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Conserved domains on  [gi|2048538642|ref|WP_215111989|]
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ketopantoate reductase family protein [Exiguobacterium sp. s75]

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 ...
7-278 8.04e-52

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: 171.58  E-value: 8.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   7 RIGIIGNGAVGLLMASLLAD-DYDVTLYGRSGSSDPLV---ITRTGVTEGTARVSFRSSQTLQETDE-DLFFVTTKAHQV 81
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARaGHDVTLVARGAHAEALRengLRLESPDGDRTTVPVPAVTDPEELGPaDLVLVAVKAYDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  82 EEATARLSGKV----PVFICSNGIAHLEYAKRR-GFH---LGVVEHGVTKRG-HEVEHRGLGRIRIGS-----TSVLHPL 147
Cdd:COG1893    82 EAAAEALAPLLgpdtVVLSLQNGLGHEERLAEAlGAErvlGGVVTIGATREEpGVVRHTGGGRLVLGEldggpSERLEAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 148 S--FQESPLHIVWEEEIEQVVIEKLFANAIINPITALCRVPNGALAGSP-YREIAQSIYDELIPL-------FAQHVSYS 217
Cdd:COG1893   162 AelLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPeARALARALMREVLAVaraegvpLPEDDLEE 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048538642 218 YIETIVERTAENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISLTVIPLLHKLILGASA 278
Cdd:COG1893   242 RVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEA 302
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
7-278 8.04e-52

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: 171.58  E-value: 8.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   7 RIGIIGNGAVGLLMASLLAD-DYDVTLYGRSGSSDPLV---ITRTGVTEGTARVSFRSSQTLQETDE-DLFFVTTKAHQV 81
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARaGHDVTLVARGAHAEALRengLRLESPDGDRTTVPVPAVTDPEELGPaDLVLVAVKAYDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  82 EEATARLSGKV----PVFICSNGIAHLEYAKRR-GFH---LGVVEHGVTKRG-HEVEHRGLGRIRIGS-----TSVLHPL 147
Cdd:COG1893    82 EAAAEALAPLLgpdtVVLSLQNGLGHEERLAEAlGAErvlGGVVTIGATREEpGVVRHTGGGRLVLGEldggpSERLEAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 148 S--FQESPLHIVWEEEIEQVVIEKLFANAIINPITALCRVPNGALAGSP-YREIAQSIYDELIPL-------FAQHVSYS 217
Cdd:COG1893   162 AelLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPeARALARALMREVLAVaraegvpLPEDDLEE 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048538642 218 YIETIVERTAENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISLTVIPLLHKLILGASA 278
Cdd:COG1893   242 RVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEA 302
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
7-273 1.03e-51

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 171.19  E-value: 1.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   7 RIGIIGNGAVGLLMASLLAD-DYDVTLYGRSG-SSDPLVITRTGVTEGTARVSFRSSQTLQE-TDEDLFFVTTKAHQVEE 83
Cdd:PRK06522    2 KIAILGAGAIGGLFGAALAQaGHDVTLVARRGaHLDALNENGLRLEDGEITVPVLAADDPAElGPQDLVILAVKAYQLPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  84 ATARLSGKV----PVFICSNGIAHLEYAKRRGFH----LGVVEHGVTKRG-HEVEHRGLGRIRIGSTSVLHPLS------ 148
Cdd:PRK06522   82 ALPSLAPLLgpdtPVLFLQNGVGHLEELAAYIGPervlGGVVTHAAELEGpGVVRHTGGGRLKIGEPDGESAAAealadl 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 149 FQESPLHIVWEEEIEQVVIEKLFANAIINPITALCRVPNGALAGSP-YREIAQSIYDEL--------IPLFAQHVSySYI 219
Cdd:PRK06522  162 LNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPdYRALIRALMEEVaavaeaegVHLSVEEVR-EYV 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2048538642 220 ETIVERTAENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISLTVIPLLHKLI 273
Cdd:PRK06522  241 RQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLL 294
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
15-279 6.00e-40

