B7VIF2 · LEU1_VIBA3
- Protein2-isopropylmalate synthase
- GeneleuA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids515 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic activity
- 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H+
Cofactor
Pathway
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2-isopropylmalate synthase activity | |
Molecular Function | acetyl-CoA C-acetyltransferase activity | |
Molecular Function | manganese ion binding | |
Biological Process | L-leucine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2-isopropylmalate synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio
Accessions
- Primary accessionB7VIF2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000149331 | 1-515 | 2-isopropylmalate synthase | |||
Sequence: MNDQVIIFDTTLRDGEQALAASLTVKEKLQIAYALERLGVDVIEAGFPISSPGDFESVQTIAKHIKDSRICALSRAVAKDIDAAAEALKVADQFRIHTFISTSTVHVQDKLRRSYDDVVEMAVKAVKHARNYTDDVEFSCEDAGRTPIDNLCRMVEAAINAGAKTINIPDTVGYTVPNEFGGIIKTLFDRVPNIDQAIISVHCHDDLGMSVANSIAAVQAGARQIEGTINGIGERAGNCSLEEIAMIIKTRQELLGVHTGLDHKEIHRTSKLVSQLCHMPIQDNKAIVGANAFSHSSGIHQDGMLKNKNTYEIMTPESIGLKNKALNLTSRSGRAAVKSHMDAMGYKDNEYNLDSLYEDFLKLADRKGQVFDYDLEALMHFANLRDEDDFYKLNYLSVQSGSVMSTTSIKLQCGDEEKCEAAVGNGPVDALYQCIYRLTGYEIALDKFDLTAKGEGEDGLGQADIIANYKGRKYHGTGVSTDIVEASGQALLHVINSIQRADTIAEMKQQKFATV |
Interaction
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-267 | Pyruvate carboxyltransferase | ||||
Sequence: VIIFDTTLRDGEQALAASLTVKEKLQIAYALERLGVDVIEAGFPISSPGDFESVQTIAKHIKDSRICALSRAVAKDIDAAAEALKVADQFRIHTFISTSTVHVQDKLRRSYDDVVEMAVKAVKHARNYTDDVEFSCEDAGRTPIDNLCRMVEAAINAGAKTINIPDTVGYTVPNEFGGIIKTLFDRVPNIDQAIISVHCHDDLGMSVANSIAAVQAGARQIEGTINGIGERAGNCSLEEIAMIIKTRQELLGVHTGLDHKEIH | ||||||
Region | 392-515 | Regulatory domain | ||||
Sequence: KLNYLSVQSGSVMSTTSIKLQCGDEEKCEAAVGNGPVDALYQCIYRLTGYEIALDKFDLTAKGEGEDGLGQADIIANYKGRKYHGTGVSTDIVEASGQALLHVINSIQRADTIAEMKQQKFATV |
Sequence similarities
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length515
- Mass (Da)56,388
- Last updated2009-02-10 v1
- Checksum71A7F203F49B6645
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FM954972 EMBL· GenBank· DDBJ | CAV17389.1 EMBL· GenBank· DDBJ | Genomic DNA |