDALKPE--YVAPL------------V 218
                        250
                 ....*....|.
gi 658549427 225 LYLASDESSYT 235
Cdd:cd05353  219 LYLCHESCEVT 229
PRK06482 PRK06482
SDR family oxidoreductase;
10-185 6.36e-20

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 85.94  E-value: 6.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:PRK06482   6 FITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVVSNAG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAE 167
Cdd:PRK06482  86 YGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLrrQGGGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAVAQE 165
                        170
                 ....*....|....*...
gi 658549427 168 LLPRGIRVNGLSPGPVET 185
Cdd:PRK06482 166 VAPFGIEFTIVEPGPART 183
PRK06949 PRK06949
SDR family oxidoreductase;
1-247 1.07e-19

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 85.20  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGR---LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL----AEAERILGDkAWVIPTDAGDIASQK---AL 70
Cdd:PRK06949   1 MGRsinLEGKVALVTGASSGLGARFAQVLAQAGAKVVLASRRVERLkelrAEIEAEGGA-AHVVSLDVTDYQSIKaavAH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  71 AETLAArwpRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQAL----------LPLLNNPSSVILCGSVSA 140
Cdd:PRK06949  80 AETEAG---TIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVakrmiarakgAGNTKPGGRIINIASVAG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 141 RIGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEAlnammAEIIKLVPLGRMGSTTEL 220
Cdd:PRK06949 157 LRVLPQIGLYCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINHHHWETEQG-----QKLVSMLPRKRVGKPEDL 231
                        250       260
                 ....*....|....*....|....*..
gi 658549427 221 AKAALYLASDESSYTVGTELLVDGGMG 247
Cdd:PRK06949 232 DGLLLLLAADESQFINGAIISADDGFG 258
PRK08416 PRK08416
enoyl-ACP reductase;
7-245 1.24e-19

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 84.82  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLA-----EAERILGDKAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:PRK08416   9 KTLVISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEAnkiaeDLEQKYGIKAKAYPLNILEPETYKELFKKIDEDFDRV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAgdvthapleawqedawdRLMGINLKGPFFLIQALLPL-LNN------------------------PSSVILCG 136
Cdd:PRK08416  89 DFFISNA-----------------IISGRAVVGGYTKFMRLKPKgLNNiytatvnafvvgaqeaakrmekvgGGSIISLS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 137 SVSARIGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEalnaMMAEIIKLVPLGRMGS 216
Cdd:PRK08416 152 STGNLVYIENYAGHGTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTDALKAFTNYEE----VKAKTEELSPLNRMGQ 227
                        250       260
                 ....*....|....*....|....*....
gi 658549427 217 TTELAKAALYLASDESSYTVGTELLVDGG 245
Cdd:PRK08416 228 PEDLAGACLFLCSEKASWLTGQTIVVDGG 256
PRK06194 PRK06194
hypothetical protein; Provisional
1-199 1.35e-19

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 85.45  E-value: 1.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDK-AWVI--PTDAGDIASQKALAETLAAR 77
Cdd:PRK06194   1 MKDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQgAEVLgvRTDVSDAAQVEALADAALER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNAGDVTHAPLeaWQEDA--WDRLMGINLKGPFFLIQALLPLL-----NNPSS---VILCGSVSARIGLPTS 147
Cdd:PRK06194  81 FGAVHLLFNNAGVGAGGLV--WENSLadWEWVLGVNLWGVIHGVRAFTPLMlaaaeKDPAYeghIVNTASMAGLLAPPAM 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 658549427 148 SVYAASKAALLSLARTLSAELLPRGIRVnGLSpgpVETPAFTKTGLSDEALN 199
Cdd:PRK06194 159 GIYNVSKHAVVSLTETLYQDLSLVTDQV-GAS---VLCPYFVPTGIWQSERN 206
PRK09134 PRK09134
SDR family oxidoreductase;
10-245 5.01e-19

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 83.44  E-value: 5.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRnpDTLAEAE------RILGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:PRK09134  13 LVTGAARRIGRAIALDLAAHGFDVAVHYN--RSRDEAEalaaeiRALGRRAVALQADLADEAEVRALVARASAALGPITL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSV--YAASKAALLSLA 161
Cdd:PRK09134  91 LVNNASLFEYDSAASFTRASWDRHMATNLRAPFVLAQAFARALPADARGLVVNMIDQRVWNLNPDFlsYTLSKAALWTAT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 162 RTLSAELLPRgIRVNGLSPGPvetpaftkTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLAsDESSYTvGTELL 241
Cdd:PRK09134 171 RTLAQALAPR-IRVNAIGPGP--------TLPSGRQSPEDFARQHAATPLGRGSTPEEIAAAVRYLL-DAPSVT-GQMIA 239

                 ....
gi 658549427 242 VDGG 245
Cdd:PRK09134 240 VDGG 243
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
18-247 6.09e-19

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


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 83.25  E-value: 6.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  18 IGLATAQAFIAEGARVAVTGRNPDTLAEAERI---LGDKaWVIPTDAGDIASQKALAETLAARWPRLDAVflnAGDVTHA 94
Cdd:PRK08415  19 IAYGIAKACFEQGAELAFTYLNEALKKRVEPIaqeLGSD-YVYELDVSKPEHFKSLAESLKKDLGKIDFI---VHSVAFA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  95 PLEAW-------QEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAE 167
Cdd:PRK08415  95 PKEALegsfletSKEAFNIAMEISVYSLIELTRALLPLLNDGASVLTLSYLGGVKYVPHYNVMGVAKAALESSVRYLAVD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 168 LLPRGIRVNGLSPGPVETPAftKTGLSDealnamMAEIIKL----VPLGRMGSTTELAKAALYLASDESSYTVGTELLVD 243
Cdd:PRK08415 175 LGKKGIRVNAISAGPIKTLA--ASGIGD------FRMILKWneinAPLKKNVSIEEVGNSGMYLLSDLSSGVTGEIHYVD 246

                 ....*..
gi 658549427 244 GG---MG 247
Cdd:PRK08415 247 AGyniMG 253
PRK06180 PRK06180
short chain dehydrogenase; Provisional
10-185 6.53e-19

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 83.43  E-value: 6.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIP---TDAGDIASQKALAEtlaARWPRLDAVFL 86
Cdd:PRK06180   8 LITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLldvTDFDAIDAVVADAE---ATFGPIDVLVN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:PRK06180  85 NAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRghIVNITSMGGLITMPGIGYYCGSKFALEGISESL 164
                        170       180
                 ....*....|....*....|.
gi 658549427 165 SAELLPRGIRVNGLSPGPVET 185
Cdd:PRK06180 165 AKEVAPFGIHVTAVEPGSFRT 185
PRK07984 PRK07984
enoyl-ACP reductase FabI;
1-245 9.68e-19

enoyl-ACP reductase FabI;


Pssm-ID: 181187 [Multi-domain]  Cd Length: 262  Bit Score: 82.64  E-value: 9.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLA--TAQAFIAEGARVAVTGRNPDTLAEAERILG--DKAWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK07984   1 MGFLSGKRILVTGVASKLSIAygIAQAMHREGAELAFTYQNDKLKGRVEEFAAqlGSDIVLPCDVAEDASIDAMFAELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  77 RWPRLDAvFLNAgdVTHAPLEAWQEDAWDRLM--------GINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSS 148
Cdd:PRK07984  81 VWPKFDG-FVHS--IGFAPGDQLDGDYVNAVTregfkiahDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 149 VYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAftKTGLSDeaLNAMMAEIIKLVPLGRMGSTTELAKAALYLA 228
Cdd:PRK07984 158 VMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLA--ASGIKD--FRKMLAHCEAVTPIRRTVTIEDVGNSAAFLC 233
                        250
                 ....*....|....*..
gi 658549427 229 SDESSYTVGTELLVDGG 245
Cdd:PRK07984 234 SDLSAGISGEVVHVDGG 250
PRK06179 PRK06179
short chain dehydrogenase; Provisional
10-200 1.08e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 82.64  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPdtlAEAERILGDKawVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:PRK06179   8 LVTGASSGIGRATAEKLARAGYRVFGTSRNP---ARAAPIPGVE--LLELDVTDDASVQAAVDEVIARAGRIDVLVNNAG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLSLARTLSAE 167
Cdd:PRK06179  83 VGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSgrIINISSVLGFLPAPYMALYAASKHAVEGYSESLDHE 162
                        170       180       190
                 ....*....|....*....|....*....|...
gi 658549427 168 LLPRGIRVNglspgPVEtPAFTKTGLSDEALNA 200
Cdd:PRK06179 163 VRQFGIRVS-----LVE-PAYTKTNFDANAPEP 189
PRK07533 PRK07533
enoyl-[acyl-carrier-protein] reductase FabI;
1-246 1.22e-18

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


Pssm-ID: 181020 [Multi-domain]  Cd Length: 258  Bit Score: 82.29  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITG--GTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILG--DKAWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK07533   5 LLPLAGKRGLVVGiaNEQSIAWGCARAFRALGAELAVTYLNDKARPYVEPLAEelDAPIFLPLDVREPGQLEAVFARIAE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  77 RWPRLDAV-----FLNAGDVtHAPLEAWQEDAWDRLMGINLKGpfFLIQALL--PLLNNPSSVILCGSVSARIGLPTSSV 149
Cdd:PRK07533  85 EWGRLDFLlhsiaFAPKEDL-HGRVVDCSREGFALAMDVSCHS--FIRMARLaePLMTNGGSLLTMSYYGAEKVVENYNL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 150 YAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAftKTGLSDeaLNAMMAEIIKLVPLGRMGSTTELAKAALYLAS 229
Cdd:PRK07533 162 MGPVKAALESSVRYLAAELGPKGIRVHAISPGPLKTRA--ASGIDD--FDALLEDAAERAPLRRLVDIDDVGAVAAFLAS 237
                        250
                 ....*....|....*..
gi 658549427 230 DESSYTVGTELLVDGGM 246
Cdd:PRK07533 238 DAARRLTGNTLYIDGGY 254
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
1-245 1.52e-18

