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Conserved domains on  [gi|446410605|ref|WP_000488460|]
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ketopantoate reductase family protein [Leptospira interrogans]

Protein Classification

ketopantoate reductase family protein( domain architecture ID 11449024)

ketopantoate reductase family protein similar to 2-dehydropantoate 2-reductase, which catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid

EC:  1.-.-.-
Gene Ontology:  GO:0016491
SCOP:  4000112

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
3-304 5.03e-78

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 239.76  E-value: 5.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   3 RILVLGSGAIAGLYAGKLVQAGCKVDFWVRKNSYE-LKRNGFQIESaPWGNFHYKVEKIFESiPKNLKEYDLILNCLKC- 80
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEaLRENGLRLES-PDGDRTTVPVPAVTD-PEELGPADLVLVAVKAy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  81 -LPDI--NLKKILGEKIPlnlpilllqnGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNRNSS 157
Cdd:COG1893   80 dLEAAaeALAPLLGPDTVvls----lqnGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 158 FICDQLVNLFNSVGVPTQNTNTIRQARWKKLMWNAPFNPISVLCGGKNTlEILENPHSCKLVIEIMKEVQTLSKLDGAEV 237
Cdd:COG1893  156 ERLEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNG-ELLADPEARALARALMREVLAVARAEGVPL 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410605 238 PSTQID-IFLQMTKTMKPYKTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYES 304
Cdd:COG1893  235 PEDDLEeRVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEA 302
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
3-304 5.03e-78

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 239.76  E-value: 5.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   3 RILVLGSGAIAGLYAGKLVQAGCKVDFWVRKNSYE-LKRNGFQIESaPWGNFHYKVEKIFESiPKNLKEYDLILNCLKC- 80
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEaLRENGLRLES-PDGDRTTVPVPAVTD-PEELGPADLVLVAVKAy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  81 -LPDI--NLKKILGEKIPlnlpilllqnGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNRNSS 157
Cdd:COG1893   80 dLEAAaeALAPLLGPDTVvls----lqnGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 158 FICDQLVNLFNSVGVPTQNTNTIRQARWKKLMWNAPFNPISVLCGGKNTlEILENPHSCKLVIEIMKEVQTLSKLDGAEV 237
Cdd:COG1893  156 ERLEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNG-ELLADPEARALARALMREVLAVARAEGVPL 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410605 238 PSTQID-IFLQMTKTMKPYKTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYES 304
Cdd:COG1893  235 PEDDLEeRVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEA 302
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
3-299 9.37e-65

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 205.97  E-value: 9.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   3 RILVLGSGAIAGLYAGKLVQAGCKVDFWVRKNSYELKRNGFQIESApWGNFHYKVEKIF---ESIPKnlkeYDLILNCLK 79
Cdd:PRK06249   7 RIGIIGTGAIGGFYGAMLARAGFDVHFLLRSDYEAVRENGLQVDSV-HGDFHLPPVQAYrsaEDMPP----CDWVLVGLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  80 CLPDINLKKILGEKIPLNLPILLLQNGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNRNSSF- 158
Cdd:PRK06249  82 TTANALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAEHLLGGLCFICSNRVGPGVIHHLAYGRVNLGYHSGPAADd 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 159 ----ICDQLVNLFNSVGVPTQNTNTIRQARWKKLMWNAPFNPISVLCGgKNTLEILENPHSCKLVIEIMKEVQTLSKLDG 234
Cdd:PRK06249 162 gitaRVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLN-ASTDPLMADPDSRALIRALMAEVIQGAAACG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410605 235 AEVPSTQIDIFLQMTKTMKPYKTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLL 299
Cdd:PRK06249 241 HTLPEGYADHMLAVTERMPDYRPSMYHDFEEGRPLELEAIYANPLAAARAAGCAMPRVEMLYQAL 305
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
11-304 1.50e-64

