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
//
