P52910 · ACS2_YEAST
- ProteinAcetyl-coenzyme A synthetase 2
- GeneACS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids683 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. 'Anaerobic' isozyme of acetyl-coenzyme A synthetase, which is required for growth on fermentable carbon sources such as glucose. May be involved in the PDH (pyruvate dehydrogenase complex) bypass.
Miscellaneous
Present with 225000 molecules/cell in log phase SD medium.
Catalytic activity
- acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
8.8 mM | acetate | |||||
1.3 mM | ATP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.34 μmol/min/mg |
Pathway
Carbohydrate metabolism; pyruvate metabolism.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 206-209 | CoA (UniProtKB | ChEBI) | ||||
Sequence: RGGK | ||||||
Binding site | 325 | CoA (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 401-403 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GEP | ||||||
Binding site | 425-430 | AMP (UniProtKB | ChEBI) | ||||
Sequence: DTMWQT | ||||||
Binding site | 425-430 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DTMWQT | ||||||
Binding site | 516 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 516 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 531 | AMP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 531 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 539 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 542 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 612 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Molecular Function | acetate-CoA ligase activity | |
Molecular Function | acid-ammonia (or amide) ligase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Biological Process | acetyl-CoA biosynthetic process | |
Biological Process | acetyl-CoA biosynthetic process from acetate | |
Biological Process | pyruvate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyl-coenzyme A synthetase 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP52910
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000208421 | 1-683 | Acetyl-coenzyme A synthetase 2 | |||
Sequence: MTIKEHKVVYEAHNVKALKAPQHFYNSQPGKGYVTDMQHYQEMYQQSINEPEKFFDKMAKEYLHWDAPYTKVQSGSLNNGDVAWFLNGKLNASYNCVDRHAFANPDKPALIYEADDESDNKIITFGELLRKVSQIAGVLKSWGVKKGDTVAIYLPMIPEAVIAMLAVARIGAIHSVVFAGFSAGSLKDRVVDANSKVVITCDEGKRGGKTINTKKIVDEGLNGVDLVSRILVFQRTGTEGIPMKAGRDYWWHEEAAKQRTYLPPVSCDAEDPLFLLYTSGSTGSPKGVVHTTGGYLLGAALTTRYVFDIHPEDVLFTAGDVGWITGHTYALYGPLTLGTASIIFESTPAYPDYGRYWRIIQRHKATHFYVAPTALRLIKRVGEAEIAKYDTSSLRVLGSVGEPISPDLWEWYHEKVGNKNCVICDTMWQTESGSHLIAPLAGAVPTKPGSATVPFFGINACIIDPVTGVELEGNDVEGVLAVKSPWPSMARSVWNHHDRYMDTYLKPYPGHYFTGDGAGRDHDGYYWIRGRVDDVVNVSGHRLSTSEIEASISNHENVSEAAVVGIPDELTGQTVVAYVSLKDGYLQNNATEGDAEHITPDNLRRELILQVRGEIGPFASPKTIILVRDLPRTRSGKIMRRVLRKVASNEAEQLGDLTTLANPEVVPAIISAVENQFFSQKKK | ||||||
Cross-link | 506 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 679 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length683
- Mass (Da)75,492
- Last updated1996-10-01 v1
- Checksum418439EDCDF308F3
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S79456 EMBL· GenBank· DDBJ | AAB35143.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U53879 EMBL· GenBank· DDBJ | AAB82387.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z73325 EMBL· GenBank· DDBJ | CAA97725.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09464.1 EMBL· GenBank· DDBJ | Genomic DNA |