A3SHP3 · A3SHP3_ROSNI
- ProteinAcetyl-coenzyme A synthetase
- GeneacsA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids649 (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 | 191-194 | CoA (UniProtKB | ChEBI) | ||||
Sequence: RGGR | ||||||
Binding site | 309 | CoA (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 385-387 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GEP | ||||||
Binding site | 409-414 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DTWWQT | ||||||
Binding site | 500 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 515 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 523 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 526 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 537 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 539 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 542 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 584 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Roseovarius
Accessions
- Primary accessionA3SHP3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 609 | 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: YRALYDASLRDPEAFWQEHGQRIDWIKPFTKVKDVNFDLGNVSIKWFEDGTLNVAANC | ||||||
Domain | 82-469 | AMP-dependent synthetase/ligase | ||||
Sequence: DRHLASRGDQTAIIWEPDSPDEEALHISYRELHARTCKMANALKELGVTRGDRVVLYMPMIPEAAYAMLACARIGAIHSVVFGGFSSDALAARVNGSEAKVVVTADEAPRGGRNTPLKTNADKALDGVSHDCKLLVVQRTGGDIPMQEGRDHWLHDLEAKVADDCPPEEMNAEDPLFILYTSGSTGAPKGVVHTSGGYLTWASMTHELVFDYHDGDIYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPTYPDASRFWQVCEKHKVNQFYTAPTAIRALMGKGREFVDRCDLSSLKLLGTVGEPINPEAWNWYNDVVGQGRCPIVDTWWQTETGGHLMTPLPGATATKPGSCTTPFFGVEPVVLDAQSGEEITSTEAEGVLCIKSS | ||||||
Domain | 531-609 | AMP-binding enzyme C-terminal | ||||
Sequence: EVESALVAHPKVSEAAVVGYPHDVKGQGIYCYVTLMAGEEYTDDLRKELRDWVRKEIGPIASPDLIQWAPGLPKTRSGK |
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length649
- Mass (Da)71,845
- Last updated2007-04-03 v1
- ChecksumD02E44055AB61559
Keywords
- Technical term