ID   BGLJ_ASPFC              Reviewed;         865 AA.
AC   B0Y8M8;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Probable beta-glucosidase J;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase J;
DE   AltName: Full=Cellobiase J;
DE   AltName: Full=Gentiobiase J;
GN   Name=bglJ; ORFNames=AFUB_077900;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDP49759.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS499599; EDP49759.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; B0Y8M8; -.
DR   SMR; B0Y8M8; -.
DR   PhylomeDB; B0Y8M8; -.
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; 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; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted.
FT   CHAIN           1..865
FT                   /note="Probable beta-glucosidase J"
FT                   /id="PRO_0000394892"
FT   DOMAIN          411..579
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        764
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   865 AA;  93022 MW;  2F9E9C76E9BDAA20 CRC64;
     MGSIDTVGMG QRAIDQIISE LSLNEKVALL SGVDAWHTFA IPRLGIPSIR TTDGPNGARG
     TRYFNGVPSA CLPCGTALGA TFDRDLIFSL GQLLAAECRA KGAHVLLGPT INIQRGPLGG
     RGFESFSEDP VLSGLAAASY CSGVQDGGVV PTLKHLVCND QEHERVAVSA LVTPRALREI
     YLLPFQLAIQ GARPGAVMTS YNKVNGLHAS ENPGLIRDIL RGEWGYEGAV ISDWFGTYSV
     ADAVNAGLDL EMPGPTRFRG PALMHALTSN KVSEKTLNER VRKVLELVQL ASRAGVPEYA
     PERKLNRPED RALLRRAAGE SVVLLKNDKN DSTNSPILPL DREKTTLVIG PNADLAAYCG
     GGSASLLAYY TVTPRQGIAD KCGAEQVVFS QGCYGHKELP LLGEHLRTIE TGQPGYTFRV
     YTEPPPASGS FKGSDSRTPV DELHMTNSSA FLMDYSHPQI SGDTYYATLE GTFEPPESGV
     YEFGLTVAGT GLLYIDGVLV VDNKTVQRAG TSFFGIGTVE ERGERYLEAG KKHHVFVEFG
     TAPTSNLQHH HGVVSFGPGG LRLGGCRKLD TDTAIQQAVQ SAAQADQVVV CVGLSGDWES
     EGFDRPHMDL PPGTEELVNA VLAVQPNAVI VVQSGTPVTM PWADKAKALL QAWYGGNEAG
     NGIADVLFGD VNPSAKLPLT FPRELSQNPS YLSYRSERGR VLYSEDIYVG YRYYDTTGQP
     PLFRFGHGLS YSTFHLRDLT VRETAPYAAN IKESSLRVSV TVSNTSARPG AEVVLVYVRP
     PAAACSVGRP VRELKGYEKV MLQPGETREV SITIPLGLAT SFWDEGCDAW LSEKGLYFVE
     AVGTGEGNTL VAPLTVQVSR VWNGL