NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19075741|ref|NP_588241|]
View 

dehydrogenase [Schizosaccharomyces pombe]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143300)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase may catalyze isomerization, decarboxylation, epimerization, C=N bond reduction, dehydration, dehalogenation, enoyl-CoA reduction, and/or carbonyl-alcohol oxidoreduction; 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

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  20423462|19011750|19011748|12604210|19027726
SCOP:  4000029

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 7-248 1.28e-90

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: 269.49  E-value: 1.28e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI----TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLeslgELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:cd05374  82 AGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGS-GRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741 163 MRELDPnWNIAITIVQPGGMQTEWASSNMQWAKPHPA---YENDRSWRPFWENYHGCEETDPNKAAELLYSIAKLDRPPQ 239
Cdd:cd05374 161 RLELAP-FGIKVTIIEPGPVRTGFADNAAGSALEDPEispYAPERKEIKENAAGVGSNPGDPEKVADVIVKALTSESPPL 239


                ....*....
gi 19075741 240 KLVLGHDSL 248
Cdd:cd05374 240 RYFLGSDAL 248
 
Name Accession Description Interval E-value
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 7-248 1.28e-90

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: 269.49  E-value: 1.28e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI----TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLeslgELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:cd05374  82 AGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGS-GRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741 163 MRELDPnWNIAITIVQPGGMQTEWASSNMQWAKPHPA---YENDRSWRPFWENYHGCEETDPNKAAELLYSIAKLDRPPQ 239
Cdd:cd05374 161 RLELAP-FGIKVTIIEPGPVRTGFADNAAGSALEDPEispYAPERKEIKENAAGVGSNPGDPEKVADVIVKALTSESPPL 239


                ....*....
gi 19075741 240 KLVLGHDSL 248
Cdd:cd05374 240 RYFLGSDAL 248
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 9-257 4.60e-67

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 210.28  E-value: 4.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSK----LLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAG 84
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKygdrLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNNAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMR 164
Cdd:PRK08263  87 YGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQR-SGHIIQISSIGGISAFPMSGIYHASKWALEGMSEALAQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  165 ELDPnWNIAITIVQPGGMQTEWASSNMQWAKPHPAYENDRSwRPFWENYHGCEETDPNKAAELLYSIAKLDRPPQKLVLG 244
Cdd:PRK08263 166 EVAE-FGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLRE-ELAEQWSERSVDGDPEAAAEALLKLVDAENPPLRLFLG 243

                        250
                 ....*....|...
gi 19075741  245 HDSLELIRKQHQD 257
Cdd:PRK08263 244 SGVLDLAKADYER 256
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-236 2.00e-63

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: 199.64  E-value: 2.00e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI----TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:COG4221   1 MSDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLealaAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  77 DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:COG4221  81 DVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARG-SGHIVNISSIAGLRPYPGGAVYAATKAAVR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741 157 GLSQTIMRELDPnWNIAITIVQPGGMQTEWASSNMqwakphpayenDRSWRPFWENYHGCEETDPNKAAELLYSIAKLDR 236
Cdd:COG4221 160 GLSESLRAELRP-TGIRVTVIEPGAVDTEFLDSVF-----------DGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPA 227
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-185 2.77e-51

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 167.02  E-value: 2.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741     7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI--TIEH-----SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLeaVAKElgalgGKALFIQGDVTDRAQVKALVEQAVERLGRLDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:pfam00106  82 VNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIK-GSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180
                  ....*....|....*....|....*.
gi 19075741   160 QTIMRELDPnWNIAITIVQPGGMQTE 185
Cdd:pfam00106 161 RSLALELAP-HGIRVNAVAPGGVDTD 185
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 7-84 2.41e-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: 38.23  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741      7 TVLITGSSKGLGYALVKVgLAQGY--NVIACSR--APDTITIEHSKLLKLKL--------DVTDVKSVETAFKDAKRRFG 74
Cdd:smart00822   2 TYLITGGLGGLGRALARW-LAERGarRLVLLSRsgPDAPGAAALLAELEAAGarvtvvacDVADRDALAAVLAAIPAVEG 80

                           90
                   ....*....|
gi 19075741     75 NVDIVINNAG 84
Cdd:smart00822  81 PLTGVIHAAG 90
 
Name Accession Description Interval E-value
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 7-248 1.28e-90

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: 269.49  E-value: 1.28e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI----TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:cd05374   2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLeslgELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:cd05374  82 AGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGS-GRIVNVSSVAGLVPTPFLGPYCASKAALEALSESL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741 163 MRELDPnWNIAITIVQPGGMQTEWASSNMQWAKPHPA---YENDRSWRPFWENYHGCEETDPNKAAELLYSIAKLDRPPQ 239
Cdd:cd05374 161 RLELAP-FGIKVTIIEPGPVRTGFADNAAGSALEDPEispYAPERKEIKENAAGVGSNPGDPEKVADVIVKALTSESPPL 239


                ....*....
gi 19075741 240 KLVLGHDSL 248
Cdd:cd05374 240 RYFLGSDAL 248
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 9-257 4.60e-67

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 210.28  E-value: 4.60e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSK----LLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAG 84
Cdd:PRK08263   7 FITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKygdrLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNNAG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMR 164
Cdd:PRK08263  87 YGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQR-SGHIIQISSIGGISAFPMSGIYHASKWALEGMSEALAQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  165 ELDPnWNIAITIVQPGGMQTEWASSNMQWAKPHPAYENDRSwRPFWENYHGCEETDPNKAAELLYSIAKLDRPPQKLVLG 244
Cdd:PRK08263 166 EVAE-FGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLRE-ELAEQWSERSVDGDPEAAAEALLKLVDAENPPLRLFLG 243

                        250
                 ....*....|...
gi 19075741  245 HDSLELIRKQHQD 257
Cdd:PRK08263 244 SGVLDLAKADYER 256
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 7-270 8.82e-65

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 204.38  E-value: 8.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI----TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK06180   6 TWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARadfeALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVLVNN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:PRK06180  86 AGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRR-GHIVNITSMGGLITMPGIGYYCGSKFALEGISESL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  163 MRELDPnWNIAITIVQPGGMQTEWASSNM-QWAKPHPAYENDRS-WRPFWENYHGCEETDPNKAAELLYSIAKLDRPPQK 240
Cdd:PRK06180 165 AKEVAP-FGIHVTAVEPGSFRTDWAGRSMvRTPRSIADYDALFGpIRQAREAKSGKQPGDPAKAAQAILAAVESDEPPLH 243

                        250       260       270
                 ....*....|....*....|....*....|..
gi 19075741  241 LVLGHDSLELIRKQHQDIGEELES--NVALST 270
Cdd:PRK06180 244 LLLGSDALRLVRAKLAALDAEIDAweAVTVST 275
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-236 2.00e-63

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: 199.64  E-value: 2.00e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI----TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:COG4221   1 MSDKGKVALITGASSGIGAATARALAAAGARVVLAARRAERLealaAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  77 DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:COG4221  81 DVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARG-SGHIVNISSIAGLRPYPGGAVYAATKAAVR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741 157 GLSQTIMRELDPnWNIAITIVQPGGMQTEWASSNMqwakphpayenDRSWRPFWENYHGCEETDPNKAAELLYSIAKLDR 236
Cdd:COG4221 160 GLSESLRAELRP-TGIRVTVIEPGAVDTEFLDSVF-----------DGDAEAAAAVYEGLEPLTPEDVAEAVLFALTQPA 227
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-196 3.55e-62

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 197.01  E-value: 3.55e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD-------TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRF 73
Cdd:COG0300   1 MSLTGKTVLITGASSGIGRALARALAARGARVVLVARDAErlealaaELRAAGARVEVVALDVTDPDAVAALAEAVLARF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  74 GNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKF 153
Cdd:COG0300  81 GPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARG-RGRIVNVSSVAGLRGLPGMAAYAASKA 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19075741 154 AVEGLSQTIMRELDPNwNIAITIVQPGGMQTE-WASSNMQWAKP 196
Cdd:COG0300 160 ALEGFSESLRAELAPT-GVRVTAVCPGPVDTPfTARAGAPAGRP 202
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 8-195 4.58e-53

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: 172.85  E-value: 4.58e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPD------TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREGAKVVLADRNEEalaelaAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:cd05233  81 NAGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKK-QGGGRIVNISSVAGLRPLPGQAAYAASKAALEGLTRS 159

                       170       180       190
                ....*....|....*....|....*....|....
gi 19075741 162 IMRELDPNwNIAITIVQPGGMQTEWASSNMQWAK 195
Cdd:cd05233 160 LALELAPY-GIRVNAVAPGLVDTPMLAKLGPEEA 192
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 7-185 2.77e-51

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 167.02  E-value: 2.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741     7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI--TIEH-----SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:pfam00106   2 VALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEKLeaVAKElgalgGKALFIQGDVTDRAQVKALVEQAVERLGRLDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:pfam00106  82 VNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIK-GSGGRIVNISSVAGLVPYPGGSAYSASKAAVIGFT 160

                         170       180
                  ....*....|....*....|....*.
gi 19075741   160 QTIMRELDPnWNIAITIVQPGGMQTE 185
Cdd:pfam00106 161 RSLALELAP-HGIRVNAVAPGGVDTD 185
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 7-186 1.51e-50

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 166.88  E-value: 1.51e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT-------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:COG1028   8 VALVTGGSSGIGRAIARALAAEGARVVITDRDAEAleaaaaeLRAAGGRALAVAADVTDEAAVEALVAAAVAAFGRLDIL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:COG1028  88 VNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERG-GGRIVNISSIAGLRGSPGQAAYAASKAAVVGLT 166

                       170       180
                ....*....|....*....|....*..
gi 19075741 160 QTIMRELDPnWNIAITIVQPGGMQTEW 186
Cdd:COG1028 167 RSLALELAP-RGIRVNAVAPGPIDTPM 192
PRK06482 PRK06482
SDR family oxidoreductase;
7-273 8.92e-46

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 155.66  E-value: 8.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSK----LLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK06482   4 TWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARygdrLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVVSN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:PRK06482  84 AGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQG-GGRIVQVSSEGGQIAYPGFSLYHATKWGIEGFVEAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  163 MRELDPnWNIAITIVQPGGMQTEWASSnMQWAKPHPAYEN-----------DRSWRPfwenyhgceETDPNKAAELLYSI 231
Cdd:PRK06482 163 AQEVAP-FGIEFTIVEPGPARTNFGAG-LDRGAPLDAYDDtpvgdlrralaDGSFAI---------PGDPQKMVQAMIAS 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 19075741  232 AKLDRPPQKLVLGHDSLELIRKQHQDIGEELES--NVALSTSVA 273
Cdd:PRK06482 232 ADQTPAPRRLTLGSDAYASIRAALSERLAALEAqkAVALSTDVD 275
PRK06182 PRK06182
short chain dehydrogenase; Validated
 7-187 1.52e-43

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 149.73  E-value: 1.52e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT-IEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGY 85
Cdd:PRK06182   5 VALVTGASSGIGKATARRLAAQGYTVYGAARRVDKMEdLASLGVHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVNNAGY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   86 GLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMRE 165
Cdd:PRK06182  85 GSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQ-RSGRIINISSMGGKIYTPLGAWYHATKFALEGFSDALRLE 163

                        170       180
                 ....*....|....*....|..
gi 19075741  166 LDPnWNIAITIVQPGGMQTEWA 187
Cdd:PRK06182 164 VAP-FGIDVVVIEPGGIKTEWG 184
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 6-196 1.79e-42

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: 145.86  E-value: 1.79e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIEH----SKLLKLKLDVTDVKSVETAFKDAKRRFG 74
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIVARseskleeAVEEIEAEAnasgQKVSYISADLSDYEEVEQAFAQAVEKGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  75 NVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:cd08939  82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQ-RPGHIVFVSSQAALVGIYGYSAYCPSKFA 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19075741 155 VEGLSQTIMRELDPNwNIAITIVQPGGMQTE-WASSNMqwAKP 196
Cdd:cd08939 161 LRGLAESLRQELKPY-NIRVSVVYPPDTDTPgFEEENK--TKP 200
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 2-204 2.06e-42

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 146.59  E-value: 2.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    2 KSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAP-DTITIEHSKLLKLklDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK06179   1 MSNSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPaRAAPIPGVELLEL--DVTDDASVQAAVDEVIARAGRIDVLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK06179  79 NNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQG-SGRIINISSVLGFLPAPYMALYAASKHAVEGYSE 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19075741  161 TIMRELDpNWNIAITIVQPGGMQTEWASSNMQWAKPHPAYENDR 204
Cdd:PRK06179 158 SLDHEVR-QFGIRVSLVEPAYTKTNFDANAPEPDSPLAEYDRER 200
PRK06914 PRK06914
SDR family oxidoreductase;
9-237 3.31e-39

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 138.62  E-value: 3.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYaLVKVGLA-QGYNVIACSRAPDtitiEHSKLLKL-------------KLDVTDVKSVETaFKDAKRRFG 74
Cdd:PRK06914   7 IVTGASSGFGL-LTTLELAkKGYLVIATMRNPE----KQENLLSQatqlnlqqnikvqQLDVTDQNSIHN-FQLVLKEIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   75 NVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:PRK06914  81 RIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQ-KSGKIINISSISGRVGFPGLSPYVSSKYA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  155 VEGLSQTIMRELDPnWNIAITIVQPGGMQTEWASSNMQWAKPHPAYENdrswrPFWENYHGCEE---------TDPNKAA 225
Cdd:PRK06914 160 LEGFSESLRLELKP-FGIDVALIEPGSYNTNIWEVGKQLAENQSETTS-----PYKEYMKKIQKhinsgsdtfGNPIDVA 233

                        250
                 ....*....|..
gi 19075741  226 ELLYSIAKLDRP 237
Cdd:PRK06914 234 NLIVEIAESKRP 245
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 7-185 1.62e-38

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: 136.18  E-value: 1.62e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKL--------KLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05332   5 VVIITGASSGIGEELAYHLARLGARLVLSARREERLEEVKSECLELgapsphvvPLDMSDLEDAEQVVEEALKLFGGLDI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd05332  85 LINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQ-GSIVVVSSIAGKIGVPFRTAYAASKHALQGF 163

                       170       180
                ....*....|....*....|....*..
gi 19075741 159 SQTIMRELDpNWNIAITIVQPGGMQTE 185
Cdd:cd05332 164 FDSLRAELS-EPNISVTVVCPGLIDTN 189
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 8-198 1.23e-37

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: 133.28  E-value: 1.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRapDTITIEHS---------KLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAKVVLAAR--SAEALHELarevrelggEAIAVVADVADAAQVERAADTAVERFGRIDT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd05360  81 WVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRG-GGALINVGSLLGYRSAPLQAAYSASKHAVRGF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19075741 159 SQTIMRELDP-NWNIAITIVQPGGMQT---EWASSNMQwAKPHP 198
Cdd:cd05360 160 TESLRAELAHdGAPISVTLVQPTAMNTpffGHARSYMG-KKPKP 202
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 7-213 1.48e-37

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 133.64  E-value: 1.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT-----IEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK12829  13 RVLVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAataarLPGAKVTATVADVADPAQVERVFDTAVERFGGLDVLVN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAG-YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK12829  93 NAGiAGPTGGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVAGRLGYPGRTPYAASKWAVVGLVK 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19075741  161 TIMRELDPNwNIAITIVQPGGMQTEwassNMQWAKPHPAYENDRSWRPFWENY 213
Cdd:PRK12829 173 SLAIELGPL-GIRVNAILPGIVRGP----RMRRVIEARAQQLGIGLDEMEQEY 220
PRK07326 PRK07326
SDR family oxidoreductase;
7-188 2.82e-37

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 132.44  E-value: 2.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT------IEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK07326   8 VALITGGSKGIGFAIAEALLAEGYKVAITARDQKELEeaaaelNNKGNVLGLAADVRDEADVQRAVDAIVAAFGGLDVLI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK07326  88 ANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRG--GGYIINISSLAGTNFFAGGAAYNASKFGLVGFSE 165

                        170       180
                 ....*....|....*....|....*...
gi 19075741  161 TIMRELDPNwNIAITIVQPGGMQTEWAS 188
Cdd:PRK07326 166 AAMLDLRQY-GIKVSTIMPGSVATHFNG 192
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 8-197 1.28e-34

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: 126.62  E-value: 1.28e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEH------SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI--V 79
Cdd:cd09805   3 VLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAKElrrvcsDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLwgL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEFESYNIEEMHRQ-MNVNFWGVAYITKEALNLMRESGkgGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd09805  83 VNNAGILGFGGDEELLPMDDYRKcMEVNLFGTVEVTKAFLPLLRRAK--GRVVNVSSMGGRVPFPAGGAYCASKAAVEAF 160

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19075741 159 SQTIMRELDPnWNIAITIVQPGGMQTEWASSNMQWAKPH 197
Cdd:cd09805 161 SDSLRRELQP-WGVKVSIIEPGNFKTGITGNSELWEKQA 198
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 7-198 3.76e-34

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 126.57  E-value: 3.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT-----IEH--SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07109  10 VVVITGASAGVGRATARAFARRGAKVVLLARGEEGLEalaaeIRAagGEALAVVADVADAEAVQAAADRAEEELGPIDTW 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK07109  90 VNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRD-RGAIIQVGSALAYRSIPLQSAYCAAKHAIRGFT 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19075741  160 QTIMRELD-PNWNIAITIVQPGGMQT---EWASSNMQWaKPHP 198
Cdd:PRK07109 169 DSLRCELLhDGSPVSVTMVQPPAVNTpqfDWARSRLPV-EPQP 210
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 7-195 5.37e-34

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 124.41  E-value: 5.37e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLK--------LKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05366   4 VAIITGAAQGIGRAIAERLAADGFNIVLADLNLEEAAKSTIQEISeagynavaVGADVTDKDDVEALIDQAVEKFGSFDV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd05366  84 MVNNAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGHGGKIINASSIAGVQGFPNLGAYSASKFAVRGL 163

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19075741 159 SQTIMRELDPNwNIAITIVQPGGMQTE-WASSNMQWAK 195
Cdd:cd05366 164 TQTAAQELAPK-GITVNAYAPGIVKTEmWDYIDEEVGE 200
PRK05693 PRK05693
SDR family oxidoreductase;
7-250 6.55e-34

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 124.52  E-value: 6.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR-APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGY 85
Cdd:PRK05693   3 VVLITGCSSGIGRALADAFKAAGYEVWATARkAEDVEALAAAGFTAVQLDVNDGAALARLAEELEAEHGGLDVLINNAGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   86 GLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMRE 165
Cdd:PRK05693  83 GAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRRS--RGLVVNIGSVSGVLVTPFAGAYCASKAAVHALSDALRLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  166 LDPnWNIAITIVQPGGMQTEWASSNMQWAKphpAYENDRS-WRPFWENYHGCEETDPNK-------AAELLYSIAKLDRP 237
Cdd:PRK05693 161 LAP-FGVQVMEVQPGAIASQFASNASREAE---QLLAEQSpWWPLREHIQARARASQDNptpaaefARQLLAAVQQSPRP 236

                        250
                 ....*....|...
gi 19075741  238 PQkLVLGHDSLEL 250
Cdd:PRK05693 237 RL-VRLGNGSRAL 248
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
7-185 1.21e-33

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 122.96  E-value: 1.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK05653   7 TALVTGASRGIGRAIALRLAADGAKVVIYDSneeaaeaLAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK05653  87 VNNAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARY-GRIVNISSVSGVTGNPGQTNYSAAKAGVIGFT 165

                        170       180
                 ....*....|....*....|....*.
gi 19075741  160 QTIMRELDPnWNIAITIVQPGGMQTE 185
Cdd:PRK05653 166 KALALELAS-RGITVNAVAPGFIDTD 190
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 7-198 1.30e-33

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: 123.15  E-value: 1.30e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:cd05344   3 VALVTAASSGIGLAIARALAREGARVAICARnrenlerAASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDIL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:cd05344  83 VNNAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERG-WGRIVNISSLTVKEPEPNLVLSNVARAGLIGLV 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19075741 160 QTIMRELDPNwNIAITIVQPGGMQTE-WASSNMQWAKPHP 198
Cdd:cd05344 162 KTLSRELAPD-GVTVNSVLPGYIDTErVRRLLEARAEKEG 200
PRK12826 PRK12826
SDR family oxidoreductase;
7-185 2.26e-33

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 122.33  E-value: 2.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD-------TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK12826   8 VALVTGAARGIGRAIAVRLAADGAEVIVVDICGDdaaataeLVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLDIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAG-YYPSPCLSMYNASKFAVEGL 158
Cdd:PRK12826  88 VANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAG-GGRIVLTSSVAGpRVGYPGLAHYAASKAGLVGF 166

                        170       180
                 ....*....|....*....|....*..
gi 19075741  159 SQTIMRELDPnWNIAITIVQPGGMQTE 185
Cdd:PRK12826 167 TRALALELAA-RNITVNSVHPGGVDTP 192
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 8-185 4.75e-33

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 121.45  E-value: 4.75e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNV-IACSRAP-------DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK05557   8 ALVTGASRGIGRAIAERLAAQGANVvINYASSEagaealvAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVDIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK05557  88 VNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMK-QRSGRIINISSVVGLMGNPGQANYAASKAGVIGFT 166

                        170       180
                 ....*....|....*....|....*.
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK05557 167 KSLARELASR-GITVNAVAPGFIETD 191
PRK08264 PRK08264
SDR family oxidoreductase;
6-188 4.88e-33

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 121.15  E-value: 4.88e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    6 STVLITGSSKGLGYALVKVGLAQG-YNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAkrrfGNVDIVINNAG 84
Cdd:PRK08264   7 KVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVTDLGPRVVPLQLDVTDPASVAAAAEAA----SDVTILVNNAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 YGLVGEF-ESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIM 163
Cdd:PRK08264  83 IFRTGSLlLEGDEDALRAEMETNYFGPLAMARAFAPVLAANG-GGAIVNVLSVLSWVNFPNLGTYSASKAAAWSLTQALR 161

                        170       180
                 ....*....|....*....|....*
gi 19075741  164 RELDPNwNIAITIVQPGGMQTEWAS 188
Cdd:PRK08264 162 AELAPQ-GTRVLGVHPGPIDTDMAA 185
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 9-185 1.14e-32

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 120.34  E-value: 1.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   9 LITGSSKGLGYALVKVGLAQGYNV-IACSRA------PDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:cd08934   7 LVTGASSGIGEATARALAAEGAAVaIAARRVdrlealADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRLDILVN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:cd08934  87 NAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLR-NKGTIVNISSVAGRVAVRNSAVYNATKFGVNAFSEG 165

                       170       180
                ....*....|....*....|....
gi 19075741 162 IMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd08934 166 LRQEVTER-GVRVVVIEPGTVDTE 188
PRK05993 PRK05993
SDR family oxidoreductase;
7-202 1.45e-32

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 120.90  E-value: 1.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIA-CSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGN-VDIVINNAG 84
Cdd:PRK05993   6 SILITGCSSGIGAYCARALQSDGWRVFAtCRKEEDVAALEAEGLEAFQLDYAEPESIAALVAQVLELSGGrLDALFNNGA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMR 164
Cdd:PRK05993  86 YGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQ-GRIVQCSSILGLVPMKYRGAYNASKFAIEGLSLTLRM 164

