BGLK_ASPFC
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 25-MAY-2022, entry version 64.
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 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: 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 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; 3.20.20.300; -; 2.
DR Gene3D; 3.40.50.1700; -; 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 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; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 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
