ID BGLG_ASPFN Reviewed; 815 AA. AC B8NMR5; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 24-JAN-2024, entry version 72. DE RecName: Full=Probable beta-glucosidase G; DE EC=3.2.1.21; DE AltName: Full=Beta-D-glucoside glucohydrolase G; DE AltName: Full=Cellobiase G; DE AltName: Full=Gentiobiase G; DE Flags: Precursor; GN Name=bglG; ORFNames=AFLA_126780; OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 OS / JCM 12722 / SRRC 167). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=332952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / RC SRRC 167; RX PubMed=25883274; DOI=10.1128/genomea.00168-15; RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E., RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.; RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes RT aflatoxin contamination of food and feed."; RL Genome Announc. 3:E0016815-E0016815(2015). 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; EQ963481; EED48455.1; -; Genomic_DNA. DR RefSeq; XP_002381871.1; XM_002381830.1. DR AlphaFoldDB; B8NMR5; -. DR SMR; B8NMR5; -. DR STRING; 332952.B8NMR5; -. DR GlyCosmos; B8NMR5; 13 sites, No reported glycans. DR EnsemblFungi; EED48455; EED48455; AFLA_126780. DR VEuPathDB; FungiDB:AFLA_012483; -. DR eggNOG; ENOG502QR4D; Eukaryota. DR HOGENOM; CLU_004542_2_3_1; -. DR OMA; YERGYAM; -. DR OrthoDB; 5486783at2759; -. DR UniPathway; UPA00696; -. DR Proteomes; UP000001875; 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; 3.40.50.1700; 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; 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:SF19; BETA-GLUCOSIDASE G-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. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..815 FT /note="Probable beta-glucosidase G" FT /id="PRO_0000394116" FT ACT_SITE 304 FT /evidence="ECO:0000250" FT CARBOHYD 40 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 58 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 229 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 276 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 343 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 350 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 402 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 507 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 563 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 584 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 623 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 662 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 715 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 815 AA; 87701 MW; FFC65DE64FB45457 CRC64; MASIAHLVVS GLLAATAVNG QNYGGSGRSD DAFSYVQPRN TTILGQYGHS PAVLPSPNAT GAGGWEEALA KAQQFVAQLT LEEKADMVTG QPGPCVGNIV AIPRLGFKGL CLQDGPLAIR VADYASVFSA GVTAASTWDK DILYERGVAM GEEFKGKGAH VALGPVAGPL GRSGYGGRNW EGFAADPYLT GVAMERTIQG YQDAGVQACA KHFIGNEQET QRNPNYNPNG TLTDVIQEAI SSNIDDRTIH ELYLWPFANA ARAKVASVMC SYQRLNGSYA CQNSKVLNGL LKEELGFQGY VQSDWGGTHS GVSSIEGGLD MNMPGGLGQY GQTPEAGSFF GKNVTFAVNN GTVDISRVDD MIVRIMTPYY WLGQDQGYPE IDPSSADLNT FSPRSTWLRE FNLTGERSRD VRGDHGELIR RHGAEATILL KNENKALPLK APKSIAVFGN DAGDTTEGAV NKATFEFGTL AAGGGSGTGR FTYLVTPLEA LKARGKQDNT LVQWWLNNTL IADSDVTSLW VPTPPDACLV FLKTWAEEGS DREYLSVDWN GNEVVDSVAS KCNNTIVVTH SSGINELPFA NHPNVTAIVA AHYPGQESGN SIVDILYGDV NPSGKLPYTI AKNGSDYNAP PTTAVETTGA DDWQAWFDEK LEIDYRYFDA HNISVLYEFG FGLSYTTFSL SDIKTEPLAE SISSVPEQLP IQPGGNPALW ESVYNVSVTV TNTGDVKGAT VPQLYVTFPD SAPAGTPPKQ LRGFDKVSLA PGESQTVGFE LMRRDLSYWD VVSQEWLIPE GEFTIRVGFS SRDLSQETKI TPVTA //