S3XD16 · S3XD16_9BACT
- ProteinAcetolactate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids562 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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
- Strain
- Taxonomic lineageBacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Campylobacteraceae > Campylobacter
Accessions
- Primary accessionS3XD16
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-120 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: TGSQMIMQALKNEGVKVVFGYPGGAALNIFDATYDEKDFELILTRHEQAAAHAADGYARVTGEVGVCIVTSGPGFTNTITGLATAYMDSIPLVLISGQVANSLIGTDAFQEIDAVG | ||||||
Domain | 194-329 | Thiamine pyrophosphate enzyme central | ||||
Sequence: IKKAVNLISKSKKPLLYLGGGVISSNATNEVRKLSEISKIPAVETLMALGVLRSDDELNLGMVGMHGKYAANMAMSEADLIFCIGARFDDRVTGKLSEFAKNAKIIHIDIDPSSISKIVNADYPIVGDIKNVLEDL | ||||||
Domain | 390-537 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: DVGQHQMWVAQYYPFKNPRTLLTSGGLGTMGYGLPAALGAAMANKNGIVVNFNGDGGVLMNMQEFQTICENKLPIINIILNNKFLGMVRQWQSLFYKERFASTDISNQPDFVKLIESFGGKGFVANTKDEFRNALKEAIKSKKTALID |
Sequence similarities
Belongs to the TPP enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length562
- Mass (Da)61,765
- Last updated2013-09-18 v1
- ChecksumDF8AC01A17FEAA96
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGYD01000011 EMBL· GenBank· DDBJ | EPH07976.1 EMBL· GenBank· DDBJ | Genomic DNA |