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ECOLI:POXB
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | poxB | |
| Protein Name(s) | Pyruvate dehydrogenase [ubiquinone]
Pyruvate oxidase POX Alpha-peptide | |
| External Links | ||
| UniProt | P07003 | |
| EMBL | X04105 U00096 AP009048 S73268 M28208 L47688 L47689 L47690 L47691 L47692 L47693 L47694 L47695 | |
| PIR | A23648 | |
| RefSeq | NP_415392.1 YP_489144.1 | |
| PDB | 3EY9 3EYA | |
| PDBsum | 3EY9 3EYA | |
| ProteinModelPortal | P07003 | |
| SMR | P07003 | |
| DIP | DIP-36216N | |
| IntAct | P07003 | |
| ChEMBL | CHEMBL3380 | |
| DrugBank | DB00336 | |
| SWISS-2DPAGE | P07003 | |
| PRIDE | P07003 | |
| EnsemblBacteria | AAC73958 BAA35585 | |
| GeneID | 12933107 946132 | |
| KEGG | ecj:Y75_p0844 eco:b0871 | |
| PATRIC | 32116949 | |
| EchoBASE | EB0747 | |
| EcoGene | EG10754 | |
| InParanoid | P07003 | |
| KO | K00156 | |
| OMA | SGYHAMM | |
| OrthoDB | EOG6C5RND | |
| PhylomeDB | P07003 | |
| BioCyc | EcoCyc:PYRUVOXID-MONOMER ECOL316407:JW0855-MONOMER MetaCyc:PYRUVOXID-MONOMER | |
| EvolutionaryTrace | P07003 | |
| PRO | PR:P07003 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P07003 | |
| GO | GO:0005829 GO:0005886 GO:0008289 GO:0000287 GO:0052737 GO:0030976 | |
| Gene3D | 3.40.50.1220 3.40.50.970 | |
| InterPro | IPR029035 IPR029061 IPR012000 IPR012001 IPR000399 IPR011766 | |
| Pfam | PF02775 PF00205 PF02776 | |
| SUPFAM | SSF52467 SSF52518 | |
| PROSITE | PS00187 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0047112 |
pyruvate oxidase activity |
ECO:0000314 |
F |
Figure 6 |
complete | |||||
|
part_of |
GO:0005829 |
cytosol |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0052737 |
pyruvate dehydrogenase (quinone) activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051289 |
protein homotetramerization |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0050660 |
flavin adenine dinucleotide binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0042867 |
pyruvate catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0030976 |
thiamine pyrophosphate binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008289 |
lipid binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006090 |
pyruvate metabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000287 |
magnesium ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000287 |
magnesium ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0030976 |
thiamine pyrophosphate binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR000399 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0052737 |
pyruvate dehydrogenase (quinone) activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008289 |
lipid binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Grabau, C et al. (1989) Lipid binding by Escherichia coli pyruvate oxidase is disrupted by small alterations of the carboxyl-terminal region. J. Biol. Chem. 264 12510-9 PubMed GONUTS page
- ↑ 2.0 2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
- ↑ Neumann, P et al. (2008) Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 105 17390-5 PubMed GONUTS page
- ↑ Chang, YY & Cronan, JE (1984) An Escherichia coli mutant deficient in pyruvate oxidase activity due to altered phospholipid activation of the enzyme. Proc. Natl. Acad. Sci. U.S.A. 81 4348-52 PubMed GONUTS page
- ↑ 5.0 5.1 Stevens, DJ & Gennis, RB (1980) Studies on the quaternary structure of Escherichia coli pyruvate oxidase. J. Biol. Chem. 255 379-83 PubMed GONUTS page
- ↑ Recny, MA & Hager, LP (1982) Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD. J. Biol. Chem. 257 12878-86 PubMed GONUTS page
- ↑ Abdel-Hamid, AM et al. (2001) Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli. Microbiology (Reading, Engl.) 147 1483-98 PubMed GONUTS page
- ↑ O'Brien, TA et al. (1977) Regulation by lipids of cofactor binding to a peripheral membrane enzyme: binding of thiamin pyrophosphate to pyruvate oxidase. Biochemistry 16 3105-9 PubMed GONUTS page
- ↑ Hamilton, SE et al. (1986) Identification of the high-affinity lipid binding site in Escherichia coli pyruvate oxidase. Biochemistry 25 8178-83 PubMed GONUTS page
- ↑ Chang, YY & Cronan, JE Jr (1983) Genetic and biochemical analyses of Escherichia coli strains having a mutation in the structural gene (poxB) for pyruvate oxidase. J. Bacteriol. 154 756-62 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Blake, R 2nd et al. (1982) Role of the divalent metal cation in the pyruvate oxidase reaction. J. Biol. Chem. 257 9605-11 PubMed GONUTS page