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 82.07  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITG--GTSGIGLATAQAFIAEGARVAVT------GRNPDTLAEAERILgDKAWVIPTDAGDIASQKALAE 72
Cdd:PRK07370   1 MLDLTGKKALVTGiaNNRSIAWGIAQQLHAAGAELGITylpdekGRFEKKVRELTEPL-NPSLFLPCDVQDDAQIEETFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  73 TLAARWPRLDAV-----FLNAGDVThAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTS 147
Cdd:PRK07370  80 TIKQKWGKLDILvhclaFAGKEELI-GDFSATSREGFARALEISAYSLAPLCKAAKPLMSEGGSIVTLTYLGGVRAIPNY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 148 SVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGlsdeALNAMMAEIIKLVPLGRMGSTTELAKAALYL 227
Cdd:PRK07370 159 NVMGVAKAALEASVRYLAAELGPKNIRVNAISAGPIRTLASSAVG----GILDMIHHVEEKAPLRRTVTQTEVGNTAAFL 234
                        250
                 ....*....|....*...
gi 658549427 228 ASDESSYTVGTELLVDGG 245
Cdd:PRK07370 235 LSDLASGITGQTIYVDAG 252
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
10-228 1.73e-18

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: 80.25  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGArvavtgrnpdtlaeaerilgdkAWVIPTDagdiasqkalaetlaarwpRLDAVFLNAG 89
Cdd:cd02266    2 LVTGGSGGIGGAIARWLASRGS----------------------PKVLVVS-------------------RRDVVVHNAA 40
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLSLARTLSAE 167
Cdd:cd02266   41 ILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLgrFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASE 120
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658549427 168 LLPRGIRVNGLSPGPVETPAFTKTGLSDEALnammaeIIKLVPLGRMGSTTELAKAALYLA 228
Cdd:cd02266  121 GWGNGLPATAVACGTWAGSGMAKGPVAPEEI------LGNRRHGVRTMPPEEVARALLNAL 175
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
4-245 2.23e-18

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 81.46  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGAR-VAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:PRK08993   8 LEGKVAVVTGCDTGLGQGMALGLAEAGCDiVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHID 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAALLS 159
Cdd:PRK08993  88 ILVNNAGLIRREDAIEFSEKDWDDVMNLNIKSVFFMSQAAAKHFiaqGNGGKIINIASMLSFQGGIRVPSYTASKSGVMG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVETPAfTKTGLSDEALNAmmaEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTE 239
Cdd:PRK08993 168 VTRLMANEWAKHNINVNAIAPGYMATNN-TQQLRADEQRSA---EILDRIPAGRWGLPSDLMGPVVFLASSASDYINGYT 243

                 ....*.
gi 658549427 240 LLVDGG 245
Cdd:PRK08993 244 IAVDGG 249
PRK06997 PRK06997
enoyl-[acyl-carrier-protein] reductase FabI;
1-245 2.28e-18

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


Pssm-ID: 180789 [Multi-domain]  Cd Length: 260  Bit Score: 81.41  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTS--GIGLATAQAFIAEGARVAVT---GRNPDTLAEAERILGDKAwVIPTDAGDIASQKALAETLA 75
Cdd:PRK06997   1 MGFLAGKRILITGLLSnrSIAYGIAKACKREGAELAFTyvgDRFKDRITEFAAEFGSDL-VFPCDVASDEQIDALFASLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAGdvtHAPLEAWQEDAWDRLMGINLKGPF--------FLIQALLPLLNNPSSVILCGSVSARIGLPTS 147
Cdd:PRK06997  80 QHWDGLDGLVHSIG---FAPREAIAGDFLDGLSRENFRIAHdisaysfpALAKAALPMLSDDASLLTLSYLGAERVVPNY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 148 SVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAftKTGLSDealnamMAEIIKLV----PLGRMGSTTELAKA 223
Cdd:PRK06997 157 NTMGLAKASLEASVRYLAVSLGPKGIRANGISAGPIKTLA--ASGIKD------FGKILDFVesnaPLRRNVTIEEVGNV 228
                        250       260
                 ....*....|....*....|..
gi 658549427 224 ALYLASDESSYTVGTELLVDGG 245
Cdd:PRK06997 229 AAFLLSDLASGVTGEITHVDSG 250
PRK06505 PRK06505
enoyl-[acyl-carrier-protein] reductase FabI;
18-245 2.43e-18

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


Pssm-ID: 180596 [Multi-domain]  Cd Length: 271  Bit Score: 81.72  E-value: 2.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  18 IGLATAQAFIAEGARVAVT------GRNPDTLAEAeriLGDKaWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAGDV 91
Cdd:PRK06505  21 IAWGIAKQLAAQGAELAFTyqgealGKRVKPLAES---LGSD-FVLPCDVEDIASVDAVFEALEKKWGKLDFVVHAIGFS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  92 THAPLEAWQEDA----WDRLMGINLKGPFFLIQALLPLLNNPSSVI-LCGSVSARIgLPTSSVYAASKAALLSLARTLSA 166
Cdd:PRK06505  97 DKNELKGRYADTtrenFSRTMVISCFSFTEIAKRAAKLMPDGGSMLtLTYGGSTRV-MPNYNVMGVAKAALEASVRYLAA 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658549427 167 ELLPRGIRVNGLSPGPVETPAftKTGLSDEalNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGG 245
Cdd:PRK06505 176 DYGPQGIRVNAISAGPVRTLA--GAGIGDA--RAIFSYQQRNSPLRRTVTIDEVGGSALYLLSDLSSGVTGEIHFVDSG 250
PRK08017 PRK08017
SDR family oxidoreductase;
7-185 2.89e-18

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 81.29  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERiLGDKAwvIPTDAGDIAS-QKALAETLAARWPRLDAVF 85
Cdd:PRK08017   3 KSVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDVARMNS-LGFTG--ILLDLDDPESvERAADEVIALTDNRLYGLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLART 163
Cdd:PRK08017  80 NNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPamLPHGEGRIVMTSSVMGLISTPGRGAYAASKYALEAWSDA 159
                        170       180
                 ....*....|....*....|..
gi 658549427 164 LSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK08017 160 LRMELRHSGIKVSLIEPGPIRT 181
PRK06139 PRK06139
SDR family oxidoreductase;
1-189 3.27e-18

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 82.08  E-value: 3.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL---AEAERILGDKAWVIPTDAGDIASQKALAETLAAR 77
Cdd:PRK06139   2 MGPLHGAVVVITGASSGIGQATAEAFARRGARLVLAARDEEALqavAEECRALGAEVLVVPTDVTDADQVKALATQAASF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPRLDAVFLNA-----GDVTHAPLEAW----QEDAWDRLMGINLKGPFFLIQALLPLLNNPSsviLCGSVSAriglPTSS 148
Cdd:PRK06139  82 GGRIDVWVNNVgvgavGRFEETPIEAHeqviQTNLIGYMRDAHAALPIFKKQGHGIFINMIS---LGGFAAQ----PYAA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 658549427 149 VYAASKAALLSLARTLSAELLP-RGIRVNGLSPGPVETPAFT 189
Cdd:PRK06139 155 AYSASKFGLRGFSEALRGELADhPDIHVCDVYPAFMDTPGFR 196
PRK08340 PRK08340
SDR family oxidoreductase;
10-246 3.49e-18

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 81.00  E-value: 3.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAgDIASQKALAETLAARWP---RLDAVFL 86
Cdd:PRK08340   4 LVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYGEVYAVKA-DLSDKDDLKNLVKEAWEllgGIDALVW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPL---EAWQEDaWDRLMGINLKGPFFLIQALLP--LLNNPSSVIL-CGSVSARIGLPTSSVYAASKAALLSL 160
Cdd:PRK08340  83 NAGNVRCEPCmlhEAGYSD-WLEAALLHLVAPGYLTTLLIQawLEKKMKGVLVyLSSVSVKEPMPPLVLADVTRAGLVQL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 161 ARTLSAELLPRGIRVNGLSPGPVETPAF--------TKTGLSDEalNAMMAEIIKLVPLGRMGSTTELAKAALYLASDES 232
Cdd:PRK08340 162 AKGVSRTYGGKGIRAYTVLLGSFDTPGArenlariaEERGVSFE--ETWEREVLERTPLKRTGRWEELGSLIAFLLSENA 239
                        250
                 ....*....|....
gi 658549427 233 SYTVGTELLVDGGM 246
Cdd:PRK08340 240 EYMLGSTIVFDGAM 253
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
10-170 4.06e-18

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: 79.06  E-value: 4.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427    10 LITGGTSGIGLATAQAFIAEGAR-VAVTGRNP------DTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:smart00822   4 LITGGLGGLGRALARWLAERGARrLVLLSRSGpdapgaAALLAELEAAGARVTVVACDVADRDALAAVLAAIPAVEGPLT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427    83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLlnNPSSVILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:smart00822  84 GVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELTADL--PLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAE 161

                   ....*...
gi 658549427   163 TLSAELLP 170
Cdd:smart00822 162 YRRARGLP 169
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
10-206 5.20e-18

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 80.19  E-value: 5.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:PRK10538   4 LVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 -DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSA 166
Cdd:PRK10538  84 lALGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMveRNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRT 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 658549427 167 ELLPRGIRVNGLSPGPVETPAFT---------KTGLSDEALNAMMAEII 206
Cdd:PRK10538 164 DLHGTAVRVTDIEPGLVGGTEFSnvrfkgddgKAEKTYQNTVALTPEDV 212
PRK12744 PRK12744
SDR family oxidoreductase;
4-188 1.57e-17

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 79.01  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGAR-VAVTGRNPDTLAEAERIL------GDKAWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK12744   6 LKGKVVLIAGGAKNLGGLIARDLAAQGAKaVAIHYNSAASKADAEETVaavkaaGAKAVAFQADLTTAAAVEKLFDDAKA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  77 RWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSviLCGSVSARIG--LPTSSVYAASK 154
Cdd:PRK12744  86 AFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKSAFFFIKEAGRHLNDNGK--IVTLVTSLLGafTPFYSAYAGSK 163
                        170       180       190
                 ....*....|....*....|....*....|....
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVETPAF 188
Cdd:PRK12744 164 APVEHFTRAASKEFGARGISVTAVGPGPMDTPFF 197
PRK06196 PRK06196
oxidoreductase; Provisional
4-186 1.81e-17

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 79.73  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILgDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:PRK06196  24 LSGKTAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI-DGVEVVMLDLADLESVRAFAERFLDSGRRIDI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGdVTHAPlEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARI------------GLPTSSV 149
Cdd:PRK06196 103 LINNAG-VMACP-ETRVGDGWEAQFATNHLGHFALVNLLWPALaaGAGARVVALSSAGHRRspirwddphftrGYDKWLA 180
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 658549427 150 YAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK06196 181 YGQSKTANALFAVHLDKLGKDQGVRAFSVHPGGILTP 217
PRK05855 PRK05855
SDR family oxidoreductase;
2-185 4.41e-17

