ID   BGLK_ASPFU              Reviewed;         767 AA.
AC   Q4WA69;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 97.
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=AFUA_7G00240;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000015; EAL84867.1; -; Genomic_DNA.
DR   RefSeq; XP_746905.1; XM_741812.1.
DR   AlphaFoldDB; Q4WA69; -.
DR   SMR; Q4WA69; -.
DR   STRING; 330879.Q4WA69; -.
DR   GlyCosmos; Q4WA69; 4 sites, No reported glycans.
DR   EnsemblFungi; EAL84867; EAL84867; AFUA_7G00240.
DR   GeneID; 3504260; -.
DR   KEGG; afm:AFUA_7G00240; -.
DR   VEuPathDB; FungiDB:Afu7g00240; -.
DR   eggNOG; ENOG502SMPY; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   InParanoid; Q4WA69; -.
DR   OMA; CWSSERG; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
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   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; Reference proteome; Secreted.
FT   CHAIN           1..767
FT                   /note="Probable beta-glucosidase K"
FT                   /id="PRO_0000394897"
FT   DOMAIN          405..552
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   REGION          727..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        477
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        749
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   767 AA;  83358 MW;  BF4924E3FE58BC4E CRC64;
     MGEICPRRED FDIDYILKNA SLLEKVSLLA GYDFWHTAPL PRFNVPSVRV SDGPNGVRGT
     KFFDGVRAAC LPCGTGLAAT WDQSLLYDAG VLIGQECLAK GAHCWLVPTV CIQRSPLGGR
     GFESFAEDPY ATGKLAAAYI RGAQSTGVIS TIKHFAANDQ EHERISVNAV MSERALREVH
     LLPFQIAIAD SAPGAVMTCY NKVNGQHLSE SKEMLDGLLR REWGWKGLIM SDWFGTYSTA
     EALNAGLGLE MPGTTRLRGP LLELAISSRK VSRATLDERA RTVLEFVQRA RKAEVSAVES
     TRDFPEDRRL NRKLAADSIV LLKNESGLLP LNPQTLTSVA LIGPNMKTAA FCGGGSASLQ
     PYYSTSPYQG ITSQLPPGVE VLYETGATSY AFIPELEASE VRTPEGQPGL RMRFYRDPPS
     VQERRVLMGF SNPELDRLFY ADIEAELIAP ATGPFQFGLA VYGSASLFLN DQLIIDNTTV
     QRGGTFFFGK GTLEETATVD LVQGQSYQIK VQFASGPSSK LVKPGVVNFG GGAGRLGMVQ
     VVDPERAIAR AVEAAKRADI TILGVGLTRD HESEGFDRSH MDLPPAVASL VTAVLDVAPD
     AILLTQSGTP FSMLPWADLV KTHLHAWFGG NELGNGIADV LFGVVNPSGK LPLSFPRRIE
     DTPTYLNFGS ERGQVTYGEG IYVGYKLLRK SPTSCALSIR ARFVVHLLCV LRFDGRHRVR
     YTECSKLGRR GRSGSSPAVY RGRSNNVVNR TSHQGAQRIS KGGFAAR
//