A0A2K8T0G8 · A0A2K8T0G8_9NOSO
- ProteinAcetyl-coenzyme A synthetase
- GeneacsA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids657 (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 | 198-201 | CoA (UniProtKB | ChEBI) | ||||
Sequence: RKDA | ||||||
Binding site | 319 | CoA (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 395-397 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GEP | ||||||
Binding site | 419-424 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DTWWQT | ||||||
Binding site | 513 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 528 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 536 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 539 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 550 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 552 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 555 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
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 > Cyanobacteriota > Cyanophyceae > Nostocales > Nostocaceae > Nostoc
Accessions
- Primary accessionA0A2K8T0G8
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 622 | N6-acetyllysine | ||||
Sequence: K |
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 | 34-88 | Acetyl-coenzyme A synthetase N-terminal | ||||
Sequence: YQRLYDKAKADPQQFWADLAGTELEWFQKWDTVLDWQPPFAKWFVGGKMNISYNC | ||||||
Domain | 96-484 | AMP-dependent synthetase/ligase | ||||
Sequence: WRKNKAALIWEGEPGDSRTLTYAQLHREVCQFANVLKQLGVKKGDRVGIYMPMIPEAAIAMLACARIGAPHGVVFGGFSAEALRDRLIDATAKLVITADGGWRKDAIVPLKEQVDKALADGAVPSVENVLVVKRTGQETYMQLGGRDHWWHDLQKGVSADCPAEPMDSEDMLFVLYTSGSTGKPKGVVHTTAGYNLYTHITTKWIFDLQDTDVYWCTADVGWITGHSYIVYGPLSNGATTVMYEGAPRASNPGCFWDVIEKYGVNIFYTAPTAIRAFIKMGEQHPNARNLSSLRLLGSVGEPINPEAWMWYHKVIGGDRCPIVDTWWQTETGGIMITPLPGAIPTKPGSATLPFPGIIADVVDLEGNTVPNNEGGYLAVRHPWPGMMRT | ||||||
Domain | 544-622 | AMP-binding enzyme C-terminal | ||||
Sequence: EVESALVSHPAVAEAAVVGKPDELKGEEVVAFVTLEGTYQASEELSKELKLHVVKEIGAIARPGEIRFTDALPKTRSGK |
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length657
- Mass (Da)72,954
- Last updated2018-04-25 v1
- Checksum3EB4AB5BF9B7A7AE
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP024785 EMBL· GenBank· DDBJ | AUB41196.1 EMBL· GenBank· DDBJ | Genomic DNA |