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Conserved domains on  [gi|545594361|ref|WP_021722833|]
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MULTISPECIES: 2-dehydropantoate 2-reductase [Lactococcus]

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 1.35e-125

2-dehydropantoate 2-reductase; Reviewed


:

Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 361.09  E-value: 1.35e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIDGWPEHVKAIKEHGLRANyngeELTAHLSVELQSEISSKEKTDLIILFTKA 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLE----DGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  81 MQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLiSGEEETA 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 161 KKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545594361 241 VVQHVETCFDpsTIGLHYPSMYQDLIKNNRlTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKEELLKAK 312
Cdd:PRK06522 236 VREYVRQVIQ--KTAANTSSMLQDLEAGRP-TEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-312 1.35e-125

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 361.09  E-value: 1.35e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIDGWPEHVKAIKEHGLRANyngeELTAHLSVELQSEISSKEKTDLIILFTKA 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLE----DGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  81 MQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLiSGEEETA 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 161 KKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545594361 241 VVQHVETCFDpsTIGLHYPSMYQDLIKNNRlTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKEELLKAK 312
Cdd:PRK06522 236 VREYVRQVIQ--KTAANTSSMLQDLEAGRP-TEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-307 3.77e-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: 291.38  E-value: 3.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIdGWPEHVKAIKEHGLRANYNGEELTAHlSVELQSEISSKEKTDLIILFTKA 80
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLV-ARGAHAEALRENGLRLESPDGDRTTV-PVPAVTDPEELGPADLVLVAVKA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  81 MQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLISGEEETA 160
Cdd:COG1893   79 YDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSERL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 161 KKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAE 240
Cdd:COG1893  159 EALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDD 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545594361 241 VVQHVETCFDPStiGLHYPSMYQDlIKNNRLTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKEE 307
Cdd:COG1893  239 LEERVAAVAEAT--ADNRSSMLQD-LEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEA 302
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-307 8.68e-79

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: 241.44  E-value: 8.68e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   10 AMGSRFGLMLHKGGNEVTLIDGWpEHVKAIKEHGLRANYNGEELTaHLSVELQSEISSKEKTDLIILFTKAMQLDKMLQD 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARG-EQLEALNQEGLRIVSLGGEFQ-FRPVSAATSPEELPPADLVIITVKAYQTEEAAAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   90 IKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLiSGEEETAKKLAEILSE 169
Cdd:TIGR00745  79 LLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGDY-VGENEAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  170 SGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAEVVQHVETCF 249
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVI 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 545594361  250 DPStiGLHYPSMYQDLIkNNRLTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKEE 307
Cdd:TIGR00745 238 RMT--AENTSSMLQDLL-RGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEA 292
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-150 5.99e-53

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: 170.49  E-value: 5.99e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361    3 ITIAGAGAMGSRFGLMLHKGGNEVTLIDGWPEHVkAIKEHGLRANYNGEELTAHLSVELQSEiSSKEKTDLIILFTKAMQ 82
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELA-AIKKNGLRLTSPGGERIVPPPAVTSAS-ESLGPIDLVIVTVKAYQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545594361   83 LDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQ 150
Cdd:pfam02558  79 TEEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITIG 146
 
Name Accession Description Interval E-value
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-312 1.35e-125

