[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24. STRAIN=HAN/WIST; 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 [GENOMIC DNA] OF 6-393. STRAIN=Wistar; TISSUE=Epididymis; PubMed=8240232 [NCBI, ExPASy, EBI, Israel, Japan] Nichols B.J., Hall L., Perry A.C.F., Denton R.M.; "Molecular cloning and deduced amino acid sequences of the gamma-subunits of rat and monkey NAD(+)-isocitrate dehydrogenases."; Biochem. J. 295:347-350(1993).

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+).
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

EMBL

U63009; AAC53341.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X74125; CAA52225.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S39064; S39064.

UniGene

Rn.2837

3D structure databases

HSSP

P00351; 1OSJ. [HSSP ENTRY / PDB]

ModBase

P41565.

Organism-specific databases

RGD

2863; Idh3g.

Gene expression databases

ArrayExpress

P41565; -.

GermOnline

ENSRNOG00000037284; Rattus norvegicus.

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

P41565.

Genome annotation databases

Ensembl

ENSRNOG00000037284; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P41565; -.

Other

ProtoNet

P41565.

UniRef

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

Keywords

ATP-binding; 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_0000014452`
`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 (By similarity).`
`CONFLICT`	`7 7`		`I -> V (in Ref. 2; CAA52225).`

Sequence information

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

Molecular weight: 42851 Da [This is the MW of the unprocessed precursor]

CRC64: 890B1A4BE3543AE4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALKVAIAAG SAAKAIFKPA LLCRPWEVLA AHEAPRRSIS SQQTIPPSAK YGGRHTVTMI 

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

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

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

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

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

       370        380        390 
MHTPDIGGQG TTSQAIQDII RHIRIINGRA VEA

P41565 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