[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1006/geno.1997.4822; PubMed=9286695 [NCBI, ExPASy, EBI, Israel, Japan] Brenner V., Nyakatura G., Rosenthal A., Platzer M.; "Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse."; Genomics 44:8-14(1997).
[2]	NUCLEOTIDE SEQUENCE. Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A.; "Comparative sequence analysis of the mouse L1cam locus and the corresponding region of human Xq28."; Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 102-108; 116-129; 150-190 AND 227-237, AND MASS SPECTROMETRY. STRAIN=C57BL/6; TISSUE=Brain; Lubec G., Kang S.U.; Submitted (APR-2007) to UniProtKB.
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-363, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1074/jbc.M411220200; PubMed=15572359 [NCBI, ExPASy, EBI, Israel, Japan] Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.; "Proteomic analysis of in vivo phosphorylated synaptic proteins."; J. Biol. Chem. 280:5972-5982(2005).

Comments

CATALYTIC ACTIVITY: Isocitrate + NAD⁺ = 2-oxoglutarate + CO₂ + NADH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
ENZYME REGULATION: Activated by increasing ADP/ATP ratios and by Ca(2+) (By similarity).
SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1 (By similarity).
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

EMBL

U68564; AAC53340.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

RefSeq

NP_032349.1; -.

UniGene

Mm.14825

3D structure databases

HSSP

P00351; 1OSJ. [HSSP ENTRY / PDB]

ModBase

P70404.

Protein-protein interaction databases

IntAct

P70404; -.

PTM databases

PhosphoSite

P70404; -.

Organism-specific databases

MGI

MGI:1099463; Idh3g.

Gene expression databases

ArrayExpress

P70404; -.

CleanEx

MM_IDH3G; -.

GermOnline

ENSMUSG00000002010; Mus musculus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0004449;	Molecular function: isocitrate dehydrogenase (NAD+) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006102;	Biological process: isocitrate metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR004434; IsoCit_DHase_NAD_mit.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11835; IDH_IMDH_dimeric; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00175; mito_nad_idh; 1.

PROSITE

PS00470; IDH_IMDH; 1.

BLOCKS

P70404.

Genome annotation databases

Ensembl

ENSMUSG00000002010; Mus musculus. [Contig view]

GeneID

15929; -.

KEGG

mmu:15929; -.

Phylogenomic databases

HOGENOM

P70404; -.

HOVERGEN

P70404; -.

Other

Idh3g; Mus musculus.

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

Keywords

ATP-binding; Direct protein sequencing; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Nucleotide-binding; Oxidoreductase; Phosphoprotein; Transit peptide; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Mitochondrion (By similarity).`
`CHAIN`	`40 393`	`354`	`Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial.`	`PRO_0000014451`
`NP_BIND`	`56 84`	`29`	`NAD (Potential).`
`NP_BIND`	`309 316`	`8`	`ATP (Potential).`
`METAL`	`254 254`		`Magnesium or manganese (By similarity).`
`BINDING`	`136 136`		`Substrate (By similarity).`
`BINDING`	`167 167`		`Substrate (By similarity).`
`BINDING`	`254 254`		`Substrate (By similarity).`
`SITE`	`174 174`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`221 221`	`1`	`Critical for catalysis (By similarity).`
`MOD_RES`	`363 363`		`Phosphothreonine.`

Sequence information

Length: 393 AA [This is the length of the unprocessed precursor]

Molecular weight: 42785 Da [This is the MW of the unprocessed precursor]

CRC64: 4023560C44C1F4D3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALKVAIAAG GAAKAMLKPT LLCRPWEVLA AHVAPRRSIS SQQTIPPSAK YGGRHTVTMI 

        70         80         90        100        110        120 
PGDGIGPELM LHVKSVFRHA CVPVDFEEVH VSSNADEEDI RNAIMAIRRN RVALKGNIET 

       130        140        150        160        170        180 
NHNLPPSHKS RNNILRTSLD LYANVIHCKS LPGVVTRHKD IDILIVRENT EGEYSSLEHE 

       190        200        210        220        230        240 
SVAGVVESLK IITKAKSLRI AEYAFKLAQE SGRKKVTAVH KANIMKLGDG LFLQCCREVA 

       250        260        270        280        290        300 
AHYPQITFDS MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG 

       310        320        330        340        350        360 
HVYAVFETAT RNTGKSIANK NIANPTATLL ASCMMLDHLK LHSYATSIRK AVLASMDNEN 

       370        380        390 
MHTPDIGGQG TTSQAIQDII RHIRIINGRA VEA

P70404 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