IDH2 isocitrate dehydrogenase (NAD(+)) IDH2 [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Official Symbol: IDH2
Official Full Name: isocitrate dehydrogenase (NAD(+)) IDH2
Primary source: SGD:S000005662
Locus tag: YOR136W
See related: AllianceGenome:SGD:S000005662; FungiDB:YOR136W; VEuPathDB:YOR136W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Contributes to isocitrate dehydrogenase (NAD+) activity. Involved in isocitrate metabolic process. Located in mitochondrion. Part of isocitrate dehydrogenase complex (NAD+). Used to study early infantile epileptic encephalopathy. Human ortholog(s) of this gene implicated in retinitis pigmentosa 90. Orthologous to human IDH3A (isocitrate dehydrogenase (NAD(+)) 3 catalytic subunit alpha). [provided by Alliance of Genome Resources, Dec 2024]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

See IDH2 in Genome Data Viewer

Location:: chromosome: XV

Exon count:: 1

Sequence:: Chromosome: XV; NC_001147.6 (580250..581359)

Chromosome XV - NC_001147.6 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001147.6

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

On the basis of a potential interaction between side chains of Cys-150 residues in IDH2 subunits in each tetramer of the enzyme, ligand binding assays of wild-type (IDH1/IDH2) and IDH1/IDH2(C150S) octameric enzymes were conducted.
Title: Basis for half-site ligand binding in yeast NAD(+)-specific isocitrate dehydrogenase.
Structural features of a ligand-free form of IDH2 suggest that formation of a disulfide bond during stationary phase in yeast transformants might stabilize an inactive form of the enzyme.
Title: Disulfide bond formation in yeast NAD+-specific isocitrate dehydrogenase.
Structural studies of Saccharomyces cerevisiae mitochondrial NADP-dependent IDH2 in different enzymatic states reveal substantial conformational changes during the catalytic reactiion.
Title: Structural studies of Saccharomyces cerevesiae mitochondrial NADP-dependent isocitrate dehydrogenase in different enzymatic states reveal substantial conformational changes during the catalytic reaction.
analysis of allosteric motion in the IDH1 and IDH2 subunits of NAD+-specific isocitrate dehydrogenase
Title: Allosteric motions in structures of yeast NAD+-specific isocitrate dehydrogenase.

Submit: New GeneRIF Correction

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables NAD binding	IEA Inferred from Electronic Annotation more info
enables RNA binding	IEA Inferred from Electronic Annotation more info
contributes_to isocitrate dehydrogenase (NAD+) activity	IDA Inferred from Direct Assay more info	PubMed
enables isocitrate dehydrogenase (NAD+) activity	IEA Inferred from Electronic Annotation more info
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in glutamate biosynthetic process	TAS Traceable Author Statement more info	PubMed
involved_in isocitrate metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in isocitrate metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in tricarboxylic acid cycle	IBA Inferred from Biological aspect of Ancestor more info
involved_in tricarboxylic acid cycle	IEA Inferred from Electronic Annotation more info
involved_in tricarboxylic acid cycle	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
part_of isocitrate dehydrogenase complex (NAD+)	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: isocitrate dehydrogenase (NAD(+)) IDH2

NP_014779.1

EC 1.1.1.41

Subunit of mitochondrial NAD(+)-dependent isocitrate dehydrogenase; complex catalyzes oxidation of isocitrate to alpha-ketoglutarate in TCA cycle; targeted to vacuole via AP-3 pathway

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001147.6 Reference assembly

Range

580250..581359

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183555.1 → NP_014779.1 TPA: isocitrate dehydrogenase (NAD(+)) IDH2 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014779.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W2J3, P28241

UniProtKB/TrEMBL

A6ZNY2, C7GN86, C8ZI98, G2WN10, N1NX01

Conserved Domains (1) summary

COG0473
Location:34 → 369

LeuB; Isocitrate/isopropylmalate dehydrogenase [Energy production and conversion, Amino acid transport and metabolism]