NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20128793|ref|NP_569835|]
View 

uncharacterized protein Dmel_CG13377, isoform A [Drosophila melanogaster]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 46-237 4.26e-24

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05374:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 248  Bit Score: 98.46  E-value: 4.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVFAGMKeaqdslpakllcGWMKIREYSEEPIAGtIIPMRLDVTREDVLREATVI 125
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATAR------------NPDKLESLGELLNDN-LEVLELDVTDEESIKAAVKE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 126 IGANlnadERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGGGNARNE 204
Cdd:cd05374  68 VIER----FGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFL 143

                       170       180       190
                ....*....|....*....|....*....|...
gi 20128793 205 GdglvAFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:cd05374 144 G----PYCASKAALEALSESLRLELAPFGIKVT 172
 
Name Accession Description Interval E-value
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 46-237 4.26e-24

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: 98.46  E-value: 4.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVFAGMKeaqdslpakllcGWMKIREYSEEPIAGtIIPMRLDVTREDVLREATVI 125
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATAR------------NPDKLESLGELLNDN-LEVLELDVTDEESIKAAVKE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 126 IGANlnadERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGGGNARNE 204
Cdd:cd05374  68 VIER----FGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFL 143

                       170       180       190
                ....*....|....*....|....*....|...
gi 20128793 205 GdglvAFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:cd05374 144 G----PYCASKAALEALSESLRLELAPFGIKVT 172
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 42-240 1.86e-19

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: 85.62  E-value: 1.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  42 SHPSRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQdslpakllcgwmKIREYSEEpIAGTIIPMRLDVTREDVLRE 121
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAE------------RLEALAAE-LGGRALAVPLDVTDEAAVEA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 122 ATviigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPT-RGRLLYLGGVSGggn 200
Cdd:COG4221  69 AV----AAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARgSGHIVNISSIAG--- 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20128793 201 aRNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVALD 240
Cdd:COG4221 142 -LRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIE 180
PRK06914 PRK06914
SDR family oxidoreductase;
46-237 2.13e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 72.36  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRVFAGMKEaqdslPAKllcgwmkiREYSEEPIAGTIIPMRLDVTREDVLREATVi 125
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRN-----PEK--------QENLLSQATQLNLQQNIKVQQLDVTDQNSI- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  126 igANLNADERGIAAV---INTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGggna 201
Cdd:PRK06914  70 --HNFQLVLKEIGRIdllVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISG---- 143

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 20128793  202 RNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:PRK06914 144 RVGFPGLSPYVSSKYALEGFSESLRLELKPFGIDVA 179
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 46-246 9.67e-14

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 68.79  E-value: 9.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793    46 RVVLITSADTALGLQLCTHLANKGYRVFAGmkeaqDSLPAKLLCGWMKIREyseepIAGTIIPMRLDVTREDVLREATVI 125
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLV-----DRSEEKLEAVAKELGA-----LGGKALFIQGDVTDRAQVKALVEQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   126 IGANLnadeRGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLLYLGGVSGggnaRNE 204
Cdd:pfam00106  71 AVERL----GRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAG----LVP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 20128793   205 GDGLVAFNASRVAVDKCAEELRKELHPYGVSVVALdTCGMTA 246
Cdd:pfam00106 143 YPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAV-APGGVD 183
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 46-181 3.62e-03

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: 37.85  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793     46 RVVLITSADTALGLQLCTHLANKGYR--VFAGMKEAQDSLPAKLLcgwMKIREYSEEPIAgtiipMRLDVTREDVLREAT 123
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARrlVLLSRSGPDAPGAAALL---AELEAAGARVTV-----VACDVADRDALAAVL 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20128793    124 viigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKA--------FVCF 181
Cdd:smart00822  73 ----AAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELtadlpldfFVLF 134
 
Name Accession Description Interval E-value
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 46-237 4.26e-24

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: 98.46  E-value: 4.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVFAGMKeaqdslpakllcGWMKIREYSEEPIAGtIIPMRLDVTREDVLREATVI 125
Cdd:cd05374   1 KVVLITGCSSGIGLALALALAAQGYRVIATAR------------NPDKLESLGELLNDN-LEVLELDVTDEESIKAAVKE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 126 IGANlnadERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGGGNARNE 204
Cdd:cd05374  68 VIER----FGRIDVLVNNAGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGsGRIVNVSSVAGLVPTPFL 143

                       170       180       190
                ....*....|....*....|....*....|...
gi 20128793 205 GdglvAFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:cd05374 144 G----PYCASKAALEALSESLRLELAPFGIKVT 172
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 42-240 1.86e-19

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: 85.62  E-value: 1.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  42 SHPSRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQdslpakllcgwmKIREYSEEpIAGTIIPMRLDVTREDVLRE 121
Cdd:COG4221   2 SDKGKVALITGASSGIGAATARALAAAGARVVLAARRAE------------RLEALAAE-LGGRALAVPLDVTDEAAVEA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 122 ATviigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPT-RGRLLYLGGVSGggn 200
Cdd:COG4221  69 AV----AAAVAEFGRLDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARgSGHIVNISSIAG--- 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20128793 201 aRNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVALD 240
Cdd:COG4221 142 -LRPYPGGAVYAATKAAVRGLSESLRAELRPTGIRVTVIE 180
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
42-239 2.28e-17

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 80.30  E-value: 2.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  42 SHPSRVVLITSADTALGLQLCTHLANKGYRVFA------GMKEAQDSLPAKllcgwmkireyseepiAGTIIPMRLDVTR 115
Cdd:COG0300   2 SLTGKTVLITGASSGIGRALARALAARGARVVLvardaeRLEALAAELRAA----------------GARVEVVALDVTD 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 116 EDVLREAtviiGANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPT-RGRLLYLGG 194
Cdd:COG0300  66 PDAVAAL----AEAVLARFGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARgRGRIVNVSS 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20128793 195 VSG-GGNArnegdGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:COG0300 142 VAGlRGLP-----GMAAYAASKAALEGFSESLRAELAPTGVRVTAV 182
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 46-236 2.33e-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: 75.01  E-value: 2.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVFAG--MKEAQDSLPAKLLC-GWMKIreyseepiagtiipMRLDVTREDVLREA 122
Cdd:cd09805   1 KAVLITGCDSGFGNLLAKKLDSLGFTVLAGclTKNGPGAKELRRVCsDRLRT--------------LQLDVTKPEQIKRA 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 123 TVIIGANLNadERGIAAVINTSG-SVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLLYLGgvSGGGNA 201
Cdd:cd09805  67 AQWVKEHVG--EKGLWGLVNNAGiLGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRRAKGRVVNVS--SMGGRV 142