2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate 2-reductase, one of four enzymes required for the de novo biosynthesis of pantothenate (vitamin B5) from Asp and 2-oxoisovalerate. Although few members of the seed alignment are characterized experimentally, nearly all from complete genomes are found in a genome-wide (but not local) context of all three other pantothenate-biosynthetic enzymes (TIGR00222, TIGR00018, TIGR00223). The gene encoding this enzyme is designated apbA in Salmonella typhimurium and panE in Escherichia coli; this protein functions as a monomer and functions in the alternative pyrimidine biosynthetic, or APB, pathway, used to synthesize the pyrimidine moiety of thiamine. Note, synthesis of the pyrimidine moiety of thiamine occurs either via the first five steps in de novo purine biosynthesis, which uses the pur gene products, or through the APB pathway. Note that this family includes both NADH and NADPH-dependent enzymes, and enzymes with broad specificity, such as a D-mandelate dehydrogease that is also a 2-dehydropantoate 2-reductase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273247 [Multi-domain]  Cd Length: 293  Bit Score: 204.84  E-value: 1.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   11 AIAGLYAGKLVQAGCKVDFWVRKNSYE-LKRNGFQIESaPWGNFHYKVEKIFESiPKNLKEYDLILNCLKCLPDINLKKI 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEaLNQEGLRIVS-LGGEFQFRPVSAATS-PEELPPADLVIITVKAYQTEEAAAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   90 LGEKIPLNLPILLLQNGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNRNSSFIcDQLVNLFNS 169
Cdd:TIGR00745  79 LLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGDYVGENEAV-EALAELLNE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  170 VGVPTQNTNTIRQARWKKLMWNAPFNPISVLCGGKNTlEILENPHSCKLVIEIMKEVQTLSKLDGAEVPSTQIDIFLQMT 249
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNG-ELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAV 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446410605  250 KTMKPY-KTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYES 304
Cdd:TIGR00745 237 IRMTAEnTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEA 292
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
180-303 7.73e-35

Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 462514 [Multi-domain]  Cd Length: 125  Bit Score: 122.72  E-value: 7.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  180 IRQARWKKLMWNAPFNPISVLCGGKNTlEILENPHSCKLVIEIMKEVQTLSKLDGAEVPSTQI-DIFLQMTKTMKPYKTS 258
Cdd:pfam08546   2 IRLARWEKLLVNAAINPLTALTGCTNG-ELLDSPEARALIRALMREAVAVAQAEGVALSEDRLiEYVLAVLRKTPDNKSS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 446410605  259 MLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYE 303
Cdd:pfam08546  81 MLQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
3-304 5.03e-78

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 239.76  E-value: 5.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   3 RILVLGSGAIAGLYAGKLVQAGCKVDFWVRKNSYE-LKRNGFQIESaPWGNFHYKVEKIFESiPKNLKEYDLILNCLKC- 80
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEaLRENGLRLES-PDGDRTTVPVPAVTD-PEELGPADLVLVAVKAy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  81 -LPDI--NLKKILGEKIPlnlpilllqnGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNRNSS 157
Cdd:COG1893   80 dLEAAaeALAPLLGPDTVvls----lqnGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 158 FICDQLVNLFNSVGVPTQNTNTIRQARWKKLMWNAPFNPISVLCGGKNTlEILENPHSCKLVIEIMKEVQTLSKLDGAEV 237
Cdd:COG1893  156 ERLEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNG-ELLADPEARALARALMREVLAVARAEGVPL 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410605 238 PSTQID-IFLQMTKTMKPYKTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYES 304
Cdd:COG1893  235 PEDDLEeRVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEA 302
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
3-299 9.37e-65

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 205.97  E-value: 9.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   3 RILVLGSGAIAGLYAGKLVQAGCKVDFWVRKNSYELKRNGFQIESApWGNFHYKVEKIF---ESIPKnlkeYDLILNCLK 79
Cdd:PRK06249   7 RIGIIGTGAIGGFYGAMLARAGFDVHFLLRSDYEAVRENGLQVDSV-HGDFHLPPVQAYrsaEDMPP----CDWVLVGLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  80 CLPDINLKKILGEKIPLNLPILLLQNGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNRNSSF- 158
Cdd:PRK06249  82 TTANALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAEHLLGGLCFICSNRVGPGVIHHLAYGRVNLGYHSGPAADd 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 159 ----ICDQLVNLFNSVGVPTQNTNTIRQARWKKLMWNAPFNPISVLCGgKNTLEILENPHSCKLVIEIMKEVQTLSKLDG 234
Cdd:PRK06249 162 gitaRVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLN-ASTDPLMADPDSRALIRALMAEVIQGAAACG 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410605 235 AEVPSTQIDIFLQMTKTMKPYKTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLL 299
Cdd:PRK06249 241 HTLPEGYADHMLAVTERMPDYRPSMYHDFEEGRPLELEAIYANPLAAARAAGCAMPRVEMLYQAL 305
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
11-304 1.50e-64

