ID   6PGL_SALPB              Reviewed;         331 AA.
AC   A9MTJ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=SPAB_02735;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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; CP000886; ABX68113.1; -; Genomic_DNA.
DR   RefSeq; WP_000815474.1; NC_010102.1.
DR   AlphaFoldDB; A9MTJ8; -.
DR   SMR; A9MTJ8; -.
DR   KEGG; spq:SPAB_02735; -.
DR   PATRIC; fig|1016998.12.peg.2587; -.
DR   HOGENOM; CLU_038716_2_0_6; -.
DR   OMA; EGNWPRD; -.
DR   BioCyc; SENT1016998:SPAB_RS11115-MON; -.
DR   UniPathway; UPA00115; UER00409.
DR   Proteomes; UP000008556; Chromosome.
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; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; Hydrolase.
FT   CHAIN           1..331
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_1000088031"
SQ   SEQUENCE   331 AA;  36436 MW;  DFFFEDD163AB2775 CRC64;
     MKQTVYTASP ESQQIHVWSL NHEGTLTLVQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV
     LAYRIAPDDG ALTFAAESAL PGSPTHISTD HHGRFVFVGS YNAGNVSVTR LQDGLPVELV
     DVVERLDGCH SANITPDNRT LWVPALKQDR ICLFTLSDDG HLVAQEPAEV NTVEGAGPRH
     MVFHPNRQYA YCVNELNSSV DVWQLKNPHG EIECVQTLDM MPADFSDTRW AADIHITPDG
     RHLYACDRTA SLITVFSVSE DGSVLSVEGF QPTEAQPRGF NIDNSGKYLI AAGQKSHHIA
     VYEITGTQGL LTEKGRYAVG QGPMWVVVNA Y