GenomeNet

Database: UniProt
Entry: Q06197
LinkDB: Q06197
Original site: Q06197 
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   Genevisible; Q06197; GM.
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   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
//
DBGET integrated database retrieval system