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19075741  165 ELDPNwNIAITIVQPGGMQTEWASSNMQWAKPHPAYEN 202
Cdd:PRK05993 165 ELQGS-GIHVSLIEPGPIETRFRANALAAFKRWIDIEN 201
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 8-189 2.24e-32

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: 119.15  E-value: 2.24e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT----IEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNA 83
Cdd:cd08929   3 ALVTGASRGIGEATARLLHAEGYRVGICARDEARLAaaaaQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  84 GYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIM 163
Cdd:cd08929  83 GVGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRG-GGTIVNVGSLAGKNAFKGGAAYNASKFGLLGLSEAAM 161

                       170       180
                ....*....|....*....|....*.
gi 19075741 164 RELDPnWNIAITIVQPGGMQTEWASS 189
Cdd:cd08929 162 LDLRE-ANIRVVNVMPGSVDTGFAGS 186
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-209 3.53e-32

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 119.20  E-value: 3.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD--------TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK12825   8 VALVTGAARGLGRAIALRLARAGADVVVHYRSDEeaaeelveAVEALGRRAQAVQADVTDKAALEAAVAAAVERFGRIDI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK12825  88 LVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQR-GGRIVNISSVAGLPGWPGRSNYAAAKAGLVGL 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMQTEwassnMQWAKPHPAYENDRSWRPF 209
Cdd:PRK12825 167 TKALARELAEY-GITVNMVAPGDIDTD-----MKEATIEEAREAKDAETPL 211
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 8-193 3.82e-32

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 118.94  E-value: 3.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSR--APDTITIEHSKLLKLKL-----DVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:cd05323   3 AIITGGASGIGLATAKLLLKKGAKVAILDRneNPGAAAELQAINPKVKAtfvqcDVTSWEQLAAAFKKAIEKFGRVDILI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  81 NNAG------YGLVGEFEsyniEEMHRQMNVNFWGVAYITKEALNLMRES--GKGGRILQISSVAGYYPSPCLSMYNASK 152
Cdd:cd05323  83 NNAGildeksYLFAGKLP----PPWEKTIDVNLTGVINTTYLALHYMDKNkgGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19075741 153 FAVEGLSQTIMRELDPNWNIAITIVQPGGMQTEWASSNMQW 193
Cdd:cd05323 159 HGVVGFTRSLADLLEYKTGVRVNAICPGFTNTPLLPDLVAK 199
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 7-185 7.04e-32

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 118.54  E-value: 7.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACS-------RAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK12939   9 RALVTGAARGLGAAFAEALAEAGATVAFNDglaaearELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAALGGLDGL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK12939  89 VNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSG-RGRIVNLASDTALWGAPKLGAYVASKGAVIGMT 167

                        170       180
                 ....*....|....*....|....*.
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK12939 168 RSLARELGGR-GITVNAIAPGLTATE 192
PRK06181 PRK06181
SDR family oxidoreductase;
7-185 7.85e-32

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 118.54  E-value: 7.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT-------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK06181   3 VVIITGASEGIGRALAVRLARAGAQLVLAARNETRlaslaqeLADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYN-IEEMHRQMNVNFWGVAYITKEALNLMRESGkgGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK06181  83 VNNAGITMWSRFDELTdLSVFERVMRVNYLGAVYCTHAALPHLKASR--GQIVVVSSLAGLTGVPTRSGYAASKHALHGF 160

                        170       180
                 ....*....|....*....|....*..
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK06181 161 FDSLRIELADD-GVAVTVVCPGFVATD 186
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 7-185 9.27e-32

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: 117.34  E-value: 9.27e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQG-YNVIACSRAPD-------TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05324   2 VALVTGANRGIGFEIVRQLAKSGpGTVILTARDVErgqaaveKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAG-YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPclsmYNASKFAVEG 157
Cdd:cd05324  82 LVNNAGiAFKGFDDSTPTREQARETMKTNFFGTVDVTQALLPLLKKS-PAGRIVNVSSGLGSLTSA----YGVSKAALNA 156

                       170       180
                ....*....|....*....|....*...
gi 19075741 158 LSQTIMRELdPNWNIAITIVQPGGMQTE 185
Cdd:cd05324 157 LTRILAKEL-KETGIKVNACCPGWVKTD 183
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-190 1.52e-31

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 117.48  E-value: 1.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI--TIEHSKLLKLKL-----DVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07666   9 NALITGAGRGIGRAVAIALAKEGVNVGLLARTEENLkaVAEEVEAYGVKVviataDVSDYEEVTAAIEQLKNELGSIDIL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK07666  89 INNAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIER-QSGDIINISSTAGQKGAAVTSAYSASKFGVLGLT 167

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQTEWASSN 190
Cdd:PRK07666 168 ESLMQEVRKH-NIRVTALTPSTVATDMAVDL 197
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 7-188 2.82e-31

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 117.35  E-value: 2.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEHSkllkLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07825   7 VVAITGGARGIGLATARALAALGARVAigdldeaLAKETAAELGLVVG----GPLDVTDPASFAAFLDAVEADLGPIDVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK07825  83 VNNAGVMPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGR-GHVVNVASLAGKIPVPGMATYCASKHAVVGFT 161

                        170       180
                 ....*....|....*....|....*....
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQTEWAS 188
Cdd:PRK07825 162 DAARLELRGT-GVHVSVVLPSFVNTELIA 189
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 6-191 3.54e-31

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: 115.92  E-value: 3.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAP---DTITIEHSKLLKLKLDVTDVKSvETAFKDAKR-RFGNVDIVIN 81
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDGYRVSLGLRNPedlAALSASGGDVEAVPYDARDPED-ARALVDALRdRFGRIDVLVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:cd08932  80 NAGIGRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGS-GRVVFLNSLSGKRVLAGNAGYSASKFALRALAHA 158

                       170       180       190
                ....*....|....*....|....*....|
gi 19075741 162 IMRELDPNwNIAITIVQPGGMQTEWASSNM 191
Cdd:cd08932 159 LRQEGWDH-GVRVSAVCPGFVDTPMAQGLT 187
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 13-189 5.58e-31

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 115.61  E-value: 5.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    13 SSKGLGYALVKVGLAQGYNVIACSRAPD------TITIEHSKLLkLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGYG 86
Cdd:pfam13561   4 NESGIGWAIARALAEEGAEVVLTDLNEAlakrveELAEELGAAV-LPCDVTDEEQVEALVAAAVEKFGRLDILVNNAGFA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    87 --LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMR 164
Cdd:pfam13561  83 pkLKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKE---GGSIVNLSSIGAERVVPNYNAYGAAKAALEALTRYLAV 159

                         170       180
                  ....*....|....*....|....*
gi 19075741   165 ELDPNwNIAITIVQPGGMQTEWASS 189
Cdd:pfam13561 160 ELGPR-GIRVNAISPGPIKTLAASG 183
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 7-186 1.32e-30

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


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 115.25  E-value: 1.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVkVGLA----QGYNVIACSR---------------APDTITIehskllkLKLDVTDVKSVETAFK 67
Cdd:cd09806   2 VVLITGCSSGIGLHLA-VRLAsdpsKRFKVYATMRdlkkkgrlweaagalAGGTLET-------LQLDVCDSKSVAAAVE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  68 DAKRRfgNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSM 147
Cdd:cd09806  74 RVTER--HVDVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRR-GSGRILVTSSVGGLQGLPFNDV 150

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19075741 148 YNASKFAVEGLSQTIMRELDPnWNIAITIVQPGGMQTEW 186
Cdd:cd09806 151 YCASKFALEGLCESLAVQLLP-FNVHLSLIECGPVHTAF 188
FabG-like PRK07231
SDR family oxidoreductase;
7-191 1.36e-30

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 114.93  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL------LKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK07231   7 VAIVTGASSGIGEGIARRFAAEGARVVVTDRNEEAAERVAAEIlaggraIAVAADVSDEADVEAAVAAALERFGSVDILV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLV-GEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK07231  87 NNAGTTHRnGPLLDVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEG-GGAIVNVASTAGLRPRPGLGWYNASKGAVITLT 165

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19075741  160 QTIMRELDPnWNIAITIVQPGGMQTEWASSNM 191
Cdd:PRK07231 166 KALAAELGP-DKIRVNAVAPVVVETGLLEAFM 196
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
9-184 1.33e-29

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 112.51  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYA----LVKVGLAQG---YNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK08643   6 LVTGAGQGIGFAiakrLVEDGFKVAivdYNEETAQAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGDLNVVVN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:PRK08643  86 NAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGHGGKIINATSQAGVVGNPELAVYSSTKFAVRGLTQT 165

                        170       180
                 ....*....|....*....|...
gi 19075741  162 IMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK08643 166 AARDLASE-GITVNAYAPGIVKT 187
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 7-185 2.25e-29

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


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 111.57  E-value: 2.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD-------TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:cd05339   1 IVLITGGGSGIGRLLALEFAKRGAKVVILDINEKgaeetanNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:cd05339  81 INNAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLER-NHGHIVTIASVAGLISPAGLADYCASKAAAVGFH 159

                       170       180       190
                ....*....|....*....|....*....|
gi 19075741 160 QTIMREL----DPnwNIAITIVQPGGMQTE 185
Cdd:cd05339 160 ESLRLELkaygKP--GIKTTLVCPYFINTG 187
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 6-185 5.01e-29

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: 110.83  E-value: 5.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL--------LKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAKLILTGRRAERLQELADELgakfpvkvLPLQLDVSDRESIEAALENLPEEFRDID 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGL-VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:cd05346  81 ILVNNAGLALgLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQ-GHIINLGSIAGRYPYAGGNVYCATKAAVR 159

                       170       180
                ....*....|....*....|....*....
gi 19075741 157 GLSQTIMRELdPNWNIAITIVQPGGMQTE 185
Cdd:cd05346 160 QFSLNLRKDL-IGTGIRVTNIEPGLVETE 187
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 7-185 4.77e-28

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 108.02  E-value: 4.77e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIAC--SRAPDTITIEHSKLLK-----LKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:cd05333   2 VALVTGASRGIGRAIALRLAAEGAKVAVTdrSEEAAAETVEEIKALGgnaaaLEADVSDREAVEALVEKVEAEFGPVDIL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:cd05333  82 VNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRS-GRIINISSVVGLIGNPGQANYAASKAGVIGFT 160

                       170       180
                ....*....|....*....|....*.
gi 19075741 160 QTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd05333 161 KSLAKELASR-GITVNAVAPGFIDTD 185
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 9-185 4.86e-28

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 108.29  E-value: 4.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVI---ACSRAP-----DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK12937   9 IVTGASRGIGAAIARRLAADGFAVAvnyAGSAAAadelvAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRIDVLV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK12937  89 NNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQ---GGRIINLSTSVIALPLPGYGPYAASKAAVEGLVH 165

                        170       180
                 ....*....|....*....|....*
gi 19075741  161 TIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK12937 166 VLANELRGR-GITVNAVAPGPVATE 189
PRK05650 PRK05650
SDR family oxidoreductase;
8-189 6.60e-28

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 108.59  E-value: 6.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNViACSRAPDTITIEHSKLLK--------LKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK05650   3 VMITGAASGLGRAIALRWAREGWRL-ALADVNEEGGEETLKLLReaggdgfyQRCDVRDYSQLTALAQACEEKWGGIDVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK05650  82 VNNAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQK-SGRIVNIASMAGLMQGPAMSSYNVAKAGVVALS 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQTEWASS 189
Cdd:PRK05650 161 ETLLVELADD-EIGVHVVCPSFFQTNLLDS 189
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-189 1.58e-27

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 106.85  E-value: 1.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVI---------ACSRApDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK05565   7 VAIVTGASGGIGRAIAELLAKEGAKVViaydineeaAQELL-EEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:PRK05565  86 ILVNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIK-RKSGVIVNISSIWGLIGASCEVLYSASKGAVNA 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19075741  158 LSQTIMRELDPnWNIAITIVQPGGMQTEWASS 189
Cdd:PRK05565 165 FTKALAKELAP-SGIRVNAVAPGAIDTEMWSS 195
PRK08017 PRK08017
SDR family oxidoreductase;
7-198 1.98e-27

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 106.71  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTItiEHSKLLKLK---LDVTDVKSVETAFKDA-----KRRFGnvdi 78
Cdd:PRK08017   4 SVLITGCSSGIGLEAALELKRRGYRVLAACRKPDDV--ARMNSLGFTgilLDLDDPESVERAADEVialtdNRLYG---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK08017  78 LFNNAGFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGE-GRIVMTSSVMGLISTPGRGAYAASKYALEAW 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMQTEWASSNMQWAKPHP 198
Cdd:PRK08017 157 SDALRMELRHS-GIKVSLIEPGPIRTRFTDNVNQTQSDKP 195
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 6-199 2.91e-27

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


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 105.95  E-value: 2.91e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKVGLAQGY-NVIACSRAPDTIT---IEH-SKLLKLKLDVTDVKSVETAFKDAKrrfgNVDIVI 80
Cdd:cd05354   4 KTVLVTGANRGIGKAFVESLLAHGAkKVYAAVRDPGSAAhlvAKYgDKVVPLRLDVTDPESIKAAAAQAK----DVDVVI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  81 NNAGYGLV-GEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:cd05354  80 NNAGVLKPaTLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGA-IVNLNSVASLKNFPAMGTYSASKSAAYSLT 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19075741 160 QTIMRELDPNwNIAITIVQPGGMQTEWAsSNMQWAKPHPA 199
Cdd:cd05354 159 QGLRAELAAQ-GTLVLSVHPGPIDTRMA-AGAGGPKESPE 196
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 8-185 3.09e-27

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: 105.87  E-value: 3.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLK-------LDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELKAELLNPNpsveveiLDVTDEERNQLVIAELEAELGGLDLVI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILqISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:cd05350  81 INAGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVL-ISSVAALRGLPGAAAYSASKAALSSLAE 159

                       170       180
                ....*....|....*....|....*
gi 19075741 161 TIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd05350 160 SLRYDVKKR-GIRVTVINPGFIDTP 183
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 9-185 6.62e-27

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: 105.05  E-value: 6.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   9 LITGSSKGLGYALVKVGLAQGYNVI--------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:cd05362   7 LVTGASRGIGRAIAKRLARDGASVVvnyasskaAAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVDILV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:cd05362  87 NNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRD---GGRIINISSSLTAAYTPNYGAYAGSKAAVEAFTR 163

                       170       180
                ....*....|....*....|....*
gi 19075741 161 TIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd05362 164 VLAKELGGR-GITVNAVAPGPVDTD 187
PRK08267 PRK08267
SDR family oxidoreductase;
1-184 1.83e-26

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 104.25  E-value: 1.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFstvlITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI-----TIEHSKLLKLKLDVTDVKSVETAFKD-AKRRFG 74
Cdd:PRK08267   1 MKSIF----ITGAASGIGRATALLFAAEGWRVGAYDINEAGLaalaaELGAGNAWTGALDVTDRAAWDAALADfAAATGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   75 NVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:PRK08267  77 RLDVLFNNAGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKAT-PGARVINTSSASAIYGQPGLAVYSATKFA 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19075741  155 VEGLSQTimreLDPNW---NIAITIVQPGGMQT 184
Cdd:PRK08267 156 VRGLTEA----LDLEWrrhGIRVADVMPLFVDT 184
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 7-208 2.29e-26

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


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 104.00  E-value: 2.29e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT---ITIE-HSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:cd05341   7 VAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEgqaAAAElGDAARFFHLDVTDEDGWTAVVDTAREAFGRLDVLVNN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:cd05341  87 AGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAG-GGSIINMSSIEGLVGDPALAAYNASKGAVRGLTKSA 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 19075741 163 MRELDP-NWNIAITIVQPGGMQTEWassnMQWAKPHPAYENDRSWRP 208
Cdd:cd05341 166 ALECATqGYGIRVNSVHPGYIYTPM----TDELLIAQGEMGNYPNTP 208
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
8-154 4.35e-26

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 107.62  E-value: 4.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL------LKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK08324 425 ALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELggpdraLGVACDVTDEAAVQAAFEEAALAFGGVDIVVS 504

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075741   82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:PRK08324 505 NAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGGSIVFIASKNAVNPGPNFGAYGAAKAA 577
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 9-236 6.91e-26

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: 102.59  E-value: 6.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   9 LITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI--------TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:cd05343  10 LVTGASVGIGAAVARALVQHGMKVVGCARRVDKIealaaecqSAGYPTLFPYQCDLSNEEQILSMFSAIRTQHQGVDVCI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESG-KGGRILQISSVAG--YYPSPCLSMYNASKFAVEG 157
Cdd:cd05343  90 NNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNvDDGHIININSMSGhrVPPVSVFHFYAATKHAVTA 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741 158 LSQTIMREL-DPNWNIAITIVQPGGMQTEWASSnmqwakphpayendrswrpfwenyhgCEETDPNKAAELLYSIAKLDR 236
Cdd:cd05343 170 LTEGLRQELrEAKTHIRATSISPGLVETEFAFK--------------------------LHDNDPEKAAATYESIPCLKP 223
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 7-185 8.18e-26

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: 102.44  E-value: 8.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKvGLA-QGYNVIACSRAPDTITIEHSKLLK-------LKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05347   7 VALVTGASRGIGFGIAS-GLAeAGANIVINSRNEEKAEEAQQLIEKegveataFTCDVSDEEAIKAAVEAIEEDFGKIDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd05347  86 LVNNAGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQG-HGKIINICSLLSELGGPPVPAYAASKGGVAGL 164

                       170       180
                ....*....|....*....|....*..
gi 19075741 159 SQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd05347 165 TKALATEWARH-GIQVNAIAPGYFATE 190
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 3-213 4.33e-25

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 100.48  E-value: 4.33e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   3 STFS----TVLITGSSKGLGYALVKVGLAQGYNV--IACSRAPD-----TITIEHSKLLK-LKLDVTDVKSVETAFKDAK 70
Cdd:cd05352   2 DLFSlkgkVAIVTGGSRGIGLAIARALAEAGADVaiIYNSAPRAeekaeELAKKYGVKTKaYKCDVSSQESVEKTFKQIQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  71 RRFGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILqISSVAGY---YPSPClSM 147
Cdd:cd05352  82 KDFGKIDILIANAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLII-TASMSGTivnRPQPQ-AA 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075741 148 YNASKFAVEGLSQTIMREldpnW---NIAITIVQPGGMQTEWassnmqwakphpAYENDRSWRPFWENY 213
Cdd:cd05352 160 YNASKAAVIHLAKSLAVE----WakyFIRVNSISPGYIDTDL------------TDFVDKELRKKWESY 212
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 7-196 9.25e-25

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 99.77  E-value: 9.25e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAP--------DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05358   5 VALVTGASSGIGKAIAIRLATAGANVVVNYRSKedaaeevvEEIKAVGGKAIAVQADVSKEEDVVALFQSAIKEFGTLDI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGygLVGEFESYNI--EEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:cd05358  85 LVNNAG--LQGDASSHEMtlEDWNKVIDVNLTGQFLCAREAIKRFRKSKIKGKIINMSSVHEKIPWPGHVNYAASKGGVK 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19075741 157 GLSQTIMRELDPnWNIAITIVQPGGMQTewASSNMQWAKP 196
Cdd:cd05358 163 MMTKTLAQEYAP-KGIRVNAIAPGAINT--PINAEAWDDP 199
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 8-219 1.48e-24

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: 98.68  E-value: 1.48e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI-----TIEHSKLLKLKLDVTDVKSVETAFKD-AKRRFGNVDIVIN 81
Cdd:cd08931   3 IFITGAASGIGRETALLFARNGWFVGLYDIDEDGLaalaaELGAENVVAGALDVTDRAAWAAALADfAAATGGRLDALFN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:cd08931  83 NAGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKAT-PGARVINTASSSAIYGQPDLAVYSATKFAVRGLTEA 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075741 162 imreLDPNW---NIAITIVQPGGMQTEWASSNMQWAKPHP----AYENDRSWRPFWENYHGCEET 219
Cdd:cd08931 162 ----LDVEWarhGIRVADVWPWFVDTPILTKGETGAAPKKglgrVLPVSDVAKVVWAAAHGVPKL 222
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 8-154 3.49e-24

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 98.23  E-value: 3.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL------LKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:cd08943   4 ALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAEKVAEAAqggpraLGVQCDVTSEAQVQSAFEQAVLEFGGLDIVVS 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075741  82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:cd08943  84 NAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAA 156
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-185 4.57e-24

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 101.46  E-value: 4.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL----LKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNA 83
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLgpdhHALAMDVSDEAQIREGFEQLHREFGRIDVLVNNA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   84 GygLVGEFESYNI----EEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK06484  88 G--VTDPTMTATLdttlEEFARLQAINLTGAYLVAREALRLMIEQGHGAAIVNVASGAGLVALPKRTAYSASKAAVISLT 165

                        170       180
                 ....*....|....*....|....*.
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK06484 166 RSLACEWAAK-GIRVNAVLPGYVRTQ 190
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-167 4.78e-24

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 96.99  E-value: 4.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAP---DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd05370   1 MKLTGNTVLITGGTSGIGLALARKFLEAGNTVIITGRREerlAEAKKELPNIHTIVLDVGDAESVEALAEALLSEYPNLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGLVGEF--ESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNASKFAV 155
Cdd:cd05370  81 ILINNAGIQRPIDLrdPASDLDKADTEIDTNLIGPIRLIKAFLPHLKKQPEAT-IVNVSSGLAFVPMAANPVYCATKAAL 159

                       170
                ....*....|..
gi 19075741 156 EGLSQTIMRELD 167
Cdd:cd05370 160 HSYTLALRHQLK 171
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 8-196 6.33e-24

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 97.17  E-value: 6.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSR--APDTITIEHSKLLKLKL---DVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK12828  10 VAITGGFGGLGRATAAWLAARGARVALIGRgaAPLSQTLPGVPADALRIggiDLVDPQAARRAVDEVNRQFGRLDALVNI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:PRK12828  90 AGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASG-GGRIVNIGAGAALKAGPGMGAYAAAKAGVARLTEAL 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19075741  163 MRELDPNwNIAITIVQPGGMQTEWASSNM------QWAKP 196
Cdd:PRK12828 169 AAELLDR-GITVNAVLPSIIDTPPNRADMpdadfsRWVTP 207
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 8-191 1.62e-23

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 96.33  E-value: 1.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT-----------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:PRK12827   9 VLITGGSGGLGRAIAVRLAADGADVIVLDIHPMRgraeadavaagIEAAGGKALGLAFDVRDFAATRAALDAGVEEFGRL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   77 DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK12827  89 DILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALPPMIRARRGGRIVNIASVAGVRGNRGQVNYAASKAGLI 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19075741  157 GLSQTIMRELDPNwNIAITIVQPGG---------MQTEWASSNM 191
Cdd:PRK12827 169 GLTKTLANELAPR-GITVNAVAPGAintpmadnaAPTEHLLNPV 211
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 7-165 1.70e-23

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 96.49  E-value: 1.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK12429   6 VALVTGAASGIGLEIALALAKEGAKVViadlndeAAAAAAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDIL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK12429  86 VNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQG-GGRIINMASVHGLVGSAGKAAYVSAKHGLIGLT 164


                 ....*.
gi 19075741  160 QTIMRE 165
Cdd:PRK12429 165 KVVALE 170
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 6-187 2.17e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 95.88  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHS----KLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK06841  16 KVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQllggNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILVN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:PRK06841  96 SAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAG-GGKIVNLASQAGVVALERHVAYCASKAGVVGMTKV 174

