ID   G6PD_MYCBO              Reviewed;         514 AA.
AC   P0A585; O08407;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; Synonyms=zwf2; OrderedLocusNames=Mb1482c;
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 looks like a
CC       classical zwf.
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DR   EMBL; BX248339; CAD96149.1; -; Genomic_DNA.
DR   RefSeq; NP_855134.1; -.
DR   HSSP; P11413; 1QKI.
DR   GeneID; 1092339; -.
DR   GenomeReviews; BX248333_GR; Mb1482c.
DR   KEGG; mbo:Mb1482c; -.
DR   HOGENOM; P0A585; -.
DR   OMA; P0A585; SRRWAGV.
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    514       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068127.
FT   ACT_SITE    268    268       Proton acceptor (By similarity).
FT   BINDING      37     37       NADP (By similarity).
FT   BINDING      69     69       NADP (By similarity).
FT   BINDING     206    206       Substrate (By similarity).
FT   BINDING     210    210       Substrate (By similarity).
SQ   SEQUENCE   514 AA;  57343 MW;  22A9CCEDC9AB062F CRC64;
     MKPAHAAASW RNPLRDKRDK RLPRIAGPCG MVIFGVTGDL ARKKVMPAVY DLANRGLLPP
     TFSLVGFARR DWSTQDFGQV VYNAVQEHCR TPFRQQNWDR LAEGFRFVPG TFDDDDAFAQ
     LAETLEKLDA ERGTGGNHAF YLAIPPKSFP VVCEQLHKSG LARPQGDRWS RVVIEKPFGH
     DLASARELNK AVNAVFPEEA VFRIDHYLGK ETVQNILALR FANQLFDPIW NAHYVDHVQI
     TMAEDIGLGG RAGYYDGIGA ARDVIQNHLM QLLALTAMEE PVSFHPAALQ AEKIKVLSAT
     RLAEPLDQTT SRGQYAAGWQ GGEKVVGLLD EEGFAEDSTT ETFAAITLEV DTRRWAGVPF
     YLRTGKRLGR RVTEIALVFR RAPHLPFDAT MTDELGTNAM VIRVQPDEGV TLRFGSKVPG
     TAMEVRDVNM DFSYGSAFAE DSPEAYERLI LDVLLGEPSL FPVNAEVELA WEILDPALEH
     WAAHGTPDAY EAGTWGPESS LEMLRRTGRE WRRP
//