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Database: UniProt
Entry: A0A101WLE5_9FIRM
LinkDB: A0A101WLE5_9FIRM
Original site: A0A101WLE5_9FIRM 
ID   A0A101WLE5_9FIRM        Unreviewed;       480 AA.
AC   A0A101WLE5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KUO75195.1};
GN   ORFNames=APF77_15845 {ECO:0000313|EMBL:KUO75195.1};
OS   Clostridia bacterium BRH_c25.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO75195.1, ECO:0000313|Proteomes:UP000057710};
RN   [1] {ECO:0000313|EMBL:KUO75195.1, ECO:0000313|Proteomes:UP000057710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO75195.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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:KUO75195.1}.
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DR   EMBL; LOES01000072; KUO75195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101WLE5; -.
DR   STRING; 1734399.APF77_15845; -.
DR   Proteomes; UP000057710; 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; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF122; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLH; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468}.
FT   ACT_SITE        375
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   480 AA;  56008 MW;  169F3D5ADE8A4196 CRC64;
     MKRIYKEFPG DFLWGGAIAA NQAEGAFDVD GKGLSIADFH AHEYKQNRDD RREDFTLKNT
     RETLTIDHKK YYPKQQGIDF FHTYKQDLSL MREMGLKCLR TSFNWARIFP KGDEIEPNQK
     GLRFYDQLID EMLANNIEPV MTISHYELPV HLVKEYGGWG NRKLVDFYVR LCEVLFQRYS
     NKVEYWITFN QINLLTFNSL GLLQENYDNM LQATYQAVHH QFVAQAMAKK IASKYDKVMV
     GTMLSDKIAH PATCKPEDIL FNMRKNQMQF LFSDVAMRGF YPGYALRYFA DNNINIVFES
     GDEELLSTFT MDYLSFSYYY TKINDASKNT YEPTDKCKNP YLAASEWGWE IDPLGLRTAL
     NTYYDRYNCP LFITENGLGA RDTVDLDGGI HDPYRIRYVN DHLIQMREAI RDGVELVGYC
     AWSPIDIVSC SSAEMSKRYG FIYVDIDDEG KGSGKRILKD SYFWYRDVIK TNGKNIIQHD
//
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