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Protein

Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial

Gene

idh2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg(2+) or Mn2+ 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

  • isocitrate dehydrogenase (NAD+) activity Source: PomBase
  • magnesium ion binding Source: InterPro
  • NAD binding Source: InterPro
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • glutamate biosynthetic process Source: PomBase
  • isocitrate metabolic process Source: PomBase
  • tricarboxylic acid cycle Source: PomBase
Complete GO annotation...

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_276964. 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 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC902.05c.
PomBaseiSPBC902.05c. idh2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

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. 11 interactions.
MINTiMINT-4708417.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0473.
HOGENOMiHOG000021113.
InParanoidiQ9USP8.
KOiK00030.
OMAiDYSCERY.
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

« Hide

        10         20         30         40         50
MSMLSTLRTA GSLRTFSRSA CYSFQRFSST KAAAGTYEGV KNANGNYTVT
60 70 80 90 100
MIAGDGIGPE IAQSVERIFK AAKVPIEWER VKVYPILKNG TTTIPDDAKE
110 120 130 140 150
SVRKNKVALK GPLATPIGKG HVSMNLTLRR TFGLFANVRP CVSITGYKTP
160 170 180 190 200
YDNVNTVLIR ENTEGEYSGI EHEVIPGVVQ SIKLITRAAS ERVIRYAFQY
210 220 230 240 250
ARQTGKNNIT VVHKATIMRM ADGLFLECAK ELAPEYPDIE LREEILDNAC
260 270 280 290 300
LKIVTDPVPY NNTVMVMPNL YGDIVSDMCA GLIGGLGLTP SGNIGNQASI
310 320 330 340 350
FEAVHGTAPD IAGKGLANPT ALLLSSVMML KHMNLNDYAK RIESAIFDTL
360 370
ANNPDARTKD LGGKSNNVQY TDAIISKLK
Length:379
Mass (Da):41,188
Last modified:July 11, 2012 - v2
Checksum:iAE2FB477AC36D963
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB62099.2.
PIRiT50386.
RefSeqiNP_595203.2. NM_001021109.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277774. 11 interactions.
MINTiMINT-4708417.

Proteomic databases

MaxQBiQ9USP8.
PaxDbiQ9USP8.
PRIDEiQ9USP8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPBC902.05c.
PomBaseiSPBC902.05c. idh2.

Phylogenomic databases

eggNOGiCOG0473.
HOGENOMiHOG000021113.
InParanoidiQ9USP8.
KOiK00030.
OMAiDYSCERY.
OrthoDBiEOG75XGWZ.

Enzyme and pathway databases

ReactomeiREACT_276964. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi20802372.
PROiQ9USP8.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 115 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.