ID   IDH_RICBR               Reviewed;         483 AA.
AC   Q1RJU4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=RBE_0289;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04370.1; -; Genomic_DNA.
DR   RefSeq; WP_011476981.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJU4; -.
DR   SMR; Q1RJU4; -.
DR   KEGG; rbe:RBE_0289; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_1_2_5; -.
DR   OrthoDB; 9767905at2; -.
DR   Proteomes; UP000001951; 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   Gene3D; 3.30.70.1570; -; 1.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR014273; Isocitrate_DH_bac-typ.
DR   InterPro; IPR040978; Isocitrate_DH_TT1725_C.
DR   InterPro; IPR046997; Isocitrate_DH_TT1725_C_sf.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR02924; ICDH_alpha; 1.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF43; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   Pfam; PF18324; Isocitrate_DH_C_bact; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass; Magnesium; Metal-binding; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..483
FT                   /note="Isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000292202"
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;  53959 MW;  D02F3B5F38A5FF9D CRC64;
     MAEFTPITIA YGDGIGPEIM EAVLYILRKA EARIRLETIE VGEKLYVKHY SSGISEQSWE
     SIERTGVILK APITTPQGGG YKSLNVTIRK TLQLFANIRP SVSFYPFTKT LHPNLNLTII
     RENEEDLYAG IEYRQTHNMY ESVKLISRTG CEKIIRYAFE YAVKNNRKKV TCLSKDNIMK
     FSDGIFHKVF NEIAKEYPQI NNEHYIIDIG TARLATKPEI FDVIVTSNLY GDIISDVAAE
     ISGSVGLAGS ANIGEHYAMF EAVHGSAPDI AGQDIANPSG LLNAAIMMLV HIGQGDIATL
     IENAWKKTIE DGMHTADIYN KDHSTKKVGT KEFAEEVVKR LGQKPEKLAK ADYPLVTKKQ
     ESNTTYKINT KEVKKLVGTD IFVGMNVASA HDIADKVNKL DIGNFELKTI SSKGLKLWPR
     DTRFETISDH WCCRFMAKDG VELKHLDITK LLETLSKANI DFIKVENLFE FDGAAGYSLA
     QGE
//