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Conserved domains on  [gi|2790394528|ref|WP_371110949|]
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ketopantoate reductase family protein [Rhizobium sp. RCC_161_2]

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 ...
3-313 8.81e-50

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: 168.50  E-value: 8.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   3 RYIIVGAGAVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSG-VQQIRLNAFDifDPPELTPGDILLLTVKSQ 81
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGdRTTVPVPAVT--DPEELGPADLVLVAVKAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  82 DAANALASWswRPVsdcgdtAAARLPVVTFQNGLATEAIALRTF--AKVYGASILTPARFTETGKVAVAGdpqVGVVTIG 159
Cdd:COG1893    80 DLEAAAEAL--APL------LGPDTVVLSLQNGLGHEERLAEALgaERVLGGVVTIGATREEPGVVRHTG---GGRLVLG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 160 RFPTGSDETAEQIAADLDRANYLAETSNDIRRWKSLKL-----------LHNVRNAlELFDgDDDLRAsVAEALVNEARC 228
Cdd:COG1893   149 ELDGGPSERLEALAELLEAAGIPVEVSDDIRGALWEKLllnaainpltaLTGAPNG-ELLA-DPEARA-LARALMREVLA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 229 ALEAAGYNFASASERAldisgwRIAQNSGIHPGQQ-STWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAVQNIAGR 307
Cdd:COG1893   226 VARAEGVPLPEDDLEE------RVAAVAEATADNRsSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKA 299

                  ....*.
gi 2790394528 308 LEHEGG 313
Cdd:COG1893   300 LEAGRA 305
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
3-313 8.81e-50

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: 168.50  E-value: 8.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   3 RYIIVGAGAVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSG-VQQIRLNAFDifDPPELTPGDILLLTVKSQ 81
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGdRTTVPVPAVT--DPEELGPADLVLVAVKAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  82 DAANALASWswRPVsdcgdtAAARLPVVTFQNGLATEAIALRTF--AKVYGASILTPARFTETGKVAVAGdpqVGVVTIG 159
Cdd:COG1893    80 DLEAAAEAL--APL------LGPDTVVLSLQNGLGHEERLAEALgaERVLGGVVTIGATREEPGVVRHTG---GGRLVLG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 160 RFPTGSDETAEQIAADLDRANYLAETSNDIRRWKSLKL-----------LHNVRNAlELFDgDDDLRAsVAEALVNEARC 228
Cdd:COG1893   149 ELDGGPSERLEALAELLEAAGIPVEVSDDIRGALWEKLllnaainpltaLTGAPNG-ELLA-DPEARA-LARALMREVLA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 229 ALEAAGYNFASASERAldisgwRIAQNSGIHPGQQ-STWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAVQNIAGR 307
Cdd:COG1893   226 VARAEGVPLPEDDLEE------RVAAVAEATADNRsSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKA 299

                  ....*.
gi 2790394528 308 LEHEGG 313
Cdd:COG1893   300 LEAGRA 305
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
6-314 6.47e-30

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 115.72  E-value: 6.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   6 IVGAGAVGASLAAQFELAGVGYALVGR-GAQISQIKRHGLSyqRPSGVQQIRLNAFDifDPPELTPGDILLLTVKSQDAA 84
Cdd:PRK06522    5 ILGAGAIGGLFGAALAQAGHDVTLVARrGAHLDALNENGLR--LEDGEITVPVLAAD--DPAELGPQDLVILAVKAYQLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  85 NALASWswRPVSDcGDTaaarlPVVTFQNGLATEAIALRTFAK--VYGAsILTPARFTET-GKVAVAGDpqvGVVTIGRF 161
Cdd:PRK06522   81 AALPSL--APLLG-PDT-----PVLFLQNGVGHLEELAAYIGPerVLGG-VVTHAAELEGpGVVRHTGG---GRLKIGEP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 162 PtGSDETAEQIAADLDRANYLAETSNDIRRWKSLKL-----------LHNVRNAlELFDgDDDLRAsVAEALVNEARCAL 230
Cdd:PRK06522  149 D-GESAAAEALADLLNAAGLDVEWSPDIRTEIWRKLwvncvinpltaLLGCTNG-ELLA-DPDYRA-LIRALMEEVAAVA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 231 EAAGYNFASasERALDISGWRIAQNSGIHPgqqSTWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAVQNIAGRLEH 310
Cdd:PRK06522  225 EAEGVHLSV--EEVREYVRQVIQKTAANTS---SMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKES 299

