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   27-MAR-2024, entry version 134.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966};
DE            Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
DE            EC=1.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00966};
DE   Contains:
DE     RecName: Full=Extracellular death factor {ECO:0000303|PubMed:17962566};
DE              Short=EDF;
GN   Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966};
GN   OrderedLocusNames=b1852, JW1841;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1704005; DOI=10.1128/jb.173.3.968-977.1991;
RA   Rowley D.L., Wolf R.E. Jr.;
RT   "Molecular characterization of the Escherichia coli K-12 zwf gene encoding
RT   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   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., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   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   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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(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 MG1655
RT   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   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, not
RT   mutation.";
RL   Science 266:1380-1383(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 321-491.
RC   STRAIN=K12;
RX   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 Entner-
RT   Doudoroff pathway.";
RL   Gene 130:155-156(1993).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   FUNCTION, AND PATHWAY.
RC   STRAIN=K12 / BW25113;
RX   PubMed=15113569; DOI=10.1016/j.ymben.2004.02.004;
RA   Zhao J., Baba T., Mori H., Shimizu K.;
RT   "Effect of zwf gene knockout on the metabolism of Escherichia coli grown on
RT   glucose or acetate.";
RL   Metab. Eng. 6:164-174(2004).
RN   [9]
RP   FUNCTION AS EXTRACELLULAR DEATH FACTOR (EDF), POSSIBLE PROTEOLYTIC
RP   PROCESSING, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=17962566; DOI=10.1126/science.1147248;
RA   Kolodkin-Gal I., Hazan R., Gaathon A., Carmeli S., Engelberg-Kulka H.;
RT   "A linear pentapeptide is a quorum-sensing factor required for mazEF-
RT   mediated cell death in Escherichia coli.";
RL   Science 318:652-655(2007).
RN   [10]
RP   EDF PRODUCTION, AND STRAIN DIFFERENCES IN ABILITY TO MAKE AND RESPOND TO
RP   EDF.
RC   STRAIN=K12 / K38 / S26, K12 / MC4100 / ATCC 35695 / DSM 6574, K12 /
RC   MG1655 / ATCC 47076, and K12 / W3110;
RX   PubMed=18310334; DOI=10.1128/jb.01918-07;
RA   Kolodkin-Gal I., Engelberg-Kulka H.;
RT   "The extracellular death factor: physiological and genetic factors
RT   influencing its production and response in Escherichia coli.";
RL   J. Bacteriol. 190:3169-3175(2008).
RN   [11]
RP   FUNCTION AS EDF, INTERACTION OF EDF WITH MAZF, AND SUBUNIT.
RX   PubMed=21419338; DOI=10.1016/j.molcel.2011.02.023;
RA   Belitsky M., Avshalom H., Erental A., Yelin I., Kumar S., London N.,
RA   Sperber M., Schueler-Furman O., Engelberg-Kulka H.;
RT   "The Escherichia coli extracellular death factor EDF induces the
RT   endoribonucleolytic activities of the toxins MazF and ChpBK.";
RL   Mol. Cell 41:625-635(2011).
RN   [12]
RP   INTERACTION WITH CEDA.
RX   PubMed=28818726; DOI=10.1016/j.ijbiomac.2017.08.073;
RA   Sharma P., Tomar A.K., Kundu B.;
RT   "Identification of functional interactome of a key cell division regulatory
RT   protein CedA of E.coli.";
RL   Int. J. Biol. Macromol. 106:763-767(2018).
CC   -!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
CC       phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966,
CC       ECO:0000269|PubMed:15113569, ECO:0000269|PubMed:17962566}.
CC   -!- FUNCTION: Probable source of extracellular death factor (EDF, sequence
CC       Asn-Asn-Trp-Asn-Asn, NNWNN) following processing and amidation. This
CC       pentapeptide stimulates cell death mediated by MazF (PubMed:17962566).
