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   16-JUN-2009, entry version 55.
DE   RecName: Full=Isocitrate dehydrogenase [NADP], mitochondrial;
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=IDP;
DE   AltName: Full=CtIDP1;
DE   Flags: Precursor;
GN   Name=IDP1;
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].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   MEDLINE=98004564; PubMed=9325427; DOI=10.1007/s002030050513;
RA   Imajo T., Kawachi H., Atomi H., Sanuki S., Yamamoto S., Ueda M.,
RA   Tanaka A.;
RT   "Immunochemically distinct NADP-linked isocitrate dehydrogenase
RT   isozymes in 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: 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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AB004556; BAA22945.1; -; Genomic_DNA.
DR   HSSP; P33198; 1LWD.
DR   SMR; O13285; 29-430.
DR   BRENDA; 1.1.1.42; 1242.
DR   GO; GO:0005739; C:mitochondrion; 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   3: Inferred from homology;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   NADP; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     27       Mitochondrion (By similarity).
FT   CHAIN        28    430       Isocitrate dehydrogenase [NADP],
FT                                mitochondrial.
FT                                /FTId=PRO_0000014424.
FT   NP_BIND     101    103       NADP (By similarity).
FT   NP_BIND     335    340       NADP (By similarity).
FT   REGION      120    126       Substrate binding (By similarity).
FT   METAL       277    277       Magnesium or manganese (By similarity).
FT   METAL       300    300       Magnesium or manganese (By similarity).
FT   BINDING     103    103       Substrate (By similarity).
FT   BINDING     108    108       NADP (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   BINDING     158    158       Substrate (By similarity).
FT   BINDING     285    285       NADP (By similarity).
FT   BINDING     353    353       NADP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   SITE        165    165       Critical for catalysis (By similarity).
FT   SITE        237    237       Critical for catalysis (By similarity).
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
//