ID   6PGL_ECO5E              Reviewed;         331 AA.
AC   B5YRG5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=6-phosphogluconolactonase {ECO:0000255|HAMAP-Rule:MF_01605};
DE            Short=6-P-gluconolactonase {ECO:0000255|HAMAP-Rule:MF_01605};
DE            EC=3.1.1.31 {ECO:0000255|HAMAP-Rule:MF_01605};
GN   Name=pgl {ECO:0000255|HAMAP-Rule:MF_01605};
GN   OrderedLocusNames=ECH74115_0870;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-
CC       phosphogluconate. {ECO:0000255|HAMAP-Rule:MF_01605}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
CC         + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01605};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       2/3. {ECO:0000255|HAMAP-Rule:MF_01605}.
CC   -!- SIMILARITY: Belongs to the cycloisomerase 2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01605}.
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DR   EMBL; CP001164; ACI36252.1; -; Genomic_DNA.
DR   RefSeq; WP_000815433.1; NC_011353.1.
DR   AlphaFoldDB; B5YRG5; -.
DR   SMR; B5YRG5; -.
DR   KEGG; ecf:ECH74115_0870; -.
DR   HOGENOM; CLU_038716_2_0_6; -.
DR   OMA; EGNWPRD; -.
DR   UniPathway; UPA00115; UER00409.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_01605; 6P_gluconolactonase; 1.
DR   InterPro; IPR022528; 6-phosphogluconolactonase_YbhE.
DR   InterPro; IPR019405; Lactonase_7-beta_prop.
DR   InterPro; IPR011045; N2O_reductase_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF10282; Lactonase; 1.
DR   SUPFAM; SSF50974; SSF50974; 1.
PE   3: Inferred from homology;
KW   Acetylation; Carbohydrate metabolism; Glucose metabolism; Hydrolase.
FT   CHAIN           1..331
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_1000148151"
FT   MOD_RES         287
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01605"
SQ   SEQUENCE   331 AA;  36391 MW;  BC4A7F215D231BDE CRC64;
     MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV
     LAYRIAPDDG ALTFAAESAL PGSPTHISTD HQGQFVFVGS YNAGNVSVTR LEDGLPVGVV
     DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH
     MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG
     RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NIDHRGKYLI AAGQKSHHIS
     VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H