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   03-AUG-2022, entry version 93.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] peroxisomal;
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=CtIDP2;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   AltName: Full=PS-NADP-IDH;
GN   Name=IDP2;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; 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   PubMed=9432010; 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 synthesis,
CC       and/or NADPH generation in the peroxisomes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC         Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
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   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- INDUCTION: By N-alkanes.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AB007994; BAA22846.1; -; Genomic_DNA.
DR   AlphaFoldDB; O13294; -.
DR   SMR; O13294; -.
DR   PRIDE; O13294; -.
DR   VEuPathDB; FungiDB:CTMYA2_041160; -.
DR   VEuPathDB; FungiDB:CTRG_00909; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11822; PTHR11822; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   SMART; SM01329; Iso_dh; 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; Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9432010"
FT   CHAIN           2..411
FT                   /note="Isocitrate dehydrogenase [NADP] peroxisomal"
FT                   /id="PRO_0000083583"
FT   BINDING         78..80
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         97..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         312..317
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            142
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            214
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
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