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Conserved domains on  [gi|19113072|ref|NP_596280|]
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sepiapterin reductase [Schizosaccharomyces pombe]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143277)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; similar to sepiapterin reductase that catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 8-245 2.07e-92

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: 271.85  E-value: 2.07e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEALQKKAK---VIAVSRSLTPELETLL-IQNPDSFVHVKGDVTEV-GKASIETAIKK-FGKLDS 81
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSpsvVVLLARSEEPLQELKEeLRPGLRVTTVKADLSDAaGVEQLLEAIRKlDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK--TKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:cd05367  81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKrgLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 160 LVMNLGSEEPDIMSVAVRPGVVDTPMQVSIRNDSNKEamggDTHNFFKELKTSGQLVAPQDIAKALSFLALnNNPKLTGQ 239
Cdd:cd05367 161 FFRVLAAEEPDVRVLSYAPGVVDTDMQREIRETSADP----ETRSRFRSLKEKGELLDPEQSAEKLANLLE-KDKFESGA 235


                ....*.
gi 19113072 240 FVEWKS 245
Cdd:cd05367 236 HVDYYD 241
 
Name Accession Description Interval E-value
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 8-245 2.07e-92

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: 271.85  E-value: 2.07e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEALQKKAK---VIAVSRSLTPELETLL-IQNPDSFVHVKGDVTEV-GKASIETAIKK-FGKLDS 81
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSpsvVVLLARSEEPLQELKEeLRPGLRVTTVKADLSDAaGVEQLLEAIRKlDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK--TKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:cd05367  81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKrgLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 160 LVMNLGSEEPDIMSVAVRPGVVDTPMQVSIRNDSNKEamggDTHNFFKELKTSGQLVAPQDIAKALSFLALnNNPKLTGQ 239
Cdd:cd05367 161 FFRVLAAEEPDVRVLSYAPGVVDTDMQREIRETSADP----ETRSRFRSLKEKGELLDPEQSAEKLANLLE-KDKFESGA 235


                ....*.
gi 19113072 240 FVEWKS 245
Cdd:cd05367 236 HVDYYD 241
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-241 2.26e-50

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: 164.96  E-value: 2.26e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTP--ELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKK 75
Cdd:COG1028   1 MTRLKGKVALVTGGSSGIGRAIARALaAEGARVVITDRDAEAleAAAAELRAAGGRALAVAADVTDEAavEALVAAAVAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  76 FGKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:COG1028  81 FGRLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAASK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHNFfkelktsGQLVAPQDIAKALSFLALNN 232
Cdd:COG1028 160 AAVVGLTRSLALElaPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPL-------GRLGTPEEVAAAVLFLASDA 232


                ....*....
gi 19113072 233 NPKLTGQFV 241
Cdd:COG1028 233 ASYITGQVL 241
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-190 4.86e-46

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.00  E-value: 4.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072     7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPeLETLLIQ---NPDSFVHVKGDVT--EVGKASIETAIKKFGKLD 80
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEgAKVVLVDRSEEK-LEAVAKElgaLGGKALFIQGDVTdrAQVKALVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:pfam00106  80 ILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMiKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIG 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 19113072   160 LVMNLGSEEPD--IMSVAVRPGVVDTPMQVSIR 190
Cdd:pfam00106 159 FTRSLALELAPhgIRVNAVAPGGVDTDMTKELR 191
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-235 5.11e-39

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 135.97  E-value: 5.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAE-ALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVGKasIETAIKKF------GKL 79
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANqLLEKGTHVISISRTENKELTKLAEQYNSNLTFHSLDLQDVHE--LETNFNEIlssiqeDNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVIL--NAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK06924  80 SSIHLinNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTkdWKVDKRVINISSGAAKNPYFGWSAYCSSKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  156 AINMLVMNLGSEEPD----IMSVAVRPGVVDTPMQVSIRnDSNKEamggDTHNF--FKELKTSGQLVAPQDIAKALSFLA 229
Cdd:PRK06924 160 GLDMFTQTVATEQEEeeypVKIVAFSPGVMDTNMQAQIR-SSSKE----DFTNLdrFITLKEEGKLLSPEYVAKALRNLL 234


                 ....*.
gi 19113072  230 LNNNPK 235
Cdd:PRK06924 235 ETEDFP 240
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 8-228 1.21e-22

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: 93.05  E-value: 1.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072     8 VILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDV--------------TEVGKASIETAI 73
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKCLKSPGSVLVLSARNDEALRQLKAEIGAERSGLrvvrvsldlgaeagLEQLLKALRELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    74 KK--FGKLdSVILNAGVLEPIAKIAD--ADINEWRKLFDINFFSVVET---VKYAIPHLRKTKGTIVIVSSGAAVRVFPA 146
Cdd:TIGR01500  82 RPkgLQRL-LLINNAGTLGDVSKGFVdlSDSTQVQNYWALNLTSMLCLtssVLKAFKDSPGLNRTVVNISSLCAIQPFKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   147 WAAYCCSKAAINMLVMNLGSEE--PDIMSVAVRPGVVDTPMQVSIRndsnKEAMGGDTHNFFKELKTSGQLVAPQDIAKA 224
Cdd:TIGR01500 161 WALYCAGKAARDMLFQVLALEEknPNVRVLNYAPGVLDTDMQQQVR----EESVDPDMRKGLQELKAKGKLVDPKVSAQK 236


                  ....
gi 19113072   225 LSFL 228
Cdd:TIGR01500 237 LLSL 240
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 7-107 9.51e-04

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: 39.00  E-value: 9.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072      7 KVILLTGSSKGIGLATAEALQKK--AKVIAVSRSLTP-----ELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFG 77
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERgaRRLVLLSRSGPDapgaaALLAELEAAGARVTVVACDVADRDalAAVLAAIPAVEG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 19113072     78 KLDSVILNAGVLEPiAKIADADINEWRKLF 107
Cdd:smart00822  81 PLTGVIHAAGVLDD-GVLASLTPERFAAVL 109
 
Name Accession Description Interval E-value
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 8-245 2.07e-92

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: 271.85  E-value: 2.07e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEALQKKAK---VIAVSRSLTPELETLL-IQNPDSFVHVKGDVTEV-GKASIETAIKK-FGKLDS 81
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSpsvVVLLARSEEPLQELKEeLRPGLRVTTVKADLSDAaGVEQLLEAIRKlDGERDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK--TKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:cd05367  81 LINNAGSLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKrgLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDM 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 160 LVMNLGSEEPDIMSVAVRPGVVDTPMQVSIRNDSNKEamggDTHNFFKELKTSGQLVAPQDIAKALSFLALnNNPKLTGQ 239
Cdd:cd05367 161 FFRVLAAEEPDVRVLSYAPGVVDTDMQREIRETSADP----ETRSRFRSLKEKGELLDPEQSAEKLANLLE-KDKFESGA 235


                ....*.
gi 19113072 240 FVEWKS 245
Cdd:cd05367 236 HVDYYD 241
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-241 2.26e-50

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: 164.96  E-value: 2.26e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTP--ELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKK 75
Cdd:COG1028   1 MTRLKGKVALVTGGSSGIGRAIARALaAEGARVVITDRDAEAleAAAAELRAAGGRALAVAADVTDEAavEALVAAAVAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  76 FGKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:COG1028  81 FGRLDILVNNAGITPP-GPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAGLRGSPGQAAYAASK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHNFfkelktsGQLVAPQDIAKALSFLALNN 232
Cdd:COG1028 160 AAVVGLTRSLALElaPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARIPL-------GRLGTPEEVAAAVLFLASDA 232


                ....*....
gi 19113072 233 NPKLTGQFV 241
Cdd:COG1028 233 ASYITGQVL 241
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 4-229 1.21e-49

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: 162.66  E-value: 1.21e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   4 TAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSlTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLD 80
Cdd:COG4221   3 DKGKVALITGASSGIGAATARALaAAGARVVLAARR-AERLEALAAELGGRALAVPLDVTDEAavEAAVAAAVAEFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:COG4221  82 VLVNNAGVA-LLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGsGHIVNISSIAGLRPYPGGAVYAATKAAVRG 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113072 160 LVMNLGSEEPD--IMSVAVRPGVVDTPMQVSIRNDSNKEAMggdthnffkELKTSGQLVAPQDIAKALSFLA 229
Cdd:COG4221 161 LSESLRAELRPtgIRVTVIEPGAVDTEFLDSVFDGDAEAAA---------AVYEGLEPLTPEDVAEAVLFAL 223
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 9-242 1.06e-46

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: 155.13  E-value: 1.06e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   9 ILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPELETLLIQ-NPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVIL 84
Cdd:cd05233   1 ALVTGASSGIGRAIARRLaREGAKVVLADRNEEALAELAAIEaLGGNAVAVQADVSDEEdvEALVEEALEEFGRLDILVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  85 NAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK-TKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMN 163
Cdd:cd05233  81 NAGIARP-GPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKqGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 164 LGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMggdthnffKELKTSGQLVAPQDIAKALSFLALNNNPKLTGQFV 241
Cdd:cd05233 160 LALElaPYGIRVNAVAPGLVDTPMLAKLGPEEAEKEL--------AAAIPLGRLGTPEEVAEAVVFLASDEASYITGQVI 231


                .
gi 19113072 242 E 242
Cdd:cd05233 232 P 232
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-190 4.86e-46

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 152.00  E-value: 4.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072     7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPeLETLLIQ---NPDSFVHVKGDVT--EVGKASIETAIKKFGKLD 80
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEgAKVVLVDRSEEK-LEAVAKElgaLGGKALFIQGDVTdrAQVKALVEQAVERLGRLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:pfam00106  80 ILVNNAGITGL-GPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMiKGSGGRIVNISSVAGLVPYPGGSAYSASKAAVIG 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 19113072   160 LVMNLGSEEPD--IMSVAVRPGVVDTPMQVSIR 190
Cdd:pfam00106 159 FTRSLALELAPhgIRVNAVAPGGVDTDMTKELR 191
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
7-198 1.52e-41

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 142.32  E-value: 1.52e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTP--ELETLLIQNPDSFVHVKGDVT---EVGKAsIETAIKKFGKLD 80
Cdd:COG0300   6 KTVLITGASSGIGRALARALaARGARVVLVARDAERleALAAELRAAGARVEVVALDVTdpdAVAAL-AEAVLARFGPID 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:COG0300  85 VLVNNAGVGGG-GPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSSVAGLRGLPGMAAYAASKAALEG 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19113072 160 LVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAM 198
Cdd:COG0300 164 FSESLRAElaPTGVRVTAVCPGPVDTPFTARAGAPAGRPLL 204
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 7-236 3.96e-39

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: 135.82  E-value: 3.96e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKKA-KVIAVSRSlTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGyRVIATARN-PDKLESLGELLNDNLEVLELDVTDEEsiKAAVKEVIERFGRIDVLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  84 LNAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVM 162
Cdd:cd05374  80 NNAGYGL-FGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFLGPYCASKAALEALSE 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 163 NLGSE-EP-DIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHNFFKELKTSGQLVA-----PQDIAKALSFLALNNNPK 235
Cdd:cd05374 159 SLRLElAPfGIKVTIIEPGPVRTGFADNAAGSALEDPEISPYAPERKEIKENAAGVGsnpgdPEKVADVIVKALTSESPP 238


                .
gi 19113072 236 L 236
Cdd:cd05374 239 L 239
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
7-235 5.11e-39

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 135.97  E-value: 5.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAE-ALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVGKasIETAIKKF------GKL 79
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANqLLEKGTHVISISRTENKELTKLAEQYNSNLTFHSLDLQDVHE--LETNFNEIlssiqeDNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVIL--NAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK06924  80 SSIHLinNAGMVAPIKPIEKAESEELITNVHLNLLAPMILTSTFMKHTkdWKVDKRVINISSGAAKNPYFGWSAYCSSKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  156 AINMLVMNLGSEEPD----IMSVAVRPGVVDTPMQVSIRnDSNKEamggDTHNF--FKELKTSGQLVAPQDIAKALSFLA 229
Cdd:PRK06924 160 GLDMFTQTVATEQEEeeypVKIVAFSPGVMDTNMQAQIR-SSSKE----DFTNLdrFITLKEEGKLLSPEYVAKALRNLL 234


                 ....*.
gi 19113072  230 LNNNPK 235
Cdd:PRK06924 235 ETEDFP 240
PRK08219 PRK08219
SDR family oxidoreductase;
7-227 9.81e-36

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 126.59  E-value: 9.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSlTPELETLLIQNPDSFVHVkGDVTEVGkaSIETAIKKFGKLDSVILNA 86
Cdd:PRK08219   4 PTALITGASRGIGAAIARELAPTHTLLLGGRP-AERLDELAAELPGATPFP-VDLTDPE--AIAAAVEQLGRLDVLVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   87 GVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMNLGS 166
Cdd:PRK08219  80 GVADL-GPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAHGHVVFINSGAGLRANPGWGSYAASKFALRALADALRE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113072  167 EEPDIMSV-AVRPGVVDTPMQVSIRndsnkeAMGGDTHNffkelktSGQLVAPQDIAKALSF 227
Cdd:PRK08219 159 EEPGNVRVtSVHPGRTDTDMQRGLV------AQEGGEYD-------PERYLRPETVAKAVRF 207
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 14-239 5.92e-35

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: 124.85  E-value: 5.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    14 SSKGIGLATAEALQKK-AKVIA--VSRSLTPELETLLIQNPDSFVHVkgDVTEVG--KASIETAIKKFGKLDSVILNAGV 88
Cdd:pfam13561   4 NESGIGWAIARALAEEgAEVVLtdLNEALAKRVEELAEELGAAVLPC--DVTDEEqvEALVAAAVEKFGRLDILVNNAGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    89 LEPIAK-IADADINEWRKLFDINFFSVVETVKYAIPHLRKtKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMNLGSE 167
Cdd:pfam13561  82 APKLKGpFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE-GGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAVE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113072   168 --EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHNFfkelktsGQLVAPQDIAKALSFLALNNNPKLTGQ 239
Cdd:pfam13561 161 lgPRGIRVNAISPGPIKTLAASGIPGFDELLAAAEARAPL-------GRLGTPEEVANAAAFLASDLASYITGQ 227
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 5-239 1.48e-34

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


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 124.45  E-value: 1.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLLI--------QNPDSfvhVKGDVTEVG--KASIETAI 73
Cdd:cd05364   2 SGKVAIITGSSSGIGAGTAILFARLgARLALTGRDAERLEETRQSclqagvseKKILL---VVADLTEEEgqDRIISTTL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  74 KKFGKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCS 153
Cdd:cd05364  79 AKFGRLDILVNNAGILAK-GGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGGRSFPGVLYYCIS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 154 KAAINMLVMNLGSE-EPDIMSV-AVRPGVVDTPMQvsiRNDSNKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALN 231
Cdd:cd05364 158 KAALDQFTRCTALElAPKGVRVnSVSPGVIVTGFH---RRMGMPEEQYIKFLSRAKETHPLGRPGTVDEVAEAIAFLASD 234


                ....*...
gi 19113072 232 NNPKLTGQ 239
Cdd:cd05364 235 ASSFITGQ 242
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 7-242 2.77e-33

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: 120.48  E-value: 2.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLL--IQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLDS 81
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKgAKVAILDRNENPGAAAELqaINPKVKATFVQCDVTswEQLAAAFKKAIEKFGRVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPIAKIADADINE-WRKLFDINFFSVVETVKYAIPHLRKTK----GTIVIVSSGAAVRVFPAWAAYCCSKAA 156
Cdd:cd05323  81 LINNAGILDEKSYLFAGKLPPpWEKTIDVNLTGVINTTYLALHYMDKNKggkgGVIVNIGSVAGLYPAPQFPVYSASKHG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 157 INMLVMNLGSEEP---DIMSVAVRPGVVDTPMQVSIrNDSNKEAMggdthnffkelkTSGQLVAPQDIAKAlsFLALNNN 233
Cdd:cd05323 161 VVGFTRSLADLLEyktGVRVNAICPGFTNTPLLPDL-VAKEAEML------------PSAPTQSPEVVAKA--IVYLIED 225


                ....*....
gi 19113072 234 PKLTGQFVE 242
Cdd:cd05323 226 DEKNGAIWI 234
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
7-229 4.66e-33

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 120.26  E-value: 4.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTpELETL---LIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLD 80
Cdd:PRK05653   6 KTALVTGASRGIGRAIALRLAADgAKVVIYDSNEE-AAEALaaeLRAAGGEARVLVFDVSdeAAVRALIEAAVEAFGALD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAI-- 157
Cdd:PRK05653  85 ILVNNAGITRD-ALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKArYGRIVNISSVSGVTGNPGQTNYSAAKAGVig 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113072  158 --NMLVMNLGSEepDIMSVAVRPGVVDTPMqvsirndsNKEAMGGDTHNFFKELkTSGQLVAPQDIAKALSFLA 229
Cdd:PRK05653 164 ftKALALELASR--GITVNAVAPGFIDTDM--------TEGLPEEVKAEILKEI-PLGRLGQPEEVANAVAFLA 226
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-239 7.11e-33

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 119.56  E-value: 7.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKV-IAVSRSLTP--ELETLLIQNPDSFVHVKGDVTEVGKAS--IETAIKKFGKLD 80
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAKEgAKVvIAYDINEEAaqELLEEIKEEGGDAIAVKADVSSEEDVEnlVEQIVEKFGKID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSS-----GAavrvfPAWAAYCCSK 154
Cdd:PRK05565  86 ILVNNAGISN-FGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKsGVIVNISSiwgliGA-----SCEVLYSASK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE-EPD-IMSVAVRPGVVDTPMQVSIRNDsNKEAMggdthnffKELKTSGQLVAPQDIAKALSFLALNN 232
Cdd:PRK05565 160 GAVNAFTKALAKElAPSgIRVNAVAPGAIDTEMWSSFSEE-DKEGL--------AEEIPLGRLGKPEEIAKVVLFLASDD 230


                 ....*..
gi 19113072  233 NPKLTGQ 239
Cdd:PRK05565 231 ASYITGQ 237
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-242 1.62e-32

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 118.82  E-value: 1.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPELETL---LIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLD 80
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLaRAGADVVVHYRSDEEAAEELveaVEALGRRAQAVQADVTdkAALEAAVAAAVERFGRID 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:PRK12825  87 ILVNNAGIFED-KPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNISSVAGLPGWPGRSNYAAAKAGLVG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  160 LVMNLGSEEPD--IMSVAVRPGVVDTPMqvsirndsnKEAMGGDtHNFFKELKTS-GQLVAPQDIAKALSFLALNNNPKL 236
Cdd:PRK12825 166 LTKALARELAEygITVNMVAPGDIDTDM---------KEATIEE-AREAKDAETPlGRSGTPEDIARAVAFLCSDASDYI 235


                 ....*.
gi 19113072  237 TGQFVE 242
Cdd:PRK12825 236 TGQVIE 241
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 1-239 2.08e-32

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 119.01  E-value: 2.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSlTPELETLLIQNPDSFVH-VKGDVTEVG--KASIETAIKKF 76
Cdd:PRK12829   6 LKPLDGLRVLVTGGASGIGRAIAEAFaEAGARVHVCDVS-EAALAATAARLPGAKVTaTVADVADPAqvERVFDTAVERF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   77 GKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PRK12829  85 GGLDVLVNNAGIAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGhgGVIIALSSVAGRLGYPGRTPYAASK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHNFFKELKT--SGQLVAPQDIAKALSFLAL 230
Cdd:PRK12829 165 WAVVGLVKSLAIElgPLGIRVNAILPGIVRGPRMRRVIEARAQQLGIGLDEMEQEYLEKisLGRMVEPEDIAATALFLAS 244


                 ....*....
gi 19113072  231 NNNPKLTGQ 239
Cdd:PRK12829 245 PAARYITGQ 253
PRK07326 PRK07326
SDR family oxidoreductase;
1-235 1.18e-31

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 116.26  E-value: 1.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTpELETLLIQ-NPDSFVH-VKGDVTEVG--KASIETAIKK 75
Cdd:PRK07326   1 MMSLKGKVALITGGSKGIGFAIAEALLAEgYKVAITARDQK-ELEEAAAElNNKGNVLgLAADVRDEAdvQRAVDAIVAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK07326  80 FGGLDVLIANAGV-GHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAGTNFFAGGAAYNASKF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  156 AINML--VMNLGSEEPDIMSVAVRPGVVDTPMQVSIRNDSNKeamggdthnfFKelktsgqlVAPQDIAKALSFLaLNNN 233
Cdd:PRK07326 159 GLVGFseAAMLDLRQYGIKVSTIMPGSVATHFNGHTPSEKDA----------WK--------IQPEDIAQLVLDL-LKMP 219


                 ..
gi 19113072  234 PK 235
Cdd:PRK07326 220 PR 221
PRK07023 PRK07023
SDR family oxidoreductase;
10-229 1.54e-31

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 116.27  E-value: 1.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPELETlliQNPDSFVHVKGDVTEVGKASIETAIKKFGKLDS------V 82
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLlQPGIAVLGVARSRHPSLAA---AAGERLAEVELDLSDAAAAAAWLAGDLLAAFVDgasrvlL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   83 ILNAGVLEPIAKIADADINEWRKLFDINffsVVETVKYAIPHLRKTKGT----IVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:PRK07023  82 INNAGTVEPIGPLATLDAAAIARAVGLN---VAAPLMLTAALAQAASDAaerrILHISSGAARNAYAGWSVYCATKAALD 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113072  159 MLVMNLGSEEPD-IMSVAVRPGVVDTPMQVSIRndsnkeamGGDTHNF-----FKELKTSGQLVAPQDIA-KALSFLA 229
Cdd:PRK07023 159 HHARAVALDANRaLRIVSLAPGVVDTGMQATIR--------ATDEERFpmrerFRELKASGALSTPEDAArRLIAYLL 228
FabG-like PRK07231
SDR family oxidoreductase;
7-229 1.98e-31

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 116.08  E-value: 1.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSR---SLTPELEtlLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLD 80
Cdd:PRK07231   6 KVAIVTGASSGIGEGIARRFaAEGARVVVTDRneeAAERVAA--EILAGGRAIAVAADVSDEAdvEAAVAAALERFGSVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:PRK07231  84 ILVNNAGTTHRNGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGgGAIVNVASTAGLRPRPGLGWYNASKGAVIT 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113072  160 LVMNLGSE-EPDIMSV-AVRPGVVDTPMQvsirndsnKEAMGGDTHNFFKELKTS---GQLVAPQDIAKALSFLA 229
Cdd:PRK07231 164 LTKALAAElGPDKIRVnAVAPVVVETGLL--------EAFMGEPTPENRAKFLATiplGRLGTPEDIANAALFLA 230
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 7-239 4.60e-31

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 114.89  E-value: 4.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVGKA--SIETAIKKFGKLDSVI 83
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLaARGARVALIGRGAAPLSQTLPGVPADALRIGGIDLVDPQAArrAVDEVNRQFGRLDALV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVM 162
Cdd:PRK12828  88 NIAGAF-VWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGgGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTE 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072  163 NLGSE--EPDIMSVAVRPGVVDTPMqvsirndSNKEAMGGDThnffkelktsGQLVAPQDIAKALSFLALNNNPKLTGQ 239
Cdd:PRK12828 167 ALAAEllDRGITVNAVLPSIIDTPP-------NRADMPDADF----------SRWVTPEQIAAVIAFLLSDEAQAITGA 228
PRK12826 PRK12826
SDR family oxidoreductase;
1-239 2.04e-30

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 113.47  E-value: 2.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELET--LLIQNPDSFVHVKGDVTEVG--KASIETAIKK 75
Cdd:PRK12826   1 TRDLEGRVALVTGAARGIGRAIAVRLAADgAEVIVVDICGDDAAATaeLVEAAGGKARARQVDVRDRAalKAAVAAGVED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRV-FPAWAAYCCS 153
Cdd:PRK12826  81 FGRLDILVANAGIF-PLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPRVgYPGLAHYAAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  154 KAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDThnffkelkTSGQLVAPQDIAKALSFLALN 231
Cdd:PRK12826 160 KAGLVGFTRALALElaARNITVNSVHPGGVDTPMAGNLGDAQWAEAIAAAI--------PLGRLGEPEDIAAAVLFLASD 231


                 ....*...
gi 19113072  232 NNPKLTGQ 239
Cdd:PRK12826 232 EARYITGQ 239
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 9-244 1.92e-29

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: 110.46  E-value: 1.92e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   9 ILLTGSSKGIGLATAEAL--QKKAKVIAVSR--SLTPELETLLIQnpDSFVHV-KGDVTEVGKASIE--TAIKKFGKLDS 81
Cdd:cd05325   1 VLITGASRGIGLELVRQLlaRGNNTVIATCRdpSAATELAALGAS--HSRLHIlELDVTDEIAESAEavAERLGDAGLDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK-TKGTIVIVSSGAA---VRVFPAWAAYCCSKAAI 157
Cdd:cd05325  79 LINNAGILHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKgARAKIINISSRVGsigDNTSGGWYSYRASKAAL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE-EPD-IMSVAVRPGVVDTpmqvsirndsnkeAMGGDTHNffkelktSGQLVAPQDIAKALSFLALNNNPK 235
Cdd:cd05325 159 NMLTKSLAVElKRDgITVVSLHPGWVRT-------------DMGGPFAK-------NKGPITPEESVAGLLKVIDNLNEE 218


                ....*....
gi 19113072 236 LTGQFVEWK 244
Cdd:cd05325 219 DSGKFLDYD 227
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 7-239 2.12e-28

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: 107.75  E-value: 2.12e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVI---AVSRSLTPELETLLIQNPDSFVHVKGDVTEV--GKASIETAIKKFGKLD 80
Cdd:cd05362   4 KVALVTGASRGIGRAIAKRLARDgASVVvnyASSKAAAEEVVAEIEAAGGKAIAVQADVSDPsqVARLFDAAEKAFGGVD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTkGTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:cd05362  84 ILVNNAGVMLK-KPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINISSSLTAAYTPNYGAYAGSKAAVEAF 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 161 VMNLGSE--EPDIMSVAVRPGVVDTPMqvsIRNDSNKEAMggdthNFFKELKTSGQLVAPQDIAKALSFLALNNNPKLTG 238
Cdd:cd05362 162 TRVLAKElgGRGITVNAVAPGPVDTDM---FYAGKTEEAV-----EGYAKMSPLGRLGEPEDIAPVVAFLASPDGRWVNG 233


                .
gi 19113072 239 Q 239
Cdd:cd05362 234 Q 234
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 5-239 7.76e-28

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: 106.42  E-value: 7.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSV 82
Cdd:cd08944   2 EGKVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQqvAALFERAVEEFGGLDLL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  83 ILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:cd08944  82 VNNAGAMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARgGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLT 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 162 MNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHNFFKELKtsGQLVAPQDIAKALSFLALNNNPKLTGQ 239
Cdd:cd08944 162 RTLAAElrHAGIRCNALAPGLIDTPLLLAKLAGFEGALGPGGFHLLIHQLQ--GRLGRPEDVAAAVVFLLSDDASFITGQ 239
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 9-229 7.77e-28

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: 106.40  E-value: 7.77e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   9 ILLTGSSKGIGLATAEAL-QKKAKVIAVSRSltpelETLLIQNPDSFVHVKGDVTEvgKASIETAIKKF----GKLDSVI 83
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLlQAGATVIALDLP-----FVLLLEYGDPLRLTPLDVAD--AAAVREVCSRLlaehGPIDALV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  84 LNAGVLEPIAKIADADiNEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVM 162
Cdd:cd05331  74 NCAGVLRPGATDPLST-EDWEQTFAVNVTGVFNLLQAVAPHMKDRRtGAIVTVASNAAHVPRISMAAYGASKAALASLSK 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113072 163 NLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEA--MGGDTHNFfkelKTS---GQLVAPQDIAKALSFLA 229
Cdd:cd05331 153 CLGLElaPYGVRCNVVSPGSTDTAMQRTLWHDEDGAAqvIAGVPEQF----RLGiplGKIAQPADIANAVLFLA 222
PRK07454 PRK07454
SDR family oxidoreductase;
10-198 9.30e-28

