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Protein

Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial

Gene

IDH3G

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 sitei82Allosteric activator citrateBy similarity1
Binding sitei95Allosteric activator citrateBy similarity1
Binding sitei98SubstrateBy similarity1
Binding sitei129SubstrateBy similarity1
Metal bindingi216Magnesium or manganese; shared with catalytic subunitBy similarity1
Binding sitei216SubstrateBy similarity1
Binding sitei274Allosteric activator ADPBy similarity1
Binding sitei275Allosteric activator ADPBy similarity1
Binding sitei286Allosteric activator ADPBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial
Alternative name(s):
Isocitric dehydrogenase subunit gamma
NAD(+)-specific ICDH subunit gamma
Gene namesi
Name:IDH3G
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei‹1MitochondrionBy similarity›1
ChainiPRO_00000144502 – 355Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrialAdd BLAST354

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

Structurei

3D structure databases

ProteinModelPortaliP41564.
SMRiP41564.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG052080.

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: Fragment.

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

P41564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ISSQQTIPPS AKYGGRHTVT MIPGDGIGPE LMLHVKSVFR HACVPVDFEE
60 70 80 90 100
VHVSSNADEE DIRNAIMAIR RNRVALKGNI ETNHNLPPSH KSRNNILRTS
110 120 130 140 150
LDLYANVIHC KSLPGVVTRH KDIDILIVRE NTEGEYSSLE HESVAGVVES
160 170 180 190 200
LKIITKAKSL RIAEYAFKLA QESGRKKVTA VHKANIMKLG DGLFLQCCRE
210 220 230 240 250
VAARYPQITF ENMIVDNTTM QLVSRPQQFD VMVMPNLYGN IVNNVCAGLV
260 270 280 290 300
GGPGLVAGAN YGHVYAVFET ATRNTGKSIA NKNIANPTAT LLASCMMLDH
310 320 330 340 350
LKLHSYATSI RKAVLASMDN ENMHTPDIGG QGTTSEAIQD IIRHIRVING

RAVEA
Length:355
Mass (Da):38,881
Last modified:November 1, 1995 - v1
Checksum:iCC1EEFF0582B6813
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74124 mRNA. Translation: CAA52224.1.
PIRiS39065.
UniGeneiMfa.6663.

Similar proteinsi

Entry informationi

Entry nameiIDH3G_MACFA
AccessioniPrimary (citable) accession number: P41564
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 27, 2017
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families