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19075741  162 IMRELDPnWNIAITIVQPGGMQTE-----WA 187
Cdd:PRK06841 175 LALEWGP-YGITVNAISPTVVLTElgkkaWA 204
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 1-162 2.30e-23

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 95.61  E-value: 2.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT---ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:COG3967   1 MKLTGNTILITGGTSGIGLALAKRLHARGNTVIITGRREEKleeAAAANPGLHTIVLDVADPASIAALAEQVTAEFPDLN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGLVGEF--ESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFAV 155
Cdd:COG3967  81 VLINNAGIMRAEDLldEAEDLADAEREITTNLLGPIRLTAAFLPHLKAQ-PEAAIVNVSSGLAFVPLAVTPTYSATKAAL 159


                ....*..
gi 19075741 156 EGLSQTI 162
Cdd:COG3967 160 HSYTQSL 166
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 7-206 2.87e-23

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 95.85  E-value: 2.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTItiEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAG-- 84
Cdd:PRK06171  11 IIIVTGGSSGIGLAIVKELLANGANVVNADIHGGDG--QHENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNNAGin 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 --------YGLVGEFEsYNIEEMHRQMNVNFWGVAYITKEALNLMrESGKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK06171  89 iprllvdeKDPAGKYE-LNEAAFDKMFNINQKGVFLMSQAVARQM-VKQHDGVIVNMSSEAGLEGSEGQSCYAATKAALN 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19075741  157 GLSQTIMRELDPnWNIAITIVQPG-----GMQTewassnmqwakphPAYENDRSW 206
Cdd:PRK06171 167 SFTRSWAKELGK-HNIRVVGVAPGileatGLRT-------------PEYEEALAY 207
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-192 3.98e-23

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 95.17  E-value: 3.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYAlVKVGLA-QGYNVI--ACSRAPD---TITI---EHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK06077   8 VVVVTGSGRGIGRA-IAVRLAkEGSLVVvnAKKRAEEmneTLKMvkeNGGEGIGVLADVSTREGCETLAKATIDRYGVAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:PRK06077  87 ILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMRE---GGAIVNIASVAGIRPAYGLSIYGAMKAAVIN 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19075741  158 LSQTIMRELDPnwNIAITIVQPGGMQTEWASSNMQ 192
Cdd:PRK06077 164 LTKYLALELAP--KIRVNAIAPGFVKTKLGESLFK 196
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 8-185 4.94e-23

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


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 94.67  E-value: 4.94e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYN-VIACSRAPD------TITIEHSKLLKLKLDVTD-----VKSVETAFKDAKrrfgn 75
Cdd:cd05325   1 VLITGASRGIGLELVRQLLARGNNtVIATCRDPSaatelaALGASHSRLHILELDVTDeiaesAEAVAERLGDAG----- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  76 VDIVINNAG----YGLVGEFESyniEEMHRQMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAG---YYPSPCLSMY 148
Cdd:cd05325  76 LDVLINNAGilhsYGPASEVDS---EDLLEVFQVNVLGPLLLTQAFLPLLLK-GARAKIINISSRVGsigDNTSGGWYSY 151

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19075741 149 NASKFAVEGLSQTIMRELDPNWnIAITIVQPGGMQTE 185
Cdd:cd05325 152 RASKAALNMLTKSLAVELKRDG-ITVVSLHPGWVRTD 187
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
7-202 5.02e-23

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 95.09  E-value: 5.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNV----IACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK07067   8 VALLTGAASGIGEAVAERYLAEGARVviadIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFNN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AGYglvgeFESYNIEEMH-----RQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:PRK07067  88 AAL-----FDMAPILDISrdsydRLFAVNVKGLFFLMQAVARHMVEQGRGGKIINMASQAGRRGEALVSHYCATKAAVIS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 19075741  158 LSQTIMRELDPNwNIAITIVQPGGMQTE-WASSNMQWAKphpaYEN 202
Cdd:PRK07067 163 YTQSAALALIRH-GINVNAIAPGVVDTPmWDQVDALFAR----YEN 203
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-194 7.01e-23

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: 94.46  E-value: 7.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGYGL 87
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAGVLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  88 VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMRELD 167
Cdd:cd05331  81 PGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRR-TGAIVTVASNAAHVPRISMAAYGASKAALASLSKCLGLELA 159

                       170       180
                ....*....|....*....|....*..
gi 19075741 168 PnWNIAITIVQPGGMQTEwassnMQWA 194
Cdd:cd05331 160 P-YGVRCNVVSPGSTDTA-----MQRT 180
PRK07454 PRK07454
SDR family oxidoreductase;
1-192 8.50e-23

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 94.26  E-value: 8.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFS-TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLK-------LKLDVTDVKSVETAFKDAKRR 72
Cdd:PRK07454   1 MSLNSMpRALITGASSGIGKATALAFAKAGWDLALVARSQDALEALAAELRStgvkaaaYSIDLSNPEAIAPGIAELLEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   73 FGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASK 152
Cdd:PRK07454  81 FGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARG-GGLIINVSSIAARNAFPQWGAYCVSK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19075741  153 FAVEGLSQTIMRELDPNwNIAITIVQPGGMQTE-WASSNMQ 192
Cdd:PRK07454 160 AALAAFTKCLAEEERSH-GIRVCTITLGAVNTPlWDTETVQ 199
PRK06398 PRK06398
aldose dehydrogenase; Validated
 8-188 1.83e-22

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 93.74  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRA-PDTITIEHskllkLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGYG 86
Cdd:PRK06398   9 AIVTGGSQGIGKAVVNRLKEEGSNVINFDIKePSYNDVDY-----FKVDVSNKEQVIKGIDYVISKYGRIDILVNNAGIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   87 LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMREL 166
Cdd:PRK06398  84 SYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGV-IINIASVQSFAVTRNAAAYVTSKHAVLGLTRSIAVDY 162

                        170       180
                 ....*....|....*....|....*
gi 19075741  167 DPnwNIAITIVQPGGMQT---EWAS 188
Cdd:PRK06398 163 AP--TIRCVAVCPGSIRTpllEWAA 185
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
7-188 2.47e-22

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 92.91  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIE--------HSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK12824   4 IALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDwfeeygftEDQVRLKELDVTDTEECAEALAEIEEEEGPVDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK12824  84 LVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQG-YGRIINISSVNGLKGQFGQTNYSAAKAGMIGF 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 19075741  159 SQTIMRELDPnWNIAITIVQPGGMQTEWAS 188
Cdd:PRK12824 163 TKALASEGAR-YGITVNCIAPGYIATPMVE 191
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
2-189 2.73e-22

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 93.33  E-value: 2.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    2 KSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAP------DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGN 75
Cdd:PRK08226   3 KLTGKTALITGALQGIGEGIARVFARHGANLILLDISPeieklaDELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   76 VDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAG-YYPSPCLSMYNASKFA 154
Cdd:PRK08226  83 IDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARK-DGRIVMMSSVTGdMVADPGETAYALTKAA 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19075741  155 VEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASS 189
Cdd:PRK08226 162 IVGLTKSLAVEYAQS-GIRVNAICPGYVRTPMAES 195
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 7-194 3.92e-22

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 92.64  E-value: 3.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPdtITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGYG 86
Cdd:PRK08220  10 TVWVTGAAQGIGYAVALAFVEAGAKVIGFDQAF--LTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGPLDVLVNAAGIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   87 LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMREL 166
Cdd:PRK08220  88 RMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQ-RSGAIVTVGSNAAHVPRIGMAAYGASKAALTSLAKCVGLEL 166

                        170       180
                 ....*....|....*....|....*...
gi 19075741  167 DPnWNIAITIVQPGGMQTEwassnMQWA 194
Cdd:PRK08220 167 AP-YGVRCNVVSPGSTDTD-----MQRT 188
PRK08219 PRK08219
SDR family oxidoreductase;
7-183 8.80e-22

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 91.15  E-value: 8.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKvGLAQGYNVIACSRAP---DTITIEHSKLLKLKLDVTDVKSVETAFKdakrRFGNVDIVINNA 83
Cdd:PRK08219   5 TALITGASRGIGAAIAR-ELAPTHTLLLGGRPAerlDELAAELPGATPFPVDLTDPEAIAAAVE----QLGRLDVLVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   84 GYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTiM 163
Cdd:PRK08219  80 GVADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAA--HGHVVFINSGAGLRANPGWGSYAASKFALRALADA-L 156

                        170       180
                 ....*....|....*....|....
gi 19075741  164 RELDPNwNIAITIVQPG----GMQ 183
Cdd:PRK08219 157 REEEPG-NVRVTSVHPGrtdtDMQ 179
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 7-184 9.44e-22

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 91.88  E-value: 9.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLG----YALVKVGLA---QGYNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK13394   9 TAVVTGAASGIGkeiaLELARAGAAvaiADLNQDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAERFGSVDIL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK13394  89 VSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKDDRGGVVIYMGSVHSHEASPLKSAYVTAKHGLLGLA 168

                        170       180
                 ....*....|....*....|....*
gi 19075741  160 QTIMRElDPNWNIAITIVQPGGMQT 184
Cdd:PRK13394 169 RVLAKE-GAKHNVRSHVVCPGFVRT 192
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 7-179 1.37e-21

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 90.91  E-value: 1.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIAC----SRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:cd05345   7 VAIVTGAGSGFGEGIARRFAQEGARVVIAdinaDGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDILVNN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  83 AGYG-LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:cd05345  87 AGIThRNKPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQG-GGVIINIASTAGLRPRPGLTWYNASKGWVVTATKA 165

                       170
                ....*....|....*...
gi 19075741 162 IMRELDPNwNIAITIVQP 179
Cdd:cd05345 166 MAVELAPR-NIRVNCLCP 182
PRK07856 PRK07856
SDR family oxidoreductase;
7-185 2.75e-21

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 90.38  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR----APDTITIEHskllkLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK07856   8 VVLVTGGTRGIGAGIARAFLAAGATVVVCGRrapeTVDGRPAEF-----HAADVRDPDQVAALVDAIVERHGRLDVLVNN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AG---YGLVGEFEsyniEEMHRQ-MNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK07856  83 AGgspYALAAEAS----PRFHEKiVELNLLAPLLVAQAANAVMQQQPGGGSIVNIGSVSGRRPSPGTAAYGAAKAGLLNL 158

                        170       180
                 ....*....|....*....|....*..
gi 19075741  159 SQTIMRELDPnwNIAITIVQPGGMQTE 185
Cdd:PRK07856 159 TRSLAVEWAP--KVRVNAVVVGLVRTE 183
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-197 2.78e-21

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 90.16  E-value: 2.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTF----STVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL--LKLKLDVTDVKSVETAFKDAkrrfG 74
Cdd:PRK07060   1 MNMAFdfsgKSVLVTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETgcEPLRLDVGDDAAIRAALAAA----G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   75 NVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:PRK07060  77 AFDGLVNCAGIASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGRGGSIVNVSSQAALVGLPDHLAYCASKAA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19075741  155 VEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASsnMQWAKPH 197
Cdd:PRK07060 157 LDAITRVLCVELGPH-GIRVNSVNPTVTLTPMAA--EAWSDPQ 196
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 7-180 3.03e-21

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 90.48  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKvGLAQ-GYNVI-------ACSRAPDTITIEH--SKLLKLKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:PRK12384   4 VAVVIGGGQTLGAFLCH-GLAEeGYRVAvadinseKAANVAQEINAEYgeGMAYGFGADATSEQSVLALSRGVDEIFGRV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   77 DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK12384  83 DLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGV 162

                        170       180
                 ....*....|....*....|....
gi 19075741  157 GLSQTIMRELDPnWNIAITIVQPG 180
Cdd:PRK12384 163 GLTQSLALDLAE-YGITVHSLMLG 185
PRK07069 PRK07069
short chain dehydrogenase; Validated
 9-162 4.28e-21

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 89.77  E-value: 4.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVI--------ACSRAPDTITIEHSK--LLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK07069   3 FITGAAGGLGRAIARRMAEQGAKVFltdindaaGLDAFAAEINAAHGEgvAFAAVQDVTDEAQWQALLAQAADAMGGLSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK07069  83 LVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPAS-IVNISSVAAFKAEPDYTAYNASKAAVASL 161


                 ....
gi 19075741  159 SQTI 162
Cdd:PRK07069 162 TKSI 165
PRK06194 PRK06194
hypothetical protein; Provisional
 7-166 4.42e-21

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 90.46  E-value: 4.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK06194   8 VAVITGAASGFGLAFARIGAALGMKLVladvqqdALDRAVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHLL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGK-----GGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:PRK06194  88 FNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEkdpayEGHIVNTASMAGLLAPPAMGIYNVSKHA 167

                        170
                 ....*....|..
gi 19075741  155 VEGLSQTIMREL 166
Cdd:PRK06194 168 VVSLTETLYQDL 179
PRK07832 PRK07832
SDR family oxidoreductase;
8-184 8.75e-21

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 89.33  E-value: 8.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI--TIEHSK------LLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07832   3 CFVTGAASGIGRATALRLAAQGAELFLTDRDADGLaqTVADARalggtvPEHRALDISDYDAVAAFAADIHAAHGSMDVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK07832  83 MNIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGRGGHLVNVSSAAGLVALPWHAAYSASKFGLRGLS 162

                        170       180
                 ....*....|....*....|....*
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK07832 163 EVLRFDLARH-GIGVSVVVPGAVKT 186
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 7-184 1.27e-20

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 88.66  E-value: 1.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVI-------ACSRA-PDTITIEHS-KLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd08940   4 VALVTGSTSGIGLGIARALAAAGANIVlngfgdaAEIEAvRAGLAAKHGvKVLYHGADLSKPAAIEDMVAYAQRQFGGVD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:cd08940  84 ILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQG-WGRIINIASVHGLVASANKSAYVAAKHGVVG 162

                       170       180
                ....*....|....*....|....*..
gi 19075741 158 LSQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:cd08940 163 LTKVVALETAGT-GVTCNAICPGWVLT 188
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 7-191 1.38e-20

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 88.22  E-value: 1.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR---------APDTI-TIEHS---------KLLKLKLDVTDVKSVETAFK 67
Cdd:cd05338   5 VAFVTGASRGIGRAIALRLAKAGATVVVAAKtasegdngsAKSLPgTIEETaeeieaaggQALPIVVDVRDEDQVRALVE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  68 DAKRRFGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSM 147
Cdd:cd05338  85 ATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQ-GHILNISPPLSLRPARGDVA 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19075741 148 YNASKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASSNM 191
Cdd:cd05338 164 YAAGKAGMSRLTLGLAAELRRH-GIAVNSLWPSTAIETPAATEL 206
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 8-199 2.64e-20

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


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 87.53  E-value: 2.64e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAP---DTITIEHSKLLKLKLDVTDVKSVETAFKDAkrrfGNVDIVINNAG 84
Cdd:cd05351  10 ALVTGAGKGIGRATVKALAKAGARVVAVSRTQadlDSLVRECPGIEPVCVDLSDWDATEEALGSV----GPVDLLVNNAA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  85 YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMR 164
Cdd:cd05351  86 VAILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVPGSIVNVSSQASQRALTNHTVYCSTKAALDMLTKVMAL 165

                       170       180       190
                ....*....|....*....|....*....|....*
gi 19075741 165 ELDPNwNIAITIVQPGGMQTEWASSNmqWAKPHPA 199
Cdd:cd05351 166 ELGPH-KIRVNSVNPTVVMTDMGRDN--WSDPEKA 197
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 7-166 2.78e-20

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 88.49  E-value: 2.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITI------EHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK05872  11 VVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAAlaaelgGDDRVLTVVADVTDLAAMQAAAEEAVERFGGIDVVV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK05872  91 ANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR--GYVLQVSSLAAFAAAPGMAAYCASKAGVEAFAN 168


                 ....*.
gi 19075741  161 TIMREL 166
Cdd:PRK05872 169 ALRLEV 174
PRK05855 PRK05855
SDR family oxidoreductase;
8-180 2.87e-20

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 90.43  E-value: 2.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYAlVKVGLA-QGYNVIACSRAPDTI--TIEHSKLLKL-----KLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK05855 318 VVVTGAGSGIGRE-TALAFArEGAEVVASDIDEAAAerTAELIRAAGAvahayRVDVSDADAMEAFAEWVRAEHGVPDIV 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK05855 397 VNNAGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGTGGHIVNVASAAAYAPSRSLPAYATSKAAVLMLS 476

                        170       180
                 ....*....|....*....|.
gi 19075741  160 QTIMRELDpNWNIAITIVQPG 180
Cdd:PRK05855 477 ECLRAELA-AAGIGVTAICPG 496
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 7-189 3.29e-20

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 87.13  E-value: 3.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVI-----ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:cd05349   2 VVLVTGASRGLGAAIARSFAREGARVVvnyyrSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIVN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  82 NA--GYGLVGE----FESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAV 155
Cdd:cd05349  82 NAliDFPFDPDqrktFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGS-GRVINIGTNLFQNPVVPYHDYTTAKAAL 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 19075741 156 EGLSQTIMRELDPnWNIAITIVQPGGMQTEWASS 189
Cdd:cd05349 161 LGFTRNMAKELGP-YGITVNMVSGGLLKVTDASA 193
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 7-189 3.30e-20

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


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 87.59  E-value: 3.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:cd08945   5 VALVTGATSGIGLAIARRLGKEGLRVFVCARgeeglatTVKELREAGVEADGRTCDVRSVPEIEALVAAAVARYGPIDVL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNL--MRESGKgGRILQISSVAG----YYPSPclsmYNASKF 153
Cdd:cd08945  85 VNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGT-GRIINIASTGGkqgvVHAAP----YSASKH 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19075741 154 AVEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASS 189
Cdd:cd08945 160 GVVGFTKALGLELART-GITVNAVCPGFVETPMAAS 194
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-190 4.71e-20

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 87.15  E-value: 4.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIAC--SRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAG 84
Cdd:PRK06463   9 VALITGGTRGIGRAIAEAFLREGAKVAVLynSAENEAKELREKGVFTIKCDVGNRDQVKKSKEVVEKEFGRVDVLVNNAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSP-CLSMYNASKFAVEGLSQTIM 163
Cdd:PRK06463  89 IMYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLS-KNGAIVNIASNAGIGTAAeGTTFYAITKAGIIILTRRLA 167

                        170       180
                 ....*....|....*....|....*..
gi 19075741  164 RELDpNWNIAITIVQPGGMQTEWASSN 190
Cdd:PRK06463 168 FELG-KYGIRVNAVAPGWVETDMTLSG 193
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 6-184 6.49e-20

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


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 86.57  E-value: 6.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAP---DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:cd05371   3 LVAVVTGGASGLGLATVERLLAQGAKVVILDLPNspgETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIVVNC 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  83 AG-------YGLVGEFEsYNIEEMHRQMNVNFWGVAYITKEALNLMRES-----GKGGRILQISSVAGYYPSPCLSMYNA 150
Cdd:cd05371  83 AGiavaaktYNKKGQQP-HSLELFQRVINVNLIGTFNVIRLAAGAMGKNepdqgGERGVIINTASVAAFEGQIGQAAYSA 161

                       170       180       190
                ....*....|....*....|....*....|....
gi 19075741 151 SKFAVEGLSQTIMRELDPnWNIAITIVQPGGMQT 184
Cdd:cd05371 162 SKGGIVGMTLPIARDLAP-QGIRVVTIAPGLFDT 194
PRK06484 PRK06484
short chain dehydrogenase; Validated
 7-184 8.45e-20

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 89.14  E-value: 8.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD-------TITIEHsklLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK06484 271 VVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEgakklaeALGDEH---LSVQADITDEAAVESAFAQIQARWGRLDVL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAgyGLVGEF---ESYNIEEMHRQMNVNFWGVAYITKEALNLMResgKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK06484 348 VNNA--GIAEVFkpsLEQSAEDFTRVYDVNLSGAFACARAAARLMS---QGGVIVNLGSIASLLALPPRNAYCASKAAVT 422

                        170       180
                 ....*....|....*....|....*...
gi 19075741  157 GLSQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK06484 423 MLSRSLACEWAPA-GIRVNTVAPGYIET 449
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
 8-189 2.80e-19

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 84.71  E-value: 2.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVI-----ACSRAPDTIT-IEHS--KLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:cd05359   1 ALVTGGSRGIGKAIALRLAERGADVVinyrkSKDAAAEVAAeIEELggKAVVVRADVSQPQDVEEMFAAVKERFGRLDVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:cd05359  81 VSNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERG-GGRIVAISSLGSIRALPNYLAVGTAKAALEALV 159

                       170       180       190
                ....*....|....*....|....*....|
gi 19075741 160 QTIMRELDPNwNIAITIVQPGGMQTEWASS 189
Cdd:cd05359 160 RYLAVELGPR-GIRVNAVSPGVIDTDALAH 188
PRK07062 PRK07062
SDR family oxidoreductase;
7-206 2.82e-19

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 85.09  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHS---------KLLKLKLDVTDVKSVeTAFKDA-KRRFGNV 76
Cdd:PRK07062  10 VAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEArlrekfpgaRLLAARCDVLDEADV-AAFAAAvEARFGGV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   77 DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK07062  89 DMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAAS-IVCVNSLLALQPEPHMVATSAARAGLL 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075741  157 GLSQTIMRELDP-----NwNIAITIVQPGgmqtewassnmQWAKPHPAYEN-DRSW 206
Cdd:PRK07062 168 NLVKSLATELAPkgvrvN-SILLGLVESG-----------QWRRRYEARADpGQSW 211
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-185 4.06e-19

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 84.24  E-value: 4.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNvIACS--------RAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRR 72
Cdd:PRK08217   1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAK-LALIdlnqekleEAVAECGALGTEVRGYAANVTDEEDVEATFAQIAED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   73 FGNVDIVINNAGY---GLV-----GEFES-YNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAgYYPSP 143
Cdd:PRK08217  80 FGQLNGLINNAGIlrdGLLvkakdGKVTSkMSLEQFQSVIDVNLTGVFLCGREAAAKMIESGSKGVIINISSIA-RAGNM 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 19075741  144 CLSMYNASKFAVEGLSQTIMRELdPNWNIAITIVQPGGMQTE 185
Cdd:PRK08217 159 GQTNYSASKAGVAAMTVTWAKEL-ARYGIRVAAIAPGVIETE 199
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 7-185 4.06e-19

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: 84.38  E-value: 4.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT----------IEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:cd05364   5 VAIITGSSSGIGAGTAILFARLGARLALTGRDAERLEetrqsclqagVSEKKILLVVADLTEEEGQDRIISTTLAKFGRL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  77 DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:cd05364  85 DILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT--KGEIVNVSSVAGGRSFPGVLYYCISKAALD 162

                       170       180
                ....*....|....*....|....*....
gi 19075741 157 GLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd05364 163 QFTRCTALELAPK-GVRVNSVSPGVIVTG 190
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 8-192 4.44e-19

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 84.08  E-value: 4.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL----LKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNA 83
Cdd:cd08944   6 AIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIaggaLALRVDVTDEQQVAALFERAVEEFGGLDLLVNNA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  84 G-YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:cd08944  86 GaMHLTPAIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARG-GGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTL 164

                       170       180       190
                ....*....|....*....|....*....|
gi 19075741 163 MRELDPNwNIAITIVQPGGMQTEWASSNMQ 192
Cdd:cd08944 165 AAELRHA-GIRCNALAPGLIDTPLLLAKLA 193
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
8-185 4.97e-19