                  ....
gi 2790394528 311 EGGV 314
Cdd:PRK06522  300 ERGL 303
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
11-301 4.20e-29

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: 113.55  E-value: 4.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  11 AVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSG-VQQIRLNAFDifDPPELTPGDILLLTVKSQDAANALAS 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLGGeFQFRPVSAAT--SPEELPPADLVIITVKAYQTEEAAAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  90 WswRPVsdcgdtAAARLPVVTFQNGLATEAIALRTFA--KVYGASILTPARFTETGKVAVAGdpqVGVVTIGRFPtGSDE 167
Cdd:TIGR00745  79 L--LPL------IGKNTKVLFLQNGLGHEERLRELLParRILGGVVTHGAVREEPGVVHHAG---LGATKIGDYV-GENE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 168 TAEQIAADLDRANYLAETSNDIRRWKSLKL-----------LHNVRNAlELFDgDDDLRAsVAEALVNEARCALEAAGYN 236
Cdd:TIGR00745 147 AVEALAELLNEAGIPAELHGDILAAIWKKLlvnaainpltaLLDCKNG-ELLE-NPEARE-LLRRLMDEVVRVARAEGVD 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790394528 237 FA--SASERALDIsgwrIAQNSGIHPgqqSTWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAV 301
Cdd:TIGR00745 224 LPddEVEELVRAV----IRMTAENTS---SMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTL 283
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
6-159 4.50e-18

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: 79.58  E-value: 4.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   6 IVGAGAVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSGVQQIRLNAFdIFDPPELTPGDILLLTVKSQDAAN 85
Cdd:pfam02558   3 ILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLRLTSPGGERIVPPPAV-TSASESLGPIDLVIVTVKAYQTEE 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790394528  86 ALAswswrpvsDCGDTAAARLPVVTFQNGLATEAIALRTF--AKVYGASILTPARFTETGKVAVAGDpqvGVVTIG 159
Cdd:pfam02558  82 ALE--------DIAPLLGPNTVVLLLQNGLGHEEVLREAVprERVLGGVTTHGAFREGPGHVHHAGP---GRITIG 146
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
3-313 8.81e-50

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: 168.50  E-value: 8.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   3 RYIIVGAGAVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSG-VQQIRLNAFDifDPPELTPGDILLLTVKSQ 81
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGdRTTVPVPAVT--DPEELGPADLVLVAVKAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  82 DAANALASWswRPVsdcgdtAAARLPVVTFQNGLATEAIALRTF--AKVYGASILTPARFTETGKVAVAGdpqVGVVTIG 159
Cdd:COG1893    80 DLEAAAEAL--APL------LGPDTVVLSLQNGLGHEERLAEALgaERVLGGVVTIGATREEPGVVRHTG---GGRLVLG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 160 RFPTGSDETAEQIAADLDRANYLAETSNDIRRWKSLKL-----------LHNVRNAlELFDgDDDLRAsVAEALVNEARC 228
Cdd:COG1893   149 ELDGGPSERLEALAELLEAAGIPVEVSDDIRGALWEKLllnaainpltaLTGAPNG-ELLA-DPEARA-LARALMREVLA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 229 ALEAAGYNFASASERAldisgwRIAQNSGIHPGQQ-STWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAVQNIAGR 307
Cdd:COG1893   226 VARAEGVPLPEDDLEE------RVAAVAEATADNRsSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKA 299

                  ....*.
gi 2790394528 308 LEHEGG 313
Cdd:COG1893   300 LEAGRA 305
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
6-314 6.47e-30

