Reviewed,
UniProtKB/Swiss-Prot Q1CUA3 (ACSA_HELPH)
Last modified
November 3, 2009.
Version 25.
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 HPAG1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 357544 [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_1000065293 | |||||
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 a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression." Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed: 16788065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000241 Genomic DNA. Translation: ABF84469.1. | |
| RefSeq | YP_627143.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1CUA3. |
Genome annotation databases | |
| GeneID | 4098779. |
| GenomeReviews | Gene locus HPAG1_0402 in contig CP000241_GR. |
| KEGG | hpa:HPAG1_0402. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q1CUA3. |
| OMA | HQRMVDT. |
Enzyme and pathway databases | |
| BioCyc | HPYL357544:HPAG1_0402-MON. |
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_HELPH | ||||||||
| Accession | Primary (citable) accession number: Q1CUA3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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