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Conserved domains on  [gi|493446887|ref|WP_006402232|]
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2-dehydropantoate 2-reductase [Burkholderia multivorans]

Protein Classification

2-dehydropantoate 2-reductase( domain architecture ID 11482284)

2-dehydropantoate 2-reductase catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid

CATH:  3.40.50.720|1.10.1040.10
EC:  1.1.1.169
Gene Ontology:  GO:0008677|GO:0015940|GO:0050661
SCOP:  4000112

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 9-332 8.01e-107

2-dehydropantoate 2-reductase; Reviewed


:

Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 314.10  E-value: 8.01e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   9 VRAAVVGVGAIGGLLAAALSRAGVAVSAYAR-GATLDALNAHGVRVIDdagATSTVAVHASDDAAALGVQDYVVIALKAQ 87
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARrGAHLDALNENGLRLED---GEITVPVLAADDPAELGPQDLVILAVKAY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  88 ALPALAARIAPLVGPDTVIVAAMNGlpwwfthglagpldgvpleaVDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRR 167
Cdd:PRK06522  78 QLPAALPSLAPLLGPDTPVLFLQNG--------------------VGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 168 GRGNRLIVGAPDSRLEAtAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRM 247
Cdd:PRK06522 138 TGGGRLKIGEPDGESAA-AEALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRAL 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 248 MEEAAQIGAKLGLSTGMSGPERI--AVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQ 325
Cdd:PRK06522 217 MEEVAAVAEAEGVHLSVEEVREYvrQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKA 296


                 ....*..
gi 493446887 326 RAANSGL 332
Cdd:PRK06522 297 KESERGL 303
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 9-332 8.01e-107

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 314.10  E-value: 8.01e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   9 VRAAVVGVGAIGGLLAAALSRAGVAVSAYAR-GATLDALNAHGVRVIDdagATSTVAVHASDDAAALGVQDYVVIALKAQ 87
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARrGAHLDALNENGLRLED---GEITVPVLAADDPAELGPQDLVILAVKAY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  88 ALPALAARIAPLVGPDTVIVAAMNGlpwwfthglagpldgvpleaVDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRR 167
Cdd:PRK06522  78 QLPAALPSLAPLLGPDTPVLFLQNG--------------------VGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 168 GRGNRLIVGAPDSRLEAtAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRM 247
Cdd:PRK06522 138 TGGGRLKIGEPDGESAA-AEALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRAL 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 248 MEEAAQIGAKLGLSTGMSGPERI--AVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQ 325
Cdd:PRK06522 217 MEEVAAVAEAEGVHLSVEEVREYvrQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKA 296


                 ....*..
gi 493446887 326 RAANSGL 332
Cdd:PRK06522 297 KESERGL 303
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 10-331 3.06e-94

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: 282.13  E-value: 3.06e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVAVSAYARGATLDALNAHGVRVIDDAGATSTVAVHASDDAAALGVQDYVVIALKAQAL 89
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGDRTTVPVPAVTDPEELGPADLVLVAVKAYDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  90 PALAARIAPLVGPDTVIVAAMNGlpwwfthglagpldgvpleaVDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRRGR 169
Cdd:COG1893   82 EAAAEALAPLLGPDTVVLSLQNG--------------------LGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 170 GNRLIVGAPDSRLEATAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRMME 249
Cdd:COG1893  142 GGRLVLGELDGGPSERLEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMR 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 250 EAAQIGAKLGLSTGMSGPERI--AVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQRA 327
Cdd:COG1893  222 EVLAVARAEGVPLPEDDLEERvaAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALE 301


                 ....
gi 493446887 328 ANSG 331
Cdd:COG1893  302 AGRA 305
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 18-329 1.43e-54