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


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 84.00  E-value: 4.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYAlVKVGLAQ-GYNVI---ACSRAPDTITIEH-----SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK08063   7 ALVTGSSRGIGKA-IALRLAEeGYDIAvnyARSRKAAEETAEEiealgRKALAVKANVGDVEKIKEMFAQIDEEFGRLDV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGefESYNIEEMHRQ--MNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK08063  86 FVNNAASGVLR--PAMELEESHWDwtMNINAKALLFCAQEAAKLMEKVG-GGKIISLSSLGSIRYLENYTTVGVSKAALE 162

                        170       180
                 ....*....|....*....|....*....
gi 19075741  157 GLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK08063 163 ALTRYLAVELAPK-GIAVNAVSGGAVDTD 190
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 9-193 1.31e-18

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 82.97  E-value: 1.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   9 LITGSSKGLGYALVKvGLAQ-GYNVIACSRAPDTITIEHSKLLKLKLDVTDV-----------KSVETAFKdakrRFGNV 76
Cdd:cd08936  14 LVTASTDGIGLAIAR-RLAQdGAHVVVSSRKQQNVDRAVATLQGEGLSVTGTvchvgkaedreRLVATAVN----LHGGV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  77 DIVINNAGYGLV-GEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAV 155
Cdd:cd08936  89 DILVSNAAVNPFfGNILDSTEEVWDKILDVNVKATALMTKAVVPEMEKRG-GGSVVIVSSVAAFHPFPGLGPYNVSKTAL 167

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19075741 156 EGLSQTIMRELDPNwNIAITIVQPGGMQTEWasSNMQW 193
Cdd:cd08936 168 LGLTKNLAPELAPR-NIRVNCLAPGLIKTSF--SSALW 202
PRK07035 PRK07035
SDR family oxidoreductase;
9-188 1.44e-18

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 82.76  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK07035  12 LVTGASRGIGEAIAKLLAQQGAHVIvssrkldGCQAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLDILVN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAG----YG--LVGEFESYNieemhRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAV 155
Cdd:PRK07035  92 NAAanpyFGhiLDTDLGAFQ-----KTVDVNIRGYFFMSVEAGKLMKEQG-GGSIVNVASVNGVSPGDFQGIYSITKAAV 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19075741  156 EGLSQTIMRELDPnWNIAITIVQPGGMQTEWAS 188
Cdd:PRK07035 166 ISMTKAFAKECAP-FGIRVNALLPGLTDTKFAS 197
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 9-185 2.31e-18

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 82.12  E-value: 2.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   9 LITGSSKGLGYALVKVGLAQGYNVI------------ACSRAPDTITIEHSkllklklDVTDVKSVETAFKDAKRRFGNV 76
Cdd:cd05326   8 IITGGASGIGEATARLFAKHGARVViadidddagqavAAELGDPDISFVHC-------DVTVEADVRAAVDTAVARFGRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  77 DIVINNAgyGLVG----EFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNASK 152
Cdd:cd05326  81 DIMFNNA--GVLGapcySILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGS-IVSVASVAGVVGGLGPHAYTASK 157

                       170       180       190
                ....*....|....*....|....*....|...
gi 19075741 153 FAVEGLSQTIMRELDPnWNIAITIVQPGGMQTE 185
Cdd:cd05326 158 HAVLGLTRSAATELGE-HGIRVNCVSPYGVATP 189
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 9-200 2.44e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 82.12  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKvGLAQ-GYNVIACSR-------APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK07523  14 LVTGSSQGIGYALAE-GLAQaGAEVILNGRdpaklaaAAESLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDILV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK07523  93 NNAGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGA-GKIINIASVQSALARPGIAPYTATKGAVGNLTK 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19075741  161 timreldpnwniaitivqpgGMQTEWASSNMQWAKPHPAY 200
Cdd:PRK07523 172 --------------------GMATDWAKHGLQCNAIAPGY 191
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 7-180 2.45e-18

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 82.30  E-value: 2.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKvGLA-QGYNVIACSRAPDTItIEHSKLLK--------LKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK08213  14 TALVTGGSRGLGLQIAE-ALGeAGARVVLSARKAEEL-EEAAAHLEalgidalwIAADVADEADIERLAEETLERFGHVD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSM----YNASKF 153
Cdd:PRK08213  92 ILVNNAGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRSMIPRGYGRIINVASVAGLGGNPPEVMdtiaYNTSKG 171

                        170       180
                 ....*....|....*....|....*..
gi 19075741  154 AVEGLSQTIMRELDPnWNIAITIVQPG 180
Cdd:PRK08213 172 AVINFTRALAAEWGP-HGIRVNAIAPG 197
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 7-190 3.80e-18

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 81.48  E-value: 3.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI--------TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05369   5 VAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLeaaaeeisSATGGRAHPIQCDVRDPEAVEAAVDETLKEFGKIDI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd05369  85 LINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAGVDAL 164

                       170       180       190
                ....*....|....*....|....*....|..
gi 19075741 159 SQTIMRELDPnWNIAITIVQPGGMQTEWASSN 190
Cdd:cd05369 165 TRSLAVEWGP-YGIRVNAIAPGPIPTTEGMER 195
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 8-180 6.49e-18

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 80.73  E-value: 6.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPdtitiehSKLLKLKLDVTDVKSVET------------AFKDAKRRFGN 75
Cdd:cd05356   4 AVVTGATDGIGKAYAEELAKRGFNVILISRTQ-------EKLDAVAKEIEEKYGVETktiaadfsagddIYERIEKELEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  76 VDI--VINNAG--YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNAS 151
Cdd:cd05356  77 LDIgiLVNNVGisHSIPEYFLETPEDELQDIINVNVMATLKMTRLILPGMVKRKKGA-IVNISSFAGLIPTPLLATYSAS 155

                       170       180
                ....*....|....*....|....*....
gi 19075741 152 KFAVEGLSQTIMRELDPNwNIAITIVQPG 180
Cdd:cd05356 156 KAFLDFFSRALYEEYKSQ-GIDVQSLLPY 183
PRK06172 PRK06172
SDR family oxidoreductase;
1-214 7.96e-18

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 80.95  E-value: 7.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFS--TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI--TIEH-----SKLLKLKLDVTDVKSVETAFKDAKR 71
Cdd:PRK06172   1 MSMTFSgkVALVTGGAAGIGRATALAFAREGAKVVVADRDAAGGeeTVALireagGEALFVACDVTRDAEVKALVEQTIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   72 RFGNVDIVINNAGYGL-VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNA 150
Cdd:PRK06172  81 AYGRLDYAFNNAGIEIeQGRLAEGSEAEFDAIMGVNVKGVWLCMKYQIPLMLAQG-GGAIVNTASVAGLGAAPKMSIYAA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075741  151 SKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASsnmqwakphPAYENDRSWRPFWENYH 214
Cdd:PRK06172 160 SKHAVIGLTKSAAIEYAKK-GIRVNAVCPAVIDTDMFR---------RAYEADPRKAEFAAAMH 213
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
 7-184 8.05e-18

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 80.93  E-value: 8.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR--------APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK08936   9 VVVITGGSTGLGRAMAVRFGKEKAKVVINYRsdeeeandVAEEIKKAGGEAIAVKGDVTVESDVVNLIQTAVKEFGTLDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK08936  89 MINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDIKGNIINMSSVHEQIPWPLFVHYAASKGGVKLM 168

                        170       180
                 ....*....|....*....|....*.
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK08936 169 TETLAMEYAPK-GIRVNNIGPGAINT 193
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 7-192 8.58e-18

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


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 80.41  E-value: 8.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYN--VIACSRapdTITIEHSKLLKL---------KLDVTDVKSVETAFKDAKRRFGN 75
Cdd:cd05367   1 VIILTGASRGIGRALAEELLKRGSPsvVVLLAR---SEEPLQELKEELrpglrvttvKADLSDAAGVEQLLEAIRKLDGE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  76 VDIVINNAG-YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:cd05367  78 RDLLINNAGsLGPVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19075741 155 VEGLSQTIMRELDPN--WNIAitivqPGGMQTEwassnMQ 192
Cdd:cd05367 158 RDMFFRVLAAEEPDVrvLSYA-----PGVVDTD-----MQ 187
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-189 8.65e-18

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 80.90  E-value: 8.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIE-----HSKLLKLKLDVTDVKSVETAFKDAKRRFGN-VDIVI 80
Cdd:PRK08642   7 TVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEAladelGDRAIALQADVTDREQVQAMFATATEHFGKpITTVV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNA--GYGLVGE----FESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSvaGYYPSPCLSM--YNASK 152
Cdd:PRK08642  87 NNAlaDFSFDGDarkkADDITWEDFQQQLEGSVKGALNTIQAALPGMREQG-FGRIINIGT--NLFQNPVVPYhdYTTAK 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19075741  153 FAVEGLSQTIMRELDPnWNIAITIVQPGGMQTEWASS 189
Cdd:PRK08642 164 AALLGLTRNLAAELGP-YGITVNMVSGGLLRTTDASA 199
PRK06124 PRK06124
SDR family oxidoreductase;
7-185 1.40e-17

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 80.14  E-value: 1.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK06124  13 VALVTGSARGLGFEIARALAGAGAHVLVNGRnaatleaAVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLDIL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGY---GLVGEFESYNIEEMhrqMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK06124  93 VNNVGArdrRPLAELDDAAIRAL---LETDLVAPILLSRLAAQRMKR-QGYGRIIAITSIAGQVARAGDAVYPAAKQGLT 168

                        170       180
                 ....*....|....*....|....*....
gi 19075741  157 GLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK06124 169 GLMRALAAEFGPH-GITSNAIAPGYFATE 196
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 7-185 1.43e-17

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 80.35  E-value: 1.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIE--HSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd05327   3 VVVITGANSGIGKETARELAKRGAHVIIACRneekgeeAAAEIKKEtgNAKVEVIQLDLSSLASVRQFAEEFLARFPRLD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGLVGEFES-YNIEemhRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVA-----------------GY 139
Cdd:cd05327  83 ILINNAGIMAPPRRLTkDGFE---LQFAVNYLGHFLLTNLLLPVLKASA-PSRIVNVSSIAhragpidfndldlennkEY 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 19075741 140 YPSPclsMYNASK-----FAVEgLSqtimRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd05327 159 SPYK---AYGQSKlanilFTRE-LA----RRLEGT-GVTVNALHPGVVRTE 200
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 7-192 1.57e-17

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 79.80  E-value: 1.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT----IEHSKLLKLKLDVTDVKSVE--TAFKD--AKRRFGNVDI 78
Cdd:cd05329   8 TALVTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDecltEWREKGFKVEGSVCDVSSRSerQELMDtvASHFGGKLNI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd05329  88 LVNNAGTNIRKEAKDYTEEDYSLIMSTNFEAAYHLSRLAHPLLKASGNGN-IVFISSVAGVIAVPSGAPYGATKGALNQL 166

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19075741 159 SqtimRELDPNW---NIAITIVQPGGMQTEWASSNMQ 192
Cdd:cd05329 167 T----RSLACEWakdNIRVNAVAPWVIATPLVEPVIQ 199
PRK07774 PRK07774
SDR family oxidoreductase;
7-185 2.69e-17

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 79.40  E-value: 2.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07774   8 VAIVTGAAGGIGQAYAEALAREGASVVvadinaeGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGIDYL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGY--GLVGEF-ESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSpclSMYNASKFAVE 156
Cdd:PRK07774  88 VNNAAIygGMKLDLlITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRG-GGAIVNQSSTAAWLYS---NFYGLAKVGLN 163

                        170       180
                 ....*....|....*....|....*....
gi 19075741  157 GLSQTIMRELDpNWNIAITIVQPGGMQTE 185
Cdd:PRK07774 164 GLTQQLARELG-GMNIRVNAIAPGPIDTE 191
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 7-181 3.61e-17

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: 78.92  E-value: 3.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR--------APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd08930   4 IILITGAAGLIGKAFCKALLSAGARLILADInapaleqlKEELTNLYKNRVIALELDITSKESIKELIESYLEKFGRIDI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGE---FESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAG--------YY-PSPCLS 146
Cdd:cd08930  84 LINNAYPSPKVWgsrFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGK-GSIINIASIYGviapdfriYEnTQMYSP 162

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19075741 147 M-YNASKFAVEGLSQTIMRELdPNWNIAITIVQPGG 181
Cdd:cd08930 163 VeYSVIKAGIIHLTKYLAKYY-ADTGIRVNAISPGG 197
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 8-196 4.35e-17

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 78.72  E-value: 4.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGY---------NVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05330   6 VLITGGGSGLGLATAVRLAKEGAklslvdlneEGLEAAKAALLEIAPDAEVLLIKADVSDEAQVEAYVDATVEQFGRIDG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGY-GLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:cd05330  86 FFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGS-GMIVNTASVGGIRGVGNQSGYAAAKHGVVG 164

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19075741 158 LSQTIMRELDpNWNIAITIVQPGGMQTEWASSNMQWAKP 196
Cdd:cd05330 165 LTRNSAVEYG-QYGIRINAIAPGAILTPMVEGSLKQLGP 202
PRK07201 PRK07201
SDR family oxidoreductase;
7-166 6.65e-17

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 80.77  E-value: 6.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLKL-------DVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07201 373 VVLITGASSGIGRATAIKVAEAGATVFLVARNGEALDELVAEIRAKGGtahaytcDLTDSAAVDHTVKDILAEHGHVDYL 452

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGL-------VGEFESYnieemHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASK 152
Cdd:PRK07201 453 VNNAGRSIrrsvensTDRFHDY-----ERTMAVNYFGAVRLILGLLPHMRERRF-GHVVNVSSIGVQTNAPRFSAYVASK 526

                        170
                 ....*....|....
gi 19075741  153 FAVEGLSQTIMREL 166
Cdd:PRK07201 527 AALDAFSDVAASET 540
PRK06123 PRK06123
SDR family oxidoreductase;
8-189 7.58e-17

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 77.90  E-value: 7.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVI--------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK06123   5 MIITGASRGIGAATALLAAERGYAVClnylrnrdAAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLDAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGyglVGE----FESYNIEEMHRQMNVNFWGVAYITKEALNLM--RESGKGGRILQISSVAGYYPSPCLSM-YNASK 152
Cdd:PRK06123  85 VNNAG---ILEaqmrLEQMDAARLTRIFATNVVGSFLCAREAVKRMstRHGGRGGAIVNVSSMAARLGSPGEYIdYAASK 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19075741  153 FAVEGLSQTIMRELdPNWNIAITIVQPGGMQTEWASS 189
Cdd:PRK06123 162 GAIDTMTIGLAKEV-AAEGIRVNAVRPGVIYTEIHAS 197
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 7-202 8.20e-17

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


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 78.04  E-value: 8.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNV----IACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:cd05363   5 TALITGSARGIGRAFAQAYVREGARVaiadINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDILVNN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:cd05363  85 AALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGRGGKIINMASQAGRRGEALVGVYCATKAAVISLTQSA 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19075741 163 MRELDPnWNIAITIVQPGGMQTE-WASSNMQWAKphpaYEN 202
Cdd:cd05363 165 GLNLIR-HGINVNAIAPGVVDGEhWDGVDAKFAR----YEN 200
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 7-180 9.17e-17

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 77.32  E-value: 9.17e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVI--------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd05357   2 VALVTGAAKRIGRAIAEALAAEGYRVVvhynrseaEAQRLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCDV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd05357  82 LVNNASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRN-GSIINIIDAMTDRPLTGYFAYCMSKAALEGL 160

                       170       180
                ....*....|....*....|..
gi 19075741 159 SQTIMRELDPnwNIAITIVQPG 180
Cdd:cd05357 161 TRSAALELAP--NIRVNGIAPG 180
PRK12742 PRK12742
SDR family oxidoreductase;
7-185 9.44e-17

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 77.49  E-value: 9.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVI---ACSR-APDTITIE-HSKLLKLklDVTDVKSVetafKDAKRRFGNVDIVIN 81
Cdd:PRK12742   8 KVLVLGGSRGIGAAIVRRFVTDGANVRftyAGSKdAAERLAQEtGATAVQT--DSADRDAV----IDVVRKSGALDILVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQISSVAG-YYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK12742  82 NAGIAVFGDALELDADDIDRLFKINIHAPYHASVEAARQMPE---GGRIIIIGSVNGdRMPVAGMAAYAASKSALQGMAR 158

                        170       180
                 ....*....|....*....|....*
gi 19075741  161 TIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK12742 159 GLARDFGPR-GITINVVQPGPIDTD 182
PRK08589 PRK08589
SDR family oxidoreductase;
7-184 1.05e-16

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 77.90  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIA------CSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK08589   8 VAVITGASTGIGQASAIALAQEGAYVLAvdiaeaVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDVLF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGY-GLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK08589  88 NNAGVdNAAGRIHEYPVDVFDKIMAVDMRGTFLMTKMLLPLMME--QGGSIINTSSFSGQAADLYRSGYNAAKGAVINFT 165

                        170       180
                 ....*....|....*....|....*
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK08589 166 KSIAIEYGRD-GIRANAIAPGTIET 189
PRK05867 PRK05867
SDR family oxidoreductase;
9-208 1.69e-16

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 77.38  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK05867  13 LITGASTGIGKRVALAYVEAGAQVAiaarhldALEKLADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGY---YPSPcLSMYNASKFAVEGL 158
Cdd:PRK05867  93 NAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGQGGVIINTASMSGHiinVPQQ-VSHYCASKAAVIHL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMQTEWAssnmqwakpHPAYENDRSWRP 208
Cdd:PRK05867 172 TKAMAVELAPH-KIRVNSVSPGYILTELV---------EPYTEYQPLWEP 211
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 8-185 1.97e-16

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 76.84  E-value: 1.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:cd05365   2 AIVTGGAAGIGKAIAGTLAKAGASVViadlkseGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  81 NNAGYGLVGEFESYNIEE-MHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:cd05365  82 NNAGGGGPKPFDMPMTEEdFEWAFKLNLFSAFRLSQLCAPHMQKAG-GGAILNISSMSSENKNVRIAAYGSSKAAVNHMT 160

                       170       180
                ....*....|....*....|....*.
gi 19075741 160 QTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd05365 161 RNLAFDLGPK-GIRVNAVAPGAVKTD 185
PRK09291 PRK09291
SDR family oxidoreductase;
7-184 2.24e-16

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 76.96  E-value: 2.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYAlVKVGLA-QGYNVIACSR-APDTITI-EHSKLLKL-----KLDVTDVKSVETAFKdakrrfGNVDI 78
Cdd:PRK09291   4 TILITGAGSGFGRE-VALRLArKGHNVIAGVQiAPQVTALrAEAARRGLalrveKLDLTDAIDRAQAAE------WDVDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGgRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK09291  77 LLNNAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKG-KVVFTSSMAGLITGPFTGAYCASKHALEAI 155

                        170       180
                 ....*....|....*....|....*.
gi 19075741  159 SQTIMRELDPnWNIAITIVQPGGMQT 184
Cdd:PRK09291 156 AEAMHAELKP-FGIQVATVNPGPYLT 180
PRK08251 PRK08251
SDR family oxidoreductase;
7-185 3.34e-16

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 76.13  E-value: 3.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKL---------KLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK08251   4 KILITGASSGLGAGMAREFAAKGRDLALCARRTDRLEELKAELLARypgikvavaALDVNDHDQVFEVFAEFRDELGGLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNAGYGlvgefESYNIEEMHRQMN-----VNFWGVAYITKEALNLMRESGKGGRILqISSVAGYYPSP-CLSMYNAS 151
Cdd:PRK08251  84 RVIVNAGIG-----KGARLGTGKFWANkataeTNFVAALAQCEAAMEIFREQGSGHLVL-ISSVSAVRGLPgVKAAYAAS 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19075741  152 KFAVEGLSQTIMRELDpNWNIAITIVQPGGMQTE 185
Cdd:PRK08251 158 KAGVASLGEGLRAELA-KTPIKVSTIEPGYIRSE 190
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 8-184 4.71e-16

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


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 75.85  E-value: 4.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT---IEH-SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNA 83
Cdd:cd05348   7 ALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAelrADFgDAVVGVEGDVRSLADNERAVARCVERFGKLDCFIGNA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  84 GY-----GLVG---EFESYNIEEMhrqMNVNFWGVAYITKEALNLMRESgKGGRILQISsVAGYYPSPCLSMYNASKFAV 155
Cdd:cd05348  87 GIwdystSLVDipeEKLDEAFDEL---FHINVKGYILGAKAALPALYAT-EGSVIFTVS-NAGFYPGGGGPLYTASKHAV 161

                       170       180
                ....*....|....*....|....*....
gi 19075741 156 EGLSQTIMRELDPnwNIAITIVQPGGMQT 184
Cdd:cd05348 162 VGLVKQLAYELAP--HIRVNGVAPGGMVT 188
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-184 5.66e-16

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 75.38  E-value: 5.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITieHSKLLKLKLDVTDvkSVETAFKDakrrFGNVDIVINNAG-- 84
Cdd:PRK06550   7 TVLITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDL--SGNFHFLQLDLSD--DLEPLFDW----VPSVDILCNTAGil 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 --YGLVgefESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSqti 162
Cdd:PRK06550  79 ddYKPL---LDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKS-GIIINMCSIASFVAGGGGAAYTASKHALAGFT--- 151

                        170       180
                 ....*....|....*....|....*
gi 19075741  163 mRELDPNW---NIAITIVQPGGMQT 184
Cdd:PRK06550 152 -KQLALDYakdGIQVFGIAPGAVKT 175
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 7-198 5.98e-16

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


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 75.58  E-value: 5.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIAcsrapdtITIEHSKLLKL---------KLDVTDVKSVETAFKdakrRFGNVD 77
Cdd:cd05368   4 VALITAAAQGIGRAIALAFAREGANVIA-------TDINEEKLKELergpgittrVLDVTDKEQVAALAK----EEGRID 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYY---PSPCLsmYNASKFA 154
Cdd:cd05368  73 VLFNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLAR-KDGSIINMSSVASSIkgvPNRFV--YSTTKAA 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19075741 155 VEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASSNMQwAKPHP 198
Cdd:cd05368 150 VIGLTKSVAADFAQQ-GIRCNAICPGTVDTPSLEERIQ-AQPDP 191
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 9-185 6.43e-16

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 75.43  E-value: 6.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVI----ACSRAPDTITIEHSK----LLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK12935  10 IVTGGAKGIGKAITVALAQEGAKVVinynSSKEAAENLVNELGKeghdVYAVQADVSKVEDANRLVEEAVNHFGKVDILV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK12935  90 NNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEA-EEGRIISISSIIGQAGGFGQTNYSAAKAGMLGFTK 168

                        170       180
                 ....*....|....*....|....*
gi 19075741  161 TIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK12935 169 SLALELAKT-NVTVNAICPGFIDTE 192
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
8-192 7.94e-16

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 75.10  E-value: 7.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIE-----HSKLLKLKLDVTDVKSVETAFKDAKRRF--GNVDIV- 79
Cdd:PRK06924   4 VIITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKlaeqyNSNLTFHSLDLQDVHELETNFNEILSSIqeDNVSSIh 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 -INNAGY----GLVGEFESyniEEMHRQMNVNFWGVAYITKEALNlMRESGKGG-RILQISSVAGYYPSPCLSMYNASKF 153
Cdd:PRK06924  84 lINNAGMvapiKPIEKAES---EELITNVHLNLLAPMILTSTFMK-HTKDWKVDkRVINISSGAAKNPYFGWSAYCSSKA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19075741  154 AVEGLSQTI-MRELDPNWNIAITIVQPGGMQTewassNMQ 192
Cdd:PRK06924 160 GLDMFTQTVaTEQEEEEYPVKIVAFSPGVMDT-----NMQ 194
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 7-190 8.25e-16

