Q9USP8 (IDH2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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
Synonyms:	glu2
ORF Names:	SPBC902.05c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	379 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 and is involved in glutamate biosynthesis. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs. Ref.3
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 Ref.5.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NAD RNA-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamate biosynthetic process Inferred from mutant phenotype Ref.3. Source: PomBase isocitrate metabolic process Inferred from mutant phenotype Ref.3. Source: PomBase tricarboxylic acid cycle Inferred from mutant phenotype Ref.3. Source: PomBase
Cellular_component	mitochondrial matrix Inferred from sequence or structural similarity. Source: PomBase
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW isocitrate dehydrogenase (NAD+) activity Inferred from mutant phenotype Ref.3. Source: PomBase magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion Potential
	Chain	28 – 379	352	Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial		PRO_0000014433
Sites
	Metal binding	247	1	Magnesium or manganese By similarity
	Metal binding	273	1	Magnesium or manganese By similarity
	Metal binding	277	1	Magnesium or manganese By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	247	1	Substrate By similarity
	Site	167	1	Critical for catalysis By similarity
	Site	214	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9USP8 [UniParc]. Last modified July 11, 2012. Version 2. Checksum: AE2FB477AC36D963	FASTA	379	41,188
	10 20 30 40 50 60 MSMLSTLRTA GSLRTFSRSA CYSFQRFSST KAAAGTYEGV KNANGNYTVT MIAGDGIGPE 70 80 90 100 110 120 IAQSVERIFK AAKVPIEWER VKVYPILKNG TTTIPDDAKE SVRKNKVALK GPLATPIGKG 130 140 150 160 170 180 HVSMNLTLRR TFGLFANVRP CVSITGYKTP YDNVNTVLIR ENTEGEYSGI EHEVIPGVVQ 190 200 210 220 230 240 SIKLITRAAS ERVIRYAFQY ARQTGKNNIT VVHKATIMRM ADGLFLECAK ELAPEYPDIE 250 260 270 280 290 300 LREEILDNAC LKIVTDPVPY NNTVMVMPNL YGDIVSDMCA GLIGGLGLTP SGNIGNQASI 310 320 330 340 350 360 FEAVHGTAPD IAGKGLANPT ALLLSSVMML KHMNLNDYAK RIESAIFDTL ANNPDARTKD 370 LGGKSNNVQY TDAIISKLK

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Comparative functional genomics of the fission yeasts." Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C. Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVISION OF GENE MODEL.
[3]	"Enzyme defects in glutamate-requiring strains of Schizosaccharomyces pombe." Barel I., MacDonald D.W. FEMS Microbiol. Lett. 113:267-272(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"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] [Europe PMC] [Abstract] Cited for: RNA-BINDING.
[5]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAB62099.2.
PIR	T50386.
RefSeq	NP_595203.2. NM_001021109.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC902.05c-1.
Proteomic databases
PaxDb	Q9USP8.
PRIDE	Q9USP8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC902.05c.1; SPBC902.05c.1:pep; SPBC902.05c.
GeneID	2541260.
KEGG	spo:SPBC902.05c.
Organism-specific databases
PomBase	SPBC902.05c.
Phylogenomic databases
eggNOG	COG0473.
HOGENOM	HOG000021113.
KO	K00030.
OrthoDB	EOG4J6W0M.
Family and domain databases
Gene3D	3.40.718.10. 1 hit.
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004434. Isocitrate_DH_NAD. IPR024084. IsoPropMal-DH-like_dom. [Graphical view]
PANTHER	PTHR11835. PTHR11835. 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...
Other
NextBio	20802372.

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:	July 11, 2012
Last modified:	May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program