ID BGLF_ASPOR Reviewed; 866 AA. AC Q2UN12; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=Probable beta-glucosidase F; DE EC=3.2.1.21; DE AltName: Full=Beta-D-glucoside glucohydrolase F; DE AltName: Full=Cellobiase F; DE AltName: Full=Gentiobiase F; DE Flags: Precursor; GN Name=bglF; ORFNames=AO090001000544; OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=510516; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42149 / RIB 40; RX PubMed=16372010; DOI=10.1038/nature04300; RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E., RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., RA Kikuchi H.; RT "Genome sequencing and analysis of Aspergillus oryzae."; RL Nature 438:1157-1161(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP007154; BAE57053.1; -; Genomic_DNA. DR RefSeq; XP_001819055.1; XM_001819003.1. DR AlphaFoldDB; Q2UN12; -. DR SMR; Q2UN12; -. DR STRING; 510516.Q2UN12; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR GlyCosmos; Q2UN12; 11 sites, No reported glycans. DR EnsemblFungi; BAE57053; BAE57053; AO090001000544. DR GeneID; 5991026; -. DR KEGG; aor:AO090001000544; -. DR VEuPathDB; FungiDB:AO090001000544; -. DR HOGENOM; CLU_004542_2_0_1; -. DR OMA; PAPYGGW; -. DR OrthoDB; 5486783at2759; -. DR UniPathway; UPA00696; -. DR Proteomes; UP000006564; Chromosome 2. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008422; F:beta-glucosidase activity; IDA:AspGD. 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; 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; IPR013783; Ig-like_fold. DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1. DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-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. DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..866 FT /note="Probable beta-glucosidase F" FT /id="PRO_0000394112" FT REGION 725..748 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 285 FT /evidence="ECO:0000250" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 73 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 257 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 328 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 360 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 395 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 421 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 474 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 659 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 664 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 724 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 866 AA; 93179 MW; 6E2148424219EA32 CRC64; MAAFPAYLAL LSYLVPGALS HPEAKTLTSR ASTEAYSPPY YPAPNGGWIS EWASAYEKAH RVVSNMTLAE KVNLTSGTGI YMGPCAGQTG SVPRFGIPNL CLHDSPLGVR NSDHNTAFPA GITVGATFDK DLMYERGVGL GEEARGKGIN VLLGPSVGPI GRKPRGGRNW EGFGADPSLQ AFGGSLTIKG MQSTGAIASL KHLIGNEQEQ HRMSSVITQG YSSNIDDRTL HELYLWPFAE SVRAGAGSVM IAYNDVNRSA CSQNSKLING ILKDELGFQG FVVTDWLAHI GGVSSALAGL DMSMPGDGAI PLLGTSYWSW ELSRSVLNGS VPVERLNDMV TRIVATWYKM GQDKDYPLPN FSSNTEDETG PLYPGALFSP SGIVNQYVNV QGNHNVTARA IARDAITLLK NNENVLPLKR NDTLKIFGTD AGTNSDGINS CTDKGCNKGV LTMGWGSGTS RLPYLITPQE AIANISSNAE FHITDTFPLG VTAGPDDIAI VFINSDSGEN YITVDGNPGD RTLAGLHAWH NGDNLVKAAA EKFSNVVVVV HTVGPILMEE WIDLDSVKAV LVAHLPGQEA GWSLTDILFG DYSPSGHLPY TIPHSESDYP ESVGLIAQPF GQIQDDYTEG LYIDYRHFLK ANITPRYPFG HGLSYTTFNF TEPNLSIIKA LDTAYPAARP PKGSTPTYPT AKPDASEVAW PKNFNRIWRY LYPYLDNPEG AAANSSKTYP YPDGYTTEPK PAPRAGGAEG GNPALWDVTF SVQVKVTNTG SRDGRAVAQL YVELPSSLGL DTPSRQLRQF EKTKILAAGE SEVLTLDVTR KDLSVWDVVV QDWKAPVNGE GVKIWVGESV ADLRVGCVVG EGCSTL //