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ECOLI:PFLA
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | pflA (synonyms: act) | |
| Protein Name(s) | Pyruvate formate-lyase 1-activating enzyme
Formate-C-acetyltransferase-activating enzyme 1 PFL-activating enzyme 1 | |
| External Links | ||
| UniProt | P0A9N4 | |
| EMBL | X08035 U00096 AP009048 | |
| PIR | S01789 | |
| RefSeq | NP_415422.1 YP_489174.1 | |
| PDB | 3C8F 3CB8 | |
| PDBsum | 3C8F 3CB8 | |
| ProteinModelPortal | P0A9N4 | |
| SMR | P0A9N4 | |
| DIP | DIP-35915N | |
| IntAct | P0A9N4 | |
| STRING | 511145.b0902 | |
| PaxDb | P0A9N4 | |
| PRIDE | P0A9N4 | |
| EnsemblBacteria | AAC73988 BAA35637 | |
| GeneID | 12930359 945517 | |
| KEGG | ecj:Y75_p0874 eco:b0902 | |
| PATRIC | 32117017 | |
| EchoBASE | EB0027 | |
| EcoGene | EG10028 | |
| eggNOG | COG1180 | |
| HOGENOM | HOG000011458 | |
| InParanoid | P0A9N4 | |
| KO | K04069 | |
| OMA | CHNPDCR | |
| OrthoDB | EOG64FKHC | |
| PhylomeDB | P0A9N4 | |
| BioCyc | EcoCyc:PFLACTENZ-MONOMER ECOL316407:JW0885-MONOMER | |
| EvolutionaryTrace | P0A9N4 | |
| PRO | PR:P0A9N4 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0A9N4 | |
| GO | GO:0005737 GO:0051539 GO:0043365 GO:0046872 GO:0016491 GO:0006974 GO:0006006 | |
| InterPro | IPR006638 IPR012838 IPR001989 IPR007197 | |
| Pfam | PF04055 | |
| SMART | SM00729 | |
| TIGRFAMs | TIGR02493 | |
| PROSITE | PS01087 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0016491 |
oxidoreductase activity |
ECO:0000314 |
F |
Fig. 2 illustrates that the over-expression of PflA allows for greater use of iron-sulfur clusters in anaerobic environments. |
complete | |||||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006974 |
cellular response to DNA damage stimulus |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051539 |
4 iron, 4 sulfur cluster binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0043365 |
[formate-C-acetyltransferase]-activating enzyme activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0018307 |
enzyme active site formation |
ECO:0000314 |
direct assay 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:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0043365 |
[formate-C-acetyltransferase]-activating enzyme activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051536 |
iron-sulfur cluster binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051539 |
4 iron, 4 sulfur cluster binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0043365 |
[formate-C-acetyltransferase]-activating enzyme activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
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 | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051539 |
4 iron, 4 sulfur cluster binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0005975 |
carbohydrate metabolic 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 | |||
|
involved_in |
GO:0006006 |
glucose metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051536 |
iron-sulfur cluster binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Yang, J et al. (2009) The iron-sulfur cluster of pyruvate formate-lyase activating enzyme in whole cells: cluster interconversion and a valence-localized [4Fe-4S]2+ state. Biochemistry 48 9234-41 PubMed GONUTS page
- ↑ Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
- ↑ Külzer, R et al. (1998) Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form. J. Biol. Chem. 273 4897-903 PubMed GONUTS page
- ↑ 4.0 4.1 Conradt, H et al. (1984) Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: isolation and structural properties. Arch. Biochem. Biophys. 228 133-42 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