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 106.20  E-value: 9.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEALQKKA-KVIAVSRSLtPELETLLIQNPDSFVHVK------GDVTEVgKASIETAIKKFGKLDSV 82
Cdd:PRK07454  10 LITGASSGIGKATALAFAKAGwDLALVARSQ-DALEALAAELRSTGVKAAaysidlSNPEAI-APGIAELLEQFGCPDVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   83 ILNAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:PRK07454  88 INNAGMAY-TGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGgGLIINVSSIAARNAFPQWGAYCVSKAALAAFT 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19113072  162 MNLGSEEPD--IMSVAVRPGVVDTPM--QVSIRNDSNKEAM 198
Cdd:PRK07454 167 KCLAEEERShgIRVCTITLGAVNTPLwdTETVQADFDRSAM 207
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 7-185 1.49e-27

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: 105.41  E-value: 1.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATA-EALQKKAKVIAVSRSL------TPELETLLIQNPDSFVHVKGDVT---EVGKAsIETAIKKF 76
Cdd:cd08939   2 KHVLITGGSSGIGKALAkELVKEGANVIIVARSEskleeaVEEIEAEANASGQKVSYISADLSdyeEVEQA-FAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  77 GKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:cd08939  81 GPPDLVVNCAGISIP-GLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRpGHIVFVSSQAALVGIYGYSAYCPSKF 159

                       170       180       190
                ....*....|....*....|....*....|..
gi 19113072 156 AINMLVMNLGSE--EPDIMSVAVRPGVVDTPM 185
Cdd:cd08939 160 ALRGLAESLRQElkPYNIRVSVVYPPDTDTPG 191
PRK06398 PRK06398
aldose dehydrogenase; Validated
 1-238 1.64e-27

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 106.07  E-value: 1.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETlliqnpdsfVHVKGDVTEVG--KASIETAIKKFG 77
Cdd:PRK06398   1 DLGLKDKVAIVTGGSQGIGKAVVNRLKEEgSNVINFDIKEPSYNDV---------DYFKVDVSNKEqvIKGIDYVISKYG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAA 156
Cdd:PRK06398  72 RIDILVNNAGI-ESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDkGVIINIASVQSFAVTRNAAAYVTSKHA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  157 INMLVMNLGSE-EPDIMSVAVRPGVVDTPM-----QVSIRNDSNKEAmggDTHNFFKELKTSGQLVAPQDIAKALSFLAL 230
Cdd:PRK06398 151 VLGLTRSIAVDyAPTIRCVAVCPGSIRTPLlewaaELEVGKDPEHVE---RKIREWGEMHPMKRVGKPEEVAYVVAFLAS 227


                 ....*...
gi 19113072  231 NNNPKLTG 238
Cdd:PRK06398 228 DLASFITG 235
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 7-185 2.11e-27

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 106.59  E-value: 2.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLtPELETLL--IQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDS 81
Cdd:PRK05872  10 KVVVVTGAARGIGAELARRLHARgAKLALVDLEE-AELAALAaeLGGDDRVLTVVADVTDLAamQAAAEEAVERFGGIDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:PRK05872  89 VVANAGIASG-GSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAAPGMAAYCASKAGVEAFA 167

                        170       180
                 ....*....|....*....|....*.
gi 19113072  162 MNLGSE-EPDIMSVAV-RPGVVDTPM 185
Cdd:PRK05872 168 NALRLEvAHHGVTVGSaYLSWIDTDL 193
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-239 2.42e-27

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: 105.22  E-value: 2.42e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSlTPELETLLIQNPDSFVHVKGDVTEVGKAS-----IETAIKKF-GKL 79
Cdd:cd05329   7 KTALVTGGTKGIGYAIVEELaGLGAEVYTCARN-QKELDECLTEWREKGFKVEGSVCDVSSRSerqelMDTVASHFgGKL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  80 DSVILNAGVLepIAKIA-DADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:cd05329  86 NILVNNAGTN--IRKEAkDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASgNGNIVFISSVAGVIAVPSGAPYGATKGAL 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPM-QVSIRNDSNKEAMGGDThnffkELKTSGQlvaPQDIAKALSFLALNNNP 234
Cdd:cd05329 164 NQLTRSLACEwaKDNIRVNAVAPWVIATPLvEPVIQQKENLDKVIERT-----PLKRFGE---PEEVAALVAFLCMPAAS 235


                ....*
gi 19113072 235 KLTGQ 239
Cdd:cd05329 236 YITGQ 240
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 7-228 6.08e-27

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: 103.60  E-value: 6.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSltPE-LETLLIQNPDSFVhVKGDVTEVGKAS--IETAIKKFGKLDSV 82
Cdd:cd08932   1 KVALVTGASRGIGIEIARALaRDGYRVSLGLRN--PEdLAALSASGGDVEA-VPYDARDPEDARalVDALRDRFGRIDVL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  83 ILNAGVLEPIAkIADADINEWRKLFDINFFSVVETVKYAIPHLR-KTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:cd08932  78 VHNAGIGRPTT-LREGSDAELEAHFSINVIAPAELTRALLPALReAGSGRVVFLNSLSGKRVLAGNAGYSASKFALRALA 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072 162 MNLGSEEPD--IMSVAVRPGVVDTPMQVSIRNDSNKEAMggdthnffkelktsgQLVAPQDIAKALSFL 228
Cdd:cd08932 157 HALRQEGWDhgVRVSAVCPGFVDTPMAQGLTLVGAFPPE---------------EMIQPKDIANLVRMV 210
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 7-227 1.16e-26

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: 103.39  E-value: 1.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLL--IQNPDSFVHVKG-DVTEVGKA--SIETAIKKFGKLDS 81
Cdd:cd08934   4 KVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALAdeLEAEGGKALVLElDVTDEQQVdaAVERTVEALGRLDI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLR-KTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:cd08934  84 LVNNAGIM-LLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLlRNKGTIVNISSVAGRVAVRNSAVYNATKFGVNAF 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072 161 VMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGdthnffkELKTSGQLVApQDIAKALSF 227
Cdd:cd08934 163 SEGLRQEvtERGVRVVVIEPGTVDTELRDHITHTITKEAYEE-------RISTIRKLQA-EDIAAAVRY 223
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 8-229 1.60e-26

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: 102.85  E-value: 1.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEALQKK-AKVIAVSRS------LTPELETLLIQNpdsfVHVKGDVT---EVGKASiETAIKKFG 77
Cdd:cd05360   2 VVVITGASSGIGRATALAFAERgAKVVLAARSaealheLAREVRELGGEA----IAVVADVAdaaQVERAA-DTAVERFG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  78 KLDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVI-VSSGAAVRVFPAWAAYCCSKAA 156
Cdd:cd05360  77 RIDTWVNNAGV-AVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALInVGSLLGYRSAPLQAAYSASKHA 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113072 157 I----NMLVMNLGSEEPDIMSVAVRPGVVDTPMQVSIRNdsnkeAMGgdthnffKELKTSGQLVAPQDIAKALSFLA 229
Cdd:cd05360 156 VrgftESLRAELAHDGAPISVTLVQPTAMNTPFFGHARS-----YMG-------KKPKPPPPIYQPERVAEAIVRAA 220
PRK06138 PRK06138
SDR family oxidoreductase;
5-238 1.92e-26

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 102.92  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELET--LLIQNPDSFVHVkGDVTEVG--KASIETAIKKFGKL 79
Cdd:PRK06138   4 AGRVAIVTGAGSGIGRATAKLFAREgARVVVADRDAEAAERVaaAIAAGGRAFARQ-GDVGSAEavEALVDFVAARWGRL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:PRK06138  83 DVLVNNAGFGC-GGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGgGSIVNTASQLALAGGRGRAAYVASKGAIA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  159 MLV--MNLGSEEPDIMSVAVRPGVVDTPM-QVSIRNDSNKEAMGGDthnfFKELKTSGQLVAPQDIAKALSFLALNNNPK 235
Cdd:PRK06138 162 SLTraMALDHATDGIRVNAVAPGTIDTPYfRRIFARHADPEALREA----LRARHPMNRFGTAEEVAQAALFLASDESSF 237


                 ...
gi 19113072  236 LTG 238
Cdd:PRK06138 238 ATG 240
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 7-238 2.45e-26

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: 102.47  E-value: 2.45e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSrsLTPELETLL---IQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLD 80
Cdd:cd08943   2 KVALVTGGASGIGLAIAKRLAAEgAAVVVAD--IDPEIAEKVaeaAQGGPRALGVQCDVTSEAqvQSAFEQAVLEFGGLD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:cd08943  80 IVVSNAGIATS-SPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGigGNIVFNASKNAVAPGPNAAAYSAAKAAEA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 159 MLVMNLGSE--EPDIMSVAVRP-GVVDTPMqvsIRNDSNKEAMG---GDTHNFFKELKTSGQLVAPQDIAKALSFLALNN 232
Cdd:cd08943 159 HLARCLALEggEDGIRVNTVNPdAVFRGSK---IWEGVWRAARAkayGLLEEEYRTRNLLKREVLPEDVAEAVVAMASED 235


                ....*.
gi 19113072 233 NPKLTG 238
Cdd:cd08943 236 FGKTTG 241
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-239 3.02e-26

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 102.45  E-value: 3.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKKAKVIAV----SRSLTPELETLLIQNPDSFVHVKGDVT---EVGKAsIETAIKKFGKL 79
Cdd:cd05366   3 KVAIITGAAQGIGRAIAERLAADGFNIVLadlnLEEAAKSTIQEISEAGYNAVAVGADVTdkdDVEAL-IDQAVEKFGSF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  80 DSVILNAGV--LEPIAKIADADINewrKLFDINFFSVVETVKYAIPHLRK--TKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:cd05366  82 DVMVNNAGIapITPLLTITEEDLK---KVYAVNVFGVLFGIQAAARQFKKlgHGGKIINASSIAGVQGFPNLGAYSASKF 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 156 AINMLVMNLGSEEPD--IMSVAVRPGVVDTPMQVSIRNDSNKEAMG--GDTHNFFKELKTSGQLVAPQDIAKALSFLALN 231
Cdd:cd05366 159 AVRGLTQTAAQELAPkgITVNAYAPGIVKTEMWDYIDEEVGEIAGKpeGEGFAEFSSSIPLGRLSEPEDVAGLVSFLASE 238


                ....*...
gi 19113072 232 NNPKLTGQ 239
Cdd:cd05366 239 DSDYITGQ 246
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 7-224 5.51e-26

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: 101.89  E-value: 5.51e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTpELETL---LIQNPDSFVH-VKGDVTEVG--KASIETAIKKFGKL 79
Cdd:cd05332   4 KVVIITGASSGIGEELAYHLARLgARLVLSARREE-RLEEVkseCLELGAPSPHvVPLDMSDLEdaEQVVEEALKLFGGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  80 DSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAI- 157
Cdd:cd05332  83 DILINNAGISMR-SLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLiERSQGSIVVVSSIAGKIGVPFRTAYAASKHALq 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 ---NMLVMNLgsEEPDIMSVAVRPGVVDTpmqvsirnDSNKEAMGGDTHNFFKELKTSGQLVAPQDIAKA 224
Cdd:cd05332 162 gffDSLRAEL--SEPNISVTVVCPGLIDT--------NIAMNALSGDGSMSAKMDDTTANGMSPEECALE 221
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 7-239 2.03e-25

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: 100.22  E-value: 2.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIA--VSRSLTPELETLLIQNPDSFVHvkGDVTEVG--KASIETAIKKFGKLDS 81
Cdd:cd05326   5 KVAIITGGASGIGEATARLFAKHgARVVIadIDDDAGQAVAAELGDPDISFVH--CDVTVEAdvRAAVDTAVARFGRLDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVL-EPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:cd05326  83 MFNNAGVLgAPCYSILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKkGSIVSVASVAGVVGGLGPHAYTASKHAVLG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 160 LVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRnDSNKEAMGGDTHNFFKELktsGQLVAPQDIAKALSFLALNNNPKLT 237
Cdd:cd05326 163 LTRSAATElgEHGIRVNCVSPYGVATPLLTAGF-GVEDEAIEEAVRGAANLK---GTALRPEDIAAAVLYLASDDSRYVS 238


                ..
gi 19113072 238 GQ 239
Cdd:cd05326 239 GQ 240
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 7-242 5.19e-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: 98.46  E-value: 5.19e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL--QKKAKVIAVSRSLTPELETL--LIQNPDSFVHVKGDVTEvgKASIETA----IKKFGK 78
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLakSGPGTVILTARDVERGQAAVekLRAEGLSVRFHQLDVTD--DASIEAAadfvEEKYGG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  79 LDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRvfpaWAAYCCSKAAI 157
Cdd:cd05324  79 LDILVNNAGIAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVNVSSGLGSL----TSAYGVSKAAL 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE--EPDIMSVAVRPGVVDTpmqvsirndsnkeAMGGDthnffKELKTsgqlvaPQDIAKALSFLALN-NNP 234
Cdd:cd05324 155 NALTRILAKElkETGIKVNACCPGWVKT-------------DMGGG-----KAPKT------PEEGAETPVYLALLpPDG 210


                ....*...
gi 19113072 235 KLTGQFVE 242
Cdd:cd05324 211 EPTGKFFS 218
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 7-238 5.65e-25

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: 98.94  E-value: 5.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTP---ELETLLIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLD 80
Cdd:cd05352   9 KVAIVTGGSRGIGLAIARALaEAGADVAIIYNSAPRaeeKAEELAKKYGVKTKAYKCDVSsqESVEKTFKQIQKDFGKID 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLEPIAkIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRV-FPA-WAAYCCSKAAI 157
Cdd:cd05352  89 ILIANAGITVHKP-ALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQgKGSLIITASMSGTIVnRPQpQAAYNASKAAV 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPMqvsirndsnKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALNNNPK 235
Cdd:cd05352 168 IHLAKSLAVEwaKYFIRVNSISPGYIDTDL---------TDFVDKELRKKWESYIPLKRIALPEELVGAYLYLASDASSY 238


                ...
gi 19113072 236 LTG 238
Cdd:cd05352 239 TTG 241
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 1-229 5.72e-25

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 99.23  E-value: 5.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLtPELETL---LIQNPDSFVHVKGDVTEVG--KASIETAIK 74
Cdd:PRK07478   1 MMRLNGKVAIITGASSGIGRAAAKLFaREGAKVVVGARRQ-AELDQLvaeIRAEGGEAVALAGDVRDEAyaKALVALAVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRV-FPAWAAYCC 152
Cdd:PRK07478  80 RFGGLDIAFNNAGTLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGgGSLIFTSTFVGHTAgFPGMAAYAA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072  153 SKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDsnkeamgGDTHNFFKELKTSGQLVAPQDIAKALSFLA 229
Cdd:PRK07478 160 SKAGLIGLTQVLAAEygAQGIRVNALLPGGTDTPMGRAMGDT-------PEALAFVAGLHALKRMAQPEEIAQAALFLA 231
PRK06181 PRK06181
SDR family oxidoreductase;
7-245 1.00e-24

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 98.51  E-value: 1.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTpELETLLIQNPDSFVHVKGDVTEVGKAS-----IETAIKKFGKLD 80
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLaRAGAQLVLAARNET-RLASLAQELADHGGEALVVPTDVSDAEacerlIEAAVARFGGID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGV--LEPIAKIADADIneWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:PRK06181  81 ILVNNAGItmWSRFDELTDLSV--FERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGLTGVPTRSGYAASKHALH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  159 MLVMNLGSE-EPDIMSVA-VRPGVVDTpmqvsirnDSNKEAMGGDThnffKELKTSG----QLVAPQDIAKALSFLALNN 232
Cdd:PRK06181 159 GFFDSLRIElADDGVAVTvVCPGFVAT--------DIRKRALDGDG----KPLGKSPmqesKIMSAEECAEAILPAIARR 226

                        250
                 ....*....|...
gi 19113072  233 NPKLTGQFVEWKS 245
Cdd:PRK06181 227 KRLLVMSLRGRLG 239
PRK09135 PRK09135
pteridine reductase; Provisional
 1-239 1.09e-24

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 98.08  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLL----IQNPDSFVHVKGDVTEVGKAS--IETAI 73
Cdd:PRK09135   1 MMTDSAKVALITGGARRIGAAIARTLHAAgYRVAIHYHRSAAEADALAaelnALRPGSAAALQADLLDPDALPelVAACV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   74 KKFGKLDSVILNAGVLEPIAkIADADINEWRKLFDIN----FFsvveTVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAA 149
Cdd:PRK09135  81 AAFGRLDALVNNASSFYPTP-LGSITEAQWDDLFASNlkapFF----LSQAAAPQLRKQRGAIVNITDIHAERPLKGYPV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  150 YCCSKAAINMLVMNLGSE-EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDThnffkELKTSGQlvaPQDIAKALSFL 228
Cdd:PRK09135 156 YCAAKAALEMLTRSLALElAPEVRVNAVAPGAILWPEDGNSFDEEARQAILART-----PLKRIGT---PEDIAEAVRFL 227

                        250
                 ....*....|.
gi 19113072  229 aLNNNPKLTGQ 239
Cdd:PRK09135 228 -LADASFITGQ 237
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 7-229 1.23e-24

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 98.03  E-value: 1.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPeletlliQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:PRK08220   9 KTVWVTGAAQGIGYAVALAFvEAGAKVIGFDQAFLT-------QEDYPFATFVLDVSDAAavAQVCQRLLAETGPLDVLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAGVLE--PIAKIADADineWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK08220  82 NAAGILRmgATDSLSDED---WQQTFAVNAGGAFNLFRAVMPQFRRQRsGAIVTVGSNAAHVPRIGMAAYGASKAALTSL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113072  161 VMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAmgGDTHNFFKELKTS---GQLVAPQDIAKALSFLA 229
Cdd:PRK08220 159 AKCVGLElaPYGVRCNVVSPGSTDTDMQRTLWVDEDGEQ--QVIAGFPEQFKLGiplGKIARPQEIANAVLFLA 230
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 7-239 2.90e-24

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 97.19  E-value: 2.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVI---AVSRSLTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLD 80
Cdd:PRK05557   6 KVALVTGASRGIGRAIAERLAAQgANVVinyASSEAGAEALVAEIGALGGKALAVQGDVSDAEsvERAVDEAKAEFGGVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLE--PIAKIADADineWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:PRK05557  86 ILVNNAGITRdnLLMRMKEED---WDRVIDTNLTGVFNLTKAVARPMMKQRsGRIINISSVVGLMGNPGQANYAASKAGV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPMqVSIRNDSNKEAMggdthnffkeLKTS--GQLVAPQDIAKALSFLALNNN 233
Cdd:PRK05557 163 IGFTKSLARElaSRGITVNAVAPGFIETDM-TDALPEDVKEAI----------LAQIplGRLGQPEEIASAVAFLASDEA 231


                 ....*.
gi 19113072  234 PKLTGQ 239
Cdd:PRK05557 232 AYITGQ 237
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-242 3.08e-24

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: 97.07  E-value: 3.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTP---ELETLLIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLD 80
Cdd:cd05358   4 KVALVTGASSGIGKAIAIRLaTAGANVVVNYRSKEDaaeEVVEEIKAVGGKAIAVQADVSkeEDVVALFQSAIKEFGTLD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGvLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:cd05358  84 ILVNNAG-LQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKikGKIINMSSVHEKIPWPGHVNYAASKGGVK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 159 MLVMNLGSEEPD--IMSVAVRPGVVDTPMQVSIRNDSNKEAmggdthnffKELK--TSGQLVAPQDIAKALSFLALNNNP 234
Cdd:cd05358 163 MMTKTLAQEYAPkgIRVNAIAPGAINTPINAEAWDDPEQRA---------DLLSliPMGRIGEPEEIAAAAAWLASDEAS 233

                       250
                ....*....|
gi 19113072 235 KLTGQ--FVE 242
Cdd:cd05358 234 YVTGTtlFVD 243
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 6-240 3.72e-24

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: 97.36  E-value: 3.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   6 EKVILLTGSSKGIGLATAEALQKKAKVIAVS-----RSLTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGK 78
Cdd:cd05355  26 GKKALITGGDSGIGRAVAIAFAREGADVAINylpeeEDDAEETKKLIEEEGRKCLLIPGDLGDESfcRDLVKEVVKEFGK 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  79 LDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLrKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:cd05355 106 LDILVNNAAYQHPQESIEDITTEQLEKTFRTNIFSMFYLTKAALPHL-KKGSSIINTTSVTAYKGSPHLLDYAATKGAIV 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 159 MLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDThnffkELKTSGQlvaPQDIAKALSFLALNNNPKL 236
Cdd:cd05355 185 AFTRGLSLQlaEKGIRVNAVAPGPIWTPLIPSSFPEEKVSEFGSQV-----PMGRAGQ---PAEVAPAYVFLASQDSSYV 256


                ....
gi 19113072 237 TGQF 240
Cdd:cd05355 257 TGQV 260
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 2-229 5.54e-24

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 96.35  E-value: 5.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    2 AETAEKVILLTGSSKGIGLATAEALQKKAKVIAV----SRSLTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKK 75
Cdd:PRK12937   1 MTLSNKVAIVTGASRGIGAAIARRLAADGFAVAVnyagSAAAADELVAEIEAAGGRAIAVQADVADAAavTRLFDAAETA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKtKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK12937  81 FGRIDVLVNNAGVM-PLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQ-GGRIINLSTSVIALPLPGYGPYAASKA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113072  156 AINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGdthnffkeLKTSGQLVAPQDIAKALSFLA 229
Cdd:PRK12937 159 AVEGLVHVLANElrGRGITVNAVAPGPVATELFFNGKSAEQIDQLAG--------LAPLERLGTPEEIAAAVAFLA 226
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 7-228 7.08e-24

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 95.65  E-value: 7.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSlTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:cd08929   1 KAALVTGASRGIGEATARLLhAEGYRVGICARD-EARLAAAAAQELEGVLGLAGDVRDEAdvRRAVDAMEEAFGGLDALV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  84 LNAGV--LEPIAKIADadINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINML- 160
Cdd:cd08929  80 NNAGVgvMKPVEELTP--EEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLs 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072 161 -VMNLGSEEPDIMSVAVRPGVVDTpmqvsirndsnkeamggdthNFFKELKTSGQLVAPQDIAKALSFL 228
Cdd:cd08929 158 eAAMLDLREANIRVVNVMPGSVDT--------------------GFAGSPEGQAWKLAPEDVAQAVLFA 206
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 5-241 7.54e-24

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: 96.07  E-value: 7.54e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLtpeletlliQNPDSFV--------HVKGDVTEVGKAS-----IE 70
Cdd:cd08936   9 ANKVALVTASTDGIGLAIARRLaQDGAHVVVSSRKQ---------QNVDRAVatlqgeglSVTGTVCHVGKAEdrerlVA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  71 TAIKKFGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAA 149
Cdd:cd08936  80 TAVNLHGGVDILVSNAAVNPFFGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRgGGSVVIVSSVAAFHPFPGLGP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 150 YCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEamggdtHNFFKELKTSgQLVAPQDIAKALSF 227
Cdd:cd08936 160 YNVSKTALLGLTKNLAPElaPRNIRVNCLAPGLIKTSFSSALWMDKAVE------ESMKETLRIR-RLGQPEDCAGIVSF 232

                       250
                ....*....|....
gi 19113072 228 LALNNNPKLTGQFV 241
Cdd:cd08936 233 LCSEDASYITGETV 246
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 7-241 1.71e-23

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 95.14  E-value: 1.71e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVT-EVG-KASIETAIKKFGKLDSVIL 84
Cdd:cd05341   6 KVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTdEDGwTAVVDTAREAFGRLDVLVN 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  85 NAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAINML--- 160
Cdd:cd05341  86 NAGILT-GGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAgGGSIINMSSIEGLVGDPALAAYNASKGAVRGLtks 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 161 -VMNLGSEEPDIMSVAVRPGVVDTPMQVSIRNDsnkeamGGDTHNFFKELktSGQLVAPQDIAKALSFLALNNNPKLTG- 238
Cdd:cd05341 165 aALECATQGYGIRVNSVHPGYIYTPMTDELLIA------QGEMGNYPNTP--MGRAGEPDEIAYAVVYLASDESSFVTGs 236


                ...
gi 19113072 239 QFV 241
Cdd:cd05341 237 ELV 239
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-239 4.87e-23

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: 93.96  E-value: 4.87e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLT--PELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDS 81
Cdd:cd05347   6 KVALVTGASRGIGFGIASGLAEAgANIVINSRNEEkaEEAQQLIEKEGVEATAFTCDVSDEEaiKAAVEAIEEDFGKIDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGV--LEPIAKIADADineWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:cd05347  86 LVNNAGIirRHPAEEFPEAE---WRDVIDVNLNGVFFVSQAVARHMIKQGhGKIINICSLLSELGGPPVPAYAASKGGVA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 159 MLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSnkeamggDTHNFFKELKTSGQLVAPQDIAKALSFLALNNNPKL 236
Cdd:cd05347 163 GLTKALATEwaRHGIQVNAIAPGYFATEMTEAVVADP-------EFNDDILKRIPAGRWGQPEDLVGAAVFLASDASDYV 235


                ...
gi 19113072 237 TGQ 239
Cdd:cd05347 236 NGQ 238
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
5-239 4.91e-23

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 97.22  E-value: 4.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPELETL-LIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLD 80
Cdd:PRK08324 421 AGKVALVTGAAGGIGKATAKRLaAEGACVVLADLDEEAAEAAAaELGGPDRALGVACDVTDEAavQAAFEEAALAFGGVD 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGvLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK--TKGTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:PRK08324 501 IVVSNAG-IAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAqgLGGSIVFIASKNAVNPGPNFGAYGAAKAAEL 579

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  159 MLVMNLGSEE-PD-IMSVAVRP-GVV-DTPMQVSIRNDSNKEAMGGDTHNFFKE------LKTSgqlVAPQDIAKALSFL 228
Cdd:PRK08324 580 HLVRQLALELgPDgIRVNGVNPdAVVrGSGIWTGEWIEARAAAYGLSEEELEEFyrarnlLKRE---VTPEDVAEAVVFL 656

                        250
                 ....*....|.
gi 19113072  229 ALNNNPKLTGQ 239
Cdd:PRK08324 657 ASGLLSKTTGA 667
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 7-239 1.03e-22

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 93.03  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLT--PELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDS 81
Cdd:PRK12429   5 KVALVTGAASGIGLEIALALAKEgAKVVIADLNDEaaAAAAEALQKAGGKAIGVAMDVTDEEaiNAGIDYAVETFGGVDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGvLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK12429  85 LVNNAG-IQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGgGRIINMASVHGLVGSAGKAAYVSAKHGLIGL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  161 --VMNLGSEEPDIMSVAVRPGVVDTPM-------QVSIRNDSNKEAMggdtHNFFKELKTSGQLVAPQDIAKALSFLALN 231
Cdd:PRK12429 164 tkVVALEGATHGVTVNAICPGYVDTPLvrkqipdLAKERGISEEEVL----EDVLLPLVPQKRFTTVEEIADYALFLASF 239


                 ....*...
gi 19113072  232 NNPKLTGQ 239
Cdd:PRK12429 240 AAKGVTGQ 247
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 10-239 1.15e-22

