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

AF045153; AAC69608.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382126; CAG97974.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_455266.1; -.

3D structure databases

HSSP

P00351; 1XAA. [HSSP ENTRY / PDB]

ModBase

O94229.

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.

ProtoNet

O94229.

Genome annotation databases

GeneID

2894997; -.

KEGG

kla:KLLA0F04103g; -.

Phylogenomic databases

HOGENOM

O94229; -.

Other

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 12`	`12`	`Mitochondrion (By similarity).`
`CHAIN`	`13 361`	`349`	`Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial.`	`PRO_0000014429`
`METAL`	`229 229`		`Magnesium or manganese (By similarity).`
`BINDING`	`110 110`		`Substrate (By similarity).`
`BINDING`	`141 141`		`Substrate (By similarity).`
`BINDING`	`229 229`		`Substrate (By similarity).`
`SITE`	`148 148`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`195 195`	`1`	`Critical for catalysis (By similarity).`

Sequence information

Length: 361 AA [This is the length of the unprocessed precursor]

Molecular weight: 39158 Da [This is the MW of the unprocessed precursor]

CRC64: 7F3D7F7C5406ECAB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRQGIAAQK KSFATLAAEQ LLPKKYGGRY TVTLIPGDGV GKEVTDSVVK IFENENIPID 

        70         80         90        100        110        120 
WETIDISGLE NTENVQRAVE SLKRNKVGLK GIWHTPADQT GHGSLNVALR KQLDIFANVA 

       130        140        150        160        170        180 
LFKSIPGVKT RLNNIDMVII RENTEGEYSG LEHESVPGVV ESLKIMTRAK SERIARFAFD 

       190        200        210        220        230        240 
FALKNNRKSV CAVHKANIMK LGDGLFRNTV NEIGANEYPE LDVKNIIVDN ASMQAVAKPH 

       250        260        270        280        290        300 
QFDVLVTPNL YGSILGNIGS ALIGGPGLVP GANFGREYAV FEPGSRHVGL DIKGQNVANP 

       310        320        330        340        350        360 
TAMILSSTLM LRHLGLNAYA DRISKATYDV ISEGKSTTRD IGGSASTSEF TNAVIEKLAK 


L

O94229 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