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ECOLI:ACCC
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | accC (synonyms: fabG) | |
| Protein Name(s) | Biotin carboxylase
Acetyl-CoA carboxylase subunit A ACC | |
| External Links | ||
| UniProt | P24182 | |
| EMBL | M79446 M80458 M83198 U18997 U00096 AP009048 M32214 | |
| PIR | JS0632 | |
| RefSeq | NP_417722.1 YP_491438.1 | |
| PDB | 1BNC 1DV1 1DV2 1K69 2GPS 2GPW 2J9G 2V58 2V59 2V5A 2VR1 2W6M 2W6N 2W6O 2W6P 2W6Q 2W6Z 2W70 2W71 3G8C 3G8D 3JZF 3JZI 3RUP 3RV3 3RV4 4HR7 | |
| PDBsum | 1BNC 1DV1 1DV2 1K69 2GPS 2GPW 2J9G 2V58 2V59 2V5A 2VR1 2W6M 2W6N 2W6O 2W6P 2W6Q 2W6Z 2W70 2W71 3G8C 3G8D 3JZF 3JZI 3RUP 3RV3 3RV4 4HR7 | |
| ProteinModelPortal | P24182 | |
| SMR | P24182 | |
| DIP | DIP-9035N | |
| IntAct | P24182 | |
| MINT | MINT-1266968 | |
| STRING | 511145.b3256 | |
| BindingDB | P24182 | |
| PaxDb | P24182 | |
| PRIDE | P24182 | |
| EnsemblBacteria | AAC76288 BAE77297 | |
| GeneID | 12933462 947761 | |
| KEGG | ecj:Y75_p3174 eco:b3256 | |
| PATRIC | 32121942 | |
| EchoBASE | EB0272 | |
| EcoGene | EG10276 | |
| eggNOG | COG0439 | |
| HOGENOM | HOG000008988 | |
| InParanoid | P24182 | |
| KO | K01961 | |
| OMA | ERCANAC | |
| OrthoDB | EOG6CVV6Z | |
| PhylomeDB | P24182 | |
| BioCyc | EcoCyc:BIOTIN-CARBOXYL-MONOMER ECOL316407:JW3224-MONOMER MetaCyc:BIOTIN-CARBOXYL-MONOMER RETL1328306-WGS:GSTH-1922-MONOMER | |
| SABIO-RK | P24182 | |
| UniPathway | UPA00655 | |
| EvolutionaryTrace | P24182 | |
| PRO | PR:P24182 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P24182 | |
| GO | GO:0005737 GO:0003989 GO:0005524 GO:0004075 GO:0046872 GO:0006633 GO:2001295 GO:0045717 | |
| Gene3D | 3.30.1490.20 3.30.470.20 3.40.50.20 | |
| InterPro | IPR004549 IPR011761 IPR013815 IPR013816 IPR011764 IPR005482 IPR005481 IPR005479 IPR016185 IPR011054 | |
| Pfam | PF02785 PF00289 PF02786 | |
| SMART | SM00878 | |
| SUPFAM | SSF51246 SSF52440 | |
| TIGRFAMs | TIGR00514 | |
| PROSITE | PS50975 PS50979 PS00866 PS00867 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
involved_in |
GO:0045717 |
negative regulation of fatty acid biosynthetic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006633 |
fatty acid biosynthetic process |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
EcoliWiki:accA |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000305 |
curator inference used in manual assertion |
GO:0004075 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004075 |
biotin carboxylase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006633 |
fatty acid biosynthetic 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 | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016874 |
ligase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003989 |
acetyl-CoA carboxylase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
| GO:0016879 |
ligase activity, forming carbon-nitrogen bonds |
ECO:0000314 |
F |
Table 1 and Experimental Procedure. Biotin carboxylase was purified and crystallized (Fig 1.). Biotin carboxylase activity was determined by 14C-bicarbonate fixation and spectrophotometric assay for 14C-labeled carboxybiotin. Biotin carboxylase activity involves forming a bond between an N on biotin and the C in HCO3-. |
complete | |||||
|
enables |
GO:0004075 |
biotin carboxylase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016874 |
ligase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006633 |
fatty acid biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006631 |
fatty acid metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006629 |
lipid metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:2001295 |
malonyl-CoA biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniPathway:UPA00655 |
P |
Seeded From UniProt |
complete | ||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Abdel-Hamid, AM & Cronan, JE (2007) Coordinate expression of the acetyl coenzyme A carboxylase genes, accB and accC, is necessary for normal regulation of biotin synthesis in Escherichia coli. J. Bacteriol. 189 369-76 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 Davis, MS et al. (2000) Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli. J. Biol. Chem. 275 28593-8 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 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
- ↑ Guchhait, RB et al. (1974) Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components. J. Biol. Chem. 249 6633-45 PubMed GONUTS page