2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate 2-reductase, one of four enzymes required for the de novo biosynthesis of pantothenate (vitamin B5) from Asp and 2-oxoisovalerate. Although few members of the seed alignment are characterized experimentally, nearly all from complete genomes are found in a genome-wide (but not local) context of all three other pantothenate-biosynthetic enzymes (TIGR00222, TIGR00018, TIGR00223). The gene encoding this enzyme is designated apbA in Salmonella typhimurium and panE in Escherichia coli; this protein functions as a monomer and functions in the alternative pyrimidine biosynthetic, or APB, pathway, used to synthesize the pyrimidine moiety of thiamine. Note, synthesis of the pyrimidine moiety of thiamine occurs either via the first five steps in de novo purine biosynthesis, which uses the pur gene products, or through the APB pathway. Note that this family includes both NADH and NADPH-dependent enzymes, and enzymes with broad specificity, such as a D-mandelate dehydrogease that is also a 2-dehydropantoate 2-reductase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273247 [Multi-domain]  Cd Length: 293  Bit Score: 204.84  E-value: 1.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   11 AIAGLYAGKLVQAGCKVDFWVRKNSYE-LKRNGFQIESaPWGNFHYKVEKIFESiPKNLKEYDLILNCLKCLPDINLKKI 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEaLNQEGLRIVS-LGGEFQFRPVSAATS-PEELPPADLVIITVKAYQTEEAAAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   90 LGEKIPLNLPILLLQNGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNRNSSFIcDQLVNLFNS 169
Cdd:TIGR00745  79 LLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGDYVGENEAV-EALAELLNE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  170 VGVPTQNTNTIRQARWKKLMWNAPFNPISVLCGGKNTlEILENPHSCKLVIEIMKEVQTLSKLDGAEVPSTQIDIFLQMT 249
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNG-ELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAV 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446410605  250 KTMKPY-KTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYES 304
Cdd:TIGR00745 237 IRMTAEnTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEA 292
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
3-304 2.08e-51

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 171.19  E-value: 2.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   3 RILVLGSGAIAGLYAGKLVQAGCKVDFWVR--KNSYELKRNGFQIESAPWGNFHYKVEKifesiPKNLKEYDLILNCLK- 79
Cdd:PRK06522   2 KIAILGAGAIGGLFGAALAQAGHDVTLVARrgAHLDALNENGLRLEDGEITVPVLAADD-----PAELGPQDLVILAVKa 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  80 -----CLPDinLKKILGEKIPLNLPILllqnGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNR 154
Cdd:PRK06522  77 yqlpaALPS--LAPLLGPDTPVLFLQN----GVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEPDG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 155 NSSFiCDQLVNLFNSVGVPTQNTNTIRQARWKKLMWNAPFNPISVLCGGKNTlEILENPHSCKLVIEIMKEVQTLSKLDG 234
Cdd:PRK06522 151 ESAA-AEALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNG-ELLADPDYRALIRALMEEVAAVAEAEG 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410605 235 AEVP-STQIDIFLQMTKTMKPYKTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYES 304
Cdd:PRK06522 229 VHLSvEEVREYVRQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKES 299
PRK12921 PRK12921
oxidoreductase;
3-303 1.38e-37

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 135.37  E-value: 1.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   3 RILVLGSGAIAGLYAGKLVQAGCKVDFWVR-KNSYELKRNGFQIESAPwGNFHYKVEKIfeSIPKNLKE-YDLILNCLK- 79
Cdd:PRK12921   2 RIAVVGAGAVGGTFGGRLLEAGRDVTFLVRpKRAKALRERGLVIRSDH-GDAVVPGPVI--TDPEELTGpFDLVILAVKa 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  80 -----CLPDInlKKILGEKIPLNLPILllqnGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIGSWNR 154
Cdd:PRK12921  79 yqldaAIPDL--KPLVGEDTVIIPLQN----GIGQLEQLEPYFGRERVLGGVVFISAQLNGDGVVVQRADHRLTFGEIPG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 155 NSSFICDQLVNLFNSVGVPTQNTNTIRQARWKKLMWNAPFNPISVLcGGKNTLEILENPHSCKLVIEIMKEVQTLSKLDG 234
Cdd:PRK12921 153 QRSERTRAVRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTAL-GRATVGGILSRPGGRDLARALLRECLAVARAEG 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410605 235 A----EVPSTQIDIFLQMTKTMKpykTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYE 303
Cdd:PRK12921 232 AplrdDVVEEIVKIFAGAPGDMK---TSMLRDMEKGRPLEIDHLQGVLLRRARAHGIPTPILDTVYALLKAYE 301
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
180-303 7.73e-35

Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 462514 [Multi-domain]  Cd Length: 125  Bit Score: 122.72  E-value: 7.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  180 IRQARWKKLMWNAPFNPISVLCGGKNTlEILENPHSCKLVIEIMKEVQTLSKLDGAEVPSTQI-DIFLQMTKTMKPYKTS 258
Cdd:pfam08546   2 IRLARWEKLLVNAAINPLTALTGCTNG-ELLDSPEARALIRALMREAVAVAQAEGVALSEDRLiEYVLAVLRKTPDNKSS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 446410605  259 MLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTIYSLLNLYE 303
Cdd:pfam08546  81 MLQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
4-150 2.58e-30

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 111.55  E-value: 2.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605    4 ILVLGSGAIAGLYAGKLVQAGCKVDFWVRKNSYE-LKRNGFQIESaPWGNFHYKVEKIFESiPKNLKEYDLILNCLKCLP 82
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAaIKKNGLRLTS-PGGERIVPPPAVTSA-SESLGPIDLVIVTVKAYQ 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410605   83 DIN----LKKILGEKIPLNLPILllqnGIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGELTIG 150
Cdd:pfam02558  79 TEEaledIAPLLGPNTVVLLLQN----GLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITIG 146
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
106-295 6.34e-08

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 53.18  E-value: 6.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 106 GIGIEEPVSILYPENEILSGLAFVCANRLDAGKILHLDYGEltigSWNRNSSFICDQ-LVNLFNSVGVPTQNTNTIRQAR 184
Cdd:PRK05708 106 GLGSQDAVAARVPHARCIFASSTEGAFRDGDWRVVFAGHGF----TWLGDPRNPTAPaWLDDLREAGIPHEWTVDILTRL 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 185 WKKLMWNAPFNPISVLCGGKNTlEILEnpHSCklvieimkEVQTL----SKL-----DGAEVPSTQIDIFLQMTKTMKPY 255
Cdd:PRK05708 182 WRKLALNCAINPLTVLHDCRNG-GLLE--HAQ--------EVAALcaelSELlrrcgQPAAAANLHEEVQRVIQATAANY 250
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446410605 256 kTSMLLDFEAGRPMEIEAILGNTIRIAEKNNLEIPHIQTI 295
Cdd:PRK05708 251 -SSMYQDVRAGRRTEISYLLGYACRAADRHGLPLPRLQHL 289
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
1-284 4.87e-04

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 41.14  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605   1 MFRILVLGSGAIAGLYAGKLVQAGCKVDFWVR-KNSYELKRNGFQIESapWGNFHYKVEK---IFESIPKNLKEYDLILN 76
Cdd:PRK08229   2 MARICVLGAGSIGCYLGGRLAAAGADVTLIGRaRIGDELRAHGLTLTD--YRGRDVRVPPsaiAFSTDPAALATADLVLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605  77 CLKCLPDINLKKILGEKIPLNLPILLLQNGIGIEEPVSILYPENEILSGL-----------AFVCANRldagkilhldyG 145
Cdd:PRK08229  80 TVKSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMvpfnvisrgpgAFHQGTS-----------G 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410605 146 ELTIGswnrnSSFICDQLVNLFNSVGVPTQNTNTIRQARWKKLMWNAPfNPISVLCGgkNTL-EILENPHSCKLVIEIMK 224
Cdd:PRK08229 149 ALAIE-----ASPALRPFAAAFARAGLPLVTHEDMRAVQWAKLLLNLN-NAVNALSG--LPLkEELAQRSYRRCLALAQR 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410605 225 EVQTLSKLDG------AEVPSTQIDIFLQM---------TKTMK--PY-KTSMLLDFEAGRPMEIEAILGNTIRIAEK 284
Cdd:PRK08229 221 EALRVLKAAGirparlTPLPPAWIPRLLRLpdplfrrlaGRMLAidPLaRSSMSDDLAAGRATEIDWINGEIVRLAGR 298
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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