ID   BGLL_ASPTN              Reviewed;         736 AA.
AC   Q0CEF3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Probable beta-glucosidase L;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase L;
DE   AltName: Full=Cellobiase L;
DE   AltName: Full=Gentiobiase L;
DE   Flags: Precursor;
GN   Name=bglL; ORFNames=ATEG_07931;
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; CH476604; EAU32193.1; -; Genomic_DNA.
DR   RefSeq; XP_001216552.1; XM_001216552.1.
DR   AlphaFoldDB; Q0CEF3; -.
DR   SMR; Q0CEF3; -.
DR   STRING; 341663.Q0CEF3; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; Q0CEF3; 5 sites, No reported glycans.
DR   EnsemblFungi; EAU32193; EAU32193; ATEG_07931.
DR   GeneID; 4322590; -.
DR   VEuPathDB; FungiDB:ATEG_07931; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   OMA; TVCGAAQ; -.
DR   OrthoDB; 2783936at2759; -.
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; 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:SF29; BETA-GLUCOSIDASE L-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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..736
FT                   /note="Probable beta-glucosidase L"
FT                   /id="PRO_0000394901"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   736 AA;  77665 MW;  120D766A541FC56B CRC64;
     MNYRVPSLKA TALAMAALTQ ALTTWDAAYE KALADLASLT QSEKVGVVSG ITWEGGPCVG
     NTYAPESIAY PSLCLQDGPL GIRFANPVTA FPAGINAGAT WDRELLRARG AAMGEEAKGL
     GVHVQLAPVA GALGKIPSAG RNWEGFTSDP YLSGIAMAET IHGMQGSGVQ ACAKHYILNE
     QEHSRETISS NVDDRTMHEV YLWPFYDAVK ANVASVMCSY NKINGTWACE NEGILDTLLK
     QELGFRGYVM SDWNAQHSTV ASANTGLDMT MPGSDFSQPP GSIYWNENLA EAVANGSVPQ
     ARVDDMVTRI LAAWYLLEQD QGYPAVAFDS RNGGKASVDV TADHADIART VARDSIVLLK
     NSNNTLPLRN PSSIAVVGSD AIVNPDGPNA CTDRGCNVGT LAQGWGSGTA EFPYLVAPLD
     AIQERSSGNG TKVVTSTTDD ATAGADAAAS ADIAIVFISS DSGEGYITVE GHQGDRNNLD
     PWHGGNDLVK AVAAVNKKTI VVVHSTGPVV LETILAQPNV VAVVWAGIPG QESGNALADV
     LYGDVSPSGK LPYTIGKSEA DYGTTWVANG ADDDFPEGLF IDYRHFDKNE IEPRYEFGFG
     LSYTRFNFSN LAINIDATSG PTSGAVDVGG AADLYDSVGT ISATVTNVGG VSGAEVAQLY
     IGFPSSAPET PPKQLRGFQK LPLAGGADGV AEFELTRRDI SYWDVGQQKW VVPEGSFQVY
     VGASSRDIRL DGSFTV
//