6PGL_KLEP7
ID 6PGL_KLEP7 Reviewed; 331 AA.
AC A6T6J6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 77.
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}; Synonyms=ybhE;
GN OrderedLocusNames=KPN78578_07560; ORFNames=KPN_00781;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=ABR76217.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000647; ABR76217.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_020316492.1; NC_009648.1.
DR PDB; 6NAU; X-ray; 1.55 A; A/B/C=1-331.
DR PDBsum; 6NAU; -.
DR AlphaFoldDB; A6T6J6; -.
DR SMR; A6T6J6; -.
DR STRING; 272620.KPN_00781; -.
DR jPOST; A6T6J6; -.
DR EnsemblBacteria; ABR76217; ABR76217; KPN_00781.
DR KEGG; kpn:KPN_00781; -.
DR HOGENOM; CLU_038716_2_0_6; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000000265; 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glucose metabolism; Hydrolase;
KW Reference proteome.
FT CHAIN 1..331
FT /note="6-phosphogluconolactonase"
FT /id="PRO_0000323499"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:6NAU"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:6NAU"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:6NAU"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6NAU"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:6NAU"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:6NAU"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:6NAU"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:6NAU"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:6NAU"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:6NAU"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:6NAU"
SQ SEQUENCE 331 AA; 36037 MW; 0D25EBDA862F667B CRC64;
MKQTVYTASP ESQQIHVWSL EADGKLTLVQ VVDAPGQVQP MVVSPNKEFL YVGVRPEFRV
LAYRITPDNG ALTFAGEAAL PGSPTHISTD HHGRFVFSAS YNQGCVSVTP LHDGLPGETI
TVVEGLEGCH SANISPDNRT LWVPALKQDR ICLFTLSDDG FLSAQEPAEV TTVEGAGPRH
MVFHPNQQYG YCVNELNSSI DVWELKDPKG NIECVQTLDM MPPDFSGVRW AADIHITPDG
GHLYACDRTA SIITVFSVSE DGSVLAVEGY QPTETQPRGF NLDHSGKYLI AAGQKSHHIA
VYDIVGEQGL LQEKGRYAVG QGPMWVVVNA H
