ID   6PGL_SALAR              Reviewed;         331 AA.
AC   A9MJH1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-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=SARI_02157;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000880; ABX22034.1; -; Genomic_DNA.
DR   RefSeq; WP_000815460.1; NC_010067.1.
DR   AlphaFoldDB; A9MJH1; -.
DR   SMR; A9MJH1; -.
DR   STRING; 41514.SARI_02157; -.
DR   EnsemblBacteria; ABX22034; ABX22034; SARI_02157.
DR   KEGG; ses:SARI_02157; -.
DR   HOGENOM; CLU_038716_2_0_6; -.
DR   OMA; EGNWPRD; -.
DR   OrthoDB; 302683at2; -.
DR   UniPathway; UPA00115; UER00409.
DR   Proteomes; UP000002084; 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; Reference proteome.
FT   CHAIN           1..331
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_1000088030"
SQ   SEQUENCE   331 AA;  36378 MW;  0391EC4FEAF8CED0 CRC64;
     MKQTVYTASP ESQQIHVWSL NHEGMLTLVQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV
     LAYRIAPDDG ALTFATESAL PGSPTHISTD HHGRFVFVGS YNAGNVSVTR LQDGLPVELV
     DVVEGLDGCH SANITPDNRT LWVPALKQDR IALFTLSDDG YLAAQEPAEV NTVEGAGPRH
     MVFHPNQQYA YCVNELNSSV DVWQLKNPHG EIECVQTLDM MPADFSDTRW AADIHITPDG
     RHLYACDRTA SLITVFSVSE DGSVLSVEGF QPTETQPRGF NIDHHGKYLI AAGQKSHHIA
     VYEIAGAQGL LTEKGRYAVG QGPMWVVVNA Y