ID   A0A1M6Q4F4_9FIRM        Unreviewed;       454 AA.
AC   A0A1M6Q4F4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN   ORFNames=SAMN02745136_01859 {ECO:0000313|EMBL:SHK15006.1};
OS   Anaerocolumna jejuensis DSM 15929.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerocolumna.
OX   NCBI_TaxID=1121322 {ECO:0000313|EMBL:SHK15006.1, ECO:0000313|Proteomes:UP000184386};
RN   [1] {ECO:0000313|EMBL:SHK15006.1, ECO:0000313|Proteomes:UP000184386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15929 {ECO:0000313|EMBL:SHK15006.1,
RC   ECO:0000313|Proteomes:UP000184386};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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         ECO:0000256|RuleBase:RU361175};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR   EMBL; FRAC01000009; SHK15006.1; -; Genomic_DNA.
DR   RefSeq; WP_073275052.1; NZ_FRAC01000009.1.
DR   AlphaFoldDB; A0A1M6Q4F4; -.
DR   STRING; 1121322.SAMN02745136_01859; -.
DR   OrthoDB; 2339329at2; -.
DR   Proteomes; UP000184386; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR03356; BGL; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361175};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184386}.
FT   ACT_SITE        163
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        359
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10055"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         413..414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   454 AA;  52544 MW;  997481FCEF9FBDD8 CRC64;
     MGFRKDFVWG AANASYQVEG APREEGKGLS IWDVFCREDG KIYENQNGDI SCDQYHRYRE
     DVKMMKDIGI QAYRFSISWP RILPDGEGEV NARGLEYYDN LVDELLANNI QPYITLYHWD
     LPYELQKKGG WMNPDIPELF YKYAAILAKH FSDRVEHFIT INEPQCIAGL GYLTGVHAPG
     LKVGAAGFFT IWHNLLKAHG MAVKAIREHA VRPVKIGMAP CSALYYPASE SEADIMAARK
     ATFHLTNNSL EDCVWNIALW CDPVFRQEYP KEVYEYFGEY LPEITKEDMA LISQPLDFYG
     QNMYNAVMVK ADKNGNPVRV KRPEGFPKTA IQWPVTPECM YWAPRFLSER YQKPLIITEN
     GMSSHDWIAL DGKVHDSSRI DFMHRYLKEY KRGANEGIDL LGYFSWSSMD NFEWAYGYSE
     RFGLIYVDYQ TQKRTMKDSG YFYRDVISCN GENL
//