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   16-JUN-2009, entry version 70.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase;
DE   AltName: Full=NAD(+)-specific ICDH;
DE   Flags: Precursor;
GN   Name=idh1; ORFNames=SPAC11G7.03;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   RNA-BINDING.
RX   MEDLINE=20426969; PubMed=10975257; DOI=10.1007/s002940000132;
RA   Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A.,
RA   van der Spek H.;
RT   "Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases
RT   from Kluyveromyces lactis and Schizosaccharomyces pombe.";
RL   Curr. Genet. 38:87-94(2000).
CC   -!- FUNCTION: Performs an essential role in the oxidative function of
CC       the citric acid cycle. Also binds RNA; specifically to the 5'-
CC       untranslated leaders of mitochondrial mRNAs.
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) +
CC       NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; CU329670; CAB16208.1; -; Genomic_DNA.
DR   PIR; T37546; T37546.
DR   RefSeq; NP_594397.1; -.
DR   HSSP; P08200; 1ISO.
DR   GeneID; 2541894; -.
DR   KEGG; spo:SPAC11G7.03; -.
DR   NMPDR; fig|4896.1.peg.4367; -.
DR   GeneDB_Spombe; SPAC11G7.03; -.
DR   OMA; O13696; NVALRKQ.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002502-MON; -.
DR   BRENDA; 1.1.1.41; 653.
DR   ArrayExpress; O13696; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IMP:GeneDB_SPombe.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IMP:GeneDB_SPombe.
DR   GO; GO:0006102; P:isocitrate metabolic process; IMP:GeneDB_SPombe.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IMP:GeneDB_SPombe.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004434; Isocitrate_DH_NAD_mit.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   NAD; Oxidoreductase; RNA-binding; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    356       Isocitrate dehydrogenase [NAD] subunit 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000014430.
FT   METAL       224    224       Magnesium or manganese (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     224    224       Substrate (By similarity).
FT   SITE        144    144       Critical for catalysis (By similarity).
FT   SITE        191    191       Critical for catalysis (By similarity).
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
//