ID   IDHP_MEDSA              Reviewed;         433 AA.
AC   Q40345;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Isocitrate dehydrogenase [NADP], chloroplastic;
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=IDP;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   Flags: Precursor; Fragment;
OS   Medicago sativa (Alfalfa).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1281435; DOI=10.1007/bf00027151;
RA   Shorrosh B.S., Dixon R.A.;
RT   "Molecular characterization and expression of an isocitrate dehydrogenase
RT   from alfalfa (Medicago sativa L).";
RL   Plant Mol. Biol. 20:801-807(1992).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in all tissues examined.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; M93672; AAA32656.1; -; mRNA.
DR   PIR; S28423; S28423.
DR   PIR; T09619; T09619.
DR   AlphaFoldDB; Q40345; -.
DR   SMR; Q40345; -.
DR   PRIDE; Q40345; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
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   Chloroplast; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW   Oxidoreductase; Plastid; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         <1..21
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..433
FT                   /note="Isocitrate dehydrogenase [NADP], chloroplastic"
FT                   /id="PRO_0000014427"
FT   BINDING         98..100
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         333..338
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         351
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            162
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            235
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   433 AA;  48383 MW;  E4421317B8A2CFE3 CRC64;
     QFSPNLSFSA FFPIITFTTA TMGFQKIKVA NPIVEMDGDE MTRIIWKYIK DKLIFPFVEL
     DIKYFDLGLP YRDETNDKVT VESAEATLKY NVAIKCATIT PDEARVKEFG LKSMWRSPNG
     TIRNILNGTV FREPIICKNI PRLIPGWTKP ICIGRHAFGD QYRATDSVIK GPGKLKLVFV
     PEGQGETTDL EVYNFTGEGG VALAMYNTDE SIRSFAEASM AVALEKKWPL YLSTKNTILK
     KYDGRFKDIF QEVYEAGWKS KYEAAGIWYE HRLIDDMVAY ALKSEGGYVW ACKNYDGDVQ
     SDFLAQGFGS LGLMTSVLVC PDGKTIEAEA AHGTVTRHFR VHQKGGETST NSIASIFAWT
     RGLAHRAKLD DNATLLDFTE KLEAACIGVV ESGKMTKDLA LILHGSKLSR EHYLNTEEFI
     DAVAAELKTK ISA