Reviewed,
UniProtKB/Swiss-Prot P69452 (LCFA_ECOL6)
Last modified
January 19, 2010.
Version 33.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Long-chain-fatty-acid--CoA ligase EC=6.2.1.3 Alternative name(s): Long-chain acyl-CoA synthetase Short name=Acyl-CoA synthetase | ||||
| Gene names |
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| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 561 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids By similarity. |
| Catalytic activity | ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA. |
| Subunit structure | Homodimer Probable. |
| Subcellular location | Membrane; Peripheral membrane protein By similarity. Note: Partially membrane-associated By similarity. |
| Miscellaneous | Activity is the highest with fatty acid substrates of > 10 carbon atoms By similarity. |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism |
| Cellular component | Membrane |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-CoA ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014075 Genomic DNA. Translation: AAN80668.1. Different initiation. |
| PIR | S41589. E64941. |
| RefSeq | NP_754103.1. |
3D structure databases | |
| SMR | P69452. Positions 16-555. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1036653. |
| GenomeReviews | Gene locus c2209 in contig AE014075_GR. |
| KEGG | ecc:c2209. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG547964. |
| OMA | PGELCIK. |
Enzyme and pathway databases | |
| BRENDA | 6.2.1.3. 292881. |
Family and domain databases | |
| InterPro | IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view] |
| Pfam | PF00501. AMP-binding. 1 hit. [Graphical view] |
| PROSITE | PS00455. AMP_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LCFA_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P69452 Secondary accession number(s): P29212 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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