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: 92.80  E-value: 1.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  10 LLTGSSKGIGLATAEAL-QKKAKVIAVSRS---LTPELETLLIQNPDSFVHVKGDVTEVGK-ASIETAIK-KFGKLDSVI 83
Cdd:cd05359   2 LVTGGSRGIGKAIALRLaERGADVVINYRKskdAAAEVAAEIEELGGKAVVVRADVSQPQDvEEMFAAVKeRFGRLDVLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  84 LNA--GVLEPIAKIadaDINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:cd05359  82 SNAaaGAFRPLSEL---TPAHWDAKMNTNLKALVHCAQQAAKLMRERGgGRIVAISSLGSIRALPNYLAVGTAKAALEAL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 161 VMNLGSEEPD--IMSVAVRPGVVDTPM-----QVSIRNDSNKEAMGgdthnffkelktSGQLVAPQDIAKALSFLALNNN 233
Cdd:cd05359 159 VRYLAVELGPrgIRVNAVSPGVIDTDAlahfpNREDLLEAAAANTP------------AGRVGTPQDVADAVGFLCSDAA 226


                ....*.
gi 19113072 234 PKLTGQ 239
Cdd:cd05359 227 RMITGQ 232
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
 8-228 1.21e-22

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: 93.05  E-value: 1.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072     8 VILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDV--------------TEVGKASIETAI 73
Cdd:TIGR01500   2 VCLVTGASRGFGRTIAQELAKCLKSPGSVLVLSARNDEALRQLKAEIGAERSGLrvvrvsldlgaeagLEQLLKALRELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    74 KK--FGKLdSVILNAGVLEPIAKIAD--ADINEWRKLFDINFFSVVET---VKYAIPHLRKTKGTIVIVSSGAAVRVFPA 146
Cdd:TIGR01500  82 RPkgLQRL-LLINNAGTLGDVSKGFVdlSDSTQVQNYWALNLTSMLCLtssVLKAFKDSPGLNRTVVNISSLCAIQPFKG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   147 WAAYCCSKAAINMLVMNLGSEE--PDIMSVAVRPGVVDTPMQVSIRndsnKEAMGGDTHNFFKELKTSGQLVAPQDIAKA 224
Cdd:TIGR01500 161 WALYCAGKAARDMLFQVLALEEknPNVRVLNYAPGVLDTDMQQQVR----EESVDPDMRKGLQELKAKGKLVDPKVSAQK 236


                  ....
gi 19113072   225 LSFL 228
Cdd:TIGR01500 237 LLSL 240
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 7-185 1.34e-22

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: 92.47  E-value: 1.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL--QKKAKVIAVSRSLTpELETLLIQNPDSFVHVKGDVTEvgKASIETAIKKFGKLDSVIL 84
Cdd:cd05354   4 KTVLVTGANRGIGKAFVESLlaHGAKKVYAAVRDPG-SAAHLVAKYGDKVVPLRLDVTD--PESIKAAAAQAKDVDVVIN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  85 NAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMN 163
Cdd:cd05354  81 NAGVLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLkANGGGAIVNLNSVASLKNFPAMGTYSASKSAAYSLTQG 160

                       170       180
                ....*....|....*....|....
gi 19113072 164 LGSE--EPDIMSVAVRPGVVDTPM 185
Cdd:cd05354 161 LRAElaAQGTLVLSVHPGPIDTRM 184
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-185 1.38e-22

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 92.33  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSLTPELEtlliqnpDSFVHVKGDVTEvgkaSIETAIKKFGKLDsVILN 85
Cdd:PRK06550   6 KTVLITGAASGIGLAQARAfLAQGAQVYGVDKQDKPDLS-------GNFHFLQLDLSD----DLEPLFDWVPSVD-ILCN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   86 -AGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMN 163
Cdd:PRK06550  74 tAGILDDYKPLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQmLERKSGIIINMCSIASFVAGGGGAAYTASKHALAGFTKQ 153

                        170       180
                 ....*....|....*....|....
gi 19113072  164 LGSEEPD--IMSVAVRPGVVDTPM 185
Cdd:PRK06550 154 LALDYAKdgIQVFGIAPGAVKTPM 177
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 7-241 1.56e-22

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 92.51  E-value: 1.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTP-----ELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKL 79
Cdd:cd08940   3 KVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAaeieaVRAGLAAKHGVKVLYHGADLSKPAaiEDMVAYAQRQFGGV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  80 DSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:cd08940  83 DILVNNAGI-QHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGwGRIINIASVHGLVASANKSAYVAAKHGVV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 159 ML--VMNLGSEEPDIMSVAVRPGVVDTPM-QVSIRNDSNKEAMGGDT--HNFFKELKTSGQLVAPQDIAKALSFLALNNN 233
Cdd:cd08940 162 GLtkVVALETAGTGVTCNAICPGWVLTPLvEKQISALAQKNGVPQEQaaRELLLEKQPSKQFVTPEQLGDTAVFLASDAA 241


                ....*...
gi 19113072 234 PKLTGQFV 241
Cdd:cd08940 242 SQITGTAV 249
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 1-239 1.91e-22

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 92.34  E-value: 1.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETL---LIQNPDSFVHVKGDVTEVG--KASIETAIKK 75
Cdd:PRK12939   2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNDGLAAEARELaaaLEAAGGRAHAIAADLADPAsvQRFFDAAAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PRK12939  82 LGGLDGLVNNAGIT-NSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGrGRIVNLASDTALWGAPKLGAYVASK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTpmqvsirnDSNKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALNN 232
Cdd:PRK12939 161 GAVIGMTRSLARElgGRGITVNAIAPGLTAT--------EATAYVPADERHAYYLKGRALERLQVPDDVAGAVLFLLSDA 232


                 ....*..
gi 19113072  233 NPKLTGQ 239
Cdd:PRK12939 233 ARFVTGQ 239
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 5-229 2.82e-22

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 92.21  E-value: 2.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEA-LQKKAKVI------AVSRSLTPELETlliQNPDSFVHVKGDVT--EVGKASIETAIKK 75
Cdd:cd08933   8 ADKVVIVTGGSRGIGRGIVRAfVENGAKVVfcargeAAGQALESELNR---AGPGSCKFVPCDVTkeEDIKTLISVTVER 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  76 FGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:cd08933  85 FGRIDCLVNNAGWHPPHQTTDETSAQEFRDLLNLNLISYFLASKYALPHLRKSQGNIINLSSLVGSIGQKQAAPYVATKG 164

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072 156 AINMLVMNLGSEEP--DIMSVAVRPGVVDTPMQVSIrndsnkEAMGGDTHNFFKELKTS---GQLVAPQDIAKALSFLA 229
Cdd:cd08933 165 AITAMTKALAVDESryGVRVNCISPGNIWTPLWEEL------AAQTPDTLATIKEGELAqllGRMGTEAESGLAALFLA 237
PRK06172 PRK06172
SDR family oxidoreductase;
1-239 3.09e-22

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 91.74  E-value: 3.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETL-LIQNPDS-FVHVKGDVTEVG--KASIETAIKK 75
Cdd:PRK06172   2 SMTFSGKVALVTGGAAGIGRATALAFAREgAKVVVADRDAAGGEETVaLIREAGGeALFVACDVTRDAevKALVEQTIAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PRK06172  82 YGRLDYAFNNAGIEIEQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLmLAQGGGAIVNTASVAGLGAAPKMSIYAASK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQvsirndsnKEAMGGDThnFFKELKTS----GQLVAPQDIAKALSFL 228
Cdd:PRK06172 162 HAVIGLTKSAAIEyaKKGIRVNAVCPAVIDTDMF--------RRAYEADP--RKAEFAAAmhpvGRIGKVEEVASAVLYL 231

                        250
                 ....*....|.
gi 19113072  229 ALNNNPKLTGQ 239
Cdd:PRK06172 232 CSDGASFTTGH 242
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 6-157 3.55e-22

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 92.02  E-value: 3.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSKGIGLATAE-ALQKKAKVIAVSRSLTPeLETLLIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLDSV 82
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEaALERGDRVVATARDTAT-LADLAEKYGDRLLPLALDVTdrAAVFAAVETAVEHFGRLDIV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113072   83 ILNAG--VLEPIAKIADADInewRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:PRK08263  82 VNNAGygLFGMIEEVTESEA---RAQIDTNFFGALWVTQAVLPYLREQrSGHIIQISSIGGISAFPMSGIYHASKWAL 156
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-239 7.53e-22

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 90.94  E-value: 7.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVsrsLTPELETL------LIQNPDSFVHVKGDVT---EVGKAsIETAIKKFG 77
Cdd:PRK08643   3 KVALVTGAGQGIGFAIAKRLVEDGFKVAI---VDYNEETAqaaadkLSKDGGKAIAVKADVSdrdQVFAA-VRQVVDTFG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGV--LEPIAKIADADINewrKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAAYCCS 153
Cdd:PRK08643  79 DLNVVVNNAGVapTTPIETITEEQFD---KVYNINVGGVIWGIQAAQEAFKKLGhgGKIINATSQAGVVGNPELAVYSST 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  154 KAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEA---MGGDTHNFFKELkTSGQLVAPQDIAKALSFL 228
Cdd:PRK08643 156 KFAVRGLTQTAARDlaSEGITVNAYAPGIVKTPMMFDIAHQVGENAgkpDEWGMEQFAKDI-TLGRLSEPEDVANCVSFL 234

                        250
                 ....*....|.
gi 19113072  229 ALNNNPKLTGQ 239
Cdd:PRK08643 235 AGPDSDYITGQ 245
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 7-195 8.94e-22

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: 90.22  E-value: 8.94e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSlTPELETLLIQNPdSFVHVKGDVTEvgKASIETA----IKKFGKLDS 81
Cdd:COG3967   6 NTILITGGTSGIGLALAKRLHARgNTVIITGRR-EEKLEEAAAANP-GLHTIVLDVAD--PASIAALaeqvTAEFPDLNV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPI-AKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:COG3967  82 LINNAGIMRAEdLLDEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQPeAAIVNVSSGLAFVPLAVTPTYSATKAALHS 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19113072 160 LVMNL-----GSeepdimSVAVR---PGVVDTPMQVSIRNDSNK 195
Cdd:COG3967 162 YTQSLrhqlkDT------SVKVIelaPPAVDTDLTGGQGGDPRA 199
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 7-239 9.72e-22

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 90.22  E-value: 9.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVsrSLTPELETLLIQNPdSFVHVKGDVTEvgKASIETAIKKFGKLDSVILN 85
Cdd:cd05368   3 KVALITAAAQGIGRAIALAFAREgANVIAT--DINEEKLKELERGP-GITTRVLDVTD--KEQVAALAKEEGRIDVLFNC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  86 AGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAA-VRVFPAWAAYCCSKAAINMLVMN 163
Cdd:cd05368  78 AGFV-HHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKdGSIINMSSVASsIKGVPNRFVYSTTKAAVIGLTKS 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072 164 LGSE--EPDIMSVAVRPGVVDTPM-QVSIRNDSNKEAMGGDthnfFKELKTSGQLVAPQDIAKALSFLALNNNPKLTGQ 239
Cdd:cd05368 157 VAADfaQQGIRCNAICPGTVDTPSlEERIQAQPDPEEALKA----FAARQPLGRLATPEEVAALAVYLASDESAYVTGT 231
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 5-185 1.13e-21

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 90.22  E-value: 1.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSlTPELETLLIQNPdSFVHVKGDVTevGKASIETAIKKFGKLDSVI 83
Cdd:cd05351   6 AGKRALVTGAGKGIGRATVKALAKAgARVVAVSRT-QADLDSLVRECP-GIEPVCVDLS--DWDATEEALGSVGPVDLLV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  84 LNAGV--LEPIAKIADADINewrKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:cd05351  82 NNAAVaiLQPFLEVTKEAFD---RSFDVNVRAVIHVSQIVARGMiaRGVPGSIVNVSSQASQRALTNHTVYCSTKAALDM 158

                       170       180       190
                ....*....|....*....|....*....|
gi 19113072 160 L----VMNLGSEEpdIMSVAVRPGVVDTPM 185
Cdd:cd05351 159 LtkvmALELGPHK--IRVNSVNPTVVMTDM 186
PRK06484 PRK06484
short chain dehydrogenase; Validated
 5-229 1.30e-21

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 92.99  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSV 82
Cdd:PRK06484 268 SPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAavESAFAQIQARWGRLDVL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   83 ILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTkGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVM 162
Cdd:PRK06484 348 VNNAGIAEVFKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMSQG-GVIVNLGSIASLLALPPRNAYCASKAAVTMLSR 426

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072  163 NLGSE--EPDIMSVAVRPGVVDTPMQVSIrndsnkEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLA 229
Cdd:PRK06484 427 SLACEwaPAGIRVNTVAPGYIETPAVLAL------KASGRADFDSIRRRIPLGRLGDPEEVAEAIAFLA 489
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
5-239 1.70e-21

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 89.78  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKKAKVIAV--SRSLTPELETL--LIQNPDSFVHVKGDVTEVGK--ASIETAIKKFGK 78
Cdd:PRK08063   3 SGKVALVTGSSRGIGKAIALRLAEEGYDIAVnyARSRKAAEETAeeIEALGRKALAVKANVGDVEKikEMFAQIDEEFGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNA--GVLEPIAKIadaDINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK08063  83 LDVFVNNAasGVLRPAMEL---EESHWDWTMNINAKALLFCAQEAAKLMEKVGgGKIISLSSLGSIRYLENYTTVGVSKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  156 AINMLVMNLGSE-EPDIMSV-AVRPGVVDTPmqvSIRNDSNKEAMGGDthnfFKELKTSGQLVAPQDIAKALSFLALNNN 233
Cdd:PRK08063 160 ALEALTRYLAVElAPKGIAVnAVSGGAVDTD---ALKHFPNREELLED----ARAKTPAGRMVEPEDVANAVLFLCSPEA 232


                 ....*.
gi 19113072  234 PKLTGQ 239
Cdd:PRK08063 233 DMIRGQ 238
PRK09242 PRK09242
SDR family oxidoreductase;
7-239 2.25e-21

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 89.42  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATA-EALQKKAKVIAVSRS---LTPELETLLIQNPDSFVH-VKGDVT--EVGKASIETAIKKFGKL 79
Cdd:PRK09242  10 QTALITGASKGIGLAIArEFLGLGADVLIVARDadaLAQARDELAEEFPEREVHgLAADVSddEDRRAILDWVEDHWDGL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVlePIAKIA-DADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:PRK09242  90 HILVNNAGG--NIRKAAiDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHAsSAIVNIGSVSGLTHVRSGAPYGMTKAAL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNK-EAMGGDThnffkELKTSGQlvaPQDIAKALSFLALNNNP 234
Cdd:PRK09242 168 LQMTRNLAVEwaEDGIRVNAVAPWYIRTPLTSGPLSDPDYyEQVIERT-----PMRRVGE---PEEVAAAVAFLCMPAAS 239


                 ....*
gi 19113072  235 KLTGQ 239
Cdd:PRK09242 240 YITGQ 244
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-241 5.48e-21

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 88.30  E-value: 5.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSlTPELETLLIQNPDSFVhVKGDVTEVG--KASIETAIKKFGKLDSVIL 84
Cdd:PRK06463   8 KVALITGGTRGIGRAIAEAFLREGAKVAVLYN-SAENEAKELREKGVFT-IKCDVGNRDqvKKSKEVVEKEFGRVDVLVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   85 NAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVrvfpAWAA-----YCCSKAAIN 158
Cdd:PRK06463  86 NAGIMY-LMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLkLSKNGAIVNIASNAGI----GTAAegttfYAITKAGII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  159 MLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMggdtHNFFKE---LKTSGQlvaPQDIAKALSFLALNNN 233
Cdd:PRK06463 161 ILTRRLAFElgKYGIRVNAVAPGWVETDMTLSGKSQEEAEKL----RELFRNktvLKTTGK---PEDIANIVLFLASDDA 233


                 ....*...
gi 19113072  234 PKLTGQFV 241
Cdd:PRK06463 234 RYITGQVI 241
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 7-179 7.07e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 88.43  E-value: 7.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAE-ALQKKAKVIAVSRSlTPELETLLIQNPDSFVHVKGDVTEvgKASIETAIK----KFGKLDS 81
Cdd:PRK06180   5 KTWLITGVSSGFGRALAQaALAAGHRVVGTVRS-EAARADFEALHPDRALARLLDVTD--FDAIDAVVAdaeaTFGPIDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGV-LEPIakIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:PRK06180  82 LVNNAGYgHEGA--IEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRrGHIVNITSMGGLITMPGIGYYCGSKFALEG 159

                        170       180
                 ....*....|....*....|..
gi 19113072  160 LVMNLGSE-EP-DIMSVAVRPG 179
Cdd:PRK06180 160 ISESLAKEvAPfGIHVTAVEPG 181
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 5-238 9.53e-21

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: 87.83  E-value: 9.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSLTpELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDS 81
Cdd:cd05345   4 EGKVAIVTGAGSGFGEGIARRfAQEGARVVIADINAD-GAERVAADIGEAAIAIQADVTKRAdvEAMVEAALSKFGRLDI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVI-VSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:cd05345  83 LVNNAGITHRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIInIASTAGLRPRPGLTWYNASKGWVVTA 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 161 VMNLGSE--EPDIMSVAVRPGVVDTPMQvsirndsnKEAMGGDTHNFFKELKTS---GQLVAPQDIAKALSFLALNNNPK 235
Cdd:cd05345 163 TKAMAVElaPRNIRVNCLCPVAGETPLL--------SMFMGEDTPENRAKFRATiplGRLSTPDDIANAALYLASDEASF 234


                ...
gi 19113072 236 LTG 238
Cdd:cd05345 235 ITG 237
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 6-185 1.38e-20

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 87.34  E-value: 1.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   6 EKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLLIQNPDSFVHVkgDVTEV--GKASIETAIKKFGKLDSV 82
Cdd:cd05371   2 GLVAVVTGGASGLGLATVERLLAQgAKVVILDLPNSPGETVAKLGDNCRFVPV--DVTSEkdVKAALALAKAKFGRLDIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  83 ILNAGVlEPIAKIADADIN------EWRKLFDINFFSVVETVKYAIPHLRKT-------KGTIVIVSSGAAVRVFPAWAA 149
Cdd:cd05371  80 VNCAGI-AVAAKTYNKKGQqphsleLFQRVINVNLIGTFNVIRLAAGAMGKNepdqggeRGVIINTASVAAFEGQIGQAA 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19113072 150 YCCSKAAINMLVM----NLGSEEPDIMSVAvrPGVVDTPM 185
Cdd:cd05371 159 YSASKGGIVGMTLpiarDLAPQGIRVVTIA--PGLFDTPL 196
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-239 1.57e-20

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 87.08  E-value: 1.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPEL-ETLLI--QNPDSFVHVKGDV-TEVGKASI-ETAIK 74
Cdd:PRK06077   1 MYSLKDKVVVVTGSGRGIGRAIAVRLAKEgSLVVVNAKKRAEEMnETLKMvkENGGEGIGVLADVsTREGCETLaKATID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNAGvLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKtKGTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PRK06077  81 RYGVADILVNNAG-LGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMRE-GGAIVNIASVAGIRPAYGLSIYGAMK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE-EPDIMSVAVRPGVVDTPMqvsirNDSNKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLAlnNN 233
Cdd:PRK06077 159 AAVINLTKYLALElAPKIRVNAIAPGFVKTKL-----GESLFKVLGMSEKEFAEKFTLMGKILDPEEVAEFVAAIL--KI 231


                 ....*.
gi 19113072  234 PKLTGQ 239
Cdd:PRK06077 232 ESITGQ 237
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 7-239 3.19e-20

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: 86.06  E-value: 3.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLLIQN--PDSFVHVKGDVT--EVGKASIETAIKKFGKLDS 81
Cdd:cd05333   1 KVALVTGASRGIGRAIALRLAAEgAKVAVTDRSEEAAAETVEEIKalGGNAAALEADVSdrEAVEALVEKVEAEFGPVDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVL--EPIAKIADADineWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:cd05333  81 LVNNAGITrdNLLMRMSEED---WDAVINVNLTGVFNVTQAVIRAMIKRRsGRIINISSVVGLIGNPGQANYAASKAGVI 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 159 MLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGgdthnfFKELKTSGQlvaPQDIAKALSFLALNNNPKL 236
Cdd:cd05333 158 GFTKSLAKElaSRGITVNAVAPGFIDTDMTDALPEKVKEKILK------QIPLGRLGT---PEEVANAVAFLASDDASYI 228


                ...
gi 19113072 237 TGQ 239
Cdd:cd05333 229 TGQ 231
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 9-185 4.31e-20

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: 85.84  E-value: 4.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   9 ILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETL---LIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLDSVI 83
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELkaeLLNPNPSVEVEILDVTdeERNQLVIAELEAELGGLDLVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  84 LNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVM 162
Cdd:cd05350  81 INAGVGKG-TSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGrGHLVLISSVAALRGLPGAAAYSASKAALSSLAE 159

                       170       180
                ....*....|....*....|....*.
gi 19113072 163 NLgSEEPDIMSVAV---RPGVVDTPM 185
Cdd:cd05350 160 SL-RYDVKKRGIRVtviNPGFIDTPL 184
PRK06947 PRK06947
SDR family oxidoreductase;
7-242 5.30e-20

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 85.63  E-value: 5.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVS----RSLTPELETLLIQNPDSFVHVKGDVTEVGK--ASIETAIKKFGKLD 80
Cdd:PRK06947   3 KVVLITGASRGIGRATAVLAAARGWSVGINyardAAAAEETADAVRAAGGRACVVAGDVANEADviAMFDAVQSAFGRLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK----GTIVIVSSGAAVRVFP-AWAAYCCSKA 155
Cdd:PRK06947  83 ALVNNAGIVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRggrgGAIVNVSSIASRLGSPnEYVDYAGSKG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  156 AINMLVMNLGSE-EPDIMSV-AVRPGVVDTPMQVSIRNDSNKEAMGGDThnffkELKTSGQlvaPQDIAKALSFLALNNN 233
Cdd:PRK06947 163 AVDTLTLGLAKElGPHGVRVnAVRPGLIETEIHASGGQPGRAARLGAQT-----PLGRAGE---ADEVAETIVWLLSDAA 234


                 ....*....
gi 19113072  234 PKLTGQFVE 242
Cdd:PRK06947 235 SYVTGALLD 243
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
1-238 5.52e-20

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 86.01  E-value: 5.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSltPELETL---LIQNPDSFVHVKGDVTEVG--KASIETAIK 74
Cdd:PRK08226   1 MGKLTGKTALITGALQGIGEGIARVFARHgANLILLDIS--PEIEKLadeLCGRGHRCTAVVADVRDPAsvAAAIKRAKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNAGV--LEPIAKIADADinewRKL-FDINFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRVF-PAWAA 149
Cdd:PRK08226  79 KEGRIDILVNNAGVcrLGSFLDMSDED----RDFhIDINIKGVWNVTKAVLPEmIARKDGRIVMMSSVTGDMVAdPGETA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  150 YCCSKAAINMLVMNLGSEEPD--IMSVAVRPGVVDTPMQVSIRNDSNKEamggDTHNFFKELKTS---GQLVAPQDIAKA 224
Cdd:PRK08226 155 YALTKAAIVGLTKSLAVEYAQsgIRVNAICPGYVRTPMAESIARQSNPE----DPESVLTEMAKAiplRRLADPLEVGEL 230

                        250
                 ....*....|....
gi 19113072  225 LSFLALNNNPKLTG 238
Cdd:PRK08226 231 AAFLASDESSYLTG 244
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 7-197 5.58e-20

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 85.54  E-value: 5.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTpELETLLIQNPDSFVHVkgDVTevGKASIETAIKKFGKLDSVILN 85
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALaQRGARVVAAARNAA-ALDRLAGETGCEPLRL--DVG--DDAAIRAALAAAGAFDGLVNC 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   86 AG--VLEPIAKIADADineWRKLFDINFFSVVETVKYAIPHLRKT--KGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:PRK07060  85 AGiaSLESALDMTAEG---FDRVMAVNARGAALVARHVARAMIAAgrGGSIVNVSSQAALVGLPDHLAYCASKAALDAIT 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19113072  162 MNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEA 197
Cdd:PRK07060 162 RVLCVElgPHGIRVNSVNPTVTLTPMAAEAWSDPQKSG 199
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 6-184 6.27e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 86.90  E-value: 6.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSlTPELETLLIQNPDSFVH---VKGDVTEVG--KASIETAIKKFGKL 79
Cdd:PRK07109   8 RQVVVITGASAGVGRATARAFARRgAKVVLLARG-EEGLEALAAEIRAAGGEalaVVADVADAEavQAAADRAEEELGPI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLR-KTKGTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:PRK07109  87 DTWVNNAMV-TVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRpRDRGAIIQVGSALAYRSIPLQSAYCAAKHAIR 165

                        170       180       190
                 ....*....|....*....|....*....|
gi 19113072  159 ----MLVMNLGSEEPDIMSVAVRPGVVDTP 184
Cdd:PRK07109 166 gftdSLRCELLHDGSPVSVTMVQPPAVNTP 195
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 1-239 7.95e-20

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 85.16  E-value: 7.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAV------SRSLTPELETLLIQNPDSFVHVKGDVTEVG--KASIET 71
Cdd:PRK12827   1 MASLDSRRVLITGGSGGLGRAIAVRLaADGADVIVLdihpmrGRAEADAVAAGIEAAGGKALGLAFDVRDFAatRAALDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   72 AIKKFGKLDSVILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAA 149
Cdd:PRK12827  81 GVEEFGRLDILVNNAGIA-TDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAGVRGNRGQVN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  150 YCCSKAAINMLVMNLGSEEPD--IMSVAVRPGVVDTPMqvsirndsNKEAMGGDthnFFKELKTSGQLVAPQDIAKALSF 227
Cdd:PRK12827 160 YAASKAGLIGLTKTLANELAPrgITVNAVAPGAINTPM--------ADNAAPTE---HLLNPVPVQRLGEPDEVAALVAF 228

                        250
                 ....*....|..
gi 19113072  228 LALNNNPKLTGQ 239
Cdd:PRK12827 229 LVSDAASYVTGQ 240
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 6-241 8.62e-20

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 85.26  E-value: 8.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   6 EKVILLTGSSKGIGLATAEALQKKAKVIAV----SRSLTPELETLLIQNPDSFV-HVKGDVTEVG--KASIETAIKKFGK 78
Cdd:cd05330   3 DKVVLITGGGSGLGLATAVRLAKEGAKLSLvdlnEEGLEAAKAALLEIAPDAEVlLIKADVSDEAqvEAYVDATVEQFGR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  79 LDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:cd05330  83 IDGFFNNAGIEGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGsGMIVNTASVGGIRGVGNQSGYAAAKHGV 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPM-QVSIR--NDSNKEAMGGDthnfFKELKTSGQLVAPQDIAKALSFLALNN 232
Cdd:cd05330 163 VGLTRNSAVEygQYGIRINAIAPGAILTPMvEGSLKqlGPENPEEAGEE----FVSVNPMKRFGEPEEVAAVVAFLLSDD 238


                ....*....
gi 19113072 233 NPKLTGQFV 241
Cdd:cd05330 239 AGYVNAAVV 247
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 7-185 8.71e-20

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 85.39  E-value: 8.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSlTPELETLLIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLDSVI 83
Cdd:PRK06200   7 QVALITGGGSGIGRALVERfLAEGARVAVLERS-AEKLASLRQRFGDHVLVVEGDVTsyADNQRAVDQTVDAFGKLDCFV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAGVLE---PIAKIADADINE-WRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:PRK06200  86 GNAGIWDyntSLVDIPAETLDTaFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPGGGGPLYTASKHAVVG 165