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: 180.19  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   18 AIGGLLAAALSRAGVAVSAYARGATLDALNAHGVRVIDDAGATSTVAVHASDDAAALGVQDYVVIALKAQALPALAARIA 97
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLGGEFQFRPVSAATSPEELPPADLVIITVKAYQTEEAAALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   98 PLVGPDTVIVAAMNGLpwwfthglagpldgvpleavDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRRGRGNRLIVGA 177
Cdd:TIGR00745  81 PLIGKNTKVLFLQNGL--------------------GHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGD 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  178 PDSRLEAtAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRMMEEAAQIGAK 257
Cdd:TIGR00745 141 YVGENEA-VEALAELLNEAGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARA 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493446887  258 LGLSTGMSGPER--IAVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQRAAN 329
Cdd:TIGR00745 220 EGVDLPDDEVEElvRAVIRMTAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
 206-327 9.31e-32

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: 115.40  E-value: 9.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  206 IRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRMMEEAAQIGAKLG--LSTGMSGPERIAVTRKLGAFKTSM 283
Cdd:pfam08546   2 IRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGvaLSEDRLIEYVLAVLRKTPDNKSSM 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 493446887  284 LQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQRA 327
Cdd:pfam08546  82 LQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 9-332 8.01e-107

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 314.10  E-value: 8.01e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   9 VRAAVVGVGAIGGLLAAALSRAGVAVSAYAR-GATLDALNAHGVRVIDdagATSTVAVHASDDAAALGVQDYVVIALKAQ 87
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARrGAHLDALNENGLRLED---GEITVPVLAADDPAELGPQDLVILAVKAY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  88 ALPALAARIAPLVGPDTVIVAAMNGlpwwfthglagpldgvpleaVDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRR 167
Cdd:PRK06522  78 QLPAALPSLAPLLGPDTPVLFLQNG--------------------VGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 168 GRGNRLIVGAPDSRLEAtAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRM 247
Cdd:PRK06522 138 TGGGRLKIGEPDGESAA-AEALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRAL 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 248 MEEAAQIGAKLGLSTGMSGPERI--AVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQ 325
Cdd:PRK06522 217 MEEVAAVAEAEGVHLSVEEVREYvrQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKA 296


                 ....*..
gi 493446887 326 RAANSGL 332
Cdd:PRK06522 297 KESERGL 303
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 10-331 3.06e-94

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: 282.13  E-value: 3.06e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVAVSAYARGATLDALNAHGVRVIDDAGATSTVAVHASDDAAALGVQDYVVIALKAQAL 89
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGDRTTVPVPAVTDPEELGPADLVLVAVKAYDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  90 PALAARIAPLVGPDTVIVAAMNGlpwwfthglagpldgvpleaVDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRRGR 169
Cdd:COG1893   82 EAAAEALAPLLGPDTVVLSLQNG--------------------LGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 170 GNRLIVGAPDSRLEATAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRMME 249
Cdd:COG1893  142 GGRLVLGELDGGPSERLEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMR 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 250 EAAQIGAKLGLSTGMSGPERI--AVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQRA 327
Cdd:COG1893  222 EVLAVARAEGVPLPEDDLEERvaAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALE 301


                 ....
gi 493446887 328 ANSG 331
Cdd:COG1893  302 AGRA 305
PRK12921 PRK12921
oxidoreductase;
10-331 5.25e-68

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 215.11  E-value: 5.25e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVAVSAYARGATLDALNAHGVRVIDDAGaTSTVAVHASDDAAAL-GVQDYVVIALKAQA 88
Cdd:PRK12921   2 RIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPKRAKALRERGLVIRSDHG-DAVVPGPVITDPEELtGPFDLVILAVKAYQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  89 LPALAARIAPLVGPDTVIVAAMNGlpwwfthglagpldgvpleaVDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRRG 168
Cdd:PRK12921  81 LDAAIPDLKPLVGEDTVIIPLQNG--------------------IGQLEQLEPYFGRERVLGGVVFISAQLNGDGVVVQR 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 169 RGNRLIVGAPDSRLEATAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRMM 248
Cdd:PRK12921 141 ADHRLTFGEIPGQRSERTRAVRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGRATVGGILSRPGGRDLARALL 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 249 EEAAQIGAKLGLSTGMSGPERI--AVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQR 326
Cdd:PRK12921 221 RECLAVARAEGAPLRDDVVEEIvkIFAGAPGDMKTSMLRDMEKGRPLEIDHLQGVLLRRARAHGIPTPILDTVYALLKAY 300


