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Database: UniProt
Entry: B3C6L2_9BACE
LinkDB: B3C6L2_9BACE
Original site: B3C6L2_9BACE 
ID   B3C6L2_9BACE            Unreviewed;       814 AA.
AC   B3C6L2;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BACINT_00548 {ECO:0000313|EMBL:EDV06986.1};
OS   Bacteroides intestinalis DSM 17393.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV06986.1, ECO:0000313|Proteomes:UP000004596};
RN   [1] {ECO:0000313|EMBL:EDV06986.1, ECO:0000313|Proteomes:UP000004596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV06986.1,
RC   ECO:0000313|Proteomes:UP000004596};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDV06986.1, ECO:0000313|Proteomes:UP000004596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV06986.1,
RC   ECO:0000313|Proteomes:UP000004596};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2008) 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   -!- 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:EDV06986.1}.
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DR   EMBL; ABJL02000006; EDV06986.1; -; Genomic_DNA.
DR   RefSeq; WP_007660315.1; NZ_ABJL02000006.1.
DR   AlphaFoldDB; B3C6L2; -.
DR   STRING; 471870.BACINT_00548; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000004596; 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; 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: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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..814
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002785292"
FT   DOMAIN          726..795
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   814 AA;  89930 MW;  FB1AEBE9E0F47ADF CRC64;
     MKKKVICSVL LGLMVSGQLV GADYIKPKKD KKTGISYYDL NKNGHLDIYE NPAFAVEERV
     RALLSQMTLE EKVGQMLTSL GWPMYERQGN TICLTEQLVR EIEEYHTGSL WGFMRADPWT
     QRTLTTGLTP ALAAKASNML QKYAIEHGRL GIPLFLAEEC PHGHMAIGTT VFPTSIGQAS
     TWNPELIRRM GRAIATEASA QGAHIGYGPV LDLARDPRWS RVEETYGEDA YLNGVMGAAL
     VKGFQGEFPR TKGKVIATLK HFAAYGWTEG GHNGGSAHVG NREMEEAIYP PFREAVAAGA
     LSVMSSYNEI DGIPCTANSN LLTGLLKERW QFKGFVVSDL YAIGGLREHG VADTDYEAAV
     KAVNAGVDSD LGTNVYAGQL VNAVKRGDVQ EVVINKAVSR ILALKFHMGL FDHPFVDERE
     PEQVVASTEH LELAREVARQ SIILLKNKNE LLPLNKKTKT IAVIGPNADN IYNMLGDYTA
     PQSESSVVTV LDGIRQKVSN DTHIIYAKGC AVRDSSKSGF QEAIEAARQS DVVVMVMGGS
     SARDFSSKYE ETGAAKVSDS HISDMESGEG YDRSTLELLG RQRELIREVG KLNKPIVLVL
     IKGRPLLLEG IEAEVDAIVD AWYPGMQGGN AVADVLFGDY NPAGRLTISV PRSVGQLPVY
     YNTKRKGNRS KYIEEEGTPR YPFGYGLSYT SFNYSDLKAE VVEAEDSCLV NISVKVRNEG
     SRDGDEVVQL YLRDEVASFT TPFKQLCGFQ RIHLKVGETK EITFRLDKKS LALYMQNEEW
     AVEPGRFTLM LGGSSEQIYQ QKEIEITKRY TFKM
//
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