A0A354AQD5 · A0A354AQD5_9GAMM
- ProteinAcetyl-coenzyme A synthetase
- Geneacs
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids651 (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. Acs undergoes a two-step reaction. In the first half reaction, Acs 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.
Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.
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: RAGR | ||||||
Binding site | 311 | CoA (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 335 | CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 387-389 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GEP | ||||||
Binding site | 411-416 | 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: I | ||||||
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 | |
Biological Process | chemotaxis |
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 > Enterobacterales > Erwiniaceae > Erwinia
Accessions
- Primary accessionA0A354AQD5
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 | 24-81 | Acetyl-coenzyme A synthetase N-terminal | ||||
Sequence: YSSMYQQSVQDPDAFWGEQGKILDWIKPFTVVKNTSFAPGNVSIRWFEDGTLNLAANC | ||||||
Domain | 83-466 | AMP-dependent synthetase/ligase | ||||
Sequence: DRHLATRGDHPAIIWEGDDSSESKTITYRELHRDVCRFANTLKELGISKGDVVAIYMPMVPEAAVAMLACARIGAVHTVIFGGFSPEAVAGRIIDCNARLVITADEGIRAGRAIPLKKNVDDALNNPNVTSVGNVVVFRRTGKDVGWKNDRDLWWHELVNKASAHHQPEEVGAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPDDVYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPKPSRMAEVVDKHKVTILYTAPTAVRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWFHKKIGNGRCPIVDTWWQTETGGFMITPLPGATALKPGSATNPFFGVQPALVDNEGNALEGATEGNLVI | ||||||
Domain | 531-609 | AMP-binding enzyme C-terminal | ||||
Sequence: EIESALVSHPLIAEAAVVGIPHGLKGQAIYAYITLNHGEEPSPELYTEVRNWVRKEIGPIATPDVLHWTDSLPKTRSGK |
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length651
- Mass (Da)71,568
- Last updated2018-11-07 v1
- ChecksumFF701C068B6DAD31
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QGAC01000020 EMBL· GenBank· DDBJ | TKJ86169.1 EMBL· GenBank· DDBJ | Genomic DNA |