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 75.11  E-value: 8.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDtitiehsKLLKLK---------------LDVTDVKSVETAFKDAKR 71
Cdd:cd05373   1 VAAVVGAGDGLGAAIARRFAAEGFSVALAARREA-------KLEALLvdiirdaggsakavpTDARDEDEVIALFDLIEE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  72 RFGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNAS 151
Cdd:cd05373  74 EIGPLEVLVYNAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGR-GTIIFTGATASLRGRAGFAAFAGA 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19075741 152 KFAVEGLSQTIMRELDP-NWNIAITIVQpGGMQTEWASSN 190
Cdd:cd05373 153 KFALRALAQSMARELGPkGIHVAHVIID-GGIDTDFIRER 191
PRK06947 PRK06947
SDR family oxidoreductase;
7-192 1.22e-15

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 74.84  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNV--------IACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK06947   4 VVLITGASRGIGRATAVLAAARGWSVginyardaAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAgyGLVGE---FESYNIEEMHRQMNVNFWGVAYITKEALNLMRES--GKGGRILQISSVAGYYPSPCLSM-YNASK 152
Cdd:PRK06947  84 LVNNA--GIVAPsmpLADMDAARLRRMFDTNVLGAYLCAREAARRLSTDrgGRGGAIVNVSSIASRLGSPNEYVdYAGSK 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19075741  153 FAVEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASSNMQ 192
Cdd:PRK06947 162 GAVDTLTLGLAKELGPH-GVRVNAVRPGLIETEIHASGGQ 200
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-185 1.39e-15

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


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 74.77  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK06935  17 VAIVTGGNTGLGQGYAVALAKAGADIIITTHGTNWdetrrlIEKEGRKVTFVQVDLTKPESAEKVVKEALEEFGKIDILV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK06935  97 NNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGS-GKIINIASMLSFQGGKFVPAYTASKHGVAGLTK 175

                        170       180
                 ....*....|....*....|....*
gi 19075741  161 TIMRELdPNWNIAITIVQPGGMQTE 185
Cdd:PRK06935 176 AFANEL-AAYNIQVNAIAPGYIKTA 199
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 9-180 1.54e-15

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 74.42  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   9 LITGSSKGLGYALVKvGLAQ-GYNVIAC-------SRAPDTITIEH-SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:cd05322   6 VVIGGGQTLGEFLCH-GLAEaGYDVAVAdinsenaEKVADEINAEYgEKAYGFGADATNEQSVIALSKGVDEIFKRVDLL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:cd05322  85 VYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGIQGRIIQINSKSGKVGSKHNSGYSAAKFGGVGLT 164

                       170       180
                ....*....|....*....|.
gi 19075741 160 QTIMRELdPNWNIAITIVQPG 180
Cdd:cd05322 165 QSLALDL-AEHGITVNSLMLG 184
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 8-184 1.65e-15

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 74.61  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAP---DTITIEH-SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNA 83
Cdd:PRK06200   9 ALITGGGSGIGRALVERFLAEGARVAVLERSAeklASLRQRFgDHVLVVEGDVTSYADNQRAVDQTVDAFGKLDCFVGNA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   84 GyglVGEFeSYNIEEM---------HRQMNVNFWGVAYITKEALNLMRESGkgGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:PRK06200  89 G---IWDY-NTSLVDIpaetldtafDEIFNVNVKGYLLGAKAALPALKASG--GSMIFTLSNSSFYPGGGGPLYTASKHA 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 19075741  155 VEGLSQTIMRELDPnwNIAITIVQPGGMQT 184
Cdd:PRK06200 163 VVGLVRQLAYELAP--KIRVNGVAPGGTVT 190
PRK07775 PRK07775
SDR family oxidoreductase;
7-206 3.03e-15

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 74.02  E-value: 3.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYAlVKVGLA-QGYNVI-------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK07775  12 PALVAGASSGIGAA-TAIELAaAGFPVAlgarrveKCEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILqISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK07775  91 LVSGAGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIF-VGSDVALRQRPHMGAYGAAKAGLEAM 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMQTewassNMQWAKP----HPAYENDRSW 206
Cdd:PRK07775 170 VTNLQMELEGT-GVRASIVHPGPTLT-----GMGWSLPaeviGPMLEDWAKW 215
PRK09072 PRK09072
SDR family oxidoreductase;
1-166 3.41e-15

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 73.82  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITI---EHSKLLKLKLDVTDVKSVE--TAFKDAKRRFGN 75
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEAlaaRLPYPGRHRWVVADLTSEAgrEAVLARAREMGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   76 VDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGgRILQISSVAGYYPSPCLSMYNASKFAV 155
Cdd:PRK09072  81 INVLINNAGVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSA-MVVNVGSTFGSIGYPGYASYCASKFAL 159

                        170
                 ....*....|.
gi 19075741  156 EGLSQTIMREL 166
Cdd:PRK09072 160 RGFSEALRREL 170
PRK06949 PRK06949
SDR family oxidoreductase;
9-185 4.85e-15

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 73.26  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVIACSRapdtiTIEHSKLLK------------LKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:PRK06949  13 LVTGASSGLGARFAQVLAQAGAKVVLASR-----RVERLKELRaeieaeggaahvVSLDVTDYQSIKAAVAHAETEAGTI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   77 DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALN--LMRESG-----KGGRILQISSVAGYYPSPCLSMYN 149
Cdd:PRK06949  88 DILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQEVAKrmIARAKGagntkPGGRIINIASVAGLRVLPQIGLYC 167

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19075741  150 ASKFAVEGLSQTIMREldpnW---NIAITIVQPGGMQTE 185
Cdd:PRK06949 168 MSKAAVVHMTRAMALE----WgrhGINVNAICPGYIDTE 202
PRK12743 PRK12743
SDR family oxidoreductase;
7-184 9.97e-15

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 72.37  E-value: 9.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYAlVKVGLA-QGYNV--------IACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK12743   4 VAIVTASDSGIGKA-CALLLAqQGFDIgitwhsdeEGAKETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:PRK12743  83 VLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGQGGRIINITSVHEHTPLPGASAYTAAKHALGG 162

                        170       180
                 ....*....|....*....|....*..
gi 19075741  158 LSQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK12743 163 LTKAMALELVEH-GILVNAVAPGAIAT 188
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 7-192 1.24e-14

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 72.32  E-value: 1.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYAlVKVGLA-QGYNV-IAC-----SRAPDT---ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:cd05355  28 KALITGGDSGIGRA-VAIAFArEGADVaINYlpeeeDDAEETkklIEEEGRKCLLIPGDLGDESFCRDLVKEVVKEFGKL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  77 DIVINNAGYglvgEFESYNIEEM-----HRQMNVNFWGVAYITKEALNLMResgKGGRILQISSVAGYYPSPCLSMYNAS 151
Cdd:cd05355 107 DILVNNAAY----QHPQESIEDItteqlEKTFRTNIFSMFYLTKAALPHLK---KGSSIINTTSVTAYKGSPHLLDYAAT 179

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19075741 152 KFAVEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASSNMQ 192
Cdd:cd05355 180 KGAIVAFTRGLSLQLAEK-GIRVNAVAPGPIWTPLIPSSFP 219
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 7-180 1.42e-14

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 72.37  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYAlVKVGLA-QGYNVIAC-----SRAPDT---ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK06701  48 VALITGGDSGIGRA-VAVLFAkEGADIAIVyldehEDANETkqrVEKEGVKCLLIPGDVSDEAFCKDAVEETVRELGRLD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNAGYGL-VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMresGKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK06701 127 ILVNNAAFQYpQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHL---KQGSAIINTGSITGYEGNETLIDYSATKGAIH 203

                        170       180
                 ....*....|....*....|....
gi 19075741  157 GLSQTIMRELDPNwNIAITIVQPG 180
Cdd:PRK06701 204 AFTRSLAQSLVQK-GIRVNAVAPG 226
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 7-239 1.98e-14

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 70.82  E-value: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPdtiTIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAG-- 84
Cdd:cd05334   3 VVLVYGGRGALGSAVVQAFKSRGWWVASIDLAE---NEEADASIIVLDSDSFTEQAKQVVASVARLSGKVDALICVAGgw 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  85 -YGLVGEFESY-NIEEMHRQmnvNFWGVAYITKEALNLMREsgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:cd05334  80 aGGSAKSKSFVkNWDLMWKQ---NLWTSFIASHLATKHLLS---GGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSL 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075741 163 MREL-DPNWNIAITIVQPGGMQTewaSSNMQWAkPHpayENDRSWrpfwenyhgceeTDPNKAAELLYSIAKLDRPPQ 239
Cdd:cd05334 154 AAENsGLPAGSTANAILPVTLDT---PANRKAM-PD---ADFSSW------------TPLEFIAELILFWASGAARPK 212
PRK06138 PRK06138
SDR family oxidoreductase;
7-184 2.33e-14

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 70.95  E-value: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD------TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK06138   7 VAIVTGAGSGIGRATAKLFAREGARVVVADRDAEaaervaAAIAAGGRAFARQGDVGSAEAVEALVDFVAARWGRLDVLV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK06138  87 NNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQG-GGSIVNTASQLALAGGRGRAAYVASKGAIASLTR 165

                        170       180
                 ....*....|....*....|....
gi 19075741  161 TIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK06138 166 AMALDHATD-GIRVNAVAPGTIDT 188
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
 9-185 3.07e-14

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 71.03  E-value: 3.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVIACSRAPDT-------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK06113  15 IITGAGAGIGKEIAITFATAGASVVVSDINADAanhvvdeIQQLGGQAFACRCDITSEQELSALADFALSKLGKVDILVN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAGYGLVGEFEsYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:PRK06113  95 NAGGGGPKPFD-MPMADFRRAYELNVFSFFHLSQLVAPEMEKNG-GGVILTITSMAAENKNINMTSYASSKAAASHLVRN 172

                        170       180
                 ....*....|....*....|....
gi 19075741  162 IMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK06113 173 MAFDLGEK-NIRVNGIAPGAILTD 195
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 1-185 3.17e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 70.94  E-value: 3.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFS----TVLITGSSKGLGYALVKvGLAQ-GYNVIA-------CSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKD 68
Cdd:PRK08085   1 MNDLFSlagkNILITGSAQGIGFLLAT-GLAEyGAEIIInditaerAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   69 AKRRFGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLM--RESGKggrILQISSVAGYYPSPCLS 146
Cdd:PRK08085  80 IEKDIGPIDVLINNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMvkRQAGK---IINICSMQSELGRDTIT 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19075741  147 MYNASKFAVEGLSQTIMRELdPNWNIAITIVQPGGMQTE 185
Cdd:PRK08085 157 PYAASKGAVKMLTRGMCVEL-ARHNIQVNGIAPGYFKTE 194
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-198 3.84e-14

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 70.18  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT---ITIEHSKLLKLKLDVTDVKSVETAfKDAKRRFGNV- 76
Cdd:PRK05786   1 MRLKGKKVAIIGVSEGLGYAVAYFALKEGAQVCINSRNENKlkrMKKTLSKYGNIHYVVGDVSSTESA-RNVIEKAAKVl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   77 ----DIVINNAGY--GLVGEFESynIEEMhrqMNVNFWGVAYITKEALNLMREsgkGGRILQISSVAGYY-PSPCLSMYN 149
Cdd:PRK05786  80 naidGLVVTVGGYveDTVEEFSG--LEEM---LTNHIKIPLYAVNASLRFLKE---GSSIVLVSSMSGIYkASPDQLSYA 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19075741  150 ASKFAVEGLSQTIMRELdPNWNIAITIVQPGGMQTEWASSNmQWAKPHP 198
Cdd:PRK05786 152 VAKAGLAKAVEILASEL-LGRGIRVNGIAPTTISGDFEPER-NWKKLRK 198
PRK05876 PRK05876
short chain dehydrogenase; Provisional
 9-190 5.85e-14

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 70.37  E-value: 5.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK05876  10 VITGGASGIGLATGTEFARRGARVVlgdvdkpGLRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:PRK05876  90 NAGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAET 169

                        170       180
                 ....*....|....*....|....*....
gi 19075741  162 IMRELDPNwNIAITIVQPGGMQTEWASSN 190
Cdd:PRK05876 170 LAREVTAD-GIGVSVLCPMVVETNLVANS 197
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 8-185 5.99e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 70.03  E-value: 5.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQG-YNVIACSRAPDT-------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK06198   9 ALVTGGTQGLGAAIARAFAERGaAGLVICGRNAEKgeaqaaeLEALGAKAVFVQADLSDVEDCRRVVAAADEAFGRLDAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK06198  89 VNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAEGTIVNIGSMSAHGGQPFLAAYCASKGALATLT 168

                        170       180
                 ....*....|....*....|....*.
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK06198 169 RNAAYALLRN-RIRVNGLNIGWMATE 193
PRK06139 PRK06139
SDR family oxidoreductase;
8-184 6.31e-14

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 70.90  E-value: 6.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK06139  10 VVITGASSGIGQATAEAFARRGARLVLAARdeealqaVAEECRALGAEVLVVPTDVTDADQVKALATQAASFGGRIDVWV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSvAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK06139  90 NNVGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISL-GGFAAQPYAAAYSASKFGLRGFSE 168

                        170       180
                 ....*....|....*....|....
gi 19075741  161 TIMRELDPNWNIAITIVQPGGMQT 184
Cdd:PRK06139 169 ALRGELADHPDIHVCDVYPAFMDT 192
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 8-185 6.48e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 69.93  E-value: 6.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLklDVTDVKSVETAFKDAKRRFGNVDIVINNAG--Y 85
Cdd:PRK06523  12 ALVTGGTKGIGAATVARLLEAGARVVTTARSRPDDLPEGVEFVAA--DLTTAEGCAAVARAVLERLGGVDILVHVLGgsS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   86 GLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSM-YNASKFAVEGLSQTIMR 164
Cdd:PRK06523  90 APAGGFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGV-IIHVTSIQRRLPLPESTTaYAAAKAALSTYSKSLSK 168

                        170       180
                 ....*....|....*....|.
gi 19075741  165 ELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK06523 169 EVAPK-GVRVNTVSPGWIETE 188
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 8-185 8.32e-14

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


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 69.48  E-value: 8.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRApdtiTIEHSKLLKLKLDVTDVKSVET---AFKDAKR-------RFGNVD 77
Cdd:cd08937   7 VVVTGAAQGIGRGVAERLAGEGARVLLVDRS----ELVHEVLAEILAAGDAAHVHTAdleTYAGAQGvvraaveRFGRVD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGLVGE-FESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVA--GYYPSPclsmYNASKFA 154
Cdd:cd08937  83 VLINNVGGTIWAKpYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQ-GVIVNVSSIAtrGIYRIP----YSAAKGG 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 19075741 155 VEGLSQTIMRELdPNWNIAITIVQPGGMQTE 185
Cdd:cd08937 158 VNALTASLAFEH-ARDGIRVNAVAPGGTEAP 187
PRK05866 PRK05866
SDR family oxidoreductase;
7-166 9.13e-14

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 70.16  E-value: 9.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT-------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK05866  42 RILLTGASSGIGEAAAEQFARRGATVVAVARREDLldavadrITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDIL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESyNIEEMH---RQMNVNFWGVAYITKEALNLMRESGKgGRILQISSvAGYYP--SPCLSMYNASKFA 154
Cdd:PRK05866 122 INNAGRSIRRPLAE-SLDRWHdveRTMVLNYYAPLRLIRGLAPGMLERGD-GHIINVAT-WGVLSeaSPLFSVYNASKAA 198

                        170
                 ....*....|..
gi 19075741  155 VEGLSQTIMREL 166
Cdd:PRK05866 199 LSAVSRVIETEW 210
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 7-180 9.43e-14

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


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 69.27  E-value: 9.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACS-RAPDTITIEHSKLLKLKLD---------VTDVKSVETA---FKDAKRRF 73
Cdd:cd05353   7 VVLVTGAGGGLGRAYALAFAERGAKVVVNDlGGDRKGSGKSSSAADKVVDeikaaggkaVANYDSVEDGekiVKTAIDAF 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  74 GNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKF 153
Cdd:cd05353  87 GRVDILVNNAGILRDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQ-KFGRIINTSSAAGLYGNFGQANYSAAKL 165

                       170       180
                ....*....|....*....|....*..
gi 19075741 154 AVEGLSQTIMRELDPNwNIAITIVQPG 180
Cdd:cd05353 166 GLLGLSNTLAIEGAKY-NITCNTIAPA 191
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 1.56e-13

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 68.95  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFSTVLITGSSK--GLGYALVKVGLAQGYNVIACSRAP------------------DTITIEHSKLLKLKLDVTDVK 60
Cdd:PRK12748   1 LPLMKKIALVTGASRlnGIGAAVCRRLAAKGIDIFFTYWSPydktmpwgmhdkepvllkEEIESYGVRCEHMEIDLSQPY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   61 SVETAFKDAKRRFGNVDIVINNAGYGLVGEFESYNIEEM--HRQMNVNfwgvAYITKEALNLMRESGK-GGRILQISSVA 137
Cdd:PRK12748  81 APNRVFYAVSERLGDPSILINNAAYSTHTRLEELTAEQLdkHYAVNVR----ATMLLSSAFAKQYDGKaGGRIINLTSGQ 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19075741  138 GYYPSPCLSMYNASKFAVEGLSQTIMRELDPNwniAITI--VQPGGMQTEWAS 188
Cdd:PRK12748 157 SLGPMPDELAYAATKGAIEAFTKSLAPELAEK---GITVnaVNPGPTDTGWIT 206
PRK07063 PRK07063
SDR family oxidoreductase;
8-204 1.66e-13

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 68.92  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT---------IEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK07063  10 ALVTGAAQGIGAAIARAFAREGAAVALADLDAALAEraaaaiardVAGARVLAVPADVTDAASVAAAVAAAEEAFGPLDV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK07063  90 LVNNAGINVFADPLAMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERG-RGSIVNIASTHAFKIIPGCFPYPVAKHGLLGL 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMQTEWASSnmQW-AKPHPAYENDR 204
Cdd:PRK07063 169 TRALGIEYAAR-NVRVNAIAPGYIETQLTED--WWnAQPDPAAARAE 212
PRK09730 PRK09730
SDR family oxidoreductase;
6-185 1.88e-13

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 68.34  E-value: 1.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    6 STVLITGSSKGLGYALVKVGLAQGY--------NVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK09730   2 AIALVTGGSRGIGRATALLLAQEGYtvavnyqqNLHAAQEVVNLITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNAGYGLV-GEFESYNIEEMHRQMNVNFWGVAYITKEALNLM--RESGKGGRILQISSVAGYYPSPCLSM-YNASKF 153
Cdd:PRK09730  82 ALVNNAGILFTqCTVENLTAERINRVLSTNVTGYFLCCREAVKRMalKHGGSGGAIVNVSSAASRLGAPGEYVdYAASKG 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19075741  154 AVEGLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK09730 162 AIDTLTTGLSLEVAAQ-GIRVNCVRPGFIYTE 192
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 7-185 1.93e-13

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 68.42  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAP-------DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07478   8 VAIITGASSGIGRAAAKLFAREGAKVVVGARRQaeldqlvAEIRAEGGEAVALAGDVRDEAYAKALVALAVERFGGLDIA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAG-YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPS-PCLSMYNASKFAVEG 157
Cdd:PRK07478  88 FNNAGtLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARG-GGSLIFTSTFVGHTAGfPGMAAYAASKAGLIG 166

                        170       180
                 ....*....|....*....|....*...
gi 19075741  158 LSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK07478 167 LTQVLAAEYGAQ-GIRVNALLPGGTDTP 193
PRK07041 PRK07041
SDR family oxidoreductase;
9-188 1.94e-13

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 68.14  E-value: 1.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI------TIEHSKLLKLKLDVTDVKSVETAFkdakRRFGNVDIVINN 82
Cdd:PRK07041   1 LVVGGSSGIGLALARAFAAEGARVTIASRSRDRLaaaaraLGGGAPVRTAALDITDEAAVDAFF----AEAGPFDHVVIT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AGYGLVGEFESYNIEEMHRQMNVNFWGvAYITKEALNLmresGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:PRK07041  77 AADTPGGPVRALPLAAAQAAMDSKFWG-AYRVARAARI----APGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGL 151

                        170       180
                 ....*....|....*....|....*..
gi 19075741  163 MRELDPnwnIAITIVQPGGMQTE-WAS 188
Cdd:PRK07041 152 ALELAP---VRVNTVSPGLVDTPlWSK 175
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 8-239 2.88e-13

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: 66.77  E-value: 2.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVkVGLAqgynviacSRAPDtitiehskllklKLDVTDvksvetafkdakRRfgnvDIVINNAGYGL 87
Cdd:cd02266   1 VLVTGGSGGIGGAIA-RWLA--------SRGSP------------KVLVVS------------RR----DVVVHNAAILD 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  88 VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGgRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMRELD 167
Cdd:cd02266  44 DGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLG-RFILISSVAGLFGAPGLGGYAASKAALDGLAQQWASEGW 122

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075741 168 PNwNIAITIVQPGgmqtEWASSNMQWAKPHPAYEndrswrpFWENYHGCEETDPNKAAELLYSIAKLDRPPQ 239
Cdd:cd02266 123 GN-GLPATAVACG----TWAGSGMAKGPVAPEEI-------LGNRRHGVRTMPPEEVARALLNALDRPKAGV 182
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
9-185 2.97e-13

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


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 68.01  E-value: 2.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVkVGLAQ-GYNVIACSRAPDTITIEHSKLLKLKL-----DVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK12481  12 IITGCNTGLGQGMA-IGLAKaGADIVGVGVAEAPETQAQVEALGRKFhfitaDLIQQKDIDSIVSQAVEVMGHIDILINN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:PRK12481  91 AGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGNGGKIINIASMLSFQGGIRVPSYTASKSAVMGLTRAL 170

                        170       180
                 ....*....|....*....|...
gi 19075741  163 MRELdPNWNIAITIVQPGGMQTE 185
Cdd:PRK12481 171 ATEL-SQYNINVNAIAPGYMATD 192
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 7-185 3.20e-13

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 68.06  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD---TITIEH-----SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK12745   4 VALVTGGRRGIGLGIARALAAAGFDLAINDRPDDeelAATQQElralgVEVIFFPADVADLSAHEAMLDAAQAAWGRIDC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGLV--GEFESYNIEEMHRQMNVNFWGVAYITKEALNLM-----RESGKGGRILQISSVAGYYPSPCLSMYNAS 151
Cdd:PRK12745  84 LVNNAGVGVKvrGDLLDLTPESFDRVLAINLRGPFFLTQAVAKRMlaqpePEELPHRSIVFVSSVNAIMVSPNRGEYCIS 163

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19075741  152 KFAVEGLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK12745 164 KAGLSMAAQLFAARLAEE-GIGVYEVRPGLIKTD 196
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
9-184 3.30e-13

