ID   6PGL_SODGM              Reviewed;         331 AA.
AC   Q2NUK0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=SG0900;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE74175.1; -; Genomic_DNA.
DR   RefSeq; WP_011410761.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NUK0; -.
DR   SMR; Q2NUK0; -.
DR   STRING; 343509.SG0900; -.
DR   EnsemblBacteria; BAE74175; BAE74175; SG0900.
DR   KEGG; sgl:SG0900; -.
DR   eggNOG; COG2706; Bacteria.
DR   HOGENOM; CLU_038716_2_0_6; -.
DR   OMA; EGNWPRD; -.
DR   OrthoDB; 302683at2; -.
DR   BioCyc; SGLO343509:SGP1_RS07665-MON; -.
DR   UniPathway; UPA00115; UER00409.
DR   Proteomes; UP000001932; 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; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; Hydrolase.
FT   CHAIN           1..331
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_0000291473"
SQ   SEQUENCE   331 AA;  35497 MW;  FBCA285148940C20 CRC64;
     MKQIVYVASP ESQQIHVWQM DNQGALTLLQ VVDTPGQGQP MVIHPARTHL YIGVRPSFGV
     VSYRIDEKGL LTEAGMAPLP GSPTQLTTDL QGETLYSVSY SGSCLSVSPI DEQGIVGAPT
     QTLEGLTHCH SANVDTTNQV LWVPCLQEDR IRLYTIGEAG HLTPRTPEAL DSVAGAGPRH
     MVFHHGGGYA YAINELSGTV NVIAIDAAGA GPRIVQTLDI MPAGFSDTRW AADIYITPDG
     RWLYCCDRTA SVISRFAVSE DGGVLRLLGH QATESQPRGF NIDSQGRFLV AAGQKSHHIA
     VYAIDAQSGA LDPLARYAVG QGPMWVSVLA R