P70404 · IDHG1_MOUSE

  • Protein
    Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial
  • Gene
    Idh3g
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Divalent metal cations; Mn2+ or Mg2+. Activity higher in presence of Mn2+ than of Mg2+. Binds 1 Mg2+ or Mn2+ ion per subunit.

Activity regulation

The heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits can be allosterically activated by citrate (CIT) or/and ADP, and the two activators can act independently or synergistically. The heterodimer composed of IDH3A and IDH3B subunits cannot be allosterically regulated and the allosteric regulation of the heterotetramer is through the IDH3G subunit and not the IDH3B subunit. The IDH3G subunit contains the allosteric site which consists of a CIT-binding site and an ADP-binding site, and the binding of CIT and ADP causes conformational changes at the allosteric site which are transmitted to the active site in the catalytic subunit (IDH3A) through a cascade of conformational changes at the heterodimer interface, leading to stabilization of the isocitrate-binding at the active site and thus activation of the enzyme. ATP can activate the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits at low concentrations but inhibits their activities at high concentrations, whereas ATP exhibits only inhibitory effect on the heterodimer composed of IDH3A and IDH3B subunits.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site120citrate (UniProtKB | ChEBI); allosteric activator
Binding site133citrate (UniProtKB | ChEBI); allosteric activator
Binding site136substrate
Binding site167substrate
Binding site254Mn2+ (UniProtKB | ChEBI); ligand shared with catalytic subunit
Binding site254substrate
Binding site312ADP (UniProtKB | ChEBI); allosteric activator
Binding site313ADP (UniProtKB | ChEBI); allosteric activator
Binding site324ADP (UniProtKB | ChEBI); allosteric activator

GO annotations

AspectTerm
Cellular Componentisocitrate dehydrogenase complex (NAD+)
Cellular Componentmitochondrion
Molecular FunctionATP binding
Molecular Functionisocitrate dehydrogenase (NAD+) activity
Molecular Functionmagnesium ion binding
Molecular FunctionNAD binding
Biological Process2-oxoglutarate metabolic process
Biological Processisocitrate metabolic process
Biological ProcessNADH metabolic process
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial
  • Alternative names
    • Isocitric dehydrogenase subunit gamma
    • NAD(+)-specific ICDH subunit gamma

Gene names

    • Name
      Idh3g

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P70404

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for transit peptide, chain, modified residue.

TypeIDPosition(s)Description
Transit peptide1-39Mitochondrion
ChainPRO_000001445140-393Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial
Modified residue130Phosphoserine
Modified residue206N6-acetyllysine
Modified residue226N6-succinyllysine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer containing one IDH3A and one IDH3B subunit and the heterodimer containing one IDH3A and one IDH3G subunit assemble into a heterotetramer (which contains two subunits of IDH3A, one of IDH3B and one of IDH3G) and further into the heterooctamer.
View interactors in UniProtKB
View CPX-556 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    393
  • Mass (Da)
    42,785
  • Last updated
    1997-02-01 v1
  • Checksum
    4023560C44C1F4D3
MALKVAIAAGGAAKAMLKPTLLCRPWEVLAAHVAPRRSISSQQTIPPSAKYGGRHTVTMIPGDGIGPELMLHVKSVFRHACVPVDFEEVHVSSNADEEDIRNAIMAIRRNRVALKGNIETNHNLPPSHKSRNNILRTSLDLYANVIHCKSLPGVVTRHKDIDILIVRENTEGEYSSLEHESVAGVVESLKIITKAKSLRIAEYAFKLAQESGRKKVTAVHKANIMKLGDGLFLQCCREVAAHYPQITFDSMIVDNTTMQLVSRPQQFDVMVMPNLYGNIVNNVCAGLVGGPGLVAGANYGHVYAVFETATRNTGKSIANKNIANPTATLLASCMMLDHLKLHSYATSIRKAVLASMDNENMHTPDIGGQGTTSQAIQDIIRHIRIINGRAVEA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U68564
EMBL· GenBank· DDBJ
AAC53340.1
EMBL· GenBank· DDBJ
mRNA
AF133093
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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