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


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 67.98  E-value: 3.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVkVGLAQ------GYNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK08993  14 VVTGCDTGLGQGMA-LGLAEagcdivGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHIDILVNN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AGygLVGEFESYNIEEMHRQ--MNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK08993  93 AG--LIRREDAIEFSEKDWDdvMNLNIKSVFFMSQAAAKHFIAQGNGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTR 170

                        170       180
                 ....*....|....*....|....*..
gi 19075741  161 TIMREldpnW---NIAITIVQPGGMQT 184
Cdd:PRK08993 171 LMANE----WakhNINVNAIAPGYMAT 193
PRK06114 PRK06114
SDR family oxidoreductase;
9-180 3.46e-13

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 67.88  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYAlVKVGLAQ-GYNVIACSRAPDT--------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK06114  12 FVTGAGSGIGQR-IAIGLAQaGADVALFDLRTDDglaetaehIEAAGRRAIQIAADVTSKADLRAAVARTEAELGALTLA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCL--SMYNASKFAVEG 157
Cdd:PRK06114  91 VNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGS-IVNIASMSGIIVNRGLlqAHYNASKAGVIH 169

                        170       180
                 ....*....|....*....|....*.
gi 19075741  158 LSQTIMREldpnW---NIAITIVQPG 180
Cdd:PRK06114 170 LSKSLAME----WvgrGIRVNSISPG 191
PRK07577 PRK07577
SDR family oxidoreductase;
1-185 4.57e-13

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 67.06  E-value: 4.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKStfSTVLITGSSKGLGYALVKVGLAQGYNVIACSR-APDTITIEhskllKLKLDVTDVKSVETAFKDAKRRFGnVDIV 79
Cdd:PRK07577   1 MSS--RTVLVTGATKGIGLALSLRLANLGHQVIGIARsAIDDFPGE-----LFACDLADIEQTAATLAQINEIHP-VDAI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAgYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK07577  73 VNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQ-GRIVNICSRA-IFGALDRTSYSAAKSALVGCT 150

                        170       180
                 ....*....|....*....|....*.
gi 19075741  160 QTIMRELDPnWNIAITIVQPGGMQTE 185
Cdd:PRK07577 151 RTWALELAE-YGITVNAVAPGPIETE 175
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 8-180 5.32e-13

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


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 67.09  E-value: 5.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL----LKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNA 83
Cdd:PRK10538   3 VLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELgdnlYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   84 GYGLVGE-FESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:PRK10538  83 GLALGLEpAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNH-GHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNL 161

                        170
                 ....*....|....*...
gi 19075741  163 MRELDPNwNIAITIVQPG 180
Cdd:PRK10538 162 RTDLHGT-AVRVTDIEPG 178
PRK12744 PRK12744
SDR family oxidoreductase;
7-184 7.12e-13

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 67.07  E-value: 7.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGyALVKVGLA-QGYNVIA------CSRAPDTITIEH-----SKLLKLKLDVTDVKSVETAFKDAKRRFG 74
Cdd:PRK12744  10 VVLIAGGAKNLG-GLIARDLAaQGAKAVAihynsaASKADAEETVAAvkaagAKAVAFQADLTTAAAVEKLFDDAKAAFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   75 NVDIVINNAGYGLVGEFESYNIEEMHRQMNVNfwgvayiTKEALNLMRESGK----GGRILQI-SSVAGYYpSPCLSMYN 149
Cdd:PRK12744  89 RPDIAINTVGKVLKKPIVEISEAEYDEMFAVN-------SKSAFFFIKEAGRhlndNGKIVTLvTSLLGAF-TPFYSAYA 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19075741  150 ASKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK12744 161 GSKAPVEHFTRAASKEFGAR-GISVTAVGPGPMDT 194
PRK07024 PRK07024
SDR family oxidoreductase;
8-180 7.92e-13

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 66.88  E-value: 7.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITI------EHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK07024   5 VFITGASSGIGQALAREYARQGATLGLVARRTDALQAfaarlpKAARVSVYAADVRDADALAAAAADFIAAHGLPDVVIA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAG--YGLVGEfESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PRK07024  85 NAGisVGTLTE-EREDLAVFREVMDTNYFGMVATFQPFIAPMRAAR-RGTLVGIASVAGVRGLPGAGAYSASKAAAIKYL 162

                        170       180
                 ....*....|....*....|.
gi 19075741  160 QTIMRELDPNwNIAITIVQPG 180
Cdd:PRK07024 163 ESLRVELRPA-GVRVVTIAPG 182
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
7-181 8.74e-13

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 67.31  E-value: 8.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI-TIEHSKLLKL-KLDVTDVKSVETAFKDakrrfgnVDIVINNAG 84
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAaNLAALPGVEFvRGDLRDPEALAAALAG-------VDAVVHLAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  85 YGLVGEfesyniEEMHRQMNVNFWGvayiTKEALNLMRESGkGGRILQISSVA--GYYPSPC--------LSMYNASKFA 154
Cdd:COG0451  74 PAGVGE------EDPDETLEVNVEG----TLNLLEAARAAG-VKRFVYASSSSvyGDGEGPIdedtplrpVSPYGASKLA 142

                       170       180
                ....*....|....*....|....*..
gi 19075741 155 VEGLSQTIMREldpnWNIAITIVQPGG 181
Cdd:COG0451 143 AELLARAYARR----YGLPVTILRPGN 165
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 7-180 1.64e-12

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 65.97  E-value: 1.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR---APDTITIEHSKL---LKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:cd08942   8 IVLVTGGSRGIGRMIAQGFLEAGARVIISARkaeACADAAEELSAYgecIAIPADLSSEEGIEALVARVAERSDRLDVLV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGG---RILQISSVAGYYPSPCLSM-YNASKFAVE 156
Cdd:cd08942  88 NNAGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATAEnpaRVINIGSIAGIVVSGLENYsYGASKAAVH 167

                       170       180
                ....*....|....*....|....
gi 19075741 157 GLSQTIMRELDPNwNIAITIVQPG 180
Cdd:cd08942 168 QLTRKLAKELAGE-HITVNAIAPG 190
PRK06500 PRK06500
SDR family oxidoreductase;
7-184 1.70e-12

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 65.75  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL----LKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK06500   8 TALITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELgesaLVIRADAGDVAAQKALAQALAEAFGRLDAVFIN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AGYGLVGEFESYNIEEMHRQMNVNFWGvAYITKEAL----NlmresgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK06500  88 AGVAKFAPLEDWDEAMFDRSFNTNVKG-PYFLIQALlpllA------NPASIVLNGSINAHIGMPNSSVYAASKAALLSL 160

                        170       180
                 ....*....|....*....|....*.
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK06500 161 AKTLSGELLPR-GIRVNAVSPGPVQT 185
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
 71-202 2.61e-12

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 65.28  E-value: 2.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   71 RRFGNVDIVINNAG-YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSV-----AGYYPspc 144
Cdd:PRK08945  88 EQFGRLDGVLHNAGlLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVgrqgrANWGA--- 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19075741  145 lsmYNASKFAVEGLSQTIMRELDpNWNIAITIVQPGGMQTewassNMQwAKPHPAyEN 202
Cdd:PRK08945 165 ---YAVSKFATEGMMQVLADEYQ-GTNLRVNCINPGGTRT-----AMR-ASAFPG-ED 211
PRK07890 PRK07890
short chain dehydrogenase; Provisional
 7-187 2.81e-12

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 65.36  E-value: 2.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD-------TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07890   7 VVVVSGVGPGLGRTLAVRAARAGADVVLAARTAErldevaaEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDAL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNA-GYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:PRK07890  87 VNNAfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAES--GGSIVMINSMVLRHSQPKYGAYKMAKGALLAA 164

                        170       180
                 ....*....|....*....|....*....
gi 19075741  159 SQTIMRELDPNwNIAITIVQPGGMqteWA 187
Cdd:PRK07890 165 SQSLATELGPQ-GIRVNSVAPGYI---WG 189
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 7-166 3.95e-12

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 64.75  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKL--LKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAG 84
Cdd:PRK06057   9 VAVITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVggLFVPTDVTDEDAVNALFDTAAETYGSVDIAFNNAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 YGLV--GEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSqti 162
Cdd:PRK06057  89 ISPPedDSILNTGLDAWQRVQDVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQISYTASKGGVLAMS--- 165


                 ....
gi 19075741  163 mREL 166
Cdd:PRK06057 166 -REL 168
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 8-186 4.68e-12

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 63.75  E-value: 4.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIehskllklklDVTDVKSVETAFKDAkrrfGNVDIVINNAGYGL 87
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDYQV----------DITDEASIKALFEKV----GHFDAIVSTAGDAE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  88 VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQISSVAGYYPSPC---LSMYNAskfAVEGLSQTIMR 164
Cdd:cd11731  67 FAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLND---GGSITLTSGILAQRPIPGgaaAATVNG---ALEGFVRAAAI 140

                       170       180
                ....*....|....*....|...
gi 19075741 165 EL-DPnwnIAITIVQPGGMQTEW 186
Cdd:cd11731 141 ELpRG---IRINAVSPGVVEESL 160
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 7-165 6.65e-12

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 64.40  E-value: 6.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKvGLAQ-GYNVIACSRAPDT-------ITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:cd08935   7 VAVITGGTGVLGGAMAR-ALAQaGAKVAALGRNQEKgdkvakeITALGGRAIALAADVLDRASLERAREEIVAQFGTVDI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAG--------------YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAGYYPSPC 144
Cdd:cd08935  86 LINGAGgnhpdattdpehyePETEQNFFDLDEEGWEFVFDLNLNGSFLPSQVFGKDMLE-QKGGSIINISSMNAFSPLTK 164

                       170       180
                ....*....|....*....|.
gi 19075741 145 LSMYNASKFAVEGLSQTIMRE 165
Cdd:cd08935 165 VPAYSAAKAAVSNFTQWLAVE 185
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
 8-156 7.19e-12

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 64.18  E-value: 7.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRapdtitiehSKLLKLKLDVTDVKSVETAFKDAKrrfgnVDIVINNAGYGL 87
Cdd:cd05254   2 ILITGATGMLGRALVRLLKERGYEVIGTGR---------SRASLFKLDLTDPDAVEEAIRDYK-----PDVIINCAAYTR 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  88 VGEFESYNIEemhrQMNVNFWGVAYITKEAlnlmreSGKGGRILQISS------VAGYY-----PSPcLSMYNASKFAVE 156
Cdd:cd05254  68 VDKCESDPEL----AYRVNVLAPENLARAA------KEVGARLIHISTdyvfdgKKGPYkeedaPNP-LNVYGKSKLLGE 136
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 8-199 7.65e-12

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


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 63.75  E-value: 7.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIAC----SRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNA 83
Cdd:cd09761   4 AIVTGGGHGIGKQICLDFLEAGDKVVFAdideERGADFAEAEGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLVNNA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  84 GYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIM 163
Cdd:cd09761  84 ARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKN--KGRIINIASTRAFQSEPDSEAYAASKGGLVALTHALA 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19075741 164 RELDPnwNIAITIVQPGGMQT-EWASSNMQWAKP-----HPA 199
Cdd:cd09761 162 MSLGP--DIRVNCISPGWINTtEQQEFTAAPLTQedhaqHPA 201
PRK07831 PRK07831
SDR family oxidoreductase;
7-159 8.73e-12

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 63.90  E-value: 8.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSS-KGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLK---------LKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:PRK07831  19 VVLVTAAAgTGIGSATARRALEEGARVVISDIHERRLGETADELAAelglgrveaVVCDVTSEAQVDALIDAAVERLGRL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   77 DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK07831  99 DVLVNNAGLGGQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIVNNASVLGWRAQHGQAHYAAAKAGVM 178


                 ...
gi 19075741  157 GLS 159
Cdd:PRK07831 179 ALT 181
PRK06101 PRK06101
SDR family oxidoreductase;
6-190 8.74e-12

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 63.73  E-value: 8.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEH---SKLLKLKLDVTDVKSVETAFKDAKRRfgnVDIVINN 82
Cdd:PRK06101   2 TAVLITGATSGIGKQLALDYAKQGWQVIACGRNQSVLDELHtqsANIFTLAFDVTDHPGTKAALSQLPFI---PELWIFN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AG---Y---GLVgefesyNIEEMHRQMNVNFWGVAYITkEALNLMREsgKGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK06101  79 AGdceYmddGKV------DATLMARVFNVNVLGVANCI-EGIQPHLS--CGHRVVIVGSIASELALPRAEAYGASKAAVA 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19075741  157 GLSQTIMRELDPNwNIAITIVQPGGMQTEWASSN 190
Cdd:PRK06101 150 YFARTLQLDLRPK-GIEVVTVFPGFVATPLTDKN 182
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 9-184 1.05e-11

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


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 63.40  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNV-IACSRAP--DTITIEHSKLLKL-KLDVTDVKSVETAFKDAKRRFGNVDIVINNAG 84
Cdd:PRK12936  10 LVTGASGGIGEEIARLLHAQGAIVgLHGTRVEklEALAAELGERVKIfPANLSDRDEVKALGQKAEADLEGVDILVNNAG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALN-LMREsgKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIM 163
Cdd:PRK12936  90 ITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHpMMRR--RYGRIINITSVVGVTGNPGQANYCASKAGMIGFSKSLA 167

                        170       180
                 ....*....|....*....|.
gi 19075741  164 RELDPNwNIAITIVQPGGMQT 184
Cdd:PRK12936 168 QEIATR-NVTVNCVAPGFIES 187
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 7-184 1.18e-11

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 63.64  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKvGLAQGYNVIACSRAPDTITIEHSKLLKLKL---------DVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd05337   3 VAIVTGASRGIGRAIAT-ELAARGFDIAINDLPDDDQATEVVAEVLAAgrraiyfqaDIGELSDHEALLDQAWEDFGRLD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGLVGEFESYNIEE--MHRQMNVNFWGVAYITKEALNLM-----RESGKGGRILQISSVAGYYPSPCLSMYNA 150
Cdd:cd05337  82 CLVNNAGIAVRPRGDLLDLTEdsFDRLIAINLRGPFFLTQAVARRMveqpdRFDGPHRSIIFVTSINAYLVSPNRGEYCI 161

                       170       180       190
                ....*....|....*....|....*....|....
gi 19075741 151 SKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:cd05337 162 SKAGLSMATRLLAYRLADE-GIAVHEIRPGLIHT 194
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 52-192 1.93e-11

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 62.88  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   52 LKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNlMRESGKGGRIL 131
Cdd:PRK12859  73 MELDLTQNDAPKELLNKVTEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFAR-GFDKKSGGRII 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075741  132 QISSVAGYYPSPCLSMYNASKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQTEWASSNMQ 192
Cdd:PRK12859 152 NMTSGQFQGPMVGELAYAATKGAIDALTSSLAAEVAHL-GITVNAINPGPTDTGWMTEEIK 211
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 8-188 2.23e-11

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 61.77  E-value: 2.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI--TIEHSKLLKLKLDVTDVKSVETAFKDAkrrfGNVDIVINNAGY 85
Cdd:cd11730   1 ALILGATGGIGRALARALAGRGWRLLLSGRDAGALagLAAEVGALARPADVAAELEVWALAQEL----GPLDLLVYAAGA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  86 GLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQIssvaGYYPS----PCLSMYNASKFAVEGLSQT 161
Cdd:cd11730  77 ILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAA---GARLVFL----GAYPElvmlPGLSAYAAAKAALEAYVEV 149

                       170       180
                ....*....|....*....|....*...
gi 19075741 162 IMRELDpnwNIAITIVQPGGMQTE-WAS 188
Cdd:cd11730 150 ARKEVR---GLRLTLVRPPAVDTGlWAP 174
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
 8-184 2.57e-11

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


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 62.55  E-value: 2.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLKL--------DVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:cd08933  12 VIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPgsckfvpcDVTKEEDIKTLISVTVERFGRIDCL 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  80 INNAGYGLVGEF-ESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNASKFAVEGL 158
Cdd:cd08933  92 VNNAGWHPPHQTtDETSAQEFRDLLNLNLISYFLASKYALPHLRKS--QGNIINLSSLVGSIGQKQAAPYVATKGAITAM 169

                       170       180
                ....*....|....*....|....*.
gi 19075741 159 SQTIMRELDPnWNIAITIVQPGGMQT 184
Cdd:cd08933 170 TKALAVDESR-YGVRVNCISPGNIWT 194
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
10-185 3.87e-11

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 61.95  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   10 ITGSSKGLGYALVKVGLAQGYNVIA-CS-RAPDTIT-IEHSKLLKLKL-----DVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK12938   8 VTGGMGGIGTSICQRLHKDGFKVVAgCGpNSPRRVKwLEDQKALGFDFiasegNVGDWDSTKAAFDKVKAEVGEIDVLVN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:PRK12938  88 NAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERG-WGRIINISSVNGQKGQFGQTNYSTAKAGIHGFTMS 166

                        170       180
                 ....*....|....*....|....
gi 19075741  162 IMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK12938 167 LAQEVATK-GVTVNTVSPGYIGTD 189
PRK08339 PRK08339
short chain dehydrogenase; Provisional
 9-185 5.51e-11

short chain dehydrogenase; Provisional


Pssm-ID: 169389 [Multi-domain]  Cd Length: 263  Bit Score: 61.79  E-value: 5.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLK--------LKLDVTDVKSVETAFKDAKRrFGNVDIVI 80
Cdd:PRK08339  12 FTTASSKGIGFGVARVLARAGADVILLSRNEENLKKAREKIKSesnvdvsyIVADLTKREDLERTVKELKN-IGEPDIFF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK08339  91 FSTGGPKPGYFMEMSMEDWEGAVKLLLYPAVYLTRALVPAMERKG-FGRIIYSTSVAIKEPIPNIALSNVVRISMAGLVR 169

                        170       180
                 ....*....|....*....|....*
gi 19075741  161 TIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK08339 170 TLAKELGPK-GITVNGIMPGIIRTD 193
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 8-165 5.75e-11

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 61.16  E-value: 5.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741     8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKL-KLDVTDVKSVETAFKDAKrrfgnVDIVINNAGYG 86
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFvEGDLTDRDALEKLLADVR-----PDAVIHLAAVG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    87 LVGEFESYNIEEMHRqmNVNfwgvayITKEALNLMRESGKgGRILQISSVA--------------GYYPSPCLSMYNASK 152
Cdd:pfam01370  76 GVGASIEDPEDFIEA--NVL------GTLNLLEAARKAGV-KRFLFASSSEvygdgaeipqeettLTGPLAPNSPYAAAK 146

                         170
                  ....*....|...
gi 19075741   153 FAVEGLSQTIMRE 165
Cdd:pfam01370 147 LAGEWLVLAYAAA 159
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
 1-181 8.19e-11

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


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 61.11  E-value: 8.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFS--TVLITGSSKGLGYALVKVGLAQGYNVIACSRAP------DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRR 72
Cdd:PRK12823   2 MNQRFAgkVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSElvhevaAELRAAGGEALALTADLETYAGAQAAMAAAVEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   73 FGNVDIVINNAGyGLV--GEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVA--GYYPSPclsmY 148
Cdd:PRK12823  82 FGRIDVLINNVG-GTIwaKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQG-GGAIVNVSSIAtrGINRVP----Y 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19075741  149 NASKFAVEGLSQTIMRELDPNwNIAITIVQPGG 181
Cdd:PRK12823 156 SAAKGGVNALTASLAFEYAEH-GIRVNAVAPGG 187
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 7-181 9.05e-11

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 60.24  E-value: 9.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDtitiehsKLLKLKL--------DVTDVKSVETAFKDakrrfgnVDI 78
Cdd:COG0702   1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPE-------KAAALAAagvevvqgDLDDPESLAAALAG-------VDA 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGEFesynieEMHRQMNVNFwgvayitkeaLNLMRESGkGGRILQISSVAGYYPSPclSMYNASKFAVEgl 158
Cdd:COG0702  67 VFLLVPSGPGGDF------AVDVEGARNL----------ADAAKAAG-VKRIVYLSALGADRDSP--SPYLRAKAAVE-- 125

                       170       180
                ....*....|....*....|...
gi 19075741 159 sqTIMRELDPNWniaiTIVQPGG 181
Cdd:COG0702 126 --EALRASGLPY----TILRPGW 142
PRK09186 PRK09186
flagellin modification protein A; Provisional
 7-181 1.15e-10

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 60.39  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIAC----SRAPD-----TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK09186   6 TILITGAGGLIGSALVKAILEAGGIVIAAdidkEALNElleslGKEFKSKKLSLVELDITDQESLEEFLSKSAEKYGKID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNA-----GYGLVgeFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAG-------YYPSPCL 145
Cdd:PRK09186  86 GAVNCAyprnkDYGKK--FFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQG-GGNLVNISSIYGvvapkfeIYEGTSM 162

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19075741  146 SM---YNASKFAVEGLSQTIMRELDpNWNIAITIVQPGG 181
Cdd:PRK09186 163 TSpveYAAIKAGIIHLTKYLAKYFK-DSNIRVNCVSPGG 200
PLN02253 PLN02253
xanthoxin dehydrogenase
 9-187 1.16e-10

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 60.99  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIEhSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PLN02253  22 LVTGGATGIGESIVRLFHKHGAKVCivdlqddLGQNVCDSLGGE-PNVCFFHCDVTVEDDVSRAVDFTVDKFGTLDIMVN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   82 NAGYG--LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGrILQISSVAGYYPSPCLSMYNASKFAVEGLS 159
Cdd:PLN02253 101 NAGLTgpPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGS-IVSLCSVASAIGGLGPHAYTGSKHAVLGLT 179

                        170       180
                 ....*....|....*....|....*...
gi 19075741  160 QTIMRELDPNwNIAITIVQPGGMQTEWA 187
Cdd:PLN02253 180 RSVAAELGKH-GIRVNCVSPYAVPTALA 206
PRK07677 PRK07677
short chain dehydrogenase; Provisional
 7-139 1.57e-10

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 60.08  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT-----IEH--SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIV 79
Cdd:PRK07677   3 VVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEeakleIEQfpGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDAL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   80 INNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQIssVAGY 139
Cdd:PRK07677  83 INNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKGIKGNIINM--VATY 140
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
8-170 1.71e-10

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 60.15  E-value: 1.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSkG-LGYALVKVGLAQGYNVIACSRAPdtitiehskllklkLDVTDVKSVETAFKDAKrrfgnVDIVINNAGYG 86
Cdd:COG1091   2 ILVTGAN-GqLGRALVRLLAERGYEVVALDRSE--------------LDITDPEAVAALLEEVR-----PDVVINAAAYT 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  87 LVGEFESyNIEEMHRqmnVNFWGVAYITKEALNLmresgkGGRILQISS--V-----AGYY-----PSPcLSMYNASKFA 154
Cdd:COG1091  62 AVDKAES-EPELAYA---VNATGPANLAEACAEL------GARLIHISTdyVfdgtkGTPYteddpPNP-LNVYGRSKLA 130

                       170
                ....*....|....*.
gi 19075741 155 VEglsqTIMRELDPNW 170
Cdd:COG1091 131 GE----QAVRAAGPRH 142
PRK05875 PRK05875
short chain dehydrogenase; Provisional
 1-185 1.74e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 60.20  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFS--TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLK---------LDVTDVKSVETAFKDA 69
Cdd:PRK05875   1 MQLSFQdrTYLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALKgagavryepADVTDEDQVARAVDAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   70 KRRFGNVDIVINNAGYGL-VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMY 148
Cdd:PRK05875  81 TAWHGRLHGVVHCAGGSEtIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGG-GGSFVGISSIAASNTHRWFGAY 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 19075741  149 NASKFAVEGLSQTIMRELDPNWnIAITIVQPGGMQTE 185
Cdd:PRK05875 160 GVTKSAVDHLMKLAADELGPSW-VRVNSIRPGLIRTD 195
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 1-166 2.04e-10

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 59.91  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFS----TVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIEHSKLLKLKLDVTDVKSVETAFKDA 69
Cdd:PRK08277   2 MPNLFSlkgkVAVITGGGGVLGGAMAKELARAGAKVAILDRnqekaeaVVAEIKAAGGEALAVKADVLDKESLEQARQQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   70 KRRFGNVDIVINNAG------------YGLVGEFESY---NIEEMHRQMNVNFWGVAYITKEALNLMREsGKGGRILQIS 134
Cdd:PRK08277  82 LEDFGPCDILINGAGgnhpkattdnefHELIEPTKTFfdlDEEGFEFVFDLNLLGTLLPTQVFAKDMVG-RKGGNIINIS 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19075741  135 SVAGYYPSPCLSMYNASKFAVEGLSQTIMREL 166
Cdd:PRK08277 161 SMNAFTPLTKVPAYSAAKAAISNFTQWLAVHF 192
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
 8-204 2.86e-10

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 59.13  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIE---HSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd05340   7 ILVTGASDGIGREAALTYARYGATVILLGRneeklrqVADHINEEggrQPQWFILDLLTCTSENCQQLAQRIAVNYPRLD 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGY-GLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVaGYYPSPCLSMYNASKFAVE 156
Cdd:cd05340  87 GVLHNAGLlGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSV-GRQGRANWGAYAVSKFATE 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 19075741 157 GLSQTIMRELDpNWNIAITIVQPGGMQTEwassnmQWAKPHPAyENDR 204
Cdd:cd05340 166 GL*QVLADEYQ-QRNLRVNCINPGGTRTA------MRASAFPT-EDPQ 205
PRK07814 PRK07814
SDR family oxidoreductase;
9-185 6.32e-10

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 58.64  E-value: 6.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGyALVKVGLAQ-GYNVIACSRA-------PDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK07814  14 VVTGAGRGLG-AAIALAFAEaGADVLIAARTesqldevAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRLDIVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQ 160
Cdd:PRK07814  93 NNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPLMLEHSGGGSVINISSTMGRLAGRGFAAYGTAKAALAHYTR 172

                        170       180
                 ....*....|....*....|....*
gi 19075741  161 TIMRELDPnwNIAITIVQPGGMQTE 185
Cdd:PRK07814 173 LAALDLCP--RIRVNAIAPGSILTS 195
PRK07985 PRK07985
SDR family oxidoreductase;
9-184 6.52e-10

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 58.85  E-value: 6.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNViACSRAPD--------TITIEHS--KLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK07985  53 LVTGGDSGIGRAAAIAYAREGADV-AISYLPVeeedaqdvKKIIEECgrKAVLLPGDLSDEKFARSLVHEAHKALGGLDI 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGL-VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMResgKGGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:PRK07985 132 MALVAGKQVaIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLP---KGASIITTSSIQAYQPSPHLLDYAATKAAILN 208

                        170       180
                 ....*....|....*....|....*..
gi 19075741  158 LSQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK07985 209 YSRGLAKQVAEK-GIRVNIVAPGPIWT 234
RmlD_sub_bind pfam04321
RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some ...
 8-172 8.55e-10

RmlD substrate binding domain; L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.


