ID   BGLI_ASPFC              Reviewed;         838 AA.
AC   B0Y3M6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Probable beta-glucosidase I;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase I;
DE   AltName: Full=Cellobiase I;
DE   AltName: Full=Gentiobiase I;
GN   Name=bglI; ORFNames=AFUB_054750;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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; DS499597; EDP51467.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y3M6; -.
DR   SMR; B0Y3M6; -.
DR   EnsemblFungi; EDP51467; EDP51467; AFUB_054750.
DR   VEuPathDB; FungiDB:AFUB_054750; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   PhylomeDB; B0Y3M6; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001699; 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; 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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted.
FT   CHAIN           1..838
FT                   /note="Probable beta-glucosidase I"
FT                   /id="PRO_0000394884"
FT   DOMAIN          395..555
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   838 AA;  92196 MW;  3684CAD544B47620 CRC64;
     MVQLDVEKTI EELTLGEKVA LTAGIDFWHT AAVPRLNIPS LRMSDGPNGV RGTRFFNGVP
     AACFPCATAL GATWDTKLLY EVGRLMGEES IAKGAHVVLG PTINTQRSPL GGRGFESFAE
     DGVLSGILAG HYCKGLQETG VAATLKHFVC NDQEHERLAV DSIVTMRAMR EIYLLPFQLA
     MRICKTACVM TAYNKVNGTH VSENKQIITD ILRKEWGWDG LVMSDWFGTY STCDAINAGL
     DLEMPGPTRW RGTALAHAVS SNKAFEFVMD ERVRNILNLH NFVEPLGIPE NAPEKALNRP
     EDQALLRRAA AESVVLMKNQ DNILPLKKEK PILVIGPNAK TAAYCGGGSA SLDAYYTVTP
     FEGVAAQSQG EVTFSQGVYS YKELPLLGPL LKTDDGKKGF KFRVYNEPPS EPNRQLIDEL
     HLESSSGFLM DYKHPKIKTF TFYVDMEGYF TPEEDGIYDF GVTVVGTGKL FVDDELVVDN
     SKNQRQGTAM FGNATVEEKG SKELKAGQTY KVVLQFGTAP TSDLDMRGVV IFGPGGFRFG
     AARRVSQEEL ISKAAELASQ ASQVVIFAGL TSEWETEGYD RDHMDLPPGS DEMISRVLDA
     NPDTVVVIQS GTPVTMPWAH KAKALLQAWF GGNECGNGIA DVLYGNVNPA AKLPLSFPVR
     LQDNPSYLNF RSERGRVLYG EDIYVGYRYY EKVDLAPLFP FGHGLSYTTF SRSDLSLATT
     PEKPQLEDGE PITVTVSVTN TGSVAGAEIV QLWVAPPPTG VNRPVRELKG FTKVFLQPGE
     TKKVEIVVEK KLATSWWDEQ REKWASEKGT YEVLVTGTGD EVLKSSFEVE KTRYWLGL