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 80.02  E-value: 4.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL---AEAERILGDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK05855 311 GPFSGKLVVVTGAGSGIGRETALAFAREGAEVVASDIDEAAAertAELIRAAGAVAHAYRVDVSDADAMEAFAEWVRAEH 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGdVTHA-PLEAWQEDAWDRLMGINLKGPFF---LIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK05855 391 GVPDIVVNNAG-IGMAgGFLDTSAEDWDRVLDVNLWGVIHgcrLFGRQMVERGTGGHIVNVASAAAYAPSRSLPAYATSK 469
                        170       180       190
                 ....*....|....*....|....*....|.
gi 658549427 155 AALLSLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK05855 470 AAVLMLSECLRAELAAAGIGVTAICPGFVDT 500
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-245 5.64e-17

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 77.52  E-value: 5.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGT--SGIGLATAQAFIAEGARVAVT--------------GRNPDTLAEAERILGDKAWVIPTDAGDI 64
Cdd:PRK12859   1 MNQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIFFTywtaydkempwgvdQDEQIQLQEELLKNGVKVSSMELDLTQN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  65 ASQKALAETLAARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARI 142
Cdd:PRK12859  81 DAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGgrIINMTSGQFQG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 143 GLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPvetpafTKTGLSDEALNammAEIIKLVPLGRMGSTTELAK 222
Cdd:PRK12859 161 PMVGELAYAATKGAIDALTSSLAAEVAHLGITVNAINPGP------TDTGWMTEEIK---QGLLPMFPFGRIGEPKDAAR 231
                        250       260
                 ....*....|....*....|...
gi 658549427 223 AALYLASDESSYTVGTELLVDGG 245
Cdd:PRK12859 232 LIKFLASEEAEWITGQIIHSEGG 254
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
7-209 6.53e-17

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 77.81  E-value: 6.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAE-----GARVAVTGRNPDTLAEAERILgdKAW---------VIPTDAGDIASQKALAE 72
Cdd:cd08941    2 KVVLVTGANSGLGLAICERLLAEddenpELTLILACRNLQRAEAACRAL--LAShpdarvvfdYVLVDLSNMVSVFAAAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  73 TLAARWPRLDAVFLNAG-------DVTHA-------PLEA----------------WQEDAWDRLMGI---NLKGPFFLI 119
Cdd:cd08941   80 ELKKRYPRLDYLYLNAGimpnpgiDWIGAikevltnPLFAvtnptykiqaegllsqGDKATEDGLGEVfqtNVFGHYYLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 120 QALLPLL---NNPSSVILCGSVSARI---------GLPTSSVYAASKAALLSLARTLSAELLPRGIRVNglspgpVETPA 187
Cdd:cd08941  160 RELEPLLcrsDGGSQIIWTSSLNASPkyfslediqHLKGPAPYSSSKYLVDLLSLALNRKFNKLGVYSY------VVHPG 233
                        250       260
                 ....*....|....*....|..
gi 658549427 188 FTKTGLSDEALNAMMAEIIKLV 209
Cdd:cd08941  234 ICTTNLTYGILPPFTWTLALPL 255
PRK07775 PRK07775
SDR family oxidoreductase;
9-207 8.93e-17

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 77.49  E-value: 8.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   9 TLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-AERILGD--KAWVIPTDAGDIASQKALAETLAARWPRLDAVF 85
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEElVDKIRADggEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLART 163
Cdd:PRK07775  93 SGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPgmIERRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVTN 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 658549427 164 LSAELLPRGIRVNGLSPGPvetpafTKTG----LSDEALNAMMAEIIK 207
Cdd:PRK07775 173 LQMELEGTGVRASIVHPGP------TLTGmgwsLPAEVIGPMLEDWAK 214
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
10-246 2.27e-16

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


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 76.12  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-------AERilGDKAWVIPTDAGDIASQKALAETLA----ARW 78
Cdd:TIGR02685   5 VVTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAAStlaaelnARR--PNSAVTCQADLSNSATLFSRCEAIIdacfRAF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   79 PRLDAVFLNAGDVTHAPLeaWQEDAWD-------------RLMGINLKGPFFLIQALLPLL---------NNPSSVILCG 136
Cdd:TIGR02685  83 GRCDVLVNNASAFYPTPL--LRGDAGEgvgdkkslevqvaELFGSNAIAPYFLIKAFAQRQagtraeqrsTNLSIVNLCD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  137 SVSARiGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPG----PVETPAFTKTglsdealnammaEIIKLVPLG 212
Cdd:TIGR02685 161 AMTDQ-PLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAPGlsllPDAMPFEVQE------------DYRRKVPLG 227
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 658549427  213 -RMGSTTELAKAALYLASDESSYTVGTELLVDGGM 246
Cdd:TIGR02685 228 qREASAEQIADVVIFLVSPKAKYITGTCIKVDGGL 262
PRK08703 PRK08703
SDR family oxidoreductase;
1-191 4.17e-16

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 74.97  E-value: 4.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERIL---GDKAWVIPTD---AGDIASQKALAET 73
Cdd:PRK08703   1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARHQKKLEKVyDAIVeagHPEPFAIRFDlmsAEEKEFEQFAATI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  74 LAARWPRLDAVFLNAGDV-THAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNP--SSVILCGSVSARIGLPTSSVY 150
Cdd:PRK08703  81 AEATQGKLDGIVHCAGYFyALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSpdASVIFVGESHGETPKAYWGGF 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 658549427 151 AASKAALLSLARTLSAE--LLPrGIRVNGLSPGPVETPAFTKT 191
Cdd:PRK08703 161 GASKAALNYLCKVAADEweRFG-NLRANVLVPGPINSPQRIKS 202
PRK05876 PRK05876
short chain dehydrogenase; Provisional
10-185 4.44e-16

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 75.38  E-value: 4.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAE---RILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:PRK05876  10 VITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQAVnhlRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLART 163
Cdd:PRK05876  90 NAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLleqGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAET 169
                        170       180
                 ....*....|....*....|..
gi 658549427 164 LSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK05876 170 LAREVTADGIGVSVLCPMVVET 191
PRK08339 PRK08339
short chain dehydrogenase; Provisional
4-245 4.61e-16

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 75.28  E-value: 4.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERILGDKAWVIPTDAGDIASQKALAETLA--ARWPR 80
Cdd:PRK08339   6 LSGKLAFTTASSKGIGFGVARVLARAGADVILLSRNEENLKKArEKIKSESNVDVSYIVADLTKREDLERTVKelKNIGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNP--SSVILCGSVSARIGLPTSSVYAASKAALL 158
Cdd:PRK08339  86 PDIFFFSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKgfGRIIYSTSVAIKEPIPNIALSNVVRISMA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 159 SLARTLSAELLPRGIRVNGLSPGPVETP-----AFTKTGLSDEALNAMMAEIIKLVPLGRMGSTTELAKAALYLASDESS 233
Cdd:PRK08339 166 GLVRTLAKELGPKGITVNGIMPGIIRTDrviqlAQDRAKREGKSVEEALQEYAKPIPLGRLGEPEEIGYLVAFLASDLGS 245
                        250
                 ....*....|..
gi 658549427 234 YTVGTELLVDGG 245
Cdd:PRK08339 246 YINGAMIPVDGG 257
PRK06079 PRK06079
enoyl-[acyl-carrier-protein] reductase FabI;
1-245 5.11e-16

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


Pssm-ID: 235694 [Multi-domain]  Cd Length: 252  Bit Score: 74.76  E-value: 5.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITG--GTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:PRK06079   2 SGILSGKKIVVMGvaNKRSIAWGCAQAIKDQGATVIYTYQNDRMKKSLQKLVDEEDLLVECDVASDESIERAFATIKERV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVflnagdvTHAPLEAWQEDAWDRLMGINLKGpFFLIQ-----ALL-------PLLNNPSSVILC---GSVSArig 143
Cdd:PRK06079  82 GKIDGI-------VHAIAYAKKEELGGNVTDTSRDG-YALAQdisaySLIavakyarPLLNPGASIVTLtyfGSERA--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 144 LPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFtkTGLSDEalNAMMAEIIKLVPLGRMGSTTELAKA 223
Cdd:PRK06079 151 IPNYNVMGIAKAALESSVRYLARDLGKKGIRVNAISAGAVKTLAV--TGIKGH--KDLLKESDSRTVDGVGVTIEEVGNT 226
                        250       260
                 ....*....|....*....|..
gi 658549427 224 ALYLASDESSYTVGTELLVDGG 245
Cdd:PRK06079 227 AAFLLSDLSTGVTGDIIYVDKG 248
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-185 5.18e-16

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 76.80  E-value: 5.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVA---VTGRNPDTLAEAERILGDKAW--VIPTDAGDiasqkALAETLAARW 78
Cdd:PRK08261 208 LAGKVALVTGAARGIGAAIAEVLARDGAHVVcldVPAAGEALAAVANRVGGTALAldITAPDAPA-----RIAEHLAERH 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAG---DVTHAPLEawqEDAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSVYAAS 153
Cdd:PRK08261 283 GGLDIVVHNAGitrDKTLANMD---EARWDSVLAVNLLAPLRITEALLAagALGDGGRIVGVSSISGIAGNRGQTNYAAS 359
                        170       180       190
                 ....*....|....*....|....*....|..
gi 658549427 154 KAALLSLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK08261 360 KAGVIGLVQALAPLLAERGITINAVAPGFIET 391
PRK07889 PRK07889
enoyl-[acyl-carrier-protein] reductase FabI;
1-249 5.65e-16

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


Pssm-ID: 236124 [Multi-domain]  Cd Length: 256  Bit Score: 74.98  E-value: 5.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITG--GTSGIGLATAQAFIAEGARVAVTGRnPDTLAEAERI---LGDKAWVIPTDAGDIASQKALAETLA 75
Cdd:PRK07889   2 MGLLEGKRILVTGviTDSSIAFHVARVAQEQGAEVVLTGF-GRALRLTERIakrLPEPAPVLELDVTNEEHLASLADRVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAGdvtHAPLEAwqedawdrlMGIN-LKGPF---------------FLIQALLPLLNNPSSVIlcG-SV 138
Cdd:PRK07889  81 EHVDGLDGVVHSIG---FAPQSA---------LGGNfLDAPWedvatalhvsayslkSLAKALLPLMNEGGSIV--GlDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 139 SARIGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTK-TGLsdEALNAMMAEiikLVPLG-RMGS 216
Cdd:PRK07889 147 DATVAWPAYDWMGVAKAALESTNRYLARDLGPRGIRVNLVAAGPIRTLAAKAiPGF--ELLEEGWDE---RAPLGwDVKD 221
                        250       260       270
                 ....*....|....*....|....*....|...
gi 658549427 217 TTELAKAALYLASDESSYTVGTELLVDGGMGSL 249
Cdd:PRK07889 222 PTPVARAVVALLSDWFPATTGEIVHVDGGAHAM 254
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
10-187 6.13e-16

