ID A0A108TGD7_9BACE Unreviewed; 784 AA.
AC A0A108TGD7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:KAA5415432.1};
GN ORFNames=F2Y81_18250 {ECO:0000313|EMBL:KAA5415432.1};
OS Bacteroides cellulosilyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=246787 {ECO:0000313|EMBL:KAA5415432.1, ECO:0000313|Proteomes:UP000448877};
RN [1] {ECO:0000313|EMBL:KAA5415432.1, ECO:0000313|Proteomes:UP000448877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A6 {ECO:0000313|EMBL:KAA5415432.1,
RC ECO:0000313|Proteomes:UP000448877};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA5415432.1}.
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DR EMBL; VVYV01000033; KAA5415432.1; -; Genomic_DNA.
DR RefSeq; WP_007216976.1; NZ_VVYV01000033.1.
DR AlphaFoldDB; A0A108TGD7; -.
DR STRING; 246787.BcellWH2_02271; -.
DR GeneID; 66306362; -.
DR eggNOG; COG1472; Bacteria.
DR Proteomes; UP000448877; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
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|RuleBase:RU361161, ECO:0000313|EMBL:KAA5415432.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..784
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030020275"
FT DOMAIN 704..773
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 784 AA; 85512 MW; 6AAF76D8961089C5 CRC64;
MKKILKRTSL LLISALMSIA AAQAQKSPQD MDRFIDALMK KMTVEEKIGQ LNLPVTGDIT
TGQAKSSDVA QKIEKGLVGG LFNLKGVDRI LEVQKLAVEK SRLGIPLLFG MDVIHGYETI
FPIPLGLSCT WDMAAIEKSA RIAAIEASAD GISWTFSPMV DISRDPRWGR VSEGSGEDPF
LGGAIAQAMV YGYQGANLQD QLHRNDEIMA CVKHFALYGA GEAGRDYNTV DMSRNRMFNE
FMYPYEAAVE AGVGSVMASF NEIDGIPATG NKWLLSDLLR GQWGFEGFVV TDFTGISEMI
EHGVGDLQTV SALALNAGVD MDMVSEGFVG TLMKSIKEGK VRMGTLNTAC RRILEAKYKL
GLFDNPYKYC DVNRPKRDIF TKEHRDAARK IAGESFVLLK NAPATAQPLA AHSSSPVTAS
PVLPLKKQGT VAVIGPLGNT RSNMPGTWSV AARLNDYPSL YEGLKEMMTG KVNITYAKGS
NLIGDAAYEE RATMFGRSLN RDNRTDQELL DEALKVAAGA DVIVAALGES SEMSGESSSR
TELGLPNVQH TLLEALLKTG KPVVLTLFTG RPLTLNWEQE HVPAILNVWF GGSEAAYAIG
DVLFGDVNPS GKLTMTFPKN VGQIPLFYNH KNTGRPLAAG KWFEKFRSNY LDVDNEPLYP
FGYGLSYTTF QYSDIALSTP TLGKDGSVTA VVTVTNTGKH DGAEVVQLYI RDLVGSITRP
VRELKGFNKI FLRAGESKTV SFTITRDLLR FYDYDLNYVA EPGDFDIMIG GNSQAVKTAK
LTLK
//