                        170       180
                 ....*....|....*....|....*..
gi 19113072  160 LVMNLGSE-EPDIMSVAVRPGVVDTPM 185
Cdd:PRK06200 166 LVRQLAYElAPKIRVNGVAPGGTVTDL 192
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 6-238 9.29e-20

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 85.16  E-value: 9.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPELETL---LIQNPDSFVHVKGDVT-EVG-KASIETAIKKFGKL 79
Cdd:PRK08936   7 GKVVVITGGSTGLGRAMAVRFgKEKAKVVINYRSDEEEANDVaeeIKKAGGEAIAVKGDVTvESDvVNLIQTAVKEFGTL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVLEPIAKiADADINEWRKLFDIN----FFSVVETVKYAIPHlrKTKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK08936  87 DVMINNAGIENAVPS-HEMSLEDWNKVINTNltgaFLGSREAIKYFVEH--DIKGNIINMSSVHEQIPWPLFVHYAASKG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  156 AINMLVMNLGSE-EPDIMSV-AVRPGVVDTPMQVSIRNDSNKEAmggDThnffKELKTSGQLVAPQDIAKALSFLALNNN 233
Cdd:PRK08936 164 GVKLMTETLAMEyAPKGIRVnNIGPGAINTPINAEKFADPKQRA---DV----ESMIPMGYIGKPEEIAAVAAWLASSEA 236


                 ....*
gi 19113072  234 PKLTG 238
Cdd:PRK08936 237 SYVTG 241
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-185 1.00e-19

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 85.08  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSLTPELETLLIQNPDSFVhVKGDVTEvgKASIETAIK----K 75
Cdd:PRK07067   1 MMRLQGKVALLTGAASGIGEAVAERyLAEGARVVIADIKPARARLAALEIGPAAIA-VSLDVTR--QDSIDRIVAaaveR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGV--LEPIAKIADADineWRKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSSGAAVRVFPAWAAYC 151
Cdd:PRK07067  78 FGGIDILFNNAALfdMAPILDISRDS---YDRLFAVNVKGLFFLMQAVARHMveQGRGGKIINMASQAGRRGEALVSHYC 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19113072  152 CSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPM 185
Cdd:PRK07067 155 ATKAAVISYTQSAALAliRHGINVNAIAPGVVDTPM 190
PRK07069 PRK07069
short chain dehydrogenase; Validated
 10-238 1.96e-19

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 84.38  E-value: 1.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEAL-QKKAKVI-------AVSRSLTPELETLL-IQNPDSFVHvkgDVTEVG--KASIETAIKKFGK 78
Cdd:PRK07069   3 FITGAAGGLGRAIARRMaEQGAKVFltdindaAGLDAFAAEINAAHgEGVAFAAVQ---DVTDEAqwQALLAQAADAMGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:PRK07069  80 LSVLVNNAGV-GSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAAFKAEPDYTAYNASKAAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  158 NML----VMNLGSEEPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMggdthnfFKELKTS---GQLVAPQDIAKALSFLAL 230
Cdd:PRK07069 159 ASLtksiALDCARRGLDVRCNSIHPTFIRTGIVDPIFQRLGEEEA-------TRKLARGvplGRLGEPDDVAHAVLYLAS 231


                 ....*...
gi 19113072  231 NNNPKLTG 238
Cdd:PRK07069 232 DESRFVTG 239
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 7-242 2.24e-19

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: 83.53  E-value: 2.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQ-KKAKVIAVSRSLTPELETLLIQNPDSfvhvkgDVTEVGKASIETAIKKFGKLDSVILN 85
Cdd:cd05334   2 RVVLVYGGRGALGSAVVQAFKsRGWWVASIDLAENEEADASIIVLDSD------SFTEQAKQVVASVARLSGKVDALICV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  86 AGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTkGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMNLG 165
Cdd:cd05334  76 AGGWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSG-GLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 166 SE----EPDIMSVAVRPGVVDTPMqvsirndsNKEAMGgdTHNFfkelktsGQLVAPQDIAKALSFLALNNNPKLTGQFV 241
Cdd:cd05334 155 AEnsglPAGSTANAILPVTLDTPA--------NRKAMP--DADF-------SSWTPLEFIAELILFWASGAARPKSGSLI 217


                .
gi 19113072 242 E 242
Cdd:cd05334 218 P 218
PRK09072 PRK09072
SDR family oxidoreductase;
6-225 2.25e-19

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 84.22  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPeLETLL--IQNPDSFVHVKGDVT-EVGKASIETAIKKFGKLDS 81
Cdd:PRK09072   5 DKRVLLTGASGGIGQALAEALAAAgARLLLVGRNAEK-LEALAarLPYPGRHRWVVADLTsEAGREAVLARAREMGGINV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK-TKGTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK09072  84 LINNAGVNH-FALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAqPSAMVVNVGSTFGSIGYPGYASYCASKFALRGF 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113072  161 vmnlgSEepdimsvAVRPGVVDTPMQV------SIRNDSNKEAMggDTHNffKELKTSGQlvAPQDIAKAL 225
Cdd:PRK09072 163 -----SE-------ALRRELADTGVRVlylaprATRTAMNSEAV--QALN--RALGNAMD--DPEDVAAAV 215
PRK08264 PRK08264
SDR family oxidoreductase;
1-185 3.31e-19

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 83.40  E-value: 3.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK--AKVIAVSRsltpELETLLIQNPDsFVHVKGDVTEvgKASIETAIKKFGK 78
Cdd:PRK08264   1 MMDIKGKVVLVTGANRGIGRAFVEQLLARgaAKVYAAAR----DPESVTDLGPR-VVPLQLDVTD--PASVAAAAEAASD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:PRK08264  74 VTILVNNAGIFRTGSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANgGGAIVNVLSVLSWVNFPNLGTYSASKAAA 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 19113072  158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPM 185
Cdd:PRK08264 154 WSLTQALRAElaPQGTRVLGVHPGPIDTDM 183
PRK06914 PRK06914
SDR family oxidoreductase;
7-236 5.32e-19

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 83.53  E-value: 5.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKA-KVIAVSRSL--TPELETLLIQ-NPDSFVHVKG-DVTEvgKASIET---AIKKFGK 78
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGyLVIATMRNPekQENLLSQATQlNLQQNIKVQQlDVTD--QNSIHNfqlVLKEIGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAG-----VLEPIAkiadadINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCC 152
Cdd:PRK06914  82 IDLLVNNAGyanggFVEEIP------VEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISGRVGFPGLSPYVS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  153 SKAAIN-------MLVMNLGseepdIMSVAVRPGVVDTPM-QVSIRNDSNKEAMGGDTHNFFKEL--------KTSGqlv 216
Cdd:PRK06914 156 SKYALEgfseslrLELKPFG-----IDVALIEPGSYNTNIwEVGKQLAENQSETTSPYKEYMKKIqkhinsgsDTFG--- 227

                        250       260
                 ....*....|....*....|
gi 19113072  217 APQDIAKALSFLALNNNPKL 236
Cdd:PRK06914 228 NPIDVANLIVEIAESKRPKL 247
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 4-157 6.12e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 83.03  E-value: 6.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    4 TAEKVILLTGSSKGIGLATAEALQKKA-KVIAVSRSLTPEletlliQNPDSFVHVKGDVTEvgKASIETAIK----KFGK 78
Cdd:PRK06179   2 SNSKVALVTGASSGIGRATAEKLARAGyRVFGTSRNPARA------APIPGVELLELDVTD--DASVQAAVDeviaRAGR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:PRK06179  74 IDVLVNNAGV-GLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVLGFLPAPYMALYAASKHAV 152
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 6-239 6.31e-19

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: 82.90  E-value: 6.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   6 EKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQ-------NPDSFvhvKGDVTEVG--KASIETAIKKF 76
Cdd:cd05337   1 RPVAIVTGASRGIGRAIATELAARGFDIAINDLPDDDQATEVVAevlaagrRAIYF---QADIGELSdhEALLDQAWEDF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  77 GKLDSVILNAGVLEPIAK-IADADINEWRKLFDIN----FF-------SVVETVK-YAIPHlrktkGTIVIVSSGAAVRV 143
Cdd:cd05337  78 GRLDCLVNNAGIAVRPRGdLLDLTEDSFDRLIAINlrgpFFltqavarRMVEQPDrFDGPH-----RSIIFVTSINAYLV 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 144 FPAWAAYCCSKAAINMLV----MNLGSEEpdIMSVAVRPGVVDTpmqvsirndsnkeAMGGDTHNFFKELKTSGQLV--- 216
Cdd:cd05337 153 SPNRGEYCISKAGLSMATrllaYRLADEG--IAVHEIRPGLIHT-------------DMTAPVKEKYDELIAAGLVPirr 217

                       250       260
                ....*....|....*....|....*
gi 19113072 217 --APQDIAKALSFLALNNNPKLTGQ 239
Cdd:cd05337 218 wgQPEDIAKAVRTLASGLLPYSTGQ 242
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 1-243 2.04e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 81.59  E-value: 2.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK--AKVIAVSRS------LTPELETLLIQnpdsFVHVKGDVTEVG--KASIE 70
Cdd:PRK06198   1 MGRLDGKVALVTGGTQGLGAAIARAFAERgaAGLVICGRNaekgeaQAAELEALGAK----AVFVQADLSDVEdcRRVVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   71 TAIKKFGKLDSVIlNAGVLEPIAKIADADINEWRKLFDIN----FFSVVETVKYAIPhlRKTKGTIVIVSSGAAVRVFPA 146
Cdd:PRK06198  77 AADEAFGRLDALV-NAAGLTDRGTILDTSPELFDRHFAVNvrapFFLMQEAIKLMRR--RKAEGTIVNIGSMSAHGGQPF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  147 WAAYCCSKAAINMLVMNLG-SEEPDIMSV-AVRPGVVDTPMQVSIRndsnKEAMGGDTHNFFKELKTS--GQLVAPQDIA 222
Cdd:PRK06198 154 LAAYCASKGALATLTRNAAyALLRNRIRVnGLNIGWMATEGEDRIQ----REFHGAPDDWLEKAAATQpfGRLLDPDEVA 229

                        250       260
                 ....*....|....*....|.
gi 19113072  223 KALSFLALNNNPKLTGQFVEW 243
Cdd:PRK06198 230 RAVAFLLSDESGLMTGSVIDF 250
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 7-239 3.65e-18

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 81.23  E-value: 3.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAV------------SRSLTPE-LETLLIqnpdsfvhvKGDVTEVG--KASIET 71
Cdd:PRK06701  47 KVALITGGDSGIGRAVAVLFAKEGADIAIvyldehedanetKQRVEKEgVKCLLI---------PGDVSDEAfcKDAVEE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   72 AIKKFGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLrKTKGTIVIVSSGAAVRVFPAWAAYC 151
Cdd:PRK06701 118 TVRELGRLDILVNNAAFQYPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL-KQGSAIINTGSITGYEGNETLIDYS 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  152 CSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHnffkeLKTSGQlvaPQDIAKALSFLA 229
Cdd:PRK06701 197 ATKGAIHAFTRSLAQSlvQKGIRVNAVAPGPIWTPLIPSDFDEEKVSQFGSNTP-----MQRPGQ---PEELAPAYVFLA 268

                        250
                 ....*....|
gi 19113072  230 LNNNPKLTGQ 239
Cdd:PRK06701 269 SPDSSYITGQ 278
PRK08267 PRK08267
SDR family oxidoreductase;
7-224 4.17e-18

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 80.75  E-value: 4.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHV-KGDVTEvgKASIETAIKKF-----GKLD 80
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAGNAWTgALDVTD--RAAWDAALADFaaatgGRLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLE--PIAKIADADInewRKLFDINFFSVVETVKYAIPHLRKTKGTIVI-VSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:PRK08267  80 VLFNNAGILRggPFEDIPLEAH---DRVIDINVKGVLNGAHAALPYLKATPGARVInTSSASAIYGQPGLAVYSATKFAV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072  158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPMqvsIRNDSNKEAMGgdthnffkELKTSGQLVAPQDIAKA 224
Cdd:PRK08267 157 RGLTEALDLEwrRHGIRVADVMPLFVDTAM---LDGTSNEVDAG--------STKRLGVRLTPEDVAEA 214
PRK08628 PRK08628
SDR family oxidoreductase;
6-160 5.87e-18

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 80.39  E-value: 5.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSKGIGLATAEALQKKAKV-IAVSRS-LTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDS 81
Cdd:PRK08628   7 DKVVIVTGGASGIGAAISLRLAEEGAIpVIFGRSaPDDEFAEELRALQPRAEFVQVDLTDDAqcRDAVEQTVAKFGRIDG 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072   82 VILNAGVLEPIAkiADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK08628  87 LVNNAGVNDGVG--LEAGREAFVASLERNLIHYYVMAHYCLPHLKASRGAIVNISSKTALTGQGGTSGYAAAKGAQLAL 163
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 5-167 7.57e-18

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 80.00  E-value: 7.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATA-EALQKKAKVIAVSRSLT--PELETLLIQNPDSFVHVKGDVTEVGKAS--IETAIKKFGKL 79
Cdd:PRK07890   4 KGKVVVVSGVGPGLGRTLAvRAARAGADVVLAARTAErlDEVAAEIDDLGRRALAVPTDITDEDQCAnlVALALERFGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:PRK07890  84 DALVNNAFRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESGGSIVMINSMVLRHSQPKYGAYKMAKGALLA 163


                 ....*...
gi 19113072  160 LVMNLGSE 167
Cdd:PRK07890 164 ASQSLATE 171
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 6-239 7.96e-18

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: 80.01  E-value: 7.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   6 EKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSltpeLETL------LIQNPDSFVHVKGDVT--EVGKASIETAIKKF 76
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALAREgARVAICARN----RENLeraaseLRAGGAGVLAVVADLTdpEDIDRLVEKAGDAF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  77 GKLDSVILNAG--VLEPIAKIADADineWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCS 153
Cdd:cd05344  77 GRVDILVNNAGgpPPGPFAELTDED---WLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLTVKEPEPNLVLSNVA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 154 KAAINMLVMNLGSE-EPDIMSV-AVRPGVVDTPmQVsIRNDSNKEAMGGDTHNFFKELKTS----GQLVAPQDIAKALSF 227
Cdd:cd05344 154 RAGLIGLVKTLSRElAPDGVTVnSVLPGYIDTE-RV-RRLLEARAEKEGISVEEAEKEVASqiplGRVGKPEELAALIAF 231

                       250
                ....*....|..
gi 19113072 228 LALNNNPKLTGQ 239
Cdd:cd05344 232 LASEKASYITGQ 243
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 3-229 9.14e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 79.95  E-value: 9.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    3 ETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELetlliqnPDSFVHVKGDVT--EVGKASIETAIKKFGKL 79
Cdd:PRK06523   6 ELAGKRALVTGGTKGIGAATVARLLEAgARVVTTARSRPDDL-------PEGVEFVAADLTtaEGCAAVARAVLERLGGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVLEP----IAKIADAdinEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSgaAVRVFP---AWAAYC 151
Cdd:PRK06523  79 DILVHVLGGSSApaggFAALTDE---EWQDELNLNLLAAVRLDRALLPGMIARgSGVIIHVTS--IQRRLPlpeSTTAYA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  152 CSKAAINMLVMNLGSE-EPD-IMSVAVRPGVVDTPMQVSIRNDSnKEAMGGDTHNFFKELKTS------GQLVAPQDIAK 223
Cdd:PRK06523 154 AAKAALSTYSKSLSKEvAPKgVRVNTVSPGWIETEAAVALAERL-AEAAGTDYEGAKQIIMDSlggiplGRPAEPEEVAE 232


                 ....*.
gi 19113072  224 ALSFLA 229
Cdd:PRK06523 233 LIAFLA 238
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 7-229 9.72e-18

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 79.70  E-value: 9.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPE--LETLLIQNPDSFVhvkGDVTEVG--KASIETAIKKFGKLDS 81
Cdd:PRK06841  16 KVAVVTGGASGIGHAIAELFaAKGARVALLDRSEDVAevAAQLLGGNAKGLV---CDVSDSQsvEAAVAAVISAFGRIDI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAI--- 157
Cdd:PRK06841  93 LVNSAGVA-LLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAgGGKIVNLASQAGVVALERHVAYCASKAGVvgm 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113072  158 -NMLVMNLGseEPDIMSVAVRPGVVDTPMqvsirndsNKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLA 229
Cdd:PRK06841 172 tKVLALEWG--PYGITVNAISPTVVLTEL--------GKKAWAGEKGERAKKLIPAGRFAYPEEIAAAALFLA 234
PRK05693 PRK05693
SDR family oxidoreductase;
7-183 1.15e-17

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 79.83  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKA-KVIAVSRSLTpELETLLIQnpdSFVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:PRK05693   2 PVVLITGCSSGIGRALADAFKAAGyEVWATARKAE-DVEALAAA---GFTAVQLDVNDGAalARLAEELEAEHGGLDVLI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAG--VLEPIAkiaDADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:PRK05693  78 NNAGygAMGPLL---DGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAGAYCASKAAVHALS 154

                        170       180
                 ....*....|....*....|....
gi 19113072  162 MNLGSE-EP-DIMSVAVRPGVVDT 183
Cdd:PRK05693 155 DALRLElAPfGVQVMEVQPGAIAS 178
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 7-191 2.18e-17

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 78.12  E-value: 2.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSltPE-LETLLIQNPDsfvhVKGDVTEVGKAS-----IETAIKKFGKL 79
Cdd:cd05370   6 NTVLITGGTSGIGLALARKFlEAGNTVIITGRR--EErLAEAKKELPN----IHTIVLDVGDAEsvealAEALLSEYPNL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  80 DSVILNAGVLEPI--------AKIADADInewrklfDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAY 150
Cdd:cd05370  80 DILINNAGIQRPIdlrdpasdLDKADTEI-------DTNLIGPIRLIKAFLPHLkKQPEATIVNVSSGLAFVPMAANPVY 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19113072 151 CCSKAAINMLVMNLGS--EEPDIMSVAVRPGVVDTPMQVSIRN 191
Cdd:cd05370 153 CATKAALHSYTLALRHqlKDTGVEVVEIVPPAVDTELHEERRN 195
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 7-186 2.72e-17

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 78.81  E-value: 2.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLT---PELETLLIQNPDSFVHV-KGDVTEVgkASIETA----IKKFG 77
Cdd:cd05327   2 KVVVITGANSGIGKETARELaKRGAHVIIACRNEEkgeEAAAEIKKETGNAKVEViQLDLSSL--ASVRQFaeefLARFP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  78 KLDSVILNAGVLEPIAKIADADINewrKLFDINFFSVVETVKYAIPHLRKTKGT-IVIVSSGAAVRV------------- 143
Cdd:cd05327  80 RLDILINNAGIMAPPRRLTKDGFE---LQFAVNYLGHFLLTNLLLPVLKASAPSrIVNVSSIAHRAGpidfndldlennk 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 19113072 144 -FPAWAAYCCSKAAiNMLVMNLGSEE---PDIMSVAVRPGVVDTPMQ 186
Cdd:cd05327 157 eYSPYKAYGQSKLA-NILFTRELARRlegTGVTVNALHPGVVRTELL 202
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 1-239 2.87e-17

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 78.40  E-value: 2.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKKAKVIAVS----RSLTPELETLLIQNPDSfVHVKGDVT---EVGkASIETAI 73
Cdd:PRK13394   2 MSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIAdlnqDGANAVADEINKAGGKA-IGVAMDVTnedAVN-AGIDKVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   74 KKFGKLDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAAYC 151
Cdd:PRK13394  80 ERFGSVDILVSNAGI-QIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHSHEASPLKSAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  152 CSKAAINML--VMNLGSEEPDIMSVAVRPGVVDTPM-QVSI----------RNDSNKEAMGGDThnffkelkTSGQLVAP 218
Cdd:PRK13394 159 TAKHGLLGLarVLAKEGAKHNVRSHVVCPGFVRTPLvDKQIpeqakelgisEEEVVKKVMLGKT--------VDGVFTTV 230

                        250       260
                 ....*....|....*....|.
gi 19113072  219 QDIAKALSFLALNNNPKLTGQ 239
Cdd:PRK13394 231 EDVAQTVLFLSSFPSAALTGQ 251
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 7-225 5.05e-17

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: 77.11  E-value: 5.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQ-NPDSFVHVKGDVTEvgKASIETAIKKF-----GKLD 80
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAElGAENVVAGALDVTD--RAAWAAALADFaaatgGRLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLE--PIAKIADADInewRKLFDINFFSVVETVKYAIPHLRKTKGTIVI-VSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:cd08931  79 ALFNNAGVGRggPFEDVPLAAH---DRMVDINVKGVLNGAYAALPYLKATPGARVInTASSSAIYGQPDLAVYSATKFAV 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPMqvsirndsnkeAMGGDTHNFFKelKTSGQLVAPQDIAKAL 225
Cdd:cd08931 156 RGLTEALDVEwaRHGIRVADVWPWFVDTPI-----------LTKGETGAAPK--KGLGRVLPVSDVAKVV 212
PRK07856 PRK07856
SDR family oxidoreductase;
7-229 5.13e-17

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 77.67  E-value: 5.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSLTPELEtlliqnPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:PRK07856   7 RVVLVTGGTRGIGAGIARAfLAAGATVVVCGRRAPETVD------GRPAEFHAADVRDPDqvAALVDAIVERHGRLDVLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK--TKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:PRK07856  81 NNAGG-SPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQqpGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNLT 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113072  162 MNLGSE-EPDIMSVAVRPGVVDTpmqvsirndSNKEAMGGDTHNFFKELKT--SGQLVAPQDIAKALSFLA 229
Cdd:PRK07856 160 RSLAVEwAPKVRVNAVVVGLVRT---------EQSELHYGDAEGIAAVAATvpLGRLATPADIAWACLFLA 221
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 1-234 9.27e-17

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: 76.78  E-value: 9.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTpELETLLIQ----NPDSFVHVKGDVT-EVGKASIETAIK 74
Cdd:cd05343   1 MERWRGRVALVTGASVGIGAAVARALvQHGMKVVGCARRVD-KIEALAAEcqsaGYPTLFPYQCDLSnEEQILSMFSAIR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  75 -KFGKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK---GTIVIVSSGAAVRVFPAWAA- 149
Cdd:cd05343  80 tQHQGVDVCINNAGLARP-EPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvddGHIININSMSGHRVPPVSVFh 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 150 -YCCSKAAINMLVMNLGSE----EPDIMSVAVRPGVVDTpmQVSIRNDSNKEAMGGDTHNFFKELKtsgqlvaPQDIAKA 224
Cdd:cd05343 159 fYAATKHAVTALTEGLRQElreaKTHIRATSISPGLVET--EFAFKLHDNDPEKAAATYESIPCLK-------PEDVANA 229

                       250
                ....*....|
gi 19113072 225 LsFLALNNNP 234
Cdd:cd05343 230 V-LYVLSTPP 238
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 8-229 1.07e-16

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: 76.45  E-value: 1.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETL---LIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSV 82
Cdd:cd05365   1 VAIVTGGAAGIGKAIAGTLAKAGASVVIADLKSEGAEAVaaaIQQAGGQAIGLECNVTSEQdlEAVVKATVSQFGGITIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  83 ILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:cd05365  81 VNNAGGGGPKPFDMPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGgGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 162 MNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDThnffkelkTSGQLVAPQDIAKALSFLA 229
Cdd:cd05365 161 RNLAFDlgPKGIRVNAVAPGAVKTDALASVLTPEIERAMLKHT--------PLGRLGEPEDIANAALFLC 222
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 7-229 1.27e-16

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: 76.55  E-value: 1.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSLT--PELETLLIQNPDSFVH-VKGDVTEvgKASIETAI----KKFGK 78
Cdd:cd05346   1 KTVLITGASSGIGEATARRfAKAGAKLILTGRRAErlQELADELGAKFPVKVLpLQLDVSD--RESIEAALenlpEEFRD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  79 LDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:cd05346  79 IDILVNNAGLALGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMiARNQGHIINLGSIAGRYPYAGGNVYCATKAAV 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113072 158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPMQ-VSIRNDSNKEAmggdthNFFKELktsgQLVAPQDIAKALSFLA 229
Cdd:cd05346 159 RQFSLNLRKDliGTGIRVTNIEPGLVETEFSlVRFHGDKEKAD------KVYEGV----EPLTPEDIAETILWVA 223
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 7-238 1.29e-16

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 76.62  E-value: 1.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSltPELETLLIQN-PDSFVHVKGDVT--EVGKASIETAIKKFGKLDSV 82
Cdd:cd05348   5 EVALITGGGSGLGRALVERfVAEGAKVAVLDRS--AEKVAELRADfGDAVVGVEGDVRslADNERAVARCVERFGKLDCF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  83 ILNAGVLEPIAKIADAdinEWRKL-------FDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:cd05348  83 IGNAGIWDYSTSLVDI---PEEKLdeafdelFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPGGGGPLYTASKH 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 156 AINMLVMNLGSE-EPDIMSVAVRPGVVDTPMQ--VSIRNDSNKEAMGGdTHNFFKELKTSGQLVAPQDIAKALSFLAL-N 231
Cdd:cd05348 160 AVVGLVKQLAYElAPHIRVNGVAPGGMVTDLRgpASLGQGETSISTPP-LDDMLKSILPLGFAPEPEDYTGAYVFLASrG 238


                ....*..
gi 19113072 232 NNPKLTG 238
Cdd:cd05348 239 DNRPATG 245
PRK06123 PRK06123
SDR family oxidoreductase;
5-242 2.00e-16

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 75.97  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKKAKVIAVS----RSLTPELETLLIQNPDSFVHVKGDVTEVGK--ASIETAIKKFGK 78
Cdd:PRK06123   1 MRKVMIITGASRGIGAATALLAAERGYAVCLNylrnRDAAEAVVQAIRRQGGEALAVAADVADEADvlRLFEAVDRELGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVLEPIAKIADADINEWRKLFDIN----FFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPA-WAAYCCS 153
Cdd:PRK06123  81 LDALVNNAGILEAQMRLEQMDAARLTRIFATNvvgsFLCAREAVKRMSTRHGGRGGAIVNVSSMAARLGSPGeYIDYAAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  154 KAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDThnffkELKTSGQlvaPQDIAKALSFLALN 231
Cdd:PRK06123 161 KGAIDTMTIGLAKEvaAEGIRVNAVRPGVIYTEIHASGGEPGRVDRVKAGI-----PMGRGGT---AEEVARAILWLLSD 232

                        250
                 ....*....|.
gi 19113072  232 NNPKLTGQFVE 242
Cdd:PRK06123 233 EASYTTGTFID 243
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-198 4.17e-16

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 74.73  E-value: 4.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKKA-KVIAVSRS------LTPELETLLIQNPDSFVHVKgDVTEVgKASIETAI 73
Cdd:PRK07666   2 AQSLQGKNALITGAGRGIGRAVAIALAKEGvNVGLLARTeenlkaVAEEVEAYGVKVVIATADVS-DYEEV-TAAIEQLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   74 KKFGKLDSVILNAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCC 152
Cdd:PRK07666  80 NELGSIDILINNAGISK-FGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMiERQSGDIINISSTAGQKGAAVTSAYSA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19113072  153 SKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIR-NDSNKEAM 198
Cdd:PRK07666 159 SKFGVLGLTESLMQEvrKHNIRVTALTPSTVATDMAVDLGlTDGNPDKV 207
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 5-239 5.88e-16

