ID   IDH_RICTY               Reviewed;         483 AA.
AC   Q68XA5;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Isocitrate dehydrogenase [NADP];
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=Oxalosuccinate decarboxylase;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=IDP;
GN   Name=icd; OrderedLocusNames=RT0256;
OS   Rickettsia typhi.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=785;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/JB.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K.,
RA   Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C.,
RA   Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G.,
RA   Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with
RT   sequences of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2)
CC       + NADPH.
CC   -!- CATALYTIC ACTIVITY: Oxalosuccinate + NADP(+) = 2-oxoglutarate +
CC       CO(2) + NADPH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AE017197; AAU03737.1; -; Genomic_DNA.
DR   RefSeq; YP_067219.1; -.
DR   GeneID; 2958917; -.
DR   GenomeReviews; AE017197_GR; RT0256.
DR   KEGG; rty:RT0256; -.
DR   HOGENOM; Q68XA5; -.
DR   OMA; Q68XA5; DNIMKMT.
DR   BioCyc; RTYP257363:RT0256-MON; -.
DR   BRENDA; 1.1.1.42; 281221.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR014273; Isocitrate_DH_bac.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR02924; ICDH_alpha; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glyoxylate bypass; Magnesium; Manganese;
KW   Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    483       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083558.
FT   METAL       208    208       Magnesium or manganese (By similarity).
FT   METAL       232    232       Magnesium or manganese (By similarity).
FT   METAL       236    236       Magnesium or manganese (By similarity).
FT   BINDING      89     89       Substrate (By similarity).
FT   BINDING      99     99       Substrate (By similarity).
FT   BINDING     121    121       Substrate (By similarity).
FT   BINDING     208    208       Substrate (By similarity).
FT   SITE        128    128       Critical for catalysis (By similarity).
FT   SITE        175    175       Critical for catalysis (By similarity).
FT   MOD_RES      83     83       Phosphoserine (By similarity).
SQ   SEQUENCE   483 AA;  54161 MW;  D6AAA410411169AF CRC64;
     MAEFTPITIA YGDGIGPEIM DAVLYILRQA EARISLETIE VGEKLYKKHY TSGISEESWN
     VIQRTGIILK APITTPQSGG YKSLNVTIRK TLQLFANIRP AVSFHPFTRT LHPNLNLTII
     RENEEDLYSG IEYRQTHNMY ESLKLISHTG CKKIIRYAFE YAVKNNRKKV TCLSKDNIMK
     FSDGIFHRVF NEIAKEYPQI DNEHYIIDIG TAKLATTPEI FDIIVTSNLY GDIISDVAAE
     ISGSVGLAGS ANIGQHYAMF EAVHGSAPDI AGKGIANPSG LLNAAIMMLV HIGQGDIASL
     IENAWKKTIE DGVHTFDIYS EHSSSKKVCT KEFAEEVIKR LGQLPMTLPK ASYPLIVKKQ
     ESKIEYKIDT TEVKKLVGTD IFINIHVFSA HDIADKINKL DIGNFELKTI SSKGLKLWPH
     DLRFEIISDH WCCRFMNKDG TEIKHLDIII LLQALSKANI DFIKVENLFE FDGVACYSLA
     QGE
//