ID   G6PD2_MYCBO             Reviewed;         466 AA.
AC   P0A587; O06573;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Probable glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf2; Synonyms=zwf; OrderedLocusNames=Mb1152;
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: D-glucose 6-phosphate + NADP(+) = D-glucono-
CC       1,5-lactone 6-phosphate + NADPH.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 1/3.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family.
CC   -!- CAUTION: M.bovis has two genes for zwf. This one is highly
CC       divergent.
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DR   EMBL; BX248337; CAD94013.1; -; Genomic_DNA.
DR   RefSeq; NP_854808.1; -.
DR   HSSP; P11413; 1QKI.
DR   GeneID; 1090448; -.
DR   GenomeReviews; BX248333_GR; Mb1152.
DR   KEGG; mbo:Mb1152; -.
DR   HOGENOM; P0A587; -.
DR   OMA; P0A587; TGDLAFK.
DR   BRENDA; 1.1.1.49; 3091.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001282; Glc-6-P_DH.
DR   InterPro; IPR019796; Glc-6-P_DH_AS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR23429; G6PDH; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   ProDom; PD001129; G6PD; 1.
DR   TIGRFAMs; TIGR00871; zwf; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    466       Probable glucose-6-phosphate 1-
FT                                dehydrogenase.
FT                                /FTId=PRO_0000068129.
FT   ACT_SITE    233    233       Proton acceptor (By similarity).
FT   BINDING      18     18       NADP (By similarity).
FT   BINDING      48     48       NADP (By similarity).
FT   BINDING     171    171       Substrate (By similarity).
FT   BINDING     175    175       Substrate (By similarity).
FT   BINDING     324    324       Substrate (By similarity).
SQ   SEQUENCE   466 AA;  52173 MW;  536302013052A596 CRC64;
     MVDGGGGASD LLVIFGITGD LARKMTFRAL YRLERHQLLD CPILGVASDD MSVGQLVKWA
     RESIGRTEKI DDAVFDRLAG RLSYLHGDVT DSQLYDSLAE LIGSACRPLY YLEMPPALFA
     PIVENLANVR LLERARVAVE KPFGHDLASA LELNARLRAV LGEDQILRVD HFLGKQPVVE
     LEYLRFANQA LAELWDRNSI SEIHITMAED FGVEDRGKFY DAVGALRDVV QNHLLQVLAL
     VTMEPPVGSS ADDLNDKKAE VFRAMAPLDP DRCVRGQYLG YTEVAGVASD SATETYVALR
     TEIDNWRWAG VPIFVRAGKE LPAKVTEVRL FLRRVPALAF LPNRRPAEPN QIVLRIDPDP
     GMRLQISAHT DDSWRDIHLD SSFAVDLGEP IRPYERLLYA GLVGDHQLFA REDSIEQTWR
     IVQPLLDNPG EIHRYDRGSW GPEAAQSLLR GHRGWQSPWL PRGTDA
//