                       170       180       190
                ....*....|....*....|....*....|....*
gi 20128793 202 RNEGDGlvAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:cd09805 143 PFPAGG--AYCASKAAVEAFSDSLRRELQPWGVKV 175
PRK06914 PRK06914
SDR family oxidoreductase;
46-237 2.13e-14

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 72.36  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRVFAGMKEaqdslPAKllcgwmkiREYSEEPIAGTIIPMRLDVTREDVLREATVi 125
Cdd:PRK06914   4 KIAIVTGASSGFGLLTTLELAKKGYLVIATMRN-----PEK--------QENLLSQATQLNLQQNIKVQQLDVTDQNSI- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  126 igANLNADERGIAAV---INTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGggna 201
Cdd:PRK06914  70 --HNFQLVLKEIGRIdllVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKsGKIINISSISG---- 143

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 20128793  202 RNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:PRK06914 144 RVGFPGLSPYVSSKYALEGFSESLRLELKPFGIDVA 179
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 46-259 7.85e-14

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: 69.70  E-value: 7.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQDSlpakllcGWMKIREYSEEPIAgtiipmrLDVTreDVLREATVI 125
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPEDL-------AALSASGGDVEAVP-------YDAR--DPEDARALV 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 126 IGANLNADerGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRP-TRGRLLYLGGVSGGGNARne 204
Cdd:cd08932  65 DALRDRFG--RIDVLVHNAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREaGSGRVVFLNSLSGKRVLA-- 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 205 gdGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL-----DTCGMTAESLYKAPVAQTMS 259
Cdd:cd08932 141 --GNAGYSASKFALRALAHALRQEGWDHGVRVSAVcpgfvDTPMAQGLTLVGAFPPEEMI 198
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 46-246 9.67e-14

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 68.79  E-value: 9.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793    46 RVVLITSADTALGLQLCTHLANKGYRVFAGmkeaqDSLPAKLLCGWMKIREyseepIAGTIIPMRLDVTREDVLREATVI 125
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLV-----DRSEEKLEAVAKELGA-----LGGKALFIQGDVTDRAQVKALVEQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   126 IGANLnadeRGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLLYLGGVSGggnaRNE 204
Cdd:pfam00106  71 AVERL----GRLDILVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLpAMIKGSGGRIVNISSVAG----LVP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 20128793   205 GDGLVAFNASRVAVDKCAEELRKELHPYGVSVVALdTCGMTA 246
Cdd:pfam00106 143 YPGGSAYSASKAAVIGFTRSLALELAPHGIRVNAV-APGGVD 183
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 46-239 9.60e-13

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: 66.73  E-value: 9.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVF------AGMKEAQDSLPAKllcgwmkireyseepiAGTIIPMRLDVTREDVL 119
Cdd:COG1028   7 KVALVTGGSSGIGRAIARALAAEGARVVitdrdaEALEAAAAELRAA----------------GGRALAVAADVTDEAAV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 120 REATviigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGg 198
Cdd:COG1028  71 EALV----AAAVAAFGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGgGRIVNISSIAG- 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20128793 199 gnaRNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:COG1028 146 ---LRGSPGQAAYAASKAAVVGLTRSLALELAPRGIRVNAV 183
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 48-239 5.89e-12

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: 64.61  E-value: 5.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  48 VLITSADTALGLQLCTHLANKGYRVF-AGMKEAQdslpakllcgwmKIREYSEEPIAGTIIPMRLDVTREDVLREATVII 126
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVlADRNEEA------------LAELAAIEALGGNAVAVQADVSDEEDVEALVEEA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 127 GANLNaderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLLYLGGVSGGGNARneg 205
Cdd:cd05233  69 LEEFG----RLDILVNNAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALpHMKKQGGGRIVNISSVAGLRPLP--- 141

                       170       180       190
                ....*....|....*....|....*....|....
gi 20128793 206 dGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:cd05233 142 -GQAAYAASKAALEGLTRSLALELAPYGIRVNAV 174
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 46-236 1.95e-10

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 60.27  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRVF-------AGMKEAQDSLPAkllcgwmkireyseepIAGTIIPMRLDVTREDV 118
Cdd:PRK12825   7 RVALVTGAARGLGRAIALRLARAGADVVvhyrsdeEAAEELVEAVEA----------------LGRRAQAVQADVTDKAA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  119 LREAtviiGANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGgvSG 197
Cdd:PRK12825  71 LEAA----VAAAVERFGRIDILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRgGRIVNIS--SV 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 20128793  198 GGNARNegDGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK12825 145 AGLPGW--PGRSNYAAAKAGLVGLTKALARELAEYGITV 181
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 48-240 3.87e-10

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: 59.23  E-value: 3.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  48 VLITSADTALGLQLCTHLANKGY-RVFAGM--KEAQDSLPAkllcgwmkireysEEPIAGTIIPMRLDVTreDVLREATV 124
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNnTVIATCrdPSAATELAA-------------LGASHSRLHILELDVT--DEIAESAE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 125 IIGANLNadERGIAAVINTSGsVF--RGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRP-TRGRLLYLGGVSGGGNA 201
Cdd:cd05325  66 AVAERLG--DAGLDVLINNAG-ILhsYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKgARAKIINISSRVGSIGD 142

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20128793 202 rNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVALD 240
Cdd:cd05325 143 -NTSGGWYSYRASKAALNMLTKSLAVELKRDGITVVSLH 180
PRK05693 PRK05693
SDR family oxidoreductase;
47-237 5.66e-10

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 59.03  E-value: 5.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   47 VVLITSADTALGLQLCTHLANKGYRVFAGMKEAQDSlpakllcgwmkireysEEPIAGTIIPMRLDVTREDVLREatviI 126
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDV----------------EALAAAGFTAVQLDVNDGAALAR----L 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  127 GANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLLYLGGVSGGGNARNEGd 206
Cdd:PRK05693  63 AEELEAEHGGLDVLINNAGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRSRGLVVNIGSVSGVLVTPFAG- 141

                        170       180       190
                 ....*....|....*....|....*....|.
gi 20128793  207 glvAFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:PRK05693 142 ---AYCASKAAVHALSDALRLELAPFGVQVM 169
PRK05650 PRK05650
SDR family oxidoreductase;
48-236 6.98e-10

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 58.90  E-value: 6.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   48 VLITSADTALGLQLCTHLANKGYRV-FAGMKEAQDSLPAKLLcgwmkireysEEPIAGTIIpMRLDVTREDVLREATVII 126
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRLaLADVNEEGGEETLKLL----------REAGGDGFY-QRCDVRDYSQLTALAQAC 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  127 GANLNaderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLLYLGGVSGggnaRNEG 205
Cdd:PRK05650  72 EEKWG----GIDVIVNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLpLFKRQKSGRIVNIASMAG----LMQG 143

