[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Brain cortex; NIH - Mammalian Gene Collection (MGC) project; Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
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

BT021907; AAX46754.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC118275; AAI18276.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001069781.1; -.

UniGene

Bt.23357

3D structure databases

ModBase

Q58CP0.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004449;	Molecular function: isocitrate dehydrogenase (NAD+) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006102;	Biological process: isocitrate metabolic process (inferred from sequence or structural similarity 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 InterPro).
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.

ProtoNet

Q58CP0.

Genome annotation databases

Ensembl

ENSBTAG00000001059; Bos taurus. [Contig view]

GeneID

614145; -.

KEGG

bta:614145; -.

Phylogenomic databases

HOVERGEN

Q58CP0; -.

Other

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`	`40 392`	`353`	`Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial.`	`PRO_0000236185`
`NP_BIND`	`55 83`	`29`	`NAD (Potential).`
`NP_BIND`	`308 315`	`8`	`ATP (Potential).`
`METAL`	`253 253`		`Magnesium or manganese (By similarity).`
`BINDING`	`135 135`		`Substrate (By similarity).`
`BINDING`	`166 166`		`Substrate (By similarity).`
`BINDING`	`253 253`		`Substrate (By similarity).`
`SITE`	`173 173`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`220 220`	`1`	`Critical for catalysis (By similarity).`
`MOD_RES`	`362 362`		`Phosphothreonine (By similarity).`

Sequence information

Length: 392 AA [This is the length of the unprocessed precursor]

Molecular weight: 42863 Da [This is the MW of the unprocessed precursor]

CRC64: 44F749F782E18EFD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALKVATAAG GAVKAALRPA LLWRPWEVLG SHEAPRRSFS QQTIPPSAKY GGRHTVTMIP 

        70         80         90        100        110        120 
GDGIGPELML HVKSVFRHAC VPVDFEEVHV SSTADEEDIR NAIMAIRRNR VALKGNIETN 

       130        140        150        160        170        180 
HNLPPSHKSR NNILRTSLDL YANVIHCKSL PGVVTRHRDI DILIVRENTE GEYSSLEHES 

       190        200        210        220        230        240 
VAGVVESLKI ITKAKSLRIA EYAFQLAQES GRKKVTAVHK ANIMKLGDGL FLQCCREVAA 

       250        260        270        280        290        300 
RYPQITFENM IVDNTTMQLV SRPQQFDVMV MPNLYGNIVN NVCAGLVGGP GLVAGANYGH 

       310        320        330        340        350        360 
VYAVFETATR NTGKSIANKN IANPTATLLA SCMMLDHLKL HSYATSIRKA VLASMDNENM 

       370        380        390 
HTPDIGGQGT TSEAIQDIIR HIRVINGRAV EA

Q58CP0 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