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Conserved domains on  [gi|488220706|ref|WP_002291914|]
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MULTISPECIES: 2-dehydropantoate 2-reductase [Lactobacillales]

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
 1-312 1.98e-119

2-dehydropantoate 2-reductase; Reviewed


:

Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 345.30  E-value: 1.98e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAEHVQQIKEHGLQANfngkEVEAKLPIVLQSEVEKEDQVDLIILFTKA 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLE----DGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  81 MQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQNLgDGKEAAA 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 161 KKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVPE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488220706 241 VIAHCESCFdpETIGLHYPSMYQDLIKNHRlTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKEDSLNVK 312
Cdd:PRK06522 236 VREYVRQVI--QKTAANTSSMLQDLEAGRP-TEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-312 1.98e-119

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 345.30  E-value: 1.98e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAEHVQQIKEHGLQANfngkEVEAKLPIVLQSEVEKEDQVDLIILFTKA 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLE----DGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  81 MQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQNLgDGKEAAA 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 161 KKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVPE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488220706 241 VIAHCESCFdpETIGLHYPSMYQDLIKNHRlTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKEDSLNVK 312
Cdd:PRK06522 236 VREYVRQVI--QKTAANTSSMLQDLEAGRP-TEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-306 1.80e-96

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: 287.14  E-value: 1.80e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAeHVQQIKEHGLQANF-NGKEVEAKLPIVlqSEVEKEDQVDLIILFTK 79
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGA-HAEALRENGLRLESpDGDRTTVPVPAV--TDPEELGPADLVLVAVK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  80 AMQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQNLGDGKEAA 159
Cdd:COG1893   78 AYDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 160 AKKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVP 239
Cdd:COG1893  158 LEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPED 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488220706 240 EVIAHCESCFdpETIGLHYPSMYQDlIKNHRLTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKE 306
Cdd:COG1893  238 DLEERVAAVA--EATADNRSSMLQD-LEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALE 301
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-306 7.39e-80

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: 244.13  E-value: 7.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   10 AMGSRFGLMLHQSGNEVLLIDGWaEHVQQIKEHGLQANFNGKEVEaKLPIVLQSEVEKEDQVDLIILFTKAMQLEKMLQD 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARG-EQLEALNQEGLRIVSLGGEFQ-FRPVSAATSPEELPPADLVIITVKAYQTEEAAAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   90 IQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQnLGDGKEAAAKKLADKLSE 169
Cdd:TIGR00745  79 LLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIG-DYVGENEAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  170 SGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVPEVIAHCESC- 248
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVi 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488220706  249 -FDPEtiglHYPSMYQDLIkNHRLTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKE 306
Cdd:TIGR00745 238 rMTAE----NTSSMLQDLL-RGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALE 291
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-150 5.21e-51

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: 165.48  E-value: 5.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706    3 IAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAEHVQqIKEHGLQANFNGKEVEAKLPIVLQSEVEKEDqVDLIILFTKAMQ 82
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAA-IKKNGLRLTSPGGERIVPPPAVTSASESLGP-IDLVIVTVKAYQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488220706   83 LEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQ 150
Cdd:pfam02558  79 TEEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITIG 146
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-312 1.98e-119

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 345.30  E-value: 1.98e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAEHVQQIKEHGLQANfngkEVEAKLPIVLQSEVEKEDQVDLIILFTKA 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLE----DGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  81 MQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQNLgDGKEAAA 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 161 KKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVPE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488220706 241 VIAHCESCFdpETIGLHYPSMYQDLIKNHRlTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKEDSLNVK 312
Cdd:PRK06522 236 VREYVRQVI--QKTAANTSSMLQDLEAGRP-TEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-306 1.80e-96

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: 287.14  E-value: 1.80e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAeHVQQIKEHGLQANF-NGKEVEAKLPIVlqSEVEKEDQVDLIILFTK 79
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVARGA-HAEALRENGLRLESpDGDRTTVPVPAV--TDPEELGPADLVLVAVK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  80 AMQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQNLGDGKEAA 159
Cdd:COG1893   78 AYDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 160 AKKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVP 239
Cdd:COG1893  158 LEALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPED 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488220706 240 EVIAHCESCFdpETIGLHYPSMYQDlIKNHRLTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKE 306
Cdd:COG1893  238 DLEERVAAVA--EATADNRSSMLQD-LEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALE 301
PRK12921 PRK12921
oxidoreductase;
1-307 1.05e-81

