ID   C3QC56_9BACE            Unreviewed;       859 AA.
AC   C3QC56;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BSAG_01251 {ECO:0000313|EMBL:EEO49540.1};
OS   Bacteroides sp. D1.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO49540.1, ECO:0000313|Proteomes:UP000003361};
RN   [1] {ECO:0000313|EMBL:EEO49540.1, ECO:0000313|Proteomes:UP000003361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1 {ECO:0000313|EMBL:EEO49540.1,
RC   ECO:0000313|Proteomes:UP000003361};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C.,
RA   White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. D1.";
RL   Submitted (MAY-2011) 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:EEO49540.1}.
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DR   EMBL; ACAB02000110; EEO49540.1; -; Genomic_DNA.
DR   RefSeq; WP_004316367.1; NZ_JH114350.1.
DR   AlphaFoldDB; C3QC56; -.
DR   HOGENOM; CLU_004542_5_1_10; -.
DR   Proteomes; UP000003361; 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; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
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; IPR008969; CarboxyPept-like_regulatory.
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.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEO49540.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..859
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002929239"
FT   DOMAIN          682..751
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   859 AA;  94674 MW;  0B900229EF61E4FC CRC64;
     MKFIIKDILI ICLFCCASSL NAQHAFPYKN PSLPTEERVN DLLNRMTLQE KIAQISHLQS
     WDVFDGQKLN TAKLAKMCGD KGYGFFEGFP LTAAQCRKNF RIIQTYLLEQ TRLGIPGFSV
     AESLHGVVHE GSTIYPQNIA IGSTFNPELA YEMTKHIAGE LNTIGVKQVL APCIDVVREL
     RWGRVEESFS EDPFLCARMA VAEVKGYMDH GISPMAKHYG PHGNPLGGLN LASVECGIRD
     LFDVYLEPFE AILAETDILA VMSSYNAWNR EPNSASKFML TDILRDRFGF RGYVYSDWGV
     IDMLKNFHET AGNDFEAASQ VLTAGLDVEA SSLCFKSLES KVLAGEFDVR YIDRAVKRVL
     RAKFELGLFE DPYLEKNSYR WPLRAKECVS LSRQIADEST VLLKNEGNLL PLDIKKLRSV
     AVIGPNADCV QFGDYTWSKN KEDGITPLQG ICRLAGKKVK VNYAQGCSIA SFDQSGIEEA
     VCAAQQSDVA LLFVGSSSTA FVRHSSAPST SGEGIDLSGV ELTGAQEELI EAVCATGKPV
     VLILVAGKPF AIPFAKKNVP AILVQWYAGE QAGNSIADIL FGKVNPSGKI SFSFPQSSGH
     LPAFYNHLTT DKGFYKEPGT YETPGRDYVF SSPNPLWAFG HGLSYTTFDL VSAIADKTHY
     QAHDTIAVKV KIANSGEVAG KEVVQLYIRD VVSTVMTPVK QLKAFEKISL NPAETKEITL
     KVPVHELYLT DNIGNRYLEP GTFEIKVGTA SDRIVHRISI EVGSKLEKTP VVDSPQIIKV
     TPSGEFITVQ GFVRDAQATP VAYVTVRAIS SGQETQTDEK GFYSINLRTD DSIAFVKARF
     ITQQMEVKGH KNINIRLVK
//