6PGL_ECOLI
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 03-AUG-2022, entry version 157.
DE RecName: Full=6-phosphogluconolactonase;
DE Short=6-P-gluconolactonase;
DE Short=Pgl;
DE EC=3.1.1.31;
GN Name=pgl; Synonyms=ybhE; OrderedLocusNames=b0767, JW0750;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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RL Unpublished observations (MAR-1996).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.
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
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 -!- 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 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_SSZK01000002.1.
DR PDB; 1RI6; X-ray; 2.00 A; A=2-331.
DR PDBsum; 1RI6; -.
DR AlphaFoldDB; P52697; -.
DR SMR; P52697; -.
DR BioGRID; 4261151; 18.
DR IntAct; P52697; 5.
DR STRING; 511145.b0767; -.
DR iPTMnet; P52697; -.
DR jPOST; P52697; -.
DR PaxDb; P52697; -.
DR PRIDE; P52697; -.
DR EnsemblBacteria; AAC73854; AAC73854; b0767.
DR EnsemblBacteria; BAA35431; BAA35431; BAA35431.
DR GeneID; 66670962; -.
DR GeneID; 946398; -.
DR KEGG; ecj:JW0750; -.
DR KEGG; eco:b0767; -.
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; EGNWPRD; -.
DR PhylomeDB; P52697; -.
DR BioCyc; EcoCyc:6PGLUCONOLACT-MON; -.
DR BioCyc; MetaCyc:6PGLUCONOLACT-MON; -.
DR UniPathway; UPA00115; UER00409.
DR EvolutionaryTrace; P52697; -.
DR PRO; PR:P52697; -.
DR Proteomes; UP000000318; Chromosome.
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: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 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
