ID IDH_STAAR Reviewed; 422 AA. AC Q6GG12; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 04-NOV-2008, entry version 29. 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=SAR1773; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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 -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BX571856; CAG40764.1; -; Genomic_DNA. DR RefSeq; YP_041160.1; -. DR SMR; Q6GG12; 3-421. DR GeneID; 2861358; -. DR GenomeReviews; BX571856_GR; SAR1773. DR KEGG; sar:SAR1773; -. DR HOGENOM; Q6GG12; -. DR BioCyc; SAUR282458:SAR1773-MON; -. 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR004439; IsoCit_DHase_NADP_prok. DR InterPro; IPR001804; IsoCit_IM_DHase. 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_0000083562. 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; 46479 MW; 65A3776BC6940AA2 CRC64; MTAEKITQGT EGLNVPNEPI IPFIIGDGIG PDIWKAASRV IDAAVEKAYN GEKRIEWKEV LAGQKAFDTT GEWLPQETLD TIKEYLIAVK GPLTTPIGGG IRSLNVALRQ ELDLFTCLRP VRWFKGVPSP VKRPQDVDMV IFRENTEDIY AGIEFKEGTT EVKKVIDFLQ NEMGATNIRF PETSGIGIKP VSKEGTERLV RAAIQYAIDN NRKSVTLVHK GNIMKFTEGS FKQWGYDLAL TEFGDQVFTW QQYDEIVEKE GRDAANVAQE KAEKEGKIII KDSIADIFLQ QILTRPAEHD VVATMNLNGD YISDALAAQV GGIGIAPGAN INYETGHAIF EATHGTAPKY AGLNKVNPSS VILSSVLMLE HLGWQEAADK ITDSIEDTIA SKVVTYDFAR LMDGAEEVST SAFADELIKN LK //