A0A377DXM2 · A0A377DXM2_ECOLX
- ProteinMultifunctional fusion protein
- GeneleuA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids887 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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).
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic activity
- (2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 1 Mg2+ or Mn2+ ion per subunit.
Pathway
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 14 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 202 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 204 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 238 | Mn2+ (UniProtKB | ChEBI) | |||
Binding site | 602-615 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 623 | substrate | |||
Binding site | 633 | substrate | |||
Binding site | 662 | substrate | |||
Site | 669 | Important for catalysis | |||
Site | 719 | Important for catalysis | |||
Binding site | 751 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 751 | substrate | |||
Binding site | 775 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 779 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 809-821 | NAD+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 2-isopropylmalate synthase activity | |
Molecular Function | 3-isopropylmalate dehydrogenase activity | |
Molecular Function | acetyl-CoA C-acetyltransferase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | manganese ion binding | |
Molecular Function | NAD binding | |
Biological Process | L-leucine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended name3-isopropylmalate dehydrogenase
- EC number
- Alternative names
- Recommended name2-isopropylmalate synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A377DXM2
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 5-267 | Pyruvate carboxyltransferase | |||
Region | 392-887 | Regulatory domain | |||
Sequence similarities
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length887
- Mass (Da)96,857
- Last updated2018-11-07 v1
- MD5 Checksum4FCED1B17EDE6649D112B4ABD24206F7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
UGFG01000001 EMBL· GenBank· DDBJ | STM40795.1 EMBL· GenBank· DDBJ | Genomic DNA |