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: 74.28  E-value: 6.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGrnpdtLAEAERilGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVFLNAG 89
Cdd:cd05334    5 LVYGGRGALGSAVVQAFKSRGWWVASID-----LAENEE--ADASIIVLDSDSFTEQAKQVVASVARLSGKVDALICVAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPLEAWQE-DAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAEL 168
Cdd:cd05334   78 GWAGGSAKSKSFvKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAEN 157
                        170       180
                 ....*....|....*....|.
gi 658549427 169 --LPRGIRVNGLSPGPVETPA 187
Cdd:cd05334  158 sgLPAGSTANAILPVTLDTPA 178
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
10-245 7.69e-16

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: 74.15  E-value: 7.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDiaSQKALAETLAArWPRLDAVFLNag 89
Cdd:cd05361    5 LVTHARHFAGPASAEALTEDGYTVVCHDASFADAAERQAFESENPGTKALSEQK--PEELVDAVLQA-GGAIDVLVSN-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHAPL----EAWQEDAWDRLMGINLKgPFFLIQALLPLLN--NPSSVILCGSVSARIGLPTSSVYAASKAALLSLART 163
Cdd:cd05361   80 DYIPRPMnpidGTSEADIRQAFEALSIF-PFALLQAAIAQMKkaGGGSIIFITSAVPKKPLAYNSLYGPARAAAVALAES 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 164 LSAELLPRGIRVNGLSPGPVETPAFTKTglSDEALN-AMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLV 242
Cdd:cd05361  159 LAKELSRDNILVYAIGPNFFNSPTYFPT--SDWENNpELRERVKRDVPLGRLGRPDEMGALVAFLASRRADPITGQFFAF 236

                 ...
gi 658549427 243 DGG 245
Cdd:cd05361  237 AGG 239
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-245 1.48e-15

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 73.60  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRN-----PDTLAEAERILGDkAWVIPTDAGDIASQKALAETLA 75
Cdd:PRK06077   1 MYSLKDKVVVVTGSGRGIGRAIAVRLAKEGSLVVVNAKKraeemNETLKMVKENGGE-GIGVLADVSTREGCETLAKATI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:PRK06077  80 DRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMREGGAIVNIASVAGIRPAYGLSIYGAMKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 156 ALLSLARTLSAELLPRgIRVNGLSPGPVEtpafTKTGLSDEALNAMMAE--IIKLVPLGRMGSTTELAKAALYLASDESs 233
Cdd:PRK06077 160 AVINLTKYLALELAPK-IRVNAIAPGFVK----TKLGESLFKVLGMSEKefAEKFTLMGKILDPEEVAEFVAAILKIES- 233
                        250
                 ....*....|..
gi 658549427 234 yTVGTELLVDGG 245
Cdd:PRK06077 234 -ITGQVFVLDSG 244
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
10-189 2.69e-15

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: 72.80  E-value: 2.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL----AEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVF 85
Cdd:cd05373    3 AVVGAGDGLGAAIARRFAAEGFSVALAARREAKLeallVDIIRDAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLART 163
Cdd:cd05373   83 YNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMlaRGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQS 162
                        170       180
                 ....*....|....*....|....*..
gi 658549427 164 LSAELLPRGIRV-NGLSPGPVETPAFT 189
Cdd:cd05373  163 MARELGPKGIHVaHVIIDGGIDTDFIR 189
PRK05993 PRK05993
SDR family oxidoreductase;
10-194 3.49e-15

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 73.14  E-value: 3.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLA--EAERILgdkawVIPTDAGDIASQKALAETLAARWP-RLDAVFL 86
Cdd:PRK05993   8 LITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAalEAEGLE-----AFQLDYAEPESIAALVAQVLELSGgRLDALFN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 N-----AGDVTHAPLEAWQEdawdrlmgiNLKGPFF----LIQALLPLL--NNPSSVILCGSVSARIGLPTSSVYAASKA 155
Cdd:PRK05993  83 NgaygqPGAVEDLPTEALRA---------QFEANFFgwhdLTRRVIPVMrkQGQGRIVQCSSILGLVPMKYRGAYNASKF 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 658549427 156 ALLSLARTLSAELLPRGIRVNGLSPGPVETpAFTKTGLS 194
Cdd:PRK05993 154 AIEGLSLTLRMELQGSGIHVSLIEPGPIET-RFRANALA 191
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
4-230 5.20e-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: 5.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRN-----PDTLAEAERiLGDKAWVIPTDAGDIASQKALAETLAARW 78
Cdd:cd09763    1 LSGKIALVTGASRGIGRGIALQLGEAGATVYITGRTilpqlPGTAEEIEA-RGGKCIPVRCDHSDDDEVEALFERVAREQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 P-RLDAVFLNAGDVTHAPLEA-----WQEDA--WDRLMGINLKGPFFLIQALLPLL---NNPSSVILC--GSVSARIGLP 145
Cdd:cd09763   80 QgRLDILVNNAYAAVQLILVGvakpfWEEPPtiWDDINNVGLRAHYACSVYAAPLMvkaGKGLIVIISstGGLEYLFNVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 146 tssvYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMmaeiiKLVPLGRMGSTTELA-KAA 224
Cdd:cd09763  160 ----YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTELVLEMPEDDEGSWHA-----KERDAFLNGETTEYSgRCV 230

                 ....*.
gi 658549427 225 LYLASD 230
Cdd:cd09763  231 VALAAD 236
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
10-170 5.41e-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: 73.57  E-value: 5.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGAR-VAVTGRNPDTLAEAERI-----LGDKAWVIPTDAGDIASQKALAETLAARWPrLDA 83
Cdd:cd05274  154 LITGGLGGLGLLVARWLAARGARhLVLLSRRGPAPRAAARAallraGGARVSVVRCDVTDPAALAALLAELAAGGP-LAG 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLlnNPSSVILCGSVSARIGLPTSSVYAASKAALLSLART 163
Cdd:cd05274  233 VIHAAGVLRDALLAELTPAAFAAVLAAKVAGALNLHELTPDL--PLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQ 310

                 ....*..
gi 658549427 164 LSAELLP 170
Cdd:cd05274  311 RRRRGLP 317
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
10-176 5.63e-15

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 73.80  E-value: 5.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRL-----DAV 84
Cdd:COG3347  429 LVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDVTAEAAVAAAFGFAGLdiggsDIG 508
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  85 FLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:COG3347  509 VANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTggqGLGGSSVFAVSKNAAAAAYGAAAAATAKAAAQHLL 588
                        170
                 ....*....|....*
gi 658549427 162 RTLSAELLPRGIRVN 176
Cdd:COG3347  589 RALAAEGGANGINAN 603
PRK08177 PRK08177
SDR family oxidoreductase;
7-185 8.29e-15

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 71.21  E-value: 8.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTlAEAERILGDKAWViPTDAGDIASQKALAETLAARwpRLDAVFL 86
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQ-DTALQALPGVHIE-KLDMNDPASLDQLLQRLQGQ--RFDLLFV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWD--RLMGINLKGPFFLIQALLPLLNNPSSVI-----LCGSVSARIGlPTSSVYAASKAALLS 159
Cdd:PRK08177  78 NAGISGPAHQSAADATAAEigQLFLTNAIAPIRLARRLLGQVRPGQGVLafmssQLGSVELPDG-GEMPLYKASKAALNS 156
                        170       180
                 ....*....|....*....|....*.
gi 658549427 160 LARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK08177 157 MTRSFVAELGEPTLTVLSMHPGWVKT 182
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
7-231 1.00e-14

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: 71.73  E-value: 1.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAER-ILGD----KAWVIPTDAGDIASQKALAETLAARWPRL 81
Cdd:cd09807    2 KTVIITGANTGIGKETARELARRGARVIMACRDMAKCEEAAAeIRRDtlnhEVIVRHLDLASLKSIRAFAAEFLAEEDRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGdVTHAPlEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIG------------LPTS 147
Cdd:cd09807   82 DVLINNAG-VMRCP-YSKTEDGFEMQFGVNHLGHFLLTNLLLDLLkkSAPSRIVNVSSLAHKAGkinfddlnseksYNTG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 148 SVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSdealNAMMAEIIKLVPLGRMGSTTELAKAALYL 227
Cdd:cd09807  160 FAYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELGRHTGIH----HLFLSTLLNPLFWPFVKTPREGAQTSIYL 235

                 ....
gi 658549427 228 ASDE 231
Cdd:cd09807  236 ALAE 239
PRK08159 PRK08159
enoyl-[acyl-carrier-protein] reductase FabI;
1-245 2.50e-14

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


Pssm-ID: 181260 [Multi-domain]  Cd Length: 272  Bit Score: 70.55  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITG--GTSGIGLATAQAFIAEGARVAVTGRNpDTLAE-----AERILGDKawVIPTDAGDIASQKALAET 73
Cdd:PRK08159   5 SGLMAGKRGLILGvaNNRSIAWGIAKACRAAGAELAFTYQG-DALKKrveplAAELGAFV--AGHCDVTDEASIDAVFET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  74 LAARWPRLDAV-----FLNAGDVTHAPLEAwQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILCGSVSARIGLPTSS 148
Cdd:PRK08159  82 LEKKWGKLDFVvhaigFSDKDELTGRYVDT-SRDNFTMTMDISVYSFTAVAQRAEKLMTDGGSILTLTYYGAEKVMPHYN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 149 VYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTG-----LSDEALNAmmaeiiklvPLGRMGSTTELAKA 223
Cdd:PRK08159 161 VMGVAKAALEASVKYLAVDLGPKNIRVNAISAGPIKTLAASGIGdfryiLKWNEYNA---------PLRRTVTIEEVGDS 231
                        250       260
                 ....*....|....*....|..
gi 658549427 224 ALYLASDESSYTVGTELLVDGG 245
Cdd:PRK08159 232 ALYLLSDLSRGVTGEVHHVDSG 253
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
10-240 2.95e-14

