A6VCI9 (A6VCI9_PSEA7) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 32.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Acetyl-coenzyme A synthetase 2 HAMAP MF_01123 EC=6.2.1.1 HAMAP MF_01123 | ||||||
| Gene names |
| ||||||
| Organism | Pseudomonas aeruginosa (strain PA7) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 381754 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 645 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. HAMAP MF_01123 |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding HAMAP MF_01123 Nucleotide-binding |
| Molecular function | Ligase HAMAP MF_01123 EMBL ABR81161.1 |
| PTM | Acetylation HAMAP MF_01123 |
| 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: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 514 | 1 | By similarity HAMAP MF_01123 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 606 | 1 | N6-acetyllysine By similarity HAMAP MF_01123 | ||||||
Sequences
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References
| [1] | Dodson R.J., Harkins D., Paulsen I.T. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000744 Genomic DNA. Translation: ABR81161.1. |
| RefSeq | YP_001350774.1. NC_009656.1. |
3D structure databases | |
| ProteinModelPortal | A6VCI9. |
| SMR | A6VCI9. Positions 7-642. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A6VCI9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5357784. |
| GenomeReviews | Gene locus PSPA7_5450 in contig CP000744_GR. |
| KEGG | pap:PSPA7_5450. |
| PATRIC | 19832395. VBIPseAer80442_5178. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0365. |
| HOGENOM | HBG547964. |
| OMA | IARTIWG. |
| PhylomeDB | A6VCI9. |
| 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 | A6VCI9_PSEA7 | ||||||||
| Accession | Primary (citable) accession number: A6VCI9 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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