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
//