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 361.09  E-value: 1.35e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIDGWPEHVKAIKEHGLRANyngeELTAHLSVELQSEISSKEKTDLIILFTKA 80
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLE----DGEITVPVLAADDPAELGPQDLVILAVKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  81 MQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLiSGEEETA 160
Cdd:PRK06522  77 YQLPAALPSLAPLLGPDTPVLFLQNGVGHLEELAAYIGPERVLGGVVTHAAELEGPGVVRHTGGGRLKIGEP-DGESAAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 161 KKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAE 240
Cdd:PRK06522 156 EALADLLNAAGLDVEWSPDIRTEIWRKLWVNCVINPLTALLGCTNGELLADPDYRALIRALMEEVAAVAEAEGVHLSVEE 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545594361 241 VVQHVETCFDpsTIGLHYPSMYQDLIKNNRlTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKEELLKAK 312
Cdd:PRK06522 236 VREYVRQVIQ--KTAANTSSMLQDLEAGRP-TEIDAIVGYVLRRGRKHGIPTPLNDALYGLLKAKESERGLY 304
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-307 3.77e-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: 291.38  E-value: 3.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIdGWPEHVKAIKEHGLRANYNGEELTAHlSVELQSEISSKEKTDLIILFTKA 80
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLV-ARGAHAEALRENGLRLESPDGDRTTV-PVPAVTDPEELGPADLVLVAVKA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  81 MQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLISGEEETA 160
Cdd:COG1893   79 YDLEAAAEALAPLLGPDTVVLSLQNGLGHEERLAEALGAERVLGGVVTIGATREEPGVVRHTGGGRLVLGELDGGPSERL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 161 KKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAE 240
Cdd:COG1893  159 EALAELLEAAGIPVEVSDDIRGALWEKLLLNAAINPLTALTGAPNGELLADPEARALARALMREVLAVARAEGVPLPEDD 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545594361 241 VVQHVETCFDPStiGLHYPSMYQDlIKNNRLTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKEE 307
Cdd:COG1893  239 LEERVAAVAEAT--ADNRSSMLQD-LEAGRPTEIDAINGAVVRLARRLGVPTPVNEALYALLKALEA 302
PRK12921 PRK12921
oxidoreductase;
1-309 4.71e-85

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 257.86  E-value: 4.71e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIdGWPEHVKAIKEHGLRANYNGEELTAHLSVELQSEiSSKEKTDLIILFTKA 80
Cdd:PRK12921   1 MRIAVVGAGAVGGTFGGRLLEAGRDVTFL-VRPKRAKALRERGLVIRSDHGDAVVPGPVITDPE-ELTGPFDLVILAVKA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  81 MQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLISGEEETA 160
Cdd:PRK12921  79 YQLDAAIPDLKPLVGEDTVIIPLQNGIGQLEQLEPYFGRERVLGGVVFISAQLNGDGVVVQRADHRLTFGEIPGQRSERT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 161 KKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAE 240
Cdd:PRK12921 159 RAVRDALAGARLEVVLSENIRQDIWRKLLFNAVMNGMTALGRATVGGILSRPGGRDLARALLRECLAVARAEGAPLRDDV 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545594361 241 VVQHVETcfDPSTIGLHYPSMYQDLIKnNRLTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKEELL 309
Cdd:PRK12921 239 VEEIVKI--FAGAPGDMKTSMLRDMEK-GRPLEIDHLQGVLLRRARAHGIPTPILDTVYALLKAYEAGP 304
apbA_panE TIGR00745
2-dehydropantoate 2-reductase; This model describes enzymes that perform as 2-dehydropantoate ...
 10-307 8.68e-79

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: 241.44  E-value: 8.68e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   10 AMGSRFGLMLHKGGNEVTLIDGWpEHVKAIKEHGLRANYNGEELTaHLSVELQSEISSKEKTDLIILFTKAMQLDKMLQD 89
Cdd:TIGR00745   1 AVGSLYGAYLARAGHDVTLLARG-EQLEALNQEGLRIVSLGGEFQ-FRPVSAATSPEELPPADLVIITVKAYQTEEAAAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   90 IKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLiSGEEETAKKLAEILSE 169
Cdd:TIGR00745  79 LLPLIGKNTKVLFLQNGLGHEERLRELLPARRILGGVVTHGAVREEPGVVHHAGLGATKIGDY-VGENEAVEALAELLNE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  170 SGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAEVVQHVETCF 249
Cdd:TIGR00745 158 AGIPAELHGDILAAIWKKLLVNAAINPLTALLDCKNGELLENPEARELLRRLMDEVVRVARAEGVDLPDDEVEELVRAVI 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 545594361  250 DPStiGLHYPSMYQDLIkNNRLTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKEE 307
Cdd:TIGR00745 238 RMT--AENTSSMLQDLL-RGRRTEIDAINGAVVRLAEKLGIDAPVNRTLYALLKALEA 292
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-150 5.99e-53

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: 170.49  E-value: 5.99e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361    3 ITIAGAGAMGSRFGLMLHKGGNEVTLIDGWPEHVkAIKEHGLRANYNGEELTAHLSVELQSEiSSKEKTDLIILFTKAMQ 82
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELA-AIKKNGLRLTSPGGERIVPPPAVTSAS-ESLGPIDLVIVTVKAYQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545594361   83 LDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQ 150
Cdd:pfam02558  79 TEEALEDIAPLLGPNTVVLLLQNGLGHEEVLREAVPRERVLGGVTTHGAFREGPGHVHHAGPGRITIG 146
ApbA_C pfam08546
Ketopantoate reductase PanE/ApbA C terminal; This is a family of 2-dehydropantoate ...
 179-306 2.52e-29

