ID   IDH_RICPR               Reviewed;         483 AA.
AC   Q9ZDR0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=icd; OrderedLocusNames=RP265;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AJ235271; CAA14727.1; -; Genomic_DNA.
DR   PIR; E71681; E71681.
DR   RefSeq; NP_220650.1; NC_000963.1.
DR   RefSeq; WP_010886251.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDR0; -.
DR   SMR; Q9ZDR0; -.
DR   STRING; 272947.RP265; -.
DR   EnsemblBacteria; CAA14727; CAA14727; CAA14727.
DR   KEGG; rpr:RP265; -.
DR   PATRIC; fig|272947.5.peg.272; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_1_2_5; -.
DR   OMA; EYDLGAR; -.
DR   Proteomes; UP000002480; Chromosome.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR014273; Isocitrate_DH_aproteobac-typ.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR040978; TT1725.
DR   PANTHER; PTHR11835:SF43; PTHR11835:SF43; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   Pfam; PF18324; TT1725; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR02924; ICDH_alpha; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW   Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..483
FT                   /note="Isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000083557"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            128
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            175
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   483 AA;  54318 MW;  17225FB9214E40A8 CRC64;
     MAAFTPITIA YGDGIGPEIM EAVLYILRKA EARISLETIE VGEKLYKKHY TSGISEESWD
     VIQRTGIILK APITTPQSGG YKSLNVTIRK TLQLFANIRP VVSFYPFTRT LHPNLNLTII
     RENEEDLYSG VEYRQTHNMY ESMKLISHTG CKKIIRYAFE YAIKNNRKKV TCLTKDNIMK
     FSDGIFHRVF NEIAKEYPQI NNEHYIIDIG TAKLATKPEI FDIIVTSNLY GDIISDVAAE
     ISGSVGLAGS ANIGQHYAMF EAVHGSAPDI AGKGIANPSG LLNAAIMMLV HIGQGDIASL
     IENAWKKTIE DGVHTFDIYN EHSSSKKVCT KEFAVEVIKR LGQLPITLPK AAYPLIVKKQ
     ESNIDYKIDT REVKKLVGTD IFINMHVFSA HDIADKINKL DIGNFELKTI SSKGLKLWPH
     DSRFEIISDH WCCRFMNKDG TEIKHLDITM LLQSLSKANI DFIKVENLFE FDGVAWYSLA
     QGE