                        170       180       190
                 ....*....|....*....|....*....|.
gi 20128793  206 DGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK05650 144 PAMSSYNVAKAGVVALSETLLVELADDEIGV 174
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 46-239 7.08e-10

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 58.27  E-value: 7.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRVFA---GMKEAQDSLPAkllcgwmkireyseepiagtIIPMRLDVTREDVL-RE 121
Cdd:PRK12828   8 KVVAITGGFGGLGRATAAWLAARGARVALigrGAAPLSQTLPG--------------------VPADALRIGGIDLVdPQ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  122 ATVIIGANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFL-RPTRGRLLylggVSGGGN 200
Cdd:PRK12828  68 AARRAVDEVNRQFGRLDALVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALtASGGGRIV----NIGAGA 143

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 20128793  201 ARNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:PRK12828 144 ALKAGPGMGAYAAAKAGVARLTEALAAELLDRGITVNAV 182
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 42-239 1.31e-09

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 58.00  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   42 SHPSRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQDslpakllcgwmkiREYSEEPIAGTIIPMRLDVTR----ED 117
Cdd:PRK06180   1 MSSMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAA-------------RADFEALHPDRALARLLDVTDfdaiDA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  118 VLREATVIIGAnlnadergIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLggVS 196
Cdd:PRK06180  68 VVADAEATFGP--------IDVLVNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRrGHIVNI--TS 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 20128793  197 GGGNARNEGDGlvAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:PRK06180 138 MGGLITMPGIG--YYCGSKFALEGISESLAKEVAPFGIHVTAV 178
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 48-240 2.36e-09

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: 56.90  E-value: 2.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  48 VLITSADTALGLQLCTHLANKGYRVF-AG-----MKEAQDSLPAKLlcgwmkireyseepiAGTIIPMRLDVTREDVLRE 121
Cdd:cd05346   3 VLITGASSGIGEATARRFAKAGAKLIlTGrraerLQELADELGAKF---------------PVKVLPLQLDVSDRESIEA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 122 ATviigANLNADERGIAAVINTSGSVfRG--QVESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLLYLGGVSG- 197
Cdd:cd05346  68 AL----ENLPEEFRDIDILVNNAGLA-LGldPAQEADLEDWETMIDTNVKGLLNVTRLILpIMIARNQGHIINLGSIAGr 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20128793 198 ----GGNarnegdglvAFNASRVAVDKCAEELRKELHPYGVSVVALD 240
Cdd:cd05346 143 ypyaGGN---------VYCATKAAVRQFSLNLRKDLIGTGIRVTNIE 180
PRK07326 PRK07326
SDR family oxidoreductase;
46-237 1.81e-08

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 54.25  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRV------FAGMKEAQDSLPAKllcgwmkireyseepiaGTIIPMRLDVTREDVL 119
Cdd:PRK07326   7 KVALITGGSKGIGFAIAEALLAEGYKVaitardQKELEEAAAELNNK-----------------GNVLGLAADVRDEADV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  120 REATviigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLLYLGGVSGgg 199
Cdd:PRK07326  70 QRAV----DAIVAAFGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGGGYIINISSLAG-- 143

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 20128793  200 naRNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:PRK07326 144 --TNFFAGGAAYNASKFGLVGFSEAAMLDLRQYGIKVS 179
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 48-265 3.81e-07

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: 50.20  E-value: 3.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  48 VLITSADTALGLQLCTHLANKGYRVF------AGMKEAQDSLPAKLLcgwmkireyseePIAGtiipmrlDVTREDVLRE 121
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGicardeARLAAAAAQELEGVL------------GLAG-------DVRDEADVRR 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 122 AtviIGANLNADErGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVA-KAFVCFLRPTRGRLLYLGGVSGggn 200
Cdd:cd08929  64 A---VDAMEEAFG-GLDALVNNAGVGVMKPVEELTPEEWRLVLDTNLTGAFYCIhKAAPALLRRGGGTIVNVGSLAG--- 136

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20128793 201 aRNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSV-------VALDTCGMTAESLYK-AP--VAQTMSLVVGAP 265
Cdd:cd08929 137 -KNAFKGGAAYNASKFGLLGLSEAAMLDLREANIRVvnvmpgsVDTGFAGSPEGQAWKlAPedVAQAVLFALEMP 210
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
44-236 4.76e-07

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 50.15  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   44 PSRVVLITSADTALGLQLCTHLANKGYRV----FAGMKEAQDslpakllcgWMKIREYSEEPIAGtiipMRLDVTREDVL 119
Cdd:PRK12824   1 MKKIALVTGAKRGIGSAIARELLNDGYRViatyFSGNDCAKD---------WFEEYGFTEDQVRL----KELDVTDTEEC 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  120 REATviigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVsgg 198
Cdd:PRK12824  68 AEAL----AEIEEEEGPVDILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGyGRIINISSV--- 140

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 20128793  199 gNARNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK12824 141 -NGLKGQFGQTNYSAAKAGMIGFTKALASEGARYGITV 177
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 45-241 5.16e-07

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 49.63  E-value: 5.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  45 SRVVLITSADTALGLQLCTHLANKGYRVfAGMKEAQdslpakllcgwmkireySEEPIAGTIIPMrldvTREDVLREATV 124
Cdd:cd05334   1 ARVVLVYGGRGALGSAVVQAFKSRGWWV-ASIDLAE-----------------NEEADASIIVLD----SDSFTEQAKQV 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 125 IigANLNADERGIAAVINTSGSVFRGQVESQN-VQQWEHMLRTNILGTLRVAKAFVCFLRPtrGRLLYLGGVSGGGNArn 203
Cdd:cd05334  59 V--ASVARLSGKVDALICVAGGWAGGSAKSKSfVKNWDLMWKQNLWTSFIASHLATKHLLS--GGLLVLTGAKAALEP-- 132

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20128793 204 eGDGLVAFNASRVAVDKCAEELRKELH--PYGVSVVA-----LDT 241
Cdd:cd05334 133 -TPGMIGYGAAKAAVHQLTQSLAAENSglPAGSTANAilpvtLDT 176
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 48-239 7.25e-07

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: 49.37  E-value: 7.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  48 VLITSADTALGLQLCTHLANKGYRVFA------GMKEAQDSLPAKllCGWMKireyseepiagtiipmRLDVTREDVLRE 121
Cdd:cd08931   3 IFITGAASGIGRETALLFARNGWFVGLydidedGLAALAAELGAE--NVVAG----------------ALDVTDRAAWAA 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 122 ATVIIGANLNAderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLLYLGGVSGG--G 199
Cdd:cd08931  65 ALADFAAATGG---RLDALFNNAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAiyG 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20128793 200 NARnegdgLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:cd08931 142 QPD-----LAVYSATKFAVRGLTEALDVEWARHGIRVADV 176
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 46-272 1.95e-06