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: 108.47  E-value: 2.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  179 NIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFENVNLDIAEVVQHVETCFDpsTIGLHY 258
Cdd:pfam08546   1 DIRLARWEKLLVNAAINPLTALTGCTNGELLDSPEARALIRALMREAVAVAQAEGVALSEDRLIEYVLAVLR--KTPDNK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 545594361  259 PSMYQDlIKNNRLTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHSKE 306
Cdd:pfam08546  79 SSMLQD-VEAGRPTEIDYINGYVVRLARKHGVPTPTNETLYALLKAKE 125
PRK08229 PRK08229
2-dehydropantoate 2-reductase; Provisional
 1-306 1.74e-13

2-dehydropantoate 2-reductase; Provisional


Pssm-ID: 236193 [Multi-domain]  Cd Length: 341  Bit Score: 70.03  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIdGWPEHVKAIKEHGLR-ANYNGEELT-AHLSVELQSEISSKEKTDLIILFT 78
Cdd:PRK08229   3 ARICVLGAGSIGCYLGGRLAAAGADVTLI-GRARIGDELRAHGLTlTDYRGRDVRvPPSAIAFSTDPAALATADLVLVTV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  79 KAMQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKaklFGDGSVelQNLISGEEE 158
Cdd:PRK08229  82 KSAATADAAAALAGHARPGAVVVSFQNGVRNADVLRAALPGATVLAGMVPFNVISRGPGA---FHQGTS--GALAIEASP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 159 TAKKLAEILSESGLN------------AKYSNNIHYSI----------------YRKaCVNGTMNGLCTILDT---NMAG 207
Cdd:PRK08229 157 ALRPFAAAFARAGLPlvthedmravqwAKLLLNLNNAVnalsglplkeelaqrsYRR-CLALAQREALRVLKAagiRPAR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 208 LGETKPAhdMVVTIVN----EFAAVAkfeNVNLDIaevvqhvetcfDPstigLHYPSMYQDLIKnNRLTEIDYINGAVSR 283
Cdd:PRK08229 236 LTPLPPA--WIPRLLRlpdpLFRRLA---GRMLAI-----------DP----LARSSMSDDLAA-GRATEIDWINGEIVR 294

                        330       340
                 ....*....|....*....|...
gi 545594361 284 KGKKYKVATPYCDFLTQLVHSKE 306
Cdd:PRK08229 295 LAGRLGAPAPVNARLCALVHEAE 317
PRK06249 PRK06249
putative 2-dehydropantoate 2-reductase;
1-301 1.45e-12

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 180488 [Multi-domain]  Cd Length: 313  Bit Score: 66.91  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVT-LIDGWPEHVkaiKEHGLRAN-YNGEELTAHlsVELQSEISSKEKTDLIILFT 78
Cdd:PRK06249   6 PRIGIIGTGAIGGFYGAMLARAGFDVHfLLRSDYEAV---RENGLQVDsVHGDFHLPP--VQAYRSAEDMPPCDWVLVGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  79 KAMQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNL-----I 153
Cdd:PRK06249  81 KTTANALLAPLIPQVAAPDAKVLLLQNGLGVEEQLREILPAEHLLGGLCFICSNRVGPGVIHHLAYGRVNLGYHsgpaaD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 154 SGEEETAKKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGETKPAHDMVVTIVNEFAAVAKFEN 233
Cdd:PRK06249 161 DGITARVEEGAALFRAAGIDSQAMPDLAQARWQKLVWNIPYNGLSVLLNASTDPLMADPDSRALIRALMAEVIQGAAACG 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545594361 234 VNLD---IAEVVQHVETCFDpstiglHYPSMYQDLIKnNRLTEIDYINGAVSRKGKKYKVATPYCDFLTQL 301
Cdd:PRK06249 241 HTLPegyADHMLAVTERMPD------YRPSMYHDFEE-GRPLELEAIYANPLAAARAAGCAMPRVEMLYQA 304
PRK05708 PRK05708
putative 2-dehydropantoate 2-reductase;
1-304 3.38e-12

putative 2-dehydropantoate 2-reductase;


