ID   6PGL_ECOLI              Reviewed;         331 AA.
AC   P52697; P75760;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   04-NOV-2026, entry version 176.
DE   RecName: Full=6-phosphogluconolactonase {ECO:0000303|PubMed:15576773};
DE            Short=6-P-gluconolactonase;
DE            Short=Pgl;
DE            EC=3.1.1.31 {ECO:0000269|PubMed:15576773};
GN   Name=pgl; Synonyms=ybhE; OrderedLocusNames=b0767, JW0750;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7665460; DOI=10.1128/jb.177.17.4851-4856.1995;
RA   Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U., Gunsalus R.P.,
RA   Shanmugam K.T.;
RT   "Genetic analysis of the modABCD (molybdate transport) operon of
RT   Escherichia coli.";
RL   J. Bacteriol. 177:4851-4856(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   IDENTIFICATION.
RA   Rudd K.E.;
RL   Unpublished observations (MAR-1996).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15576773; DOI=10.1128/jb.186.24.8248-8253.2004;
RA   Thomason L.C., Court D.L., Datta A.R., Khanna R., Rosner J.L.;
RT   "Identification of the Escherichia coli K-12 ybhE gene as pgl, encoding 6-
RT   phosphogluconolactonase.";
RL   J. Bacteriol. 186:8248-8253(2004).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=31390539; DOI=10.1016/j.ymben.2019.08.003;
RA   Long C.P., Antoniewicz M.R.;
RT   "Metabolic flux responses to deletion of 20 core enzymes reveal flexibility
RT   and limits of E. coli metabolism.";
RL   Metab. Eng. 55:249-257(2019).
RN   [9] {ECO:0007744|PDB:1RI6}
RP   X-RAY CRYSTALLOGRAPHY IN APO FORM.
RA   Lima C.D., Kniewel R., Solorzano V., Wu J.;
RT   "Structure of a putative 7-bladed propeller isomerase.";
RL   Submitted (NOV-2003) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-
CC       phosphogluconate. {ECO:0000269|PubMed:15576773}.
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:0000269|PubMed:15576773};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       2/3.
CC   -!- DISRUPTION PHENOTYPE: Reduces growth on glucose by 20% and causes a
CC       decrease in native reaction flux. {ECO:0000269|PubMed:31390539}.
CC   -!- SIMILARITY: Belongs to the cycloisomerase 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=U27192; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U27192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U00096; AAC73854.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35431.1; -; Genomic_DNA.
DR   PIR; G64812; G64812.
DR   RefSeq; NP_415288.1; NC_000913.3.
DR   RefSeq; WP_000815435.1; NZ_CP009789.1.
DR   PDB; 1RI6; X-ray; 2.00 A; A=2-331.
DR   AlphaFoldDB; P52697; -.
DR   SMR; P52697; -.
DR   BioGRID; 4261151; 23.
DR   FunCoup; P52697; 243.
DR   IntAct; P52697; 5.
DR   STRING; 511145.b0767; -.
DR   iPTMnet; P52697; -.
DR   jPOST; P52697; -.
DR   PaxDb; 511145-b0767; -.
DR   EnsemblBacteria; AAC73854; AAC73854; b0767.
DR   GeneID; 67173260; -.
DR   GeneID; 86945650; -.
DR   GeneID; 946398; -.
DR   KEGG; ecj:JW0750; -.
DR   KEGG; eco:b0767; -.
DR   KEGG; ecoc:C3026_03890; -.
DR   PATRIC; fig|1411691.4.peg.1511; -.
DR   EchoBASE; EB3020; -.
DR   eggNOG; COG2706; Bacteria.
DR   HOGENOM; CLU_038716_2_0_6; -.
DR   InParanoid; P52697; -.
DR   OMA; AAIRMSH; -.
DR   OrthoDB; 9790815at2; -.
DR   PhylomeDB; P52697; -.
DR   BioCyc; EcoCyc:6PGLUCONOLACT-MONOMER; -.
DR   BioCyc; MetaCyc:6PGLUCONOLACT-MONOMER; -.
DR   UniPathway; UPA00115; UER00409.
DR   EvolutionaryTrace; P52697; -.
DR   PRO; PR:P52697; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IDA:EcoCyc.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; EXP:EcoCyc.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IEA:UniProtKB-UniRule.
DR   FunFam; 2.130.10.10:FF:000051; 6-phosphogluconolactonase; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   HAMAP; MF_01605; 6P_gluconolactonase; 1.
DR   InterPro; IPR022528; 6PGL_YbhE-like.
DR   InterPro; IPR050282; Cycloisomerase_2.
DR   InterPro; IPR019405; Lactonase_7-beta_prop.
DR   InterPro; IPR011045; N2O_reductase_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   NCBIfam; NF008258; pgl; 1.
DR   PANTHER; PTHR30344:SF1; 6-PHOSPHOGLUCONOLACTONASE; 1.
DR   PANTHER; PTHR30344; 6-PHOSPHOGLUCONOLACTONASE-RELATED; 1.
DR   Pfam; PF10282; Lactonase; 1.
DR   SUPFAM; SSF50974; Nitrous oxide reductase, N-terminal domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Carbohydrate metabolism; Glucose metabolism;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..331
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_0000171132"
FT   MOD_RES         287
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   CONFLICT        37..52
FT                   /note="QVQPMVVSPDKRYLYV -> RCSRWWSARTNVISML (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319..331
FT                   /note="VGQGPMWVVVNAH -> SGRDQCGWWLTHTKR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          14..20
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          26..33
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          47..54
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   TURN            55..58
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          59..65
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          72..79
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          85..89
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          93..100
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   TURN            101..104
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          105..112
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          115..123
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          138..145
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          150..156
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          162..171
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          178..183
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          187..194
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   TURN            195..198
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          199..206
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          213..219
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          231..236
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          240..247
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   TURN            248..251
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          252..258
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          265..272
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          274..276
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          286..292
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   TURN            294..296
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          298..305
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   TURN            306..309
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          310..318
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:1RI6"
FT   STRAND          325..331
FT                   /evidence="ECO:0007829|PDB:1RI6"
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
//