Q8KBY0 (ACSA_CHLTE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 64.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acetyl-coenzyme A synthetase Short name=AcCoA synthetase Short name=Acs EC=6.2.1.1 Alternative name(s): Acetate--CoA ligase Acyl-activating enzyme | ||||||
| Gene names |
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| Organism | Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 194439 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum ›  |
Protein attributes
| Sequence length | 659 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity. HAMAP-Rule MF_01123 |
| Catalytic activity | ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123 |
| Cofactor | Magnesium By similarity. |
| Post-translational modification | Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123 |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | acetyl-CoA biosynthetic process from acetate 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 metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| 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-Rule MF_01123 | PRO_0000208360 | |||||
Regions | |||||||||
| Region | 423 – 428 | 6 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 529 | 1 | By similarity | ||||||
| Metal binding | 549 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 551 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 554 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 323 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 347 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 399 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 512 | 1 | Substrate By similarity | ||||||
| Binding site | 527 | 1 | Substrate By similarity | ||||||
| Binding site | 535 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 538 | 1 | Substrate By similarity | ||||||
| Binding site | 596 | 1 | Coenzyme A | ||||||
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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE006470 Genomic DNA. Translation: AAM72877.1. |
| RefSeq | NP_662535.2. NC_002932.3. |
3D structure databases | |
| ProteinModelPortal | Q8KBY0. |
| SMR | Q8KBY0. Positions 23-656. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 194439.CT1652. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAM72877; AAM72877; CT1652. |
| GeneID | 1006138. |
| KEGG | cte:CT1652. |
| PATRIC | 21401177. VBIChlTep116050_1493. |
Phylogenomic databases | |
| eggNOG | COG0365. |
| HOGENOM | HOG000229981. |
| KO | K01895. |
| OMA | EDIYFCT. |
| ProtClustDB | PRK00174. |
Enzyme and pathway databases | |
| BioCyc | CTEP194439:GHN0-1646-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01123. Ac_CoA_synth. |
| InterPro | IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view] |
| Pfam | PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 1 hit. PF13193. DUF4009. 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 program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |