NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489516055|ref|WP_003420888|]
View 

ketopantoate reductase family protein [Clostridioides difficile]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
11-307 1.81e-90

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: 271.73  E-value: 1.81e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  11 KVVFFGVGAVGATFAEQFLNSKYDFKILCNKERKKRYLEDGFIINGKRYDF-----DYVTRDEYKQEADFIIIGLKYNNL 85
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGDRttvpvPAVTDPEELGPADLVLVAVKAYDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  86 KENIKELDGLVGKNTVIMSLLNGVDSEEIIGERFGIEKMVYSYVTNIDAKKINNNIIHTTNGIIVFGNKDNSEDRKTNII 165
Cdd:COG1893   82 EAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSERLEAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 166 TEVFDDVNIEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVEN 245
Cdd:COG1893  162 AELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDDLEE 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489516055 246 SLHRILEHSKEGRTSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIESR 307
Cdd:COG1893  242 RVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAG 303
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
11-307 1.81e-90

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: 271.73  E-value: 1.81e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  11 KVVFFGVGAVGATFAEQFLNSKYDFKILCNKERKKRYLEDGFIINGKRYDF-----DYVTRDEYKQEADFIIIGLKYNNL 85
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGDRttvpvPAVTDPEELGPADLVLVAVKAYDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  86 KENIKELDGLVGKNTVIMSLLNGVDSEEIIGERFGIEKMVYSYVTNIDAKKINNNIIHTTNGIIVFGNKDNSEDRKTNII 165
Cdd:COG1893   82 EAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSERLEAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 166 TEVFDDVNIEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVEN 245
Cdd:COG1893  162 AELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDDLEE 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489516055 246 SLHRILEHSKEGRTSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIESR 307
Cdd:COG1893  242 RVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAG 303
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
19-307 9.04e-65

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: 205.61  E-value: 9.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055   19 AVGATFAEQFLNSKYDFKILCNKERKKRYLEDGFIINGKRYDFDY-----VTRDEYKQEADFIIIGLKYNNLKENIKELD 93
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLGGEFQFrpvsaATSPEELPPADLVIITVKAYQTEEAAALLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055   94 GLVGKNTVIMSLLNGVDSEEIIGERFGIEKMVYSYVTNIDAKKINNNIIHTTNGIIVFGNKDNSEDRKTNIiTEVFDDVN 173
Cdd:TIGR00745  81 PLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGDYVGENEAVEAL-AELLNEAG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  174 IEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVENSLHRILEH 253
Cdd:TIGR00745 160 IPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVIRM 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489516055  254 SKEGRTSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIESR 307
Cdd:TIGR00745 240 TAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
11-307 1.61e-55

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 181.97  E-value: 1.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  11 KVVFFGVGAVGATFAEQFLNSKYD--FkILCNKERKKRYLEDGF-IINGKRYDFDYVTRD-EYKQEADFIIIGLKYNNLK 86
Cdd:PRK06522   2 KIAILGAGAIGGLFGAALAQAGHDvtL-VARRGAHLDALNENGLrLEDGEITVPVLAADDpAELGPQDLVILAVKAYQLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  87 ENIKELDGLVGKNTVIMSLLNGVDSEEIIGERFGIEKMVYSYVTNIDAKKINNNIIHTTNGIIVFGNKDnSEDRKTNIIT 166
Cdd:PRK06522  81 AALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEPD-GESAAAEALA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 167 EVFDDVNIEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVENS 246
Cdd:PRK06522 160 DLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEEVREY 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489516055 247 LHRILEHSKEGRTSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIESR 307
Cdd:PRK06522 240 VRQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESE 300
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
181-305 5.56e-44

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: 146.60  E-value: 5.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  181 DIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVENSLHRILEHSKEGRTS 260
Cdd:pfam08546   1 DIRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGVALSEDRLIEYVLAVLRKTPDNKSS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 489516055  261 MLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIE 305
Cdd:pfam08546  81 MLQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
11-307 1.81e-90

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: 271.73  E-value: 1.81e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  11 KVVFFGVGAVGATFAEQFLNSKYDFKILCNKERKKRYLEDGFIINGKRYDF-----DYVTRDEYKQEADFIIIGLKYNNL 85
Cdd:COG1893    2 KIAILGAGAIGGLLGARLARAGHDVTLVARGAHAEALRENGLRLESPDGDRttvpvPAVTDPEELGPADLVLVAVKAYDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  86 KENIKELDGLVGKNTVIMSLLNGVDSEEIIGERFGIEKMVYSYVTNIDAKKINNNIIHTTNGIIVFGNKDNSEDRKTNII 165
Cdd:COG1893   82 EAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSERLEAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 166 TEVFDDVNIEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVEN 245
Cdd:COG1893  162 AELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDDLEE 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489516055 246 SLHRILEHSKEGRTSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIESR 307
Cdd:COG1893  242 RVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAG 303
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
19-307 9.04e-65

