A0A364KMN2 · A0A364KMN2_TALAM
- ProteinAcetolactate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids688 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- 2 pyruvate + H+ = (2S)-2-acetolactate + CO2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 1 thiamine pyrophosphate per subunit.
Pathway
Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | acetolactate synthase complex | |
Cellular Component | mitochondrion | |
Molecular Function | acetolactate synthase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | pyruvate decarboxylase activity | |
Molecular Function | thiamine pyrophosphate binding | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | valine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetolactate synthase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Trichocomaceae > Talaromyces > Talaromyces sect. Talaromyces
Accessions
- Primary accessionA0A364KMN2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 40-70 | Disordered | |||
Compositional bias | 41-70 | Polar residues | |||
Domain | 89-204 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | |||
Domain | 287-430 | Thiamine pyrophosphate enzyme central | |||
Domain | 495-642 | Thiamine pyrophosphate enzyme TPP-binding | |||
Sequence similarities
Belongs to the TPP enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length688
- Mass (Da)75,295
- Last updated2018-11-07 v1
- Checksum427A79D156F93B67
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 41-70 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MIKG01000001 EMBL· GenBank· DDBJ | RAO64792.1 EMBL· GenBank· DDBJ | Genomic DNA |