Reviewed,
UniProtKB/Swiss-Prot B5Z6E9 (ACSA_HELPG)
Last modified
November 3, 2009.
Version 11.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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 |
| ||||
| Organism | Helicobacter pylori (strain G27) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 563041 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter |
Protein attributes
| Sequence length | 662 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| 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. |
| 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 – 662 | 662 | Acetyl-coenzyme A synthetase HAMAP MF_01123 | PRO_1000137265 | |||||
Sites | |||||||||
| Active site | 527 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 623 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Helicobacter pylori strain G27." Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S., Ottemann K.M., Stein M., Salama N.R., Guillemin K. J. Bacteriol. 191:447-448(2009) [PubMed: 18952803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP001173 Genomic DNA. Translation: ACI27148.1. | |
| RefSeq | YP_002266014.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 6963271. |
| GenomeReviews | Gene locus HPG27_383 in contig CP001173_GR. |
| KEGG | hpg:HPG27_383. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | HQRMVDT. |
Family and domain databases | |
| HAMAP | MF_01123. [Tree] |
| InterPro | IPR011904. Ac_CoA_lig_AcsA. 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_HELPG | ||||||||
| Accession | Primary (citable) accession number: B5Z6E9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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