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: 48.17  E-value: 1.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLC-THLANKGYRVFAGMKEaQDSLpakllcgwmkiREYSEEPIAGtIIPMRLDVTredvlrEATV 124
Cdd:cd05354   4 KTVLVTGANRGIGKAFVeSLLAHGAKKVYAAVRD-PGSA-----------AHLVAKYGDK-VVPLRLDVT------DPES 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 125 IIGANLNADErgIAAVINTSG-SVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFL-RPTRGRLLYLGGVSGGGNAR 202
Cdd:cd05354  65 IKAAAAQAKD--VDVVINNAGvLKPATLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLkANGGGAIVNLNSVASLKNFP 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 203 NEGdglvAFNASRVAVDKCAEELRKELHPYGVSVValdtcgmtaeSLYKAPVAQTMSLVVGAPTQYTADV 272
Cdd:cd05354 143 AMG----TYSASKSAAYSLTQGLRAELAAQGTLVL----------SVHPGPIDTRMAAGAGGPKESPETV 198
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 46-236 2.84e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 48.04  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRV-FAGMKEAQDSLPAKLLCGwmkireyseepiAGTIIPMRLDVTREDVLREATV 124
Cdd:PRK05872  10 KVVVVTGAARGIGAELARRLHARGAKLaLVDLEEAELAALAAELGG------------DDRVLTVVADVTDLAAMQAAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  125 iiganlNADER--GIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLLYLGGVSGGGNAr 202
Cdd:PRK05872  78 ------EAVERfgGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERRGYVLQVSSLAAFAAA- 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 20128793  203 negDGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK05872 151 ---PGMAAYCASKAGVEAFANALRLEVAHHGVTV 181
PRK06181 PRK06181
SDR family oxidoreductase;
46-236 3.28e-06

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 47.67  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYR-VFAGMKEAQ-DSLPAKLlcgwmkiREYSEEPIAgtiipMRLDVTREDVLREAT 123
Cdd:PRK06181   2 KVVIITGASEGIGRALAVRLARAGAQlVLAARNETRlASLAQEL-------ADHGGEALV-----VPTDVSDAEACERLI 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  124 VIIGANLNaderGIAAVINTSGSVFRGQVESQNVQQW-EHMLRTNILGTLRVAKAFVCFLRPTRGRLLYLGGVSG--GGN 200
Cdd:PRK06181  70 EAAVARFG----GIDILVNNAGITMWSRFDELTDLSVfERVMRVNYLGAVYCTHAALPHLKASRGQIVVVSSLAGltGVP 145

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 20128793  201 ARNegdglvAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK06181 146 TRS------GYAASKHALHGFFDSLRIELADDGVAV 175
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 46-252 3.30e-06

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: 47.79  E-value: 3.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRV-FAGMKEAQDSLPAKLLCGwmkiREYSEEPIagTIIPMrlDVTREDVLREatv 124
Cdd:cd05364   4 KVAIITGSSSGIGAGTAILFARLGARLaLTGRDAERLEETRQSCLQ----AGVSEKKI--LLVVA--DLTEEEGQDR--- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 125 IIGANLNADERgIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLLYLGGVSGGgnarNE 204
Cdd:cd05364  73 IISTTLAKFGR-LDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKTKGEIVNVSSVAGG----RS 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20128793 205 GDGLVAFNASRVAVDKCAEELRKELHPYGVSVVALDTcGMTAESLYKA 252
Cdd:cd05364 148 FPGVLYYCISKAALDQFTRCTALELAPKGVRVNSVSP-GVIVTGFHRR 194
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 45-237 3.31e-06

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 47.59  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   45 SRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQDSlpakllcgwmkireyseEPIAG-TIIPMrlDVTREDVLREA- 122
Cdd:PRK06179   4 SKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARA-----------------APIPGvELLEL--DVTDDASVQAAv 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  123 -TVIiganlnaDERG-IAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSggg 199
Cdd:PRK06179  65 dEVI-------ARAGrIDVLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGsGRIINISSVL--- 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20128793  200 narnegdGLV------AFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:PRK06179 135 -------GFLpapymaLYAASKHAVEGYSESLDHEVRQFGIRVS 171
PRK08017 PRK08017
SDR family oxidoreductase;
48-236 5.29e-06

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 47.00  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   48 VLITSADTALGLQLCTHLANKGYRVFAGMKEAQDSlpakllcgwMKIREYSEEPIAgtiipMRLDvTREDVLREATVIIG 127
Cdd:PRK08017   5 VLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV---------ARMNSLGFTGIL-----LDLD-DPESVERAADEVIA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  128 ANLNAdergIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPT-RGRLLYLGGVSGGGNARNEGd 206
Cdd:PRK08017  70 LTDNR----LYGLFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHgEGRIVMTSSVMGLISTPGRG- 144

                        170       180       190
                 ....*....|....*....|....*....|
gi 20128793  207 glvAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK08017 145 ---AYAASKYALEAWSDALRMELRHSGIKV 171
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 45-236 7.07e-06

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 46.95  E-value: 7.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   45 SRVVLITSADTALGLQLCTHLANKGYRVFAgmkEAQDSLPAKLLCgwmkireyseEPIAGTIIPMRLDVTREDVLREATv 124
Cdd:PRK08263   3 EKVWFITGASRGFGRAWTEAALERGDRVVA---TARDTATLADLA----------EKYGDRLLPLALDVTDRAAVFAAV- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  125 iiganlnadERGIAA------VINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSG 197
Cdd:PRK08263  69 ---------ETAVEHfgrldiVVNNAGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRsGHIIQISSIGG 139

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 20128793  198 GGNARNEGdglvAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK08263 140 ISAFPMSG----IYHASKWALEGMSEALAQEVAEFGIKV 174
PRK06482 PRK06482
SDR family oxidoreductase;
45-237 7.18e-06

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 46.65  E-value: 7.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   45 SRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQ--DSLPAKllcgwmkireYSEepiAGTIIPmrLDVTREDVLREa 122
Cdd:PRK06482   2 SKTWFITGASSGFGRGMTERLLARGDRVAATVRRPDalDDLKAR----------YGD---RLWVLQ--LDVTDSAAVRA- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  123 tvIIGANLNADERgIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGgvSGGGNA 201
Cdd:PRK06482  66 --VVDRAFAALGR-IDVVVSNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGgGRIVQVS--SEGGQI 140