Pssm-ID: 427865 [Multi-domain]  Cd Length: 284  Bit Score: 58.44  E-value: 8.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741     8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPdtitiehskllklkLDVTDVKSVETAFKDAKRrfgnvDIVINNAGYGL 87
Cdd:pfam04321   1 ILITGANGQLGTELRRLLAERGIEVVALTRAE--------------LDLTDPEAVARLLREIKP-----DVVVNAAAYTA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    88 VGEFESynieEMHRQMNVNFWGVAYITKEAlnlmreSGKGGRILQISS-------VAGYY-----PSPcLSMYNASKFAV 155
Cdd:pfam04321  62 VDKAES----EPDLAYAINALAPANLAEAC------AAVGAPLIHISTdyvfdgtKPRPYeeddeTNP-LNVYGRTKLAG 130

                         170
                  ....*....|....*..
gi 19075741   156 EglsQTImRELDPNWNI 172
Cdd:pfam04321 131 E---QAV-RAAGPRHLI 143
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 7-180 8.93e-10

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 58.10  E-value: 8.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT---ITIEH-SKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINN 82
Cdd:PRK08265   8 VAIVTGGATLIGAAVARALVAAGARVAIVDIDADNgaaVAASLgERARFIATDITDDAAIERAVATVVARFGRVDILVNL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 A-GYGLVGeFESyNIEEMHRQMNVNFWGVAYITKEALNLMResGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQT 161
Cdd:PRK08265  88 AcTYLDDG-LAS-SRADWLAALDVNLVSAAMLAQAAHPHLA--RGGGAIVNFTSISAKFAQTGRWLYPASKAAIRQLTRS 163

                        170
                 ....*....|....*....
gi 19075741  162 IMRELDPNwNIAITIVQPG 180
Cdd:PRK08265 164 MAMDLAPD-GIRVNSVSPG 181
PRK07074 PRK07074
SDR family oxidoreductase;
6-208 1.02e-09

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 57.86  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI-----TIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK07074   3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALaafadALGDARFVPVACDLTDAASLAAALANAAAERGPVDVLV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAGYGLVGEFESYNIEEMHRQMNVNFWGvAYITKEALNL-MRESGKGGrILQISSVAGY----YPSpclsmYNASKFAV 155
Cdd:PRK07074  83 ANAGAARAASLHDTTPASWRADNALNLEA-AYLCVEAVLEgMLKRSRGA-VVNIGSVNGMaalgHPA-----YSAAKAGL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19075741  156 EGLSQTIMRELDpNWNIAITIVQPGGMQTE-W---ASSNMQwakphpAYENDRSWRP 208
Cdd:PRK07074 156 IHYTKLLAVEYG-RFGIRANAVAPGTVKTQaWearVAANPQ------VFEELKKWYP 205
PRK08278 PRK08278
SDR family oxidoreductase;
7-134 4.63e-09

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 56.07  E-value: 4.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNV--IACSRAPD-----TItieHS----------KLLKLKLDVTDVKSVETAFKDA 69
Cdd:PRK08278   8 TLFITGASRGIGLAIALRAARDGANIviAAKTAEPHpklpgTI---HTaaeeieaaggQALPLVGDVRDEDQVAAAVAKA 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075741   70 KRRFGNVDIVINNAGYGLVGEFESYnieEMHR---QMNVNFWGVAYITKEALNLMRESGkGGRILQIS 134
Cdd:PRK08278  85 VERFGGIDICVNNASAINLTGTEDT---PMKRfdlMQQINVRGTFLVSQACLPHLKKSE-NPHILTLS 148
PRK07023 PRK07023
SDR family oxidoreductase;
9-185 5.96e-09

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 55.40  E-value: 5.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVIACSRA--PDTITIEHSKLLKLKLDVTDVKSVET--------AFKDAKRRFgnvdI 78
Cdd:PRK07023   5 IVTGHSRGLGAALAEQLLQPGIAVLGVARSrhPSLAAAAGERLAEVELDLSDAAAAAAwlagdllaAFVDGASRV----L 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAG-YGLVGEFESYNIEEMHRQMNVNFWGVAYITkEALNLMRESGKGGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:PRK07023  81 LINNAGtVEPIGPLATLDAAAIARAVGLNVAAPLMLT-AALAQAASDAAERRILHISSGAARNAYAGWSVYCATKAALDH 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19075741  158 LSQTImrELDPNWNIAITIVQPG----GMQTE 185
Cdd:PRK07023 160 HARAV--ALDANRALRIVSLAPGvvdtGMQAT 189
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
 7-134 6.36e-09

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 55.53  E-value: 6.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYN-VIACSRA------PDTI-----TIEHS--KLLKLKLDVTDVKSVETAFKDAKRR 72
Cdd:cd09762   5 TLFITGASRGIGKAIALKAARDGANvVIAAKTAephpklPGTIytaaeEIEAAggKALPCIVDIRDEDQVRAAVEKAVEK 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075741  73 FGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQIS 134
Cdd:cd09762  85 FGGIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKKS-KNPHILNLS 145
PRK07576 PRK07576
short chain dehydrogenase; Provisional
 1-180 7.02e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 55.35  E-value: 7.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFS----TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD-------TITIEHSKLLKLKLDVTDVKSVETAFKDA 69
Cdd:PRK07576   1 MTTMFDfagkNVVVVGGTSGINLGIAQAFARAGANVAVASRSQEkvdaavaQLQQAGPEGLGVSADVRDYAAVEAAFAQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   70 KRRFGNVDIVINNAGyglvGEFESyNIEEMHRQ-----MNVNFWGVAYITKEALNLMREsgKGGRILQISSVAGYYPSPC 144
Cdd:PRK07576  81 ADEFGPIDVLVSGAA----GNFPA-PAAGMSANgfktvVDIDLLGTFNVLKAAYPLLRR--PGASIIQISAPQAFVPMPM 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 19075741  145 LSMYNASKFAVEGLSQTIMRELDPNwNIAITIVQPG 180
Cdd:PRK07576 154 QAHVCAAKAGVDMLTRTLALEWGPE-GIRVNSIVPG 188
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 7-189 1.10e-08

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 54.16  E-value: 1.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTIT-IEHSKLLKLKLDVTDVKSVETAFKdakrrfgNVDIVINNAGy 85
Cdd:cd05243   1 KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEkLEAAGAEVVVGDLTDAESLAAALE-------GIDAVISAAG- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  86 glVGEFESYNIEEmhrqmnVNFWGvayitkeALNLMRESGKGG--RILQISSVAGYYPSPCLSM----YNASKFAVEGLs 159
Cdd:cd05243  73 --SGGKGGPRTEA------VDYDG-------NINLIDAAKKAGvkRFVLVSSIGADKPSHPLEAlgpyLDAKRKAEDYL- 136

                       170       180       190
                ....*....|....*....|....*....|
gi 19075741 160 qtimRELDPNWniaiTIVQPGGMQTEWASS 189
Cdd:cd05243 137 ----RASGLDY----TIVRPGGLTDDPAGT 158
PRK07806 PRK07806
SDR family oxidoreductase;
7-169 1.51e-08

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 54.34  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIA--CSRAP------DTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDI 78
Cdd:PRK07806   8 TALVTGSSRGIGADTAKILAGAGAHVVVnyRQKAPrankvvAEIEAAGGRASAVGADLTDEESVAALMDTAREEFGGLDA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAGYGL-VGEFESYNIeEMHRQMNVNfwgvayITKEALNLMREsgkGGRILQISS-VAGYYPS-PCLSMYN---ASK 152
Cdd:PRK07806  88 LVLNASGGMeSGMDEDYAM-RLNRDAQRN------LARAALPLMPA---GSRVVFVTShQAHFIPTvKTMPEYEpvaRSK 157

                        170
                 ....*....|....*..
gi 19075741  153 FAVEglsqTIMRELDPN 169
Cdd:PRK07806 158 RAGE----DALRALRPE 170
PRK09242 PRK09242
SDR family oxidoreductase;
7-189 1.55e-08

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 54.37  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLK---------LKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK09242  11 TALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELAEefperevhgLAADVSDDEDRRAILDWVEDHWDGLH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYYPSPCLSMYNASKFAVEG 157
Cdd:PRK09242  91 ILVNNAGGNIRKAAIDYTEDEWRGIFETNLFSAFELSRYAHPLLKQHAS-SAIVNIGSVSGLTHVRSGAPYGMTKAALLQ 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19075741  158 LSqtimRELDPNW---NIAITIVQPGGMQTEWASS 189
Cdd:PRK09242 170 MT----RNLAVEWaedGIRVNAVAPWYIRTPLTSG 200
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 9-192 4.74e-08

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 53.14  E-value: 4.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKvglaqgynviACSRAPDTITIEHSKLLKL-----------------KLDVTDVKSVETAFKDAKR 71
Cdd:PRK07097  14 LITGASYGIGFAIAK----------AYAKAGATIVFNDINQELVdkglaayrelgieahgyVCDVTDEDGVQAMVSQIEK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   72 RFGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSPCLSMYNAS 151
Cdd:PRK07097  84 EVGVIDILVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKG-HGKIINICSMMSELGRETVSAYAAA 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19075741  152 KFAVEGLSQtimreldpnwNIAitivqpggmqTEWASSNMQ 192
Cdd:PRK07097 163 KGGLKMLTK----------NIA----------SEYGEANIQ 183
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
 7-142 7.05e-08

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 52.20  E-value: 7.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITG--SSKGLGYALVKVGLAQGYNViACSRAPDTITIEHSKLLK--------LKLDVTDVKSVETAFKDAKRRFGNV 76
Cdd:cd05372   3 RILITGiaNDRSIAWGIAKALHEAGAEL-AFTYQPEALRKRVEKLAErlgesalvLPCDVSNDEEIKELFAEVKKDWGKL 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  77 DIVINNAGYG----LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQISsvagYYPS 142
Cdd:cd05372  82 DGLVHSIAFApkvqLKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNP---GGSIVTLS----YLGS 144
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 7-84 8.70e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 52.34  E-value: 8.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIEHSK--LLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:PRK06197  18 VAVVTGANTGLGYETAAALAAKGAHVVLAVRnldkgkaAAARITAATPGadVTLQELDLTSLASVRAAADALRAAYPRID 97


                 ....*..
gi 19075741   78 IVINNAG 84
Cdd:PRK06197  98 LLINNAG 104
PRK08628 PRK08628
SDR family oxidoreductase;
8-165 1.14e-07

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 51.88  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVgLAQ--GYNVIACSRAPD-----TITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVI 80
Cdd:PRK08628  10 VIVTGGASGIGAAISLR-LAEegAIPVIFGRSAPDdefaeELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   81 NNAG----YGLvgefESyNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNASKFAVE 156
Cdd:PRK08628  89 NNAGvndgVGL----EA-GREAFVASLERNLIHYYVMAHYCLPHLKAS--RGAIVNISSKTALTGQGGTSGYAAAKGAQL 161


                 ....*....
gi 19075741  157 GLSqtimRE 165
Cdd:PRK08628 162 ALT----RE 166
PRK09135 PRK09135
pteridine reductase; Provisional
 8-180 1.35e-07

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 51.47  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIA----------------CSRAPDTITIehskllkLKLDVTDVKSVETAFKDAKR 71
Cdd:PRK09135   9 ALITGGARRIGAAIARTLHAAGYRVAIhyhrsaaeadalaaelNALRPGSAAA-------LQADLLDPDALPELVAACVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   72 RFGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkGGRILQISSVAGYYPSPCLSMYNAS 151
Cdd:PRK09135  82 AFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQ--RGAIVNITDIHAERPLKGYPVYCAA 159

                        170       180
                 ....*....|....*....|....*....
gi 19075741  152 KFAVEGLSQTIMRELDPnwNIAITIVQPG 180
Cdd:PRK09135 160 KAALEMLTRSLALELAP--EVRVNAVAPG 186
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 1-185 1.76e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 51.20  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLK--------LKLDVTDVKSVETAFKDAkrr 72
Cdd:PRK06125   3 LHLAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAahgvdvavHALDLSSPEAREQLAAEA--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   73 fGNVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGkGGRILQISSVAGYYPSP---CLSMYN 149
Cdd:PRK06125  80 -GDIDILVNNAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARG-SGVIVNVIGAAGENPDAdyiCGSAGN 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19075741  150 AS--KF--AVEGLSqtimreldPNWNIAITIVQPGGMQTE 185
Cdd:PRK06125 158 AAlmAFtrALGGKS--------LDDGVRVVGVNPGPVATD 189
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 8-185 2.04e-07

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 50.91  E-value: 2.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYAlVKVGLAQ-GYNVIACSRAP--------DTITIEHSKLLKLKLDVTDVKSVETAF-KDAKRRFGNVD 77
Cdd:cd09763   6 ALVTGASRGIGRG-IALQLGEaGATVYITGRTIlpqlpgtaEEIEARGGKCIPVRCDHSDDDEVEALFeRVAREQQGRLD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNA--GYGLVGEFESYNIEEMHRQM-----NVNFWGVAYITKEALNLMRESGKgGRILQISSVAG--YYPSPclsMY 148
Cdd:cd09763  85 ILVNNAyaAVQLILVGVAKPFWEEPPTIwddinNVGLRAHYACSVYAAPLMVKAGK-GLIVIISSTGGleYLFNV---AY 160

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19075741 149 NASKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd09763 161 GVGKAAIDRMAADMAHELKPH-GVAVVSLWPGFVRTE 196
3KS_SDR_c cd08941
3-keto steroid reductase, classical (c) SDRs; 3-keto steroid reductase (in concert with other ...
 8-180 3.28e-07

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


Pssm-ID: 187645 [Multi-domain]  Cd Length: 290  Bit Score: 50.46  E-value: 3.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYN------VIAC---SRAPDTItiehSKLLK-----------LKLDVTDVKSVETAFK 67
Cdd:cd08941   4 VLVTGANSGLGLAICERLLAEDDEnpeltlILACrnlQRAEAAC----RALLAshpdarvvfdyVLVDLSNMVSVFAAAK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  68 DAKRRFGNVDIVINNAGYG--------------LVGEFESYNIEEMHRQ-------------------MNVNFWGVAYIT 114
Cdd:cd08941  80 ELKKRYPRLDYLYLNAGIMpnpgidwigaikevLTNPLFAVTNPTYKIQaegllsqgdkatedglgevFQTNVFGHYYLI 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075741 115 KEALNLMRESGKGGRILQISSV---AGYY----------PSPclsmYNASKFAVEGLSQTIMRELDpNWNIAITIVQPG 180
Cdd:cd08941 160 RELEPLLCRSDGGSQIIWTSSLnasPKYFslediqhlkgPAP----YSSSKYLVDLLSLALNRKFN-KLGVYSYVVHPG 233
PRK12747 PRK12747
short chain dehydrogenase; Provisional
 9-185 4.09e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 50.07  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKvGLAQGYNVIAC---SRAPDT------ITIEHSKLLKLKLDVTDVKSVETAFK----DAKRRFGN 75
Cdd:PRK12747   8 LVTGASRGIGRAIAK-RLANDGALVAIhygNRKEEAeetvyeIQSNGGSAFSIGANLESLHGVEALYSsldnELQNRTGS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   76 V--DIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkgGRILQISSVAGYYPSPCLSMYNASKF 153
Cdd:PRK12747  87 TkfDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDN---SRIINISSAATRISLPDFIAYSMTKG 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 19075741  154 AVEGLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK12747 164 AINTMTFTLAKQLGAR-GITVNAILPGFIKTD 194
PRK06953 PRK06953
SDR family oxidoreductase;
6-185 4.53e-07

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 49.69  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTI-TIEHSKLLKLKLDVTDVKSVET-AFK-DAKRrfgnVDIVINN 82
Cdd:PRK06953   2 KTVLIVGASRGIGREFVRQYRADGWRVIATARDAAALaALQALGAEALALDVADPASVAGlAWKlDGEA----LDAAVYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   83 AG-YG-LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESG--------KGGRILQISSVAGYypspclsMYNASK 152
Cdd:PRK06953  78 AGvYGpRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAGgvlavlssRMGSIGDATGTTGW-------LYRASK 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 19075741  153 FAVeglsQTIMRELDPNWNIAITI-VQPGGMQTE 185
Cdd:PRK06953 151 AAL----NDALRAASLQARHATCIaLHPGWVRTD 180
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
 7-141 6.14e-07

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 49.41  E-value: 6.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIehskllklklDVTDVKSVETAFKD-AKRRFGNVDIVINNAGY 85
Cdd:cd05328   1 TIVITGAASGIGAATAELLEDAGHTVIGIDLREADVIA----------DLSTPEGRAAAIADvLARCSGVLDGLVNCAGV 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075741  86 GlvGEFESYNIeemhrqMNVNFWGVAYITKEALNLMREsGKGGRILQISSVAGYYP 141
Cdd:cd05328  71 G--GTTVAGLV------LKVNYFGLRALMEALLPRLRK-GHGPAAVVVSSIAGAGW 117
PRK12746 PRK12746
SDR family oxidoreductase;
9-185 7.70e-07

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 49.26  E-value: 7.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVK--------VGLAQGYNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRF------G 74
Cdd:PRK12746  10 LVTGASRGIGRAIAMrlandgalVAIHYGRNKQAADETIREIESNGGKAFLIEADLNSIDGVKKLVEQLKNELqirvgtS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   75 NVDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgkgGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:PRK12746  90 EIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE---GRVINISSAEVRLGFTGSIAYGLSKGA 166

                        170       180       190
                 ....*....|....*....|....*....|.
gi 19075741  155 VEGLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK12746 167 LNTMTLPLAKHLGER-GITVNTIMPGYTKTD 196
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
 8-81 2.00e-06

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 47.62  E-value: 2.00e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAkrrfgnvDIVIN 81
Cdd:cd05244   2 IAIIGATGRTGSAIVREALARGHEVTALVRDPAKLPAEHEKLKVVQGDVLDLEDVKEALEGQ-------DAVIS 68
PRK06603 PRK06603
enoyl-[acyl-carrier-protein] reductase FabI;
53-184 2.34e-06

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


Pssm-ID: 168626 [Multi-domain]  Cd Length: 260  Bit Score: 47.69  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   53 KLDVTDVKSVETAFKDAKRRFGNVDIVINNAGYG----LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGG 128
Cdd:PRK06603  64 ELDVTNPKSISNLFDDIKEKWGSFDFLLHGMAFAdkneLKGRYVDTSLENFHNSLHISCYSLLELSRSAEALMHD---GG 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075741  129 RILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQT 184
Cdd:PRK06603 141 SIVTLTYYGAEKVIPNYNVMGVAKAALEASVKYLANDMGEN-NIRVNAISAGPIKT 195
FabI COG0623
Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl- ...
 7-138 2.50e-06

Enoyl-[acyl-carrier-protein] reductase FabI [Lipid transport and metabolism]; Enoyl-[acyl-carrier-protein] reductase FabI is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440388 [Multi-domain]  Cd Length: 254  Bit Score: 47.71  E-value: 2.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITG--SSKGLGYALVKVGLAQGYNViACSRAPDTITIEHSKLLK-------LKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:COG0623   7 RGLITGvaNDRSIAWGIAKALHEEGAEL-AFTYQGEALKKRVEPLAEelgsalvLPCDVTDDEQIDALFDEIKEKWGKLD 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075741  78 IVINNAGYG----LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsgkGGRILQISSVAG 138
Cdd:COG0623  86 FLVHSIAFApkeeLGGRFLDTSREGFLLAMDISAYSLVALAKAAEPLMNE---GGSIVTLTYLGA 147
PRK08177 PRK08177
SDR family oxidoreductase;
7-185 2.75e-06