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 249.39  E-value: 1.05e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIdGWAEHVQQIKEHGLQANFNGKEVEAKLPIVLQSEvEKEDQVDLIILFTKA 80
Cdd:PRK12921   1 MRIAVVGAGAVGGTFGGRLLEAGRDVTFL-VRPKRAKALRERGLVIRSDHGDAVVPGPVITDPE-ELTGPFDLVILAVKA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  81 MQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQNLGDGKEAAA 160
Cdd:PRK12921  79 YQLDAAIPDLKPLVGEDTVIIPLQNGIGQLEQLEPYFGRERVLGGVVFISAQLNGDGVVVQRADHRLTFGEIPGQRSERT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 161 KKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVPE 240
Cdd:PRK12921 159 RAVRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGRATVGGILSRPGGRDLARALLRECLAVARAEGAPLRDDV 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488220706 241 VIAHCEscFDPETIGLHYPSMYQDLIKNHRLtEIDYINGAISRKGKKYGVATPYCDFLTELVHAKED 307
Cdd:PRK12921 239 VEEIVK--IFAGAPGDMKTSMLRDMEKGRPL-EIDHLQGVLLRRARAHGIPTPILDTVYALLKAYEA 302
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-306 7.39e-80

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: 244.13  E-value: 7.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   10 AMGSRFGLMLHQSGNEVLLIDGWaEHVQQIKEHGLQANFNGKEVEaKLPIVLQSEVEKEDQVDLIILFTKAMQLEKMLQD 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARG-EQLEALNQEGLRIVSLGGEFQ-FRPVSAATSPEELPPADLVIITVKAYQTEEAAAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   90 IQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQnLGDGKEAAAKKLADKLSE 169
Cdd:TIGR00745  79 LLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIG-DYVGENEAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  170 SGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVPEVIAHCESC- 248
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVi 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488220706  249 -FDPEtiglHYPSMYQDLIkNHRLTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKE 306
Cdd:TIGR00745 238 rMTAE----NTSSMLQDLL-RGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALE 291
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-150 5.21e-51

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: 165.48  E-value: 5.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706    3 IAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAEHVQqIKEHGLQANFNGKEVEAKLPIVLQSEVEKEDqVDLIILFTKAMQ 82
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAA-IKKNGLRLTSPGGERIVPPPAVTSASESLGP-IDLVIVTVKAYQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488220706   83 LEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQ 150
Cdd:pfam02558  79 TEEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITIG 146
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
 179-306 1.07e-28

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: 106.93  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  179 NIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVATIVNEFAKVAAVEKIELDVPEVIAHCESCFdpETIGLHY 258
Cdd:pfam08546   1 DIRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGVALSEDRLIEYVLAVL--RKTPDNK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 488220706  259 PSMYQDlIKNHRLTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKE 306
Cdd:pfam08546  79 SSMLQD-VEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
1-293 1.62e-19

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 86.94  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEV-LLIDGWAEHVQqikEHGLQAN-----FNGKEVEAklpivlQSEVEKEDQVDLI 74
Cdd:PRK06249   6 PRIGIIGTGAIGGFYGAMLARAGFDVhFLLRSDYEAVR---ENGLQVDsvhgdFHLPPVQA------YRSAEDMPPCDWV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  75 ILFTKAMQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIyIGntmwtaGL-------EGPGQVKLFGSGSV 147
Cdd:PRK06249  77 LVGLKTTANALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAEHL-LG------GLcficsnrVGPGVIHHLAYGRV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 148 elqNLG--------DGKEAAAKKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGKTSTAHKMVA 219
Cdd:PRK06249 150 ---NLGyhsgpaadDGITARVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNASTDPLMADPDSRALIR 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488220706 220 TIVNEFakVAAVEKIELDVPEVIAhcESCFD-PETIGLHYPSMYQDLIKNHRLtEIDYINGAISRKGKKYGVATP 293
Cdd:PRK06249 227 ALMAEV--IQGAAACGHTLPEGYA--DHMLAvTERMPDYRPSMYHDFEEGRPL-ELEAIYANPLAAARAAGCAMP 296
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
1-304 3.48e-18

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 83.22  E-value: 3.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAEHVQQIKEHG-----LQANFNGKEVEAKLPivlqsevEKEDQVDLII 75
Cdd:PRK05708   3 MTWHILGAGSLGSLWACRLARAGLPVRLILRDRQRLAAYQQAGgltlvEQGQASLYAIPAETA-------DAAEPIHRLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  76 LFTKAMQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGsvelQN-LGD 154
Cdd:PRK05708  76 LACKAYDAEPAVASLAHRLAPGAELLLLQNGLGSQDAVAARVPHARCIFASSTEGAFRDGDWRVVFAGHG----FTwLGD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 155 GKEAAAKKLADKLSESGLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELgktsTAHKM-VATIVNEFAKV----- 228
Cdd:PRK05708 152 PRNPTAPAWLDDLREAGIPHEWTVDILTRLWRKLALNCAINPLTVLHDCRNGGL----LEHAQeVAALCAELSELlrrcg 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488220706 229 --AAVEKIELDVPEVIahcescfdpETIGLHYPSMYQDlIKNHRLTEIDYINGAISRKGKKYGVATPYCDFLTELVHA 304
Cdd:PRK05708 228 qpAAAANLHEEVQRVI---------QATAANYSSMYQD-VRAGRRTEISYLLGYACRAADRHGLPLPRLQHLQQRLVA 295
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
 1-306 1.18e-15