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 74.61  E-value: 5.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKKAKVIAV-SRSLTPELETL---LIQNPDSFVHVKGDVTEVG--KASIETAIKKFGK 78
Cdd:PRK12745   1 MRPVALVTGGRRGIGLGIARALAAAGFDLAInDRPDDEELAATqqeLRALGVEVIFFPADVADLSahEAMLDAAQAAWGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVlEPI--AKIADADINEWRKLFDIN-----FFS-VVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAA 149
Cdd:PRK12745  81 IDCLVNNAGV-GVKvrGDLLDLTPESFDRVLAINlrgpfFLTqAVAKRMLAQPEPEELPhRSIVFVSSVNAIMVSPNRGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  150 YCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDThnffkELKTSGQlvaPQDIAKALSF 227
Cdd:PRK12745 160 YCISKAGLSMAAQLFAARlaEEGIGVYEVRPGLIKTDMTAPVTAKYDALIAKGLV-----PMPRWGE---PEDVARAVAA 231

                        250
                 ....*....|..
gi 19113072  228 LALNNNPKLTGQ 239
Cdd:PRK12745 232 LASGDLPYSTGQ 243
PRK06484 PRK06484
short chain dehydrogenase; Validated
 3-229 6.39e-16

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 76.43  E-value: 6.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    3 ETAEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEvgKASIETAI----KKFGK 78
Cdd:PRK06484   2 KAQSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSD--EAQIREGFeqlhREFGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVLEPIAK-IADADINEWRKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK06484  80 IDVLVNNAGVTDPTMTaTLDTTLEEFARLQAINLTGAYLVAREALRLMIEQGhgAAIVNVASGAGLVALPKRTAYSASKA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113072  156 AINMLVMNLGSE--EPDIMSVAVRPGVVDTPMqVSIRNDSNKEamggDTHNFFKELKTsGQLVAPQDIAKALSFLA 229
Cdd:PRK06484 160 AVISLTRSLACEwaAKGIRVNAVLPGYVRTQM-VAELERAGKL----DPSAVRSRIPL-GRLGRPEEIAEAVFFLA 229
PRK06182 PRK06182
short chain dehydrogenase; Validated
 4-235 9.32e-16

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 74.61  E-value: 9.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    4 TAEKVILLTGSSKGIGLATAEALQKKA-KVIAVSRSLTpELETLliqnPDSFVHV-KGDVT--EVGKASIETAIKKFGKL 79
Cdd:PRK06182   1 MQKKVALVTGASSGIGKATARRLAAQGyTVYGAARRVD-KMEDL----ASLGVHPlSLDVTdeASIKAAVDTIIAEEGRI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGvLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSS--GAAVRVFPAWaaYCCSKAA 156
Cdd:PRK06182  76 DVLVNNAG-YGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSmgGKIYTPLGAW--YHATKFA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  157 I----NMLVMNLgsEEPDIMSVAVRPGVVDTP----MQVSIRNDSNKEAMGGDTHNFFKELK---TSGQLVAPQDIAKAL 225
Cdd:PRK06182 153 LegfsDALRLEV--APFGIDVVVIEPGGIKTEwgdiAADHLLKTSGNGAYAEQAQAVAASMRstyGSGRLSDPSVIADAI 230

                        250
                 ....*....|
gi 19113072  226 SFLALNNNPK 235
Cdd:PRK06182 231 SKAVTARRPK 240
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 7-184 1.06e-15

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 73.97  E-value: 1.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLT----PELETLL--IQNPDSFVHVKG-----------DVTEVgKAS 68
Cdd:cd05338   4 KVAFVTGASRGIGRAIALRLAKAgATVVVAAKTASegdnGSAKSLPgtIEETAEEIEAAGgqalpivvdvrDEDQV-RAL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  69 IETAIKKFGKLDSVILNAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAW 147
Cdd:cd05338  83 VEATVDQFGRLDILVNNAGAIW-LSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAgQGHILNISPPLSLRPARGD 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19113072 148 AAYCCSKAAINMLVMNLGSE--EPDIMSVAVRPG-VVDTP 184
Cdd:cd05338 162 VAYAAGKAGMSRLTLGLAAElrRHGIAVNSLWPStAIETP 201
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 7-160 1.09e-15

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: 74.24  E-value: 1.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKKA-KVIA------------VSRSLTPELETLL--IQNPDSFV----HVKGDVTEVGka 67
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGfTVLAgcltkngpgakeLRRVCSDRLRTLQldVTKPEQIKraaqWVKEHVGEKG-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  68 sietaikkfgkLDSVILNAGVLEPIAkiadadINEW------RKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAV 141
Cdd:cd09805  79 -----------LWGLVNNAGILGFGG------DEELlpmddyRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVSSMGGR 141

                       170
                ....*....|....*....
gi 19113072 142 RVFPAWAAYCCSKAAINML 160
Cdd:cd09805 142 VPFPAGGAYCASKAAVEAF 160
PRK07985 PRK07985
SDR family oxidoreductase;
10-239 1.23e-15

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 74.65  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEALQKKAKVIAVS-----RSLTPELETLLIQNPDSFVHVKGDVTE--VGKASIETAIKKFGKLDSV 82
Cdd:PRK07985  53 LVTGGDSGIGRAAAIAYAREGADVAISylpveEEDAQDVKKIIEECGRKAVLLPGDLSDekFARSLVHEAHKALGGLDIM 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   83 ILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKtKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVM 162
Cdd:PRK07985 133 ALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPK-GASIITTSSIQAYQPSPHLLDYAATKAAILNYSR 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  163 NLGSE--EPDIMSVAVRPGVVDTPMQVSirndsnkeamGGDTHNFFKE------LKTSGQlvaPQDIAKALSFLALNNNP 234
Cdd:PRK07985 212 GLAKQvaEKGIRVNIVAPGPIWTALQIS----------GGQTQDKIPQfgqqtpMKRAGQ---PAELAPVYVYLASQESS 278


                 ....*
gi 19113072  235 KLTGQ 239
Cdd:PRK07985 279 YVTAE 283
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 5-189 2.04e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 73.68  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRS---LTPELETLLIQNPDSFVHVK-GDVT---EVGKAsIETAIKKF 76
Cdd:PRK05875   6 QDRTYLVTGGGSGIGKGVAAGLvAAGAAVMIVGRNpdkLAAAAEEIEALKGAGAVRYEpADVTdedQVARA-VDAATAWH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   77 GKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK05875  85 GRLHGVVHCAGGSETIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELvRGGGGSFVGISSIAASNTHRWFGAYGVTKS 164

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19113072  156 AINMLVMnLGSEEPDIMSV---AVRPGVVDTPMQVSI 189
Cdd:PRK05875 165 AVDHLMK-LAADELGPSWVrvnSIRPGLIRTDLVAPI 200
PRK07024 PRK07024
SDR family oxidoreductase;
9-185 2.83e-15

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 73.04  E-value: 2.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    9 ILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSF-VHVKG-DVTEVgkASIETA----IKKFGKLDSV 82
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKAArVSVYAaDVRDA--DALAAAaadfIAAHGLPDVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   83 ILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVK-YAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV 161
Cdd:PRK07024  83 IANAGISVGTLTEEREDLAVFREVMDTNYFGMVATFQpFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYL 162

                        170       180
                 ....*....|....*....|....*.
gi 19113072  162 MNLGSE--EPDIMSVAVRPGVVDTPM 185
Cdd:PRK07024 163 ESLRVElrPAGVRVVTIAPGYIRTPM 188
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 8-185 2.90e-15

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: 72.66  E-value: 2.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATA-EALQKKAKVIAVSRSLTPELET--LLIQNPDSFVHVKGDVT---EVGKASiETAIKKFGKLDS 81
Cdd:cd05339   1 IVLITGGGSGIGRLLAlEFAKRGAKVVILDINEKGAEETanNVRKAGGKVHYYKCDVSkreEVYEAA-KKIKKEVGDVTI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAI--- 157
Cdd:cd05339  80 LINNAGVV-SGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNhGHIVTIASVAGLISPAGLADYCASKAAAvgf 158

                       170       180       190
                ....*....|....*....|....*....|
gi 19113072 158 -NMLVMNLGSEE-PDIMSVAVRPGVVDTPM 185
Cdd:cd05339 159 hESLRLELKAYGkPGIKTTLVCPYFINTGM 188
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 7-228 3.76e-15

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 72.57  E-value: 3.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVS--RSLTPELETLLIQNPD-SFVHVKGDVT--EVGKASIETAIKKFGKLDS 81
Cdd:PRK06113  12 KCAIITGAGAGIGKEIAITFATAGASVVVSdiNADAANHVVDEIQQLGgQAFACRCDITseQELSALADFALSKLGKVDI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGVLEPiaKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK06113  92 LVNNAGGGGP--KPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNgGGVILTITSMAAENKNINMTSYASSKAAASHL 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  161 VMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDThnffkELKTSGQlvaPQDIAKALSFL 228
Cdd:PRK06113 170 VRNMAFDlgEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHT-----PIRRLGQ---PQDIANAALFL 231
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 10-185 4.09e-15

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: 71.40  E-value: 4.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  10 LLTGSSKGIGLATAEALQKKA-KVIAVSRSLTPeletllIQNPDSFVHVKGDVTEVGKAS-IETAIKKFGKLDSVILNAG 87
Cdd:cd11730   2 LILGATGGIGRALARALAGRGwRLLLSGRDAGA------LAGLAAEVGALARPADVAAELeVWALAQELGPLDLLVYAAG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  88 VLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIvssGAAVRV--FPAWAAYCCSKAAINMLVMNLG 165
Cdd:cd11730  76 AILG-KPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVFL---GAYPELvmLPGLSAYAAAKAALEAYVEVAR 151

                       170       180
                ....*....|....*....|
gi 19113072 166 SEEPDIMSVAVRPGVVDTPM 185
Cdd:cd11730 152 KEVRGLRLTLVRPPAVDTGL 171
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 9-187 4.54e-15

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: 71.07  E-value: 4.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   9 ILLTGSSKGIGLATAEALQKK-AKVIAVSRSltpeletlliqnpDSFVHVkgDVTEvgKASIETAIKKFGKLDSVILNAG 87
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHgHEVITAGRS-------------SGDYQV--DITD--EASIKALFEKVGHFDAIVSTAG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  88 VLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKtKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMNLGSE 167
Cdd:cd11731  64 DAE-FAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLND-GGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIE 141

                       170       180
                ....*....|....*....|.
gi 19113072 168 EPDIMSV-AVRPGVVDTPMQV 187
Cdd:cd11731 142 LPRGIRInAVSPGVVEESLEA 162
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 5-199 6.57e-15

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 71.97  E-value: 6.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATA-EALQKKAKViaVSRSLTP-ELETlliqnpDSFVHVKGDVT---EVgKASIETAIKKFGKL 79
Cdd:PRK06171   8 QGKIIIVTGGSSGIGLAIVkELLANGANV--VNADIHGgDGQH------ENYQFVPTDVSsaeEV-NHTVAEIIEKFGRI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGV---------LEPIAK--IADADineWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAW 147
Cdd:PRK06171  79 DGLVNNAGIniprllvdeKDPAGKyeLNEAA---FDKMFNINQKGVFLMSQAVARQMVKQHdGVIVNMSSEAGLEGSEGQ 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19113072  148 AAYCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVD-TPMqvsiRNDSNKEAMG 199
Cdd:PRK06171 156 SCYAATKAALNSFTRSWAKElgKHNIRVVGVAPGILEaTGL----RTPEYEEALA 206
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 5-229 6.92e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 71.68  E-value: 6.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKK-AKVI------AVSRSLTPELETLliqnpdsFVHVkgDVT--EVGKASIETAIKK 75
Cdd:PRK06057   6 AGRVAVITGGGSGIGLATARRLAAEgATVVvgdidpEAGKAAADEVGGL-------FVPT--DVTdeDAVNALFDTAAET 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGVLEP-IAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSS-----GAAVrvfpAWA 148
Cdd:PRK06057  77 YGSVDIAFNNAGISPPeDDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQgKGSIINTASfvavmGSAT----SQI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  149 AYCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQvsirndsnKEAMGGDTHNFFKELK--TSGQLVAPQDIAKA 224
Cdd:PRK06057 153 SYTASKGGVLAMSRELGVQfaRQGIRVNALCPGPVNTPLL--------QELFAKDPERAARRLVhvPMGRFAEPEEIAAA 224


                 ....*
gi 19113072  225 LSFLA 229
Cdd:PRK06057 225 VAFLA 229
PRK07063 PRK07063
SDR family oxidoreductase;
1-229 8.18e-15

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 71.62  E-value: 8.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEA-LQKKAKVIAVSRS---LTPELETL-LIQNPDSFVHVKGDVTEVG--KASIETAI 73
Cdd:PRK07063   2 MNRLAGKVALVTGAAQGIGAAIARAfAREGAAVALADLDaalAERAAAAIaRDVAGARVLAVPADVTDAAsvAAAVAAAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   74 KKFGKLDSVILNAGV---LEPIAkIADADineWRKLFDINFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRVFPAWAA 149
Cdd:PRK07063  82 EAFGPLDVLVNNAGInvfADPLA-MTDED---WRRCFAVDLDGAWNGCRAVLPGmVERGRGSIVNIASTHAFKIIPGCFP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  150 YCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDS-NKEAMGGDTHnffkELKTSGQLVAPQDIAKALS 226
Cdd:PRK07063 158 YPVAKHGLLGLTRALGIEyaARNVRVNAIAPGYIETQLTEDWWNAQpDPAAARAETL----ALQPMKRIGRPEEVAMTAV 233


                 ...
gi 19113072  227 FLA 229
Cdd:PRK07063 234 FLA 236
PRK07814 PRK07814
SDR family oxidoreductase;
7-242 1.47e-14

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 70.96  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTpELETLL--IQNPDSFVH-VKGDV--TEVGKASIETAIKKFGKLD 80
Cdd:PRK07814  11 QVAVVTGAGRGLGAAIALAFaEAGADVLIAARTES-QLDEVAeqIRAAGRRAHvVAADLahPEATAGLAGQAVEAFGRLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEPIAkIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:PRK07814  90 IVVNNVGGTMPNP-LLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSggGSVINISSTMGRLAGRGFAAYGTAKAALA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  159 MLVMNLGSE-EPDIMSVAVRPGVVDT-PMQVSIRNDSNKEAMGGDThnffkELKTSGQlvaPQDIAKALSFLALNNNPKL 236
Cdd:PRK07814 169 HYTRLAALDlCPRIRVNAIAPGSILTsALEVVAANDELRAPMEKAT-----PLRRLGD---PEDIAAAAVYLASPAGSYL 240


                 ....*.
gi 19113072  237 TGQFVE 242
Cdd:PRK07814 241 TGKTLE 246
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 7-236 2.88e-14

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: 70.18  E-value: 2.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL----QKKAKVIAVSRSLTPE---LETLLIQNPDSFVHVKGDVTEvgKASIETAIK--KFG 77
Cdd:cd09806   1 TVVLITGCSSGIGLHLAVRLasdpSKRFKVYATMRDLKKKgrlWEAAGALAGGTLETLQLDVCD--SKSVAAAVErvTER 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  78 KLDSVILNAGV--LEPIAKIAdadINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:cd09806  79 HVDVLVCNAGVglLGPLEALS---EDAMASVFDVNVFGTVRMLQAFLPDMKRRGsGRILVTSSVGGLQGLPFNDVYCASK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTP-MQVSIRNDSNKEAMGGD---THNFFKE-LKTSGQLV-----APQDIA 222
Cdd:cd09806 156 FALEGLCESLAVQllPFNVHLSLIECGPVHTAfMEKVLGSPEEVLDRTADditTFHFFYQyLAHSKQVFreaaqNPEEVA 235

                       250
                ....*....|....
gi 19113072 223 KALSFLALNNNPKL 236
Cdd:cd09806 236 EVFLTAIRAPKPPL 249
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 7-239 3.25e-14

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: 69.92  E-value: 3.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQK---KAKVIAVSRSLTPELETLLiqNPDSFvHVKGDVTEVG--KASIETAIKKFGKLDS 81
Cdd:cd09761   2 KVAIVTGGGHGIGKQICLDFLEagdKVVFADIDEERGADFAEAE--GPNLF-FVHGDVADETlvKFVVYAMLEKLGRIDV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAI---- 157
Cdd:cd09761  79 LVNNAARGSK-GILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNKGRIINIASTRAFQSEPDSEAYAASKGGLvalt 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGseePDIMSVAVRPGVVDTPMQvsirndsnKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALNNNPKLT 237
Cdd:cd09761 158 HALAMSLG---PDIRVNCISPGWINTTEQ--------QEFTAAPLTQEDHAQHPAGRVGTPKDIANLVLFLCQQDAGFIT 226


                ..
gi 19113072 238 GQ 239
Cdd:cd09761 227 GE 228
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
7-239 4.49e-14

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 69.41  E-value: 4.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKA-KVIAVSRS---LTPELETLLIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLD 80
Cdd:PRK12824   3 KIALVTGAKRGIGSAIARELLNDGyRVIATYFSgndCAKDWFEEYGFTEDQVRLKELDVTdtEECAEALAEIEEEEGPVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEPIAkIADADINEWRKLFDINFFSVVETVKYAIPHLR-KTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:PRK12824  83 ILVNNAGITRDSV-FKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCeQGYGRIINISSVNGLKGQFGQTNYSAAKAGMIG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  160 LVMNLGSE--EPDIMSVAVRPGVVDTPMQvsirndsnkEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALNNNPKLT 237
Cdd:PRK12824 162 FTKALASEgaRYGITVNCIAPGYIATPMV---------EQMGPEVLQSIVNQIPMKRLGTPEEIAAAVAFLVSEAAGFIT 232


                 ..
gi 19113072  238 GQ 239
Cdd:PRK12824 233 GE 234
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 12-185 5.10e-14

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: 69.17  E-value: 5.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  12 TGSSKGIGLATAEALQKKA-KVIAVSRslTPELETLLIQNPDSFVHVKGDVTEV---GKASIETAIKKFGK-LDSVIL-- 84
Cdd:cd05356   7 TGATDGIGKAYAEELAKRGfNVILISR--TQEKLDAVAKEIEEKYGVETKTIAAdfsAGDDIYERIEKELEgLDIGILvn 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  85 NAGVLEPIA-KIADADINEWRKLFDINFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVM 162
Cdd:cd05356  85 NVGISHSIPeYFLETPEDELQDIINVNVMATLKMTRLILPGmVKRKKGAIVNISSFAGLIPTPLLATYSASKAFLDFFSR 164

                       170       180
                ....*....|....*....|....*..
gi 19113072 163 NLGSE----EPDIMSvaVRPGVVDTPM 185
Cdd:cd05356 165 ALYEEyksqGIDVQS--LLPYLVATKM 189
PLN02253 PLN02253
xanthoxin dehydrogenase
 7-229 5.33e-14

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 69.85  E-value: 5.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKV--IAVSRSLTPELETLLIQNPD-SFVHvkGDVT---EVGKAsIETAIKKFGKL 79
Cdd:PLN02253  19 KVALVTGGATGIGESIVRLFHKHgAKVciVDLQDDLGQNVCDSLGGEPNvCFFH--CDVTvedDVSRA-VDFTVDKFGTL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVL-EPIAKIADADINEWRKLFDINFFSVVETVKYA----IPhlrKTKGTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PLN02253  96 DIMVNNAGLTgPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAarimIP---LKKGSIVSLCSVASAIGGLGPHAYTGSK 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVS-IRNDSNKEAMGGDTHNFF-KELKTSGQLVAPQDIAKALSFLA 229
Cdd:PLN02253 173 HAVLGLTRSVAAElgKHGIRVNCVSPYAVPTALALAhLPEDERTEDALAGFRAFAgKNANLKGVELTVDDVANAVLFLA 251
PRK07774 PRK07774
SDR family oxidoreductase;
1-239 9.09e-14

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 68.62  E-value: 9.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVI----------AVSRSLTPELETLliqnpdsfVHVKGDVT--EVGKA 67
Cdd:PRK07774   1 MGRFDDKVAIVTGAAGGIGQAYAEALaREGASVVvadinaegaeRVAKQIVADGGTA--------IAVQVDVSdpDSAKA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   68 SIETAIKKFGKLDSVILNAGV-----LEPIAKIadaDINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAv 141
Cdd:PRK07774  73 MADATVSAFGGIDYLVNNAAIyggmkLDLLITV---PWDYYKKFMSVNLDGALVCTRAVYKHMAKRGgGAIVNQSSTAA- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  142 rvFPAWAAYCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTpmqvsirnDSNKEAMGGDthnFFKE------LKTSG 213
Cdd:PRK07774 149 --WLYSNFYGLAKVGLNGLTQQLARElgGMNIRVNAIAPGPIDT--------EATRTVTPKE---FVADmvkgipLSRMG 215

                        250       260
                 ....*....|....*....|....*.
gi 19113072  214 QlvaPQDIAKALSFLALNNNPKLTGQ 239
Cdd:PRK07774 216 T---PEDLVGMCLFLLSDEASWITGQ 238
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 5-239 1.27e-13

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: 67.99  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEALQKK-AKVIavsrsltpeletLLIQNPDSFVHVKGDVTEVGKAS-------IETAIKK- 75
Cdd:cd05340   3 NDRIILVTGASDGIGREAALTYARYgATVI------------LLGRNEEKLRQVADHINEEGGRQpqwfildLLTCTSEn 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  76 -----------FGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRV 143
Cdd:cd05340  71 cqqlaqriavnYPRLDGVLHNAGLLGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDaGSLVFTSSSVGRQG 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 144 FPAWAAYCCSKAAINMLVMNLgSEEPDIMSVAVR---PGVVDTPMQVSIRNDSNKEamggdthnffkelktsgQLVAPQD 220
Cdd:cd05340 151 RANWGAYAVSKFATEGL*QVL-ADEYQQRNLRVNcinPGGTRTAMRASAFPTEDPQ-----------------KLKTPAD 212

                       250
                ....*....|....*....
gi 19113072 221 IAKALSFLALNNNPKLTGQ 239
Cdd:cd05340 213 IMPLYLWLMGDDSRRKTGM 231
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 7-239 1.83e-13

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 67.94  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRS-LTPELETLLIQNPDSFVHVKGDVTEVGKAS--IETAIKKFGKLDSV 82
Cdd:cd08937   5 KVVVVTGAAQGIGRGVAERLaGEGARVLLVDRSeLVHEVLAEILAAGDAAHVHTADLETYAGAQgvVRAAVERFGRVDVL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  83 ILNAG---VLEPIAKIADADIN-EWRKlfdiNFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRVFPawAAYCCSKAAI 157
Cdd:cd08937  85 INNVGgtiWAKPYEHYEEEQIEaEIRR----SLFPTLWCCRAVLPHmLERQQGVIVNVSSIATRGIYR--IPYSAAKGGV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRN-----DSNKEAMGG--DTHNFFKELKTSGQLvapQDIAKALSFL 228
Cdd:cd08937 159 NALTASLAFEhaRDGIRVNAVAPGGTEAPPRKIPRNaapmsEQEKVWYQRivDQTLDSSLMGRYGTI---DEQVRAILFL 235

                       250
                ....*....|.
gi 19113072 229 ALNNNPKLTGQ 239
Cdd:cd08937 236 ASDEASYITGT 246
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 1-192 2.38e-13

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 67.34  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQ----NPDSFVHVKGDVTEVGKAS--IETAIK 74
Cdd:PRK12935   1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVINYNSSKEAAENLVNelgkEGHDVYAVQADVSKVEDANrlVEEAVN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNAGVLE--PIAKIADADineWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYC 151
Cdd:PRK12935  81 HFGKVDILVNNAGITRdrTFKKLNRED---WERVIDVNLSSVFNTTSAVLPYITEAEeGRIISISSIIGQAGGFGQTNYS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19113072  152 CSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRND 192
Cdd:PRK12935 158 AAKAGMLGFTKSLALElaKTNVTVNAICPGFIDTEMVAEVPEE 200
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 5-184 3.22e-13

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: 67.48  E-value: 3.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSR------SLTPELEtlliQNPDSFVHVKGDVTEvgKASIETA----I 73
Cdd:cd08935   4 KNKVAVITGGTGVLGGAMARALaQAGAKVAALGRnqekgdKVAKEIT----ALGGRAIALAADVLD--RASLERAreeiV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  74 KKFGKLDSVILNAGVLEPIAKIA-------------DADINEWRKLFDINFF-SVVETVKYAIPHLRKTKGTIVIVSSGA 139
Cdd:cd08935  78 AQFGTVDILINGAGGNHPDATTDpehyepeteqnffDLDEEGWEFVFDLNLNgSFLPSQVFGKDMLEQKGGSIINISSMN 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 19113072 140 AVRVFPAWAAYCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTP 184
Cdd:cd08935 158 AFSPLTKVPAYSAAKAAVSNFTQWLAVEfaTTGVRVNAIAPGFFVTP 204
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 7-239 4.13e-13

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: 66.71  E-value: 4.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:cd05349   1 QVVLVTGASRGLGAAIARSFAREgARVVVNYYRSTESAEAVAAEAGERAIAIQADVRDRDqvQAMIEEAKNHFGPVDTIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  84 LNAGV---LEPIAKIADADInEWRKLFD-INFF--SVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAA 156
Cdd:cd05349  81 NNALIdfpFDPDQRKTFDTI-DWEDYQQqLEGAvkGALNLLQAVLPDFKERGsGRVINIGTNLFQNPVVPYHDYTTAKAA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 157 INMLVMNLGSE--EPDIMSVAVRPGVVDTpmqvsirndsnKEAMGGDTHNFFKELKTS---GQLVAPQDIAKALSFLALN 231
Cdd:cd05349 160 LLGFTRNMAKElgPYGITVNMVSGGLLKV-----------TDASAATPKEVFDAIAQTtplGKVTTPQDIADAVLFFASP 228


                ....*...
gi 19113072 232 NNPKLTGQ 239
Cdd:cd05349 229 WARAVTGQ 236
PRK05855 PRK05855
SDR family oxidoreductase;
7-183 4.40e-13

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 68.08  E-value: 4.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETL-LIQNPDSFVHVK----GDVTEVgKASIETAIKKFGKLD 80
Cdd:PRK05855 316 KLVVVTGAGSGIGRETALAFAREgAEVVASDIDEAAAERTAeLIRAAGAVAHAYrvdvSDADAM-EAFAEWVRAEHGVPD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVlePIA-KIADADINEWRKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSSGAA---VRVFPawaAYCCSK 154
Cdd:PRK05855 395 IVVNNAGI--GMAgGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMveRGTGGHIVNVASAAAyapSRSLP---AYATSK 469

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDT 183
Cdd:PRK05855 470 AAVLMLSECLRAElaAAGIGVTAICPGFVDT 500
PRK06500 PRK06500
SDR family oxidoreductase;
1-229 5.29e-13

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 66.52  E-value: 5.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTP------EL--ETLLIQNpDSfvhvkGDVTEvGKASIET 71
Cdd:PRK06500   1 MSRLQGKTALITGGTSGIGLETARQFLAEgARVAITGRDPASleaaraELgeSALVIRA-DA-----GDVAA-QKALAQA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   72 AIKKFGKLDSVILNAGVLEpIAKIADADINEWRKLFDIN----FFsvveTVKYAIPHLrkTKGTIVIVSSGAAVRV-FPA 146
Cdd:PRK06500  74 LAEAFGRLDAVFINAGVAK-FAPLEDWDEAMFDRSFNTNvkgpYF----LIQALLPLL--ANPASIVLNGSINAHIgMPN 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  147 WAAYCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPM--QVSIrNDSNKEAMGGDthnfFKELKTSGQLVAPQDIA 222
Cdd:PRK06500 147 SSVYAASKAALLSLAKTLSGEllPRGIRVNAVSPGPVQTPLygKLGL-PEATLDAVAAQ----IQALVPLGRFGTPEEIA 221


