ID   BGLK_ASPFC              Reviewed;         766 AA.
AC   B0YBJ3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-MAY-2023, entry version 67.
DE   RecName: Full=Probable beta-glucosidase K;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase K;
DE   AltName: Full=Cellobiase K;
DE   AltName: Full=Gentiobiase K;
GN   Name=bglK; ORFNames=AFUB_086800;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
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=CBS 144.89 / FGSC A1163 / CEA10;
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; DS499601; EDP47974.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YBJ3; -.
DR   SMR; B0YBJ3; -.
DR   GlyCosmos; B0YBJ3; 4 sites, No reported glycans.
DR   EnsemblFungi; EDP47974; EDP47974; AFUB_086800.
DR   VEuPathDB; FungiDB:AFUB_086800; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   PhylomeDB; B0YBJ3; -.
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; 2.60.120.260; 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; 2.
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; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF13; BETA-GLUCOSIDASE K-RELATED; 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; 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; Secreted.
FT   CHAIN           1..766
FT                   /note="Probable beta-glucosidase K"
FT                   /id="PRO_0000394896"
FT   DOMAIN          369..528
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   REGION          726..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        748
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   766 AA;  83471 MW;  ED55686E32079CB7 CRC64;
     MGEICPRRED FDIDYILKNA SLLEKVSLLA GYDFWHTAPL PRFNVPSVRV SDGPNGVRGT
     KFFDGVRAAC LPCGTGLAAT WDQSLLYDAG VLIGQDVYPT AAYIRGAQST GVISTIKHFA
     ANDQEHERIS VNAVMSERAL REVHLLPFQI AIADSAPGAV MTCYNKVNGQ HLSESKEMLD
     GLLRREWGWK GLIMSDWFGT YSTAEALNAG LDLEMPGPTR LRGPLLELAI SSRKVSRATL
     DERARTVLEF VQRARKAEVS AVESTRDFPE DRRLNRKLAA DSIVLLKNES GLLPLNPQTL
     TSVALIGPNM KTAAFCGGGS ASLQPYYSTS PYQGITSQLP PGVEVLYETG ATSYAFIPEL
     AASEVRTPEG QPGLGMRFYR DPPSVQERRV VEETIIQESS WQLMGFSNPE LDRLFHADIE
     AELIAPATGP FQFGLAVYGS ASLFLDDQLI IDNTTVQRGG TFFFGKGTLE ETATVDLVQG
     QSYQIKVQFA SGPSSKLVKP GVVNFGGGAG RLGMVQVVDP ERAIARAVEA AKRADITILG
     VGLTRDHESE GFDRSHMDLP PAVASLVTAV LDVAPDAILL TQSGTPFSML PWADLVKTHL
     HAWFGGNELG NGIADVLFGV VNPSGKLPLS FPRRIEDTPT YLNFGSERGQ VTYGEGIYVG
     YKLLRKSPTS CALSIRVRSA PVHPCCFRSN SLLTRFVPQA RFVVHLLCVL RFDGRHRVRY
     TECSKLGRRG RSGSSPAVYR GRSNNVVNRT SHQGAQRISK GGFAAR
//