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 76.19  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIdGWAEHVQQIKEHGLQ-ANFNGKEVEAKLP-IVLQSEVEKEDQVDLIILFT 78
Cdd:PRK08229   3 ARICVLGAGSIGCYLGGRLAAAGADVTLI-GRARIGDELRAHGLTlTDYRGRDVRVPPSaIAFSTDPAALATADLVLVTV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706  79 KAMQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVKLFGSGSVELQNlgdgkEA 158
Cdd:PRK08229  82 KSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMVPFNVISRGPGAFHQGTSGALAIEA-----SP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 159 AAKKLADKLSESGLNAHFSDNIHYSIYRKACVNgTMNGLCTILDVNM-AELGKTSTaHKMVATIVNEFAKVAAVEKIE-- 235
Cdd:PRK08229 157 ALRPFAAAFARAGLPLVTHEDMRAVQWAKLLLN-LNNAVNALSGLPLkEELAQRSY-RRCLALAQREALRVLKAAGIRpa 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706 236 -------------LDVPE----VIAHCESCFDPETiglhYPSMYQDLIKnHRLTEIDYINGAISRKGKKYGVATPYCDFL 298
Cdd:PRK08229 235 rltplppawiprlLRLPDplfrRLAGRMLAIDPLA----RSSMSDDLAA-GRATEIDWINGEIVRLAGRLGAPAPVNARL 309


                 ....*...
gi 488220706 299 TELVHAKE 306
Cdd:PRK08229 310 CALVHEAE 317
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 1-107 9.01e-07

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: 49.65  E-value: 9.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLidgWA---EHVQQIKEHGLQANFNGkevEAKLP--IVLQSEVEKE-DQVDLI 74
Cdd:COG0240    1 MKIAVLGAGSWGTALAKVLARNGHEVTL---WGrdpEVAEEINETRENPRYLP---GVKLPenLRATSDLEEAlAGADLV 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488220706  75 ILFTKAMQLEKMLQDIQSLIKKDTEVLCLLNGI 107
Cdd:COG0240   75 LLAVPSQALREVLEQLAPLLPPGAPVVSATKGI 107
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
1-118 7.02e-05

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


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 43.90  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLidgWA---EHVQQIKEHglqanfngKEVEAKLP-IVLQSEVEKE-------D 69
Cdd:PRK00094   2 MKIAVLGAGSWGTALAIVLARNGHDVTL---WArdpEQAAEINAD--------RENPRYLPgIKLPDNLRATtdlaealA 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488220706  70 QVDLIILFTKAMQLEKMLQDIQSLIKKDTEVLCLLNGIGHE------DIIEKFVP 118
Cdd:PRK00094  71 DADLILVAVPSQALREVLKQLKPLLPPDAPIVWATKGIEPGtgkllsEVLEEELP 125
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-46 3.06e-04

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 41.59  E-value: 3.06e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSGNEVLLIDGWAEHVQQIKEHGLQA 46
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLV 141
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-116 1.81e-03

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: 39.28  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRF-GLMLHQ--SGNEVLLIDGWAEHVQQIKE-HGLQANFNGKEVEAklpivlqsevekedQVDLIIL 76
Cdd:COG0345    3 MKIGFIGAGNMGSAIiKGLLKSgvPPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAA--------------QADVVVL 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488220706  77 FTKAMQLEKMLQDIQSLIKKDTEVLCLLNGIGHEDIIEKF 116
Cdd:COG0345   69 AVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLATLEEAL 108
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-98 1.89e-03

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: 39.34  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488220706   1 MKIAIAGAGAMGSRFGLMLHQSG--NEVLLIDGWAEHVQQIKEHGLqanfnGKEVEAKLPIVLQsevekedQVDLIILFT 78
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLERALELGV-----IDRAATDLEEAVA-------DADLVVLAV 69

                         90       100
                 ....*....|....*....|
gi 488220706  79 KAMQLEKMLQDIQSLIKKDT 98
Cdd:COG0287   70 PVGATIEVLAELAPHLKPGA 89
 
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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