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Database: UniProt
Entry: Q0T2Y9_SHIF8
LinkDB: Q0T2Y9_SHIF8
Original site: Q0T2Y9_SHIF8 
ID   Q0T2Y9_SHIF8            Unreviewed;       755 AA.
AC   Q0T2Y9;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   Name=bglX {ECO:0000313|EMBL:ABF04326.1};
GN   OrderedLocusNames=SFV_2208 {ECO:0000313|EMBL:ABF04326.1};
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF04326.1, ECO:0000313|Proteomes:UP000000659};
RN   [1] {ECO:0000313|EMBL:ABF04326.1, ECO:0000313|Proteomes:UP000000659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401 {ECO:0000313|EMBL:ABF04326.1,
RC   ECO:0000313|Proteomes:UP000000659};
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; CP000266; ABF04326.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0T2Y9; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; sfv:SFV_2208; -.
DR   HOGENOM; CLU_004542_5_1_6; -.
DR   Proteomes; UP000000659; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT   DOMAIN          675..744
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   755 AA;  82427 MW;  6CE4ECAD771C8A66 CRC64;
     MSLVLQPALA DDLFGNHPLM PEARDAFVTD LLKKMTVDEK IGQLRLISVG PDNPKEAIRE
     MIKDGQVGAI FNTVTRQDIR AMQDQVMELS RLKIPLFFAY DVLHGQRTVF PISLGLASSF
     NLDAVKTVGR VSAYEAADDG LNMTWAPMVD VSRDPRWGRA SEGFGEDTYL TSIMGKTMVE
     AMQGKSPADR YSVMTSVKHF AAYGAVEGGK EYNTVDMSPQ RLFNDYMPPY KAGLDAGSGA
     VMVALNSLNG TPATSDSWLL KDVLRDQWGF KGITVSDHGA IKELIKHGTA ADPEDAVRVA
     LKSGINMSMS DEYYSKYLPG LIKSGKVTMA ELDDAARHVL NVKYDMGLFN DPYSHLGPKE
     SDPVDTNAES RLHRKEAREV ARESLVLLKN RLETLPLKKS ATIAVVGPLA DSKRDVMGSW
     SAAGVADQSV TVLTGIKNSV GENGKVLYAK GANVTSDKGI IDFLNQYEEA VKVDPRSPQE
     MIDEAVQTAK QSDVVVAVVG EAQGMAHEAS SRTDITIPQG QRDLIAALKA TGKPLVLVLM
     NGRPLALVKE DQQADAILET WFAGTEGGNA IADVLFGDYN PSGKLPISFP RSVGQIPVYY
     SHLNTGRPYN ADKPNKYTSR YFDEANGALY PFGYGLSYTT FTVSDVKLSA PTMKRDGKVT
     ASVQVTNTGK REGATVVQMY LQDVTASMSR PVKQLKGFEK ITLKPGETQT VSFPIDIEAL
     KFWNQQMKYD AEPGKFNVFI GTDSARVKKG EFELL
//
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