A0A8J2BRD1 · A0A8J2BRD1_9BACT
- ProteinAcetyl-coenzyme A synthetase
- Geneacs
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids674 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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.
Catalytic activity
- acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 208-211 | CoA (UniProtKB | ChEBI) | |||
Binding site | 326 | CoA (UniProtKB | ChEBI) | |||
Binding site | 402-404 | ATP (UniProtKB | ChEBI) | |||
Binding site | 426-431 | ATP (UniProtKB | ChEBI) | |||
Binding site | 515 | ATP (UniProtKB | ChEBI) | |||
Binding site | 530 | ATP (UniProtKB | ChEBI) | |||
Binding site | 538 | CoA (UniProtKB | ChEBI) | |||
Binding site | 541 | ATP (UniProtKB | ChEBI) | |||
Binding site | 552 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 554 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 557 | Mg2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | acetate-CoA ligase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Biological Process | acetyl-CoA biosynthetic process from acetate |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyl-coenzyme A synthetase
- EC number
- Short namesAcCoA synthetase ; Acs
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Verrucomicrobiota > Methylacidiphilae > Methylacidiphilales > Methylacidiphilaceae > Candidatus Methylacidithermus
Accessions
- Primary accessionA0A8J2BRD1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 624 | N6-acetyllysine | |||
Post-translational modification
Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 44-97 | Acetyl-coenzyme A synthetase N-terminal | |||
Domain | 109-485 | AMP-dependent synthetase/ligase | |||
Domain | 546-624 | AMP-binding enzyme C-terminal | |||
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length674
- Mass (Da)75,824
- Last updated2022-05-25 v1
- Checksum1A0988DD05C6AE3E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CAJNOB010000067 EMBL· GenBank· DDBJ | CAF0704474.1 EMBL· GenBank· DDBJ | Genomic DNA |