ID   IDHH_YEAST              Reviewed;         420 AA.
AC   P53982;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-DEC-2008, entry version 66.
DE   RecName: Full=Isocitrate dehydrogenase [NADP];
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=IDP;
GN   Name=IDP3; OrderedLocusNames=YNL009W; ORFNames=N2870;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313269; PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
RA   Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA   Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA   Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA   Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA   Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA   Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA   Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA   Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA   Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA   Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA   Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA   Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA   Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT   and its evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
CC   -!- FUNCTION: May function in the production of NADPH for fatty acid
CC       and sterol synthesis.
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2)
CC       + NADPH.
CC   -!- CATALYTIC ACTIVITY: Oxalosuccinate + NADP(+) = 2-oxoglutarate +
CC       CO(2) + NADPH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- INTERACTION:
CC       P33203:PRP40; NbExp=1; IntAct=EBI-8892, EBI-701;
CC       P39940:RSP5; NbExp=1; IntAct=EBI-8892, EBI-16219;
CC       P40318:SSM4; NbExp=1; IntAct=EBI-8892, EBI-18208;
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; Z71285; CAA95869.1; -; Genomic_DNA.
DR   EMBL; AY693154; AAT93173.1; -; Genomic_DNA.
DR   PIR; S62921; S62921.
DR   RefSeq; NP_014389.1; -.
DR   HSSP; P33198; 1LWD.
DR   SMR; P53982; 3-407.
DR   DIP; DIP:4693N; -.
DR   IntAct; P53982; 4.
DR   PeptideAtlas; P53982; -.
DR   Ensembl; YNL009W; Saccharomyces cerevisiae.
DR   GeneID; 855723; -.
DR   GenomeReviews; Y13139_GR; YNL009W.
DR   KEGG; sce:YNL009W; -.
DR   NMPDR; fig|4932.3.peg.5467; -.
DR   CYGD; YNL009w; -.
DR   SGD; S000004954; IDP3.
DR   HOGENOM; P53982; -.
DR   LinkHub; P53982; -.
DR   NextBio; 980090; -.
DR   GermOnline; YNL009W; Saccharomyces cerevisiae.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005777; C:peroxisome; IDA:SGD.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:InterPro.
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:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IMP:SGD.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR   GO; GO:0006740; P:NADPH regeneration; TAS:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR004790; IsoCit_DHase_NADP-dep_euk.
DR   InterPro; IPR001804; IsoCit_IM_DHase.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11822; IDH_NADP_euk; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glyoxylate bypass; Magnesium; Manganese;
KW   Metal-binding; NADP; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    420       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083588.
FT   NP_BIND      75     77       NADP (By similarity).
FT   NP_BIND     310    315       NADP (By similarity).
FT   REGION       94    100       Substrate binding (By similarity).
FT   METAL       252    252       Magnesium or manganese (By similarity).
FT   METAL       275    275       Magnesium or manganese (By similarity).
FT   BINDING      77     77       Substrate (By similarity).
FT   BINDING      82     82       NADP (By similarity).
FT   BINDING     109    109       Substrate (By similarity).
FT   BINDING     132    132       Substrate (By similarity).
FT   BINDING     260    260       NADP (By similarity).
FT   BINDING     328    328       NADP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   SITE        139    139       Critical for catalysis (By similarity).
FT   SITE        212    212       Critical for catalysis (By similarity).
SQ   SEQUENCE   420 AA;  47856 MW;  4094007E13FCD506 CRC64;
     MSKIKVVHPI VEMDGDEQTR VIWKLIKEKL ILPYLDVDLK YYDLSIQERD RTNDQVTKDS
     SYATLKYGVA VKCATITPDE ARMKEFNLKE MWKSPNGTIR NILGGTVFRE PIIIPKIPRL
     VPHWEKPIII GRHAFGDQYR ATDIKIKKAG KLRLQFSSDD GKENIDLKVY EFPKSGGIAM
     AMFNTNDSIK GFAKASFELA LKRKLPLFFT TKNTILKNYD NQFKQIFDNL FDKEYKEKFQ
     ALKITYEHRL IDDMVAQMLK SKGGFIIAMK NYDGDVQSDI VAQGFGSLGL MTSILITPDG
     KTFESEAAHG TVTRHFRKHQ RGEETSTNSI ASIFAWTRAI IQRGKLDNTD DVIKFGNLLE
     KATLDTVQVG GKMTKDLALM LGKTNRSSYV TTEEFIDEVA KRLQNMMLSS NEDKKGMCKL
//