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Conserved domains on  [gi|613101167|gb|EZX09559|]
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hypothetical protein V068_01988 [Staphylococcus aureus C0630]

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
 1-310 2.76e-116

2-dehydropantoate 2-reductase; Reviewed


:

Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 337.21  E-value: 2.76e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGYTSHVEAVKQHGLNItingEAFELNIPMYHFNDQPDESIYDVVFLFPKS 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRL----EDGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  81 MQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELvDEGKENV 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 161 IKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVDE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 241 VFEYLVDLNEKVGAHYPSMYQDLIvNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQRHAQ 310
Cdd:PRK06522 236 VREYVRQVIQKTAANTSSMLQDLE-AGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-310 2.76e-116

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 337.21  E-value: 2.76e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGYTSHVEAVKQHGLNItingEAFELNIPMYHFNDQPDESIYDVVFLFPKS 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRL----EDGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  81 MQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELvDEGKENV 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 161 IKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVDE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 241 VFEYLVDLNEKVGAHYPSMYQDLIvNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQRHAQ 310
Cdd:PRK06522 236 VREYVRQVIQKTAANTSSMLQDLE-AGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-306 6.47e-110

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: 320.79  E-value: 6.47e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   10 ALGSGFGAKLFQAGYDVTLIDGYtSHVEAVKQHGLNITINGEAFELNiPMYHFNDQPDESIYDVVFLFPKSMQLKEVMEA 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARG-EQLEALNQEGLRIVSLGGEFQFR-PVSAATSPEELPPADLVIITVKAYQTEEAAAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   90 MKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELVDEGkENVIKVADLLNE 169
Cdd:TIGR00745  79 LLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGDYVGEN-EAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  170 AELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVDEVFEYLVDLN 249
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVI 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 613101167  250 EKVGAHYPSMYQDLIvNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQ 306
Cdd:TIGR00745 238 RMTAENTSSMLQDLL-RGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-308 5.94e-98

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: 290.60  E-value: 5.94e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGyTSHVEAVKQHGLNIT-INGEAFELNIPMYhfNDQPDESIYDVVFLFPK 79
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVAR-GAHAEALRENGLRLEsPDGDRTTVPVPAV--TDPEELGPADLVLVAVK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  80 SMQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELVDEGKEN 159
Cdd:COG1893   78 AYDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 160 VIKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVD 239
Cdd:COG1893  158 LEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPED 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101167 240 EVFEYLVDLNEKVGAHYPSMYQDlIVNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQRH 308
Cdd:COG1893  238 DLEERVAAVAEATADNRSSMLQD-LEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAGRA 305
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-151 5.43e-47

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: 155.08  E-value: 5.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167    3 IAIAGSGALGSGFGAKLFQAGYDVTLIDGyTSHVEAVKQHGLNITINGEAFeLNIPMYHFNDQPDESIYDVVFLFPKSMQ 82
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILR-GAELAAIKKNGLRLTSPGGER-IVPPPAVTSASESLGPIDLVIVTVKAYQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101167   83 LKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGE 151
Cdd:pfam02558  79 TEEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITIGE 147
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-310 2.76e-116

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 337.21  E-value: 2.76e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGYTSHVEAVKQHGLNItingEAFELNIPMYHFNDQPDESIYDVVFLFPKS 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRL----EDGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  81 MQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELvDEGKENV 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 161 IKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVDE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 241 VFEYLVDLNEKVGAHYPSMYQDLIvNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQRHAQ 310
Cdd:PRK06522 236 VREYVRQVIQKTAANTSSMLQDLE-AGRPTEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-306 6.47e-110

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: 320.79  E-value: 6.47e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   10 ALGSGFGAKLFQAGYDVTLIDGYtSHVEAVKQHGLNITINGEAFELNiPMYHFNDQPDESIYDVVFLFPKSMQLKEVMEA 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARG-EQLEALNQEGLRIVSLGGEFQFR-PVSAATSPEELPPADLVIITVKAYQTEEAAAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   90 MKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELVDEGkENVIKVADLLNE 169
Cdd:TIGR00745  79 LLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGDYVGEN-EAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  170 AELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVDEVFEYLVDLN 249
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVI 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 613101167  250 EKVGAHYPSMYQDLIvNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQ 306
Cdd:TIGR00745 238 RMTAENTSSMLQDLL-RGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEAE 293
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-308 5.94e-98

