M0FKV8 · M0FKV8_9EURY
- Protein3-isopropylmalate dehydratase large subunit
- GeneleuC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids437 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic activity
- (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit.
Pathway
Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3-isopropylmalate dehydratase activity | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Biological Process | L-leucine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-isopropylmalate dehydratase large subunit
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax
Accessions
- Primary accessionM0FKV8
Proteomes
Interaction
Subunit
Heterodimer of LeuC and LeuD.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-290 | Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha | ||||
Sequence: GDYVEADVDVAMAHDITGPLAFRTFDEVTGDDGELFAPDRTVFTIDHHAPADGVQAANNHNAVREFAAEHGAHQFDVGDGICHAVLVEEGFVGPGDLVIGADSHSTTYGGIGAFGTGVGSTDLGTALATGELWFRVPKTLRFEVDGDLGDGVYAKDLILRFIGDVGFDGCTYMAAEYAGSTIESLPIHERLVLSNMAIEMGGKAGLVAPDERTESYLERQTGNEIDLGDAFVSDDDADYEAVHTYDAADLAPQVSKPSNPENAVDVTEV | ||||||
Domain | 290-414 | Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha | ||||
Sequence: VAGTELDQLFVGTCTNGRYEDIKIVADILAGETIAPNVRMVVVPASKSVYQHMLGTGVFQTLTDAGAVIQSAGCGPCAGYHQGVLGDGDVCLATANRNFPGREGSMESSVYLSSPATVGASALYG |
Sequence similarities
Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length437
- Mass (Da)45,953
- Last updated2013-04-03 v1
- Checksum534B27B9BBA931CA
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AOLE01000037 EMBL· GenBank· DDBJ | ELZ60545.1 EMBL· GenBank· DDBJ | Genomic DNA |