A0A2K8SP30 · A0A2K8SP30_9NOSO
- ProteinAcetolactate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids636 (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 | |
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 > Cyanobacteriota > Cyanophyceae > Nostocales > Nostocaceae > Nostoc
Accessions
- Primary accessionA0A2K8SP30
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 | 1-28 | Polar residues | ||||
Sequence: MRSSVSAGESLSQITLPQTENHKQSRPS | ||||||
Region | 1-34 | Disordered | ||||
Sequence: MRSSVSAGESLSQITLPQTENHKQSRPSSPPVVP | ||||||
Domain | 39-155 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: GGFALLDSLHRHGVDYIFGYPGGAILPIYDDLYKVEATGAMKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNLVTGIATAYMDSIPMIVVTGQVARPSIGTDAFQETDIY | ||||||
Domain | 232-366 | Thiamine pyrophosphate enzyme central | ||||
Sequence: INAAIQLITESRRPLLYVGGGAIAASAHEEIKELAELFNIPVTTTLMGIGAFDEHHPLALGMLGMHGTAYANFAVSDCDLLICVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRIPEVPIVGDVRNVLVD | ||||||
Domain | 429-577 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: DVGQHQMWAAQFLKNGPRRWISSAGLGTMGFGLPAAMGAKVAFPDEEVICISGDASFQMCLQELGTLAQYGINVKTIIINNGWQGMVRQWQQAFYGERYSCSNMEVGMPDVELLAKAYGIKGMVISDRSQLKDAIAEMLAHKGPVIVNV |
Sequence similarities
Belongs to the TPP enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length636
- Mass (Da)68,946
- Last updated2018-04-25 v1
- ChecksumDBB1F575E4E97CB3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-28 | Polar residues | ||||
Sequence: MRSSVSAGESLSQITLPQTENHKQSRPS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP024785 EMBL· GenBank· DDBJ | AUB37234.1 EMBL· GenBank· DDBJ | Genomic DNA |