                 ....*
gi 493446887 327 AANSG 331
Cdd:PRK12921 301 EAGPG 305
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 18-329 1.43e-54

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: 180.19  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   18 AIGGLLAAALSRAGVAVSAYARGATLDALNAHGVRVIDDAGATSTVAVHASDDAAALGVQDYVVIALKAQALPALAARIA 97
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLGGEFQFRPVSAATSPEELPPADLVIITVKAYQTEEAAALLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   98 PLVGPDTVIVAAMNGLpwwfthglagpldgvpleavDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRRGRGNRLIVGA 177
Cdd:TIGR00745  81 PLIGKNTKVLFLQNGL--------------------GHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGD 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  178 PDSRLEAtAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRMMEEAAQIGAK 257
Cdd:TIGR00745 141 YVGENEA-VEALAELLNEAGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARA 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493446887  258 LGLSTGMSGPER--IAVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQRAAN 329
Cdd:TIGR00745 220 EGVDLPDDEVEElvRAVIRMTAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
10-300 7.79e-33

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 123.53  E-value: 7.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVAVSAYARGaTLDALNAHGVRVIDDAGATSTVAVHASDDAAALGVQDYVVIALKAQAL 89
Cdd:PRK06249   7 RIGIIGTGAIGGFYGAMLARAGFDVHFLLRS-DYEAVRENGLQVDSVHGDFHLPPVQAYRSAEDMPPCDWVLVGLKTTAN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  90 PALAARIAPLVGPDTVIVAAMNGLpwwfthglagpldgvpleAVDPAgaVSAALPPAQAIGCVVHLSSSTDAPGVVRRGR 169
Cdd:PRK06249  86 ALLAPLIPQVAAPDAKVLLLQNGL------------------GVEEQ--LREILPAEHLLGGLCFICSNRVGPGVIHHLA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 170 GNRLIVG-----APDSRLEATAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELA 244
Cdd:PRK06249 146 YGRVNLGyhsgpAADDGITARVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNASTDPLMADPDSRALI 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493446887 245 LRMMEEAAQIGAKLGLSTGMSGPER-IAVTRKLGAFKTSMLQDFEAGRPLEIGPILG 300
Cdd:PRK06249 226 RALMAEVIQGAAACGHTLPEGYADHmLAVTERMPDYRPSMYHDFEEGRPLELEAIYA 282
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
 206-327 9.31e-32

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: 115.40  E-value: 9.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  206 IRTEIWAKLWGNMNMNPLSALTGSTAEQLLDDPFTHELALRMMEEAAQIGAKLG--LSTGMSGPERIAVTRKLGAFKTSM 283
Cdd:pfam08546   2 IRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGvaLSEDRLIEYVLAVLRKTPDNKSSM 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 493446887  284 LQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAVLGLLRQRA 327
Cdd:pfam08546  82 LQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
 7-325 1.36e-24

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 102.00  E-value: 1.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   7 GAVRAAVVGVGAIGGLLAAALSRAGVAVSAYARGATLDALNAHGVRVIDDAGATSTVA---VHASDDAAALGVQDYVVIA 83
Cdd:PRK08229   1 MMARICVLGAGSIGCYLGGRLAAAGADVTLIGRARIGDELRAHGLTLTDYRGRDVRVPpsaIAFSTDPAALATADLVLVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  84 LKAQALPALAARIAPLVGPDTVIVAAMNGlpwwfthglagpldgvpleaVDPAGAVSAALPPAQAIGCVVHLSSSTDAPG 163
Cdd:PRK08229  81 VKSAATADAAAALAGHARPGAVVVSFQNG--------------------VRNADVLRAALPGATVLAGMVPFNVISRGPG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 164 VVRRGRGNRLIVGAPdsrleATAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNmNPLSALTGST-AEQLLDDPFTHE 242
Cdd:PRK08229 141 AFHQGTSGALAIEAS-----PALRPFAAAFARAGLPLVTHEDMRAVQWAKLLLNLN-NAVNALSGLPlKEELAQRSYRRC 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 243 LALrMMEEAAQIGAKLGLSTGMSGPERIAVTRKL-----GAFK--------------TSMLQDFEAGRPLEIGPILGVFP 303
Cdd:PRK08229 215 LAL-AQREALRVLKAAGIRPARLTPLPPAWIPRLlrlpdPLFRrlagrmlaidplarSSMSDDLAAGRATEIDWINGEIV 293