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 20128793  202 RNEGDGLvaFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:PRK06482 141 AYPGFSL--YHATKWGIEGFVEAVAQEVAPFGIEFT 174
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 48-236 1.13e-05

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: 45.78  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  48 VLITSADTALGLQLCTHLANKGYRVF--AGMKEAQDSLPAKLLCGwmkireyseepiAGTIIPMRLDVTREDVLREATVI 125
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVAlaARRTDRLDELKAELLNP------------NPSVEVEILDVTDEERNQLVIAE 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 126 IGANLNaderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLLYLGGVSGGGNARne 204
Cdd:cd05350  69 LEAELG----GLDLVIINAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALpQFRAKGRGHLVLISSVAALRGLP-- 142

                       170       180       190
                ....*....|....*....|....*....|..
gi 20128793 205 gdGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:cd05350 143 --GAAAYSASKAALSSLAESLRYDVKKRGIRV 172
PRK09291 PRK09291
SDR family oxidoreductase;
45-236 1.36e-05

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 45.76  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   45 SRVVLITSADTALGLQLCTHLANKGYRVFAGMKeaqdslpakllcGWMKIREYSEEPI-AGTIIPM-RLDVTRE-DVLRE 121
Cdd:PRK09291   2 SKTILITGAGSGFGREVALRLARKGHNVIAGVQ------------IAPQVTALRAEAArRGLALRVeKLDLTDAiDRAQA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  122 ATVIIGANLNAdergiaAVINTSGSVFRGQVEsqNV-QQWEhmlrTNILGTLRVAKAFVC-FLRPTRGRLLYLGGVSGgg 199
Cdd:PRK09291  70 AEWDVDVLLNN------AGIGEAGAVVDIPVE--LVrELFE----TNVFGPLELTQGFVRkMVARGKGKVVFTSSMAG-- 135

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 20128793  200 naRNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK09291 136 --LITGPFTGAYCASKHALEAIAEAMHAELKPFGIQV 170
PRK08264 PRK08264
SDR family oxidoreductase;
46-272 1.36e-05

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 45.65  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYR-VFAGmkeAQDslPAKLlcgwmkireyseEPIAGTIIPMRLDVTREDVLREAtv 124
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQLLARGAAkVYAA---ARD--PESV------------TDLGPRVVPLQLDVTDPASVAAA-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  125 iigANLNADergIAAVINTSGsVFRGQ--VESQNVQQWEHMLRTNILGTLRVAKAFVCFL-RPTRGRLL----YLGGVSG 197
Cdd:PRK08264  68 ---AEAASD---VTILVNNAG-IFRTGslLLEGDEDALRAEMETNYFGPLAMARAFAPVLaANGGGAIVnvlsVLSWVNF 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20128793  198 GGNArnegdglvAFNASRVAVDKCAEELRKELHPYGVSVValdtcgmtaeSLYKAPVAQTMSLVVGAPTQYTADV 272
Cdd:PRK08264 141 PNLG--------TYSASKAAAWSLTQALRAELAPQGTRVL----------GVHPGPIDTDMAAGLDAPKASPADV 197
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
46-236 1.84e-05

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 46.38  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRVF-AGMKEAQDSLPAKLLCGwmkireyseepiAGTIIPMRLDVTREDVLREA-- 122
Cdd:PRK08324 423 KVALVTGAAGGIGKATAKRLAAEGACVVlADLDEEAAEAAAAELGG------------PDRALGVACDVTDEAAVQAAfe 490

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  123 TVII--GanlnaderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLR--PTRGRLLYLGGVsgg 198
Cdd:PRK08324 491 EAALafG--------GVDIVVSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKaqGLGGSIVFIASK--- 559

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 20128793  199 gNARNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK08324 560 -NAVNPGPNFGAYGAAKAAELHLVRQLALELGPDGIRV 596
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 46-239 3.19e-05

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: 44.66  E-value: 3.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVF--AGMKEAQDSlpakllcgwmKIREYSEEPIagTIIPMRLDVTREDVLREAT 123
Cdd:cd05347   6 KVALVTGASRGIGFGIASGLAEAGANIVinSRNEEKAEE----------AQQLIEKEGV--EATAFTCDVSDEEAIKAAV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 124 viigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAK-AFVCFLRPTRGRLLYLGGVsgggNAR 202
Cdd:cd05347  74 ----EAIEEDFGKIDILVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQaVARHMIKQGHGKIINICSL----LSE 145

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20128793 203 NEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:cd05347 146 LGGPPVPAYAASKGGVAGLTKALATEWARHGIQVNAI 182
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
42-236 4.84e-05

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 44.00  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   42 SHPSRVVLITSADTALGLQLCTHLANKGYRVFAGM--KEAQDSLPAKLlcgwmkireyseEPIAGTIIPMRLDVTREDVL 119
Cdd:PRK05653   2 SLQGKTALVTGASRGIGRAIALRLAADGAKVVIYDsnEEAAEALAAEL------------RAAGGEARVLVFDVSDEAAV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  120 REAtviiganLNADER---GIAAVINTSGsVFR-GQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGG 194
Cdd:PRK05653  70 RAL-------IEAAVEafgALDILVNNAG-ITRdALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARyGRIVNISS 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 20128793  195 VSG-GGNArnegdGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK05653 142 VSGvTGNP-----GQTNYSAAKAGVIGFTKALALELASRGITV 179
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 45-280 5.97e-05

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 43.94  E-value: 5.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   45 SRVVLITSADTALGLQLCTHLANKGYRV--FAGMKEAQDSLPAKLLCGwmkireysEEPIAGTIIPMRLDVTREDVLREA 122
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADGADVivLDIHPMRGRAEADAVAAG--------IEAAGGKALGLAFDVRDFAATRAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  123 tviiganLNADERGIA---AVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR--GRLLYLGGVSG 197
Cdd:PRK12827  78 -------LDAGVEEFGrldILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARrgGRIVNIASVAG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  198 GGNARnegdGLVAFNASRVAVDKCAEELRKELHPYGVSV-----VALDTcGMTAESLYKAPVAQTMSL-VVGAPTQYTAD 271
Cdd:PRK12827 151 VRGNR----GQVNYAASKAGLIGLTKTLANELAPRGITVnavapGAINT-PMADNAAPTEHLLNPVPVqRLGEPDEVAAL 225

                        250
                 ....*....|..
gi 20128793  272 VL---SPDALHV 280
Cdd:PRK12827 226 VAflvSDAASYV 237
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 45-197 7.46e-05