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: 205.61  E-value: 9.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055   19 AVGATFAEQFLNSKYDFKILCNKERKKRYLEDGFIINGKRYDFDY-----VTRDEYKQEADFIIIGLKYNNLKENIKELD 93
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARGEQLEALNQEGLRIVSLGGEFQFrpvsaATSPEELPPADLVIITVKAYQTEEAAALLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055   94 GLVGKNTVIMSLLNGVDSEEIIGERFGIEKMVYSYVTNIDAKKINNNIIHTTNGIIVFGNKDNSEDRKTNIiTEVFDDVN 173
Cdd:TIGR00745  81 PLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGDYVGENEAVEAL-AELLNEAG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  174 IEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVENSLHRILEH 253
Cdd:TIGR00745 160 IPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVIRM 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489516055  254 SKEGRTSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIESR 307
Cdd:TIGR00745 240 TAENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
11-307 1.61e-55

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 181.97  E-value: 1.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  11 KVVFFGVGAVGATFAEQFLNSKYD--FkILCNKERKKRYLEDGF-IINGKRYDFDYVTRD-EYKQEADFIIIGLKYNNLK 86
Cdd:PRK06522   2 KIAILGAGAIGGLFGAALAQAGHDvtL-VARRGAHLDALNENGLrLEDGEITVPVLAADDpAELGPQDLVILAVKAYQLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  87 ENIKELDGLVGKNTVIMSLLNGVDSEEIIGERFGIEKMVYSYVTNIDAKKINNNIIHTTNGIIVFGNKDnSEDRKTNIIT 166
Cdd:PRK06522  81 AALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEPD-GESAAAEALA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 167 EVFDDVNIEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVENS 246
Cdd:PRK06522 160 DLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEEVREY 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489516055 247 LHRILEHSKEGRTSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIESR 307
Cdd:PRK06522 240 VRQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESE 300
PRK12921 PRK12921
oxidoreductase;
11-296 2.29e-51

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 171.19  E-value: 2.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  11 KVVFFGVGAVGATFAEQFLNSKYDFKILCNKERKKRYLEDGFIINGKRYDFDY-----VTRDEYKQEADFIIIGLKYNNL 85
Cdd:PRK12921   2 RIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPKRAKALRERGLVIRSDHGDAVVpgpviTDPEELTGPFDLVILAVKAYQL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  86 KENIKELDGLVGKNTVIMSLLNGVDSEEIIGERFGIEKmVYSYVTNIDAKKINNNIIH-TTNGIIVFGNKDNSEDRKTNI 164
Cdd:PRK12921  82 DAAIPDLKPLVGEDTVIIPLQNGIGQLEQLEPYFGRER-VLGGVVFISAQLNGDGVVVqRADHRLTFGEIPGQRSERTRA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 165 ITEVFDDVNIEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVE 244
Cdd:PRK12921 161 VRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGRATVGGILSRPGGRDLARALLRECLAVARAEGAPLRDDVVE 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489516055 245 NSLHRILEHSKEGRTSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQT 296
Cdd:PRK12921 241 EIVKIFAGAPGDMKTSMLRDMEKGRPLEIDHLQGVLLRRARAHGIPTPILDT 292
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
181-305 5.56e-44

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: 146.60  E-value: 5.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  181 DIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMREVVAIAQAKGISLTEDDVENSLHRILEHSKEGRTS 260
Cdd:pfam08546   1 DIRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGVALSEDRLIEYVLAVLRKTPDNKSS 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 489516055  261 MLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQTFFYMIKVIE 305
Cdd:pfam08546  81 MLQDVEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
12-152 2.89e-19

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: 82.28  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055   12 VVFFGVGAVGATFAEQFLNSKYDFKILCNKERKKRYLEDGFIINGKRYDFDYVTR-----DEYKQEADFIIIGLKYNNLK 86
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNGLRLTSPGGERIVPPPavtsaSESLGPIDLVIVTVKAYQTE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489516055   87 ENIKELDGLVGKNTVIMSLLNGVDSEEIIGERFGIEKmVYSYVTNIDAKKINNNII-HTTNGIIVFG 152
Cdd:pfam02558  81 EALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRER-VLGGVTTHGAFREGPGHVhHAGPGRITIG 146
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
74-274 1.15e-12

