ID   BGLS_WICAO              Reviewed;         825 AA.
AC   P06835;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Beta-glucosidase;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Cellobiase;
DE   AltName: Full=Gentiobiase;
DE   Flags: Precursor;
OS   Wickerhamomyces anomalus (Yeast) (Hansenula anomala).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=4927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Acetaetherius;
RX   PubMed=2995925; DOI=10.1093/nar/13.17.6273;
RA   Kohchi C., Toh-e A.;
RT   "Nucleotide sequence of Candida pelliculosa beta-glucosidase gene.";
RL   Nucleic Acids Res. 13:6273-6282(1985).
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   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; X02903; CAA26662.1; -; Genomic_DNA.
DR   PIR; B23783; GLHQ.
DR   AlphaFoldDB; P06835; -.
DR   SMR; P06835; -.
DR   BindingDB; P06835; -.
DR   ChEMBL; CHEMBL4168; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
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; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
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   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..825
FT                   /note="Beta-glucosidase"
FT                   /id="PRO_0000011777"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
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        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        537
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        556
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        578
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        667
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        690
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        718
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        733
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        761
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   825 AA;  89561 MW;  A43852FF3DE58B74 CRC64;
     MLLPLYGLAS FLVLSQAALV NTSAPQASND DPFNHSPSFY PTPQGGRIND GKWQAAFYRA
     RELVDQMSIA EKVNLTTGVG SASGPCSGNT GSVPRLNISS ICVQDGPLSV RAADLTDVFP
     CGMAASSSFN KQLIYDRAVA IGSEFKGKGA DAILGPVYGP MGVKAAGGRG WEGHGPDPYL
     EGVIAYLQTI GIQSQGVVST AKHLIGNEQE HFRFAKKDKH AGKIDPGMFN TSSSLSSEID
     DRAMHEIYLW PFAEAVRGGV SSIMCSYNKL NGSHACQNSY LLNYLLKEEL GFQGFVMTDW
     GALYSGIDAA NAGLDMDMPC EAQYFGGNLT TAVLNGTLPQ DRLDDMATRI LSALIYSGVH
     NPDGPNYNAQ TFLTEGHEYF KQQEGDIVVL NKHVDVRSDI NRAVALRSAV EGVVLLKNEH
     ETLPLGREKV KRISILGQAA GDDSKGTSCS LRGCGSGAIG TGYGSGAGTF SYFVTPADGI
     GARAQQEKIS YEFIGDSWNQ AAAMDSALYA DAAIEVANSV AGEEIGDVDG NYGDLNNLTL
     WHNAVPLIKN ISSINNNTIV IVTSGQQIDL EPFIDNENVT AVIYSSYLGQ DFGTVLAKVL
     FGDENPSGKL PFTIAKDVND YIPVIEKVDV PDPVDKFTES IYVDYRYFDK YNKPVRYEFG
     YGLSYSNFSL SDIEIQTLQP FSENAEPAAN YSETYQYKQS NMDPSEYTVP EGFKELANYT
     YPYIHDASSI KANSSYDYPE GYSTEQLDGP KSLAAGGLGG NHTCGMLVTL SLLKSQIKVL
     MLVGLHLNCM LDIQIMMNSQ HLQCNYVDLK RCFWIKIILK LFLLN