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: 43.48  E-value: 7.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  45 SRVVLITSADTALGLQLCTHLANKGYRV-FAGMKEAQDSLPAKLLcgwmkIREYSEEPIAgtiipMRLDVTREDVLREat 123
Cdd:cd08930   2 DKIILITGAAGLIGKAFCKALLSAGARLiLADINAPALEQLKEEL-----TNLYKNRVIA-----LELDITSKESIKE-- 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20128793 124 viIGANLNADERGIAAVINTSGSVFRGQ---VESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLLYLGGVSG 197
Cdd:cd08930  70 --LIESYLEKFGRIDILINNAYPSPKVWgsrFEEFPYEQWNEVLNVNLGGAFLCSQAFIkLFKKQGKGSIINIASIYG 145
PRK07577 PRK07577
SDR family oxidoreductase;
44-239 1.15e-04

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 42.79  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   44 PSRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQDSLPAKLLCgwmkireyseepiagtiipmrldVTREDVLREAT 123
Cdd:PRK07577   2 SSRTVLVTGATKGIGLALSLRLANLGHQVIGIARSAIDDFPGELFA-----------------------CDLADIEQTAA 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  124 VIIGANlnaDERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGGGnAR 202
Cdd:PRK07577  59 TLAQIN---EIHPVDAIVNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREqGRIVNICSRAIFG-AL 134

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 20128793  203 NEgdglVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:PRK07577 135 DR----TSYSAAKSALVGCTRTWALELAEYGITVNAV 167
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 139-265 2.27e-04

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 41.35  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 139 AVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGGGNARNEGdglvAFNASRVA 217
Cdd:cd02266  34 VVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRlGRFILISSVAGLFGAPGLG----GYAASKAA 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 20128793 218 VDKCAEELRKELHPYGVSVVALdTCGMTAES-LYKAPVAQTMSLVVGAP 265
Cdd:cd02266 110 LDGLAQQWASEGWGNGLPATAV-ACGTWAGSgMAKGPVAPEEILGNRRH 157
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 46-238 2.38e-04

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: 41.84  E-value: 2.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKG-YRVFAGM------KEAQDSLPAKLLcgwmKIReyseepiagtiiPMRLDVTREDV 118
Cdd:cd05324   1 KVALVTGANRGIGFEIVRQLAKSGpGTVILTArdvergQAAVEKLRAEGL----SVR------------FHQLDVTDDAS 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 119 LREATVIIGANLNaderGIAAVINTSGSVFRG-QVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYlggVS 196
Cdd:cd05324  65 IEAAADFVEEKYG----GLDILVNNAGIAFKGfDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKSPaGRIVN---VS 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20128793 197 GGgnarnEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVA 238
Cdd:cd05324 138 SG-----LGSLTSAYGVSKAALNALTRILAKELKETGIKVNA 174
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 46-236 2.90e-04

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: 41.88  E-value: 2.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRV--FAGMKEAQDslpakllcgwmkiREYSEEPIAGT-IIPMRLDVTREDVLREA 122
Cdd:cd05344   2 KVALVTAASSGIGLAIARALAREGARVaiCARNRENLE-------------RAASELRAGGAgVLAVVADLTDPEDIDRL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 123 TVIIGANLNaderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSgggnA 201
Cdd:cd05344  69 VEKAGDAFG----RVDILVNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGwGRIVNISSLT----V 140

                       170       180       190
                ....*....|....*....|....*....|....*
gi 20128793 202 RNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:cd05344 141 KEPEPNLVLSNVARAGLIGLVKTLSRELAPDGVTV 175
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 46-230 4.00e-04

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: 41.34  E-value: 4.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVfAGMKEAQDSLPAklLCGWMKIREYseepiaGTIIPMRLDVTREDVLREATVI 125
Cdd:cd05343   7 RVALVTGASVGIGAAVARALVQHGMKV-VGCARRVDKIEA--LAAECQSAGY------PTLFPYQCDLSNEEQILSMFSA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 126 IganlNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGT---LRVAKAFVCFLRPTRGRLLYLGGVSggGNAR 202
Cdd:cd05343  78 I----RTQHQGVDVCINNAGLARPEPLLSGKTEGWKEMFDVNVLALsicTREAYQSMKERNVDDGHIININSMS--GHRV 151

                       170       180
                ....*....|....*....|....*...
gi 20128793 203 NEGDGLVAFNASRVAVDKCAEELRKELH 230
Cdd:cd05343 152 PPVSVFHFYAATKHAVTALTEGLRQELR 179
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 112-236 4.07e-04

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: 41.16  E-value: 4.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 112 DVTREDVLREATviigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLL 190
Cdd:cd05352  66 DVSSQESVEKTF----KQIQKDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAkIFKKQGKGSLI 141

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 20128793 191 YLGGVSggGNARNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:cd05352 142 ITASMS--GTIVNRPQPQAAYNASKAAVIHLAKSLAVEWAKYFIRV 185
PRK06182 PRK06182
short chain dehydrogenase; Validated
 44-295 4.73e-04

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 41.10  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   44 PSRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQdslpakllcgwmKIREYSEepiAGtIIPMRLDVTREDVLREA- 122
Cdd:PRK06182   2 QKKVALVTGASSGIGKATARRLAAQGYTVYGAARRVD------------KMEDLAS---LG-VHPLSLDVTDEASIKAAv 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  123 -TVIiganlnADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSG--- 197
Cdd:PRK06182  66 dTII------AEEGRIDVLVNNAGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRsGRIINISSMGGkiy 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  198 ---GGnarnegdglvAFNASRVAVDKCAEELRKELHPYGVSVVALDTCGM-------TAESLYK-------APVAQTMSL 260
Cdd:PRK06182 140 tplGA----------WYHATKFALEGFSDALRLEVAPFGIDVVVIEPGGIktewgdiAADHLLKtsgngayAEQAQAVAA 209

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 20128793  261 vvGAPTQYTADVLSPDAL--HVIERALWDYVPQQRYA 295
Cdd:PRK06182 210 --SMRSTYGSGRLSDPSViaDAISKAVTARRPKTRYA 244
PRK07069 PRK07069
short chain dehydrogenase; Validated
 49-218 4.88e-04

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 41.23  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   49 LITSADTALGLQLCTHLANKGYRVF-------AGMKEAQDSLPAKllCGwmkireyseepiAGTIIPMRLDVTREDVLRE 121
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFltdindaAGLDAFAAEINAA--HG------------EGVAFAAVQDVTDEAQWQA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  122 ATviigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGggn 200
Cdd:PRK07069  69 LL----AQAADAMGGLSVLVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQpASIVNISSVAA--- 141

                        170
                 ....*....|....*...
gi 20128793  201 ARNEGDgLVAFNASRVAV 218
Cdd:PRK07069 142 FKAEPD-YTAYNASKAAV 158
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 46-237 5.66e-04

