ID   IDH2_CANTR              Reviewed;         411 AA.
AC   O13294;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] peroxisomal;
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   AltName: Full=PS-NADP-IDH;
DE   AltName: Full=CtIDP2;
GN   Name=IDP2;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   MEDLINE=98092307; PubMed=9432010;
RX   DOI=10.1111/j.1432-1033.1997.00205.x;
RA   Kawachi H., Shimizu K., Atomi H., Sanuki S., Ueda M., Tanaka A.;
RT   "Gene analysis of an NADP-linked isocitrate dehydrogenase localized in
RT   peroxisomes of the n-alkane-assimilating yeast Candida tropicalis.";
RL   Eur. J. Biochem. 250:205-211(1997).
CC   -!- FUNCTION: May play a role in N-alkane metabolism, glutamate
CC       synthesis, and/or NADPH generation in the peroxisomes.
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   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- INDUCTION: By N-alkanes.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AB007994; BAA22846.1; -; Genomic_DNA.
DR   HSSP; P33198; 1LWD.
DR   BRENDA; 1.1.1.42; 1242.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:EC.
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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004790; Isocitrate_DH_NADP-dep_euk.
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   Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese;
KW   Metal-binding; NADP; Oxidoreductase; Peroxisome;
KW   Tricarboxylic acid cycle.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    411       Isocitrate dehydrogenase [NADP]
FT                                peroxisomal.
FT                                /FTId=PRO_0000083583.
FT   NP_BIND      78     80       NADP (By similarity).
FT   NP_BIND     312    317       NADP (By similarity).
FT   REGION       97    103       Substrate binding (By similarity).
FT   METAL       254    254       Magnesium or manganese (By similarity).
FT   METAL       277    277       Magnesium or manganese (By similarity).
FT   BINDING      80     80       Substrate (By similarity).
FT   BINDING      85     85       NADP (By similarity).
FT   BINDING     112    112       Substrate (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   BINDING     262    262       NADP (By similarity).
FT   BINDING     330    330       NADP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   SITE        142    142       Critical for catalysis (By similarity).
FT   SITE        214    214       Critical for catalysis (By similarity).
SQ   SEQUENCE   411 AA;  46171 MW;  3E47A093C45F5915 CRC64;
     MGEIQKITVK NPIVEMDGDE MTRIIWQFIK DKLILPYLNV DLKYYDLGIE YRDKTDDKVT
     TDAAEAILQY GVGVKCATIT PDEARVKEFN LKKMWLSPNG TLRNVIGGTV FREPIVIDNI
     PRIVPSWEKP IIIGRHAFGD QYKATDVVIP AAGDLKLVFK PKDGGEVQEF PVYQFDGPGV
     ALSMYNTDAS ITDFAESSFQ LAIERKLNLF SSTKNTILKK YDGKFKDIFE GLYASKYKTK
     MDELGIWYEH RLIDDMVAQM LKSKGGYIIA MKNYDGDVQS DIVAQGFGSL GLMTSVLVTP
     DGKAFESEAA HGTVTRHYRQ HQQGKETSTN SIASIYAWTR GLIQRGKLDD TPEVVKFAEE
     LEKAVIETVS KDNIMTKDLA LTQGKTDRSS YVTTEEFIDG VANRLNKNLG Y
//