ID   IDH1_CANTR              Reviewed;         430 AA.
AC   O13285;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Isocitrate dehydrogenase [NADP], mitochondrial;
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=CtIDP1;
DE   AltName: Full=IDP;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   Flags: Precursor;
GN   Name=IDP1;
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].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   PubMed=9325427; DOI=10.1007/s002030050513;
RA   Imajo T., Kawachi H., Atomi H., Sanuki S., Yamamoto S., Ueda M., Tanaka A.;
RT   "Immunochemically distinct NADP-linked isocitrate dehydrogenase isozymes in
RT   mitochondria and peroxisomes of Candida tropicalis.";
RL   Arch. Microbiol. 168:389-395(1997).
CC   -!- FUNCTION: Mitochondrial IDP1 may regulate flux through the
CC       tricarboxylic acid cycle and respiration. Its probably critical
CC       function is the production of NADPH.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AB004556; BAA22945.1; -; Genomic_DNA.
DR   AlphaFoldDB; O13285; -.
DR   SMR; O13285; -.
DR   VEuPathDB; FungiDB:CTMYA2_016810; -.
DR   VEuPathDB; FungiDB:CTRG_01521; -.
DR   GO; GO:0005739; C:mitochondrion; 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   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR00127; nadp_idh_euk; 1.
DR   PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..430
FT                   /note="Isocitrate dehydrogenase [NADP], mitochondrial"
FT                   /id="PRO_0000014424"
FT   BINDING         101..103
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         335..340
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            165
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            237
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   430 AA;  48009 MW;  205A319496F0CCEB CRC64;
     MIRASAIQRT AMLLRQLRGF STSATLADKI KVKNPIVELD GDEMTRIIWQ KIKDQLILPY
     LDVDLKYYDL GIESRDATDD QITIDAANAI KEYGVGVKCA TITPDEARVK EFHLKKMWLS
     PNGTIRNILG GTVFRESIII PCIPRLIPGW EKPIVIGRHA FGDQYKATDL VINEPGRLEL
     RFTPASGGEA QTQKVYDYTG PGVGLAMYNT DESITGFAHA SFKMALAKGL PLYMSTKNTI
     LKKYDGRFKD IFQQIYEQDY AAEFEKQGLW YEHRLIDDMV AQMIKSKGGF VMALKNYDGD
     VQSDIVAQGF GSLGLMTSAL MTPDGKAYEA EAAHGTVTRH YRQHQQGKET STNSIASIFA
     WTRGLAQRGK LDETPDVVDF ASKLEQATID TVEVDRIMTK DLALAMGKTD RSAYVTTTEF
     LDAVADRLKK
//