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Q9USP8

- IDH2_SCHPO

UniProt

Q9USP8 - IDH2_SCHPO

Protein

Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial

Gene

idh2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (11 Jul 2012)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

    Cofactori

    Binds 1 magnesium or manganese ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei129 – 1291SubstrateBy similarity
    Binding sitei139 – 1391SubstrateBy similarity
    Binding sitei160 – 1601SubstrateBy similarity
    Sitei167 – 1671Critical for catalysisBy similarity
    Sitei214 – 2141Critical for catalysisBy similarity
    Metal bindingi247 – 2471Magnesium or manganeseBy similarity
    Binding sitei247 – 2471SubstrateBy similarity
    Metal bindingi273 – 2731Magnesium or manganeseBy similarity
    Metal bindingi277 – 2771Magnesium or manganeseBy similarity

    GO - Molecular functioni

    1. isocitrate dehydrogenase (NAD+) activity Source: PomBase
    2. magnesium ion binding Source: InterPro
    3. NAD binding Source: InterPro
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. glutamate biosynthetic process Source: PomBase
    2. isocitrate metabolic process Source: PomBase
    3. tricarboxylic acid cycle Source: PomBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NAD, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_213505. Citric acid cycle (TCA cycle).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial (EC:1.1.1.41)
    Alternative name(s):
    Isocitric dehydrogenase
    NAD(+)-specific ICDH
    Gene namesi
    Name:idh2
    Synonyms:glu2
    ORF Names:SPBC902.05c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC902.05c.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: PomBase
    2. mitochondrion Source: PomBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
    BLAST
    Chaini28 – 379352Isocitrate dehydrogenase [NAD] subunit 2, mitochondrialPRO_0000014433Add
    BLAST

    Proteomic databases

    MaxQBiQ9USP8.
    PaxDbiQ9USP8.
    PRIDEiQ9USP8.

    Interactioni

    Subunit structurei

    Octamer of two non-identical subunits IDH1 and IDH2.By similarity

    Protein-protein interaction databases

    BioGridi277774. 12 interactions.
    MINTiMINT-4708417.
    STRINGi4896.SPBC902.05c-1.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0473.
    HOGENOMiHOG000021113.
    KOiK00030.
    OrthoDBiEOG75XGWZ.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR001804. Isocitrate/isopropylmalate_DH.
    IPR004434. Isocitrate_DH_NAD.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11835. PTHR11835. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00175. mito_nad_idh. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9USP8-1 [UniParc]FASTAAdd to Basket

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    MSMLSTLRTA GSLRTFSRSA CYSFQRFSST KAAAGTYEGV KNANGNYTVT    50
    MIAGDGIGPE IAQSVERIFK AAKVPIEWER VKVYPILKNG TTTIPDDAKE 100
    SVRKNKVALK GPLATPIGKG HVSMNLTLRR TFGLFANVRP CVSITGYKTP 150
    YDNVNTVLIR ENTEGEYSGI EHEVIPGVVQ SIKLITRAAS ERVIRYAFQY 200
    ARQTGKNNIT VVHKATIMRM ADGLFLECAK ELAPEYPDIE LREEILDNAC 250
    LKIVTDPVPY NNTVMVMPNL YGDIVSDMCA GLIGGLGLTP SGNIGNQASI 300
    FEAVHGTAPD IAGKGLANPT ALLLSSVMML KHMNLNDYAK RIESAIFDTL 350
    ANNPDARTKD LGGKSNNVQY TDAIISKLK 379
    Length:379
    Mass (Da):41,188
    Last modified:July 11, 2012 - v2
    Checksum:iAE2FB477AC36D963
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB62099.2.
    PIRiT50386.
    RefSeqiNP_595203.2. NM_001021109.2.

    Genome annotation databases

    EnsemblFungiiSPBC902.05c.1; SPBC902.05c.1:pep; SPBC902.05c.
    GeneIDi2541260.
    KEGGispo:SPBC902.05c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB62099.2 .
    PIRi T50386.
    RefSeqi NP_595203.2. NM_001021109.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 277774. 12 interactions.
    MINTi MINT-4708417.
    STRINGi 4896.SPBC902.05c-1.

    Proteomic databases

    MaxQBi Q9USP8.
    PaxDbi Q9USP8.
    PRIDEi Q9USP8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC902.05c.1 ; SPBC902.05c.1:pep ; SPBC902.05c .
    GeneIDi 2541260.
    KEGGi spo:SPBC902.05c.

    Organism-specific databases

    PomBasei SPBC902.05c.

    Phylogenomic databases

    eggNOGi COG0473.
    HOGENOMi HOG000021113.
    KOi K00030.
    OrthoDBi EOG75XGWZ.

    Enzyme and pathway databases

    Reactomei REACT_213505. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    NextBioi 20802372.
    PROi Q9USP8.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR001804. Isocitrate/isopropylmalate_DH.
    IPR004434. Isocitrate_DH_NAD.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view ]
    PANTHERi PTHR11835. PTHR11835. 1 hit.
    Pfami PF00180. Iso_dh. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00175. mito_nad_idh. 1 hit.
    PROSITEi PS00470. IDH_IMDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    Entry informationi

    Entry nameiIDH2_SCHPO
    AccessioniPrimary (citable) accession number: Q9USP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: July 11, 2012
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3