F7VRY0 · F7VRY0_SORMK
- ProteinAcetolactate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids689 (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 | |
---|---|---|
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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Sordariaceae > Sordaria
Accessions
- Primary accessionF7VRY0
Proteomes
Organism-specific databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 37-77 | Polar residues | ||||
Sequence: SNRSVQTRHQSTAAAEAARPTPSQNFQPEPTPSNVQPLSGR | ||||||
Region | 37-80 | Disordered | ||||
Sequence: SNRSVQTRHQSTAAAEAARPTPSQNFQPEPTPSNVQPLSGRKTD | ||||||
Domain | 89-202 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: TGGEIFHEMMLRHNVKHIFGYPGGAILPVFDAIYNSPHFDFISRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADALADGTPMVVFSGQVPTTAIGSDAFQEADVI | ||||||
Domain | 286-428 | Thiamine pyrophosphate enzyme central | ||||
Sequence: IHRVARLINIAKKPVIYAGHGVVQSKGGPELLRALSEKASIPVTTTLHGLGAFDELDEKSLHMLGMHGAAYANKAVQESDLIICLGGRFDDRVTLNLNKFAPAAKAAANEGRGGIVHFEILPKNINKVVQATEAVEGDVATNI | ||||||
Domain | 496-643 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: GVGQHQMWTAQHFRWRHPRTMITSGGLGTMGFGLPAAIGAKVAKPDALVIDIDGDASFGMTLTELSTAAQFNIGVKVIVLNNEEQGMVTQWQNLFYDDRYSHTHQKNPDFVKLGDAMGVQAKRISKPDEVVEGLKWLINSEGPALLEV |
Sequence similarities
Belongs to the TPP enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length689
- Mass (Da)74,787
- Last updated2011-09-21 v1
- Checksum802F105D746F6F52
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 37-77 | Polar residues | ||||
Sequence: SNRSVQTRHQSTAAAEAARPTPSQNFQPEPTPSNVQPLSGR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CABT02000005 EMBL· GenBank· DDBJ | CCC08266.1 EMBL· GenBank· DDBJ | Genomic DNA |