ID   BGLE_NEOFI              Reviewed;        1045 AA.
AC   A1DLJ5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
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=NFIA_050080;
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 /
RC   NRRL 181 / 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: 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; DS027698; EAW15666.1; -; Genomic_DNA.
DR   RefSeq; XP_001257563.1; XM_001257562.1.
DR   AlphaFoldDB; A1DLJ5; -.
DR   SMR; A1DLJ5; -.
DR   STRING; 331117.A1DLJ5; -.
DR   GlyCosmos; A1DLJ5; 9 sites, No reported glycans.
DR   EnsemblFungi; EAW15666; EAW15666; NFIA_050080.
DR   GeneID; 4584078; -.
DR   KEGG; nfi:NFIA_050080; -.
DR   VEuPathDB; FungiDB:NFIA_050080; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OMA; VVMESWI; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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; 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; 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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF20; BETA-GLUCOSIDASE E-RELATED; 1.
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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Cellulose degradation;
KW   Glycoprotein; Glycosidase; Hydrolase; Membrane; Polysaccharide degradation;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1045
FT                   /note="Probable beta-glucosidase E"
FT                   /id="PRO_0000394875"
FT   TOPO_DOM        1..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..1045
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..74
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   ACT_SITE        430
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        577
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        893
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        902
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        988
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1045 AA;  114875 MW;  9587BF4A3DA770F8 CRC64;
     MAPPDSTHGG SFRDHLKTND RSSTSKGKQR YAPLHEAIPE EISSFRSPSE YADADTDSDS
     DHENSGSYQL RPVDRYGSHH SSAFIPVIRD DGGVETYLDS ITEAEQELLS ASKQYDLFDD
     DDSDDLDSDE EATLRYKLKD RLKRRRARLQ AWPPVKYARI WWRTLLAVIV TLAVVVWGFL
     SFAVSHREEP KVWPMVPSDS WFPSPKGGTL KHWEESYKKA QSLVRNMTLV EKVNITTGIG
     WQMGLCVGNT GLRFADHVSA FPAGITTGST WNRELMRERG VAMGREARLK GVNVLLGPSM
     GPLGMMPAGG RNWEGFGSDP VLQAVAAAET IRGIQSNGVM ATAKHFVMNE QEHFRQPFEW
     GIPTALSSNV GDRALHEVFA WPFAESIRAD VASVMCSYQM VNNSHACENS KLLNGILKDE
     LGFQGFVQSD WLAQRSGINS VLGGLDMSMP GDGLHWVDGK SLWGSELTRA VLNTSVPVER
     LNDMVTRIVA AWYHLGQDTW ERPPPEGNGG PNFSSWTNDK VGWLHTGSND GSYAVVNHYV
     DAQGTGPEAH SIIARKVAAE GTVLLKNVDR TLPLSRNASS PSGGILRVGI YGDDAGPASG
     PNACPDRGCN QGTLATGWGS GTVEFPYLVS PIEALESAWS TEIESTAYLR NAVMPADAVD
     KDLCLVFVNA DSGEGYISAG GIHGDRNDLF LQKGGDTLVR TVASNCGGGQ GKTVIVIHAV
     GPVVMESWID LPGVHAVLLS NLPGQESGNA LMDVLFGEVD ASGRLPYTIG KSLEDYGPGA
     QVLYEPNAPV PQADFLDALY IDYRHFDRYN ITPRFEFGFG LSYTTFELSD LSISPLQRKS
     RSPPPRPADA VAPPVYDTSL PDPASALFPT GFQPIFKYIY PYLSNLDGTA PRNYSFYPKG
     YNETQSPSPA GGGAGGHPAL YEEMVSVKLQ VSNTGDRKGQ EVVQLYVSFP PDVTEEGDWV
     EVDSDADKTG EKQRERMKIE FPERVLRNFT KIELEPSERR EVQMTLSRKD LSYWSTREQN
     WVMPEGKFQI WVGRSSRDLP LMGEY
//