6PGL_PECCP
ID 6PGL_PECCP Reviewed; 332 AA.
AC C6DCH7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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}; OrderedLocusNames=PC1_1280;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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}.
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DR EMBL; CP001657; ACT12327.1; -; Genomic_DNA.
DR RefSeq; WP_015839555.1; NC_012917.1.
DR AlphaFoldDB; C6DCH7; -.
DR SMR; C6DCH7; -.
DR STRING; 561230.PC1_1280; -.
DR EnsemblBacteria; ACT12327; ACT12327; PC1_1280.
DR KEGG; pct:PC1_1280; -.
DR eggNOG; COG2706; Bacteria.
DR HOGENOM; CLU_038716_2_0_6; -.
DR OMA; EGNWPRD; -.
DR OrthoDB; 302683at2; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000002736; 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 Carbohydrate metabolism; Glucose metabolism; Hydrolase.
FT CHAIN 1..332
FT /note="6-phosphogluconolactonase"
FT /id="PRO_1000215698"
SQ SEQUENCE 332 AA; 36139 MW; C956F937BA23CC0E CRC64;
MQQVVYVASP ESQQIHVWQL GAQGNLTLLQ TVDVPGQVQP MVIAPNKRHL YVGVRPDFRV
LSYRIDEQGK LTEAGVASLP GSPTHLSTDN DGRFLFSASY SGACVSVSPI GADGIVGEPI
QQLDGLEGCH STNIDPTNRV VWAPCLKEDR IRLYDLGATG ELSVHRQAEM TTVAGAGPRH
MAFHPNQRFA YCVNELDSSV DVYQLDAASG ELEKVQTLDA MPAGFNDTRW AADIHITPNG
RFLYISDRTA SLLSIFQVSE DGSALTLTGH QPTETQPRGF NIDNTGEFLI SAGQKSQHIE
VYHIDQNTGD LQPLARYAVG QGPMWVSVLA LD
