ID   G6PD_ECOL6              Reviewed;         491 AA.
AC   P0AC54; P22992; P78069; Q60134; Q60139;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; OrderedLocusNames=c2265;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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.
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DR   EMBL; AE014075; AAN80722.1; -; Genomic_DNA.
DR   RefSeq; NP_754157.1; -.
DR   HSSP; P11413; 1QKI.
DR   GeneID; 1036807; -.
DR   GenomeReviews; AE014075_GR; c2265.
DR   KEGG; ecc:c2265; -.
DR   HOGENOM; P0AC54; -.
DR   OMA; P0AC54; IEYAWKW.
DR   BRENDA; 1.1.1.49; 292881.
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    491       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068120.
FT   ACT_SITE    239    239       Proton acceptor (By similarity).
FT   BINDING      18     18       NADP (By similarity).
FT   BINDING      50     50       NADP (By similarity).
FT   BINDING     177    177       Substrate (By similarity).
FT   BINDING     181    181       Substrate (By similarity).
FT   BINDING     344    344       Substrate (By similarity).
SQ   SEQUENCE   491 AA;  55704 MW;  263F07D298EAFCD3 CRC64;
     MAVTQTAQAC DLVIFGAKGD LARRKLLPSL YQLEKAGQLN PDTRIIGVGR ADWDKAAYTK
     VVREALETFM KETIDEGLWD TLSARLDFCN LDVNDTAAFS RLGAMLDQKN RITINYFAMP
     PSTFGAICKG LGEAKLNAKP ARVVMEKPLG TSLATSQEIN DQVGEYFEEC QVYRIDHYLG
     KETVLNLLAL RFANSLFVNN WDNRTIDHVE ITVAEEVGIE GRWGYFDKAG QMRDMIQNHL
     LQILCMIAMS PPSDLSADSI RDEKVKVLKS LRRIDRSNVR EKTVRGQYTA GFAQGKKVPG
     YLEEEGANKS SNTETFVAIR VDIDNWRWAG VPFYLRTGKR LPTKCSEVVV YFKTPELNLF
     KESWQDLPQN KLTIRLQPDE GVDIQVLNKV PGLDHKHNLQ ITKLDLSYSE TFNQTHLADA
     YERLLLETMR GIQALFVRRD EVEEAWKWVD SITEAWAMDN DAPKPYQAGT WGPVASVAMI
     TRDGRSWNEF E
//