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: 71.63  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFI-AEGARVAVTGRNP---------DTLAEAERiLGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:cd08953  209 LVTGGAGGIGRALARALArRYGARLVLLGRSPlppeeewkaQTLAALEA-LGARVLYISADVTDAAAVRRLLEKVRERYG 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQAL--LPLlnnpSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:cd08953  288 AIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQALadEPL----DFFVLFSSVSAFFGGAGQADYAAANAFL 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAellpRGIRVNGLSpgpVETPAFTKTGLSDEALNAMMAEIIKLVPLgrmgsTTELAKAALY--LASDESSYT 235
Cdd:cd08953  364 DAFAAYLRQ----RGPQGRVLS---INWPAWREGGMAADLGARELLARAGLLPI-----EPEEGLQALEqaLSSDLPQVL 431

                 ....*
gi 658549427 236 VGTEL 240
Cdd:cd08953  432 VSPGD 436
PRK07791 PRK07791
short chain dehydrogenase; Provisional
1-249 8.45e-14

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 69.32  E-value: 8.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVT--GRNPDTLAEAE----------RILGDKAWVIPTDAGDIASQK 68
Cdd:PRK07791   1 MGLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVVNdiGVGLDGSASGGsaaqavvdeiVAAGGEAVANGDDIADWDGAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  69 ALAETLAARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPS--------SVILCGSVSA 140
Cdd:PRK07791  81 NLVDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRAESkagravdaRIINTSSGAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 141 RIGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGpvetpafTKTGLSDEALNAMMAEiiklVPLGR--MGSTT 218
Cdd:PRK07791 161 LQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA-------ARTRMTETVFAEMMAK----PEEGEfdAMAPE 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 658549427 219 ELAKAALYLASDESSYTVGTELLVDGGMGSL 249
Cdd:PRK07791 230 NVSPLVVWLGSAESRDVTGKVFEVEGGKISV 260
PRK08690 PRK08690
enoyl-[acyl-carrier-protein] reductase FabI;
1-245 1.27e-13

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


Pssm-ID: 169553 [Multi-domain]  Cd Length: 261  Bit Score: 68.46  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTS--GIGLATAQAFIAEGARVAVTGRNpDTLAEAERILG---DKAWVIPTDAGDIASQKALAETLA 75
Cdd:PRK08690   1 MGFLQGKKILITGMISerSIAYGIAKACREQGAELAFTYVV-DKLEERVRKMAaelDSELVFRCDVASDDEINQVFADLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  76 ARWPRLDAVFLNAGdvtHAPLEAWQEDAWDRL------MGINLKGPFF--LIQALLPLLNNPSSVILCGS-VSARIGLPT 146
Cdd:PRK08690  80 KHWDGLDGLVHSIG---FAPKEALSGDFLDSIsreafnTAHEISAYSLpaLAKAARPMMRGRNSAIVALSyLGAVRAIPN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 147 SSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAftKTGLSDeaLNAMMAEIIKLVPLGRMGSTTELAKAALY 226
Cdd:PRK08690 157 YNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLA--ASGIAD--FGKLLGHVAAHNPLRRNVTIEEVGNTAAF 232
                        250
                 ....*....|....*....
gi 658549427 227 LASDESSYTVGTELLVDGG 245
Cdd:PRK08690 233 LLSDLSSGITGEITYVDGG 251
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
6-190 2.67e-13

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: 67.24  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   6 DKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL----AEAERILGDKAWVIPTDAGDIASQ-KALAETLAArwpr 80
Cdd:cd05356    1 GTWAVVTGATDGIGKAYAEELAKRGFNVILISRTQEKLdavaKEIEEKYGVETKTIAADFSAGDDIyERIEKELEG---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFL--NAGDVTHAP---LEAWQEDAWDrLMGINLKGPFFLIQALLP-LLNNPSSVIL-CGSVSARIGLPTSSVYAAS 153
Cdd:cd05356   77 LDIGILvnNVGISHSIPeyfLETPEDELQD-IINVNVMATLKMTRLILPgMVKRKKGAIVnISSFAGLIPTPLLATYSAS 155
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 658549427 154 KAALLSLARTLSAELLPRGIRVNGLSPGPVETpAFTK 190
Cdd:cd05356  156 KAFLDFFSRALYEEYKSQGIDVQSLLPYLVAT-KMSK 191
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
10-170 2.81e-13

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: 66.05  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   10 LITGGTSGIGLATAQAFIAEGAR-VAVTGRNPDTLAEAERIL------GDKAWVIPTDAGDIASQKALAETLAARWPRLD 82
Cdd:pfam08659   4 LITGGLGGLGRELARWLAERGARhLVLLSRSAAPRPDAQALIaelearGVEVVVVACDVSDPDAVAALLAEIKAEGPPIR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   83 AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLlnNPSSVILCGSVSARIGLPTSSVYAASKAALLSLAR 162
Cdd:pfam08659  84 GVIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEATPDE--PLDFFVLFSSIAGLLGSPGQANYAAANAFLDALAE 161

                  ....*...
gi 658549427  163 TLSAELLP 170
Cdd:pfam08659 162 YRRSQGLP 169
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
7-204 5.71e-13

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: 66.92  E-value: 5.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTlAEAERILGDKAWVIPTDAGDIASQKALAEtlAARWPR------ 80
Cdd:cd09805    1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNG-PGAKELRRVCSDRLRTLQLDVTKPEQIKR--AAQWVKehvgek 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 -LDAVFLNAGDVTHAPLEAWQE-DAWDRLMGINLKGPFFLIQALLPLLNNPSS-VILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:cd09805   78 gLWGLVNNAGILGFGGDEELLPmDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGrVVNVSSMGGRVPFPAGGAYCASKAAV 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAE 204
Cdd:cd09805  158 EAFSDSLRRELQPWGVKVSIIEPGNFKTGITGNSELWEKQAKKLWER 204
PRK08251 PRK08251
SDR family oxidoreductase;
5-185 1.21e-12

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 65.34  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   5 TDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE-----AERILGDKAWVIPTDAGDIASQKALAETLAARWP 79
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEElkaelLARYPGIKVAVAALDVNDHDQVFEVFAEFRDELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  80 RLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIGLP-TSSVYAASKAA 156
Cdd:PRK08251  81 GLDRVIVNAGIGKGARLGTGKFWANKATAETNFVAALAQCEAAMEIFreQGSGHLVLISSVSAVRGLPgVKAAYAASKAG 160
                        170       180
                 ....*....|....*....|....*....
gi 658549427 157 LLSLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK08251 161 VASLGEGLRAELAKTPIKVSTIEPGYIRS 189
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
1-229 1.21e-12

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: 65.61  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAE--AERILGDKAWVIP-----TDAGDIASqkaLAET 73
Cdd:cd05343    1 MERWRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEAlaAECQSAGYPTLFPyqcdlSNEEQILS---MFSA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  74 LAARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFL----IQALLPLLNNPSSVILCGSVSAR--IGLPTS 147
Cdd:cd05343   78 IRTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICtreaYQSMKERNVDDGHIININSMSGHrvPPVSVF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 148 SVYAASKAALLSLARTLSAEL--LPRGIRVNGLSPGPVETPAFTKTGLSDEALNAMMAEIIKLVPLGrmgsttELAKAAL 225
Cdd:cd05343  158 HFYAATKHAVTALTEGLRQELreAKTHIRATSISPGLVETEFAFKLHDNDPEKAAATYESIPCLKPE------DVANAVL 231

                 ....
gi 658549427 226 YLAS 229
Cdd:cd05343  232 YVLS 235
PRK08278 PRK08278
SDR family oxidoreductase;
1-180 1.79e-12

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 65.31  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGR----NPD------TLAEAERILGDKAWVIPTDAGDIASQKAL 70
Cdd:PRK08278   1 MMSLSGKTLFITGASRGIGLAIALRAARDGANIVIAAKtaepHPKlpgtihTAAEEIEAAGGQALPLVGDVRDEDQVAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  71 AETLAARWPRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVS-ARIGLPT 146
Cdd:PRK08278  81 VAKAVERFGGIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLkksENPHILTLSPPLNlDPKWFAP 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 658549427 147 SSVYAASKAALLSLARTLSAELLPRGIRVNGLSP 180
Cdd:PRK08278 161 HTAYTMAKYGMSLCTLGLAEEFRDDGIAVNALWP 194
PRK12428 PRK12428
coniferyl-alcohol dehydrogenase;
22-248 1.86e-12

coniferyl-alcohol dehydrogenase;


Pssm-ID: 237099 [Multi-domain]  Cd Length: 241  Bit Score: 65.02  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  22 TAQAFIAEGARVAVTGRNPDTLAEAErilgdkawVIPTDAGDIASQKALAETLAARwprLDAVFLNAGDVTHAPLEAwqe 101
Cdd:PRK12428   1 TARLLRFLGARVIGVDRREPGMTLDG--------FIQADLGDPASIDAAVAALPGR---IDALFNIAGVPGTAPVEL--- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 102 dawdrLMGINLKGPFFLIQALLPLLNNPSSVILCGSVS---------------------------ARIGLPTSSVYAASK 154
Cdd:PRK12428  67 -----VARVNFLGLRHLTEALLPRMAPGGAIVNVASLAgaewpqrlelhkalaatasfdegaawlAAHPVALATGYQLSK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 155 AALLSL-ARTLSAELLPRGIRVNGLSPGPVETPAFT--KTGLSDEALNAMMAeiiklvPLGRMGSTTELAKAALYLASDE 231
Cdd:PRK12428 142 EALILWtMRQAQPWFGARGIRVNCVAPGPVFTPILGdfRSMLGQERVDSDAK------RMGRPATADEQAAVLVFLCSDA 215
                        250
                 ....*....|....*..
gi 658549427 232 SSYTVGTELLVDGGMGS 248
Cdd:PRK12428 216 ARWINGVNLPVDGGLAA 232
PRK06182 PRK06182
short chain dehydrogenase; Validated
7-186 2.50e-12

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 64.98  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERiLGdkAWVIPTDAGDIASQKALAETLAARWPRLDAVFL 86
Cdd:PRK06182   4 KVALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLAS-LG--VHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  87 NAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASKAALLSLARTL 164
Cdd:PRK06182  81 NAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSgrIINISSMGGKIYTPLGAWYHATKFALEGFSDAL 160
                        170       180
                 ....*....|....*....|..
gi 658549427 165 SAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK06182 161 RLEVAPFGIDVVVIEPGGIKTE 182
PRK07023 PRK07023
SDR family oxidoreductase;
10-185 8.42e-12

