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Q9USP8 (IDH2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Potential
Chain28 – 379352Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial
PRO_0000014433

Sites

Metal binding2471Magnesium or manganese By similarity
Metal binding2731Magnesium or manganese By similarity
Metal binding2771Magnesium or manganese By similarity
Binding site1291Substrate By similarity
Binding site1391Substrate By similarity
Binding site1601Substrate By similarity
Binding site2471Substrate By similarity
Site1671Critical for catalysis By similarity
Site2141Critical for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9USP8 [UniParc].

Last modified July 11, 2012. Version 2.
Checksum: AE2FB477AC36D963

FASTA37941,188
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRT50386.
RefSeqNP_595203.2. NM_001021109.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277774. 12 interactions.
MINTMINT-4708417.
STRING4896.SPBC902.05c-1.

Proteomic databases

MaxQBQ9USP8.
PaxDbQ9USP8.
PRIDEQ9USP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC902.05c.1; SPBC902.05c.1:pep; SPBC902.05c.
GeneID2541260.
KEGGspo:SPBC902.05c.

Organism-specific databases

PomBaseSPBC902.05c.

Phylogenomic databases

eggNOGCOG0473.
HOGENOMHOG000021113.
KOK00030.
OrthoDBEOG75XGWZ.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00175. mito_nad_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802372.
PROQ9USP8.

Entry information

Entry nameIDH2_SCHPO
AccessionPrimary (citable) accession number: Q9USP8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 11, 2012
Last modified: June 11, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names