IDH1_SCHPO
ID IDH1_SCHPO Reviewed; 356 AA.
AC O13696;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial;
DE EC=1.1.1.41 {ECO:0000269|PubMed:10975257};
DE AltName: Full=Isocitric dehydrogenase;
DE AltName: Full=NAD(+)-specific ICDH;
DE Flags: Precursor;
GN Name=idh1; ORFNames=SPAC11G7.03;
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 FUNCTION, CATALYTIC ACTIVITY, AND 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).
CC -!- FUNCTION: Performs an essential role in the oxidative function of the
CC citric acid cycle. Also binds RNA; specifically to the 5'-untranslated
CC leaders of mitochondrial mRNAs. {ECO:0000269|PubMed:10975257}.
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:0000269|PubMed:10975257};
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:0000250}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16208.1; -; Genomic_DNA.
DR PIR; T37546; T37546.
DR RefSeq; NP_594397.1; NM_001019820.2.
DR AlphaFoldDB; O13696; -.
DR SMR; O13696; -.
DR BioGRID; 278384; 3.
DR ComplexPortal; CPX-559; Mitochondrial isocitrate dehydrogenase complex (NAD+).
DR STRING; 4896.SPAC11G7.03.1; -.
DR MaxQB; O13696; -.
DR PaxDb; O13696; -.
DR PRIDE; O13696; -.
DR EnsemblFungi; SPAC11G7.03.1; SPAC11G7.03.1:pep; SPAC11G7.03.
DR GeneID; 2541894; -.
DR KEGG; spo:SPAC11G7.03; -.
DR PomBase; SPAC11G7.03; idh1.
DR VEuPathDB; FungiDB:SPAC11G7.03; -.
DR eggNOG; KOG0784; Eukaryota.
DR HOGENOM; CLU_031953_0_0_1; -.
DR InParanoid; O13696; -.
DR OMA; TCAHKAN; -.
DR PhylomeDB; O13696; -.
DR Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:O13696; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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: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 Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; RNA-binding; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..356
FT /note="Isocitrate dehydrogenase [NAD] subunit 1,
FT mitochondrial"
FT /id="PRO_0000014430"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 144
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 191
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 38758 MW; 11B482F42B467AAC CRC64;
MFKSLVRKSS AFQPLKYGGK YTVTLIPGDG IGRETSNAVT EIFKTANVPI EFEEIDVTGM
EKNNKSSGDA LHEAIQSLKR NKVGLKGILF TPFEKGGHTS FNVALRKELD IYASLVLIKN
IPGFKTRHDN VDFAIIRENT EGEYSGLEHQ SVPGVVESLK IITEYKSKRI AQFAFDFALQ
NGRKSVTCIH KANIMKLADG LFRRTFYDVA NGYDAITPKD LIVDNASMQA VSRPQQFDVL
VMPNLYGSIL SNIGSALVGG PGVIPGANFG RDYALFEPGC RHVGLSITGR GEANPTAAIL
SACLMLRHLG LKDYADLINA ATYSVIEEGK TLTKDLGGSA STGDFTHAIL ERMESL
