ID   G6PD_HELPY              Reviewed;         425 AA.
AC   P56110;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-NOV-2008, entry version 53.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; OrderedLocusNames=HP_1101;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD08144.1; -; Genomic_DNA.
DR   PIR; E64657; E64657.
DR   RefSeq; NP_207892.1; -.
DR   HSSP; P11411; 1DPG.
DR   GeneID; 899637; -.
DR   GenomeReviews; AE000511_GR; HP_1101.
DR   KEGG; hpy:HP1101; -.
DR   NMPDR; fig|85962.1.peg.1088; -.
DR   TIGR; HP_1101; -.
DR   HOGENOM; P56110; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001282; Glc-6-P_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
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   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    425       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068123.
FT   ACT_SITE    225    225       Proton acceptor (By similarity).
FT   BINDING      12     12       NADP (By similarity).
FT   BINDING      44     44       NADP (By similarity).
FT   BINDING     165    165       Substrate (By similarity).
FT   BINDING     169    169       Substrate (By similarity).
SQ   SEQUENCE   425 AA;  49541 MW;  EF5A5C1C5AC7B6DB CRC64;
     MLDFDLVLFG ATGDLAMRKL FVSLYEIYTH YGFKNDSRII ASGRKELSNE EFLTLLCEKT
     QLHSREKGRE FLAHISYLCV RLDNPKDFEE LSKIATKNKP LIFYFSISPS FFATTAQHLA
     KNALNHANTR LILEKPLGHD LKTCKEIFQS ISVFFKEEQI FRIDHYLGKK GVQNILELRL
     NNPILNILWD QISAVEICVY ETLGVEERGE FYDKIGALRD MVQNHLLQVL SLIATDLPNN
     LKDLRKEKIK VLKTLQPPKD FKKQVIRAQY QGYRDENKVH KESQTETFVA IKAFLDTPKF
     KGVPFYLKHA KKMPHNQASV KIHFNAVNTL EFFLSQDKIT LTLKDHQNPL ILETHNKQEF
     LRPYAKLLYD AIQNNHNNFA HQLELEASWV FIDTLIEGFM NNATPLYSYE SHHLNESEFL
     KPLYQ
//