                 ....*..
gi 19113072  223 KALSFLA 229
Cdd:PRK06500 222 KAVLYLA 228
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 1-239 5.35e-13

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 66.48  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDS---FVHVKGDVTEVgKASIETAIKKFG 77
Cdd:PRK12936   1 MFDLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERvkiFPANLSDRDEV-KALGQKAEADLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGVLEP--IAKIADADineWRKLFDINFFSVVE-TVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PRK12936  80 GVDILVNNAGITKDglFVRMSDED---WDSVLEVNLTATFRlTRELTHPMMRRRYGRIINITSVVGVTGNPGQANYCASK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIrNDSNKEAMGGDTHnfFKELKTSGQlvapqdIAKALSFLALNN 232
Cdd:PRK12936 157 AGMIGFSKSLAQEiaTRNVTVNCVAPGFIESAMTGKL-NDKQKEAIMGAIP--MKRMGTGAE------VASAVAYLASSE 227


                 ....*..
gi 19113072  233 NPKLTGQ 239
Cdd:PRK12936 228 AAYVTGQ 234
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 7-239 5.72e-13

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: 66.49  E-value: 5.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSLTPELETLLIQNPDSFVhVKGDVTEvgKASIETAI----KKFGKLDS 81
Cdd:cd05363   4 KTALITGSARGIGRAFAQAyVREGARVAIADINLEAARATAAEIGPAACA-ISLDVTD--QASIDRCVaalvDRWGSIDI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEpIAKIADADINEWRKLFDIN----FFSVVETVKYAIPHLRktKGTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:cd05363  81 LVNNAALFD-LAPIVDITRESYDRLFAINvsgtLFMMQAVARAMIAQGR--GGKIINMASQAGRRGEALVGVYCATKAAV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE--EPDIMSVAVRPGVVDTPM--QVSIRNDSNKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALNNN 233
Cdd:cd05363 158 ISLTQSAGLNliRHGINVNAIAPGVVDGEHwdGVDAKFARYENRPRGEKKRLVGEAVPFGRMGRAEDLTGMAIFLASTDA 237


                ....*.
gi 19113072 234 PKLTGQ 239
Cdd:cd05363 238 DYIVAQ 243
PRK06482 PRK06482
SDR family oxidoreductase;
7-183 1.24e-12

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 65.91  E-value: 1.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIG-LATAEALQKKAKVIAVSRSLTpELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:PRK06482   3 KTWFITGASSGFGrGMTERLLARGDRVAATVRRPD-ALDDLKARYGDRLWVLQLDVTDSAavRAVVDRAFAALGRIDVVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAG--VLEPIAKIADADInewRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK06482  82 SNAGygLFGAAEELSDAQI---RRQIDTNLIGSIQVIRAALPHLRRQGgGRIVQVSSEGGQIAYPGFSLYHATKWGIEGF 158

                        170       180
                 ....*....|....*....|....*
gi 19113072  161 VMNLGSE-EP-DIMSVAVRPGVVDT 183
Cdd:PRK06482 159 VEAVAQEvAPfGIEFTIVEPGPART 183
PRK06949 PRK06949
SDR family oxidoreductase;
7-185 1.36e-12

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 65.55  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSlTPELETLL--IQNPDSFVHVKG-DVTEVG--KASIETAIKKFGKLD 80
Cdd:PRK06949  10 KVALVTGASSGLGARFAQVLaQAGAKVVLASRR-VERLKELRaeIEAEGGAAHVVSlDVTDYQsiKAAVAHAETEAGTID 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVlEPIAKIADADINEWRKLFDIN----FFSVVETVKYAIPHLR-----KTKGTIVIVSSGAAVRVFPAWAAYC 151
Cdd:PRK06949  89 ILVNNSGV-STTQKLVDVTPADFDFVFDTNtrgaFFVAQEVAKRMIARAKgagntKPGGRIINIASVAGLRVLPQIGLYC 167

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19113072  152 CSKAA-INML-VMNLGSEEPDIMSVAVRPGVVDTPM 185
Cdd:PRK06949 168 MSKAAvVHMTrAMALEWGRHGINVNAICPGYIDTEI 203
PRK07062 PRK07062
SDR family oxidoreductase;
7-167 1.37e-12

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 65.45  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEA-LQKKAKVIAVSRS---LTPELETLLIQNPDSFVHVKG-DVTEVG--KASIETAIKKFGKL 79
Cdd:PRK07062   9 RVAVVTGGSSGIGLATVELlLEAGASVAICGRDeerLASAEARLREKFPGARLLAARcDVLDEAdvAAFAAAVEARFGGV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGvLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:PRK07062  89 DMLVNNAG-QGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASaAASIVCVNSLLALQPEPHMVATSAARAGLL 167


                 ....*....
gi 19113072  159 MLVMNLGSE 167
Cdd:PRK07062 168 NLVKSLATE 176
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-197 1.77e-12

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 65.14  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELET--LLIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLDSV 82
Cdd:PRK06935  16 KVAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWDETrrLIEKEGRKVTFVQVDLTkpESAEKVVKEALEEFGKIDIL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   83 ILNAGVL--EPIAKIADADineWRKLFDINFFSVVE-TVKYAIPHLRKTKGTIVIVSS------GAAVrvfPAWAAyccS 153
Cdd:PRK06935  96 VNNAGTIrrAPLLEYKDED---WNAVMDINLNSVYHlSQAVAKVMAKQGSGKIINIASmlsfqgGKFV---PAYTA---S 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 19113072  154 KAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEA 197
Cdd:PRK06935 167 KHGVAGLTKAFANElaAYNIQVNAIAPGYIKTANTAPIRADKNRND 212
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 7-224 1.78e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 65.35  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVI------AVSRSLTPELE-----TLLIQNPDSFvhvkgdvtevgKASIETAIK 74
Cdd:PRK07825   6 KVVAITGGARGIGLATARALAALgARVAigdldeALAKETAAELGlvvggPLDVTDPASF-----------AAFLDAVEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCS 153
Cdd:PRK07825  75 DLGPIDVLVNNAGVM-PVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRgRGHVVNVASLAGKIPVPGMATYCAS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113072  154 KAAINMLVMNLGSE-EPDIMSV-AVRPGVVDTPMQVSIRndsnkeAMGGdthnffkeLKTsgqlVAPQDIAKA 224
Cdd:PRK07825 154 KHAVVGFTDAARLElRGTGVHVsVVLPSFVNTELIAGTG------GAKG--------FKN----VEPEDVAAA 208
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 9-185 1.79e-12

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: 65.21  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   9 ILLTGSSKGIGLATAEAL-------------QKKAkviAVSRSLTPELETLLIqnpdsfvhvkGDVTEVGKA-SIETAIK 74
Cdd:cd08951  10 IFITGSSDGLGLAAARTLlhqghevvlharsQKRA---ADAKAACPGAAGVLI----------GDLSSLAETrKLADQVN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  75 KFGKLDSVILNAGVL-EPIAKIADADINewrKLFDINFFSvvetvKYAIPHLRKTKGTIVIVSSG-------------AA 140
Cdd:cd08951  77 AIGRFDAVIHNAGILsGPNRKTPDTGIP---AMVAVNVLA-----PYVLTALIRRPKRLIYLSSGmhrggnaslddidWF 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19113072 141 VRVFPAWAAYCCSKAAINMLVMNLGSEEPDIMSVAVRPGVVDTPM 185
Cdd:cd08951 149 NRGENDSPAYSDSKLHVLTLAAAVARRWKDVSSNAVHPGWVPTKM 193
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 7-241 4.06e-12

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 64.31  E-value: 4.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKG---DVT-EVG-KASIETAIKKFGKLDS 81
Cdd:PRK07097  11 KIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYRELGIEAHGyvcDVTdEDGvQAMVSQIEKEVGVIDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGVLEPIAkIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK07097  91 LVNNAGIIKRIP-MLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMiKKGHGKIINICSMMSELGRETVSAYAAAKGGLKML 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  161 VMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKeamgGDTHNF--FKELKT-SGQLVAPQDIAKALSFLALNNNPK 235
Cdd:PRK07097 170 TKNIASEygEANIQCNGIGPGYIATPQTAPLRELQAD----GSRHPFdqFIIAKTpAARWGDPEDLAGPAVFLASDASNF 245


                 ....*.
gi 19113072  236 LTGQFV 241
Cdd:PRK07097 246 VNGHIL 251
PRK05650 PRK05650
SDR family oxidoreductase;
9-157 4.67e-12

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 63.91  E-value: 4.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    9 ILLTGSSKGIGLATAEALQKKAKVIAVS----RSLTPELETLLIQNPDSFVhVKGDVTEVG--KASIETAIKKFGKLDSV 82
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLALAdvneEGGEETLKLLREAGGDGFY-QRCDVRDYSqlTALAQACEEKWGGIDVI 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113072   83 ILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:PRK05650  82 VNNAGVASG-GFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKsGRIVNIASMAGLMQGPAMSSYNVAKAGV 156
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 5-229 4.68e-12

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: 63.76  E-value: 4.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEALQK-KAKVIAVSRSLTPELETL--LIQNPDSFVH-VKGDV--TEVGKASIETAIKKFGK 78
Cdd:cd05369   2 KGKVAFITGGGTGIGKAIAKAFAElGASVAIAGRKPEVLEAAAeeISSATGGRAHpIQCDVrdPEAVEAAVDETLKEFGK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  79 LDSVILNAG--VLEPIAKIADadiNEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAW-----AAyc 151
Cdd:cd05369  82 IDILINNAAgnFLAPAESLSP---NGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPfqvhsAA-- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 152 cSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTpmqvsirndsnKEAMG--GDTHNFFKELKTS---GQLVAPQDIAKA 224
Cdd:cd05369 157 -AKAGVDALTRSLAVEwgPYGIRVNAIAPGPIPT-----------TEGMErlAPSGKSEKKMIERvplGRLGTPEEIANL 224


                ....*
gi 19113072 225 LSFLA 229
Cdd:cd05369 225 ALFLL 229
PRK12743 PRK12743
SDR family oxidoreductase;
7-185 7.02e-12

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 63.51  E-value: 7.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAV-----------------SRSLTPELETLLIQNPDSfvhvkgdvtevGKASI 69
Cdd:PRK12743   3 QVAIVTASDSGIGKACALLLAQQGFDIGItwhsdeegaketaeevrSHGVRAEIRQLDLSDLPE-----------GAQAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   70 ETAIKKFGKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK--TKGTIVIVSSGAAVRVFPAW 147
Cdd:PRK12743  72 DKLIQRLGRIDVLVNNAGAMTK-APFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKqgQGGRIINITSVHEHTPLPGA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19113072  148 AAYCCSKAAINML--VMNLGSEEPDIMSVAVRPGVVDTPM 185
Cdd:PRK12743 151 SAYTAAKHALGGLtkAMALELVEHGILVNAVAPGAIATPM 190
PRK09730 PRK09730
SDR family oxidoreductase;
7-242 7.18e-12

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 63.33  E-value: 7.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVS----RSLTPELETLLIQNPDSFVHVKGDVTEVGK--ASIETAIKKFGKLD 80
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYTVAVNyqqnLHAAQEVVNLITQAGGKAFVLQADISDENQvvAMFTAIDQHDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEPIAKIADADINEWRKLFDIN----FFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPA-WAAYCCSKA 155
Cdd:PRK09730  82 ALVNNAGILFTQCTVENLTAERINRVLSTNvtgyFLCCREAVKRMALKHGGSGGAIVNVSSAASRLGAPGeYVDYAASKG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  156 AINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVS----IRNDSNKEAMggdthnffkELKTSGQlvaPQDIAKALSFLA 229
Cdd:PRK09730 162 AIDTLTTGLSLEvaAQGIRVNCVRPGFIYTEMHASggepGRVDRVKSNI---------PMQRGGQ---PEEVAQAIVWLL 229

                        250
                 ....*....|...
gi 19113072  230 LNNNPKLTGQFVE 242
Cdd:PRK09730 230 SDKASYVTGSFID 242
PRK12742 PRK12742
SDR family oxidoreductase;
1-240 7.34e-12

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 63.24  E-value: 7.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVhVKGDVTEvgKASIETAIKKFGKLD 80
Cdd:PRK12742   1 MGAFTGKKVLVLGGSRGIGAAIVRRFVTDGANVRFTYAGSKDAAERLAQETGATA-VQTDSAD--RDAVIDVVRKSGALD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVL---EPIakiaDADINEWRKLFDIN----FFSVVETVkyaiphlRKTK--GTIVIVSSGAAVRV-FPAWAAY 150
Cdd:PRK12742  78 ILVVNAGIAvfgDAL----ELDADDIDRLFKINihapYHASVEAA-------RQMPegGRIIIIGSVNGDRMpVAGMAAY 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  151 CCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSirNDSNKEAMGGdthnfFKELKTSGQlvaPQDIAKALSFL 228
Cdd:PRK12742 147 AASKSALQGMARGLARDfgPRGITINVVQPGPIDTDANPA--NGPMKDMMHS-----FMAIKRHGR---PEEVAGMVAWL 216

                        250
                 ....*....|..
gi 19113072  229 ALNNNPKLTGQF 240
Cdd:PRK12742 217 AGPEASFVTGAM 228
PRK08589 PRK08589
SDR family oxidoreductase;
1-239 7.52e-12

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 63.64  E-value: 7.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPElETL--LIQNPDSFVHVKGDVTEVG--KASIETAIKK 75
Cdd:PRK08589   1 MKRLENKVAVITGASTGIGQASAIALaQEGAYVLAVDIAEAVS-ETVdkIKSNGGKAKAYHVDISDEQqvKDFASEIKEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVS--SGAAVRVFPawAAYCCS 153
Cdd:PRK08589  80 FGRVDVLFNNAGVDNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMMEQGGSIINTSsfSGQAADLYR--SGYNAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  154 KAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMqVSIRNDSNKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALN 231
Cdd:PRK08589 158 KGAVINFTKSIAIEygRDGIRANAIAPGTIETPL-VDKLTGTSEDEAGKTFRENQKWMTPLGRLGKPEEVAKLVVFLASD 236


                 ....*...
gi 19113072  232 NNPKLTGQ 239
Cdd:PRK08589 237 DSSFITGE 244
PRK07074 PRK07074
SDR family oxidoreductase;
7-229 1.07e-11

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 62.86  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDS-FVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDArFVPVACDLTDAAslAAALANAAAERGPVDVLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAGVLEPIAkIADADINEWRKLFDINFFSVVETVKYAIPHLRK-TKGTIVIVSSGAAVRVF--PAWAAyccSKAAINML 160
Cdd:PRK07074  83 ANAGAARAAS-LHDTTPASWRADNALNLEAAYLCVEAVLEGMLKrSRGAVVNIGSVNGMAALghPAYSA---AKAGLIHY 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113072  161 VMNLGSE--EPDIMSVAVRPGVVDTPMQvsirndsnkEAMGGDTHNFFKELKTSGQL---VAPQDIAKALSFLA 229
Cdd:PRK07074 159 TKLLAVEygRFGIRANAVAPGTVKTQAW---------EARVAANPQVFEELKKWYPLqdfATPDDVANAVLFLA 223
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 5-198 1.29e-11

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 62.65  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAE-ALQKKAKVIAVSRS-LTPELETLLIQNPDSFVHVKGDV-TEVG-KASIETAIKKFGKLD 80
Cdd:PRK12823   7 AGKVVVVTGAAQGIGRGVALrAAAEGARVVLVDRSeLVHEVAAELRAAGGEALALTADLeTYAGaQAAMAAAVEAFGRID 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAG---VLEPIAKIADADIN-EWRKlfdiNFFSVVETVKYAIPHLRKT-KGTIVIVSSGA--AVRVFPawaaYCCS 153
Cdd:PRK12823  87 VLINNVGgtiWAKPFEEYEEEQIEaEIRR----SLFPTLWCCRAVLPHMLAQgGGAIVNVSSIAtrGINRVP----YSAA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 19113072  154 KAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRN---DSNKEAM 198
Cdd:PRK12823 159 KGGVNALTASLAFEyaEHGIRVNAVAPGGTEAPPRRVPRNaapQSEQEKA 208
PRK06128 PRK06128
SDR family oxidoreductase;
10-239 1.54e-11

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 62.95  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEALQKKAKVIAVSrsLTPELET------LLIQNPD-SFVHVKGDVTEVG--KASIETAIKKFGKLD 80
Cdd:PRK06128  59 LITGADSGIGRATAIAFAREGADIALN--YLPEEEQdaaevvQLIQAEGrKAVALPGDLKDEAfcRQLVERAVKELGGLD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLrKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK06128 137 ILVNIAGKQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHL-PPGASIINTGSIQSYQPSPTLLDYASTKAAIVAF 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  161 VMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNK-EAMGGDThnffkELKTSGQlvaPQDIAKALSFLALNNNPKLT 237
Cdd:PRK06128 216 TKALAKQvaEKGIRVNAVAPGPVWTPLQPSGGQPPEKiPDFGSET-----PMKRPGQ---PVEMAPLYVLLASQESSYVT 287


                 ..
gi 19113072  238 GQ 239
Cdd:PRK06128 288 GE 289
PRK07201 PRK07201
SDR family oxidoreductase;
7-185 1.65e-11

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 63.43  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSlTPELETL--LIQNPDSFVHV-KGDVT--EVGKASIETAIKKFGKLD 80
Cdd:PRK07201 372 KVVLITGASSGIGRATAIKVaEAGATVFLVARN-GEALDELvaEIRAKGGTAHAyTCDLTdsAAVDHTVKDILAEHGHVD 450

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGvlepiAKIADADINEWRKLFD------INFFSVVETVKYAIPHLR-KTKGTIVIVSSGAAVRVFPAWAAYCCS 153
Cdd:PRK07201 451 YLVNNAG-----RSIRRSVENSTDRFHDyertmaVNYFGAVRLILGLLPHMReRRFGHVVNVSSIGVQTNAPRFSAYVAS 525

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19113072  154 KAAINMLVMNLGSEEPD--IMSVAVRPGVVDTPM 185
Cdd:PRK07201 526 KAALDAFSDVAASETLSdgITFTTIHMPLVRTPM 559
PRK05717 PRK05717
SDR family oxidoreductase;
7-183 1.88e-11

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 62.21  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVS---RSLTPELETLLIQNPdsfVHVKGDVTEVGKASIETA--IKKFGKLDS 81
Cdd:PRK05717  11 RVALVTGAARGIGLGIAAWLIAEGWQVVLAdldRERGSKVAKALGENA---WFIAMDVADEAQVAAGVAevLGQFGRLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGVLEP-IAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSK----AA 156
Cdd:PRK05717  88 LVCNAAIADPhNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHNGAIVNLASTRARQSEPDTEAYAASKggllAL 167

                        170       180
                 ....*....|....*....|....*..
gi 19113072  157 INMLVMNLGseePDIMSVAVRPGVVDT 183
Cdd:PRK05717 168 THALAISLG---PEIRVNAVSPGWIDA 191
PRK08703 PRK08703
SDR family oxidoreductase;
5-187 2.18e-11

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 61.87  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTpELETLLIQ-----NPDSFVhVKGDVTEVGKASIE----TAIK 74
Cdd:PRK08703   5 SDKTILVTGASQGLGEQVAKAYAAAgATVILVARHQK-KLEKVYDAiveagHPEPFA-IRFDLMSAEEKEFEqfaaTIAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KF-GKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCC 152
Cdd:PRK08703  83 ATqGKLDGIVHCAGYFYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSpDASVIFVGESHGETPKAYWGGFGA 162

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19113072  153 SKAAINMLVMNLGSE---EPDIMSVAVRPGVVDTPMQV 187
Cdd:PRK08703 163 SKAALNYLCKVAADEwerFGNLRANVLVPGPINSPQRI 200
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 1-229 2.25e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 61.95  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPElETLLIQNPDSFVHVKGDVT--EVGKASIETAIKKFG 77
Cdd:PRK08265   1 MIGLAGKVAIVTGGATLIGAAVARALvAAGARVAIVDIDADNG-AAVAASLGERARFIATDITddAAIERAVATVVARFG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNA------GvlepiakiADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSS-----GAAVR-VFP 145
Cdd:PRK08265  80 RVDILVNLActylddG--------LASSRADWLAALDVNLVSAAMLAQAAHPHLARGGGAIVNFTSisakfAQTGRwLYP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  146 AwaayccSKAAINMLVMNLGSE-EPD-IMSVAVRPG-----VVDTpmqVSIRNDSNKEAMGGDTHNFfkelktsGQLVAP 218
Cdd:PRK08265 152 A------SKAAIRQLTRSMAMDlAPDgIRVNSVSPGwtwsrVMDE---LSGGDRAKADRVAAPFHLL-------GRVGDP 215

                        250
                 ....*....|.
gi 19113072  219 QDIAKALSFLA 229
Cdd:PRK08265 216 EEVAQVVAFLC 226
PRK08177 PRK08177
SDR family oxidoreductase;
7-185 3.00e-11

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 61.20  E-value: 3.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSltPELETLLIQNPDsfVHV-KGDVTEVgkASIETAIKKFG--KLDSV 82
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLlERGWQVTATVRG--PQQDTALQALPG--VHIeKLDMNDP--ASLDQLLQRLQgqRFDLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   83 ILNAGVLEPIAK-IADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAA---YCCSKAAIN 158
Cdd:PRK08177  76 FVNAGISGPAHQsAADATAAEIGQLFLTNAIAPIRLARRLLGQVRPGQGVLAFMSSQLGSVELPDGGEmplYKASKAALN 155

                        170       180
                 ....*....|....*....|....*....
gi 19113072  159 MLVMNLGSE--EPDIMSVAVRPGVVDTPM 185
Cdd:PRK08177 156 SMTRSFVAElgEPTLTVLSMHPGWVKTDM 184
PRK07041 PRK07041
SDR family oxidoreductase;
10-241 4.18e-11

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 60.82  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEA-LQKKAKVIAVSRSLtPELETLL--IQNPDSFVHVKGDVTEvgKASIETAIKKFGKLDSVILNA 86
Cdd:PRK07041   1 LVVGGSSGIGLALARAfAAEGARVTIASRSR-DRLAAAAraLGGGAPVRTAALDITD--EAAVDAFFAEAGPFDHVVITA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   87 GVLE--PIAKIadaDINEWRKLFDINFFSVVETVKYaiPHLRKTkGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMNL 164
Cdd:PRK07041  78 ADTPggPVRAL---PLAAAQAAMDSKFWGAYRVARA--ARIAPG-GSLTFVSGFAAVRPSASGVLQGAINAALEALARGL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113072  165 GSEEPDIMSVAVRPGVVDTPMQVSIRNDSnKEAMGGDThnffKELKTSGQLVAPQDIAKALSFLAlnNNPKLTGQFV 241
Cdd:PRK07041 152 ALELAPVRVNTVSPGLVDTPLWSKLAGDA-REAMFAAA----AERLPARRVGQPEDVANAILFLA--ANGFTTGSTV 221
PRK07035 PRK07035
SDR family oxidoreductase;
7-159 7.14e-11

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 60.41  E-value: 7.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPeLETLliqnPDSFV-----------HVkGDVTEVgKASIETAIK 74
Cdd:PRK07035   9 KIALVTGASRGIGEAIAKLLaQQGAHVIVSSRKLDG-CQAV----ADAIVaaggkaealacHI-GEMEQI-DALFAHIRE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNAGVLEPIAKIADADINEWRKLFDIN----FFSVVETVKYaiphLRK-TKGTIVIVSSGAAVRVFPAWAA 149
Cdd:PRK07035  82 RHGRLDILVNNAAANPYFGHILDTDLGAFQKTVDVNirgyFFMSVEAGKL----MKEqGGGSIVNVASVNGVSPGDFQGI 157

                        170
                 ....*....|.
gi 19113072  150 YCCSKAA-INM 159
Cdd:PRK07035 158 YSITKAAvISM 168
PRK08251 PRK08251
SDR family oxidoreductase;
7-186 8.49e-11

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 60.33  E-value: 8.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETL----LIQNPDSFVHVKG-DVTE---VGKAsIETAIKKFGK 78
Cdd:PRK08251   3 QKILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELkaelLARYPGIKVAVAAlDVNDhdqVFEV-FAEFRDELGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVLE--PIAKiADADINewRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFP-AWAAYCCSK 154
Cdd:PRK08251  82 LDRVIVNAGIGKgaRLGT-GKFWAN--KATAETNFVAALAQCEAAMEIFREQgSGHLVLISSVSAVRGLPgVKAAYAASK 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19113072  155 AAINMLVMNLGSEEPD--IMSVAVRPGVVDTPMQ 186
Cdd:PRK08251 159 AGVASLGEGLRAELAKtpIKVSTIEPGYIRSEMN 192
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 5-229 1.29e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 59.67  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRS------LTPELETLLIQNPDSFVhvkGDVTEvgKASIETAIKKFG 77
Cdd:PRK06125   6 AGKRVLITGASKGIGAAAAEAFAAEgCHLHLVARDadaleaLAADLRAAHGVDVAVHA---LDLSS--PEAREQLAAEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLR-KTKGTIV--IVSSGAAVRvfpawAAYCCSK 154
Cdd:PRK06125  81 DIDILVNNAGAI-PGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKaRGSGVIVnvIGAAGENPD-----ADYICGS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAiNMLVMN----LGSEEPD--IMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHnfFKELKTS---GQLVAPQDIAKAL 225
Cdd:PRK06125 155 AG-NAALMAftraLGGKSLDdgVRVVGVNPGPVATDRMLTLLKGRARAELGDESR--WQELLAGlplGRPATPEEVADLV 231


                 ....
gi 19113072  226 SFLA 229
Cdd:PRK06125 232 AFLA 235
PRK07577 PRK07577
SDR family oxidoreductase;
7-241 2.18e-10

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 58.97  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKA-KVIAVSRSLTPELETLLIQnpdsfvhvkGDVTEVGK-ASIETAIKKFGKLDSVIL 84
Cdd:PRK07577   4 RTVLVTGATKGIGLALSLRLANLGhQVIGIARSAIDDFPGELFA---------CDLADIEQtAATLAQINEIHPVDAIVN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   85 NAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSS----GAAVRvfpawAAYCCSKAAINM 159
Cdd:PRK07577  75 NVGIALP-QPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMkLREQGRIVNICSraifGALDR-----TSYSAAKSALVG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  160 LVMNLGSE--EPDIMSVAVRPGVVDTPMqvsIRNDSnkeAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALNNNPKLT 237
Cdd:PRK07577 149 CTRTWALElaEYGITVNAVAPGPIETEL---FRQTR---PVGSEEEKRVLASIPMRRLGTPEEVAAAIAFLLSDDAGFIT 222


                 ....
gi 19113072  238 GQFV 241
Cdd:PRK07577 223 GQVL 226
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 5-167 3.83e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 58.43  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSL---TPELETLLIQNPDSFvHVKGDVTEVG--KASIETAIKKFGK 78
Cdd:PRK07576   8 AGKNVVVVGGTSGINLGIAQAFARAgANVAVASRSQekvDAAVAQLQQAGPEGL-GVSADVRDYAavEAAFAQIADEFGP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAG--VLEPIAKIAdadINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAA 156
Cdd:PRK07576  87 IDVLVSGAAgnFPAPAAGMS---ANGFKTVVDIDLLGTFNVLKAAYPLLRRPGASIIQISAPQAFVPMPMQAHVCAAKAG 163

