A0A037YDD8 · A0A037YDD8_ECOLX
- ProteinAcetyl-coenzyme A synthetase
- Geneacs
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids652 (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 | |
---|---|---|
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A037YDD8
Proteomes
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
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-81 | Acetyl-coenzyme A synthetase N-terminal | ||||
Sequence: YEAMYQQSINAPDTFWGEQGKILDWIKPYQKVKNTSFAPGNVSIKWYEDGTLNLAANC | ||||||
Domain | 83-467 | AMP-dependent synthetase/ligase | ||||
Sequence: DRHLQENGDRTAIIWEGDDASQSKHISYKELHRDVCRFANTLLELGIKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPEAVAGRIIDSNSRLVITSDEGVRAGRSIPLKKNVDDALKNPNVTSVEHVVVLKRTGGKIDWQEGRDLWWHDLVEQASDQHQAEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGPLACGATTLMFEGVPNWPTPARMAQVVDKHQVNILYTAPTAIRALMAEGDKAIEGTDRSSLRILGSVGEPINPEAWEWYWKKIGNEKCPVVDTWWQTETGGFMITPLPGATELKAGSATRPFFGVQPALVDNEGNPLEGATEGSLVIT | ||||||
Domain | 531-609 | AMP-binding enzyme C-terminal | ||||
Sequence: EIESALVAHPKIAEAAVVGIPHNIKGQAIYAYVTLNHGEEPSPELYAEVRNWVRKEIGPLATPDVLHWTDSLPKTRSGK |
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length652
- Mass (Da)72,066
- Last updated2014-07-09 v1
- Checksum4DCA1C1990D6FC6A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP023197 EMBL· GenBank· DDBJ | BCG38921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AASCBU010000006 EMBL· GenBank· DDBJ | EFA8784043.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AASLUY010000008 EMBL· GenBank· DDBJ | EFE0299542.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AASZRA010000004 EMBL· GenBank· DDBJ | EFI6951537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AATGUC010000011 EMBL· GenBank· DDBJ | EFL0833246.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AATHUK010000021 EMBL· GenBank· DDBJ | EFL4330458.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AATJOC010000016 EMBL· GenBank· DDBJ | EFM0254810.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAVTXU010000082 EMBL· GenBank· DDBJ | EGE1989555.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BGDN01000082 EMBL· GenBank· DDBJ | GDP74450.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DABESF010000015 EMBL· GenBank· DDBJ | HAI5419915.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DABGKZ010000015 EMBL· GenBank· DDBJ | HAJ5150844.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DABUSX010000004 EMBL· GenBank· DDBJ | HAN5764410.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MOKI01000006 EMBL· GenBank· DDBJ | OJR56210.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP049201 EMBL· GenBank· DDBJ | QIF14864.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
NPIM01000112 EMBL· GenBank· DDBJ | RVE14292.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UFZA01000001 EMBL· GenBank· DDBJ | STE03633.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
UGGJ01000004 EMBL· GenBank· DDBJ | STN84879.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CABWJB010000001 EMBL· GenBank· DDBJ | VWM62281.1 EMBL· GenBank· DDBJ | Genomic DNA |