6PGL_BORBU
ID 6PGL_BORBU Reviewed; 235 AA.
AC O51240;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=6-phosphogluconolactonase;
DE Short=6PGL;
DE EC=3.1.1.31;
GN Name=pgl; Synonyms=devB; OrderedLocusNames=BB_0222;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
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 glucosamine/galactosamine-6-phosphate
CC isomerase family. 6-phosphogluconolactonase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000783; AAC66602.1; -; Genomic_DNA.
DR PIR; F70127; F70127.
DR RefSeq; NP_212356.1; NC_001318.1.
DR RefSeq; WP_002661712.1; NC_001318.1.
DR AlphaFoldDB; O51240; -.
DR SMR; O51240; -.
DR STRING; 224326.BB_0222; -.
DR PRIDE; O51240; -.
DR EnsemblBacteria; AAC66602; AAC66602; BB_0222.
DR KEGG; bbu:BB_0222; -.
DR PATRIC; fig|224326.49.peg.620; -.
DR HOGENOM; CLU_053947_3_0_12; -.
DR OMA; FLVDERC; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd01400; 6PGL; 1.
DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR039104; PGLS.
DR PANTHER; PTHR11054; PTHR11054; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..235
FT /note="6-phosphogluconolactonase"
FT /id="PRO_0000090089"
SQ SEQUENCE 235 AA; 27198 MW; A3B16EE42D9E44F8 CRC64;
MEFLYSDEEN YLKDRFFDFF NMNVDKDKYT SIGICGGRSI VNFLSVFLKQ NFSFRRSHFF
LVDERCVPLN DENSNYNLLN KNFFSKMVDK NLISISKFHA FVYSEIDEAT AIHDYNIEFN
SRFNIFDFII VSVGEDGHIA SLFPSRKLLF SDVEGYQYEY NSPKFPSKRI SLTPKSLFGS
KAVVLLFMGV DKKCALENFL ASNSSINECP ARLLKEHPNL LVLTNIKRDE SYAGS