A0A239K095 · A0A239K095_9MICO
- ProteinAcetolactate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids605 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | |
Molecular Function | acetolactate synthase activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | magnesium ion binding | |
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 lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales
Accessions
- Primary accessionA0A239K095
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MSQKMTNPPGRPGPTTKTASTSSEVM | ||||||
Domain | 26-142 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: MTGAQSLVRSLEEVGVDTVFGIPGGAILPAYDPLMDSGKLRHILVRHEQAGGHAASGYAHATGRVGVTIATSGPGATNLVTPLADANMDSIPMVAITGQVGASLIGTDAFQEADIVG | ||||||
Domain | 216-351 | Thiamine pyrophosphate enzyme central | ||||
Sequence: VREAAKLLATAKRPVLYVGGGIIRSGASDALRRLVDESGAAVVTTLMARGAVPDSHPQNLGMPGMHGTVAAVAALQKADLVVALGARFDDRVTGKLSSFAPKAAIVHADIDPAEIGKNRVVDVPIVGDLQEVITDL | ||||||
Domain | 415-570 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: GVGQHQMWASQFIRYEHPNTWINSGGLGTMGYSVPAAMGAKVGQPDREVWAIDGDGCFQMTNQELATCVINEIPIKVAVINNSSLGMVRQWQTLFYDNRYSNTDLHTGHGTRRVPDFVKLAAAYGCAGLRAESEAEVDATIKRAKEIDDQPVIIDF |
Sequence similarities
Belongs to the TPP enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length605
- Mass (Da)64,496
- Last updated2017-11-22 v1
- Checksum64A2A92FA63B3871
Keywords
- Technical term