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 47.33  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPdtitiEHSKLLK-------LKLDVTDVKSVET-AFKDAKRRFgnvDI 78
Cdd:PRK08177   3 TALIIGASRGLGLGLVDRLLERGWQVTATVRGP-----QQDTALQalpgvhiEKLDMNDPASLDQlLQRLQGQRF---DL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   79 VINNAG-YG-LVGEFESYNIEEMHRQMNVNfwGVAYItKEALNLMRESGKGGRILQ-ISSVAGYY---PSPCLSMYNASK 152
Cdd:PRK08177  75 LFVNAGiSGpAHQSAADATAAEIGQLFLTN--AIAPI-RLARRLLGQVRPGQGVLAfMSSQLGSVelpDGGEMPLYKASK 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 19075741  153 FAVEGLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:PRK08177 152 AALNSMTRSFVAELGEP-TLTVLSMHPGWVKTD 183
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 6-106 3.00e-06

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 47.49  E-value: 3.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKVGLAQGYNVIA----CSRAPDTITIEHSKLLKLKLDVTDVKSVEtAFKDAKRRFGNVDIVIN 81
Cdd:cd08951   8 KRIFITGSSDGLGLAAARTLLHQGHEVVLharsQKRAADAKAACPGAAGVLIGDLSSLAETR-KLADQVNAIGRFDAVIH 86

                        90       100
                ....*....|....*....|....*
gi 19075741  82 NAGYGLvGEFESYNIEEMHRQMNVN 106
Cdd:cd08951  87 NAGILS-GPNRKTPDTGIPAMVAVN 110
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 6-138 3.74e-06

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 47.70  E-value: 3.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAPdtitiehSKLLKLKLDVTDVKSVETAF-KDAKRRFGnVDIVINNAG 84
Cdd:cd08259 164 DTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSP-------EKLKILKELGADYVIDGSKFsEDVKKLGG-ADVVIELVG 235

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19075741  85 yglvgefeSYNIEEMHRQMNvnfwgvayitkealnlmresgKGGRILQISSVAG 138
Cdd:cd08259 236 --------SPTIEESLRSLN---------------------KGGRLVLIGNVTP 260
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 6-84 6.28e-06

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


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 46.98  E-value: 6.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKvGLAQGY--NVIACSR--APDTITIEHSKLLKLK----------LDVTDVKSVETAFKDAKR 71
Cdd:cd08953 206 GVYLVTGGAGGIGRALAR-ALARRYgaRLVLLGRspLPPEEEWKAQTLAALEalgarvlyisADVTDAAAVRRLLEKVRE 284

                        90
                ....*....|...
gi 19075741  72 RFGNVDIVINNAG 84
Cdd:cd08953 285 RYGAIDGVIHAAG 297
PRK07370 PRK07370
enoyl-[acyl-carrier-protein] reductase FabI;
50-189 7.39e-06

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


Pssm-ID: 180949 [Multi-domain]  Cd Length: 258  Bit Score: 46.25  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   50 LKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGY----GLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMREsg 125
Cdd:PRK07370  62 LFLPCDVQDDAQIEETFETIKQKWGKLDILVHCLAFagkeELIGDFSATSREGFARALEISAYSLAPLCKAAKPLMSE-- 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19075741  126 kGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQTeWASS 189
Cdd:PRK07370 140 -GGSIVTLTYLGGVRAIPNYNVMGVAKAALEASVRYLAAELGPK-NIRVNAISAGPIRT-LASS 200
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 7-147 9.53e-06

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 46.18  E-value: 9.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIAcsrapdtITIEHSKlLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAGyg 86
Cdd:PRK13771 165 TVLVTGAGGGVGIHAIQVAKALGAKVIA-------VTSSESK-AKIVSKYADYVIVGSKFSEEVKKIGGADIVIETVG-- 234

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075741   87 lvgefeSYNIEEMHRQMNVnfwgvayitkealnlmresgkGGRILQISSVAgyyPSPCLSM 147
Cdd:PRK13771 235 ------TPTLEESLRSLNM---------------------GGKIIQIGNVD---PSPTYSL 265
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 6-138 1.31e-05

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 45.97  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSKGLGYALVKVGLAQG--YNVIAC------SRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd09810   2 GTVVITGASSGLGLAAAKALARRGewHVVMACrdflkaEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLD 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075741  78 IVINNAGYGLVGEFE-SYNIEEMHRQMNVNFWGVAYITKEAL-NLMRESGKGGRILQISSVAG 138
Cdd:cd09810  82 ALVCNAAVYLPTAKEpRFTADGFELTVGVNHLGHFLLTNLLLeDLQRSENASPRIVIVGSITH 144
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 7-185 1.35e-05

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 45.54  E-value: 1.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVI-------ACSRAPDTITIE--HSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd09807   3 TVIITGANTGIGKETARELARRGARVImacrdmaKCEEAAAEIRRDtlNHEVIVRHLDLASLKSIRAFAAEFLAEEDRLD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAGYGLVGEFESYNIEEMhrQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYY------------PSPCL 145
Cdd:cd09807  83 VLINNAGVMRCPYSKTEDGFEM--QFGVNHLGHFLLTNLLLDLLKKSAP-SRIVNVSSLAHKAgkinfddlnsekSYNTG 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19075741 146 SMYNASKFAVEGLSQTIMRELDPNwNIAITIVQPGGMQTE 185
Cdd:cd09807 160 FAYCQSKLANVLFTRELARRLQGT-GVTVNALHPGVVRTE 198
PRK05717 PRK05717
SDR family oxidoreductase;
9-180 2.03e-05

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 44.88  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    9 LITGSSKGLGYALVKVGLAQGYNVIAC----SRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVDIVINNAG 84
Cdd:PRK05717  14 LVTGAARGIGLGIAAWLIAEGWQVVLAdldrERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVCNAA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   85 YG--LVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMResGKGGRILQISSVAGYYPSPCLSMYNASKFAVEGLSQTI 162
Cdd:PRK05717  94 IAdpHNTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLR--AHNGAIVNLASTRARQSEPDTEAYAASKGGLLALTHAL 171

                        170
                 ....*....|....*...
gi 19075741  163 MRELDPnwNIAITIVQPG 180
Cdd:PRK05717 172 AISLGP--EIRVNAVSPG 187
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
 7-156 2.27e-05

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 45.28  E-value: 2.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVI-ACSRA--PDTITIEHSKLLKLKL-----DVTDVKSVETAFKDAKRrfgnvDI 78
Cdd:cd05260   1 RALITGITGQDGSYLAEFLLEKGYEVHgIVRRSssFNTDRIDHLYINKDRItlhygDLTDSSSLRRAIEKVRP-----DE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  79 VINNAGYGLVGefESYNIEEmhRQMNVNFWGVAYItkeaLNLMRESGKGGRILQISSVAGY--------------YP-SP 143
Cdd:cd05260  76 IYHLAAQSHVK--VSFDDPE--YTAEVNAVGTLNL----LEAIRILGLDARFYQASSSEEYgkvqelpqsettpfRPrSP 147

                       170
                ....*....|...
gi 19075741 144 clsmYNASKFAVE 156
Cdd:cd05260 148 ----YAVSKLYAD 156
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 7-180 3.59e-05

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 44.16  E-value: 3.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDtitieHSKLLKLKLDVTDVKSVETAFKDA---KRRFGNVDIVINna 83
Cdd:cd05271   2 VVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEA-----YARRLLVMGDLGQVLFVEFDLRDDesiRKALEGSDVVIN-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  84 gygLVG---EFESYNIEemhrqmNVNFWGVAYITKEAlnlmRESGKgGRILQISSVAGYYPSPclSMYNASKFAVEGLsq 160
Cdd:cd05271  75 ---LVGrlyETKNFSFE------DVHVEGPERLAKAA----KEAGV-ERLIHISALGADANSP--SKYLRSKAEGEEA-- 136

                       170       180
                ....*....|....*....|
gi 19075741 161 tiMRELDPNWniaiTIVQPG 180
Cdd:cd05271 137 --VREAFPEA----TIVRPS 150
PRK08703 PRK08703
SDR family oxidoreductase;
7-208 3.59e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 44.15  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSR-------APDTITIE-HSKLLKLKLDVTDVKSVE---TAFKDAKRRFGN 75
Cdd:PRK08703   8 TILVTGASQGLGEQVAKAYAAAGATVILVARhqkklekVYDAIVEAgHPEPFAIRFDLMSAEEKEfeqFAATIAEATQGK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   76 VDIVINNAGYGL-VGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNASKFA 154
Cdd:PRK08703  88 LDGIVHCAGYFYaLSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQS-PDASVIFVGESHGETPKAYWGGFGASKAA 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19075741  155 VEGLSQTIMRELDPNWNIAITIVQPGGMQTEwassnmQWAKPHPAyeNDRSWRP 208
Cdd:PRK08703 167 LNYLCKVAADEWERFGNLRANVLVPGPINSP------QRIKSHPG--EAKSERK 212
PRK06196 PRK06196
oxidoreductase; Provisional
 7-84 9.40e-05

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 43.13  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD-----TITIEHSKLlkLKLDVTDVKSVE---TAFKDAKRRfgnVDI 78
Cdd:PRK06196  28 TAIVTGGYSGLGLETTRALAQAGAHVIVPARRPDvareaLAGIDGVEV--VMLDLADLESVRafaERFLDSGRR---IDI 102


                 ....*.
gi 19075741   79 VINNAG 84
Cdd:PRK06196 103 LINNAG 108
PRK08340 PRK08340
SDR family oxidoreductase;
8-84 1.07e-04

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 42.87  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKL------KLDVTDVKSVETAFKDAKRRFGNVDIVIN 81
Cdd:PRK08340   3 VLVTASSRGIGFNVARELLKKGARVVISSRNEENLEKALKELKEYgevyavKADLSDKDDLKNLVKEAWELLGGIDALVW 82


                 ...
gi 19075741   82 NAG 84
Cdd:PRK08340  83 NAG 85
PRK08416 PRK08416
enoyl-ACP reductase;
7-185 1.55e-04

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 42.45  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    7 TVLITGSSKGLGYALVK------VGLAQGYNviACSRAPDTITIEHSKLLKLK-----LDVTDVKSVETAFKDAKRRFGN 75
Cdd:PRK08416  10 TLVISGGTRGIGKAIVYefaqsgVNIAFTYN--SNVEEANKIAEDLEQKYGIKakaypLNILEPETYKELFKKIDEDFDR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   76 VDIVINNA---GYGLVGEFESYnieemhrqMNVNFWGVAYI-----------TKEALNLMRESGkGGRILQISSVAGYYP 141
Cdd:PRK08416  88 VDFFISNAiisGRAVVGGYTKF--------MRLKPKGLNNIytatvnafvvgAQEAAKRMEKVG-GGSIISLSSTGNLVY 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19075741  142 SPCLSMYNASKFAVEGLSQTIMRELDpNWNIAITIVQPGGMQTE 185
Cdd:PRK08416 159 IENYAGHGTSKAAVETMVKYAATELG-EKNIRVNAVSGGPIDTD 201
Gne_like_SDR_e cd05238
Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; ...
 7-158 2.26e-04

Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs; Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187549 [Multi-domain]  Cd Length: 305  Bit Score: 41.99  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQG--YNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKdakrrfGNVDIVINNAG 84
Cdd:cd05238   2 KVLITGASGFVGQRLAERLLSDVpnERLILIDVVSPKAPSGAPRVTQIAGDLAVPALIEALAN------GRPDVVFHLAA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  85 Y---GLVGEFESYnieemhrqMNVNFWGVAYItkeaLNLMRESGKGGRILQISSVAGYYPSPC-----------LSMYNA 150
Cdd:cd05238  76 IvsgGAEADFDLG--------YRVNVDGTRNL----LEALRKNGPKPRFVFTSSLAVYGLPLPnpvtdhtaldpASSYGA 143


                ....*...
gi 19075741 151 SKFAVEGL 158
Cdd:cd05238 144 QKAMCELL 151
PLN02240 PLN02240
UDP-glucose 4-epimerase
 1-174 2.64e-04

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 41.87  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFSTVLITGsskGLGYA---LVKVGLAQGYNVI-------ACSRAPD---TITIEHSKLLKL-KLDVTDVKSVETAF 66
Cdd:PLN02240   1 MSLMGRTILVTG---GAGYIgshTVLQLLLAGYKVVvidnldnSSEEALRrvkELAGDLGDNLVFhKVDLRDKEALEKVF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   67 kdAKRRFgnvDIVINNAGYGLVGEfesyNIEEMHRQMNVNFWGvayiTKEALNLMREsgKGGRILQISSVAGYY--P--S 142
Cdd:PLN02240  78 --ASTRF---DAVIHFAGLKAVGE----SVAKPLLYYDNNLVG----TINLLEVMAK--HGCKKLVFSSSATVYgqPeeV 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 19075741  143 PC--------LSMYNASKFAVEGlsqtIMREL---DPNWNIAI 174
Cdd:PLN02240 143 PCteefplsaTNPYGRTKLFIEE----ICRDIhasDPEWKIIL 181
NAD_binding_10 pfam13460
NAD(P)H-binding;
12-84 3.31e-04

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 40.67  E-value: 3.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075741    12 GSSKGLGYALVKVGLAQGYNVIACSRAPDTIT--IEHSKLLKLKLDVTDVKSVETAFKDakrrfgnVDIVINNAG 84
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLAdlEDHPGVEVVDGDVLDPDDLAEALAG-------QDAVISALG 68
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-84 4.31e-04

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


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 41.15  E-value: 4.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   6 STVLITGSSkGLGYALVKVGLAQGYNVIACSRAPDTItiehSKLLKLKLDVTdVKSVETAFKDAKRRFGN--VDIVINNA 83
Cdd:cd05188 136 DTVLVLGAG-GVGLLAAQLAKAAGARVIVTDRSDEKL----ELAKELGADHV-IDYKEEDLEEELRLTGGggADVVIDAV 209


                .
gi 19075741  84 G 84
Cdd:cd05188 210 G 210
PRK06483 PRK06483
dihydromonapterin reductase; Provisional
 6-39 5.86e-04

dihydromonapterin reductase; Provisional


Pssm-ID: 180586 [Multi-domain]  Cd Length: 236  Bit Score: 40.30  E-value: 5.86e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 19075741    6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAP 39
Cdd:PRK06483   3 APILITGAGQRIGLALAWHLLAQGQPVIVSYRTH 36
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 1-165 6.64e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 40.62  E-value: 6.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFSTVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITiEHSKLLKLKLDVTDVKSVETAF--------KDAKRR 72
Cdd:PLN02780  49 LKKYGSWALVTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLK-DVSDSIQSKYSKTQIKTVVVDFsgdidegvKRIKET 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   73 FGNVD--IVINNAG--YGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKGGRILQISSVAGYYPS-PCLSM 147
Cdd:PLN02780 128 IEGLDvgVLINNVGvsYPYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSdPLYAV 207

                        170
                 ....*....|....*...
gi 19075741  148 YNASKFAVEGLSQTIMRE 165
Cdd:PLN02780 208 YAATKAYIDQFSRCLYVE 225
PRK09009 PRK09009
SDR family oxidoreductase;
8-84 7.90e-04

SDR family oxidoreductase;


Pssm-ID: 181609 [Multi-domain]  Cd Length: 235  Bit Score: 40.05  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    8 VLITGSSKGLGYALVKVGLAQ--GYNVIA--CSRAPDTitiEHSKLLKLKLDVTDvksvETAFKDAKRRFGNVDIVINNA 83
Cdd:PRK09009   3 ILIVGGSGGIGKAMVKQLLERypDATVHAtyRHHKPDF---QHDNVQWHALDVTD----EAEIKQLSEQFTQLDWLINCV 75


                 .
gi 19075741   84 G 84
Cdd:PRK09009  76 G 76
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 7-205 8.29e-04

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 40.41  E-value: 8.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPdtITIEHSKLLKLKLDVtdvksveTAFKDAkrrFGNVDIVINNAGYG 86
Cdd:cd05232   1 KVLVTGANGFIGRALVDKLLSRGEEVRIAVRNA--ENAEPSVVLAELPDI-------DSFTDL---FLGVDAVVHLAARV 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  87 LVGEFESYNIEEMHRQMNvnfwgvayiTKEALNLMRESGKGG--RILQISSVAGY------YP----SPCL--SMYNASK 152
Cdd:cd05232  69 HVMNDQGADPLSDYRKVN---------TELTRRLARAAARQGvkRFVFLSSVKVNgegtvgAPfdetDPPApqDAYGRSK 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075741 153 FAVEglsqTIMRELDPNWNIAITIVQP-----GGMQTEWASSnMQWAKPHP-----AYENDRS 205
Cdd:cd05232 140 LEAE----RALLELGASDGMEVVILRPpmvygPGVRGNFARL-MRLIDRGLplppgAVKNRRS 197
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 74-179 1.29e-03

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 39.48  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  74 GNVDIVINNAGYG-LVGEFESYNIEEMHRQMN-VNFWGVAyITKEALNLMRESgKGGRILQISSVAGYYPSPCLSMYNAS 151
Cdd:cd05361  71 GAIDVLVSNDYIPrPMNPIDGTSEADIRQAFEaLSIFPFA-LLQAAIAQMKKA-GGGSIIFITSAVPKKPLAYNSLYGPA 148

                        90       100
                ....*....|....*....|....*...
gi 19075741 152 KFAVEGLSQTIMRELDPNwNIAITIVQP 179
Cdd:cd05361 149 RAAAVALAESLAKELSRD-NILVYAIGP 175
PRK07424 PRK07424
bifunctional sterol desaturase/short chain dehydrogenase; Validated
 7-84 1.69e-03

bifunctional sterol desaturase/short chain dehydrogenase; Validated


Pssm-ID: 236016 [Multi-domain]  Cd Length: 406  Bit Score: 39.68  E-value: 1.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075741    7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIE-HSKLLKLKLDVTDVKSvETAFKDAKRRfgnVDIVINNAG 84
Cdd:PRK07424 180 TVAVTGASGTLGQALLKELHQQGAKVVALTSNSDKITLEiNGEDLPVKTLHWQVGQ-EAALAELLEK---VDILIINHG 254
PRK09134 PRK09134
SDR family oxidoreductase;
1-83 2.06e-03

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 38.76  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    1 MKSTFSTVLITGSSKGLGYALVkVGLA-QGYNV-IACSRAPD-------TITIEHSKLLKLKLDVTDVKSVETAFKDAKR 71
Cdd:PRK09134   5 SMAAPRAALVTGAARRIGRAIA-LDLAaHGFDVaVHYNRSRDeaealaaEIRALGRRAVALQADLADEAEVRALVARASA 83

                         90
                 ....*....|..
gi 19075741   72 RFGNVDIVINNA 83
Cdd:PRK09134  84 ALGPITLLVNNA 95
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 7-84 2.41e-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: 38.23  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741      7 TVLITGSSKGLGYALVKVgLAQGY--NVIACSR--APDTITIEHSKLLKLKL--------DVTDVKSVETAFKDAKRRFG 74
Cdd:smart00822   2 TYLITGGLGGLGRALARW-LAERGarRLVLLSRsgPDAPGAAALLAELEAAGarvtvvacDVADRDALAAVLAAIPAVEG 80

                           90
                   ....*....|
gi 19075741     75 NVDIVINNAG 84
Cdd:smart00822  81 PLTGVIHAAG 90
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 7-84 2.56e-03

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


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 38.98  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTitieHSKLLKLKLDVTdVKSVETAFKDAKRRFGN---VDIVINNA 83
Cdd:COG0604 142 TVLVHGAAGGVGSAAVQLAKALGARVIATASSPEK----AELLRALGADHV-IDYREEDFAERVRALTGgrgVDVVLDTV 216


                .
gi 19075741  84 G 84
Cdd:COG0604 217 G 217
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 7-182 2.64e-03

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


Pssm-ID: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 38.73  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVI-AC---SRAPDTITI-----EHSKLLKLKLDVTDVKSVETAFKDAKRRFGNVD 77
Cdd:cd09809   3 VIIITGANSGIGFETARSFALHGAHVIlACrnmSRASAAVSRileewHKARVEAMTLDLASLRSVQRFAEAFKAKNSPLH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  78 IVINNAgyGLVGEFESYNIEEMHRQMNVNFWGVAYITKEALNLMRESGKgGRILQISSVAGYY----------------P 141
Cdd:cd09809  83 VLVCNA--AVFALPWTLTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAP-ARVIVVSSESHRFtdlpdscgnldfsllsP 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19075741 142 SP----CLSMYNASKFAVEGLSQTIMRELDPNwNIAITIVQPGGM 182
Cdd:cd09809 160 PKkkywSMLAYNRAKLCNILFSNELHRRLSPR-GITSNSLHPGNM 203
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
 8-164 3.05e-03

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 38.45  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   8 VLITGSSKGLGYALVKVGLAQGYNVIACSRAPDTITIEHSKLLKLKLDVTDVKSVETAFKDAkrrfgnvDIVINNAGYGL 87
Cdd:cd05264   2 VLIVGGNGFIGSHLVDALLEEGPQVRVFDRSIPPYELPLGGVDYIKGDYENRADLESALVGI-------DTVIHLASTTN 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741  88 VGEFESYNIEEMhrQMNVNFwgvayiTKEALNLMRESGKGGRILqISSVAGYY-------------PSPcLSMYNASKFA 154
Cdd:cd05264  75 PATSNKNPILDI--QTNVAP------TVQLLEACAAAGIGKIIF-ASSGGTVYgvpeqlpisesdpTLP-ISSYGISKLA 144

                       170       180
                ....*....|....*....|
gi 19075741 155 VE----------GLSQTIMR 164
Cdd:cd05264 145 IEkylrlyqylyGLDYTVLR 164
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
 7-122 4.26e-03

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 37.16  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741     7 TVLITGSSKGLGYALVKVGLAQG-YNVIACSR--APDTITIEHSKLLK--------LKLDVTDVKSVETAFKDAKRRFGN 75
Cdd:pfam08659   2 TYLITGGLGGLGRELARWLAERGaRHLVLLSRsaAPRPDAQALIAELEargvevvvVACDVSDPDAVAALLAEIKAEGPP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 19075741    76 VDIVINNAGYGLVGEFESYNIEEMHRQMNVNFWGvayitkeALNLMR 122
Cdd:pfam08659  82 IRGVIHAAGVLRDALLENMTDEDWRRVLAPKVTG-------TWNLHE 121
PRK07102 PRK07102
SDR family oxidoreductase;
6-158 6.17e-03

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 37.21  E-value: 6.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741    6 STVLITGSSKGLGYALVKVGLAQGYNVIACSRAPDT-------ITIEHSKLLKL-KLDVTDVKSVETAFKDAKRRFgnvD 77
Cdd:PRK07102   2 KKILIIGATSDIARACARRYAAAGARLYLAARDVERlerladdLRARGAVAVSThELDILDTASHAAFLDSLPALP---D 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   78 IVInnAGYGLVGEFES--YNIEEMHRQMNVNFWGVAYITKEALNLMrESGKGGRILQISSVAGYYPSPCLSMYNASKFAV 155
Cdd:PRK07102  79 IVL--IAVGTLGDQAAceADPALALREFRTNFEGPIALLTLLANRF-EARGSGTIVGISSVAGDRGRASNYVYGSAKAAL 155


                 ....*..
gi 19075741  156 ----EGL 158
Cdd:PRK07102 156 taflSGL 162
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
 7-80 6.90e-03

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 37.63  E-value: 6.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075741   7 TVLITGSSKGLGYALVKVGLAQGYNVIACSRAPD-TITIEH-----SKLLKLKLDVTDVKSVETAFKDAKRrfgNVDIVI 80
Cdd:cd05227   1 LVLVTGATGFIASHIVEQLLKAGYKVRGTVRSLSkSAKLKAllkaaGYNDRLEFVIVDDLTAPNAWDEALK---GVDYVI 77
 
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