                        170
                 ....*....|.
gi 19113072  157 INMLVMNLGSE 167
Cdd:PRK07576 164 VDMLTRTLALE 174
PRK07775 PRK07775
SDR family oxidoreductase;
10-229 4.14e-10

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 58.61  E-value: 4.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQ---NPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVIL 84
Cdd:PRK07775  14 LVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKiraDGGEAVAFPLDVTDPDsvKSFVAQAEEALGEIEVLVS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   85 NAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLR-KTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINMLV-- 161
Cdd:PRK07775  94 GAGDTYF-GKLHEISTEQFESQVQIHLVGANRLATAVLPGMIeRRRGDLIFVGSDVALRQRPHMGAYGAAKAGLEAMVtn 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113072  162 MNLGSEEPDIMSVAVRPGVVDTPMQVSIRNDSnKEAMGGD-------THNFFkelktsgqlVAPQDIAKALSFLA 229
Cdd:PRK07775 173 LQMELEGTGVRASIVHPGPTLTGMGWSLPAEV-IGPMLEDwakwgqaRHDYF---------LRASDLARAITFVA 237
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 5-158 5.52e-10

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 57.99  E-value: 5.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTP--ELETLLIQNPDSFVHVKGDVTEvgKASIETA----IKKFG 77
Cdd:PRK08277   9 KGKVAVITGGGGVLGGAMAKELaRAGAKVAILDRNQEKaeAVVAEIKAAGGEALAVKADVLD--KESLEQArqqiLEDFG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAG--------------VLEPIAKIADADINEWRKLFDINFF-SVVETVKYAIPHLRKTKGTIVIVSSGAAVR 142
Cdd:PRK08277  87 PCDILINGAGgnhpkattdnefheLIEPTKTFFDLDEEGFEFVFDLNLLgTLLPTQVFAKDMVGRKGGNIINISSMNAFT 166

                        170
                 ....*....|....*.
gi 19113072  143 VFPAWAAYCCSKAAIN 158
Cdd:PRK08277 167 PLTKVPAYSAAKAAIS 182
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 8-239 5.76e-10

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: 57.89  E-value: 5.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTpeletlliqnpdsfvHVKGDVTEvgKASIETAI-----KKFGKLDS 81
Cdd:cd05328   1 TIVITGAASGIGAATAELLeDAGHTVIGIDLREA---------------DVIADLST--PEGRAAAIadvlaRCSGVLDG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  82 VILNAGVLEPiakiADADInewrkLFDINFFSVVETVKYAIPHLRKTKG-TIVIVSSGAAV------------------- 141
Cdd:cd05328  64 LVNCAGVGGT----TVAGL-----VLKVNYFGLRALMEALLPRLRKGHGpAAVVVSSIAGAgwaqdklelakalaagtea 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 142 --------RVFPAWAAYCCSKAAINMLVMNLGSE---EPDIMSVAVRPGVVDTPMQVSIRNDSnkeaMGGDTHNFFKElk 210
Cdd:cd05328 135 ravalaehAGQPGYLAYAGSKEALTVWTRRRAATwlyGAGVRVNTVAPGPVETPILQAFLQDP----RGGESVDAFVT-- 208

                       250       260
                ....*....|....*....|....*....
gi 19113072 211 TSGQLVAPQDIAKALSFLALNNNPKLTGQ 239
Cdd:cd05328 209 PMGRRAEPDEIAPVIAFLASDAASWINGA 237
PRK09291 PRK09291
SDR family oxidoreductase;
7-183 6.31e-10

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 57.70  E-value: 6.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKA-KVIAVSR------SLTPELETLLIqnpdSFVHVKGDVTEvgkasiETAIKKFGKL 79
Cdd:PRK09291   3 KTILITGAGSGFGREVALRLARKGhNVIAGVQiapqvtALRAEAARRGL----ALRVEKLDLTD------AIDRAQAAEW 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVIL--NAGVLEPIAkIADADINEWRKLFDINFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAA 156
Cdd:PRK09291  73 DVDVLlnNAGIGEAGA-VVDIPVELVRELFETNVFGPLELTQGFVRKmVARGKGKVVFTSSMAGLITGPFTGAYCASKHA 151

                        170       180
                 ....*....|....*....|....*....
gi 19113072  157 INMLVMNLGSE-EPDIMSVA-VRPGVVDT 183
Cdd:PRK09291 152 LEAIAEAMHAElKPFGIQVAtVNPGPYLT 180
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 5-241 8.21e-10

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: 57.49  E-value: 8.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEA-LQKKAKVIAVSRSLTPELETLL-IQNPDSFVHVKGDV-TEVGKASIETAI-KKFGKLD 80
Cdd:cd08942   5 AGKIVLVTGGSRGIGRMIAQGfLEAGARVIISARKAEACADAAEeLSAYGECIAIPADLsSEEGIEALVARVaERSDRLD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-----GTIVIVSSGAAVRVFPAWA-AYCCSK 154
Cdd:cd08942  85 VLVNNAGATWG-APLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAAtaenpARVINIGSIAGIVVSGLENySYGASK 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 155 AAINMLVMNLGSEEPD--IMSVAVRPGVVDTPMQVSIRND-SNKEAmggdthnffkELKTS--GQLVAPQDIAKALSFLA 229
Cdd:cd08942 164 AAVHQLTRKLAKELAGehITVNAIAPGRFPSKMTAFLLNDpAALEA----------EEKSIplGRWGRPEDMAGLAIMLA 233

                       250
                ....*....|..
gi 19113072 230 LNNNPKLTGQFV 241
Cdd:cd08942 234 SRAGAYLTGAVI 245
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-239 9.18e-10

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: 57.55  E-value: 9.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSlTPELETLLIQNPDSFVHVKG---DVTEVG--KASIETAIKKFGKLD 80
Cdd:cd08945   4 EVALVTGATSGIGLAIARRLgKEGLRVFVCARG-EEGLATTVKELREAGVEADGrtcDVRSVPeiEALVAAAVARYGPID 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLE--PIAKIADadiNEWRKLFDINF---FSVVETVKYAIPHLRKTKGTIV-IVSSGAAVRVFPAwAAYCCSK 154
Cdd:cd08945  83 VLVNNAGRSGggATAELAD---ELWLDVVETNLtgvFRVTKEVLKAGGMLERGTGRIInIASTGGKQGVVHA-APYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRN------DSNKEAMggdtHNFFKELKTSGQLVAPQDIAKALS 226
Cdd:cd08945 159 HGVVGFTKALGLElaRTGITVNAVCPGFVETPMAASVREhyadiwEVSTEEA----FDRITARVPLGRYVTPEEVAGMVA 234

                       250
                ....*....|...
gi 19113072 227 FLALNNNPKLTGQ 239
Cdd:cd08945 235 YLIGDGAAAVTAQ 247
PRK08278 PRK08278
SDR family oxidoreductase;
7-167 2.18e-09

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 56.45  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTP-------------ELETLLIQNpdsfVHVKGDVTEVG--KASIE 70
Cdd:PRK08278   7 KTLFITGASRGIGLAIALRAaRDGANIVIAAKTAEPhpklpgtihtaaeEIEAAGGQA----LPLVGDVRDEDqvAAAVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   71 TAIKKFGKLDSVILNAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIVSS---GAAVRVFPAW 147
Cdd:PRK08278  83 KAVERFGGIDICVNNASAIN-LTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLSpplNLDPKWFAPH 161

                        170       180
                 ....*....|....*....|
gi 19113072  148 AAYCCSKAAINMLVMNLGSE 167
Cdd:PRK08278 162 TAYTMAKYGMSLCTLGLAEE 181
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 7-157 3.41e-09

(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: 55.79  E-value: 3.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLLIQNPDSFV-HVK---------GDVTEVGKASIETAIKK 75
Cdd:cd05353   6 RVVLVTGAGGGLGRAYALAFAERgAKVVVNDLGGDRKGSGKSSSAADKVVdEIKaaggkavanYDSVEDGEKIVKTAIDA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  76 FGKLDSVILNAGVLE--PIAKIADADineWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCC 152
Cdd:cd05353  86 FGRVDILVNNAGILRdrSFAKMSEED---WDLVMRVHLKGSFKVTRAAWPYMRKQKfGRIINTSSAAGLYGNFGQANYSA 162


                ....*
gi 19113072 153 SKAAI 157
Cdd:cd05353 163 AKLGL 167
PRK05866 PRK05866
SDR family oxidoreductase;
7-185 3.73e-09

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 55.90  E-value: 3.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRsltpeletlliqNPDSFVHVKGDVTEVG----------------KASI 69
Cdd:PRK05866  41 KRILLTGASSGIGEAAAEQFARRgATVVAVAR------------REDLLDAVADRITRAGgdamavpcdlsdldavDALV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   70 ETAIKKFGKLDSVILNAGvlEPIAKIADADINEW---RKLFDINFFSVVETVKYAIPH-LRKTKGTIVIVSS-GAAVRVF 144
Cdd:PRK05866 109 ADVEKRIGGVDILINNAG--RSIRRPLAESLDRWhdvERTMVLNYYAPLRLIRGLAPGmLERGDGHIINVATwGVLSEAS 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19113072  145 PAWAAYCCSKAAINMLVMNLGSEEPD--IMSVAVRPGVVDTPM 185
Cdd:PRK05866 187 PLFSVYNASKAALSAVSRVIETEWGDrgVHSTTLYYPLVATPM 229
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 7-242 3.88e-09

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 55.47  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAV---SRSLTPELETLLIQ-NPDSFVHVKGDV-----TEVGKASIETAIKK-- 75
Cdd:PRK12747   5 KVALVTGASRGIGRAIAKRLANDGALVAIhygNRKEEAEETVYEIQsNGGSAFSIGANLeslhgVEALYSSLDNELQNrt 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 -FGKLDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKgTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PRK12747  85 gSTKFDILINNAGI-GPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDNS-RIINISSAATRISLPDFIAYSMTK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGDTHNFfkelktsGQLVAPQDIAKALSFLALNN 232
Cdd:PRK12747 163 GAINTMTFTLAKQlgARGITVNAILPGFIKTDMNAELLSDPMMKQYATTISAF-------NRLGEVEDIADTAAFLASPD 235

                        250
                 ....*....|
gi 19113072  233 NPKLTGQFVE 242
Cdd:PRK12747 236 SRWVTGQLID 245
PRK05867 PRK05867
SDR family oxidoreductase;
10-238 4.25e-09

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 55.43  E-value: 4.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETL---LIQNPDSFVHVKGDVTEVGKAS--IETAIKKFGKLDSVIL 84
Cdd:PRK05867  13 LITGASTGIGKRVALAYVEAGAQVAIAARHLDALEKLadeIGTSGGKVVPVCCDVSQHQQVTsmLDQVTAELGGIDIAVC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   85 NAGVLEpIAKIADADINEWRKLFDINFFSVVETVKYAI-PHLRKTKGTIVIVS---SGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK05867  93 NAGIIT-VTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAkAMVKQGQGGVIINTasmSGHIINVPQQVSHYCASKAAVIHL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  161 VMNLGSE-EP-DIMSVAVRPGVVDTPMQVSIrndsnkeamgGDTHNFFKELKTSGQLVAPQDIAKALSFLALNNNPKLTG 238
Cdd:PRK05867 172 TKAMAVElAPhKIRVNSVSPGYILTELVEPY----------TEYQPLWEPKIPLGRLGRPEELAGLYLYLASEASSYMTG 241
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 10-223 5.39e-09

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 55.35  E-value: 5.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELET----LLIQNPDsfVH-VKGDV---TEVGKASIEtAIKKFGKLDS 81
Cdd:PRK05876  10 VITGGASGIGLATGTEFARRGARVVLGDVDKPGLRQavnhLRAEGFD--VHgVMCDVrhrEEVTHLADE-AFRLLGHVDV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:PRK05876  87 VFSNAGIVVG-GPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLleQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVG 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113072  160 LVMNLGSE-EPDIMSVAVRpgvvdTPMQVSIRNDSNKEAMGG------DTHNFFKELKTSGQLVAPQDIAK 223
Cdd:PRK05876 166 LAETLAREvTADGIGVSVL-----CPMVVETNLVANSERIRGaacaqsSTTGSPGPLPLQDDNLGVDDIAQ 231
PRK06101 PRK06101
SDR family oxidoreductase;
8-206 6.74e-09

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 54.88  E-value: 6.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    8 VILLTGSSKGIGLATAEALQKK-AKVIAVSRSltPELETLLIQNPDSFVHVKGDVTEVGKASIETAIKKFGKlDSVILNA 86
Cdd:PRK06101   3 AVLITGATSGIGKQLALDYAKQgWQVIACGRN--QSVLDELHTQSANIFTLAFDVTDHPGTKAALSQLPFIP-ELWIFNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   87 GVLEPIAK-IADADIneWRKLFDINFFSVVETVKYAIPHLRKTKgTIVIVSSGAAVRVFPAWAAYCCSKAAINMLVMNLG 165
Cdd:PRK06101  80 GDCEYMDDgKVDATL--MARVFNVNVLGVANCIEGIQPHLSCGH-RVVIVGSIASELALPRAEAYGASKAAVAYFARTLQ 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113072  166 SE--EPDIMSVAVRPGVVDT----------PMQVSIRNDSN---KEAMGGDTHNFF 206
Cdd:PRK06101 157 LDlrPKGIEVVTVFPGFVATpltdkntfamPMIITVEQASQeirAQLARGKSHIYF 212
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 5-183 1.02e-08

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: 54.37  E-value: 1.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   5 AEKVILLTGSSKGIGLATAEALQKKAKVIAVS-RSLTPELETLLIQNPDS---FVHVKGDVT---EVGKASIETAIKKFG 77
Cdd:cd09763   2 SGKIALVTGASRGIGRGIALQLGEAGATVYITgRTILPQLPGTAEEIEARggkCIPVRCDHSdddEVEALFERVAREQQG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  78 KLDSVILNA-----GVLEPIAK-IADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAwAAY 150
Cdd:cd09763  82 RLDILVNNAyaavqLILVGVAKpFWEEPPTIWDDINNVGLRAHYACSVYAAPLMVKAgKGLIVIISSTGGLEYLFN-VAY 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 19113072 151 CCSKAAINMLVMNLGSE-EPD-IMSVAVRPGVVDT 183
Cdd:cd09763 161 GVGKAAIDRMAADMAHElKPHgVAVVSLWPGFVRT 195
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-239 1.44e-08

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: 53.82  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEALQKKAKVIAV----SRSLTPELETLLIQNPDSFVHVKGDVTEVGK--ASIETAIKKFGKLD 80
Cdd:cd05357   1 AVALVTGAAKRIGRAIAEALAAEGYRVVVhynrSEAEAQRLKDELNALRNSAVLVQADLSDFAAcaDLVAAAFRAFGRCD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRK-TKGTIVIVSSGAAVRVFPAWAAYCCSKAAINM 159
Cdd:cd05357  81 VLVNNASAFYP-TPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGsRNGSIINIIDAMTDRPLTGYFAYCMSKAALEG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 160 LVMNLGSE-EPDIMSVAVRPGVVDTP--MQVSIRNDS-NKEAMggdthnffkelktsGQLVAPQDIAKALSFLAlnNNPK 235
Cdd:cd05357 160 LTRSAALElAPNIRVNGIAPGLILLPedMDAEYRENAlRKVPL--------------KRRPSAEEIADAVIFLL--DSNY 223


                ....
gi 19113072 236 LTGQ 239
Cdd:cd05357 224 ITGQ 227
PRK09009 PRK09009
SDR family oxidoreductase;
9-243 1.73e-08

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 53.53  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    9 ILLTGSSKGIGLATAEALQ---KKAKVIAVSRSLTPELETlliqnpDSFVHVKGDVTEvgKASIETAIKKFGKLDSVILN 85
Cdd:PRK09009   3 ILIVGGSGGIGKAMVKQLLeryPDATVHATYRHHKPDFQH------DNVQWHALDVTD--EAEIKQLSEQFTQLDWLINC 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   86 AGVLEPIAKIADADINEwrklFDINFFSVVETV---------KYAIPHLRKTkgtiviVSSGAAV---RV-------FPA 146
Cdd:PRK09009  75 VGMLHTQDKGPEKSLQA----LDADFFLQNITLntlpslllaKHFTPKLKQS------ESAKFAVisaKVgsisdnrLGG 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  147 WAAYCCSKAAINMLVMNLGSEEPDIMS----VAVRPGVVDTPMQVSirndsnkeamggdthnfFKELKTSGQLVAPQDIA 222
Cdd:PRK09009 145 WYSYRASKAALNMFLKTLSIEWQRSLKhgvvLALHPGTTDTALSKP-----------------FQQNVPKGKLFTPEYVA 207

                        250       260
                 ....*....|....*....|.
gi 19113072  223 KALSFLALNNNPKLTGQFVEW 243
Cdd:PRK09009 208 QCLLGIIANATPAQSGSFLAY 228
PRK07831 PRK07831
SDR family oxidoreductase;
5-135 2.09e-08

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 53.50  E-value: 2.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSS-KGIGLATAE-ALQKKAKVIaVS----RSLTPELETLLIQNPDSFVH-VKGDVT--EVGKASIETAIKK 75
Cdd:PRK07831  16 AGKVVLVTAAAgTGIGSATARrALEEGARVV-ISdiheRRLGETADELAAELGLGRVEaVVCDVTseAQVDALIDAAVER 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGvLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVIV 135
Cdd:PRK07831  95 LGRLDVLVNNAG-LGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIV 153
PRK05993 PRK05993
SDR family oxidoreductase;
1-183 3.53e-08

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 52.72  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETaeKVILLTGSSKGIGLATAEALQKKA-KVIAVSR------SLTPE-LETLLIqnpdsfvhvkgDVTEvgKASIETA 72
Cdd:PRK05993   1 MDMK--RSILITGCSSGIGAYCARALQSDGwRVFATCRkeedvaALEAEgLEAFQL-----------DYAE--PESIAAL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   73 IKKF-----GKLDSVILNAGVLEPIAkIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPA 146
Cdd:PRK05993  66 VAQVlelsgGRLDALFNNGAYGQPGA-VEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGqGRIVQCSSILGLVPMKY 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19113072  147 WAAYCCSKAAIN--MLVMNLGSEEPDIMSVAVRPGVVDT 183
Cdd:PRK05993 145 RGAYNASKFAIEglSLTLRMELQGSGIHVSLIEPGPIET 183
PRK07806 PRK07806
SDR family oxidoreductase;
1-156 4.17e-08

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 52.41  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPELETLLIQNPDSFVH---VKGDVT--EVGKASIETAIK 74
Cdd:PRK07806   1 MGDLPGKTALVTGSSRGIGADTAKILaGAGAHVVVNYRQKAPRANKVVAEIEAAGGRasaVGADLTdeESVAALMDTARE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNA-GVLEpiakiADADINEWRKLfdiNFFSVVETVKYAIPHLRkTKGTIVIVSSGAA-----VRVFPAWA 148
Cdd:PRK07806  81 EFGGLDALVLNAsGGME-----SGMDEDYAMRL---NRDAQRNLARAALPLMP-AGSRVVFVTSHQAhfiptVKTMPEYE 151


                 ....*...
gi 19113072  149 AYCCSKAA 156
Cdd:PRK07806 152 PVARSKRA 159
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
5-229 8.41e-08

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 51.55  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKKA-KVIAVSRSLTPELETLLIQNPD---SFVHVKGDVT--EVGKASIETAIKKFGK 78
Cdd:PRK12938   2 SQRIAYVTGGMGGIGTSICQRLHKDGfKVVAGCGPNSPRRVKWLEDQKAlgfDFIASEGNVGdwDSTKAAFDKVKAEVGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVLEPIA--KIADADineWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK12938  82 IDVLVNNAGITRDVVfrKMTRED---WTAVIDTNLTSLFNVTKQVIDGMvERGWGRIINISSVNGQKGQFGQTNYSTAKA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113072  156 AINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMGGdthnffKELKTSGQlvaPQDIAKALSFLA 229
Cdd:PRK12938 159 GIHGFTMSLAQEvaTKGVTVNTVSPGYIGTDMVKAIRPDVLEKIVAT------IPVRRLGS---PDEIGSIVAWLA 225
PRK06139 PRK06139
SDR family oxidoreductase;
1-184 1.10e-07

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 51.64  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSR---SLTPELETLLIQNPDSFVhVKGDVTEVG--KASIETAIK 74
Cdd:PRK06139   2 MGPLHGAVVVITGASSGIGQATAEAFARRgARLVLAARdeeALQAVAEECRALGAEVLV-VPTDVTDADqvKALATQAAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTKGTIVI--VSSGAAVRVfPAWAAYCC 152
Cdd:PRK06139  81 FGGRIDVWVNNVGV-GAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFInmISLGGFAAQ-PYAAAYSA 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19113072  153 SKAAINMLVMNLGSE---EPDIMSVAVRPGVVDTP 184
Cdd:PRK06139 159 SKFGLRGFSEALRGEladHPDIHVCDVYPAFMDTP 193
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
9-181 2.16e-07

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 50.75  E-value: 2.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   9 ILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELEtllIQNPDSFVHVKGDVTEvgKASIETAIKKFgklDSVILNAG 87
Cdd:COG0451   2 ILVTGGAGFIGSHLARRLLARgHEVVGLDRSPPGAAN---LAALPGVEFVRGDLRD--PEALAAALAGV---DAVVHLAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  88 vlepiakIADADINEWRKLFDINFFSVVETVKYAIPH-LRKtkgtIVIVSSGAAVRVFPAWA----------AYCCSKAA 156
Cdd:COG0451  74 -------PAGVGEEDPDETLEVNVEGTLNLLEAARAAgVKR----FVYASSSSVYGDGEGPIdedtplrpvsPYGASKLA 142

                       170       180
                ....*....|....*....|....*
gi 19113072 157 INMLVMNLgSEEPDIMSVAVRPGVV 181
Cdd:COG0451 143 AELLARAY-ARRYGLPVTILRPGNV 166
PRK07832 PRK07832
SDR family oxidoreductase;
7-185 2.39e-07

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 50.43  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAVS-------RSLTPELETLLIQNPDsfvHVKGDVTEVG--KASIETAIKKFG 77
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELFLTdrdadglAQTVADARALGGTVPE---HRALDISDYDavAAFAADIHAAHG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGvlepIAKIADAD---INEWRKLFDINFFSVVETVKYAIPHLRKTK--GTIVIVSSGAAVRVFPAWAAYCC 152
Cdd:PRK07832  78 SMDVVMNIAG----ISAWGTVDrltHEQWRRMVDVNLMGPIHVIETFVPPMVAAGrgGHLVNVSSAAGLVALPWHAAYSA 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19113072  153 SKAAINML--VMNLGSEEPDIMSVAVRPGVVDTPM 185
Cdd:PRK07832 154 SKFGLRGLseVLRFDLARHGIGVSVVVPGAVKTPL 188
PRK12746 PRK12746
SDR family oxidoreductase;
7-242 3.11e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 50.03  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKAKVIAV--SRSLTPELETL--LIQNPDSFVHVKGDVTEVG--KASIETAIKKF---- 76
Cdd:PRK12746   7 KVALVTGASRGIGRAIAMRLANDGALVAIhyGRNKQAADETIreIESNGGKAFLIEADLNSIDgvKKLVEQLKNELqirv 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   77 --GKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLRkTKGTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PRK12746  87 gtSEIDILVNNAGIGTQ-GTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLR-AEGRVINISSAEVRLGFTGSIAYGLSK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSnkeamggDTHNFFKELKTSGQLVAPQDIAKALSFLALNN 232
Cdd:PRK12746 165 GALNTMTLPLAKHlgERGITVNTIMPGYTKTDINAKLLDDP-------EIRNFATNSSVFGRIGQVEDIADAVAFLASSD 237

                        250
                 ....*....|
gi 19113072  233 NPKLTGQFVE 242
Cdd:PRK12746 238 SRWVTGQIID 247
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 10-192 3.94e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 49.77  E-value: 3.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEAL-QKKAKVIAVSRSlTPELETLLIQNPDSFVHVKG---DVTEvgKASIETAIKKF----GKLDS 81
Cdd:PRK07523  14 LVTGSSQGIGYALAEGLaQAGAEVILNGRD-PAKLAAAAESLKGQGLSAHAlafDVTD--HDAVRAAIDAFeaeiGPIDI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   82 VILNAGvLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:PRK07523  91 LVNNAG-MQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMiARGAGKIINIASVQSALARPGIAPYTATKGAVGNL 169

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19113072  161 VMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRND 192
Cdd:PRK07523 170 TKGMATDwaKHGLQCNAIAPGYFDTPLNAALVAD 203
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 3-190 4.33e-07

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 49.57  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    3 ETAEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVGK-----ASIETAIKKFG 77
Cdd:PRK08217   2 DLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLEEAVAECGALGTEVRGYAANVTDeedveATFAQIAEDFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGVLEP--IAKIADADIN------EWRKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSSGAAVRVFpAW 147
Cdd:PRK08217  82 QLNGLINNAGILRDglLVKAKDGKVTskmsleQFQSVIDVNLTGVFLCGREAAAKMieSGSKGVIINISSIARAGNM-GQ 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19113072  148 AAYCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIR 190
Cdd:PRK08217 161 TNYSASKAGVAAMTVTWAKElaRYGIRVAAIAPGVIETEMTAAMK 205
PRK06124 PRK06124
SDR family oxidoreductase;
5-239 5.76e-07

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 49.33  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    5 AEKVILLTGSSKGIGLATAEALQKK-AKVIAVSR---SLTPELETL----LIQNPDSFvhvkgDVT--EVGKASIETAIK 74
Cdd:PRK06124  10 AGQVALVTGSARGLGFEIARALAGAgAHVLVNGRnaaTLEAAVAALraagGAAEALAF-----DIAdeEAVAAAFARIDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   75 KFGKLDSVILNAGVLE--PIAKIADADInewRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYC 151
Cdd:PRK06124  85 EHGRLDILVNNVGARDrrPLAELDDAAI---RALLETDLVAPILLSRLAAQRMKRQGyGRIIAITSIAGQVARAGDAVYP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  152 CSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDT-PMQVSIRNDSNKEAMggdthnffkELKTS-GQLVAPQDIAKALSF 227
Cdd:PRK06124 162 AAKQGLTGLMRALAAEfgPHGITSNAIAPGYFATeTNAAMAADPAVGPWL---------AQRTPlGRWGRPEEIAGAAVF 232

                        250
                 ....*....|..
gi 19113072  228 LALNNNPKLTGQ 239
Cdd:PRK06124 233 LASPAASYVNGH 244
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 8-241 6.30e-07

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: 49.11  E-value: 6.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLT--PELETLLIQNPDSFVHVKGDVTEVgkasIETAIKKFGKLDSVIL 84
Cdd:cd05361   3 IALVTHARHFAGPASAEALtEDGYTVVCHDASFAdaAERQAFESENPGTKALSEQKPEEL----VDAVLQAGGAIDVLVS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  85 N---AGVLEPIAKIADADINEWRKLFDINFFSVVETvkyAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAAINML 160
Cdd:cd05361  79 NdyiPRPMNPIDGTSEADIRQAFEALSIFPFALLQA---AIAQMKKAGgGSIIFITSAVPKKPLAYNSLYGPARAAAVAL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 161 VMNLGSE--EPDIMSVAVRPGVVDT----PMQVSIRNDSNKEAMGGDThnffkelkTSGQLVAPQDIAKALSFLALNNNP 234
Cdd:cd05361 156 AESLAKElsRDNILVYAIGPNFFNSptyfPTSDWENNPELRERVKRDV--------PLGRLGRPDEMGALVAFLASRRAD 227


