ID Q83QA4_SHIFL Unreviewed; 477 AA.
AC Q83QA4; A0A0H2VXL3; Q7UBQ7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 4.
DT 27-MAR-2024, entry version 133.
DE SubName: Full=6-phospho-beta-glucosidase A {ECO:0000313|EMBL:AAN44371.2};
GN Name=bglA {ECO:0000313|EMBL:AAN44371.2};
GN OrderedLocusNames=SF2887 {ECO:0000313|EMBL:AAN44371.2};
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623 {ECO:0000313|EMBL:AAN44371.2, ECO:0000313|Proteomes:UP000001006};
RN [1] {ECO:0000313|EMBL:AAN44371.2, ECO:0000313|Proteomes:UP000001006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; AE005674; AAN44371.2; -; Genomic_DNA.
DR RefSeq; NP_708664.2; NC_004337.2.
DR RefSeq; WP_005051722.1; NZ_WPGW01000018.1.
DR AlphaFoldDB; Q83QA4; -.
DR PaxDb; 198214-SF2887; -.
DR GeneID; 1025852; -.
DR KEGG; sfl:SF2887; -.
DR KEGG; sft:NCTC1_03176; -.
DR PATRIC; fig|198214.7.peg.3436; -.
DR HOGENOM; CLU_001859_0_2_6; -.
DR Proteomes; UP000001006; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001006}.
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 477 AA; 55129 MW; 5CD3A9D78DD7211C CRC64;
MKKLTLPKDF LWGGAVAAHQ VEGGWNKGGK GPSICDVLTC GAHGVPREIT KEVLPGKYYP
NHEAVDFYGH YKEDIKLFAE MGFKCFRTSI AWTRIFPKGD EAQPNEEGLK FYDSLFDELL
KYNIEPVITL SHFEMPLHLV QQYGSWTNRK FVDFFVRFAE VVFERYKHKV KYWMTFNEIN
NQRNWRAPLF GYCCSGVVYT EHDNPEETMY QVLHHQFVAS ALAVKAARRI NPEMKVGCML
AMVPLYPYSC NPDDVMFAQE SMRERYVFTD VQLCGYYPSY VLNEWERRGF NIKMEDGDLD
VLREGTCDYL GFSYYMTNAV KAEGGTGDAI SGFEGSVPNP YVKASDWGWQ IDPVGLRYAL
CELYERYQRP LFIVENGFGA YDKVEEDGSI NDDYRIDYLR AHIEEMKKAV TYDGVDLMGY
TPWGCIDCVS FTTGQYSKRY GFIYVNKHDD GTGDMSRSRK KSFNWYKEVI ASNGEKL
//
