6PGL_BACSU
ID 6PGL_BACSU Reviewed; 349 AA.
AC O34499;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=6-phosphogluconolactonase {ECO:0000303|PubMed:22960854};
DE EC=3.1.1.31 {ECO:0000269|PubMed:22960854};
GN Name=pgl; Synonyms=ykgB; OrderedLocusNames=BSU13010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22960854; DOI=10.1038/nchembio.1063;
RA Plata G., Fuhrer T., Sauer U., Vitkup D.;
RT "Global probabilistic annotation of metabolic networks enables enzyme
RT discovery.";
RL Nat. Chem. Biol. 8:848-854(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-
CC phosphogluconate. {ECO:0000269|PubMed:22960854}.
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:0000269|PubMed:22960854};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 2/3. {ECO:0000269|PubMed:22960854}.
CC -!- SIMILARITY: Belongs to the cycloisomerase 2 family. {ECO:0000305}.
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DR EMBL; AJ002571; CAA05581.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13158.1; -; Genomic_DNA.
DR PIR; D69856; D69856.
DR RefSeq; NP_389184.1; NC_000964.3.
DR RefSeq; WP_003244689.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34499; -.
DR SMR; O34499; -.
DR IntAct; O34499; 1.
DR MINT; O34499; -.
DR STRING; 224308.BSU13010; -.
DR jPOST; O34499; -.
DR PaxDb; O34499; -.
DR PRIDE; O34499; -.
DR EnsemblBacteria; CAB13158; CAB13158; BSU_13010.
DR GeneID; 937980; -.
DR KEGG; bsu:BSU13010; -.
DR PATRIC; fig|224308.179.peg.1413; -.
DR eggNOG; COG2706; Bacteria.
DR InParanoid; O34499; -.
DR OMA; EGNWPRD; -.
DR PhylomeDB; O34499; -.
DR BioCyc; BSUB:BSU13010-MON; -.
DR UniPathway; UPA00115; UER00409.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011048; Haem_d1_sf.
DR InterPro; IPR019405; Lactonase_7-beta_prop.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF10282; Lactonase; 1.
DR SUPFAM; SSF51004; SSF51004; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..349
FT /note="6-phosphogluconolactonase"
FT /id="PRO_0000171144"
FT REGION 125..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 38411 MW; B8711D1D523CF5FF CRC64;
MTKYIGYVGT YTKGGSEGIY SFELDTEKKA LSEPKLAAKL GNPTYVATNK NNTILYSIEK
ADGQGGVAAY QIDKNSGELT FLNHQLIDGP SPCHVSVDDQ NQFVLTANYH SGKVHVFPVQ
EDGSLQSPVS EAAHTGKGPH ERQEKPHTHY AGFTPEHNYV VAVDLGIDKL YTYKLKDGVL
TESGSHSFAP GAGPRHIAFH PKEKYAYVMT ELSNEVIALE YNPTAGEFRE IQVVSAIPDD
FTDNSQGSAI HVTQDGRFVY VANRGHDSIA VFEVNQYSGE LAFVERVSTE GNWPRDFVFD
PTEGFLVASN EETGNLVLFE RDKETGRLTL LPSTVSVPYP VCVKFLHQV