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 63.11  E-value: 8.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARV---------AVTGRNPDTLAEAERILGDKAwviptdagdiASQKALAETLAARWPR 80
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAVlgvarsrhpSLAAAAGERLAEVELDLSDAA----------AAAAWLAGDLLAAFVD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 ---LDAVFLNAGDVTH-APLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS--VILCGSVSARIGLPTSSVYAASK 154
Cdd:PRK07023  75 gasRVLLINNAGTVEPiGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAErrILHISSGAARNAYAGWSVYCATK 154
                        170       180       190
                 ....*....|....*....|....*....|.
gi 658549427 155 AALLSLARTLSAElLPRGIRVNGLSPGPVET 185
Cdd:PRK07023 155 AALDHHARAVALD-ANRALRIVSLAPGVVDT 184
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
6-181 1.02e-11

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 63.39  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   6 DKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERILGD----KAWVIPTDAGDIASQKALAETLAARWPR 80
Cdd:cd09809    1 GKVIIITGANSGIGFETARSFALHGAHVILACRNMSRASAAvSRILEEwhkaRVEAMTLDLASLRSVQRFAEAFKAKNSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LDAVFLNAGdvTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL--NNPSSVILCGSVSARIG-LPTSS--------- 148
Cdd:cd09809   81 LHVLVCNAA--VFALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLrrSAPARVIVVSSESHRFTdLPDSCgnldfslls 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 658549427 149 ----------VYAASKAALLSLARTLSAELLPRGIRVNGLSPG 181
Cdd:cd09809  159 ppkkkywsmlAYNRAKLCNILFSNELHRRLSPRGITSNSLHPG 201
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
10-164 1.37e-11

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 63.31  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGA-RVAVTGRNPDTLAEAERILG---DKAWVIPTDAGDIASQKALAETLAARWPRLDAVF 85
Cdd:cd09810    5 VITGASSGLGLAAAKALARRGEwHVVMACRDFLKAEQAAQEVGmpkDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDALV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAG-DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL----NNPSSVILCGSVSARIGLPTSSV-YAASKAALLS 159
Cdd:cd09810   85 CNAAvYLPTAKEPRFTADGFELTVGVNHLGHFLLTNLLLEDLqrseNASPRIVIVGSITHNPNTLAGNVpPRATLGDLEG 164

                 ....*
gi 658549427 160 LARTL 164
Cdd:cd09810  165 LAGGL 169
PRK09186 PRK09186
flagellin modification protein A; Provisional
4-245 2.40e-11

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 61.93  E-value: 2.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILG--DKAWVIPTDAGDIASQKALAETLAA---RW 78
Cdd:PRK09186   2 LKGKTILITGAGGLIGSALVKAILEAGGIVIAADIDKEALNELLESLGkeFKSKKLSLVELDITDQESLEEFLSKsaeKY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNA-------G----DVThapLEAWQEDawdrlMGINLKGPFFLIQALL--------PLLNNPSSVIlcGSVS 139
Cdd:PRK09186  82 GKIDGAVNCAyprnkdyGkkffDVS---LDDFNEN-----LSLHLGSSFLFSQQFAkyfkkqggGNLVNISSIY--GVVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 140 ARI----GLP-TSSV-YAASKAALLSLARTLSAELLPRGIRVNGLSPGpvetpaftktGLSDEALNAMMAEIIKLVPLGR 213
Cdd:PRK09186 152 PKFeiyeGTSmTSPVeYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPG----------GILDNQPEAFLNAYKKCCNGKG 221
                        250       260       270
                 ....*....|....*....|....*....|..
gi 658549427 214 MGSTTELAKAALYLASDESSYTVGTELLVDGG 245
Cdd:PRK09186 222 MLDPDDICGTLVFLLSDQSKYITGQNIIVDDG 253
PRK06953 PRK06953
SDR family oxidoreductase;
7-185 2.57e-11

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 61.24  E-value: 2.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAeAERILGDKAWVIP-TDAGDIAsqkALAETLAARwpRLDAVF 85
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALA-ALQALGAEALALDvADPASVA---GLAWKLDGE--ALDAAV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAG--DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVIlcGSVSARIGL------PTSSVYAASKAAL 157
Cdd:PRK06953  76 YVAGvyGPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGGVL--AVLSSRMGSigdatgTTGWLYRASKAAL 153
                        170       180
                 ....*....|....*....|....*...
gi 658549427 158 LSLARtlSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK06953 154 NDALR--AASLQARHATCIALHPGWVRT 179
PRK08594 PRK08594
enoyl-[acyl-carrier-protein] reductase FabI;
120-245 3.87e-11

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


Pssm-ID: 236308 [Multi-domain]  Cd Length: 257  Bit Score: 61.28  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 120 QALLPLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETpaFTKTGLSDeaLN 199
Cdd:PRK08594 131 REAKKLMTEGGSIVTLTYLGGERVVQNYNVMGVAKASLEASVKYLANDLGKDGIRVNAISAGPIRT--LSAKGVGG--FN 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 658549427 200 AMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGG 245
Cdd:PRK08594 207 SILKEIEERAPLRRTTTQEEVGDTAAFLFSDLSRGVTGENIHVDSG 252
PRK07102 PRK07102
SDR family oxidoreductase;
7-186 4.15e-11

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 61.09  E-value: 4.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTL-AEAERILGDKAWVIPTDAGDIASQKALAETLAARWPRLDAVF 85
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLYLAARDVERLeRLADDLRARGAVAVSTHELDILDTASHAAFLDSLPALPDIVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAG----------DVTHAPLEawqedawdrlMGINLKGPFFLIQALLPLLNNPSSVILCG--SVSARIGLPTSSVYAAS 153
Cdd:PRK07102  82 IAVGtlgdqaaceaDPALALRE----------FRTNFEGPIALLTLLANRFEARGSGTIVGisSVAGDRGRASNYVYGSA 151
                        170       180       190
                 ....*....|....*....|....*....|...
gi 658549427 154 KAALLSLARTLSAELLPRGIRVNGLSPGPVETP 186
Cdd:PRK07102 152 KAALTAFLSGLRNRLFKSGVHVLTVKPGFVRTP 184
PRK07806 PRK07806
SDR family oxidoreductase;
1-88 1.05e-10

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 60.12  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRN----PDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAA 76
Cdd:PRK07806   1 MGDLPGKTALVTGSSRGIGADTAKILAGAGAHVVVNYRQkaprANKVVAEIEAAGGRASAVGADLTDEESVAALMDTARE 80
                         90
                 ....*....|..
gi 658549427  77 RWPRLDAVFLNA 88
Cdd:PRK07806  81 EFGGLDALVLNA 92
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
10-185 1.26e-10

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: 59.81  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDAGDIASQKALAETLAArWPRLDAVFLNAG 89
Cdd:cd08951   11 FITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAADAKAACPGAAGVLIGDLSSLAETRKLADQVNA-IGRFDAVIHNAG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 dVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP---LLNNPSSVILCGSVS------ARIGLPTSSVYAASKAALLSL 160
Cdd:cd08951   90 -ILSGPNRKTPDTGIPAMVAVNVLAPYVLTALIRRpkrLIYLSSGMHRGGNASlddidwFNRGENDSPAYSDSKLHVLTL 168
                        170       180
                 ....*....|....*....|....*
gi 658549427 161 ARtlSAELLPRGIRVNGLSPGPVET 185
Cdd:cd08951  169 AA--AVARRWKDVSSNAVHPGWVPT 191
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
10-183 1.92e-10

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 59.61  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGdkawvIPTDAGDIASQKALAETLAarwpRLDAVFLNAG 89
Cdd:COG0451    3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPG-----VEFVRGDLRDPEALAAALA----GVDAVVHLAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 DVTHApleawqEDAWDRLMGINLKGPFFLIQALlpLLNNPSSVILCGSVSA--RIGLPTS--------SVYAASKAALLS 159
Cdd:COG0451   74 PAGVG------EEDPDETLEVNVEGTLNLLEAA--RAAGVKRFVYASSSSVygDGEGPIDedtplrpvSPYGASKLAAEL 145
                        170       180
                 ....*....|....*....|....
gi 658549427 160 LARTLSAEllpRGIRVNGLSPGPV 183
Cdd:COG0451  146 LARAYARR---YGLPVTILRPGNV 166
PRK06197 PRK06197
short chain dehydrogenase; Provisional
10-143 1.99e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 59.65  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA-ERILGDKAW----VIPTDAGDIASQKALAETLAARWPRLDAV 84
Cdd:PRK06197  20 VVTGANTGLGYETAAALAAKGAHVVLAVRNLDKGKAAaARITAATPGadvtLQELDLTSLASVRAAADALRAAYPRIDLL 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658549427  85 FLNAGdVTHAPLEAwQEDAWDRLMGINLKGPFFLIQALLP-LLNNPSS-VILCGSVSARIG 143
Cdd:PRK06197 100 INNAG-VMYTPKQT-TADGFELQFGTNHLGHFALTGLLLDrLLPVPGSrVVTVSSGGHRIR 158
PRK09291 PRK09291
SDR family oxidoreductase;
5-185 4.91e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 58.09  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   5 TDKYTLITGGTSGIGLATAQAFIAEG----ARVAVTGRNPDTLAEAERiLGDKAWVIP---TDAGDIASqkalaetlAAR 77
Cdd:PRK09291   1 MSKTILITGAGSGFGREVALRLARKGhnviAGVQIAPQVTALRAEAAR-RGLALRVEKldlTDAIDRAQ--------AAE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  78 WPrLDAVFLNAG-----DVTHAPLEAWQEdawdrLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARIGLPTSSVY 150
Cdd:PRK09291  72 WD-VDVLLNNAGigeagAVVDIPVELVRE-----LFETNVFGPLELTQGFVRkmVARGKGKVVFTSSMAGLITGPFTGAY 145
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 658549427 151 AASKAALLSLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:PRK09291 146 CASKHALEAIAEAMHAELKPFGIQVATVNPGPYLT 180
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
124-248 3.89e-09

