ID   G6PD_ECOLI              Reviewed;         491 AA.
AC   P0AC53; 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 33.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=zwf; OrderedLocusNames=b1852, JW1841;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=91123224; PubMed=1704005;
RA   Rowley D.L., Wolf R.E. Jr.;
RT   "Molecular characterization of the Escherichia coli K-12 zwf gene
RT   encoding glucose 6-phosphate dehydrogenase.";
RL   J. Bacteriol. 173:968-977(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97251358; PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
RA   Yamamoto Y., Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-368.
RC   STRAIN=Various ECOR strains;
RX   MEDLINE=95064015; PubMed=7973728; DOI=10.1126/science.7973728;
RA   Guttman D.S., Dykhuizen D.E.;
RT   "Clonal divergence in Escherichia coli as a result of recombination,
RT   not mutation.";
RL   Science 266:1380-1383(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 321-491.
RC   STRAIN=K12;
RX   MEDLINE=93345818; PubMed=8344525; DOI=10.1016/0378-1119(93)90362-7;
RA   Carter A.T., Pearson B.M., Dickinson J.R., Lancashire W.E.;
RT   "Sequence of the Escherichia coli K-12 edd and eda genes of the
RT   Entner-Doudoroff pathway.";
RL   Gene 130:155-156(1993).
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   -!- INTERACTION:
CC       P0A988:dnaN; NbExp=1; IntAct=EBI-555656, EBI-542385;
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family.
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DR   EMBL; M55005; AAA24775.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74922.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15660.1; -; Genomic_DNA.
DR   EMBL; U13783; AAA57018.1; -; Genomic_DNA.
DR   EMBL; U13784; AAA57019.1; -; Genomic_DNA.
DR   EMBL; U13785; AAA57020.1; -; Genomic_DNA.
DR   EMBL; U13786; AAA57021.1; -; Genomic_DNA.
DR   EMBL; U13787; AAA57022.1; -; Genomic_DNA.
DR   EMBL; U13788; AAA57023.1; -; Genomic_DNA.
DR   EMBL; U13789; AAA57024.1; -; Genomic_DNA.
DR   EMBL; U13790; AAA57025.1; -; Genomic_DNA.
DR   EMBL; U13791; AAA57026.1; -; Genomic_DNA.
DR   EMBL; U13792; AAA57027.1; -; Genomic_DNA.
DR   EMBL; U13793; AAA57028.1; -; Genomic_DNA.
DR   EMBL; U13794; AAA57029.1; -; Genomic_DNA.
DR   EMBL; X63694; CAA45220.1; -; Genomic_DNA.
DR   PIR; D64947; D64947.
DR   RefSeq; AP_002472.1; -.
DR   RefSeq; NP_416366.1; -.
DR   HSSP; P11413; 1QKI.
DR   IntAct; P0AC53; 46.
DR   SWISS-2DPAGE; P0AC53; -.
DR   ECO2DBASE; F048.8; 6TH EDITION.
DR   GeneID; 946370; -.
DR   GenomeReviews; AP009048_GR; JW1841.
DR   GenomeReviews; U00096_GR; b1852.
DR   KEGG; ecj:JW1841; -.
DR   KEGG; eco:b1852; -.
DR   EchoBASE; EB1203; -.
DR   EcoGene; EG11221; zwf.
DR   HOGENOM; P0AC53; -.
DR   OMA; P0AC53; IEYAWKW.
DR   BioCyc; EcoCyc:GLU6PDEHYDROG-MON; -.
DR   BioCyc; MetaCyc:GLU6PDEHYDROG-MON; -.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    491       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068118.
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).
FT   VARIANT     100    100       S -> N (in strain: ECOR 4 and ECOR 10).
FT   CONFLICT    268    293       LKSLRRIDRSNVREKTVRGQYTAGFA -> PEVSSPHRPLQ
FT                                RTRKNRTRAIYCVP (in Ref. 1; AAA24775).
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
//