ID A0AA37N6J5_BACUN Unreviewed; 780 AA. AC A0AA37N6J5; DT 24-JAN-2024, integrated into UniProtKB/TrEMBL. DT 24-JAN-2024, sequence version 1. DT 27-NOV-2024, entry version 6. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BQNL01000001; GKH12248.1; -; Genomic_DNA. DR Proteomes; UP001055048; Unassembled WGS sequence. DR GO; GO:0008422; F:beta-glucosidase activity; IEA:TreeGrafter. DR GO; GO:0009251; P:glucan catabolic process; IEA:TreeGrafter. DR FunFam; 2.60.40.10:FF:000495; Periplasmic beta-glucosidase; 1. DR FunFam; 3.20.20.300:FF:000005; Periplasmic beta-glucosidase; 1. DR FunFam; 3.40.50.1700:FF:000004; Periplasmic beta-glucosidase; 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; IPR051915; Cellulose_Degrad_GH3. 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|ARBA:ARBA00023295, 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 //