ID IDHC_SOYBN Reviewed; 413 AA. AC Q06197; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 27-MAR-2024, entry version 137. DE RecName: Full=Isocitrate dehydrogenase [NADP]; DE Short=IDH; DE EC=1.1.1.42 {ECO:0000269|PubMed:8467073}; DE AltName: Full=IDP; DE AltName: Full=NADP(+)-specific ICDH; DE AltName: Full=Oxalosuccinate decarboxylase; GN Name=IDH1; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine; OC Glycine subgen. Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND COFACTOR. RC STRAIN=cv. Harosoy-L1; TISSUE=Root nodule; RX PubMed=8467073; DOI=10.1007/bf00027108; RA Udvardi M.K., McDermott T.R., Kahn M.L.; RT "Isolation and characterization of a cDNA encoding NADP(+)-specific RT isocitrate dehydrogenase from soybean (Glycine max)."; RL Plant Mol. Biol. 21:739-752(1993). 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 Evidence={ECO:0000269|PubMed:8467073}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:8467073}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:8467073}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000250|UniProtKB:O88844}; CC -!- SUBUNIT: Heterodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Leaves, nodules and roots with the relative amount CC of 1:3.4:7.7. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA33978.1; 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; L12157; AAA33978.1; ALT_INIT; mRNA. DR RefSeq; XP_014622642.1; XM_014767156.1. DR AlphaFoldDB; Q06197; -. DR SMR; Q06197; -. DR STRING; 3847.Q06197; -. DR PaxDb; 3847-GLYMA14G39160-2; -. DR ProMEX; Q06197; -. DR EnsemblPlants; KRH17285; KRH17285; GLYMA_14G211000. DR Gramene; KRH17285; KRH17285; GLYMA_14G211000. DR eggNOG; KOG1526; Eukaryota. DR HOGENOM; CLU_023296_1_1_1; -. DR InParanoid; Q06197; -. DR OMA; EYPVYNF; -. DR OrthoDB; 423at2759; -. DR Proteomes; UP000008827; Chromosome 14. 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. DR Genevisible; Q06197; GM. PE 1: Evidence at protein level; KW Cytoplasm; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; KW Oxidoreductase; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..413 FT /note="Isocitrate dehydrogenase [NADP]" FT /id="PRO_0000083585" FT BINDING 78..80 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 80 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 85 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 97..103 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 112 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 135 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 215 FT /ligand="substrate" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000250|UniProtKB:O88844" FT BINDING 255 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 263 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 278 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 282 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 313..318 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT BINDING 331 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:O75874" FT SITE 142 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT SITE 215 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" SQ SEQUENCE 413 AA; 46050 MW; 78B90E53C6D686B5 CRC64; MAAFQKIKVA NPIVEMDGDE MTRVIWKSIK DKLILPFLEL DIKYYDLGLP YRDETDDKVT IESAEATLKY NVAIKCATIT PDEARVKEFG LKSMWKSPNG TIRNILNGTV FREPILCKNI PRLVPGWTKA ICIGRHAFGD QYRATDTVIK GAGKLKLVFV PEGQGEETEF EVFNFTGEGG VSLAMYNTDE SIRSFAEASM ATALEKKWPL YLSTKNTILK KYDGRFKDIF QEVYEASWKS KFEAAGIWYE HRLIDDMVAY ALKSEGGYVW ACKNYDGDVQ SDFLAQGFGS LGLMTSVLVC PDGKTIEAEA AHGTVTRHFR VHQKGGETST NSIASIFAWT RGLAHRAKLD DNAKLLDFTE KLEAACIGVV EAGKMTKDLA LILHGSKLSR EHYLNTEEFI DAVAAELSAR LSA //