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Protein

Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial

Gene

Idh3g

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Cofactori

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

Enzyme regulationi

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei120Allosteric activator citrateBy similarity1
Binding sitei133Allosteric activator citrateBy similarity1
Binding sitei136SubstrateBy similarity1
Binding sitei167SubstrateBy similarity1
Metal bindingi254Magnesium or manganese; shared with catalytic subunitBy similarity1
Binding sitei254SubstrateBy similarity1
Binding sitei312Allosteric activator ADPBy similarity1
Binding sitei313Allosteric activator ADPBy similarity1
Binding sitei324Allosteric activator ADPBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processTricarboxylic acid cycle
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-71403. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial
Alternative name(s):
Isocitric dehydrogenase subunit gamma
NAD(+)-specific ICDH subunit gamma
Gene namesi
Name:Idh3g
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1099463. Idh3g.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 39MitochondrionBy similarityAdd BLAST39
ChainiPRO_000001445140 – 393Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrialAdd BLAST354

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei130PhosphoserineBy similarity1
Modified residuei206N6-acetyllysineCombined sources1
Modified residuei226N6-succinyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP70404.
PaxDbiP70404.
PeptideAtlasiP70404.
PRIDEiP70404.

PTM databases

iPTMnetiP70404.
PhosphoSitePlusiP70404.
SwissPalmiP70404.

Expressioni

Gene expression databases

BgeeiENSMUSG00000002010.
CleanExiMM_IDH3G.
ExpressionAtlasiP70404. baseline and differential.
GenevisibleiP70404. MM.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

BioGridi200511. 1 interactor.
IntActiP70404. 4 interactors.
MINTiMINT-1861482.
STRINGi10090.ENSMUSP00000056502.

Structurei

3D structure databases

ProteinModelPortaliP70404.
SMRiP70404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0784. Eukaryota.
COG0473. LUCA.
GeneTreeiENSGT00590000083091.
HOVERGENiHBG052080.
InParanoidiP70404.
KOiK00030.
OMAiGTSMFEP.
OrthoDBiEOG091G094X.
PhylomeDBiP70404.
TreeFamiTF315033.

Family and domain databases

InterProiView protein in InterPro
IPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
PfamiView protein in Pfam
PF00180. Iso_dh. 1 hit.
SMARTiView protein in SMART
SM01329. Iso_dh. 1 hit.
TIGRFAMsiTIGR00175. mito_nad_idh. 1 hit.
PROSITEiView protein in PROSITE
PS00470. IDH_IMDH. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P70404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKVAIAAG GAAKAMLKPT LLCRPWEVLA AHVAPRRSIS SQQTIPPSAK
60 70 80 90 100
YGGRHTVTMI PGDGIGPELM LHVKSVFRHA CVPVDFEEVH VSSNADEEDI
110 120 130 140 150
RNAIMAIRRN RVALKGNIET NHNLPPSHKS RNNILRTSLD LYANVIHCKS
160 170 180 190 200
LPGVVTRHKD IDILIVRENT EGEYSSLEHE SVAGVVESLK IITKAKSLRI
210 220 230 240 250
AEYAFKLAQE SGRKKVTAVH KANIMKLGDG LFLQCCREVA AHYPQITFDS
260 270 280 290 300
MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG
310 320 330 340 350
HVYAVFETAT RNTGKSIANK NIANPTATLL ASCMMLDHLK LHSYATSIRK
360 370 380 390
AVLASMDNEN MHTPDIGGQG TTSQAIQDII RHIRIINGRA VEA
Length:393
Mass (Da):42,785
Last modified:February 1, 1997 - v1
Checksum:i4023560C44C1F4D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68564 mRNA. Translation: AAC53340.1.
AF133093 Genomic DNA. No translation available.
CCDSiCCDS30212.1.
RefSeqiNP_032349.1. NM_008323.1.
UniGeneiMm.14825.

Genome annotation databases

EnsembliENSMUST00000052761; ENSMUSP00000056502; ENSMUSG00000002010.
GeneIDi15929.
KEGGimmu:15929.
UCSCiuc009tmp.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiIDHG1_MOUSE
AccessioniPrimary (citable) accession number: P70404
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: August 30, 2017
This is version 151 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families