B3R1X2 (ACSA_CUPTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 29.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 164546 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus |
Protein attributes
| Sequence length | 660 AA. |
| Sequence status | Complete. |
| 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. 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) | |
| 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: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 660 | 660 | Acetyl-coenzyme A synthetase HAMAP MF_01123 | PRO_1000137262 | |||||
Sites | |||||||||
| Active site | 530 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 625 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia." Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C. Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: R1 / LMG 19424. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU633749 Genomic DNA. Translation: CAQ69969.1. |
| RefSeq | YP_002006032.1. NC_010528.1. |
3D structure databases | |
| ProteinModelPortal | B3R1X2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B3R1X2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6453493. |
| GenomeReviews | Gene locus RALTA_A2028 in contig CU633749_GR. |
| KEGG | cti:RALTA_A2028. |
| PATRIC | 21530682. VBICupTai42494_1989. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG547964. |
| OMA | VISVSGH. |
| ProtClustDB | PRK00174. |
Family and domain databases | |
| HAMAP | MF_01123. Ac_CoA_synth. [Tree] |
| InterPro | IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view] |
| KO | K01895. |
| PANTHER | PTHR24095:SF42. PTHR24095:SF42. 1 hit. |
| Pfam | PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 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_CUPTR | ||||||||
| Accession | Primary (citable) accession number: B3R1X2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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