ID   BGLS_CALSA              Reviewed;         455 AA.
AC   P10482;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Beta-glucosidase A;
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=bglA;
OS   Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=44001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2851713; DOI=10.1007/bf00333402;
RA   Love D.R., Bergquist P.L.;
RT   "Sequence structure and expression of a cloned beta-glucosidase gene from
RT   an extreme thermophile.";
RL   Mol. Gen. Genet. 213:84-92(1988).
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   -!- MISCELLANEOUS: C.saccharolyticum is an extreme thermophile and appears
CC       to be a Gram-positive anaerobic bacterium.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; X12575; CAA31087.1; -; Genomic_DNA.
DR   PIR; S03813; S03813.
DR   AlphaFoldDB; P10482; -.
DR   SMR; P10482; -.
DR   BindingDB; P10482; -.
DR   ChEMBL; CHEMBL4622; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   BRENDA; 3.2.1.21; 1055.
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; IPR017736; Glyco_hydro_1_beta-glucosidase.
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   TIGRFAMs; TIGR03356; BGL; 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..455
FT                   /note="Beta-glucosidase A"
FT                   /id="PRO_0000063875"
FT   ACT_SITE        165
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        363
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   455 AA;  53492 MW;  9443ABB7EFC499E1 CRC64;
     MDMSFPKGFL WGAATASYQI EGAWNEDGKG ESIWDRFTHQ KRNILYGHNG DVACDHYHRF
     EEDVSLMKEL GLKAYRFSIA WTRIFPDGFG TVNQKGLEFY DRLINKLVEN GIEPVVTLYH
     WDLPQKLQDI GGWANPEIVN YYFDYAMLVI NRYKDKVKKW ITFNEPYCIA FLGYFHGIHA
     PGIKDFKVAM DVVHSLMLSH FKVVKAVKEN NIDVEVGITL NLTPVYLQTE RLGYKVSEIE
     REMVSLSSQL DNQLFLDPVL KGSYPQKLLD YLVQKDLLDS QKALSMQQEV KENFIFPDFL
     GINYYTRAVR LYDENSSWIF PIRWEHPAGE YTEMGWEVFP QGLFDLLIWI KESYPQIPIY
     ITENGAAYND IVTEDGKVHD SKRIEYLKQH FEAARKAIEN GVDLRGYFVW SLMDNFEWAM
     GYTKRFGIIY VDYETQKRIK KDSFYFYQQY IKENS