ID   BGLL_ASPFU              Reviewed;         739 AA.
AC   Q4WGT3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=AFUA_7G06140;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000009; EAL86858.1; -; Genomic_DNA.
DR   RefSeq; XP_748896.1; XM_743803.1.
DR   AlphaFoldDB; Q4WGT3; -.
DR   SMR; Q4WGT3; -.
DR   STRING; 330879.Q4WGT3; -.
DR   GlyCosmos; Q4WGT3; 3 sites, No reported glycans.
DR   EnsemblFungi; EAL86858; EAL86858; AFUA_7G06140.
DR   GeneID; 3506305; -.
DR   KEGG; afm:AFUA_7G06140; -.
DR   VEuPathDB; FungiDB:Afu7g06140; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   InParanoid; Q4WGT3; -.
DR   OMA; MYGWDAY; -.
DR   OrthoDB; 2783936at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..739
FT                   /note="Probable beta-glucosidase L"
FT                   /id="PRO_0000394900"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  78381 MW;  DCDFA27EB664D341 CRC64;
     MQTLFLSLLA AAVTVHAYGS GGSNWDQAYS RAKDALQKLN QTEKVGLVTG VKWMGGPCVG
     NTYKPESIDY PSLCLQDSPL GIRFANPVTA FPAGINAGAT WDTQLLYARG AAMGAEAKGL
     GIHVQLGPVA GPLGKNPNGG RNWEGFSVDP YLSGVAMEKT IRGMQDSGVQ ACAKHWLGNE
     QEHYRDTISS NIGDRAAHEL YVWPFMDAVK AGVASVMCSY NKVNGTWACE SDALNNKLMK
     EELGFPGYIM SDWNAQHSTV NSAVSGLDMT MPGSDFSNPP GSIFWGSNLE AAVADGSVPQ
     SRLDDMVTRI LAAWYLVGQD QGYPPVAFSS WNGGKANVDV TADHGTVARA VARDSIVLLK
     NGHGTLPLRK PKSLAIVGSD AIVNPAGPNA CSDRGCNNGT LAMGWGSGTA EFPYLVGPLD
     AIQKRAAADG TKIVPSATDD PTAGASAAAA AETAIVFINS DSGEGYITVE GNLGDRNNLD
     PWHNGNELVK AVAAASKNVI VVIHSVGPII LETILAQPSV KAIVWAGLPG QESGNALVDV
     IYGDTTPSGK LPYTIAKQAA DYGASWINAE TDDFPEGLYV DYRHFDAKGI APRYEFGYGL
     SYTTFKYSGL WVNMDASAGA ANGQVVPGGP ADLFEVVGQV SVSVRNNGRV AGAEVAQLYL
     GLPDSAPATP PKQLRGFQKL MLQPGQTGRA TFKLTRRDLS YWDVQQQKWV VPSGTFKVYV
     GSSSRDIREE GSFRVRRGW
//