ID   BGLA_ASPTE              Reviewed;         861 AA.
AC   D0VKF5;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   22-FEB-2023, entry version 45.
DE   RecName: Full=Probable beta-glucosidase A;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase A;
DE   AltName: Full=Cellobiase A;
DE   AltName: Full=Gentiobiase A;
DE   Flags: Precursor;
GN   Name=bglA; Synonyms=bgl1;
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SUK-1;
RA   Abdul Hani A.M., Shaiful Adzni S., Nik Marzuki S.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC       involved in the degradation of cellulosic biomass. Catalyzes the last
CC       step releasing glucose from the inhibitory cellobiose (By similarity).
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; GU078571; ACY03273.1; -; mRNA.
DR   AlphaFoldDB; D0VKF5; -.
DR   SMR; D0VKF5; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; D0VKF5; 11 sites, No reported glycans.
DR   VEuPathDB; FungiDB:ATEG_03047; -.
DR   UniPathway; UPA00696; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF12; BETA-GLUCOSIDASE A-RELATED; 1.
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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..861
FT                   /note="Probable beta-glucosidase A"
FT                   /id="PRO_0000394098"
FT   REGION          735..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        543
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        669
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        713
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   861 AA;  93333 MW;  F0D2FDF24D07B8D0 CRC64;
     MKLSILEAAA LTAASVASAQ DDLAYSPPYY PSPWADGHGE WSNAYKRAVD IVSQMTLTEK
     VNLTTGTGWE LERCVGQTGS VPRLGIPSLC LQDSPLGIRM SDYNSAFPAG INVAATWDKT
     LAYQRGKAMG EEFSDKGIDV QLGPAAGPLG RSPDGGRNWE GFSPDPALTG VLFAETIKGI
     QDAGVIATAK HYILNEQEHF RQVGEAQGYG FNITETVSSN VDDKTMHELY LWPFADAVRA
     GVGAVMCSYN QINNSYGCQN SLTLNKLLKA ELGFQGFVMS DWSAHHSGVG AALAGLDMSM
     PGDISFDSGT SFYGTNLTVG VLNGTIPQWR VDDMAVRIMA AYYKVGRDRL WTPPNFSSWT
     RDEYGFAHFF PSEGAYERVN EFVNVQRDHA QVIRRIGADS VVLLKNDGAL PLTGQEKTVG
     ILGEDAGSNP KGANGCSDRG CDKGTLAMAW GSGTANFPYL VTPEQAIQNE VLKGRGNVFA
     VTDNYDTQQI AAVASQSTVS LVFVNADAGE GYLNVDGNMG DRKNLTLWQN GEEVIKTVTE
     HCNNTVVVIH SVGPVLIDEW YAHPNVTGIL WAGLPGQESG NAIADVLYGR VNPGGKTPFT
     WGKTRASYGD YLLTEPNNGN GAPQDNFNEG VFIDYRRFDK YNETPIYEFG HGLSYTTFEL
     SGLQVQLING SSYVPTTGQT SAAQTFGKVE DASSYLYPEG LKRISKFIYP WLNSTDLKAS
     TGDPDYGEPN FEYIPEGATD GSPQPRLPAS GGPGGNPGLY EDLFQVSVTI TNTGKVAGDE
     VPQLYVSLGG PNEPKRVLRK FERLHLAPGQ QKVWTTTLNR RDLANWDVVA QDWKITPYAK
     TIFVGTSSRK LPLAGRLPRV Q
//