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 115.72  E-value: 6.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   6 IVGAGAVGASLAAQFELAGVGYALVGR-GAQISQIKRHGLSyqRPSGVQQIRLNAFDifDPPELTPGDILLLTVKSQDAA 84
Cdd:PRK06522    5 ILGAGAIGGLFGAALAQAGHDVTLVARrGAHLDALNENGLR--LEDGEITVPVLAAD--DPAELGPQDLVILAVKAYQLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  85 NALASWswRPVSDcGDTaaarlPVVTFQNGLATEAIALRTFAK--VYGAsILTPARFTET-GKVAVAGDpqvGVVTIGRF 161
Cdd:PRK06522   81 AALPSL--APLLG-PDT-----PVLFLQNGVGHLEELAAYIGPerVLGG-VVTHAAELEGpGVVRHTGG---GRLKIGEP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 162 PtGSDETAEQIAADLDRANYLAETSNDIRRWKSLKL-----------LHNVRNAlELFDgDDDLRAsVAEALVNEARCAL 230
Cdd:PRK06522  149 D-GESAAAEALADLLNAAGLDVEWSPDIRTEIWRKLwvncvinpltaLLGCTNG-ELLA-DPDYRA-LIRALMEEVAAVA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 231 EAAGYNFASasERALDISGWRIAQNSGIHPgqqSTWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAVQNIAGRLEH 310
Cdd:PRK06522  225 EAEGVHLSV--EEVREYVRQVIQKTAANTS---SMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKES 299

                  ....
gi 2790394528 311 EGGV 314
Cdd:PRK06522  300 ERGL 303
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
11-301 4.20e-29

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: 113.55  E-value: 4.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  11 AVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSG-VQQIRLNAFDifDPPELTPGDILLLTVKSQDAANALAS 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLGGeFQFRPVSAAT--SPEELPPADLVIITVKAYQTEEAAAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  90 WswRPVsdcgdtAAARLPVVTFQNGLATEAIALRTFA--KVYGASILTPARFTETGKVAVAGdpqVGVVTIGRFPtGSDE 167
Cdd:TIGR00745  79 L--LPL------IGKNTKVLFLQNGLGHEERLRELLParRILGGVVTHGAVREEPGVVHHAG---LGATKIGDYV-GENE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 168 TAEQIAADLDRANYLAETSNDIRRWKSLKL-----------LHNVRNAlELFDgDDDLRAsVAEALVNEARCALEAAGYN 236
Cdd:TIGR00745 147 AVEALAELLNEAGIPAELHGDILAAIWKKLlvnaainpltaLLDCKNG-ELLE-NPEARE-LLRRLMDEVVRVARAEGVD 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2790394528 237 FA--SASERALDIsgwrIAQNSGIHPgqqSTWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAV 301
Cdd:TIGR00745 224 LPddEVEELVRAV----IRMTAENTS---SMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTL 283
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
1-312 1.97e-21

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 93.14  E-value: 1.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   1 MTRYIIVGAGAVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSGvQQIRLNAFDI---FDPPELTPGDILLLT 77
Cdd:PRK08229    2 MARICVLGAGSIGCYLGGRLAAAGADVTLIGRARIGDELRAHGLTLTDYRG-RDVRVPPSAIafsTDPAALATADLVLVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  78 VKSQD---AANALASWSwRPVSdcgdtaaarlPVVTFQNGLATEAIaLRtfAKVYGASILT-----------PARFTE-- 141
Cdd:PRK08229   81 VKSAAtadAAAALAGHA-RPGA----------VVVSFQNGVRNADV-LR--AALPGATVLAgmvpfnvisrgPGAFHQgt 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 142 TGKVAVAGDPQVgvvtigrfptgsdetaEQIAADLDRANYLAETSNDIRRWKSLKLLHNVRNALELFDG--------DDD 213
Cdd:PRK08229  147 SGALAIEASPAL----------------RPFAAAFARAGLPLVTHEDMRAVQWAKLLLNLNNAVNALSGlplkeelaQRS 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 214 LRASVAEALvNEARCALEAAGYNFASA-------SERALDISGW---RIAQNS-GIHP-GQQSTWQSFARGASSEVDFLN 281
Cdd:PRK08229  211 YRRCLALAQ-REALRVLKAAGIRPARLtplppawIPRLLRLPDPlfrRLAGRMlAIDPlARSSMSDDLAAGRATEIDWIN 289
                         330       340       350
                  ....*....|....*....|....*....|.
gi 2790394528 282 GEIVLLGRLHNIPTPYNEAVQNIAGRLEHEG 312
Cdd:PRK08229  290 GEIVRLAGRLGAPAPVNARLCALVHEAERAG 320
PRK12921 PRK12921
oxidoreductase;
3-301 5.83e-21

