ID   IDHC_TOBAC              Reviewed;         415 AA.
AC   P50218;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Isocitrate dehydrogenase [NADP];
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=IDP;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=Oxalosuccinate decarboxylase;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8616254; DOI=10.1007/bf00020116;
RA   Galvez S., Hodges M., Decottignies P., Lancien M., Sangwan R., Dubois F.,
RA   Lemarechal P., Cretin C., Gadal P.;
RT   "Identification of a tobacco cDNA encoding a cytosolic NADP-isocitrate
RT   dehydrogenase.";
RL   Plant Mol. Biol. 30:307-320(1996).
CC   -!- FUNCTION: May supply 2-oxoglutarate for amino acid biosynthesis and
CC       ammonia assimilation via the glutamine synthetase/glutamate synthase
CC       (GS/GOGAT) pathway. {ECO:0000250}.
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: Heterodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; X77944; CAA54912.1; -; mRNA.
DR   PIR; S65065; S65065.
DR   RefSeq; NP_001312892.1; NM_001325963.1.
DR   AlphaFoldDB; P50218; -.
DR   SMR; P50218; -.
DR   STRING; 4097.P50218; -.
DR   PaxDb; 4097-P50218; -.
DR   GeneID; 107815853; -.
DR   KEGG; nta:107815853; -.
DR   OrthoDB; 423at2759; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006739; P:NADP metabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW   Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..415
FT                   /note="Isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000083586"
FT   BINDING         77..79
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         96..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
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            141
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            214
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   415 AA;  46729 MW;  F9469AA113DB2CFC CRC64;
     MTFDKIKVEN PIVEMDGDEM TRVIWKSIKD KLICPFLELD IKYFDLGLPH RDATDDKVTV
     ESAEATQKYN VAIKCATITP DEARVKEFNL KSMWRSPNGT IRNILNGTVF REPIMCKNIP
     RLVPGWTKPI CIGRHAFGDQ YRATDTVIQG AGKLKLVFVP EGTDEKTEFE VYNFTGAGGV
     ALSMYNTDES VRSFAEASMN MAYQKKWPLY LSTKNTILKK YDGRFKDIFQ EVYEANWKSK
     YEEAGIWYEH RLIDDMAAYA LKSEGGYVWA CKNYDGDVQS DFLAQGFGSL GLMTSVLVCP
     DGKTIEAEAA HGTVTRHYRV HQKGGETSTN SIASIFAWTR GLAHRATLDN NERLLDFTEK
     LEAACIGAVE SGKMTKDLAL IIHGSKLSRD HYLNTEEFID AVADELKARL LKAKA
//