ID   BGL1_SACFI              Reviewed;         876 AA.
AC   P22506;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Beta-glucosidase 1;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
DE   Flags: Precursor;
GN   Name=BGL1;
OS   Saccharomycopsis fibuligera (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycopsidaceae; Saccharomycopsis.
OX   NCBI_TaxID=4944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3146949; DOI=10.1128/aem.54.12.3147-3155.1988;
RA   Machida M., Ohtsuki I., Fukui S., Yamashita I.;
RT   "Nucleotide sequences of Saccharomycopsis fibuligera genes for
RT   extracellular beta-glucosidases as expressed in Saccharomyces cerevisiae.";
RL   Appl. Environ. Microbiol. 54:3147-3155(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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; M22475; AAA34314.1; -; Genomic_DNA.
DR   PIR; A45956; A45956.
DR   AlphaFoldDB; P22506; -.
DR   SMR; P22506; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   CLAE; BGL3A_SACFI; -.
DR   UniPathway; UPA00696; -.
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-UniPathway.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..17
FT   CHAIN           18..876
FT                   /note="Beta-glucosidase 1"
FT                   /id="PRO_0000011779"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        389
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        426
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        544
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        585
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        739
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        780
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        790
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   876 AA;  96231 MW;  DBB4ABB9E4A32F1E CRC64;
     MLMIVQLLVF ALGLAVAVPI QNYTQSPSQR DESSQWVSPH YYPTPQGGRL QDVWQEAYAR
     AKAIVGQMTI VEKVNLTTGT GWQLDPCVGN TGSVPRFGIP NLCLQDGPLG VRFADFVTGY
     PSGLATGATF NKDLFLQRGQ ALGHEFNSKG VHIALGPAVG PLGVKARGGR NFEAFGSDPY
     LQGTAAAATI KGLQENNVMA CVKHFIGNEQ EKYRQPDDIN PATNQTTKEA ISANIPDRAM
     HALYLWPFAD SVRAGVGSVM CSYNRVNNTY ACENSYMMNH LLKEELGFQG FVVSDWGAQL
     SGVYSAISGL DMSMPGEVYG GWNTGTSFWG QNLTKAIYNE TVPIERLDDM ATRILAALYA
     TNSFPTEDHL PNFSSWTTKE YGNKYYADNT TEIVKVNYNV DPSNDFTEDT ALKVAEESIV
     LLKNENNTLP ISPEKAKRLL LSGIAAGPDP IGYQCEDQSC TNGALFQGWG SGSVGSPKYQ
     VTPFEEISYL ARKNKMQFDY IRESYDLAQV TKVASDAHLS IVVVSAASGE GYITVDGNQG
     DRKNLTLWNN GDKLIETVAE NCANTVVVVT STGQINFEGF ADHPNVTAIV WAGPLGDRSG
     TAIANILFGK ANPSGHLPFT IAKTDDDYIP IETYSPSSGE PEDNHLVEND LLVDYRYFEE
     KNIEPRYAFG YGLSYNEYEV SNAKVSAAKK VDEELPEPAT YLSEFSYQNA KDSKNPSDAF
     APADLNRVNE YLYPYLDSNV TLKDGNYEYP DGYSTEQRTT PNQPGGGLGG NDALWEVAYN
     STDKFVPQGN STDKFVPQLY LKHPEDGKFE TPIQLRGFEK VELSPGEKKT VDLRLLRRDL
     SVWDTTRQSW IVESGTYEAL IGVAVNDIKT SVLFTI