Reviewed,
UniProtKB/Swiss-Prot Q8KBY0 (ACSA_CHLTE)
Last modified
June 16, 2009.
Version 39.
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 | Chlorobium tepidum [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1097 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum |
Protein attributes
| Sequence length | 659 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 – 659 | 659 | Acetyl-coenzyme A synthetase HAMAP MF_01123 | PRO_0000208360 | |||||
Sites | |||||||||
| Active site | 529 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 621 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS. |
Cross-references
Sequence databases | |
|---|---|
| AE006470 Genomic DNA. Translation: AAM72877.1. | |
| RefSeq | NP_662535.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PG4 based on UniProtKB Q8ZKF6. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1006138. |
| GenomeReviews | Gene locus CT1652 in contig AE006470_GR. |
| KEGG | cte:CT1652. |
| NMPDR | fig|194439.1.peg.1629. |
| TIGR | CT1652. |
Phylogenomic databases | |
| HOGENOM | Q8KBY0. |
Enzyme and pathway databases | |
| BioCyc | CTEP194439:CT_1652-MON. |
| BRENDA | 6.2.1.1. 189605. |
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_CHLTE | ||||||||
| Accession | Primary (citable) accession number: Q8KBY0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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