6PGL_ECO55
ID 6PGL_ECO55 Reviewed; 331 AA.
AC B7LB75;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=EC55989_0747;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAU96615.1; -; Genomic_DNA.
DR RefSeq; WP_000815435.1; NC_011748.1.
DR AlphaFoldDB; B7LB75; -.
DR SMR; B7LB75; -.
DR EnsemblBacteria; CAU96615; CAU96615; EC55989_0747.
DR GeneID; 66670962; -.
DR KEGG; eck:EC55989_0747; -.
DR HOGENOM; CLU_038716_2_0_6; -.
DR OMA; EGNWPRD; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000000746; 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 Acetylation; Carbohydrate metabolism; Glucose metabolism; Hydrolase.
FT CHAIN 1..331
FT /note="6-phosphogluconolactonase"
FT /id="PRO_1000185836"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01605"
SQ SEQUENCE 331 AA; 36308 MW; D731044CFCF31A8F CRC64;
MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV
LAYRIAPDDG ALTFAAESAL PGSPTHISTD HQGQFVFVGS YNAGNVSVTR LEDGLPVGVV
DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH
MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG
RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NVDHSGKYLI AAGQKSHHIS
VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H