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: 40.83  E-value: 5.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVF--AGMKEAQDSLPAKLlcgwmkireyseEPIAGTIIPMRLDVTREDVLREAt 123
Cdd:cd05360   1 QVVVITGASSGIGRATALAFAERGAKVVlaARSAEALHELAREV------------RELGGEAIAVVADVADAAQVERA- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 124 viigANLNADERG-IAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGGGNA 201
Cdd:cd05360  68 ----ADTAVERFGrIDTWVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGgGALINVGSLLGYRSA 143

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20128793 202 RNEGdglvAFNASRVAVDKCAEELRKELHPYGVSVV 237
Cdd:cd05360 144 PLQA----AYSASKHAVRGFTESLRAELAHDGAPIS 175
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 45-239 8.20e-04

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 40.54  E-value: 8.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   45 SRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQDSlpAKllcgwmKIREYSEEPIagtiipmRLDVTREDVLREATV 124
Cdd:PRK06463   7 GKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAENE--AK------ELREKGVFTI-------KCDVGNRDQVKKSKE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  125 IIGANLNAdergIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRP-TRGRLLYLggvsgggnARN 203
Cdd:PRK06463  72 VVEKEFGR----VDVLVNNAGIMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLsKNGAIVNI--------ASN 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 20128793  204 EGDGLVAFNASRVAVDKCA-----EELRKELHPYGVSVVAL 239
Cdd:PRK06463 140 AGIGTAAEGTTFYAITKAGiiiltRRLAFELGKYGIRVNAV 180
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 46-239 8.81e-04

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 40.31  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRVF------AGMKEAQDSLPAkllcgwmkireyseepiAG-TIIPMRLDVTREDV 118
Cdd:PRK08213  13 KTALVTGGSRGLGLQIAEALGEAGARVVlsarkaEELEEAAAHLEA-----------------LGiDALWIAADVADEAD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  119 LREATVIIGANLNaderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTL----RVAKafVCFLRPTRGRLLYLGG 194
Cdd:PRK08213  76 IERLAEETLERFG----HVDILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFllsqAVAK--RSMIPRGYGRIINVAS 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 20128793  195 VSG-GGNARnEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:PRK08213 150 VAGlGGNPP-EVMDTIAYNTSKGAVINFTRALAAEWGPHGIRVNAI 194
PRK09072 PRK09072
SDR family oxidoreductase;
44-255 1.17e-03

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 39.92  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   44 PSRVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQ--DSLPAKLlcgwmkireyseePIAGTIIPMRLDVT----RED 117
Cdd:PRK09072   4 KDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEklEALAARL-------------PYPGRHRWVVADLTseagREA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  118 VLREATVIIGANLnadergiaaVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLR-PTRGRLLYLGGVS 196
Cdd:PRK09072  71 VLARAREMGGINV---------LINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRaQPSAMVVNVGSTF 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  197 GG-GNArnegdGLVAFNASRVAVDKCAEELRKELHPYGVSVvaldtcgmtaesLYKAPVA 255
Cdd:PRK09072 142 GSiGYP-----GYASYCASKFALRGFSEALRRELADTGVRV------------LYLAPRA 184
PRK08267 PRK08267
SDR family oxidoreductase;
48-239 1.48e-03

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 39.54  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   48 VLITSADTALGLQLCTHLANKGYRVFA------GMKEAQDSLPakllcgwmkireyseepiAGTIIPMRLDVTREDVLRE 121
Cdd:PRK08267   4 IFITGAASGIGRATALLFAAEGWRVGAydineaGLAALAAELG------------------AGNAWTGALDVTDRAAWDA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  122 A----TVIIGANLNadergiaAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRG-RLLYLGGVS 196
Cdd:PRK08267  66 AladfAAATGGRLD-------VLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGaRVINTSSAS 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20128793  197 G-GGNArnegdGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:PRK08267 139 AiYGQP-----GLAVYSATKFAVRGLTEALDLEWRRHGIRVADV 177
PRK12826 PRK12826
SDR family oxidoreductase;
45-236 1.54e-03

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 39.51  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   45 SRVVLITSADTALGLQLCTHLANKGYRVFA-GMKEAQDSLPAKLLcgwmkireyseEPIAGTIIPMRLDVTREDVLrEAT 123
Cdd:PRK12826   6 GRVALVTGAARGIGRAIAVRLAADGAEVIVvDICGDDAAATAELV-----------EAAGGKARARQVDVRDRAAL-KAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  124 VIIGANLNAderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR-GRLLYLGGVSGGGNAR 202
Cdd:PRK12826  74 VAAGVEDFG---RLDILVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGgGRIVLTSSVAGPRVGY 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 20128793  203 negDGLVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:PRK12826 151 ---PGLAHYAASKAGLVGFTRALALELAARNITV 181
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 46-285 1.79e-03

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: 39.16  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVFA------GMKEAQDSLPAKLLCGWMKIREYSeepiagtiipmrLDVTREDvl 119
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIvarsesKLEEAVEEIEAEANASGQKVSYIS------------ADLSDYE-- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 120 rEATVIIgANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLLYLggVSGGG 199
Cdd:cd08939  68 -EVEQAF-AQAVEKGGPPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVF--VSSQA 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 200 narnegdGLV------AFNASRVAVDKCAEELRKELHPYGVSVVAL-----DTCGMTAESLYKAPVAQTMSLVVGAptqY 268
Cdd:cd08939 144 -------ALVgiygysAYCPSKFALRGLAESLRQELKPYNIRVSVVyppdtDTPGFEEENKTKPEETKAIEGSSGP---I 213

                       250
                ....*....|....*..
gi 20128793 269 TADvlspDALHVIERAL 285
Cdd:cd08939 214 TPE----EAARIIVKGL 226
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 46-238 2.25e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 38.93  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRVFAGMKEAQ--DSLPAKLLCGwmkireyseepiagtiiPMRLDVTREDVLREAT 123
Cdd:PRK07060  10 KSVLVTGASSGIGRACAVALAQRGARVVAAARNAAalDRLAGETGCE-----------------PLRLDVGDDAAIRAAL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  124 VIIGAnlnADergiaAVINTSG-SVFRGQVESQNvQQWEHMLRTNILGTLRVAKAFVcflrptRGRLlylgGVSGGGNAR 202
Cdd:PRK07060  73 AAAGA---FD-----GLVNCAGiASLESALDMTA-EGFDRVMAVNARGAALVARHVA------RAMI----AAGRGGSIV 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 20128793  203 NEGD--GLVAFN------ASRVAVDKCAEELRKELHPYGVSVVA 238
Cdd:PRK07060 134 NVSSqaALVGLPdhlaycASKAALDAITRVLCVELGPHGIRVNS 177
PRK07832 PRK07832
SDR family oxidoreductase;
48-241 2.85e-03