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: 140.51  E-value: 6.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  15 AVGLLMASLLAD-DYDVTLYGRSGSSDPLVITRTGVTEGTARVSFRSSQTLQETDE----DLFFVTTKAHQVEEATARLS 89
Cdd:TIGR00745   1 AVGSLYGAYLARaGHDVTLLARGEQLEALNQEGLRIVSLGGEFQFRPVSAATSPEElppaDLVIITVKAYQTEEAAALLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  90 GKVP----VFICSNGIAHLEYAKRRGFH----LGVVEHGVTKRGH-EVEHRGLGRIRIGSTS-----VLHPLS-FQESPL 154
Cdd:TIGR00745  81 PLIGkntkVLFLQNGLGHEERLRELLPArrilGGVVTHGAVREEPgVVHHAGLGATKIGDYVgeneaVEALAElLNEAGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 155 HIVWEEEIEQVVIEKLFANAIINPITALCRVPNGALAGSPY-REIAQSIYDELIPLF-AQHVSYS------YIETIVERT 226
Cdd:TIGR00745 161 PAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEaRELLRRLMDEVVRVArAEGVDLPddeveeLVRAVIRMT 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2048538642 227 AENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISLTVIPLLHKLILGASAS 279
Cdd:TIGR00745 241 AENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
169-273 2.26e-23

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: 92.29  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 169 KLFANAIINPITALCRVPNGALAGSPY-REIAQSIYDELIPLF-AQHVSYS------YIETIVERTAENRSSMLRDLEEG 240
Cdd:pfam08546   9 KLLVNAAINPLTALTGCTNGELLDSPEaRALIRALMREAVAVAqAEGVALSedrlieYVLAVLRKTPDNKSSMLQDVEAG 88
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2048538642 241 RPTEVDAILKPVIEKAEQMQISLTVIPLLHKLI 273
Cdd:pfam08546  89 RPTEIDYINGYVVRLARKHGVPTPTNETLYALL 121
 
Name Accession Description Interval E-value
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
7-278 8.04e-52

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: 171.58  E-value: 8.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   7 RIGIIGNGAVGLLMASLLAD-DYDVTLYGRSGSSDPLV---ITRTGVTEGTARVSFRSSQTLQETDE-DLFFVTTKAHQV 81
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARaGHDVTLVARGAHAEALRengLRLESPDGDRTTVPVPAVTDPEELGPaDLVLVAVKAYDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  82 EEATARLSGKV----PVFICSNGIAHLEYAKRR-GFH---LGVVEHGVTKRG-HEVEHRGLGRIRIGS-----TSVLHPL 147
Cdd:COG1893    82 EAAAEALAPLLgpdtVVLSLQNGLGHEERLAEAlGAErvlGGVVTIGATREEpGVVRHTGGGRLVLGEldggpSERLEAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 148 S--FQESPLHIVWEEEIEQVVIEKLFANAIINPITALCRVPNGALAGSP-YREIAQSIYDELIPL-------FAQHVSYS 217
Cdd:COG1893   162 AelLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPeARALARALMREVLAVaraegvpLPEDDLEE 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2048538642 218 YIETIVERTAENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISLTVIPLLHKLILGASA 278
Cdd:COG1893   242 RVAAVAEATADNRSSMLQDLEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEA 302
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
7-273 1.03e-51

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 171.19  E-value: 1.03e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   7 RIGIIGNGAVGLLMASLLAD-DYDVTLYGRSG-SSDPLVITRTGVTEGTARVSFRSSQTLQE-TDEDLFFVTTKAHQVEE 83
Cdd:PRK06522    2 KIAILGAGAIGGLFGAALAQaGHDVTLVARRGaHLDALNENGLRLEDGEITVPVLAADDPAElGPQDLVILAVKAYQLPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  84 ATARLSGKV----PVFICSNGIAHLEYAKRRGFH----LGVVEHGVTKRG-HEVEHRGLGRIRIGSTSVLHPLS------ 148
Cdd:PRK06522   82 ALPSLAPLLgpdtPVLFLQNGVGHLEELAAYIGPervlGGVVTHAAELEGpGVVRHTGGGRLKIGEPDGESAAAealadl 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 149 FQESPLHIVWEEEIEQVVIEKLFANAIINPITALCRVPNGALAGSP-YREIAQSIYDEL--------IPLFAQHVSySYI 219
Cdd:PRK06522  162 LNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPdYRALIRALMEEVaavaeaegVHLSVEEVR-EYV 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2048538642 220 ETIVERTAENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISLTVIPLLHKLI 273
Cdd:PRK06522  241 RQVIQKTAANTSSMLQDLEAGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLL 294
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
15-279 6.00e-40

