ID   IDH_RICFE               Reviewed;         483 AA.
AC   Q4UKR1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
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=RF_1015;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY61866.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000053; AAY61866.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041405360.1; NC_007109.1.
DR   AlphaFoldDB; Q4UKR1; -.
DR   SMR; Q4UKR1; -.
DR   STRING; 315456.RF_1015; -.
DR   EnsemblBacteria; AAY61866; AAY61866; RF_1015.
DR   KEGG; rfe:RF_1015; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_1_2_5; -.
DR   OrthoDB; 1551125at2; -.
DR   Proteomes; UP000008548; 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; Metal-binding; NADP; Oxidoreductase;
KW   Phosphoprotein; Tricarboxylic acid cycle.
FT   CHAIN           1..483
FT                   /note="Isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000292203"
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;  54062 MW;  57322A4AD6884B3C CRC64;
     MAEFTPITIA YGDGIGPEIM EAVLYILRKA EARIRLETIE VGEKLYKKHY TSGISEESWE
     SIQRTGIILK APITTPQGGG YKSLNVTIRK TLQLFANIRP SVSFHPFTMT LHPHLNLTII
     RENEEDLYAG IEYRQTHNMY ESIKLISHTG CEKIIRYAFE YAVKNNRKKV TCLSKDNIMK
     FSDGVFHKIF NEIAKEYPQI NNEHYIIDIG TARLATKPEI FDVIVTSNLY GDIISDVAAE
     ISGSVGLAGS ANIGQHYAMF EAVHGSAPDI AGKDIANPSG LLNAAIMMLV HIGQGDIASL
     IENAWKKTIE DGVHTADIYN EQNSSKKVGT KEFAEEVTKR LGQIPTKLPK ADYPLIAEKQ
     ESNIDYKIDT NEVKKLVGTD IFVNMNISSA HDIADKINKL DLGNIELKTI SSKGLKLWPR
     DTRFETISDH WCCRFMNKDG TEIKHLDITR LLEALSKANI DFIKVENLFE FDGVAGYSLA
     QGE