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: 290.60  E-value: 5.94e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGyTSHVEAVKQHGLNIT-INGEAFELNIPMYhfNDQPDESIYDVVFLFPK 79
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVAR-GAHAEALRENGLRLEsPDGDRTTVPVPAV--TDPEELGPADLVLVAVK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  80 SMQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELVDEGKEN 159
Cdd:COG1893   78 AYDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 160 VIKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVD 239
Cdd:COG1893  158 LEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPED 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101167 240 EVFEYLVDLNEKVGAHYPSMYQDlIVNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQRH 308
Cdd:COG1893  238 DLEERVAAVAEATADNRSSMLQD-LEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEAGRA 305
PRK12921 PRK12921
oxidoreductase;
1-307 8.60e-65

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 206.25  E-value: 8.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIdGYTSHVEAVKQHGLNITINGEAFELNIPMYhfnDQPDESI--YDVVFLFP 78
Cdd:PRK12921   1 MRIAVVGAGAVGGTFGGRLLEAGRDVTFL-VRPKRAKALRERGLVIRSDHGDAVVPGPVI---TDPEELTgpFDLVILAV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  79 KSMQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGELVDEGKE 158
Cdd:PRK12921  77 KAYQLDAAIPDLKPLVGEDTVIIPLQNGIGQLEQLEPYFGRERVLGGVVFISAQLNGDGVVVQRADHRLTFGEIPGQRSE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 159 NVIKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNV 238
Cdd:PRK12921 157 RTRAVRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGRATVGGILSRPGGRDLARALLRECLAVARAEGAPLRD 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101167 239 DEVFEYLVDLNEKVGAHYPSMYQDLIvNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKESQR 307
Cdd:PRK12921 237 DVVEEIVKIFAGAPGDMKTSMLRDME-KGRPLEIDHLQGVLLRRARAHGIPTPILDTVYALLKAYEAGP 304
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-151 5.43e-47

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: 155.08  E-value: 5.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167    3 IAIAGSGALGSGFGAKLFQAGYDVTLIDGyTSHVEAVKQHGLNITINGEAFeLNIPMYHFNDQPDESIYDVVFLFPKSMQ 82
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILR-GAELAAIKKNGLRLTSPGGER-IVPPPAVTSASESLGPIDLVIVTVKAYQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101167   83 LKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGE 151
Cdd:pfam02558  79 TEEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITIGE 147
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
 179-304 7.73e-39

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: 133.12  E-value: 7.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  179 DLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNVHLNVDEVFEYLVDLNEKVGAHYPS 258
Cdd:pfam08546   1 DIRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGVALSEDRLIEYVLAVLRKTPDNKSS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 613101167  259 MYQDlIVNNRKTEIDYINGAVATLGKQRHIEAPVNRFITDLIHTKE 304
Cdd:pfam08546  81 MLQD-VEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
1-291 4.19e-25

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 102.35  E-value: 4.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIdgYTSHVEAVKQHGLNI-TINGeAFELNiPMYHFNDQPDESIYDVVFLFPK 79
Cdd:PRK06249   6 PRIGIIGTGAIGGFYGAMLARAGFDVHFL--LRSDYEAVRENGLQVdSVHG-DFHLP-PVQAYRSAEDMPPCDWVLVGLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  80 SMQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGEL----VDE 155
Cdd:PRK06249  82 TTANALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAEHLLGGLCFICSNRVGPGVIHHLAYGRVNLGYHsgpaADD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 156 G-KENVIKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSYAKCLIYKLTQEIVHVATIDNV 234
Cdd:PRK06249 162 GiTARVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNASTDPLMADPDSRALIRALMAEVIQGAAACGH 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 613101167 235 HLnvDEVF-EYLVDLNEKVGAHYPSMYQDLiVNNRKTEIDYINGAVATLGKQRHIEAP 291
Cdd:PRK06249 242 TL--PEGYaDHMLAVTERMPDYRPSMYHDF-EEGRPLELEAIYANPLAAARAAGCAMP 296
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
 1-305 2.17e-24

