ID   6PGL_MYCLE              Reviewed;         247 AA.
AC   Q49700;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=6-phosphogluconolactonase;
DE            Short=6PGL;
DE            EC=3.1.1.31;
GN   Name=pgl; Synonyms=devB; OrderedLocusNames=ML0579; ORFNames=B1496_F1_31;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
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   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       2/3.
CC   -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC       isomerase family. 6-phosphogluconolactonase subfamily. {ECO:0000305}.
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DR   EMBL; U00013; AAA17114.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30087.1; -; Genomic_DNA.
DR   PIR; S72775; S72775.
DR   RefSeq; NP_301491.1; NC_002677.1.
DR   RefSeq; WP_010907815.1; NC_002677.1.
DR   AlphaFoldDB; Q49700; -.
DR   SMR; Q49700; -.
DR   STRING; 272631.ML0579; -.
DR   EnsemblBacteria; CAC30087; CAC30087; CAC30087.
DR   KEGG; mle:ML0579; -.
DR   PATRIC; fig|272631.5.peg.1008; -.
DR   Leproma; ML0579; -.
DR   eggNOG; COG0363; Bacteria.
DR   HOGENOM; CLU_053947_1_0_11; -.
DR   OMA; YQLFEFE; -.
DR   UniPathway; UPA00115; UER00409.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   CDD; cd01400; 6PGL; 1.
DR   InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR   InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR039104; PGLS.
DR   PANTHER; PTHR11054; PTHR11054; 1.
DR   Pfam; PF01182; Glucosamine_iso; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR01198; pgl; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..247
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_0000090100"
SQ   SEQUENCE   247 AA;  26161 MW;  70FECAA8728FC34E CRC64;
     MSASVEIFSD SKTMVGAAGK RLASTIQSAV AARERALIVL TGGSSGIGLL RDLATRGQQI
     DWSRVHLFWG DERYVPKDDD ERNEKQARVA LLDHIDIPPS QVHPMPAGDG EFGNDLEAAA
     LAYEQLLAAY AAPGYPTPNF DVHLMGMGPE GHINSLFPNT VAVRETSRMV VGVRNSPKPP
     PERITLTLNA IQRSREVWLM VSGTAKADAV AAAMGGAPSA SIPAAGAVGL ETTLWLLDEE
     AAAKIPG