ID   BGLA_ASPTN              Reviewed;         861 AA.
AC   Q0CTD7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-MAY-2023, entry version 66.
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; ORFNames=ATEG_03047;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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; CH476597; EAU36321.1; -; Genomic_DNA.
DR   RefSeq; XP_001212225.1; XM_001212225.1.
DR   AlphaFoldDB; Q0CTD7; -.
DR   SMR; Q0CTD7; -.
DR   STRING; 341663.Q0CTD7; -.
DR   GlyCosmos; Q0CTD7; 11 sites, No reported glycans.
DR   EnsemblFungi; EAU36321; EAU36321; ATEG_03047.
DR   GeneID; 4318025; -.
DR   VEuPathDB; FungiDB:ATEG_03047; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OMA; YYPSPWA; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..861
FT                   /note="Probable beta-glucosidase A"
FT                   /id="PRO_0000394099"
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;  93356 MW;  053DBE0B894FFBC2 CRC64;
     MKLSILEAAA LTAASVVSAQ DDLAYSPPYY PSPWADGHGE WSNAYKRAVD IVSQMTLTEK
     VNLTTGTGWE LERCVGQTGS VPRLGIPSLC LQDSPLGIRM SDYNSAFPAG INVAATWDKK
     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 GFLNVDGNMG DRKNLTLWQN GEEVIKTVTE
     HCNNTVVVIH SVGPVLIDEW YAHPNVTGIL WAGLPGQESG NAIADVLYGR VNPGGKTPFT
     WGKTRASYGD YLLTEPNNGN GAPQDNFNEG VFIDYRRFDK YNETPIYEFG HGLSYTTFEL
     SGLQVQLING SSYVPTTGQT SAAQAFGKVE DASSYLYPEG LKRISKFIYP WLNSTDLKAS
     TGDPEYGEPN FEYIPEGATD GSPQPRLPAS GGPGGNPGLY EDLFQVSVTI TNTGKVAGDE
     VPQLYVSLGG PNEPKRVLRK FERLHIAPGQ QKVWTTTLNR RDLANWDVVA QDWKITPYAK
     TIFVGTSSRK LPLAGRLPRV Q
//