                ....*..
gi 19113072 235 KLTGQFV 241
Cdd:cd05361 228 PITGQFF 234
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 7-239 6.33e-07

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 49.17  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSL------TPELETLLIQNpdsfVHVKGDVT--EVGKASIETAIKKFG 77
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALgEAGARVVLSARKAeeleeaAAHLEALGIDA----LWIAADVAdeADIERLAEETLERFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGVLEPiAKIADADINEWRKLFDIN----FFSVVETVKYAIphLRKTKGTIVIVSS-----GAAVRVFPAwA 148
Cdd:PRK08213  89 HVDILVNNAGATWG-APAEDHPVEAWDKVMNLNvrglFLLSQAVAKRSM--IPRGYGRIINVASvaglgGNPPEVMDT-I 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  149 AYCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPM-QVSIrndsnkEAMGGDthnfFKELKTSGQLVAPQDIAKAL 225
Cdd:PRK08213 165 AYNTSKGAVINFTRALAAEwgPHGIRVNAIAPGFFPTKMtRGTL------ERLGED----LLAHTPLGRLGDDEDLKGAA 234

                        250
                 ....*....|....
gi 19113072  226 SFLALNNNPKLTGQ 239
Cdd:PRK08213 235 LLLASDASKHITGQ 248
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 7-157 8.48e-07

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 48.72  E-value: 8.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLA-----------------TAEALQKKAKVIAVSRSLTP-----ELETLLIQNPDSFVhvkgdvtev 64
Cdd:PRK08945  13 RIILVTGAGDGIGREaaltyarhgatvillgrTEEKLEAVYDEIEAAGGPQPaiiplDLLTATPQNYQQLA--------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   65 gkASIEtaiKKFGKLDSVILNAGVLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSS--GAAV 141
Cdd:PRK08945  84 --DTIE---EQFGRLDGVLHNAGLLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPaASLVFTSSsvGRQG 158

                        170
                 ....*....|....*.
gi 19113072  142 RVFpaWAAYCCSKAAI 157
Cdd:PRK08945 159 RAN--WGAYAVSKFAT 172
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-241 1.35e-06

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 48.15  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSK--GIGLATAEALQKKAKVI-------------AVSRSLTP-ELETLLIQNPDSFVHVKGDVTEVGKAS- 68
Cdd:PRK12748   5 KKIALVTGASRlnGIGAAVCRRLAAKGIDIfftywspydktmpWGMHDKEPvLLKEEIESYGVRCEHMEIDLSQPYAPNr 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   69 -IETAIKKFGKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFS-VVETVKYAIPHLRKTKGTIVIVSSGAAVRVFPA 146
Cdd:PRK12748  85 vFYAVSERLGDPSILINNAAYSTH-TRLEELTAEQLDKHYAVNVRAtMLLSSAFAKQYDGKAGGRIINLTSGQSLGPMPD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  147 WAAYCCSKAAINMLVMNLGSEEPD--IMSVAVRPGVVDTPMqvsirndsnkeaMGGDTHNFFKELKTSGQLVAPQDIAKA 224
Cdd:PRK12748 164 ELAYAATKGAIEAFTKSLAPELAEkgITVNAVNPGPTDTGW------------ITEELKHHLVPKFPQGRVGEPVDAARL 231

                        250
                 ....*....|....*..
gi 19113072  225 LSFLALNNNPKLTGQFV 241
Cdd:PRK12748 232 IAFLVSEEAKWITGQVI 248
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 8-184 1.45e-06

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: 47.76  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEALQKKA-KVIAVSRSLTpELETLLIQ----NPDSFVHVKGDVTEVGK--ASIETAIKKFGKLD 80
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGfSVALAARREA-KLEALLVDiirdAGGSAKAVPTDARDEDEviALFDLIEEEIGPLE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  81 SVILNAG--VLEPIAKIADAdinEWRKLFDINFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAI 157
Cdd:cd05373  80 VLVYNAGanVWFPILETTPR---VFEKVWEMAAFGGFLAAREAAKRmLARGRGTIIFTGATASLRGRAGFAAFAGAKFAL 156

                       170       180       190
                ....*....|....*....|....*....|
gi 19113072 158 NMLVMNLGSE-EPDIMSVA--VRPGVVDTP 184
Cdd:cd05373 157 RALAQSMARElGPKGIHVAhvIIDGGIDTD 186
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 8-108 2.91e-06

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: 47.75  E-value: 2.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   8 VILLTGSSKGIGLATAEAL--QKKAKVIAVSRS-LTPE----LETL--LIQNPDSFVHVKGDVTEVG--KASIETAIKKF 76
Cdd:cd08953 207 VYLVTGGAGGIGRALARALarRYGARLVLLGRSpLPPEeewkAQTLaaLEALGARVLYISADVTDAAavRRLLEKVRERY 286

                        90       100       110
                ....*....|....*....|....*....|..
gi 19113072  77 GKLDSVILNAGVLEPiAKIADADINEWRKLFD 108
Cdd:cd08953 287 GAIDGVIHAAGVLRD-ALLAQKTAEDFEAVLA 317
PRK06114 PRK06114
SDR family oxidoreductase;
7-238 3.45e-06

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 46.70  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSLTPELETLL--IQNPD-SFVHVKGDVTEvgKASIETAIKK----FGK 78
Cdd:PRK06114   9 QVAFVTGAGSGIGQRIAIGLaQAGADVALFDLRTDDGLAETAehIEAAGrRAIQIAADVTS--KADLRAAVARteaeLGA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVILNAGVLEPIAKiADADINEWRKLFDINFFSVVETVKY-AIPHLRKTKGTIV-IVS-SGAAVRVFPAWAAYCCSKA 155
Cdd:PRK06114  87 LTLAVNAAGIANANPA-EEMEEEQWQTVMDINLTGVFLSCQAeARAMLENGGGSIVnIASmSGIIVNRGLLQAHYNASKA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  156 AINMLVMNLGSEEPD--IMSVAVRPGVVDTPMqvsirndsNKEAMGGDTHNFFKELKTSGQLVAPQDIAKALSFLALNNN 233
Cdd:PRK06114 166 GVIHLSKSLAMEWVGrgIRVNSISPGYTATPM--------NTRPEMVHQTKLFEEQTPMQRMAKVDEMVGPAVFLLSDAA 237


                 ....*
gi 19113072  234 PKLTG 238
Cdd:PRK06114 238 SFCTG 242
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-182 3.59e-06

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 46.68  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAE-ALQKKAKVIAVSRS------LTPELETLliqnpDSFVHVKGDV--TEVGKASIETAIKKFG 77
Cdd:PRK05786   6 KKVAIIGVSEGLGYAVAYfALKEGAQVCINSRNenklkrMKKTLSKY-----GNIHYVVGDVssTESARNVIEKAAKVLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAG--VLEPIAKIADADinewrKLFDINFFSVVETVKYAIPHLRKTKgTIVIVSS-GAAVRVFPAWAAYCCSK 154
Cdd:PRK05786  81 AIDGLVVTVGgyVEDTVEEFSGLE-----EMLTNHIKIPLYAVNASLRFLKEGS-SIVLVSSmSGIYKASPDQLSYAVAK 154

                        170       180       190
                 ....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE--EPDIMSVAVRPGVVD 182
Cdd:PRK05786 155 AGLAKAVEILASEllGRGIRVNGIAPTTIS 184
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 6-239 3.98e-06

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 46.62  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQN-PDSFVHVKGDVT---EVgKASIETAIKKFGK-LD 80
Cdd:PRK08642   5 EQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALADElGDRAIALQADVTdreQV-QAMFATATEHFGKpIT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   81 SVILNAGV---LEPIA--KIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSK 154
Cdd:PRK08642  84 TVVNNALAdfsFDGDArkKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGfGRIINIGTNLFQNPVVPYHDYTTAK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  155 AAINMLVMNLGSE-EPD-IMSVAVRPGVVDTpmqvsirndsnKEAMGGDTHNFFKELKTS---GQLVAPQDIAKALSFLA 229
Cdd:PRK08642 164 AALLGLTRNLAAElGPYgITVNMVSGGLLRT-----------TDASAATPDEVFDLIAATtplRKVTTPQEFADAVLFFA 232

                        250
                 ....*....|
gi 19113072  230 LNNNPKLTGQ 239
Cdd:PRK08642 233 SPWARAVTGQ 242
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 7-186 4.03e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 46.94  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSL---TPELETLLIQNPDSFVHVKG-DVTEVgkASIETAI----KKFG 77
Cdd:PRK06197  17 RVAVVTGANTGLGYETAAALaAKGAHVVLAVRNLdkgKAAAARITAATPGADVTLQElDLTSL--ASVRAAAdalrAAYP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGVL-EPIAKIADAdinewrklFDINF-------FSVVETVkyaIPHLRKTKGT-IVIVSSG-----AAV-- 141
Cdd:PRK06197  95 RIDLLINNAGVMyTPKQTTADG--------FELQFgtnhlghFALTGLL---LDRLLPVPGSrVVTVSSGghrirAAIhf 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113072  142 ------RVFPAWAAYCCSKAAiNMLVM-----NLGSEEPDIMSVAVRPGVVDTPMQ 186
Cdd:PRK06197 164 ddlqweRRYNRVAAYGQSKLA-NLLFTyelqrRLAAAGATTIAVAAHPGVSNTELA 218
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 6-239 4.75e-06

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: 46.56  E-value: 4.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   6 EKVILLTGSSKGIGLATAEAL-QKKAKVIAVSRSL--TPELETLLIQNPDSFVH-VKGDVTEVGKAS--IETAIKKFGKL 79
Cdd:cd08930   2 DKIILITGAAGLIGKAFCKALlSAGARLILADINApaLEQLKEELTNLYKNRVIaLELDITSKESIKelIESYLEKFGRI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  80 DSVILNAG--VLEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAV------------RVF 144
Cdd:cd08930  82 DILINNAYpsPKVWGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQgKGSIINIASIYGViapdfriyentqMYS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 145 PawAAYCCSKAAINMLVMNLGSEEPD--IMSVAVRPG-VVDTPMQVSIRNDSNKEAMGGdthnffkelktsgqLVAPQDI 221
Cdd:cd08930 162 P--VEYSVIKAGIIHLTKYLAKYYADtgIRVNAISPGgILNNQPSEFLEKYTKKCPLKR--------------MLNPEDL 225

                       250
                ....*....|....*...
gi 19113072 222 AKALSFLALNNNPKLTGQ 239
Cdd:cd08930 226 RGAIIFLLSDASSYVTGQ 243
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 2-229 9.36e-06

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 46.06  E-value: 9.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   2 AETAEKVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLLIQNPDsfvHVKGDVTEV-GKASIETAIKKFGKL 79
Cdd:COG3347 421 KPLAGRVALVTGGAGGIGRATAARLAAEgAAVVVADLDGEAAEAAAAELGGG---YGADAVDATdVDVTAEAAVAAAFGF 497

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  80 DSVILNAGVLEP--IAKIADADINEWRKLFDINFFSVVETVkYAIPHLRKTKGT---------IVIVSSGAAVRVFPAwA 148
Cdd:COG3347 498 AGLDIGGSDIGVanAGIASSSPEEETRLSFWLNNFAHLSTG-QFLVARAAFQGTggqglggssVFAVSKNAAAAAYGA-A 575

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072 149 AYCCSKAAINMLVMNLGSEEPDIMSVAVRPGVVDTPMQVSIRN-------DSNKEAMGGDTHNFFKELKTSGQLVAPQDI 221
Cdd:COG3347 576 AAATAKAAAQHLLRALAAEGGANGINANRVNPDAVLDGSAIWAsaaraerAAAYGIGNLLLEEVYRKRVALAVLVLAEDI 655


                ....*...
gi 19113072 222 AKALSFLA 229
Cdd:COG3347 656 AEAAAFFA 663
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 6-137 1.27e-05

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 45.03  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSKGIGLATAEALQKKAKVIAV-------SRSLTPELETLliQNPDSFVHVKGDVT---EVgKASIETAIKK 75
Cdd:PRK12384   2 NQVAVVIGGGQTLGAFLCHGLAEEGYRVAVadinsekAANVAQEINAE--YGEGMAYGFGADATseqSV-LALSRGVDEI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113072   76 FGKLDSVILNAGVLEPiAKIADADINEWRKLFDIN----FFSVVETVKYAIPhlRKTKGTIVIVSS 137
Cdd:PRK12384  79 FGRVDLLVYNAGIAKA-AFITDFQLGDFDRSLQVNlvgyFLCAREFSRLMIR--DGIQGRIIQINS 141
PRK06194 PRK06194
hypothetical protein; Provisional
 1-157 1.51e-05

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 45.01  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVGKAS-----IETAIKK 75
Cdd:PRK06194   1 MKDFAGKVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALDRAVAELRAQGAEVLGVRTDVSDAAqvealADAALER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   76 FGKLDSVILNAGVlEPIAKIADADINEWRKLFDINFFSVVETVKYAIPHL-------RKTKGTIVIVSSGAAVRVFPAWA 148
Cdd:PRK06194  81 FGAVHLLFNNAGV-GAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMlaaaekdPAYEGHIVNTASMAGLLAPPAMG 159


                 ....*....
gi 19113072  149 AYCCSKAAI 157
Cdd:PRK06194 160 IYNVSKHAV 168
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 7-149 1.61e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 44.67  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETL--LIQNPDSFVHVKGDV--TEVGKASIETAIKKFGKLDS 81
Cdd:PRK07677   2 KVVIITGGSSGMGKAMAKRFAEEgANVVITGRTKEKLEEAKleIEQFPGQVLTVQMDVrnPEDVQKMVEQIDEKFGRIDA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113072   82 VILNAG--VLEPIAKIAdadINEWRKLFDI----NFFSVVETVKYAIPhlRKTKGTIV-IVSS---GAAVRVFPAWAA 149
Cdd:PRK07677  82 LINNAAgnFICPAEDLS---VNGWNSVIDIvlngTFYCSQAVGKYWIE--KGIKGNIInMVATyawDAGPGVIHSAAA 154
PRK07102 PRK07102
SDR family oxidoreductase;
78-224 2.37e-05

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 44.14  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   78 KLDSVILNAGVLePIAKIADADINEWRKLFDINFFSVVETVKYAIPHLRKTK-GTIVIVSSGAAVRVFPAWAAYCCSKAA 156
Cdd:PRK07102  76 LPDIVLIAVGTL-GDQAACEADPALALREFRTNFEGPIALLTLLANRFEARGsGTIVGISSVAGDRGRASNYVYGSAKAA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113072  157 INMLVMNLGSE--EPDIMSVAVRPGVVDTPMqvsirndsnkeamggdTHNffkeLKTSGQLVA-PQDIAKA 224
Cdd:PRK07102 155 LTAFLSGLRNRlfKSGVHVLTVKPGFVRTPM----------------TAG----LKLPGPLTAqPEEVAKD 205
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 10-158 4.20e-05

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 43.70  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   10 LLTGSSKGIGLATAEALQKKA-----------KVIAVSRSLTPELETLLIQNpdSFVHVKGDVTEvGKASIETAIKKfgk 78
Cdd:PLN02780  57 LVTGPTDGIGKGFAFQLARKGlnlvlvarnpdKLKDVSDSIQSKYSKTQIKT--VVVDFSGDIDE-GVKRIKETIEG--- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   79 LDSVIL--NAGVLEPIAK-IADADINEWRKLFDINFFSVVETVKYAIPH-LRKTKGTIVIVSSGAAVRV--FPAWAAYCC 152
Cdd:PLN02780 131 LDVGVLinNVGVSYPYARfFHEVDEELLKNLIKVNVEGTTKVTQAVLPGmLKRKKGAIINIGSGAAIVIpsDPLYAVYAA 210


                 ....*.
gi 19113072  153 SKAAIN 158
Cdd:PLN02780 211 TKAYID 216
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 7-229 7.24e-05

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 42.92  E-value: 7.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRS---LTPELETLLIQNPDSFVHVKGDVTEvgKASIETAIKKF---GKL 79
Cdd:PRK08339   9 KLAFTTASSKGIGFGVARVLARAgADVILLSRNeenLKKAREKIKSESNVDVSYIVADLTK--REDLERTVKELkniGEP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHL-RKTKGTIVIVSSGAAVRVFPAWAAYCCSKAAIN 158
Cdd:PRK08339  87 DIFFFSTGGPKP-GYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMeRKGFGRIIYSTSVAIKEPIPNIALSNVVRISMA 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113072  159 MLVMNLGSE-EPDIMSV-AVRPGVVDTPMQVSIRNDSNKEAmGGDTHNFFKELKT---SGQLVAPQDIAKALSFLA 229
Cdd:PRK08339 166 GLVRTLAKElGPKGITVnGIMPGIIRTDRVIQLAQDRAKRE-GKSVEEALQEYAKpipLGRLGEPEEIGYLVAFLA 240
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-238 1.07e-04

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 42.20  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKVIAVSRSLTPELETLLIQNPDSFVHVKGDVT--EVGKASIETAIKKFGKLDSVI 83
Cdd:PRK12481   9 KVAIITGCNTGLGQGMAIGLAKAgADIVGVGVAEAPETQAQVEALGRKFHFITADLIqqKDIDSIVSQAVEVMGHIDILI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAGVL--EPIAKIADADineWRKLFDIN----FFSVVETVKYAIPhlRKTKGTIVIVSS----GAAVRVfpawAAYCCS 153
Cdd:PRK12481  89 NNAGIIrrQDLLEFGNKD---WDDVININqktvFFLSQAVAKQFVK--QGNGGKIINIASmlsfQGGIRV----PSYTAS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  154 KAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMQVSIRNDSNKEAMggdthnfFKELKTSGQLVAPQDIAKALSFLALN 231
Cdd:PRK12481 160 KSAVMGLTRALATElsQYNINVNAIAPGYMATDNTAALRADTARNEA-------ILERIPASRWGTPDDLAGPAIFLSSS 232


                 ....*..
gi 19113072  232 NNPKLTG 238
Cdd:PRK12481 233 ASDYVTG 239
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 7-139 1.38e-04

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 42.37  E-value: 1.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   7 KVILLTGSSKGIGLATAEAL------QKKAKVIAVSRSLtPELET----LLIQNPDS-----FVHVK-GDVTEVGKASIE 70
Cdd:cd08941   2 KVVLVTGANSGLGLAICERLlaeddeNPELTLILACRNL-QRAEAacraLLASHPDArvvfdYVLVDlSNMVSVFAAAKE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072  71 TAiKKFGKLDSVILNAGvlepiakIADADINEWRKLFDINFFSVVETVKyaIPHLRKTKGTIVIVSSGA 139
Cdd:cd08941  81 LK-KRYPRLDYLYLNAG-------IMPNPGIDWIGAIKEVLTNPLFAVT--NPTYKIQAEGLLSQGDKA 139
PRK07578 PRK07578
short chain dehydrogenase; Provisional
 9-101 2.02e-04

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 40.95  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    9 ILLTGSSKGIGLATAEALQKKAKVIAVSRSltpeletlliqnpDSFVHVkgDVTEvgKASIETAIKKFGKLDSVILNAGV 88
Cdd:PRK07578   3 ILVIGASGTIGRAVVAELSKRHEVITAGRS-------------SGDVQV--DITD--PASIRALFEKVGKVDAVVSAAGK 65

                         90
                 ....*....|....*
gi 19113072   89 LE--PIAKIADADIN 101
Cdd:PRK07578  66 VHfaPLAEMTDEDFN 80
PRK08017 PRK08017
SDR family oxidoreductase;
6-157 3.51e-04

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 40.84  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    6 EKVILLTGSSKGIGLATAEALQKKA-KVIAVSRsltpELETLLIQNPDSFVHVKGDVTEvgKASIETAIKKF-----GKL 79
Cdd:PRK08017   2 QKSVLITGCSSGIGLEAALELKRRGyRVLAACR----KPDDVARMNSLGFTGILLDLDD--PESVERAADEVialtdNRL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAG--VLEPIAKIADAdinEWRKLFDINFFSVVETVKYAIPHLRKT-KGTIVIVSSGAAVRVFPAWAAYCCSKAA 156
Cdd:PRK08017  76 YGLFNNAGfgVYGPLSTISRQ---QMEQQFSTNFFGTHQLTMLLLPAMLPHgEGRIVMTSSVMGLISTPGRGAYAASKYA 152


                 .
gi 19113072  157 I 157
Cdd:PRK08017 153 L 153
PRK06953 PRK06953
SDR family oxidoreductase;
7-185 5.60e-04

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 40.06  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKA-KVIAVSRslTPE----LETLliqnpDSFVHVKgDVTEvgKASIETAIKKFG--KL 79
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGwRVIATAR--DAAalaaLQAL-----GAEALAL-DVAD--PASVAGLAWKLDgeAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   80 DSVILNAGVLEP----IAKIADADinewrklFDINFFSVVETVKYAIPHL----RKTKGTIVIVSSG----AAVRVFPAW 147
Cdd:PRK06953  72 DAAVYVAGVYGPrtegVEPITRED-------FDAVMHTNVLGPMQLLPILlplvEAAGGVLAVLSSRmgsiGDATGTTGW 144

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19113072  148 AaYCCSKAAINMLVMNLGSEEPDIMSVAVRPGVVDTPM 185
Cdd:PRK06953 145 L-YRASKAALNDALRAASLQARHATCIALHPGWVRTDM 181
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 7-107 9.51e-04

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: 39.00  E-value: 9.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072      7 KVILLTGSSKGIGLATAEALQKK--AKVIAVSRSLTP-----ELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFG 77
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERgaRRLVLLSRSGPDapgaaALLAELEAAGARVTVVACDVADRDalAAVLAAIPAVEG 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 19113072     78 KLDSVILNAGVLEPiAKIADADINEWRKLF 107
Cdd:smart00822  81 PLTGVIHAAGVLDD-GVLASLTPERFAAVL 109
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 10-107 2.55e-03

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: 37.54  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    10 LLTGSSKGIGLATAEAL-QKKAK-VIAVSRSLTP-----ELETLLIQNPDSFVHVKGDVTEvgKASIETAI----KKFGK 78
Cdd:pfam08659   4 LITGGLGGLGRELARWLaERGARhLVLLSRSAAPrpdaqALIAELEARGVEVVVVACDVSD--PDAVAALLaeikAEGPP 81

                          90       100
                  ....*....|....*....|....*....
gi 19113072    79 LDSVILNAGVLEPiAKIADADINEWRKLF 107
Cdd:pfam08659  82 IRGVIHAAGVLRD-ALLENMTDEDWRRVL 109
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-241 2.93e-03

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 38.23  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    1 MAETAEKVILLTGSS--KGIGLATAEALQKKAKVI------AVSRSLT--------PELETLLIQNPDSFVHVKGDVT-- 62
Cdd:PRK12859   1 MNQLKNKVAVVTGVSrlDGIGAAICKELAEAGADIfftywtAYDKEMPwgvdqdeqIQLQEELLKNGVKVSSMELDLTqn 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   63 EVGKASIETAIKKFGKLDSVILNAgvlepiAKIADADINEW-RKLFDINFFSVVE-----TVKYAIPHLRKTKGTIVIVS 136
Cdd:PRK12859  81 DAPKELLNKVTEQLGYPHILVNNA------AYSTNNDFSNLtAEELDKHYMVNVRattllSSQFARGFDKKSGGRIINMT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072  137 SGAAVRVFPAWAAYCCSKAAINMLVMNLGSE--EPDIMSVAVRPGVVDTPMqvsirndsnkeaMGGDTHNFFKELKTSGQ 214
Cdd:PRK12859 155 SGQFQGPMVGELAYAATKGAIDALTSSLAAEvaHLGITVNAINPGPTDTGW------------MTEEIKQGLLPMFPFGR 222

                        250       260
                 ....*....|....*....|....*..
gi 19113072  215 LVAPQDIAKALSFLALNNNPKLTGQFV 241
Cdd:PRK12859 223 IGEPKDAARLIKFLASEEAEWITGQII 249
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 9-159 2.96e-03

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 37.99  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    9 ILLTGSSKGIGLATAEA-LQKKAKVIAVSRSLTPELETLliqNPDSFVHVKGDVTEvgKASIETAIKKF----GKLDSVI 83
Cdd:PRK06483   5 ILITGAGQRIGLALAWHlLAQGQPVIVSYRTHYPAIDGL---RQAGAQCIQADFST--NAGIMAFIDELkqhtDGLRAII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAGvlepiAKIADADINEWRKLFDiNFFSVVETVKYAI-----PHLRK---TKGTIVIVSSGAAVRVFPAWAAYCCSKA 155
Cdd:PRK06483  80 HNAS-----DWLAEKPGAPLADVLA-RMMQIHVNAPYLLnlaleDLLRGhghAASDIIHITDYVVEKGSDKHIAYAASKA 153


                 ....*
gi 19113072  156 AI-NM 159
Cdd:PRK06483 154 ALdNM 158
PRK07791 PRK07791
short chain dehydrogenase; Provisional
 7-157 3.60e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 37.73  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKK-AKV----IAVSRSLTPELETLLIQNPDSFVHVKG-------DVTEVGKAS--IETA 72
Cdd:PRK07791   7 RVVIVTGAGGGIGRAHALAFAAEgARVvvndIGVGLDGSASGGSAAQAVVDEIVAAGGeavangdDIADWDGAAnlVDAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   73 IKKFGKLDSVILNAGVLEPiAKIADADINEWRKLFDINFFSVVETVKYAIPHLR-KTK------GTIVIVSSGAAVRVFP 145
Cdd:PRK07791  87 VETFGGLDVLVNNAGILRD-RMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRaESKagravdARIINTSSGAGLQGSV 165

                        170
                 ....*....|..
gi 19113072  146 AWAAYCCSKAAI 157
Cdd:PRK07791 166 GQGNYSAAKAGI 177
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-229 6.49e-03

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 37.16  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    7 KVILLTGSSKGIGLATAEALQKKA-KVIAVSRSLTPELETLLIQNPDSFVHVKGDVTEVG--KASIETAIKKFGKLDSVI 83
Cdd:PRK08993  11 KVAVVTGCDTGLGQGMALGLAEAGcDIVGINIVEPTETIEQVTALGRRFLSLTADLRKIDgiPALLERAVAEFGHIDILV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072   84 LNAGVLEPIAKIADADINeWRKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSS----GAAVRVfpawAAYCCSKAAI 157
Cdd:PRK08993  91 NNAGLIRREDAIEFSEKD-WDDVMNLNIKSVFFMSQAAAKHFiaQGNGGKIINIASmlsfQGGIRV----PSYTASKSGV 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113072  158 nMLVMNLGSEE---PDIMSVAVRPGVVDTPMQVSIRNDS--NKEAMggdthnffkELKTSGQLVAPQDIAKALSFLA 229
Cdd:PRK08993 166 -MGVTRLMANEwakHNINVNAIAPGYMATNNTQQLRADEqrSAEIL---------DRIPAGRWGLPSDLMGPVVFLA 232
PRK08340 PRK08340
SDR family oxidoreductase;
9-137 7.81e-03

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 36.71  E-value: 7.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113072    9 ILLTGSSKGIGLATAEALQKKAKVIAVSRSLTPELETLLIQ-NPDSFVH-VKGDVTEvgKASIETAIKK----FGKLDSV 82
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKElKEYGEVYaVKADLSD--KDDLKNLVKEawelLGGIDAL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113072   83 ILNAGVL--EPiAKIADADINEWRKLFDINFFSVVETVKYAIPHL--RKTKGTIVIVSS 137
Cdd:PRK08340  81 VWNAGNVrcEP-CMLHEAGYSDWLEAALLHLVAPGYLTTLLIQAWleKKMKGVLVYLSS 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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