Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A7C5HDX9 · A0A7C5HDX9_9BACT

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 1 Mg2+ or Mn2+ ion per subunit.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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
IDPosition(s)Description
Binding site78-91NAD+ (UniProtKB | ChEBI)
Binding site98substrate
Binding site108substrate
Binding site136substrate
Site143Important for catalysis
Site189Important for catalysis
Binding site221Mg2+ (UniProtKB | ChEBI)
Binding site221substrate
Binding site245Mg2+ (UniProtKB | ChEBI)
Binding site249Mg2+ (UniProtKB | ChEBI)
Binding site278-290NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3-isopropylmalate dehydrogenase activity
Molecular Functionmagnesium ion binding
Molecular FunctionNAD binding
Biological ProcessL-leucine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3-isopropylmalate dehydrogenase
  • EC number
  • Alternative names
    • 3-IPM-DH
    • Beta-IPM dehydrogenase
      (IMDH
      )

Gene names

    • Name
      leuB
    • ORF names
      ENK93_01255
      , ENK97_03645

Organism names

  • Taxonomic identifier
  • Strains
    • HyVt-620
    • HyVt-624
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Campylobacteraceae

Accessions

  • Primary accession
    A0A7C5HDX9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-350Isopropylmalate dehydrogenase-like

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    358
  • Mass (Da)
    39,405
  • Last updated
    2020-12-02 v1
  • MD5 Checksum
    B01266490ED7DCE70E36150CC632EF49
MAKIYKIAVIKGDGIGPEIVDEAIKVLDALASVSDFDFKYRELLMGGIAYDITGDPLPEETIEGCKEADAVLFGAIGGEKWDSLPRDKRPESGLLRLRQALDLYANYRPVKVYDELVDASTLKRKVVEGVDMLVMRELTGGIYFGQPRERGEEKAFNTMVYTRREVERIAHEGFKAAMKRNKRVCSVDKANVLEVSQFWRNIVEEVAQAYPEVQLTHMYVDNAAMQLVRNPRQFDVILTGNIFGDILSDEASMISGSIGLLPSASVGGKVALYEPIHGSAPDIAGQGIANPIATIASAAMMLRFSFGEEDAANRIEEAIEQILRDGCRTKDIADYGAKEVCSTTELGSYIAEYVSKNA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DRSG01000166
EMBL· GenBank· DDBJ
HHD77854.1
EMBL· GenBank· DDBJ
Genomic DNA
DRSC01000074
EMBL· GenBank· DDBJ
HHD83481.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help