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 38.87  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   48 VLITSADTALGLQLCTHLANKGYRVF------AGMKEAQDSLPAkllCGwmkireyseepiaGTIIPMR-LDVTREDVLR 120
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFltdrdaDGLAQTVADARA---LG-------------GTVPEHRaLDISDYDAVA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  121 EatviIGANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVC-FLRPTRGRllYLGGVSGGG 199
Cdd:PRK07832  67 A----FAADIHAAHGSMDVVMNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPpMVAAGRGG--HLVNVSSAA 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 20128793  200 narnegdGLV------AFNASRVAVDKCAEELRKELHPY--GVSVV---ALDT 241
Cdd:PRK07832 141 -------GLValpwhaAYSASKFGLRGLSEVLRFDLARHgiGVSVVvpgAVKT 186
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 46-236 2.88e-03

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: 38.72  E-value: 2.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRVF--AGMKEAQDSLPAKLLcgwmkireyseEPIAGTIIPMRLDVTREDVLREAT 123
Cdd:cd05332   4 KVVIITGASSGIGEELAYHLARLGARLVlsARREERLEEVKSECL-----------ELGAPSPHVVPLDMSDLEDAEQVV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 124 VIIGANLnadeRGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRP-TRGRLLYLGGVSG--GGN 200
Cdd:cd05332  73 EEALKLF----GGLDILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIErSQGSIVVVSSIAGkiGVP 148

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20128793 201 ARnegdglVAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:cd05332 149 FR------TAYAASKHALQGFFDSLRAELSEPNISV 178
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 46-236 3.18e-03

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: 38.41  E-value: 3.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  46 RVVLITSADTALGLQLCTHLANKGYRV---FAGMKEAQDSLPAKLlcgwmkireyseEPIAGTIIPMRLDVTREDVLR-- 120
Cdd:cd05362   4 KVALVTGASRGIGRAIAKRLARDGASVvvnYASSKAAAEEVVAEI------------EAAGGKAIAVQADVSDPSQVArl 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 121 --EATVIIGanlnaderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTrGRLLYLGgvSGG 198
Cdd:cd05362  72 fdAAEKAFG--------GVDILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDG-GRIINIS--SSL 140

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 20128793 199 GNARNEGDGlvAFNASRVAVDKCAEELRKELHPYGVSV 236
Cdd:cd05362 141 TAAYTPNYG--AYAGSKAAVEAFTRVLAKELGGRGITV 176
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 46-181 3.62e-03

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: 37.85  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793     46 RVVLITSADTALGLQLCTHLANKGYR--VFAGMKEAQDSLPAKLLcgwMKIREYSEEPIAgtiipMRLDVTREDVLREAT 123
Cdd:smart00822   1 GTYLITGGLGGLGRALARWLAERGARrlVLLSRSGPDAPGAAALL---AELEAAGARVTV-----VACDVADRDALAAVL 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20128793    124 viigANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKA--------FVCF 181
Cdd:smart00822  73 ----AAIPAVEGPLTGVIHAAGVLDDGVLASLTPERFAAVLAPKAAGAWNLHELtadlpldfFVLF 134
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 48-234 4.68e-03

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: 37.83  E-value: 4.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  48 VLITSADTALGLQLCTHLANKGYRVFAgmkeaqdslpakLLCGWMKIREYseePIAGTIIPMrlDVTREDVLREATviig 127
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIA------------LDLPFVLLLEY---GDPLRLTPL--DVADAAAVREVC---- 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793 128 ANLNADERGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLLylggVSGGGNARNEGD- 206
Cdd:cd05331  60 SRLLAEHGPIDALVNCAGVLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAI----VTVASNAAHVPRi 135

                       170       180
                ....*....|....*....|....*...
gi 20128793 207 GLVAFNASRVAVDKCAEELRKELHPYGV 234
Cdd:cd05331 136 SMAAYGASKAALASLSKCLGLELAPYGV 163
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 46-197 5.63e-03

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 37.95  E-value: 5.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRV-FAGMKEAQDSLPAKLLcgwmkireyseEPIAGTIIPMRLDVTREDvlreaTV 124
Cdd:PRK13394   8 KTAVVTGAASGIGKEIALELARAGAAVaIADLNQDGANAVADEI-----------NKAGGKAIGVAMDVTNED-----AV 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20128793  125 IIGANLNADERG-IAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTR--GRLLYLGGVSG 197
Cdd:PRK13394  72 NAGIDKVAERFGsVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDrgGVVIYMGSVHS 147
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 46-238 6.08e-03

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 37.51  E-value: 6.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   46 RVVLITSADTALGLQLCTHLANKGYRVFAGM---KEAQDSLPAKllcgwmkIREYseepiAGTIIPMRLDVTRED----V 118
Cdd:PRK05565   6 KVAIVTGASGGIGRAIAELLAKEGAKVVIAYdinEEAAQELLEE-------IKEE-----GGDAIAVKADVSSEEdvenL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  119 LREATVIIGanlnaderGIAAVINTSGSVFRGQVESQNVQQWEHMLRTNILGTLRVAKAFV-CFLRPTRGRLLYLGGVSG 197
Cdd:PRK05565  74 VEQIVEKFG--------KIDILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALpYMIKRKSGVIVNISSIWG 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 20128793  198 GGNARNEgdglVAFNASRVAVDKCAEELRKELHPYGVSVVA 238
Cdd:PRK05565 146 LIGASCE----VLYSASKGAVNAFTKALAKELAPSGIRVNA 182
PRK06947 PRK06947
SDR family oxidoreductase;
44-239 8.55e-03

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 37.09  E-value: 8.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793   44 PSRVVLITSADTALGLQLCTHLANKGYRVfaGMKEAQDSLPAKLLCGWMKIREYSEEPIAGtiipmrldvtreDVLREAT 123
Cdd:PRK06947   1 MRKVVLITGASRGIGRATAVLAAARGWSV--GINYARDAAAAEETADAVRAAGGRACVVAG------------DVANEAD 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20128793  124 VIIGANLNADERG-IAAVINTSGSVFRGQ-VESQNVQQWEHMLRTNILGTLRVAKAFVCFLRPTRGRLlylGG----VSG 197
Cdd:PRK06947  67 VIAMFDAVQSAFGrLDALVNNAGIVAPSMpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGR---GGaivnVSS 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 20128793  198 GGNARNEGDGLVAFNASRVAVDKCAEELRKELHPYGVSVVAL 239
Cdd:PRK06947 144 IASRLGSPNEYVDYAGSKGAVDTLTLGLAKELGPHGVRVNAV 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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