IDHC_TOBAC
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 03-AUG-2022, entry version 99.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PRIDE; P50218; -.
DR GeneID; 107815853; -.
DR KEGG; nta:107815853; -.
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 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 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