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: 140.51  E-value: 6.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  15 AVGLLMASLLAD-DYDVTLYGRSGSSDPLVITRTGVTEGTARVSFRSSQTLQETDE----DLFFVTTKAHQVEEATARLS 89
Cdd:TIGR00745   1 AVGSLYGAYLARaGHDVTLLARGEQLEALNQEGLRIVSLGGEFQFRPVSAATSPEElppaDLVIITVKAYQTEEAAALLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  90 GKVP----VFICSNGIAHLEYAKRRGFH----LGVVEHGVTKRGH-EVEHRGLGRIRIGSTS-----VLHPLS-FQESPL 154
Cdd:TIGR00745  81 PLIGkntkVLFLQNGLGHEERLRELLPArrilGGVVTHGAVREEPgVVHHAGLGATKIGDYVgeneaVEALAElLNEAGI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 155 HIVWEEEIEQVVIEKLFANAIINPITALCRVPNGALAGSPY-REIAQSIYDELIPLF-AQHVSYS------YIETIVERT 226
Cdd:TIGR00745 161 PAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEaRELLRRLMDEVVRVArAEGVDLPddeveeLVRAVIRMT 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2048538642 227 AENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISLTVIPLLHKLILGASAS 279
Cdd:TIGR00745 241 AENTSSMLQDLLRGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
169-273 2.26e-23

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: 92.29  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 169 KLFANAIINPITALCRVPNGALAGSPY-REIAQSIYDELIPLF-AQHVSYS------YIETIVERTAENRSSMLRDLEEG 240
Cdd:pfam08546   9 KLLVNAAINPLTALTGCTNGELLDSPEaRALIRALMREAVAVAqAEGVALSedrlieYVLAVLRKTPDNKSSMLQDVEAG 88
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2048538642 241 RPTEVDAILKPVIEKAEQMQISLTVIPLLHKLI 273
Cdd:pfam08546  89 RPTEIDYINGYVVRLARKHGVPTPTNETLYALL 121
PRK12921 PRK12921
oxidoreductase;
7-270 4.67e-22

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 93.00  E-value: 4.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   7 RIGIIGNGAVGLLMASLLAD-DYDVTLYGRSGSSDPL----VITRTGVTEGTARVSFRSSQTLQETDEDLFFVTTKAHQV 81
Cdd:PRK12921    2 RIAVVGAGAVGGTFGGRLLEaGRDVTFLVRPKRAKALrergLVIRSDHGDAVVPGPVITDPEELTGPFDLVILAVKAYQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  82 EEATARLSGKVP---VFIC-SNGIAHLE----YAKRRGFHLGVV--EHGVTKRGHeVEHRGLGRIRIGSTS--------- 142
Cdd:PRK12921   82 DAAIPDLKPLVGedtVIIPlQNGIGQLEqlepYFGRERVLGGVVfiSAQLNGDGV-VVQRADHRLTFGEIPgqrsertra 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 143 ---VLHPLSFqESPLH-----IVWEeeieqvvieKLFANAIINPITALCRVPNGALAGSPY-REIAQSIYDElIPLFAQH 213
Cdd:PRK12921  161 vrdALAGARL-EVVLSenirqDIWR---------KLLFNAVMNGMTALGRATVGGILSRPGgRDLARALLRE-CLAVARA 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048538642 214 VSYSYIETIVERT--------AENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISL----TVIPLLH 270
Cdd:PRK12921  230 EGAPLRDDVVEEIvkifagapGDMKTSMLRDMEKGRPLEIDHLQGVLLRRARAHGIPTpildTVYALLK 298
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
8-139 4.71e-17

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: 76.12  E-value: 4.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   8 IGIIGNGAVGLLMASLLAD-DYDVTLYGRSGSsdPLVITRTG--VTEGTARVSFRSSQTLQETDE----DLFFVTTKAHQ 80
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKaGHDVTLILRGAE--LAAIKKNGlrLTSPGGERIVPPPAVTSASESlgpiDLVIVTVKAYQ 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048538642  81 VEEATA----RLSGKVPVFICSNGIAHLEYAKRRGFH----LGVVEHGVTKRGH-EVEHRGLGRIRIG 139
Cdd:pfam02558  79 TEEALEdiapLLGPNTVVLLLQNGLGHEEVLREAVPRervlGGVTTHGAFREGPgHVHHAGPGRITIG 146
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
1-272 5.12e-08

