P29102 · LEU3_BRANA
- Protein3-isopropylmalate dehydrogenase, chloroplastic
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids406 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
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
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 3/4.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 117-130 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GYKWDKNEKHLKPE | ||||||
Binding site | 137 | substrate | ||||
Sequence: R | ||||||
Binding site | 147 | substrate | ||||
Sequence: R | ||||||
Binding site | 175 | substrate | ||||
Sequence: R | ||||||
Site | 182 | Important for catalysis | ||||
Sequence: Y | ||||||
Site | 233 | Important for catalysis | ||||
Sequence: K | ||||||
Binding site | 265 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 265 | substrate | ||||
Sequence: D | ||||||
Binding site | 289 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 293 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 323-335 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSAPDIAGQDKAN |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | 3-isopropylmalate dehydrogenase activity | |
Molecular Function | magnesium 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 name3-isopropylmalate dehydrogenase, chloroplastic
- EC number
- Short names3-IPM-DH; IMDH
- Alternative names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica
Accessions
- Primary accessionP29102
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-34 | Chloroplast | ||||
Sequence: MAAALQTNIRPVKFPATLRALTKQSSPAPFRVRC | ||||||
Chain | PRO_0000014456 | 35-406 | 3-isopropylmalate dehydrogenase, chloroplastic | |||
Sequence: AAASPGKKRYNITLLPGDGIGPEVISIAKNVLQQAGSLEGLEFSFQEMPVGGAALDLVGVPLPEETVSAAKESDAVLLGAIGGYKWDKNEKHLKPETGLLQLRAGLKVFANLRPATVLPQLVDASTLKREVAEGVDLMVVRELTGGIYFGVPRGIKTNENGEEVGYNTEVYAAHEIDRIARVAFETARKRRGKLCSVDKANVLDASILWRRRVTALAAEYPDVELSHMYVDNAAMQLVRDPKQFDTIVTNNIFGDILSDEASMITGSIGMLPSASLSDSGPGLFEPIHGSAPDIAGQDKANPLATILSAAMLLKYGLGEEKAAKRIEDAVLGALNKGFRTGDIYSAGTKLVGCKEMGEEVLKSVDSHVQASV | ||||||
Modified residue | 71 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length406
- Mass (Da)43,351
- Last updated1992-12-01 v1
- Checksum2C8CCEA3B28FF192
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59970 EMBL· GenBank· DDBJ | CAA42596.1 EMBL· GenBank· DDBJ | mRNA |