ID   BGLS_AGRSA              Reviewed;         459 AA.
AC   P12614;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Beta-glucosidase;
DE            EC=3.2.1.21;
DE   AltName: Full=Amygdalase;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
GN   Name=abg;
OS   Agrobacterium sp. (strain ATCC 21400).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=74562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2826395; DOI=10.1128/jb.170.1.301-307.1988;
RA   Wakarchuk W.W., Greenberg N.M., Kilburn D.G., Miller R.C. Jr.,
RA   Warren R.A.J.;
RT   "Structure and transcription analysis of the gene encoding a cellobiase
RT   from Agrobacterium sp. strain ATCC 21400.";
RL   J. Bacteriol. 170:301-307(1988).
RN   [2]
RP   ACTIVE SITE GLU-359.
RA   Withers S.G., Warren R.A.J., Street I.P., Rupitz K., Kempton J.B.,
RA   Aebersold R.;
RT   "Unequivocal demonstration of the involvement of a glutamate residue as a
RT   nucleophile in the mechanism of a 'retaining' glycosidase.";
RL   J. Am. Chem. Soc. 112:5887-5889(1990).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; M19033; AAA22085.1; -; Genomic_DNA.
DR   PIR; A28673; GLAG.
DR   AlphaFoldDB; P12614; -.
DR   SMR; P12614; -.
DR   BindingDB; P12614; -.
DR   ChEMBL; CHEMBL1075038; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
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; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..459
FT                   /note="Beta-glucosidase"
FT                   /id="PRO_0000063869"
FT   ACT_SITE        171
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        359
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055,
FT                   ECO:0000269|Ref.2"
SQ   SEQUENCE   459 AA;  51170 MW;  AAB799153493A682 CRC64;
     MTDPNTLAAR FPGDFLFGVA TASFQIEGST KADGRKPSIW DAFCNMPGHV FGRHNGDIAC
     DHYNRWEEDL DLIKEMGVEA YRFSLAWPRI IPDGFGPINE KGLDFYDRLV DGCKARGIKT
     YATLYHWDLP LTLMGDGGWA SRSTAHAFQR YAKTVMARLG DRLDAVATFN EPWCAVWLSH
     LYGVHAPGER NMEAALAAMH HINLAHGFGV EASRHVAPKV PVGLVLNAHS AIPASDGEAD
     LKAAERAFQF HNGAFFDPVF KGEYPAEMME ALGDRMPVVE AEDLGIISQK LDWWGLNYYT
     PMRVADDATP GVEFPATMPA PAVSDVKTDI GWEVYAPALH TLVETLYERY DLPECYITEN
     GACYNMGVEN GQVNDQPRLD YYAEHLGIVA DLIRDGYPMR GYFAWSLMDN FEWAEGYRMR
     FGLVHVDYQT QVRTVKNSGK WYSALASGFP KGNHGVAKG
//