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Protein

Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial

Gene

IDH3A

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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.

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

GO - Molecular functioni

  • isocitrate dehydrogenase (NAD+) activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB

GO - Biological processi

  • tricarboxylic acid cycle Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processTricarboxylic acid cycle
LigandNAD

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

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
ChainiPRO_00000835901 – ›90Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrialAdd BLAST›90

Proteomic databases

PeptideAtlasiP56471.
PRIDEiP56471.

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

ProteinModelPortaliP56471.
SMRiP56471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiView protein in InterPro
IPR024084. IsoPropMal-DH-like_dom.
PfamiView protein in Pfam
PF00180. Iso_dh. 1 hit.

Sequencei

Sequence statusi: Fragments.

P56471-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AGGVKTVTLI PGDGIGPEIS AAVMKIFDAA KAPIQANVRP CVSIEGYKFN
60 70 80 90
EMYLDTVCLN IETACFATIK CSDFTEEICR EVAENCKDIK
Length:90
Mass (Da):9,691
Last modified:July 15, 1998 - v1
Checksum:iC843422E73477480
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-adjacent residuesi35 – 36Curated2
Non-adjacent residuesi48 – 49Curated2
Non-adjacent residuesi60 – 61Curated2
Non-adjacent residuesi70 – 71Curated2
Non-terminal residuei901

Sequence databases

UniGeneiSsc.5389.

Entry informationi

Entry nameiIDH3A_PIG
AccessioniPrimary (citable) accession number: P56471
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: September 27, 2017
This is version 76 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. SIMILARITY comments
    Index of protein domains and families