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 100.85  E-value: 2.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIdGYTSHVEAVKQHGLNIT-INGEAFELNIPMYHFNDQPDE-SIYDVVFLFP 78
Cdd:PRK08229   3 ARICVLGAGSIGCYLGGRLAAAGADVTLI-GRARIGDELRAHGLTLTdYRGRDVRVPPSAIAFSTDPAAlATADLVLVTV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  79 KSMQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHlLGSGpveiGELVDEGKE 158
Cdd:PRK08229  82 KSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMVPFNVISRGPGAFH-QGTS----GALAIEASP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 159 NVIKVADLLNEAELNGVISKDLYQSIWKK--ICVNGTANALStvlecNM---ASLNESSYAKCLIyKLTQEIVHV---AT 230
Cdd:PRK08229 157 ALRPFAAAFARAGLPLVTHEDMRAVQWAKllLNLNNAVNALS-----GLplkEELAQRSYRRCLA-LAQREALRVlkaAG 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 231 IDNVHLN--VDEVFEYLVDLNE----KVGAHY----P----SMYQDLIVnNRKTEIDYINGAVATLGKQRHIEAPVNRFI 296
Cdd:PRK08229 231 IRPARLTplPPAWIPRLLRLPDplfrRLAGRMlaidPlarsSMSDDLAA-GRATEIDWINGEIVRLAGRLGAPAPVNARL 309


                 ....*....
gi 613101167 297 TDLIHTKES 305
Cdd:PRK08229 310 CALVHEAER 318
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
1-307 1.05e-11

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 64.35  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGYTSHVEAVKQH-GLNITINGEAFELNIPMyhfnDQPD--ESIYDvVFLF 77
Cdd:PRK05708   3 MTWHILGAGSLGSLWACRLARAGLPVRLILRDRQRLAAYQQAgGLTLVEQGQASLYAIPA----ETADaaEPIHR-LLLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167  78 PKSMQLKEVMEAMKPHIDNETIVVCTMNGLKHEEVIAQYVAQSQIVRGVTTWTAGLESPGHSHLLGSGPVEIGelvDEGK 157
Cdd:PRK05708  78 CKAYDAEPAVASLAHRLAPGAELLLLQNGLGSQDAVAARVPHARCIFASSTEGAFRDGDWRVVFAGHGFTWLG---DPRN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167 158 ENVIKVADLLNEAELNGVISKDLYQSIWKKICVNGTANALSTVLECNMASLNESSyakCLIYKLTQEIV-------HVAT 230
Cdd:PRK05708 155 PTAPAWLDDLREAGIPHEWTVDILTRLWRKLALNCAINPLTVLHDCRNGGLLEHA---QEVAALCAELSellrrcgQPAA 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101167 231 IDNVHLNVDEVFeylvdlnEKVGAHYPSMYQDlIVNNRKTEIDYINGAVATLGkQRH-IEAPVNRFITDLIHTKESQR 307
Cdd:PRK05708 232 AANLHEEVQRVI-------QATAANYSSMYQD-VRAGRRTEISYLLGYACRAA-DRHgLPLPRLQHLQQRLVAHLRAR 300
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-132 2.38e-06

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: 48.14  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGY---DVTLIDGYTSHVEAV-KQHGLNITI-NGEAFElnipmyhfndqpdESiyDVVF 75
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLLKSGVppeDIIVSDRSPERLEALaERYGVRVTTdNAEAAA-------------QA--DVVV 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101167  76 LFPKSMQLKEVMEAMKPHIDNETIVVCTMNGLKHEEvIAQYV-AQSQIVR-----------GVTTWTAG 132
Cdd:COG0345   68 LAVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLAT-LEEALgGGAPVVRampntpalvgeGVTALAAG 135
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
1-121 6.12e-04

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


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 40.82  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101167   1 MKIAIAGSGALGSGFGAKLFQAGYDVTLIDGYTSHVEAVKQHGLNIT-INGEAFELNIpmyHFNDQPDESIYD---VVFL 76
Cdd:PRK00094   2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRyLPGIKLPDNL---RATTDLAEALADadlILVA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 613101167  77 FPkSMQLKEVMEAMKPHIDNETIVVCTMNGLKHE------EVIAQYVAQSQ 121
Cdd:PRK00094  79 VP-SQALREVLKQLKPLLPPDAPIVWATKGIEPGtgkllsEVLEEELPDLA 128
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 3-30 1.43e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 39.76  E-value: 1.43e-03
                         10        20
                 ....*....|....*....|....*...
gi 613101167   3 IAIAGSGALGSGFGAKLFQAGYDVTLID 30
Cdd:PRK06130   7 LAIIGAGTMGSGIAALFARKGLQVVLID 34
 
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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