ID   BGLL_NEOFI              Reviewed;         739 AA.
AC   A1DCV5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=NFIA_027390;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027695; EAW19665.1; -; Genomic_DNA.
DR   RefSeq; XP_001261562.1; XM_001261561.1.
DR   AlphaFoldDB; A1DCV5; -.
DR   SMR; A1DCV5; -.
DR   STRING; 36630.CADNFIAP00002473; -.
DR   EnsemblFungi; EAW19665; EAW19665; NFIA_027390.
DR   GeneID; 4587975; -.
DR   KEGG; nfi:NFIA_027390; -.
DR   VEuPathDB; FungiDB:NFIA_027390; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   OMA; GYPPVAF; -.
DR   OrthoDB; 321444at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006702; 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; 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; 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   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; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..739
FT                   /note="Probable beta-glucosidase L"
FT                   /id="PRO_0000394903"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   739 AA;  78745 MW;  B1C91E318B77381A CRC64;
     MQNLFLSLLA AAVTVHAYGS GGSNWDQAYS RAKDALQKLS QTEKVGLVTG VKWMGGPCVG
     NTYKPESIDY PSLCLQDSPL GIRFANPVTA FPAGINAGAT WDTQLLYARG AAMGAEAKGL
     GVHVQLGPVA GPLGKNPNGG RNWEGFSVDP YLSGVAMEKT IRGMQDSGVQ ACAKHWLGNE
     QEHYRDTISS NIGDRAAHEL YVWPFMDAVK ADVASVMCSY NKVNGTWACE SDAINNKLMK
     EELGFPGYIM SDWNAQHSTV NSAVSGLDMT MPGSDFSNPP GSIFWGSNLE AAVADGSVPQ
     SRLDDMVTRI LAAWYLVGQD KGYPPVAFSS WNGGKANVDV TADHGTVARA VARDSIVLLK
     NDQRTLPLRK PKSLAIVGLD AIVNPAGPNA CSDRGCNNGT LAMGWGSGTA EFPYLVGPLD
     AIQKRAAADG TKIVPSTTDD PTAGASAAAA AETAIVFINS DSGEGYITVE GNLGDRNNLD
     PWHNGNELVK AVAAASKNVI VVVHSVGPII LETILAQPSV KAIVWAGLPG QESGNALVDV
     IYGDTAPSGK LPYTIAKQAA DYGASWINAE TDDFTEGLYI DYRHFDAKGI APRYEFGYGL
     SYTTFKYSGL WVNVYTSAGA ANGKVVPGGP ADLFEVVGQV SVFVRNNGRV AGAEVAQLYI
     GLPDSAPATP PKQLRGFQKM MLQPGQMGRA TFELTRRDLS YWDVQQQKWV VPSGTFKVYV
     GSSSRDIREE GSFRVRRGW