ID   BGLS_KLUMA              Reviewed;         845 AA.
AC   P07337;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   25-MAY-2022, entry version 96.
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   Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=4911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12424 / NRRL Y-610;
RX   PubMed=2835179; DOI=10.1007/bf00436876;
RA   Raynal A., Gerbaud C., Francingues M.C., Guerineau M.;
RT   "Sequence and transcription of the beta-glucosidase gene of Kluyveromyces
RT   fragilis cloned in Saccharomyces cerevisiae.";
RL   Curr. Genet. 12:175-184(1987).
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; X05918; CAA29353.1; -; Genomic_DNA.
DR   PIR; A29148; GLVK.
DR   AlphaFoldDB; P07337; -.
DR   SMR; P07337; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   PRIDE; P07337; -.
DR   BRENDA; 3.2.1.21; 1120.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..?
FT   CHAIN           ?..845
FT                   /note="Beta-glucosidase"
FT                   /id="PRO_0000011778"
FT   DOMAIN          408..568
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        621
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   845 AA;  93917 MW;  78D4C1550D5992B5 CRC64;
     MSKFDVEQLL SELNQDEKIS LLSAVDFWHT KKIERLGIPA VRVSDGPNGI RGTKFFDGVP
     SGCFPNGTGL ASTFDRDLLE TAGKLMAKES IAKNAAVILG PTTNMQRGPL GGRGFESFSE
     DPYLAGMATS SVVKGMQGEG IAATVKHFVC NDLEDQRFSS NSIVSERALR EIYLEPFRLA
     VKHANPVCIM TAYNKVNGDH CSQSKKLLID ILRDEWKWDG MLMSDWFGTY TTAAAIKNGL
     DIEFPGPTRW RTRALVSHSL NSREQITTED VDDRVRQVLK MIKFVVDNLE KTGIVENGPE
     STSNNTKETS DLLREIAADS IVLLKNKNNY LTSKERRQYH VIGPNAKAKT SSGGGSASMN
     SYYVVSPYEG IVNKLGKEVD YTVGAYSHKS IGGLAESSLI DAAKPADAEN AGLIAKFYSN
     PVEERSEDEE PFHVTKVNRS NVHLFDFKHE KVDPKNPYFF VTLTGQYVPQ EDGDYIFSLQ
     VYGSGLFYLN DELIIDQKHN QERGSFCFGA GTKERTKKLT LKKGQVYNVR VEYGSGPTSG
     LVGEFGAGGF QAGVIKAIDD DEEIRNAAEL AAKHDKAVLI IGLNGEWETE GYDRENMDLP
     KRTNELVRAV LKANPNTVIV NQSGTPVEFP WLEEANALVQ AWYGGNELGN AIADVLYGDV
     VPNGKLSLSW PFKLQDNPAF LNFKTEFGRV VYGEDIFVGY RYYEKLQRKV AFPFGYGLSY
     TTFELDISDF KVTDDKIDIS VDVKNTGDKF AGSEVVQVYF SALNSKVSRP VKELKGFEKV
     HLEPGEKKTV NIELELKDAI SYFNEELGKW HVEAGEYLVS VGTSSDDILS VKEFKVEKDL
     YWKGL