P45359 · THLA_CLOAB
- ProteinAcetyl-CoA acetyltransferase
- GenethlA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids392 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA (PubMed:1685080, PubMed:26391388).
Involved in solvent production (PubMed:1685080, PubMed:26391388).
Involved in solvent production (PubMed:1685080, PubMed:26391388).
Catalytic activity
- 2 acetyl-CoA = acetoacetyl-CoA + CoA
Activity regulation
Regulated by a redox-switch modulation. Reversibly inactivated by oxidative stress through the disulfide bond formation between two catalytic residues, Cys-88 and Cys-378, which enables the enzyme to protect its active site from oxygen radicals and be reactivated upon switching back to a reducing condition.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 88 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 96 | acetate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 279-280 | acetate (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Active site | 348 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 378 | Proton acceptor | ||||
Sequence: C | ||||||
Binding site | 386 | acetate (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acetyl-CoA C-acetyltransferase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyl-CoA acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionP45359
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 77 | 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Y-153 and K-286. | ||||
Sequence: V → Q | ||||||
Mutagenesis | 153 | 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Q-77 and K-286. | ||||
Sequence: N → Y | ||||||
Mutagenesis | 286 | 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Q-77 and Y-153. | ||||
Sequence: A → K |
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000206403 | 1-392 | Acetyl-CoA acetyltransferase | |||
Sequence: MKEVVIASAVRTAIGSYGKSLKDVPAVDLGATAIKEAVKKAGIKPEDVNEVILGNVLQAGLGQNPARQASFKAGLPVEIPAMTINKVCGSGLRTVSLAAQIIKAGDADVIIAGGMENMSRAPYLANNARWGYRMGNAKFVDEMITDGLWDAFNDYHMGITAENIAERWNISREEQDEFALASQKKAEEAIKSGQFKDEIVPVVIKGRKGETVVDTDEHPRFGSTIEGLAKLKPAFKKDGTVTAGNASGLNDCAAVLVIMSAEKAKELGVKPLAKIVSYGSAGVDPAIMGYGPFYATKAAIEKAGWTVDELDLIESNEAFAAQSLAVAKDLKFDMNKVNVNGGAIALGHPIGASGARILVTLVHAMQKRDAKKGLATLCIGGGQGTAILLEKC | ||||||
Disulfide bond | 88↔378 | In inhibited form | ||||
Sequence: CGSGLRTVSLAAQIIKAGDADVIIAGGMENMSRAPYLANNARWGYRMGNAKFVDEMITDGLWDAFNDYHMGITAENIAERWNISREEQDEFALASQKKAEEAIKSGQFKDEIVPVVIKGRKGETVVDTDEHPRFGSTIEGLAKLKPAFKKDGTVTAGNASGLNDCAAVLVIMSAEKAKELGVKPLAKIVSYGSAGVDPAIMGYGPFYATKAAIEKAGWTVDELDLIESNEAFAAQSLAVAKDLKFDMNKVNVNGGAIALGHPIGASGARILVTLVHAMQKRDAKKGLATLC |
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Length392
- Mass (Da)41,241
- Last updated1995-11-01 v1
- Checksum024D9B21D200856D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U08465 EMBL· GenBank· DDBJ | AAA82724.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF072734 EMBL· GenBank· DDBJ | AAC26023.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE001437 EMBL· GenBank· DDBJ | AAK80816.1 EMBL· GenBank· DDBJ | Genomic DNA |