ID   IDH_STAES               Reviewed;         422 AA.
AC   Q8CNX4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 42.
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; Synonyms=citC; OrderedLocusNames=SE_1370;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AE015929; AAO04969.1; -; Genomic_DNA.
DR   RefSeq; NP_764925.1; -.
DR   HSSP; P39126; 1HQS.
DR   SMR; Q8CNX4; 3-421.
DR   GeneID; 1058012; -.
DR   GenomeReviews; AE015929_GR; SE_1370.
DR   KEGG; sep:SE1370; -.
DR   HOGENOM; Q8CNX4; -.
DR   OMA; Q8CNX4; RDWGYEL.
DR   BioCyc; SEPI176280:SE_1370-MON; -.
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; IPR004439; Isocitrate_DH_NADP_prok.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   PANTHER; PTHR11835:SF1; NADP_IDH_prok; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR00183; prok_nadp_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glyoxylate bypass; Magnesium; Manganese;
KW   Metal-binding; NADP; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    422       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083565.
FT   NP_BIND     344    350       NADP (By similarity).
FT   METAL       310    310       Magnesium or manganese (By similarity).
FT   BINDING      94     94       NADP (By similarity).
FT   BINDING     103    103       Substrate (By similarity).
FT   BINDING     105    105       Substrate (By similarity).
FT   BINDING     109    109       Substrate (By similarity).
FT   BINDING     119    119       Substrate (By similarity).
FT   BINDING     143    143       Substrate (By similarity).
FT   BINDING     357    357       NADP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     396    396       NADP (By similarity).
FT   BINDING     400    400       NADP (By similarity).
FT   SITE        150    150       Critical for catalysis (By similarity).
FT   SITE        220    220       Critical for catalysis (By similarity).
SQ   SEQUENCE   422 AA;  46619 MW;  31EA599CF275A83C CRC64;
     MSAEKITQSK DGLNVPNEPI IPFIIGDGIG PDIWKAASRV IDAAVEKAYN GEKRIEWKEV
     LAGQKAYDET GEWLPQETLE TIKEYLIAVK GPLTTPIGGG IRSLNVALRQ ELDLFTCLRP
     VRWFKGVPSP VKRPEDVDMV IFRENTEDIY AGIEFKQGTS EVKKVIDFLQ NEMGATNIRF
     PETSGIGIKP VSKEGTERLV RAAIQYALDN NRKSVTLVHK GNIMKFTEGS FKQWGYDLAH
     NEFGDKVFTW QQYDEIVEQK GKDAANEAQS KAEQEGKIII KDSIADIFLQ QILTRPAEHD
     VVATMNLNGD YISDALAAQV GGIGIAPGAN INYETGHAIF EATHGTAPKY AGLNKVNPSS
     EILSSVLMLE HLGWQEAADK ITDSIEATIA SKIVTYDFAR LMDGAKEVST SDFADELIKN
     IR
//