ID   BGLI_ASPTN              Reviewed;         839 AA.
AC   Q0CAF5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=ATEG_09329;
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; CH476607; EAU30466.1; -; Genomic_DNA.
DR   RefSeq; XP_001217951.1; XM_001217950.1.
DR   AlphaFoldDB; Q0CAF5; -.
DR   SMR; Q0CAF5; -.
DR   STRING; 341663.Q0CAF5; -.
DR   EnsemblFungi; EAU30466; EAU30466; ATEG_09329.
DR   GeneID; 4353962; -.
DR   VEuPathDB; FungiDB:ATEG_09329; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OMA; GPTINTQ; -.
DR   OrthoDB; 175854at2759; -.
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; 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..839
FT                   /note="Probable beta-glucosidase I"
FT                   /id="PRO_0000394889"
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"
SQ   SEQUENCE   839 AA;  91689 MW;  C8380485BAA0EFDE CRC64;
     MTRLDVEKTI EELTLGEKVA LTAGIDFWHT ASVPRLNIPT LRMSDGPNGV RGTRFFNGVP
     AACFPCATAL GATWDTELLH ECGRLMGEES IAKGSHIILG PTINTQRSPL GGRGFESFAE
     DGVLSGNLAG YMSKGIQEKG VAATLKHFVC NDQEHERLAV DSIVTMRAMR EIYLMPFQLA
     MRICPTACVM TAYNKVNGTH VSENKQIITD ILRKEWGWDG LVMSDWFGTY STSEAINAGL
     DLEMPGKTRW RSTPLAHAVS SNKVAEFVMD ERVRNVLNLV NFVEPLGIPE NCPEKALNRP
     QDQALLRRAA AESIVLMKND DNILPLKKDK PILVIGPNAK IAAYCGGGSA SLDPYYTVTP
     FEGVSAKSTG AVTFSQGVYS HKQLPELGPL MKSADGKKGF SFRVYKEPVS APSRELVDEL
     HLVSSSGFLM DYVHPKIDSL TFYVDMEGYF TPEEDGVYDF GVTVVGTGKL LIDGETVVDN
     TKNQRPGSAF FGTATVEEQG SKELKAGQTY KVVLEFGTAP TSDLDTRGVV VFGPGGFRFG
     ASRRVSQEEL IAKAADAAAQ AEQVVIFAGL TSEWETEGHD RDHMDLPPGS DEMIQRVLAA
     NPNTAVVIQS GTPVTMPWAA QTKALVQAWF GGNECGNGIA DVLYGDVNPA GKLPLSFPVR
     LQDNPSYLNF RSERGRVLYG EDVYVGYRYY EKVNLAPLFP FGHGLSYTTF ERSDLTLATV
     PEKPQYETAG EPITASVTVT NTGPVAGAEV VQLWVRPPPT GVNRPVRELK GFAKVMLNPG
     EQKRVDIVVE KKLATSWWDE QREMWASEKG QYEVQVTGTG ADVLTSSFAV EKTRFWLGL