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 27-MAR-2024, entry version 116. 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; GN Name=ICDH-1; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Desiree; TISSUE=Leaf; RX 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 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 -!- SEQUENCE CAUTION: CC Sequence=CAA53300.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; X75638; CAA53300.1; ALT_INIT; mRNA. DR PIR; S47013; S47013. DR PIR; T07402; T07402. DR AlphaFoldDB; P50217; -. DR SMR; P50217; -. DR STRING; 4113.P50217; -. DR PaxDb; 4113-PGSC0003DMT400081790; -. DR eggNOG; KOG1526; Eukaryota. DR InParanoid; P50217; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; P50217; baseline and differential. 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..416 FT /note="Isocitrate dehydrogenase [NADP]" FT /id="PRO_0000083584" 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 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 //