Q9UQW6 · ERG10_SCHPO
- ProteinAcetyl-CoA acetyltransferase
- Geneerg10
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids395 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity).
Erg10 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (By similarity).
The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase eg10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hcs1 (Probable)
Erg10 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (By similarity).
The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase eg10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hcs1 (Probable)
Catalytic activity
- 2 acetyl-CoA = acetoacetyl-CoA + CoAThis reaction proceeds in the forward direction.
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 | 90 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 185 | CoA (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 185 | K+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 230 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 246 | K+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 247 | K+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 249 | K+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 250 | CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 347 | K+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Active site | 351 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 381 | Proton acceptor | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | acetyl-CoA C-acetyltransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | ergosterol biosynthetic process | |
Biological Process | fatty acid beta-oxidation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyl-CoA acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionQ9UQW6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000310395 | 1-395 | Acetyl-CoA acetyltransferase | |||
Sequence: MVNTEVYIVSAVRTPMGSFGGSFASLPATKLGSIAIKGALERVNIKPSDVDEVFMGNVVSANLGQNPARQCALGAGLPRSIVCTTVNKVCASGMKATILGAQTIMTGNAEIVVAGGTESMSNAPYYAPKNRFGAKYGNVELVDGLLRDGLSDAYDGLPMGNAAELCAEEHSIDRASQDAFAISSYKRAQNAQATKAFEQEIVPVEVPVGRGKPNKLVTEDEEPKNLNEDKLKSVRAVFKSNGTVTAANASTLNDGASALVLMSAAKVKELGLKPLAKIIGWGEAAQDPERFTTSPSLAIPKALKHAGIEASQVDYYEINEAFSVVAVANTKILGLDPERVNINGGGVAMGHPLGSSGSRIICTLAYILAQKDAKIGVAAVCNGGGGASSIVIERV |
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length395
- Mass (Da)40,998
- Last updated2000-05-01 v1
- Checksum382822A9EF686544
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 387 | in Ref. 1; BAA13846 | ||||
Sequence: A → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D89184 EMBL· GenBank· DDBJ | BAA13846.1 EMBL· GenBank· DDBJ | mRNA | ||
CU329671 EMBL· GenBank· DDBJ | CAA22123.1 EMBL· GenBank· DDBJ | Genomic DNA |