                        330       340
                 ....*....|....*....|..
gi 493446887 304 ELGRRLNVPTPYCDAVLGLLRQ 325
Cdd:PRK08229 294 RLAGRLGAPAPVNARLCALVHE 315
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 12-177 3.13e-22

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: 90.75  E-value: 3.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   12 AVVGVGAIGGLLAAALSRAGVAVSAYARGATLDALNAHGVRVIDDAGATSTVAVHASDDAAALGVQDYVVIALKAQALPA 91
Cdd:pfam02558   2 AILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLRLTSPGGERIVPPPAVTSASESLGPIDLVIVTVKAYQTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887   92 LAARIAPLVGPDTVIVAAMNGLpwwfthglagpldgvpleavDPAGAVSAALPPAQAIGCVVHLSSSTDAPGVVRRGRGN 171
Cdd:pfam02558  82 ALEDIAPLLGPNTVVLLLQNGL--------------------GHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPG 141


                  ....*.
gi 493446887  172 RLIVGA 177
Cdd:pfam02558 142 RITIGE 147
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
13-332 3.37e-15

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 74.75  E-value: 3.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  13 VVGVGAIGGLLAAALSRAGVAVSAYAR-GATLDALNAHGVRVIDDAGATSTVAVHASDDAAALGVQDYVViALKA-QALP 90
Cdd:PRK05708   7 ILGAGSLGSLWACRLARAGLPVRLILRdRQRLAAYQQAGGLTLVEQGQASLYAIPAETADAAEPIHRLLL-ACKAyDAEP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  91 ALAaRIAPLVGPDTVIVAAMNGLpwwfthglaGPLDgvpleavdpagAVSAALPPAQAIgcvvhLSSST-----DAPG-V 164
Cdd:PRK05708  86 AVA-SLAHRLAPGAELLLLQNGL---------GSQD-----------AVAARVPHARCI-----FASSTegafrDGDWrV 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 165 VRRGRGNRLIVGAPDSrleaTAARFAALLSAGGFDVESTPAIRTEIWAKLWGNMNMNPLSALTGSTAEQLLD-----DPF 239
Cdd:PRK05708 140 VFAGHGFTWLGDPRNP----TAPAWLDDLREAGIPHEWTVDILTRLWRKLALNCAINPLTVLHDCRNGGLLEhaqevAAL 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887 240 THELAlRMMEEAAQIGAKLGLstgmsGPERIAVTRKLGAFKTSMLQDFEAGRPLEIGPILGVFPELGRRLNVPTPYCDAV 319
Cdd:PRK05708 216 CAELS-ELLRRCGQPAAAANL-----HEEVQRVIQATAANYSSMYQDVRAGRRTEISYLLGYACRAADRHGLPLPRLQHL 289

                        330
                 ....*....|...
gi 493446887 320 LGLLRQRAANSGL 332
Cdd:PRK05708 290 QQRLVAHLRARGL 302
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 10-106 2.37e-07

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 51.28  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVA--VSAYAR-GATLDALNAHGvrVIDDAgatstvavhASDDAAALGVQDYVVIALKA 86
Cdd:COG0287    3 RIAIIGLGLIGGSLALALKRAGLAheVVGVDRsPETLERALELG--VIDRA---------ATDLEEAVADADLVVLAVPV 71

                         90       100
                 ....*....|....*....|
gi 493446887  87 QALPALAARIAPLVGPDTVI 106
Cdd:COG0287   72 GATIEVLAELAPHLKPGAIV 91
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 12-114 3.52e-07

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 50.83  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  12 AVVGVGAIGGLLAAALSRAGVA---VSAYAR-GATLDAL-NAHGVRVIDDAGAtstvAVHASDdaaalgvqdYVVIALKA 86
Cdd:COG0345    6 GFIGAGNMGSAIIKGLLKSGVPpedIIVSDRsPERLEALaERYGVRVTTDNAE----AAAQAD---------VVVLAVKP 72

