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Database: UniProt
Entry: R6LFR7_9BACE
LinkDB: R6LFR7_9BACE
Original site: R6LFR7_9BACE 
ID   R6LFR7_9BACE            Unreviewed;       777 AA.
AC   R6LFR7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BN506_00569 {ECO:0000313|EMBL:CDB73032.1};
OS   Bacteroides cellulosilyticus CAG:158.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1263038 {ECO:0000313|EMBL:CDB73032.1, ECO:0000313|Proteomes:UP000018191};
RN   [1] {ECO:0000313|EMBL:CDB73032.1, ECO:0000313|Proteomes:UP000018191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:158 {ECO:0000313|Proteomes:UP000018191};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:CDB73032.1}.
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DR   EMBL; CBEB010000390; CDB73032.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6LFR7; -.
DR   Proteomes; UP000018191; Unassembled WGS sequence.
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; 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:SF16; LYSOSOMAL 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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018191};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..777
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004412634"
FT   DOMAIN          692..761
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   777 AA;  86339 MW;  A8C7C02EBEE1D6E7 CRC64;
     MNRKLILSAA LSGLMLTATA QTTVAPAIPR DGKIEKKVEA LLKKMTLEEK IGQMTELTID
     VITKRDNSTQ EFQIDDALLD TVIGKYKVGS ILNVPQGVAQ SKEKWEEIIR KIQDKSMKVM
     GIPCIYGVDQ IHGTTYTLGG TFFPQGINMA ATFNRELVRE GARISAYETK AGSIPWTYAP
     VLDLARDARW PRHWENYGED CYVNAEMGRE AVFGFQGSDP NHIGKQQVAA CIKHYMGYGV
     PVSGKDRTPS SITVQDMREK HFAPFLEGIK AGALSVMVNS AMNNGLPFHA NYELLTEWLK
     EDLNWDGMIV TDWADINNLY TRDKIAGSKK EAIKIAINAG IDMSMVPYEW SFCTYLKELV
     EEGEVPMSRI DDAVRRVLRM KYRLGLFETP AYNHKDFPLF GGKEHAAAAL QAAEESLVLL
     KNTDHILPLP KDKKLLITGP NANSMRTLNG GWSYTWQGHR ADELAADYNT ILESFTQKFG
     ASNIIYEPGV TYKEGGAWWE ENAPEIDKAV AAAANADYII ACVGENSYCE TPGNLNNLFL
     SESQLNLVKA LAATGKPVVL VLNEGRPRIV NEIEPLAKAV INTMLPGNYG GDALANLVAG
     DANFSGKMPY TYPKEINSLF TYDYKPCEDL EKMSGAYDYD AVMSVQWAFG YGLSYTTYAY
     SNLKADKNNF TADDVLTFTV DVKNTGNRIG KESVLLFSSD LIASLTPDIR RLRAFEKVEL
     QPGETKTVTL KVKGSDLAFV GYDGKWILEK GDFRIQTGNQ TLNITCTDTR KWDTPNK
//
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