6PGL_SALG2
ID 6PGL_SALG2 Reviewed; 331 AA.
AC B5R752;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=SG0763;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933173; CAR36659.1; -; Genomic_DNA.
DR RefSeq; WP_000815476.1; NC_011274.1.
DR AlphaFoldDB; B5R752; -.
DR SMR; B5R752; -.
DR EnsemblBacteria; CAR36659; CAR36659; SG0763.
DR KEGG; seg:SG0763; -.
DR HOGENOM; CLU_038716_2_0_6; -.
DR OMA; EGNWPRD; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000008321; 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_1000148164"
SQ SEQUENCE 331 AA; 36283 MW; 16929272EFC9CE7A CRC64;
MKQTVYTASP ESQQIHVWSL NHEGTLTLVQ VVDVPGQVQT MVVSPDKRYL YVGVRPEFRV
LAYRIAPDDG ALTFAAESAL PGSPTHISTD HHGRFVFVGS YNAGNVSVTR LQDGLPVELV
GVVEGLDGCH SANITPDNRT LWVPALKQDR ICLFTLSDDG HLVAQEPAEV NTVEGAGPRH
MVFHPNRQYA YCVNELNSSV DVWQLKNPHG EIECVQTLDM MPADFSDTRW AADIHITPDG
RHLYACDRTA SLITVFSVSE DGSVLSVEGF QPTEAQPRGF NIDNSGKYLI AAGQKSHHIA
VYEITGTQGL LTEKGRYAVG QGPMWVVVNA Y