IDHC_SOYBN
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 03-AUG-2022, entry version 129.
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.GLYMA14G39160.2; -.
DR PRIDE; Q06197; -.
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; IQKRWPL; -.
DR OrthoDB; 769322at2759; -.
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 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 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
