Reviewed, UniProtKB/Swiss-Prot Q9USP8 (IDH2_SCHPO)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase
    NAD(+)-specific ICDH

Gene names

Name:	idh2
ORF Names:	SPBC902.05c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.
Catalytic activity	Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Subunit structure	Octamer of two non-identical subunits IDH1 and IDH2 By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NAD RNA-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from mutant phenotype. Source: GeneDB_SPombe isocitrate metabolic process Inferred from mutant phenotype. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	mitochondrion Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW isocitrate dehydrogenase (NAD+) activity Inferred from mutant phenotype. Source: GeneDB_SPombe magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 378		Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial		PRO_0000014433
Sites
	Metal binding	246	1	Magnesium or manganese By similarity
	Metal binding	272	1	Magnesium or manganese By similarity
	Metal binding	276	1	Magnesium or manganese By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	246	1	Substrate By similarity
	Site	166	1	Critical for catalysis By similarity
	Site	213	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9USP8-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: F2C03935DDC90FA2	FASTA	378	41,060
	10 20 30 40 50 60 MSMLSTLRTA GSLRTFSRSA CYSFRFSSTK AAAGTYEGVK NANGNYTVTM IAGDGIGPEI 70 80 90 100 110 120 AQSVERIFKA AKVPIEWERV KVYPILKNGT TTIPDDAKES VRKNKVALKG PLATPIGKGH 130 140 150 160 170 180 VSMNLTLRRT FGLFANVRPC VSITGYKTPY DNVNTVLIRE NTEGEYSGIE HEVIPGVVQS 190 200 210 220 230 240 IKLITRAASE RVIRYAFQYA RQTGKNNITV VHKATIMRMA DGLFLECAKE LAPEYPDIEL 250 260 270 280 290 300 REEILDNACL KIVTDPVPYN NTVMVMPNLY GDIVSDMCAG LIGGLGLTPS GNIGNQASIF 310 320 330 340 350 360 EAVHGTAPDI AGKGLANPTA LLLSSVMMLK HMNLNDYAKR IESAIFDTLA NNPDARTKDL 370 GGKSNNVQYT DAIISKLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from Kluyveromyces lactis and Schizosaccharomyces pombe." Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A., van der Spek H. Curr. Genet. 38:87-94(2000) [PubMed: 10975257] [Abstract] Cited for: RNA-BINDING.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAB62099.1.
PIR	T50386.
RefSeq	NP_595203.1.
3D structure databases
HSSP	HSSP built from PDB template 1HQS based on UniProtKB P39126.
ModBase	Search...
Genome annotation databases
GeneID	2541260.
KEGG	spo:SPBC902.05c.
NMPDR	fig|4896.1.peg.1069.
Organism-specific databases
GeneDB_Spombe	SPBC902.05c.
Phylogenomic databases
OMA	Q9USP8. GGNSKCS.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003292-MON.
BRENDA	1.1.1.41. 653.
Gene expression databases
ArrayExpress	Q9USP8.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004434. Isocitrate_DH_NAD_mit. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00175. mito_nad_idh. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IDH2_SCHPO

Accession

Primary (citable) accession number: Q9USP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)