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 01-MAY-2013, entry version 85.
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 (strain ATCC 700392 / 26695) (Campylobacter
OS pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX 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(+) = 6-phospho-D-
CC glucono-1,5-lactone + 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; NC_000915.1.
DR RefSeq; YP_006935016.1; NC_018939.1.
DR ProteinModelPortal; P56110; -.
DR STRING; 85962.HP1101; -.
DR PRIDE; P56110; -.
DR EnsemblBacteria; AAD08144; AAD08144; HP_1101.
DR GeneID; 13870294; -.
DR GeneID; 899637; -.
DR KEGG; heo:C694_05680; -.
DR KEGG; hpy:HP1101; -.
DR PATRIC; 20593541; VBIHelPyl33062_1150.
DR eggNOG; COG0364; -.
DR KO; K00036; -.
DR OMA; ENFSDEA; -.
DR ProtClustDB; PRK05722; -.
DR UniPathway; UPA00115; UER00408.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR PANTHER; PTHR23429; PTHR23429; 1.
DR Pfam; PF02781; G6PD_C; 2.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP;
KW Oxidoreductase; Reference proteome.
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
//
