ID   IDH_RICCN               Reviewed;         483 AA.
AC   Q92IR7;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=RC0353;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02891.1; -; Genomic_DNA.
DR   PIR; A97744; A97744.
DR   RefSeq; WP_010977008.1; NC_003103.1.
DR   AlphaFoldDB; Q92IR7; -.
DR   SMR; Q92IR7; -.
DR   GeneID; 927516; -.
DR   KEGG; rco:RC0353; -.
DR   PATRIC; fig|272944.4.peg.402; -.
DR   HOGENOM; CLU_031953_1_2_5; -.
DR   Proteomes; UP000000816; 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; Manganese; Metal-binding; NADP;
KW   Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
FT   CHAIN           1..483
FT                   /note="Isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000083556"
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;  53936 MW;  126975F8A50545A4 CRC64;
     MAEFTPITIA YGDGIGPEIM EAVLYILRKA EARIRLETIE VGEKLYKKHY TSGISEESWE
     SIQRTGIILK APITTPQGGG YKSLNVTIRK TLQLFANIRP AVSLHPFTRT LHPNLNLTII
     RENEEDLYAG IEYRQTHNMY ESMKLISHTG CEKIIRYAFE YAVKNNRKKV MCLSKDNIMK
     FSDGVLHKVF NEIAKEYPQI NNAHYIIDIG TARLATKPEI FDVIVTSNLY GDIISDVAAE
     ISGSVGLAGS ANIGQHYAMF EAVHGSAPDI AGKDIANPSG LLNAAIMMLV HIGQGDIATL
     IENAWKKTIE DGVHTADIYN EQSSSKKVGT KEFAEEVTKR LGQLPTKLPK ADYPLIAEKQ
     ESNIDYKIDT KEVKKLVGTD IFVNMNVSSA HDIADKINKL DLGNFELKTI SSKGLKLWPR
     DTRFETVSDH WCCRFMNKDG TEIKHLDITR LLEALSTANI DFIKVENLFE FDGVAGYSLA
     QGE
//