NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 26032 / G217B;
DOI=10.1002/(SICI)1097-0061(19990630)15:9<799::AID-YEA419>3.3.CO;2-E; PubMed=10398348 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson C.H., McEwen J.E.;
"Isolation of a Histoplasma capsulatum cDNA that complements a mitochondrial NAD(+)-isocitrate dehydrogenase subunit I-deficient mutant of Saccharomyces cerevisiae.";
Yeast 15:799-804(1999).

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.
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

AF009036; AAB63461.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P08200; 1ISO. [HSSP ENTRY / PDB]

ModBase

O13302.

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.

Other

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 35`	`35`	`Mitochondrion (Potential).`
`CHAIN`	`36 388`	`353`	`Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial.`	`PRO_0000014428`
`METAL`	`255 255`		`Magnesium or manganese (By similarity).`
`BINDING`	`137 137`		`Substrate (By similarity).`
`BINDING`	`168 168`		`Substrate (By similarity).`
`BINDING`	`255 255`		`Substrate (By similarity).`
`SITE`	`175 175`	`1`	`Critical for catalysis (By similarity).`
`SITE`	`222 222`	`1`	`Critical for catalysis (By similarity).`

Sequence information

Length: 388 AA [This is the length of the unprocessed precursor]

Molecular weight: 42222 Da [This is the MW of the unprocessed precursor]

CRC64: 7E80888D17CEBEF7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFSLRTAQPA QSLFRAATNT YSTSLPRSAI AARSFATVQS DIFKPTKYGG KYTVTLIPGD 

        70         80         90        100        110        120 
GIGTEVAESV KTIFKADNVP IEWEQVDVSG LDAGNKHSED LFKESIASLK RNKLGLKGIL 

       130        140        150        160        170        180 
HTPVERSGHQ SFNVALRQEL DIYASIVLIK NIPGYKTRHD NVDLCIIREN TEGEYSGLEH 

       190        200        210        220        230        240 
QSVSGVVESL KIITRAKSER IAKFAFSFAL ANNRKKVTCI HKANIMKLAD GLFRSTFHKV 

       250        260        270        280        290        300 
AESYPTLETN DMIVDNASMQ AVARPQQFDV MVMPNLYGGI LSNVGAALVG GPGIVPGCNM 

       310        320        330        340        350        360 
GRDVAVFEPG CRHVGLDIKG KDQANPTALI LSGSMLLRHL GLDEHANRIS KAVYDVIGEG 

       370        380 
VTRTRDMGGQ ASTHEFTRAV LDKMESAL

O13302 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