ID   BGL2_SACFI              Reviewed;         880 AA.
AC   P22507;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Beta-glucosidase 2;
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=BGL2;
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; M22476; AAA34315.1; -; Genomic_DNA.
DR   PIR; B45956; B45956.
DR   AlphaFoldDB; P22507; -.
DR   SMR; P22507; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   CLAE; BGL3B_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..880
FT                   /note="Beta-glucosidase 2"
FT                   /id="PRO_0000011780"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        548
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        589
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        712
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        743
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        794
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   880 AA;  96799 MW;  C95061283090814C CRC64;
     MLLILELLVL IIGLGVALPV QTHNLTDNQG FDEESSQWIS PHYYPTPQGG RLQGVWQDAY
     TKAKALVSQM TIVEKVNLTT GTGWQLGPCV GNTGSVPRFG IPNLCLQDGP LGVRLTDFST
     GYPSGMATGA TFNKDLFLQR GQALGHEFNS KGVHIALGPA VGPLGVKARG GRNFEAFGSD
     PYLQGIAAAA TIKGLQENNV MACVKHFIGN EQDIYRQPSN SKVDPEYDPA TKESISANIP
     DRAMHELYLW PFADSIRAGV GSVMCSYNRV NNTYSCENSY MINHLLKEEL GFQGFVVSDW
     AAQMSGAYSA ISGLDMSMPG ELLGGWNTGK SYWGQNLTKA VYNETVPIER LDDMATRILA
     ALYATNSFPT KDRLPNFSSF TTKEYGNEFF VDKTSPVVKV NHFVDPSNDF TEDTALKVAE
     ESIVLLKNEK NTLPISPNKV RKLLLSGIAA GPDPKGYECS DQSCVDGALF EGWGSGSVGY
     PKYQVTPFEE ISANARKNKM QFDYIRESFD LTQVSTVASD AHMSIVVVSA VSGEGYLIID
     GNRGDKNNVT LWHNSDNLIK AVAENCANTV VVITSTGQVD VESFADHPNV TAIVWAGPLG
     DRSGTAIANI LFGNANPSGH LPFTVAKSND DYIPIVTYNP PNGEPEDNTL AEHDLLVDYR
     YFEEKNIEPR YAFGYGLSYN EYKVSNAKVS AAKKVDEELP QPKLYLAEYS YNKTEEINNP
     EDAFFPSNAR RIQEFLYPYL DSNVTLKDGN YEYPDGYSTE QRTTPIQPGG GLGGNDALWE
     VAYKVEVDVQ NLGNSTDKFV PQLYLKHPED GKFETPVQLR GFEKVELSPG EKKTVEFELL
     RRDLSVWDTT RQSWIVESGT YEALIGVAVN DIKTSVLFTI