ID   BGLE_ASPFC              Reviewed;        1033 AA.
AC   B0YD91;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Probable beta-glucosidase E;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase E;
DE   AltName: Full=Cellobiase E;
DE   AltName: Full=Gentiobiase E;
GN   Name=bglE; ORFNames=AFUB_094720;
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: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; DS499602; EDP47625.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YD91; -.
DR   SMR; B0YD91; -.
DR   EnsemblFungi; EDP47625; EDP47625; AFUB_094720.
DR   VEuPathDB; FungiDB:AFUB_094720; -.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   PhylomeDB; B0YD91; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Cellulose degradation;
KW   Glycoprotein; Glycosidase; Hydrolase; Membrane; Polysaccharide degradation;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1033
FT                   /note="Probable beta-glucosidase E"
FT                   /id="PRO_0000394871"
FT   TOPO_DOM        1..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..1033
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        593
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        909
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        918
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        976
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1033 AA;  113423 MW;  68768F797E72DE92 CRC64;
     MAPPDSTHGG SFRDHLKTND RSSTSKGKQR YSPLQEAIPE EISSFRSPSE YADTDSDSDL
     ERSGSYKLRP VDRYGSHHSS AFIPVIREEN GVETYLDSIT EAEQELLSAS KQYDLVDDDD
     SSDFDSDEEA TLRYRLKDRL KRRRARLQAW QPVKYARIWW RTLLAVVVTL VVVVWGFLSF
     AVSHREEPTV WPMVPSDSWF PSPKGGTLKH WEESYKKAQS LVRNMTLVEK VNITTGIGWQ
     MGLCVGNTGP ADIVKFPSLC LQDGPQGLRF ADHVSAFPAG ITTGSTWNRE LMRERGVAMG
     REARLKGVNV LLGPSMGPLG MMPAGGRNWE GFGSDPVLQA VAAAETIRGI QSNGVMATAK
     HFVMNEQEHF RQPFEWGIPT ALSSNVGDRA LHEVFAWPFA ESIRADVASV MCSYQMVNNS
     HACENSKLLN GILKDELGFQ GFVQSDWLAQ RSGINSALGG LDMSMPGDGL HWVDGKSLWG
     SELTRAVLNT SVPVERLNDM VTRIVAAWYH LGQDTWERPP PEGNGGPNFS SWTNDEVGWL
     HTGSNDGSYA RVNHYVDAQG TGPEAHSIIA RKVAAEGTVL LKNVDRTLPL SRNASSPSGG
     ILRVGIYGDD AGPALGPNAC PDRGCNQGTL ATGWGSGTVE FPYLVSPIEA LESAWSTEIE
     STAYLRNAVM PADAVDKDLC LVFVNADSGE GYISAGGIHG DRNDLFLQKG GDTLVRTVSS
     NCGGGQGKTV VVIHAVGPVV MESWIDLPGV HAVLLANLPG QESGNALVDV LFGEVDASGR
     LPYTIGKSLE DYGPGAQVLY EPNAPVPQVD FLDALYIDYR HFDRHNITPR FEFGFGLSYT
     TFELLDLSIS PLQQKSRSVP PRPADAVAPP VYDISLPDPA SALFPAGFQP VFKYIYPYLS
     NLDGTAPHNY SFYPKGYNET QRPSPAGGGA GGHPALYEEM VSVKLQVSNT GDRKGQEVVQ
     VYVSFPPDFP ERVLRNFTKI ELEPSERREV QMTLSRKDLS YWSTREQNWV MPEGKFQIWV
     GRSSRDLPLM GEY