IDH2_SCHPO
ID IDH2_SCHPO Reviewed; 379 AA.
AC Q9USP8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial;
DE EC=1.1.1.41 {ECO:0000305|PubMed:7903653};
DE AltName: Full=Isocitric dehydrogenase;
DE AltName: Full=NAD(+)-specific ICDH;
DE Flags: Precursor;
GN Name=idh2; Synonyms=glu2; ORFNames=SPBC902.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7903653; DOI=10.1111/j.1574-6968.1993.tb06525.x;
RA Barel I., MacDonald D.W.;
RT "Enzyme defects in glutamate-requiring strains of Schizosaccharomyces
RT pombe.";
RL FEMS Microbiol. Lett. 113:267-272(1993).
RN [4]
RP RNA-BINDING.
RX PubMed=10975257; DOI=10.1007/s002940000132;
RA Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A., van der Spek H.;
RT "Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from
RT Kluyveromyces lactis and Schizosaccharomyces pombe.";
RL Curr. Genet. 38:87-94(2000).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Performs an essential role in the oxidative function of the
CC citric acid cycle and is involved in glutamate biosynthesis
CC (PubMed:7903653). Also binds RNA; specifically to the 5'-untranslated
CC leaders of mitochondrial mRNAs (PubMed:10975257).
CC {ECO:0000269|PubMed:10975257, ECO:0000269|PubMed:7903653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH;
CC Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41;
CC Evidence={ECO:0000305|PubMed:7903653};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; CU329671; CAB62099.2; -; Genomic_DNA.
DR PIR; T50386; T50386.
DR RefSeq; NP_595203.2; NM_001021109.2.
DR AlphaFoldDB; Q9USP8; -.
DR SMR; Q9USP8; -.
DR BioGRID; 277774; 12.
DR ComplexPortal; CPX-559; Mitochondrial isocitrate dehydrogenase complex (NAD+).
DR STRING; 4896.SPBC902.05c.1; -.
DR MaxQB; Q9USP8; -.
DR PaxDb; Q9USP8; -.
DR EnsemblFungi; SPBC902.05c.1; SPBC902.05c.1:pep; SPBC902.05c.
DR GeneID; 2541260; -.
DR KEGG; spo:SPBC902.05c; -.
DR PomBase; SPBC902.05c; idh2.
DR VEuPathDB; FungiDB:SPBC902.05c; -.
DR eggNOG; KOG0785; Eukaryota.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; Q9USP8; -.
DR OMA; CVRPCRY; -.
DR Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:Q9USP8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IMP:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; IMP:PomBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IMP:PomBase.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Magnesium; Manganese; Metal-binding;
KW Mitochondrion; NAD; Oxidoreductase; Reference proteome; RNA-binding;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..379
FT /note="Isocitrate dehydrogenase [NAD] subunit 2,
FT mitochondrial"
FT /id="PRO_0000014433"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT SITE 167
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 214
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 41188 MW; AE2FB477AC36D963 CRC64;
MSMLSTLRTA GSLRTFSRSA CYSFQRFSST KAAAGTYEGV KNANGNYTVT MIAGDGIGPE
IAQSVERIFK AAKVPIEWER VKVYPILKNG TTTIPDDAKE SVRKNKVALK GPLATPIGKG
HVSMNLTLRR TFGLFANVRP CVSITGYKTP YDNVNTVLIR ENTEGEYSGI EHEVIPGVVQ
SIKLITRAAS ERVIRYAFQY ARQTGKNNIT VVHKATIMRM ADGLFLECAK ELAPEYPDIE
LREEILDNAC LKIVTDPVPY NNTVMVMPNL YGDIVSDMCA GLIGGLGLTP SGNIGNQASI
FEAVHGTAPD IAGKGLANPT ALLLSSVMML KHMNLNDYAK RIESAIFDTL ANNPDARTKD
LGGKSNNVQY TDAIISKLK
