NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC MYA-539 / JBD100;
DOI=10.1007/s002940000132; PubMed=10975257 [NCBI, ExPASy, EBI, Israel, Japan]
Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A., van der Spek H.;
"Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from Kluyveromyces lactis and Schizosaccharomyces pombe.";
Curr. Genet. 38:87-94(2000).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).

Comments

FUNCTION: Performs an essential role in the oxidative function of the citric acid cycle (By similarity).
CATALYTIC ACTIVITY: Isocitrate + NAD⁺ = 2-oxoglutarate + CO₂ + NADH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2 (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

AF045154; AAC69609.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382125; CAG99173.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_454086.1; -.

3D structure databases

HSSP

P00351; 1XAA. [HSSP ENTRY / PDB]

ModBase

O94230.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from InterPro).
GO:0004449;	Molecular function: isocitrate dehydrogenase (NAD+) activity (inferred from electronic annotation from InterPro).
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: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.

Genome annotation databases

GeneID

2894289; -.

KEGG

kla:KLLA0E03058g; -.

Phylogenomic databases

HOGENOM

O94230; -.

Other

ProtoNet

O94230.

UniRef

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

Keywords

Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 14`	`14`	`Mitochondrion (By similarity).`
`CHAIN`	`15 368`	`354`	`Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial.`	`PRO_0000014432`
`METAL`	`236 236`		`Magnesium or manganese (By similarity).`
`METAL`	`262 262`		`Magnesium or manganese (By similarity).`
`METAL`	`266 266`		`Magnesium or manganese (By similarity).`
`BINDING`	`118 118`		`Substrate (By similarity).`
`BINDING`	`128 128`		`Substrate (By similarity).`
`BINDING`	`149 149`		`Substrate (By similarity).`
`BINDING`	`236 236`		`Substrate (By similarity).`
`SITE`	`156 156`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`203 203`	`1`	`Critical for catalysis (By similarity).`

Sequence information

Length: 368 AA [This is the length of the unprocessed precursor]

Molecular weight: 39579 Da [This is the MW of the unprocessed precursor]

CRC64: E6BFAE7F676F5FB6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFRQSIVKQS CRFLATKKQP SIGRYTGKPN PKTGKYTVSF IEGDGVGPEI SKSVKAIFSA 

        70         80         90        100        110        120 
AKVPIEWESC DVSPIFVNGL TTIPDPAVAS INKNLIALKG PLATPIGKGH RSLNLTLRKT 

       130        140        150        160        170        180 
FGLFANVRPA KSIEGYKTTY ENVNLVLIRE NTEGEYSGIE HVVAPGVVQS IKLITQDASE 

       190        200        210        220        230        240 
RVIRYAFEYA RAVDRSKVLV VHKSTIQRLA DGLFVDVAKK LSSEYPDIEL QTELLDNTVL 

       250        260        270        280        290        300 
KTVQHPEAYD DVVVVCPNLY GDILSDLNSG LSAGSLGLTP SANIGHTVSI FEAVHGSAPD 

       310        320        330        340        350        360 
IAGQNKANPT ALLLSSVMML NHMGLTEHAD KIEKAVLTTI ASDAKNRTGD LGGSASTSSF 


TDAVIERL

O94230 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