ID   6PGL_YERPB              Reviewed;         334 AA.
AC   B2K8S8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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}; OrderedLocusNames=YPTS_1259;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001048; ACC88234.1; -; Genomic_DNA.
DR   RefSeq; WP_011191955.1; NZ_CP009780.1.
DR   AlphaFoldDB; B2K8S8; -.
DR   SMR; B2K8S8; -.
DR   GeneID; 66842386; -.
DR   KEGG; ypb:YPTS_1259; -.
DR   PATRIC; fig|502801.10.peg.608; -.
DR   OMA; EGNWPRD; -.
DR   BioCyc; YPSE502801:YPTS_RS06495-MON; -.
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   Carbohydrate metabolism; Glucose metabolism; Hydrolase.
FT   CHAIN           1..334
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_1000148170"
SQ   SEQUENCE   334 AA;  36445 MW;  4BDAC8AA5983B4B0 CRC64;
     MKQAVYVASP DSQQIHVWQL DSAGELTLLQ TVDVPGQVQP MAISPNQRHL YVGVRPDFGI
     VSYHIADDGT LTAAGMAPLP GSPTHIDTDR QGRFLFSASY SFNCVSISPI DTHGVVQAPI
     QQLDDLPAPH SANIDPTNQI LLVPCLKEDK VRLFDLSAEG QLTPHAQADI TVAAGAGPRH
     MAFHPNHQVA YCVNELNSSV DVYQISNNGQ EYHLVQSLDA MPADFTGTRW AADIHITPNG
     RYLYISDRTA NLLGIFTVSK DGRVISLVGH HLTEAQPRGF NIDHSGNFLI ASGQKSDHIE
     VYRIDQNTGE LTTLKRYPVG KGPMWVSIRG AQNS