[1]	PROTEIN SEQUENCE. TISSUE=Heart; DOI=10.1021/bi00488a010; PubMed=2252888 [NCBI, ExPASy, EBI, Israel, Japan] Huang Y.C., Colman R.F.; "Subunit location and sequences of the cysteinyl peptides of pig heart NAD-dependent isocitrate dehydrogenase."; Biochemistry 29:8266-8273(1990).
[2]	PROTEIN SEQUENCE OF 40-62. TISSUE=Heart; DOI=10.1021/bi00447a023; PubMed=2605193 [NCBI, ExPASy, EBI, Israel, Japan] Saha A., Huang Y.C., Colman R.F.; "Cysteinyl peptide labeled by 3-bromo-2-ketoglutarate in the active site of pig heart NAD+-dependent isocitrate dehydrogenase."; Biochemistry 28:8425-8431(1989).
[3]	PROTEIN SEQUENCE OF 76-86. TISSUE=Heart; PubMed=2745437 [NCBI, ExPASy, EBI, Israel, Japan] Huang Y.C., Colman R.F.; "Aspartyl peptide labeled by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5'-diphosphate in the allosteric ADP site of pig heart NAD+-dependent isocitrate dehydrogenase."; J. Biol. Chem. 264:12208-12214(1989).

Comments

CATALYTIC ACTIVITY: Isocitrate + NAD⁺ = 2-oxoglutarate + CO₂ + NADH.
ENZYME REGULATION: Activated by increasing ADP/ATP ratios and by Ca(2+).
SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1.
SUBCELLULAR LOCATION: Mitochondrion.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

C35834; C35834.

3D structure databases

ModBase

P41566.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0004449;	Molecular function: isocitrate dehydrogenase (NAD+) activity (inferred from mutant phenotype from UniProtKB).
GO:0006102;	Biological process: isocitrate metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

PANTHER

PTHR11835; IDH_IMDH_dimeric; 1.

PROSITE

PS00470; IDH_IMDH; PARTIAL.

ProtoNet

P41566.

Phylogenomic databases

HOVERGEN

P41566; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >106`	`>106`	`Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial.`	`PRO_0000083592`
`NON_CONS`	`62 63`
`NON_CONS`	`75 76`
`NON_CONS`	`86 87`
`NON_TER`	`106 106`

Sequence information

Length: 106 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 11334 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: AB0A66AB845C49AB [This is a checksum on the sequence]

        10         20         30         40         50         60 
FSQQTIPPSA KYGGILTVTM SPGDGDGPEL MLTVXXXXXS ACVPVDFEEV VVSSNADEED 

        70         80         90        100 
IRTSLDLYAN VIHCKLGDGL FLQCCKNIAN PTATLLASCM MLDHLK

P41566 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools