ID   BGLI_NEOFI              Reviewed;         838 AA.
AC   A1DFA8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=NFIA_080070;
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; DS027696; EAW18065.1; -; Genomic_DNA.
DR   RefSeq; XP_001259962.1; XM_001259961.1.
DR   AlphaFoldDB; A1DFA8; -.
DR   SMR; A1DFA8; -.
DR   STRING; 36630.CADNFIAP00006674; -.
DR   EnsemblFungi; EAW18065; EAW18065; NFIA_080070.
DR   GeneID; 4586518; -.
DR   KEGG; nfi:NFIA_080070; -.
DR   VEuPathDB; FungiDB:NFIA_080070; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OMA; GPTINTQ; -.
DR   OrthoDB; 175854at2759; -.
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; 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; Reference proteome; Secreted.
FT   CHAIN           1..838
FT                   /note="Probable beta-glucosidase I"
FT                   /id="PRO_0000394891"
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;  91973 MW;  4023757A8C6017FF CRC64;
     MVQLDVEKTI EELTLGEKVA LTAGIDFWHT AAVPRLNIPS LRLSDGPNGV RGTRFFNGVP
     AACFPCATAL GATWDTKLLH EVGRLMGEES IAKGTHVVLG PTINIQRSPL GGRGFESFAE
     DGVLSGILAG HYCKGLQETG VAATLKHFVC NDQEHERLAV DSIVTMRAMR EIYLLPFQLA
     MRICKTACVM TAYNKINGTH VSENKQIITD ILRKEWGWDG LVMSDWFGTY STSDAINAGL
     DLEMPGPTRW RGTALAHAVS SNKAFEFVVD ERVRNILNLH NFVEPLGIPE NAPEKALNRP
     EDQALLRRAA AESVVLMKNQ DNILPLKKEK PILVIGPNAK TAAYCGGGSA SLDAYYTVTP
     FEGVSAQSQG EVKFSQGVYS YKELPLLGPL LKTDDGKKGF KFRVYNEPPS EPNRQLIDEL
     HLESSSGFLM DYKHPKIKTF TFYVDMEGYF TPEEDGIYDF GVTVVGTGKL FVDDELVVDN
     SKNQRQGTAM FGNATVEEKG SKELKAGQTY KVVLQFGTAP TSDLDMRGVV IFGPGGFRFG
     AARRVSQEEL ISKAAELASQ ASQVVIFAGL TSEWETEGHD RDHMDLPPGS DEMISRVLDA
     NPNAVVVIQS GTPVTMPWAH KAKALLQAWF GGNECGNGIA DVLYGAVNPA AKLPLSFPVR
     LQDNPSYLNF RSERGRVLYG EDVYVGYRYY EKVDLAPLFP FGHGLSYTTF SRSDLSLATT
     PEKPQLEDGE PITATVSVTN TGSVAGAEIV QLWVAPPPTG VNRPVRELKG FAKVFLQPGE
     TKKVEIVVEK KLATSWWDEQ REKWASEKGT YEVLVTGTGD EVLKTSFEVG KTRYWLGL