ID   IDH_MYCBO               Reviewed;         409 AA.
AC   P65098; O53389;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=Mb3371c;
OS   Mycobacterium bovis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   MEDLINE=22709107; PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA   Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA   Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA   Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(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   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; BX248345; CAD95494.1; -; Genomic_DNA.
DR   RefSeq; NP_857016.1; -.
DR   HSSP; P33198; 1LWD.
DR   GeneID; 1093830; -.
DR   GenomeReviews; BX248333_GR; Mb3371c.
DR   KEGG; mbo:Mb3371c; -.
DR   HOGENOM; P65098; -.
DR   OMA; P65098; AICIKGM.
DR   BRENDA; 1.1.1.42; 3091.
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:0006102; P:isocitrate metabolic process; IEA:InterPro.
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; IPR004790; Isocitrate_DH_NADP-dep_euk.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11822; IDH_NADP_euk; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   TIGRFAMs; TIGR00127; nadp_idh_euk; 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    409       Isocitrate dehydrogenase [NADP].
FT                                /FTId=PRO_0000083554.
FT   NP_BIND      78     80       NADP (By similarity).
FT   NP_BIND     313    318       NADP (By similarity).
FT   REGION       97    103       Substrate binding (By similarity).
FT   METAL       255    255       Magnesium or manganese (By similarity).
FT   METAL       278    278       Magnesium or manganese (By similarity).
FT   BINDING      80     80       Substrate (By similarity).
FT   BINDING      85     85       NADP (By similarity).
FT   BINDING     112    112       Substrate (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   BINDING     263    263       NADP (By similarity).
FT   BINDING     331    331       NADP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   SITE        142    142       Critical for catalysis (By similarity).
FT   SITE        215    215       Critical for catalysis (By similarity).
FT   MOD_RES      97     97       Phosphoserine (By similarity).
SQ   SEQUENCE   409 AA;  45514 MW;  FDBC1989DF42383A CRC64;
     MSNAPKIKVS GPVVELDGDE MTRVIWKLIK DMLILPYLDI RLDYYDLGIE HRDATDDQVT
     IDAAYAIKKH GVGVKCATIT PDEARVEEFN LKKMWLSPNG TIRNILGGTI FREPIVISNV
     PRLVPGWTKP IVIGRHAFGD QYRATNFKVD QPGTVTLTFT PADGSAPIVH EMVSIPEDGG
     VVLGMYNFKE SIRDFARASF SYGLNAKWPV YLSTKNTILK AYDGMFKDEF ERVYEEEFKA
     QFEAAGLTYE HRLIDDMVAA CLKWEGGYVW ACKNYDGDVQ SDTVAQGYGS LGLMTSVLMT
     ADGKTVEAEA AHGTVTRHYR QYQAGKPTST NPIASIFAWT RGLQHRGKLD GTPEVIDFAH
     KLESVVIATV ESGKMTKDLA ILIGPEQDWL NSEEFLDAIA DNLEKELAN
//