Reviewed,
UniProtKB/Swiss-Prot Q8X5T5 (ACSA_ECO57)
Last modified
February 9, 2010.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acetyl-coenzyme A synthetase EC=6.2.1.1 Alternative name(s): Acetate--CoA ligase Acyl-activating enzyme | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 652 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates cheY, the response regulator involved in flagellar movement and chemotaxis By similarity. HAMAP MF_01123 |
| Catalytic activity | ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP MF_01123 |
| Post-translational modification | Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP MF_01123 |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | AMP binding Inferred from electronic annotation. Source: InterPro ATP bindingInferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 652 | 652 | Acetyl-coenzyme A synthetase HAMAP MF_01123 | PRO_0000208364 | |||||
Sites | |||||||||
| Active site | 517 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 609 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG59267.1. BA000007 Genomic DNA. Translation: BAB38474.1. |
| PIR | C91260. G86100. |
| RefSeq | NP_290702.1. NP_313078.1. |
3D structure databases | |
| SMR | Q8X5T5. Positions 5-647. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 914284. 960055. |
| GenomeReviews | Gene locus Z5668 in contig AE005174_GR. Gene locus ECs5051 in contig BA000007_GR. |
| KEGG | ece:Z5668. ecs:ECs5051. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG547964. |
| OMA | TRVKNTS. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS5051-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01123. Ac_CoA_synth. [Tree] |
| InterPro | IPR011904. Ac_CoA_lig_AcsA. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view] |
| Pfam | PF00501. AMP-binding. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02188. Ac_CoA_lig_AcsA. 1 hit. |
| PROSITE | PS00455. AMP_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACSA_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8X5T5 | ||||||||
| 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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