CC       Artificial peptides with altered sequence show that NNGNN, GNWNG and
CC       NWN no longer stimulate MazF's endoribonuclease activity; other
CC       peptides (NNGN, GNWMM, NNWNG, NNNWNNN) retain MazF-stimulating
CC       activity. NNWNN, NNGN, GNWMM and NNWNG prevent cognate antitoxin MazE
CC       from inhibiting MazF; although NNNWNNN stimulates MazF it does not do
CC       so in the presence of MazE. EDF also stimulates ChpB's endoribonuclease
CC       activity in vitro; in this case NWN partially stimulates ChpB, whereas
CC       NNGNN, GNWNN, NNWNG, GNWNG and NNNWNNN do not. Only the wild-type EDF
CC       peptide prevents cognate antitoxin ChpS from inhibiting ChpB
CC       (PubMed:21419338). {ECO:0000269|PubMed:17962566,
CC       ECO:0000269|PubMed:21419338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC         lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00966};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:15113569}.
CC   -!- SUBUNIT: EDF binds to MazF; mutated EDF (sequence NNGNN) does not
CC       (PubMed:21419338). In pull-down experiments interacts with CedA
CC       (PubMed:28818726). {ECO:0000269|PubMed:21419338,
CC       ECO:0000269|PubMed:28818726}.
CC   -!- INTERACTION:
CC       P0AC53; P0A988: dnaN; NbExp=2; IntAct=EBI-555656, EBI-542385;
CC       P0AC53; P0AC53: zwf; NbExp=2; IntAct=EBI-555656, EBI-555656;
CC   -!- PTM: Probably processed by the ClpPX protease to generate the
CC       extracellular death factor (EDF). It is thought that processing
CC       produces Asn-Asn-Trp-Asp-Asn which is amidated to generate Asn-Asn-Trp-
CC       Asn-Asn (Probable). {ECO:0000305|PubMed:17962566}.
CC   -!- DISRUPTION PHENOTYPE: Loss of production of extracellular death factor.
CC       {ECO:0000269|PubMed:17962566}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00966}.
CC   -!- CAUTION: Strain K12 / MG1655 is deficient in both production and
CC       response to EDF, unlike strains K12 / MC4100, K12 / W3110 and K12 /
CC       K38, all of which make and respond to EDF.
CC       {ECO:0000305|PubMed:18310334}.
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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; NP_416366.1; NC_000913.3.
DR   RefSeq; WP_000301727.1; NZ_STEB01000009.1.
DR   AlphaFoldDB; P0AC53; -.
DR   SMR; P0AC53; -.
DR   BioGRID; 4259154; 32.
DR   DIP; DIP-35780N; -.
DR   IntAct; P0AC53; 48.
DR   MINT; P0AC53; -.
DR   STRING; 511145.b1852; -.
DR   jPOST; P0AC53; -.
DR   PaxDb; 511145-b1852; -.
DR   EnsemblBacteria; AAC74922; AAC74922; b1852.
DR   GeneID; 83576926; -.
DR   GeneID; 946370; -.
DR   KEGG; ecj:JW1841; -.
DR   KEGG; eco:b1852; -.
DR   PATRIC; fig|1411691.4.peg.397; -.
DR   EchoBASE; EB1203; -.
DR   eggNOG; COG0364; Bacteria.
DR   HOGENOM; CLU_013524_5_0_6; -.
DR   InParanoid; P0AC53; -.
DR   OMA; ERAGYYE; -.
DR   OrthoDB; 9802739at2; -.
DR   PhylomeDB; P0AC53; -.
DR   BioCyc; EcoCyc:GLU6PDEHYDROG-MONOMER; -.
DR   BioCyc; MetaCyc:GLU6PDEHYDROG-MONOMER; -.
DR   SABIO-RK; P0AC53; -.
DR   UniPathway; UPA00115; UER00408.
DR   PRO; PR:P0AC53; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:EcoCyc.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IMP:EcoCyc.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR   GO; GO:0009372; P:quorum sensing; IMP:EcoCyc.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00966; G6PD; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00871; zwf; 1.
DR   PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
DR   SWISS-2DPAGE; P0AC53; -.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase;
KW   Quorum sensing; Reference proteome.
FT   CHAIN           1..491
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068118"
FT   CHAIN           199..203
FT                   /note="Extracellular death factor"
FT                   /id="PRO_0000404298"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         50
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         92..93
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         147
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00966"
FT   VARIANT         100
FT                   /note="S -> N (in strain: ECOR 4 and ECOR 10)"
FT   CONFLICT        268..293
FT                   /note="LKSLRRIDRSNVREKTVRGQYTAGFA -> PEVSSPHRPLQRTRKNRTRAIY
FT                   CVP (in Ref. 1; AAA24775)"
FT                   /evidence="ECO:0000305"
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
//