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 55.78  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 124 PLLNNPSSVILCGSVSARIGLPTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVETPAFTKTGlsdeALNAMMA 203
Cdd:PRK06603 134 ALMHDGGSIVTLTYYGAEKVIPNYNVMGVAKAALEASVKYLANDMGENNIRVNAISAGPIKTLASSAIG----DFSTMLK 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 658549427 204 EIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGG---MGS 248
Cdd:PRK06603 210 SHAATAPLKRNTTQEDVGGAAVYLFSELSKGVTGEIHYVDCGyniMGS 257
PRK07578 PRK07578
short chain dehydrogenase; Provisional
60-184 8.85e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 53.66  E-value: 8.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  60 DAGDIASQKALAETLAarwpRLDAVFLNAGDVTHAPLEAWQEDAW-----DRLMG-INLkgpfflIQALLPLLNNPSSVI 133
Cdd:PRK07578  39 DITDPASIRALFEKVG----KVDAVVSAAGKVHFAPLAEMTDEDFnvglqSKLMGqVNL------VLIGQHYLNDGGSFT 108
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 658549427 134 LCGSVSARIGLPTSSVYAASKAALLSLARTLSAELlPRGIRVNGLSPGPVE 184
Cdd:PRK07578 109 LTSGILSDEPIPGGASAATVNGALEGFVKAAALEL-PRGIRINVVSPTVLT 158
PRK06940 PRK06940
short chain dehydrogenase; Provisional
171-245 9.61e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180766 [Multi-domain]  Cd Length: 275  Bit Score: 54.64  E-value: 9.61e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658549427 171 RGIRVNGLSPGPVETPaftktgLSDEALN----AMMAEIIKLVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGG 245
Cdd:PRK06940 190 RGARINSISPGIISTP------LAQDELNgprgDGYRNMFAKSPAGRPGTPDEIAALAEFLMGPRGSFITGSDFLVDGG 262
KR_2_FAS_SDR_x cd08955
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ...
10-170 7.39e-08

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: 52.29  E-value: 7.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGAR-VAVTGRNPDTLAEAERI-----LGDKAWVIPTDAGDIASQKALAETLAARWPRLDA 83
Cdd:cd08955  153 LITGGLGGLGLLVAEWLVERGARhLVLTGRRAPSAAARQAIaaleeAGAEVVVLAADVSDRDALAAALAQIRASLPPLRG 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQAL--LPLlnnpSSVILCGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:cd08955  233 VIHAAGVLDDGVLANQDWERFRKVLAPKVQGAWNLHQLTqdLPL----DFFVLFSSVASLLGSPGQANYAAANAFLDALA 308

                 ....*....
gi 658549427 162 RTLSAELLP 170
Cdd:cd08955  309 HYRRARGLP 317
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
4-249 1.75e-07

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 50.94  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNP-----DTLAEAeRILGDKAWVIPTDAGDIASQKALAETlAARW 78
Cdd:PRK07792  10 LSGKVAVVTGAAAGLGRAEALGLARLGATVVVNDVASaldasDVLDEI-RAAGAKAVAVAGDISQRATADELVAT-AVGL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  79 PRLDAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLP----------------LLNNPSSVILCGSVsari 142
Cdd:PRK07792  88 GGLDIVVNNAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAywrakakaaggpvygrIVNTSSEAGLVGPV---- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 143 GLPTssvYAASKAALLSLarTLSAEL-LPR-GIRVNGLSPgpvetpaftktglsdEALNAMMAEIIKLVPLGRMG----- 215
Cdd:PRK07792 164 GQAN---YGAAKAGITAL--TLSAARaLGRyGVRANAICP---------------RARTAMTADVFGDAPDVEAGgidpl 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 658549427 216 STTELAKAALYLASDESSYTVGTELLVDGGMGSL 249
Cdd:PRK07792 224 SPEHVVPLVQFLASPAAAEVNGQVFIVYGPMVTL 257
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
10-167 6.92e-07

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 48.83  E-value: 6.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   10 LITGGTSGIGLATAQAFIAEGARVAVTGRnpDTLAEAERILGDKAWVIptdaGDIASQKALAETLAArwPRLDAVFlNAG 89
Cdd:pfam01370   2 LVTGATGFIGSHLVRRLLEKGYEVIGLDR--LTSASNTARLADLRFVE----GDLTDRDALEKLLAD--VRPDAVI-HLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   90 DVTHAPleAWQEDAWDrLMGINLKGPFFLIQALlpLLNNPSSVILCGSVSA--------------RIGLPTSSVYAASKA 155
Cdd:pfam01370  73 AVGGVG--ASIEDPED-FIEANVLGTLNLLEAA--RKAGVKRFLFASSSEVygdgaeipqeettlTGPLAPNSPYAAAKL 147
                         170
                  ....*....|..
gi 658549427  156 ALLSLARTLSAE 167
Cdd:pfam01370 148 AGEWLVLAYAAA 159
PLN02730 PLN02730
enoyl-[acyl-carrier-protein] reductase
118-249 8.50e-07

enoyl-[acyl-carrier-protein] reductase


Pssm-ID: 178331 [Multi-domain]  Cd Length: 303  Bit Score: 49.00  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 118 LIQALLPLLNNPSSVI-LCGSVSARIGLPTSSVYAASKAALLSLARTLSAELLPR-GIRVNGLSPGPVETPAFTKTGLSD 195
Cdd:PLN02730 160 LLQHFGPIMNPGGASIsLTYIASERIIPGYGGGMSSAKAALESDTRVLAFEAGRKyKIRVNTISAGPLGSRAAKAIGFID 239
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 658549427 196 EALNAMMAEiiklVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGGMGSL 249
Cdd:PLN02730 240 DMIEYSYAN----APLQKELTADEVGNAAAFLASPLASAITGATIYVDNGLNAM 289
PLN02780 PLN02780
ketoreductase/ oxidoreductase
8-185 8.94e-07

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 49.09  E-value: 8.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   8 YTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDK------AWVIPTDAGDIASQ-KALAETLAArwpr 80
Cdd:PLN02780  55 WALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKDVSDSIQSKysktqiKTVVVDFSGDIDEGvKRIKETIEG---- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  81 LD-AVFLNAGDVTHAPLEAWQE---DAWDRLMGINLKGPFFLIQALLP--LLNNPSSVILCGSVSARI--GLPTSSVYAA 152
Cdd:PLN02780 131 LDvGVLINNVGVSYPYARFFHEvdeELLKNLIKVNVEGTTKVTQAVLPgmLKRKKGAIINIGSGAAIVipSDPLYAVYAA 210
                        170       180       190
                 ....*....|....*....|....*....|...
gi 658549427 153 SKAALLSLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:PLN02780 211 TKAYIDQFSRCLYVEYKKSGIDVQCQVPLYVAT 243
PRK08303 PRK08303
short chain dehydrogenase; Provisional
1-181 1.12e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236229 [Multi-domain]  Cd Length: 305  Bit Score: 48.46  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   1 MGRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRN----------PDTLAE-AERI--LGDKAWVIPTDAGDIASQ 67
Cdd:PRK08303   3 MKPLRGKVALVAGATRGAGRGIAVELGAAGATVYVTGRStrarrseydrPETIEEtAELVtaAGGRGIAVQVDHLVPEQV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  68 KALAETLAARWPRLDaVFLN---AGDVT---HAPLeaWQEDAWDRLMGINLKGPFFLIQA--LLPLL-NNPSSVIL---- 134
Cdd:PRK08303  83 RALVERIDREQGRLD-ILVNdiwGGEKLfewGKPV--WEHSLDKGLRMLRLAIDTHLITShfALPLLiRRPGGLVVeitd 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 658549427 135 ----CGSVSARIglptSSVYAASKAALLSLARTLSAELLPRGIRVNGLSPG 181
Cdd:PRK08303 160 gtaeYNATHYRL----SVFYDLAKTSVNRLAFSLAHELAPHGATAVALTPG 206
PLN00015 PLN00015
protochlorophyllide reductase
10-140 2.06e-06

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 47.78  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGA-RVAVTGRNPDTLAEAERILG---DKAWVIPTDAGDIASQKALAETLAARWPRLDAVF 85
Cdd:PLN00015   1 IITGASSGLGLATAKALAETGKwHVVMACRDFLKAERAAKSAGmpkDSYTVMHLDLASLDSVRQFVDNFRRSGRPLDVLV 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  86 LNAG-DVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSS-VILCGSVSA 140
Cdd:PLN00015  81 CNAAvYLPTAKEPTFTADGFELSVGTNHLGHFLLSRLLLDDLkksDYPSKrLIIVGSITG 140
PRK05854 PRK05854
SDR family oxidoreductase;
4-143 3.52e-06

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 46.98  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNP----DTLAEAERILGDKAWVI-PTDAGDIASQKALAETLAARW 78
Cdd:PRK05854  12 LSGKRAVVTGASDGLGLGLARRLAAAGAEVILPVRNRakgeAAVAAIRTAVPDAKLSLrALDLSSLASVAALGEQLRAEG 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549427  79 PRLDAVFLNAGdVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSS-VILCGSVSARIG 143
Cdd:PRK05854  92 RPIHLLINNAG-VMTPPERQTTADGFELQFGTNHLGHFALTAHLLPLLRAGRArVTSQSSIAARRG 156
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
4-180 6.88e-06

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 45.90  E-value: 6.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   4 LTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPD----------TLAEAERILGDKAWVIPTDAGDIASQKALAET 73
Cdd:cd09762    1 LAGKTLFITGASRGIGKAIALKAARDGANVVIAAKTAEphpklpgtiyTAAEEIEAAGGKALPCIVDIRDEDQVRAAVEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  74 LAARWPRLDAVFLNA-----GDVTHAPLEawqedAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCGSVSAR-IGL 144
Cdd:cd09762   81 AVEKFGGIDILVNNAsaislTGTLDTPMK-----RYDLMMGVNTRGTYLCSKACLPYLkksKNPHILNLSPPLNLNpKWF 155
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 658549427 145 PTSSVYAASKAALLSLARTLSAELLPRGIRVNGLSP 180
Cdd:cd09762  156 KNHTAYTMAKYGMSMCVLGMAEEFKPGGIAVNALWP 191
PRK06300 PRK06300
enoyl-(acyl carrier protein) reductase; Provisional
118-246 8.47e-06

enoyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 235776 [Multi-domain]  Cd Length: 299  Bit Score: 45.96  E-value: 8.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 118 LIQALLPLLNNPSSVI-LCGSVSARIGLPTSSVYAASKAALLSLARTLSAELLPR-GIRVNGLSPGPVETPAFTKTGLSD 195
Cdd:PRK06300 159 LLSHFGPIMNPGGSTIsLTYLASMRAVPGYGGGMSSAKAALESDTKVLAWEAGRRwGIRVNTISAGPLASRAGKAIGFIE 238
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 658549427 196 EALNAMMAEiiklVPLGRMGSTTELAKAALYLASDESSYTVGTELLVDGGM 246
Cdd:PRK06300 239 RMVDYYQDW----APLPEPMEAEQVGAAAAFLVSPLASAITGETLYVDHGA 285
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-185 9.40e-06