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 67.29  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  74 DFIIIGLKY--NNLKENIkeLDGLVGKNTVIMSLLNGVDSEEIIGERFGIEKmVYSYVTNIDAKKINNNII-HTTNGIIV 150
Cdd:PRK06249  74 DWVLVGLKTtaNALLAPL--IPQVAAPDAKVLLLQNGLGVEEQLREILPAEH-LLGGLCFICSNRVGPGVIhHLAYGRVN 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 151 FG--NKDNSEDRKTNIITEV---FDDVNIEYVLSKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQSSEHLRELAKSAMR 225
Cdd:PRK06249 151 LGyhSGPAADDGITARVEEGaalFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNASTDPLMADPDSRALIRALMA 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489516055 226 EVVAIAQAKGISLTEDDVEnSLHRILEHSKEGRTSMLQDVEAHRPTEVD 274
Cdd:PRK06249 231 EVIQGAAACGHTLPEGYAD-HMLAVTERMPDYRPSMYHDFEEGRPLELE 278
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
72-307 4.12e-09

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 56.93  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055  72 EADFIIIGLKYNNLKENIKELDGLVGKNTVIMSLLNGVDSEEIIGERFG----IEKMVysyvtnidakkiNNNIIHT--- 144
Cdd:PRK08229  73 TADLVLVTVKSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPgatvLAGMV------------PFNVISRgpg 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 145 -----TNGIIVFGNKDNSEDrktniITEVFDDVNIEYVLSKDIQRDMWWKYMVNIGvNQTSAILGAPygvfqssehLR-E 218
Cdd:PRK08229 141 afhqgTSGALAIEASPALRP-----FAAAFARAGLPLVTHEDMRAVQWAKLLLNLN-NAVNALSGLP---------LKeE 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 219 LAKSAMREVVAIAQAKGISLTED--------------------DVENSLHRI-----LEHSKEGRTSMLQDVEAHRPTEV 273
Cdd:PRK08229 206 LAQRSYRRCLALAQREALRVLKAagirparltplppawiprllRLPDPLFRRlagrmLAIDPLARSSMSDDLAAGRATEI 285
                        250       260       270
                 ....*....|....*....|....*....|....
gi 489516055 274 DMFSKNICKLGKKYSIPTPINQTFFYMIKVIESR 307
Cdd:PRK08229 286 DWINGEIVRLAGRLGAPAPVNARLCALVHEAERA 319
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
179-295 1.06e-04

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 43.16  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055 179 SKDIQRDMWWKYMVNIGVNQTSAILGAPYGVFQssEHLRELAkSAMREVVAIAQAKGISLTEDDVENSLHRILEHSKEGR 258
Cdd:PRK05708 174 TVDILTRLWRKLALNCAINPLTVLHDCRNGGLL--EHAQEVA-ALCAELSELLRRCGQPAAAANLHEEVQRVIQATAANY 250
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489516055 259 TSMLQDVEAHRPTEVDMFSKNICKLGKKYSIPTPINQ 295
Cdd:PRK05708 251 SSMYQDVRAGRRTEISYLLGYACRAADRHGLPLPRLQ 287
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
8-125 2.93e-04

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: 41.59  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055   8 SQKKVVFFGVGAVGATFAEQFLNSKYDFK--ILCNKERKKR-YLEDGFIINgkrydfdyVTRDEYK--QEADFIIIGLKY 82
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKSGVPPEdiIVSDRSPERLeALAERYGVR--------VTTDNAEaaAQADVVVLAVKP 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489516055  83 NNLKENIKELDGLVGKNTVIMSLLNGVdSEEIIGERFGIEKMV 125
Cdd:COG0345   73 QDLAEVLEELAPLLDPDKLVISIAAGV-TLATLEEALGGGAPV 114
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
14-108 2.50e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 36.44  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516055   14 FFGVGAVGATFAEQFLNS-KYDFKILCNKERKK-RYLEDGFIINGKRydfdyVTRDEYKQEADFIIIGLKYNNLKENIKE 91
Cdd:pfam03807   2 FIGAGNMGEALARGLVAAgPHEVVVANSRNPEKaEELAEEYGVGATA-----VDNEEAAEEADVVFLAVKPEDAPDVLSE 76
                          90
                  ....*....|....*..
gi 489516055   92 LDGLVgKNTVIMSLLNG 108
Cdd:pfam03807  77 LSDLL-KGKIVISIAAG 92
 
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