6PGL_ECO57
ID 6PGL_ECO57 Reviewed; 331 AA.
AC Q8X926;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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};
GN OrderedLocusNames=Z0938, ECs0795;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG55096.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34218.1; -; Genomic_DNA.
DR PIR; C90728; C90728.
DR PIR; D85579; D85579.
DR RefSeq; NP_308822.1; NC_002695.1.
DR RefSeq; WP_000815433.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X926; -.
DR SMR; Q8X926; -.
DR STRING; 155864.EDL933_0841; -.
DR EnsemblBacteria; AAG55096; AAG55096; Z0938.
DR EnsemblBacteria; BAB34218; BAB34218; ECs_0795.
DR GeneID; 917534; -.
DR KEGG; ece:Z0938; -.
DR KEGG; ecs:ECs_0795; -.
DR PATRIC; fig|386585.9.peg.915; -.
DR eggNOG; COG2706; Bacteria.
DR HOGENOM; CLU_038716_2_0_6; -.
DR OMA; EGNWPRD; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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;
KW Reference proteome.
FT CHAIN 1..331
FT /note="6-phosphogluconolactonase"
FT /id="PRO_0000171134"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01605"
SQ SEQUENCE 331 AA; 36391 MW; BC4A7F215D231BDE 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 NIDHRGKYLI AAGQKSHHIS
VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H