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 45.44  E-value: 9.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   7 KYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPD-TLAEAERILGDKAWVIPTDAGDIASQKALAETL--AARWPRLDA 83
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKGTHVISISRTENkELTKLAEQYNSNLTFHSLDLQDVHELETNFNEIlsSIQEDNVSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  84 VFL--NAGDVTH-APLEAWQEDAWDRLMGINLKGPFFLIQALLP---LLNNPSSVILCGSVSARIGLPTSSVYAASKAAL 157
Cdd:PRK06924  82 IHLinNAGMVAPiKPIEKAESEELITNVHLNLLAPMILTSTFMKhtkDWKVDKRVINISSGAAKNPYFGWSAYCSSKAGL 161
                        170       180       190
                 ....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAE--LLPRGIRVNGLSPGPVET 185
Cdd:PRK06924 162 DMFTQTVATEqeEEEYPVKIVAFSPGVMDT 191
DUF1776 pfam08643
Fungal family of unknown function (DUF1776); This is a fungal family of unknown function. One ...
80-175 9.90e-06

Fungal family of unknown function (DUF1776); This is a fungal family of unknown function. One of the proteins in this family Swiss:P32792 has been localized to the mitochondria.


Pssm-ID: 370028  Cd Length: 295  Bit Score: 45.88  E-value: 9.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   80 RLDAV-FLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLL---NNPSSVILCG-SVSARIGLPTSSVYAASK 154
Cdd:pfam08643  92 RLRGViLVPSLSYPTGPIENIPPSSWASEFNSRLLNYYLTLQGLLPLLrsrSQKAQIIVFNpSISSSLNLPYHAPEALVS 171
                          90       100
                  ....*....|....*....|.
gi 658549427  155 AALLSLARTLSAELLPRGIRV 175
Cdd:pfam08643 172 SALSTLFTTLKRELRPHGIDV 192
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
8-185 1.05e-05

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: 45.29  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427    8 YTLITGGTSGIGLATAQAFI----AEGARVAVTGRNPDTLAEAERILGDK--AWVIPTDAGDIASQKALAETLAA----- 76
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAkclkSPGSVLVLSARNDEALRQLKAEIGAErsGLRVVRVSLDLGAEAGLEQLLKAlrelp 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   77 RWPRLD--AVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPF-------FLIQALLPLLNNPSSVILCGSVSARIGLPTS 147
Cdd:TIGR01500  82 RPKGLQrlLLINNAGTLGDVSKGFVDLSDSTQVQNYWALNLTsmlcltsSVLKAFKDSPGLNRTVVNISSLCAIQPFKGW 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 658549427  148 SVYAASKAALLSLARTLSAELLPRGIRVNGLSPGPVET 185
Cdd:TIGR01500 162 ALYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDT 199
PRK06720 PRK06720
hypothetical protein; Provisional
3-89 2.21e-05

hypothetical protein; Provisional


Pssm-ID: 180669 [Multi-domain]  Cd Length: 169  Bit Score: 43.81  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   3 RLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDT-LAEAERI--LGDKAWVIPTDAGDIAS-QKALAETLAArW 78
Cdd:PRK06720  13 KLAGKVAIVTGGGIGIGRNTALLLAKQGAKVIVTDIDQESgQATVEEItnLGGEALFVSYDMEKQGDwQRVISITLNA-F 91
                         90
                 ....*....|.
gi 658549427  79 PRLDAVFLNAG 89
Cdd:PRK06720  92 SRIDMLFQNAG 102
PRK05884 PRK05884
SDR family oxidoreductase;
10-245 2.95e-05

SDR family oxidoreductase;


Pssm-ID: 135642 [Multi-domain]  Cd Length: 223  Bit Score: 44.03  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIptDAGDIASQKALAETLAArwpRLDAvflnag 89
Cdd:PRK05884   4 LVTGGDTDLGRTIAEGFRNDGHKVTLVGARRDDLEVAAKELDVDAIVC--DNTDPASLEEARGLFPH---HLDT------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  90 dVTHAPLEAWQE------------DAWDRLMGINLKGPFFLIQALLPLLNNPSSVIlcgSVSARiGLPTSSVYAASKAAL 157
Cdd:PRK05884  73 -IVNVPAPSWDAgdprtysladtaNAWRNALDATVLSAVLTVQSVGDHLRSGGSII---SVVPE-NPPAGSAEAAIKAAL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427 158 LSLARTLSAELLPRGIRVNGLSPGPVETPAFtktglsdEALNAMMAEIiklvplgrmgsTTELAKAALYLASDESSYTVG 237
Cdd:PRK05884 148 SNWTAGQAAVFGTRGITINAVACGRSVQPGY-------DGLSRTPPPV-----------AAEIARLALFLTTPAARHITG 209

                 ....*...
gi 658549427 238 TELLVDGG 245
Cdd:PRK05884 210 QTLHVSHG 217
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
10-67 7.44e-05

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 42.98  E-value: 7.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWViptDAGDIASQ 67
Cdd:cd08243  147 LIRGGTSSVGLAALKLAKALGATVTATTRSPERAALLKELGADEVVI---DDGAIAEQ 201
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
10-89 7.65e-05

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 43.08  E-value: 7.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGtSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKawVIPTDAGDIASQKALAETlaarwPRLDAVFLNAG 89
Cdd:cd05188  139 LVLGA-GGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADH--VIDYKEEDLEEELRLTGG-----GGADVVIDAVG 210
KR_1_SDR_x cd08952
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
9-170 2.70e-04

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: 41.77  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   9 TLITGGTSGIGLATAQAFIAEGAR--VAVTGRNPDTLAEAERI-----LGDKAWVIPTDAGDIASQKALAETLAARWPrL 81
Cdd:cd08952  233 VLVTGGTGALGAHVARWLARRGAEhlVLTSRRGPDAPGAAELVaeltaLGARVTVAACDVADRDALAALLAALPAGHP-L 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  82 DAVFLNAGDVTHAPLEAWQEDAWDRLMGINLKGPFFLIQALLPLlnNPSSVILCGSVSARIGLPTSSVYAASKAALLSLA 161
Cdd:cd08952  312 TAVVHAAGVLDDGPLDDLTPERLAEVLRAKVAGARHLDELTRDR--DLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALA 389

                 ....*....
gi 658549427 162 RTLSAELLP 170
Cdd:cd08952  390 ERRRARGLP 398
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
10-64 3.11e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 41.51  E-value: 3.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAWVIPTDA---GDI 64
Cdd:PRK08655   4 SIIGGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKELGVEYANDNIDAakdADI 61
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
10-126 3.21e-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: 41.04  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEA----ERILGDK-AWVIPTDAGDIASQKALAETLAARWPRLDAV 84
Cdd:cd09808    5 LITGANSGIGKAAALAIAKRGGTVHMVCRNQTRAEEArkeiETESGNQnIFLHIVDMSDPKQVWEFVEEFKEEGKKLHVL 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 658549427  85 FLNAGDVTHAplEAWQEDAWDRLMGINLKGPFFLIQALLPLL 126
Cdd:cd09808   85 INNAGCMVNK--RELTEDGLEKNFATNTLGTYILTTHLIPVL 124
PRK09009 PRK09009
SDR family oxidoreductase;
10-186 6.51e-04

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 40.05  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAE--GARVAVTGRNPDTLAEAERILgdkaWvIPTDAGDIASQKALAETLaarwPRLDAVfLN 87
Cdd:PRK09009   4 LIVGGSGGIGKAMVKQLLERypDATVHATYRHHKPDFQHDNVQ----W-HALDVTDEAEIKQLSEQF----TQLDWL-IN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  88 AGDVTHAP-------LEAWQEDAWDRLMGINLKGPFFLIQALLPLLNNPSSVILcGSVSARIGLPTSS------VYAASK 154
Cdd:PRK09009  74 CVGMLHTQdkgpeksLQALDADFFLQNITLNTLPSLLLAKHFTPKLKQSESAKF-AVISAKVGSISDNrlggwySYRASK 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 658549427 155 AALLSLARTLSAE---LLPRGIrVNGLSPGPVETP 186
Cdd:PRK09009 153 AALNMFLKTLSIEwqrSLKHGV-VLALHPGTTDTA 186
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
10-55 1.52e-03

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 38.96  E-value: 1.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDKAW 55
Cdd:cd05276  144 LIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACRALGADVAI 189
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
10-103 1.60e-03

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 38.67  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDtlaEAERILGDKAWVIptdAGDIASQKALAETLAArwprLDAVFLNAG 89
Cdd:COG0702    3 LVTGATGFIGRRVVRALLARGHPVRALVRDPE---KAAALAAAGVEVV---QGDLDDPESLAAALAG----VDAVFLLVP 72
                         90
                 ....*....|....
gi 658549427  90 DVTHAPLEAWQEDA 103
Cdd:COG0702   73 SGPGGDFAVDVEGA 86
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
10-85 2.52e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 38.04  E-value: 2.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAV--TGRNPDTL-AEAERIlgdkawviptdAGDIASQKALAETLAARWPrlDAVF 85
Cdd:cd05265    4 LIIGGTRFIGKALVEELLAAGHDVTVfnRGRTKPDLpEGVEHI-----------VGDRNDRDALEELLGGEDF--DVVV 69
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
2-85 4.19e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 37.94  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549427   2 GRLTDKYTLITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERILGDkaWVIptDAGDIASQKALAETLAARWPrl 81
Cdd:cd08261  155 AGVTAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGAD--DTI--NVGDEDVAARLRELTDGEGA-- 228

                 ....
gi 658549427  82 DAVF 85
Cdd:cd08261  229 DVVI 232
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
10-85 4.32e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 37.82  E-value: 4.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549427  10 LITGGTSGIGLATAQAFIAEGARVAVTGRNPDTLAEAERiLGDKAwVIPTDAGDIASQkALAETLAARWprlDAVF 85
Cdd:COG0604  144 LVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRA-LGADH-VIDYREEDFAER-VRALTGGRGV---DVVL 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH