ID   D2A734_SHIF2            Unreviewed;       479 AA.
AC   D2A734;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=6-phospho-beta-glucosidase A {ECO:0000313|EMBL:ADA75218.1};
GN   Name=bglA {ECO:0000313|EMBL:ADA75218.1};
GN   OrderedLocusNames=SFxv_3166 {ECO:0000313|EMBL:ADA75218.1};
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020 {ECO:0000313|EMBL:ADA75218.1, ECO:0000313|Proteomes:UP000001884};
RN   [1] {ECO:0000313|EMBL:ADA75218.1, ECO:0000313|Proteomes:UP000001884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017 {ECO:0000313|EMBL:ADA75218.1,
RC   ECO:0000313|Proteomes:UP000001884};
RX   PubMed=19955273; DOI=10.1128/JCM.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP001383; ADA75218.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2A734; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; sfe:SFxv_3166; -.
DR   PATRIC; fig|591020.3.peg.3423; -.
DR   HOGENOM; CLU_001859_0_2_6; -.
DR   Proteomes; UP000001884; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF348; 6-PHOSPHO-BETA-GLUCOSIDASE ASCB-RELATED; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468}.
FT   ACT_SITE        377
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   479 AA;  55342 MW;  DEA42405FEEC0CF7 CRC64;
     MIVKKLTLPK DFLWGGAVAA HQVEGGWNKG GKGPSICDVL TCGAHGVPRE ITKEVLPGKY
     YPNHEAVDFY GHYKEDIKLF AEMGFKCFRT SIAWTRIFPK GDEAQPNEEG LKFYDSLFDE
     LLKYNIEPVI TLSHFEMPLH LVQQYGSWTN RKFVDFFVRF AEVVFERYKH KVKYWMTFNE
     INNQRNWRAP LFGYCCSGVV YTEHDNPEET MYQVLHHQFV ASALAVKAAR RINPEMKVGC
     MLAMVPLYPY SCNPDDVMFA QESMRERYVF TDVQLCGYYP SYVLNEWERR GFNIKMEDGD
     LDVLREGTCD YLGFSYYMTN AVKAEGGTGD AISGFEGSVP NPYVKASDWG WQIDPVGLRY
     ALCELYERYQ RPLFIVENGF GAYDKVEEDG SINDDYRIDY LRAHIEEMKK AVTYDGVDLM
     GYTPWGCIDC VSFTTGQYSK RYGFIYVNKH DDGTGDMSRS RKKSFNWYKE VIASNGEKL
//