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 53.04  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   1 MMNSIKRIGIIGNGAVGLLMASLLAD-DYDVTLYGRSgssDPLVITRTGVTEGTARVSFR--SSQTLQETDE----DLFF 73
Cdd:PRK06249    1 MDSETPRIGIIGTGAIGGFYGAMLARaGFDVHFLLRS---DYEAVRENGLQVDSVHGDFHlpPVQAYRSAEDmppcDWVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  74 VTTKAHQ--------------------------VEEATARLSGKVPV-----FICSNGiahleyakrrgfhlgvVEHGVt 122
Cdd:PRK06249   78 VGLKTTAnallaplipqvaapdakvlllqnglgVEEQLREILPAEHLlgglcFICSNR----------------VGPGV- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 123 krgheVEHRGLGRIRIG----------STSVLHPLS--FQESPLHIVWEEEIEQVVIEKLFANAIINPITALCRVPNGAL 190
Cdd:PRK06249  141 -----IHHLAYGRVNLGyhsgpaaddgITARVEEGAalFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNASTDPL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 191 AGSPY-REIAQSIYDELIpLFAQ----HVSYSYIETIV---ERTAENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQIS 262
Cdd:PRK06249  216 MADPDsRALIRALMAEVI-QGAAacghTLPEGYADHMLavtERMPDYRPSMYHDFEEGRPLELEAIYANPLAAARAAGCA 294
                         330
                  ....*....|
gi 2048538642 263 LTVIPLLHKL 272
Cdd:PRK06249  295 MPRVEMLYQA 304
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
7-272 2.81e-07

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 50.87  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   7 RIGIIGNGAVGLLMASLLAD-DYDVTLYGRSGSSDPLVITRTGVT--EGTARVSFRSSQTLQETDEDL--FFVTTKAHQV 81
Cdd:PRK05708    4 TWHILGAGSLGSLWACRLARaGLPVRLILRDRQRLAAYQQAGGLTlvEQGQASLYAIPAETADAAEPIhrLLLACKAYDA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  82 EEATA----RLSGKVPVFICSNG------IAHlEYAKRRGFHLGVVEHGVTKRGHEVEHRGLGRIRIGSTSvlHPLS--- 148
Cdd:PRK05708   84 EPAVAslahRLAPGAELLLLQNGlgsqdaVAA-RVPHARCIFASSTEGAFRDGDWRVVFAGHGFTWLGDPR--NPTApaw 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 149 ---FQESPLHIVWEEEIEQVVIEKLFANAIINPITAL--CRvpNGALAGSPyREIAqSIYDELIPLFA---QHVSYSYIE 220
Cdd:PRK05708  161 lddLREAGIPHEWTVDILTRLWRKLALNCAINPLTVLhdCR--NGGLLEHA-QEVA-ALCAELSELLRrcgQPAAAANLH 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2048538642 221 TIVER----TAENRSSMLRDLEEGRPTEVDAILKPVIEKAEQMQISLtviPLLHKL 272
Cdd:PRK05708  237 EEVQRviqaTAANYSSMYQDVRAGRRTEISYLLGYACRAADRHGLPL---PRLQHL 289
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
6-259 4.35e-04

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 41.14  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642   6 KRIGIIGNGAVGLLMAS-LLADDYDVTLYGRSGSSDP-----LVIT-RTG--VTEGTARVSFRSSQTLQEtDEDLFFVTT 76
Cdd:PRK08229    3 ARICVLGAGSIGCYLGGrLAAAGADVTLIGRARIGDElrahgLTLTdYRGrdVRVPPSAIAFSTDPAALA-TADLVLVTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642  77 KAHQVEEATARLSGKVP----VFICSNGIAHL----EYAKRRGFHLGVVEHGVTKRGHEVEHRGL-GRIRIGSTSVLHPL 147
Cdd:PRK08229   82 KSAATADAAAALAGHARpgavVVSFQNGVRNAdvlrAALPGATVLAGMVPFNVISRGPGAFHQGTsGALAIEASPALRPF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048538642 148 S--FQESPLHIVWEEEIEQVVIEKLFANaIINPITALCRVPNGA-LAGSPYREI---AQS------------------IY 203
Cdd:PRK08229  162 AaaFARAGLPLVTHEDMRAVQWAKLLLN-LNNAVNALSGLPLKEeLAQRSYRRClalAQRealrvlkaagirparltpLP 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048538642 204 DELIP--------LFAQhvsysyietIVERT----AENRSSMLRDLEEGRPTEVDAILKPVIEKAEQM 259
Cdd:PRK08229  241 PAWIPrllrlpdpLFRR---------LAGRMlaidPLARSSMSDDLAAGRATEIDWINGEIVRLAGRL 299
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
6-33 2.33e-03

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 38.94  E-value: 2.33e-03
                          10        20
                  ....*....|....*....|....*...
gi 2048538642   6 KRIGIIGNGAVGLLMASLLADDYDVTLY 33
Cdd:COG2907     4 MRIAVIGSGISGLTAAWLLSRRHDVTLF 31
 
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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