(data stored in ACNUC7421 zone)

SWISSPROT: 6PGL_ECO27

ID   6PGL_ECO27              Reviewed;         331 AA.
AC   B7ULP0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=E2348C_0644;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to
CC       6-phosphogluconate. {ECO:0000255|HAMAP-Rule:MF_01605}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-
CC         gluconate + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57955, ChEBI:CHEBI:58759;
CC         EC=3.1.1.31; 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):
CC       step 2/3. {ECO:0000255|HAMAP-Rule:MF_01605}.
CC   -!- SIMILARITY: Belongs to the cycloisomerase 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01605}.
DR   EMBL; FM180568; CAS08192.1; -; Genomic_DNA.
DR   RefSeq; WP_000815414.1; NC_011601.1.
DR   SMR; B7ULP0; -.
DR   EnsemblBacteria; CAS08192; CAS08192; E2348C_0644.
DR   KEGG; ecg:E2348C_0644; -.
DR   KO; K07404; -.
DR   OMA; EGNWPRD; -.
DR   BioCyc; ECOL574521:E2348C_RS03460-MONOMER; -.
DR   UniPathway; UPA00115; UER00409.
DR   Proteomes; UP000008205; 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;
DR   PRODOM; B7ULP0.
DR   SWISS-2DPAGE; B7ULP0.
KW   Acetylation; Carbohydrate metabolism; Complete proteome;
KW   Glucose metabolism; Hydrolase.
FT   CHAIN         1    331       6-phosphogluconolactonase.
FT                                /FTId=PRO_1000185835.
FT   MOD_RES     287    287       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01605}.
SQ   SEQUENCE   331 AA;  36293 MW;  457820D7279EAC52 CRC64;
     MKQTVYIASP ESQQIHVWNL NHEGALTLTQ VVDVPGQVQP MVVSPDKRYL YVGVRPEFRV
     LAYRIAPDDG ALTFAAESAL PGSPTHISTD HLGQFVFVGS YNAGNVSVTR LEDGLPVGVV
     DVVEGLDGCH SANISPDNRT LWVPALKQDR ICLFTVSDDG HLVAQDPAEV TTVEGAGPRH
     MVFHPNEQYA YCVNELNSSV DVWELKDPHG NIECVQTLDM MPENFSDTRW AADIHITPDG
     RHLYACDRTA SLITVFSVSE DGSVLSKEGF QPTETQPRGF NVDHSGKYLI AAGQKSHHIS
     VYEIVGEQGL LHEKGRYAVG QGPMWVVVNA H
//

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