ID   A0AA37N6J5_BACUN        Unreviewed;       780 AA.
AC   A0AA37N6J5;
DT   24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2024, sequence version 1.
DT   29-MAY-2024, entry version 3.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=CE91St12_04580 {ECO:0000313|EMBL:GKH12248.1};
OS   Bacteroides uniformis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=820 {ECO:0000313|EMBL:GKH12248.1, ECO:0000313|Proteomes:UP001055048};
RN   [1] {ECO:0000313|EMBL:GKH12248.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CE91-St12 {ECO:0000313|EMBL:GKH12248.1};
RA   Sato Y., Atarashi K., Plichta R.D., Arai Y., Sasajima S., Kearney M.S.,
RA   Suda W., Takeshita K., Sasaki T., Okamoto S., Skelly N.A., Okamura Y.,
RA   Vlamakis H., Li Y., Tanoue T., Takei H., Nittono H., Narushima S., Irie J.,
RA   Itoh H., Moriya K., Sugiura Y., Suematsu M., Moritoki N., Shibata S.,
RA   Littman R.D., Fischbach A.M., Uwamino Y., Inoue T., Honda A., Hattori M.,
RA   Murai T., Xavier J.R., Hirose N., Honda K.;
RT   "Novel bile acid biosynthetic pathways are enriched in the microbiome of
RT   centenarians.";
RL   Submitted (JAN-2022) 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:GKH12248.1}.
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DR   EMBL; BQNL01000001; GKH12248.1; -; Genomic_DNA.
DR   Proteomes; UP001055048; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..780
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041323974"
FT   DOMAIN          700..769
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   780 AA;  85436 MW;  5B54DFF5415EBDAC CRC64;
     MNMKKIFKRT SLLLATALIG VTATVQAQKS PQDMDRFIDA LMRRMTVEEK IGQLNLPVTG
     EITTGQAKSS DVAKKIEQGL VGGLFNLKGV AKIRDVQKLA VENSRLGIPL LFGMDVIHGY
     ETIFPIPLGL SCTWDMAAIG QSARIAAIEA SADGISWTFS PMVDISRDPR WGRVSEGSGE
     DPFLGGAIAR AMVLGYQGKD LNDQLTRNDE IMACVKHFAL YGAGEAGRDY NTVDMSRNRM
     FNEYMYPYEA AVHAGVGSVM ASFNEVDGVP ATANHWLMTN VLRKQWGFNG FVVTDFTGIS
     EMVEHGIGNL QTVSARALNA GVDMDMVSEG FVGTLKKSLT EGKITMKTLD AACRRILEAK
     YKLGLFDDPY KYCDLSRPAR DIFTRKHRDA ARRIAAESFV LLKNEPFEGQ GKKSSRPVLP
     LEKQGTVAVI GPLGNTRSNM PGTWSVAARL NDYPSLYEGL KEMTAGRVNI TYAKGSNLIG
     DAAYEERATL FGRSLSRDNR TDKKLLDEAL KVASGADVIV AALGESSEMS GESSSRTDLD
     IPDVQRTLLE ALLKTGKPVV LTLFTGRPLT LTWEQEHVPA ILNVWFGGSE AAYAIGDVLF
     GDVNPSGKLT MTFPKNVGQL PLFYNHKNTG RPLAAGNWFE KFRSNYLDVD NEPLYPFGYG
     LSYTTFQYSD IALSTPVMGQ NGSTTAVVTV TNTGKRDGAE VVQLYIRDLV GSITRPVREL
     KGFEKVFLKA GESKTVSFKI TPELLRFYDY DLNHVAEPGD FDVMIGGSSQ AEKTARLTLK
//