A0A5P9QCB9 · A0A5P9QCB9_9MICO
- ProteinAcetolactate synthase
- GeneilvB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids636 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- H+ + 2 pyruvate = (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 > Luteimicrobium
Accessions
- Primary accessionA0A5P9QCB9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-17 | Pro residues | ||||
Sequence: MVQGPIPAPPRQATPSP | ||||||
Region | 1-46 | Disordered | ||||
Sequence: MVQGPIPAPPRQATPSPVRPSARPATAKPARPAARKVAGEGVGQVA | ||||||
Domain | 57-172 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: TGAESIVRSLEAVGVDTVFGIPGGAILPLYDPLMDSQKLRHILVRHEQGGGHAASGYAHASGKVGVCMATSGPGATNLVTPIADANIDSIPMVAITGQVAASSIGTDAFQEADIVG | ||||||
Domain | 246-381 | Thiamine pyrophosphate enzyme central | ||||
Sequence: IREAAKLLATARKPVLYVGGGVVRADASAELRRLVDLSGAPAVTTLMARGALPDSHPQNLGMPGMHGTVPAVAALQQADLVVALGARFDDRVTGRLDSFAPNAVVVHADIDPAEIGKNRAVDVPIVGDLREVLADL | ||||||
Domain | 445-600 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: GVGQHQMWAAQFIRYEHPRTWINSGGLGTMGYSVPAAMGAKVARPDATVWAIDGDGCFQMTNQELATCVINEIPIKVAVVNNSSLGMVRQWQTLFYNERYSNTDLHTGHGTRRVPDFVKMADAYGCVGLRCETKADVDATIKRALEIDDQPVVVDF |
Sequence similarities
Belongs to the TPP enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length636
- Mass (Da)67,601
- Last updated2020-04-22 v1
- Checksum997BCB3C28DF1406
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-17 | Pro residues | ||||
Sequence: MVQGPIPAPPRQATPSP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP045529 EMBL· GenBank· DDBJ | QFU98886.1 EMBL· GenBank· DDBJ | Genomic DNA |