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Protein

Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial

Gene

IDH3B

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Plays a structural role to facilitate the assembly and ensure the full activity 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

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 - Biological processi

Keywordsi

Biological processTricarboxylic acid cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
Alternative name(s):
Isocitric dehydrogenase subunit beta
NAD(+)-specific ICDH subunit beta
Gene namesi
Name:IDH3B
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_00000835911 – 103Isocitrate dehydrogenase [NAD] subunit beta, mitochondrialAdd BLAST103

Proteomic databases

PaxDbiP56472.
PeptideAtlasiP56472.
PRIDEiP56472.

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

STRINGi9823.ENSSSCP00000007635.

Structurei

3D structure databases

ProteinModelPortaliP56472.
SMRiP56472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0784. Eukaryota.
COG0473. LUCA.
InParanoidiP56472.

Sequencei

Sequence statusi: Fragments.

P56472-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASRSQAEDVR VEGAFPVTML PGDGVGPELM AAVGVIECLK LGDGLFLQCC
60 70 80 90 100
EEVAELYPKN IANPTATLLA SCMMLDHLKT SDMGGYATCQ DFTEAVIGAL

SHP
Length:103
Mass (Da):10,803
Last modified:July 15, 1998 - v1
Checksum:i83D811D29EA7756B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-adjacent residuesi33 – 34Curated2
Non-adjacent residuesi40 – 41Curated2
Non-adjacent residuesi59 – 60Curated2
Non-adjacent residuesi79 – 80Curated2

Sequence databases

PIRiB35834.
UniGeneiSsc.3464.

Entry informationi

Entry nameiIDH3B_PIG
AccessioniPrimary (citable) accession number: P56472
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: September 27, 2017
This is version 79 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