A0A7D9D1W2 · A0A7D9D1W2_9GAMM
- ProteinAcetyl-coenzyme A synthetase
- Geneacs
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids647 (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 | 189-192 | CoA (UniProtKB | ChEBI) | |||
Binding site | 309 | CoA (UniProtKB | ChEBI) | |||
Binding site | 333 | CoA (UniProtKB | ChEBI) | |||
Binding site | 385-387 | ATP (UniProtKB | ChEBI) | |||
Binding site | 409-414 | ATP (UniProtKB | ChEBI) | |||
Binding site | 498 | ATP (UniProtKB | ChEBI) | |||
Binding site | 513 | ATP (UniProtKB | ChEBI) | |||
Binding site | 521 | CoA (UniProtKB | ChEBI) | |||
Binding site | 524 | ATP (UniProtKB | ChEBI) | |||
Binding site | 535 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 537 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 540 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 582 | CoA (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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Woeseiales > Woeseiaceae > environmental samples
Accessions
- Primary accessionA0A7D9D1W2
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 607 | 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 | 22-79 | Acetyl-coenzyme A synthetase N-terminal | |||
Domain | 81-465 | AMP-dependent synthetase/ligase | |||
Domain | 529-607 | AMP-binding enzyme C-terminal | |||
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length647
- Mass (Da)71,818
- Last updated2020-12-02 v1
- Checksum915240EC5A9EABAD
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LR633967 EMBL· GenBank· DDBJ | VUX55831.1 EMBL· GenBank· DDBJ | Genomic DNA |