B0XMC1 · ER10A_ASPFC
- ProteinAcetyl-CoA acetyltransferase erg10A, mitochondrial
- Geneerg10A
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids433 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mitochondrial acetyl-CoA acetyltransferase that catalyzes both the formation and degradation of acetoacetyl-CoA (PubMed:32005728).
Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis (PubMed:32005728).
Plays an important role in growth, morphogenesis and maintaining mitochondrial function including the response to oxidative stresses (PubMed:32005728).
Has no overlapping function with erg10B and seems not to be involved in ergosterol biosynthesis (PubMed:32005728).
Plays an important role in growth, morphogenesis and maintaining mitochondrial function including the response to oxidative stresses (PubMed:32005728).
Miscellaneous
Even though it is not involved in catalysis directly, the Cl- anion stabilizes the catalytic site via both direct and water-mediated hydrogen bonds to catalytic residues and residues adjacent.
Catalytic activity
- 2 acetyl-CoA = acetoacetyl-CoA + CoAThis reaction proceeds in the forward direction.
Cofactor
Biotechnology
Mitochondrial erg10A is essential for A.fumigatus cell viability and might be a potential drug target to feed the antifungal drug development pipeline.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
26 μM | CoA | |||||
43 μM | acetoacetyl-CoA | |||||
232 μM | acetyl-CoA |
Pathway
Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 124 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 219 | K+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 229 | CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 262 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 280 | K+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 284 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 387 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 415 | Proton acceptor | ||||
Sequence: C | ||||||
Binding site | 416 | chloride (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | acetyl-CoA C-acyltransferase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyl-CoA acetyltransferase erg10A, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionB0XMC1
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Leads to lethality.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-34 | Mitochondrion | ||||
Sequence: MAIQTTTGLAARLVAKRATFPASRRNFSASRSAL | ||||||
Chain | PRO_0000454145 | 35-433 | Acetyl-CoA acetyltransferase erg10A, mitochondrial | |||
Sequence: KEIQEAYILSGARTPTAKFNGSFVSVSAPELGAVAIKSAVSKSGVPVEKITDVYMGNVLQGAVGQAPARQASMFAGLSPTVESMTVNKVCASGLKAVALAAQNIQLGLAEAQVAGGMENMSRVPYYLPRSTQLPPFGEIKLQDGLIQDGLWDVYNQFHMGICAEKTAKKYEISREEQDQYAIQSYQRAQAAWKENKFAEEIAPVTVKGKKGETVVERDEGYENLRIDKMATLKPAFLRDGTGTVTAGNASTMNDGASALVLGSKAIAREFAQGNRALARIVSTADAAIDPVDFPVAPAKAVPIALERAGITKDQVAVWEFNEAFAAVIKANEKILGLQNARVNPLGGAISLGHALGSSGSRILVTLLHQLQPGEYGVAAICNGGGAATAMVVQKLDRVD |
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length433
- Mass (Da)45,710
- Last updated2008-04-08 v1
- Checksum4D5B4C442DAAABA0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS499594 EMBL· GenBank· DDBJ | EDP55365.1 EMBL· GenBank· DDBJ | Genomic DNA |