ID   BGLA_ENTAG              Reviewed;         480 AA.
AC   Q59437;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Beta-glucosidase A;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Gentiobiase;
GN   Name=bglA;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WD4;
RX   PubMed=7750731; DOI=10.1111/j.1574-6968.1995.tb07512.x;
RA   Marri L., Valentini S., Venditti D.;
RT   "Cloning and nucleotide sequence of the bglA gene from Erwinia herbicola
RT   and expression of beta-glucosidase activity in Escherichia coli.";
RL   FEMS Microbiol. Lett. 128:135-138(1995).
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; X79911; CAA56282.1; -; Genomic_DNA.
DR   PIR; S49182; S49182.
DR   AlphaFoldDB; Q59437; -.
DR   SMR; Q59437; -.
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   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; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 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..480
FT                   /note="Beta-glucosidase A"
FT                   /id="PRO_0000063877"
FT   ACT_SITE        177
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        378
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   480 AA;  53889 MW;  60493E7CDD69C403 CRC64;
     MKNGMLALGM TAADVPDNFL WGAASAAYQV EGATNKDGKG RSVWDYYLDE KHLAGPGISG
     ALRLTFTDRD QYLKDIQLFK ELGLNSYRFS HRLDTYYPDG QGPVNLRAVA HYRQFITDLE
     AAGIKPLVTL YHWDMPESLS AAGGWENRES VEWFQRYAEV IFANFSDQVD QFVLINEPTV
     EVATKIMAEK RLKGEELTLP PIVPAGSYLE TSLKSYNHIL LASAAAAESF KVKGYKGRLG
     IALPFFPVLT TENASDEDKA DARLVDGILN RWFLDAMYKG NYPADVLKLA ADRHLNIDVQ
     PGDAERIHDA GLGFLGINYY APFFIRHQKN ASEVYSPEII FPKNEKLAFN GAVRPDQFSA
     LLERVRDEYG NPPVIITENG AGFEGEDQLT NGKVNDVNRC LYLVDHIHAM RESIARGANV
     QGYYVWSSHD NLEWLSGYKS RFGMIYVDYD TQKRTPKLSA EIYGKIIRGE NISDVDCKSD