O69635 (ACSA_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 78.
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 | Mycobacterium tuberculosis | ||||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 651 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 Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | cell wall Inferred from direct assay. Source: MTBBASE plasma membraneInferred from direct assay. Source: MTBBASE |
| 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 – 651 | 651 | Acetyl-coenzyme A synthetase HAMAP MF_01123 | PRO_0000208369 | |||||
Sites | |||||||||
| Active site | 525 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 617 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842583 Genomic DNA. Translation: CAA17989.1. AE000516 Genomic DNA. Translation: AAK48135.1. |
| PIR | D70789. |
| RefSeq | NP_218184.1. NC_000962.2. NP_338321.1. NC_002755.2. |
3D structure databases | |
| ProteinModelPortal | O69635. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000001628; EBMYCP00000001628; EBMYCG00000001628. EBMYCT00000071474; EBMYCP00000069533; EBMYCG00000071469. |
| GeneID | 885479. 922721. |
| GenomeReviews | Gene locus MT3768 in contig AE000516_GR. Gene locus Rv3667 in contig AL123456_GR. |
| KEGG | mtc:MT3768. mtu:Rv3667. |
| PATRIC | 18130050. VBIMycTub22151_4118. |
| TIGR | MT3768. |
Organism-specific databases | |
| TubercuList | Rv3667. |
Phylogenomic databases | |
| GeneTree | EBGT00050000015141. |
| HOGENOM | HBG547964. |
| OMA | HQRMVDT. |
| PhylomeDB | O69635. |
| 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_MYCTU | ||||||||
| Accession | Primary (citable) accession number: O69635 | ||||||||
| 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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