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Protein

Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial

Gene

IDH3A

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic subunit of the enzyme which catalyzes 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

Catalytic activityi

Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

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 sitei96SubstrateBy similarity1
Binding sitei106SubstrateBy similarity1
Binding sitei127SubstrateBy similarity1
Sitei134Critical for catalysisBy similarity1
Sitei181Critical for catalysisBy similarity1
Metal bindingi214Magnesium or manganeseBy similarity1
Metal bindingi238Magnesium or manganeseBy similarity1
Metal bindingi242Magnesium or manganeseBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 42NADSequence analysisAdd BLAST29

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processTricarboxylic acid cycle
LigandMagnesium, Manganese, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC:1.1.1.41)
Alternative name(s):
Isocitric dehydrogenase subunit alpha
NAD(+)-specific ICDH subunit alpha
Gene namesi
Name:IDH3A
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‹1 – 8MitochondrionBy similarity›8
ChainiPRO_00000144379 – 347Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrialAdd BLAST339

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei58N6-succinyllysineBy similarity1
Modified residuei82PhosphothreonineBy similarity1
Modified residuei204N6-acetyllysineBy similarity1
Modified residuei324N6-acetyllysine; alternateBy similarity1
Modified residuei324N6-succinyllysine; alternateBy similarity1
Modified residuei331N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ28480.

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

IntActiQ28480. 1 interactor.
MINTiMINT-6732892.

Structurei

3D structure databases

ProteinModelPortaliQ28480.
SMRiQ28480.
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.

Q28480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QKQVTRGFTG GVQTVTLIPG DGIGPEISAA VMKIFDAAKA PIQWEERNVT
60 70 80 90 100
AIQGPGGKWM IPSEAKESMD KNKMGLKGPL KTPIAAGHPS MNLLLRKTFD
110 120 130 140 150
LYANVRPCVS IEGYKTPYTD VNIVTIRENT EGEYSGIEHV IVDGVVQSIK
160 170 180 190 200
LITEGGSKRI AEFAFEYARN NHRSNVTAVH KANIMRMSDG LFLQKCREVA
210 220 230 240 250
ENCKDIKFNE MYLDTVCLNM VQDPSQFDVL VMPNLYGDIL SDLCAGLIGG
260 270 280 290 300
LGVTPSGNIG ANGVAIFESV HGTAPDIAGK DMANPTALLL SAVMMLRHMG
310 320 330 340
LFDHAARIEA ACFATIKDGK SLTKDLGGNA KCSDFTEEIC RRVKDLD
Length:347
Mass (Da):37,598
Last modified:July 15, 1998 - v2
Checksum:i9100B663642131B9
GO

Sequence cautioni

The sequence CAA60637 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87172 mRNA. Translation: CAA60637.1. Different initiation.
PIRiS58664.
UniGeneiMfa.6661.

Similar proteinsi

Entry informationi

Entry nameiIDH3A_MACFA
AccessioniPrimary (citable) accession number: Q28480
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: September 27, 2017
This is version 93 of the entry and version 2 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