Pssm-ID: 235572 [Multi-domain]  Cd Length: 305  Bit Score: 65.89  E-value: 3.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIDGWPEHVKAIKEHG-LRANYNGEelTAHLSVELQSEiSSKEKTDLIILFTK 79
Cdd:PRK05708   3 MTWHILGAGSLGSLWACRLARAGLPVRLILRDRQRLAAYQQAGgLTLVEQGQ--ASLYAIPAETA-DAAEPIHRLLLACK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361  80 AMQLDKMLQDIKPLIDEHTKVLCLLNGIGHEDTIEKYVSKNNIFIGNTMWTAGLEGPGKAKLFGDGSVELQNLISGeeeT 159
Cdd:PRK05708  80 AYDAEPAVASLAHRLAPGAELLLLQNGLGSQDAVAARVPHARCIFASSTEGAFRDGDWRVVFAGHGFTWLGDPRNP---T 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361 160 AKKLAEILSESGLNAKYSNNIHYSIYRKACVNGTMNGLCTILDTNMAGLGEtkpAHDMVVTIVNEFAAV-------AKFE 232
Cdd:PRK05708 157 APAWLDDLREAGIPHEWTVDILTRLWRKLALNCAINPLTVLHDCRNGGLLE---HAQEVAALCAELSELlrrcgqpAAAA 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545594361 233 NVNLDIAEVVQhvetcfdpsTIGLHYPSMYQDlIKNNRLTEIDYINGAVSRKGKKYKVATPYCDFLTQLVHS 304
Cdd:PRK05708 234 NLHEEVQRVIQ---------ATAANYSSMYQD-VRAGRRTEISYLLGYACRAADRHGLPLPRLQHLQQRLVA 295
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 1-107 2.23e-08

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: 54.66  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLidgW---PEHVKAIKEHGLRANY-NGEELTAHLSV--ELQSEIsskEKTDLI 74
Cdd:COG0240    1 MKIAVLGAGSWGTALAKVLARNGHEVTL---WgrdPEVAEEINETRENPRYlPGVKLPENLRAtsDLEEAL---AGADLV 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 545594361  75 ILFTKAMQLDKMLQDIKPLIDEHTKVLCLLNGI 107
Cdd:COG0240   75 LLAVPSQALREVLEQLAPLLPPGAPVVSATKGI 107
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
1-107 4.62e-06

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


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 47.37  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLidgW---PEHVKAIKEHGLRANY-NGEELTAHLSVE--LQSEISSKektDLI 74
Cdd:PRK00094   2 MKIAVLGAGSWGTALAIVLARNGHDVTL---WardPEQAAEINADRENPRYlPGIKLPDNLRATtdLAEALADA---DLI 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 545594361  75 ILFTKAMQLDKMLQDIKPLIDEHTKVLCLLNGI 107
Cdd:PRK00094  76 LVAVPSQALREVLKQLKPLLPPDAPIVWATKGI 108
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-120 5.12e-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: 46.98  E-value: 5.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRF-GLMLHKG--GNEVTLIDGWPEHVKAIKE-HGLRANYNGEELTAhlsvelqseisskeKTDLIIL 76
Cdd:COG0345    3 MKIGFIGAGNMGSAIiKGLLKSGvpPEDIIVSDRSPERLEALAErYGVRVTTDNAEAAA--------------QADVVVL 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 545594361  77 FTKAMQLDKMLQDIKPLIDEHTKVLCLLNGIGHEdTIEKYVSKN 120
Cdd:COG0345   69 AVKPQDLAEVLEELAPLLDPDKLVISIAAGVTLA-TLEEALGGG 111
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-46 3.87e-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: 3.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGGNEVTLIDGWPEHVKAIKEHGLRA 46
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLV 141
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-98 1.36e-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: 39.72  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594361   1 MRITIAGAGAMGSRFGLMLHKGG--NEVTLIDGWPEHVKAIKEHGLranynGEELTAHLSVELqseisskEKTDLIILFT 78
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLERALELGV-----IDRAATDLEEAV-------ADADLVVLAV 69

                         90       100
                 ....*....|....*....|
gi 545594361  79 KAMQLDKMLQDIKPLIDEHT 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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