ID   BGLI_ASPCL              Reviewed;         838 AA.
AC   A1CA51;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=ACLA_010450;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027049; EAW12619.1; -; Genomic_DNA.
DR   RefSeq; XP_001274045.1; XM_001274044.1.
DR   AlphaFoldDB; A1CA51; -.
DR   SMR; A1CA51; -.
DR   STRING; 344612.A1CA51; -.
DR   GlyCosmos; A1CA51; 3 sites, No reported glycans.
DR   EnsemblFungi; EAW12619; EAW12619; ACLA_010450.
DR   GeneID; 4706951; -.
DR   KEGG; act:ACLA_010450; -.
DR   VEuPathDB; FungiDB:ACLA_010450; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OMA; TYYVDME; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006701; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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; 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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 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_0000394883"
FT   DOMAIN          395..555
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  92243 MW;  C7AE89A3507382F3 CRC64;
     MVQFDVEKTL EELTLGEKVA LTAGTDFWHT AAVPRLNIPS LRMSDGPNGV RGTRFFNGTR
     AACFPCSTAL GATWDTELLY EVGRLMAEES IAKGSHIILG PTINTQRSPL GGRGFESFAE
     DGVLSGLLAG NYCKGLQDKG VAATLKHFVC NDQEHERLAV DSIVTMRAMR EIYLMPFHLA
     MRLCKTACVM TAYNKINGTH VSENKQIITD ILRKEWGWDG LVMSDWFGTY STSDAINAGL
     DLEMPGPTRW RGTALAHAVS SNKAFEYVLD ERVRNVLNLH NFVEPLGIPE NAPEEALNRP
     EDQALLRRAA AESVVLMKNE DNILPLKKEK SILVIGPNAK TAAYCGGGSA SLDAYYTVAP
     FDGVKAKSEG EVSFSQGVYS YNELPVLGPL LKTEEGEKGF KFRVYNEPSS NPNRELLDEL
     RLENSLGFLM DYKHPKVTSF LFYADMEGYF TPEEDGIYDF GVTVQGTGKL YIDGELVVDN
     SKNQRQGTAF FGNATVEEKG SKELKAGQTY KVVVEFGSAP TSDLDMRGVV VFGPGGFRFG
     AARRVGQEEL ISKAAELASQ ADQVVIFAGL TSEWETEGHD RDHMDLPAGS DEMISRVLDA
     NPNAVVVIQS GTPVTMPWAH KTKALLQAWF GGNECGNGIA DVLYGDVNPS AKLPLSFPVR
     LQDNPSYLNF RSERGRVLYG EDVYVGYRYY EKVDLAPLFP FGHGLSYTTF SRSDLSLATV
     PEKRQLEDGE PITATVTVTN TGDVAGAEVV QLWIVPPPTG VNRPVRELKG FAKVFLNPGE
     SKTVEIVVEK KLATSWWDEQ REKWASEKGT YKVLVTGTGD EVLKSSFEVE KTRFWLGL
//