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 91.46  E-value: 5.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   3 RYIIVGAGAVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSGVQQIRLNAFDifDPPELT-PGDILLLTVKSQ 81
Cdd:PRK12921    2 RIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPKRAKALRERGLVIRSDHGDAVVPGPVIT--DPEELTgPFDLVILAVKAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  82 DAANALAswSWRPVsdCG-DTAaarlpVVTFQNGLATEAiALRTF---AKVYGASILTPARFTETGKVAVAGDPQvgvVT 157
Cdd:PRK12921   80 QLDAAIP--DLKPL--VGeDTV-----IIPLQNGIGQLE-QLEPYfgrERVLGGVVFISAQLNGDGVVVQRADHR---LT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 158 IGRFPTGSDETAEQIAADLDRANYLAETSNDIRR--WKslKLLHNV----------RNALELFDGDDDlrASVAEALVNE 225
Cdd:PRK12921  147 FGEIPGQRSERTRAVRDALAGARLEVVLSENIRQdiWR--KLLFNAvmngmtalgrATVGGILSRPGG--RDLARALLRE 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790394528 226 ARCALEAAGYNFASASERalDISGwRIAQNSGIHpgQQSTWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAV 301
Cdd:PRK12921  223 CLAVARAEGAPLRDDVVE--EIVK-IFAGAPGDM--KTSMLRDMEKGRPLEIDHLQGVLLRRARAHGIPTPILDTV 293
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
6-159 4.50e-18

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: 79.58  E-value: 4.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   6 IVGAGAVGASLAAQFELAGVGYALVGRGAQISQIKRHGLSYQRPSGVQQIRLNAFdIFDPPELTPGDILLLTVKSQDAAN 85
Cdd:pfam02558   3 ILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLRLTSPGGERIVPPPAV-TSASESLGPIDLVIVTVKAYQTEE 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2790394528  86 ALAswswrpvsDCGDTAAARLPVVTFQNGLATEAIALRTF--AKVYGASILTPARFTETGKVAVAGDpqvGVVTIG 159
Cdd:pfam02558  82 ALE--------DIAPLLGPNTVVLLLQNGLGHEEVLREAVprERVLGGVTTHGAFREGPGHVHHAGP---GRITIG 146
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
188-309 3.47e-13

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: 65.33  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 188 DIRRWKSLKLLHN-VRNALE-LFDGD-DDLRAS-----VAEALVNEARCALEAAGYNFASasERALDISGWRIAQNSGIH 259
Cdd:pfam08546   1 DIRLARWEKLLVNaAINPLTaLTGCTnGELLDSpearaLIRALMREAVAVAQAEGVALSE--DRLIEYVLAVLRKTPDNK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2790394528 260 PgqqSTWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNEAVQNIAGRLE 309
Cdd:pfam08546  79 S---SMLQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
2-302 2.85e-12

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 66.28  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528   2 TRYIIVGAGAVGASLAAQFELAGVGYALVGRGAQISQikrhglSYQRPSGVQ-----QIRLNAFDIFDPPELTPGDILLL 76
Cdd:PRK05708    3 MTWHILGAGSLGSLWACRLARAGLPVRLILRDRQRLA------AYQQAGGLTlveqgQASLYAIPAETADAAEPIHRLLL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528  77 TVKSQDAANALASWSWRPvsdcgdTAAARLpvVTFQNGLAT-EAIALRT-FAKVYGASILTPARFTETGKVAVAGDPQ-- 152
Cdd:PRK05708   77 ACKAYDAEPAVASLAHRL------APGAEL--LLLQNGLGSqDAVAARVpHARCIFASSTEGAFRDGDWRVVFAGHGFtw 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 153 VGVVtigrfptgSDETAEQIAADLDRANYLAETSNDI--RRWKSLKL---------LHNVRNAlelfdgddDLRASVAE- 220
Cdd:PRK05708  149 LGDP--------RNPTAPAWLDDLREAGIPHEWTVDIltRLWRKLALncainpltvLHDCRNG--------GLLEHAQEv 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2790394528 221 -ALVNEARCALEAAGYNFASASeraLDISGWRIAQnsGIHPGQQSTWQSFARGASSEVDFLNGEIVLLGRLHNIPTPYNE 299
Cdd:PRK05708  213 aALCAELSELLRRCGQPAAAAN---LHEEVQRVIQ--ATAANYSSMYQDVRAGRRTEISYLLGYACRAADRHGLPLPRLQ 287

                  ...
gi 2790394528 300 AVQ 302
Cdd:PRK05708  288 HLQ 290
 
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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