ID IDH_STAAW Reviewed; 422 AA. AC Q8NW61; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 25-NOV-2008, entry version 36. 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=MW1638; OS Staphylococcus aureus (strain MW2). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=196620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5; RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., RA Yamamoto K., Hiramatsu K.; RT "Genome and virulence determinants of high virulence community- RT acquired MRSA."; RL Lancet 359:1819-1827(2002). 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; BA000033; BAB95503.1; -; Genomic_DNA. DR RefSeq; NP_646455.1; -. DR HSSP; P39126; 1HQS. DR SMR; Q8NW61; 3-421. DR GeneID; 1003750; -. DR GenomeReviews; BA000033_GR; MW1638. DR KEGG; sam:MW1638; -. DR HOGENOM; Q8NW61; -. DR BioCyc; SAUR196620:MW1638-MON; -. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:InterPro. 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 GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. 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_0000083564. 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; 46437 MW; 11AE808D40093BC7 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 SEFGDQVFTW QQYDEIVEKE GRDAANAAQE KAEKEGKIII KDSIADIFLQ QILTRPAEHD VVATMNLNGD YISDALAAQV GGIGIAPGAN INYETGHAIF EATHGTAPKY AGLNKVNPSS VILSSVLMLE HLGWQEAADK ITDSIEDTIA SKVVTYDFAR LMDGAEEVST SAFADELIKN LK //