ID   IDHC_SOLTU              Reviewed;         416 AA.
AC   P50217;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 57.
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=ICDH-1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   MEDLINE=95232202; PubMed=7716247; DOI=10.1104/pp.107.3.905;
RA   Fieuw S., Mueller-Roeber B., Galvez S., Willmitzer L.;
RT   "Cloning and expression analysis of the cytosolic NADP(+)-dependent
RT   isocitrate dehydrogenase from potato. Implications for nitrogen
RT   metabolism.";
RL   Plant Physiol. 107:905-913(1995).
CC   -!- FUNCTION: May supply 2-oxoglutarate for amino acid biosynthesis
CC       and ammonia assimilation.
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: Heterodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; X75638; CAA53300.1; ALT_INIT; mRNA.
DR   PIR; S47013; S47013.
DR   PIR; T07402; T07402.
DR   HSSP; P33198; 1LWD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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: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; 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   ProDom; PD328597; Nadp_idh_plant; 1.
DR   TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glyoxylate bypass; Magnesium; Manganese; Metal-binding;
KW   NADP; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    416       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083584.
FT   NP_BIND      77     79       NADP (By similarity).
FT   NP_BIND     312    317       NADP (By similarity).
FT   REGION       96    102       Substrate binding (By similarity).
FT   METAL       254    254       Magnesium or manganese (By similarity).
FT   METAL       277    277       Magnesium or manganese (By similarity).
FT   BINDING      79     79       Substrate (By similarity).
FT   BINDING      84     84       NADP (By similarity).
FT   BINDING     111    111       Substrate (By similarity).
FT   BINDING     134    134       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        141    141       Critical for catalysis (By similarity).
FT   SITE        214    214       Critical for catalysis (By similarity).
SQ   SEQUENCE   416 AA;  46792 MW;  B9A9D6AD53AB090D CRC64;
     MAFQKITVQN PIVEMDGDEM TRVIWKSIKD KLILPFLELD IKYFSLGLPH RDATDDKVTV
     ESAEATQKYN VAIKCATITP DEARVKEFNL KSMWRSPNGT IRNILNGTVF REPIMCKNIP
     RLVPGWTKPI CIGRHAFGDQ YRATDTVIKG AGKLKLVFVP EGSDEKTEFE VYNFTGAGGV
     ALSMYNTDES VRSFAEASMN MAFQKKWPLY LSTKNTILKK YDGRFKDIFQ EVYEANWKSK
     YEEAGIWYEH RLIDDMVAYA LKSEGGYVWA CKNYDGDVQS DFLAQGFGSL GLMTSVLVCP
     DGKTIEAEAA HGTVTRHYRV HQKGGETSTN SIASIFAWTR GLAHRATLDN NERLLDFTEK
     LEAACIGAVE SGKMTKDLAL IIIHGSKLSR EHYLNTEEFI DAVADELKAR LLKAKA
//