A0A0H5BP58 · A0A0H5BP58_BLAVI
- ProteinAcetyl-coenzyme A synthetase
- GeneacsA_4
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids650 (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 | 190-193 | CoA (UniProtKB | ChEBI) | ||||
Sequence: RGGR | ||||||
Binding site | 308 | CoA (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 332 | CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 384-386 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GEP | ||||||
Binding site | 408-413 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DTWWQT | ||||||
Binding site | 497 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 512 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 520 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 523 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 534 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 536 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 539 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 581 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R |
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Blastochloridaceae > Blastochloris
Accessions
- Primary accessionA0A0H5BP58
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 606 | N6-acetyllysine | ||||
Sequence: K |
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 | 23-80 | Acetyl-coenzyme A synthetase N-terminal | ||||
Sequence: YREIYAASVKDPVAFWGEHGKRIHWFAPYTKVKNTSYDPHNVSIKWYEDGLTNVAYNC | ||||||
Domain | 82-465 | AMP-dependent synthetase/ligase | ||||
Sequence: DRHLATRGDQVAIIWEGDNPAEDKKITYRELYEEVCRFANVLKSRGVKKGDRVTLYLPMIPEAAYAMLACARIGAIHSVVFGGFSPDSLAGRIEDAGSTVIVTADEGLRGGRKVPLKLNTDAACDRAGGVESVIVVRRTGANVPMRSGRDVYYDEIAKNMPAECAVAEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTHQYVFDYHDGDIYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPTISRFWEVIDKHKVNIFYTAPTAIRSLMQAGEAPVTKTSRASLRLLGSVGEPINPEAWEWYHRVVGDHRCPIVDTWWQTETGGILITPLPGAIKLKPGSATLPFFGVVPEVVDANGQVLDGVCEGNLVLSD | ||||||
Domain | 528-606 | AMP-binding enzyme C-terminal | ||||
Sequence: EVESALVAHPKVSEAAVVGYPHDIKGQGIYAYVTLMSDIEPSEELRKELVNWVRKEIGPIAQPDLIQFAPSLPKTRSGK |
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length650
- Mass (Da)71,851
- Last updated2015-10-14 v1
- ChecksumC09C92745FD2F2DE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP014854 EMBL· GenBank· DDBJ | BAR98788.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LN907867 EMBL· GenBank· DDBJ | CUU43878.1 EMBL· GenBank· DDBJ | Genomic DNA |