                         90       100
                 ....*....|....*....|....*...
gi 493446887  87 QALPALAARIAPLVGPDTVIVAAMNGLP 114
Cdd:COG0345   73 QDLAEVLEELAPLLDPDKLVISIAAGVT 100
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
10-113 3.72e-07

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 50.84  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVAVSAYAR-GATLDALNAHGVRVIDDAGATSTVAVHASDD-AAALGVQDYVVIALKAQ 87
Cdd:PRK00094   3 KIAVLGAGSWGTALAIVLARNGHDVTLWARdPEQAAEINADRENPRYLPGIKLPDNLRATTDlAEALADADLILVAVPSQ 82

                         90       100
                 ....*....|....*....|....*.
gi 493446887  88 ALPALAARIAPLVGPDTVIVAAMNGL 113
Cdd:PRK00094  83 ALREVLKQLKPLLPPDAPIVWATKGI 108
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 10-113 9.24e-06

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 46.57  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVAVSAYAR-GATLDALNAHGVRVIDDAGATSTVAVHASDD-AAALGVQDYVVIALKAQ 87
Cdd:COG0240    2 KIAVLGAGSWGTALAKVLARNGHEVTLWGRdPEVAEEINETRENPRYLPGVKLPENLRATSDlEEALAGADLVLLAVPSQ 81

                         90       100
                 ....*....|....*....|....*.
gi 493446887  88 ALPALAARIAPLVGPDTVIVAAMNGL 113
Cdd:COG0240   82 ALREVLEQLAPLLPPGAPVVSATKGI 107
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 10-123 2.26e-05

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 46.14  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVA--VSAYARGA-TLDALNAHGvrVIDDAgatstvavhASDDAAALGVQDYVVIALKA 86
Cdd:PRK14806   5 RVVVIGLGLIGGSFAKALRERGLAreVVAVDRRAkSLELAVSLG--VIDRG---------EEDLAEAVSGADVIVLAVPV 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493446887  87 QALPALAARIAPLVGPDTVI--------------VAAMNGLPWWFT--HGLAG 123
Cdd:PRK14806  74 LAMEKVLADLKPLLSEHAIVtdvgstkgnvvdaaRAVFGELPAGFVpgHPIAG 126
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
10-106 2.18e-04

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 42.26  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVA--VSAYARGA-TLDALNAHGV--RVIDDAGAtstvavhASDDAaalgvqDYVVIAL 84
Cdd:PRK07502   8 RVALIGIGLIGSSLARAIRRLGLAgeIVGADRSAeTRARARELGLgdRVTTSAAE-------AVKGA------DLVILCV 74

                         90       100
                 ....*....|....*....|..
gi 493446887  85 KAQALPALAARIAPLVGPDTVI 106
Cdd:PRK07502  75 PVGASGAVAAEIAPHLKPGAIV 96
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 10-114 1.08e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 40.14  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  10 RAAVVGVGAIGGLLAAALSRAGVAVSAYARGAtlDALnAHGVRVIDDA---GATSTVAVHA-------SDDAAALGVQDY 79
Cdd:PRK06130   6 NLAIIGAGTMGSGIAALFARKGLQVVLIDVME--GAL-ERARGVIERAlgvYAPLGIASAGmgrirmeAGLAAAVSGADL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 493446887  80 VV------IALKAQalpaLAARIAPLVGPDTVIVAAMNGLP 114
Cdd:PRK06130  83 VIeavpekLELKRD----VFARLDGLCDPDTIFATNTSGLP 119
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 13-107 6.80e-03

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 37.96  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493446887  13 VVGVGAIGGLLAAALSRAGVAVSAYARGATLDALN-AHGVRVIDDAGATSTVAVhasdDAAALgvqdyVVIALKAQALPA 91
Cdd:PRK06545   5 IVGLGLIGGSLALAIKAAGPDVFIIGYDPSAAQLArALGFGVIDELAADLQRAA----AEADL-----IVLAVPVDATAA 75

                         90
                 ....*....|....*.
gi 493446887  92 LAARIAPLVGPDTVIV 107
Cdd:PRK06545  76 LLAELADLELKPGVIV 91
 
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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