A0A0U5AEU6 · A0A0U5AEU6_9BACT
- ProteinAcetyl-coenzyme A synthetase
- GeneacsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids660 (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 | 200-203 | CoA (UniProtKB | ChEBI) | |||
Binding site | 320 | CoA (UniProtKB | ChEBI) | |||
Binding site | 396-398 | ATP (UniProtKB | ChEBI) | |||
Binding site | 420-425 | ATP (UniProtKB | ChEBI) | |||
Binding site | 509 | ATP (UniProtKB | ChEBI) | |||
Binding site | 524 | ATP (UniProtKB | ChEBI) | |||
Binding site | 532 | CoA (UniProtKB | ChEBI) | |||
Binding site | 535 | ATP (UniProtKB | ChEBI) | |||
Binding site | 546 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 548 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 551 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 593 | 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 > Thermodesulfobacteriota > Thermodesulfobacteria > Thermodesulfobacteriales > Thermodesulfobacteriaceae > Caldimicrobium
Accessions
- Primary accessionA0A0U5AEU6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 618 | N6-acetyllysine | |||
Post-translational modification
Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 32-88 | Acetyl-coenzyme A synthetase N-terminal | |||
Domain | 100-487 | AMP-dependent synthetase/ligase | |||
Domain | 540-618 | AMP-binding enzyme C-terminal | |||
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length660
- Mass (Da)74,657
- Last updated2016-03-16 v1
- MD5 Checksum76B0FE73B3BDECE6C6D732FA519CAB80
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP014945 EMBL· GenBank· DDBJ | BAU22515.1 EMBL· GenBank· DDBJ | Genomic DNA |