ID BGLC_ASPOR Reviewed; 638 AA. AC Q2UFP8; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 72. DE RecName: Full=Probable beta-glucosidase C; DE EC=3.2.1.21; DE AltName: Full=Beta-D-glucoside glucohydrolase C; DE AltName: Full=Cellobiase C; DE AltName: Full=Gentiobiase C; DE Flags: Precursor; GN Name=bglC; ORFNames=AO090026000123; 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 -!- SEQUENCE CAUTION: CC Sequence=BAE59617.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AP007159; BAE59617.1; ALT_INIT; Genomic_DNA. DR AlphaFoldDB; Q2UFP8; -. DR SMR; Q2UFP8; -. DR STRING; 510516.Q2UFP8; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR GlyCosmos; Q2UFP8; 9 sites, No reported glycans. DR EnsemblFungi; BAE59617; BAE59617; AO090026000123. DR OrthoDB; 2657687at2759; -. DR UniPathway; UPA00696; -. DR Proteomes; UP000006564; Chromosome 3. 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 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 PANTHER; PTHR30620:SF120; BETA-GLUCOSIDASE C; 1. DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1. DR Pfam; PF00933; Glyco_hydro_3; 1. DR Pfam; PF01915; Glyco_hydro_3_C; 1. DR PRINTS; PR00133; GLHYDRLASE3. 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; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..638 FT /note="Probable beta-glucosidase C" FT /id="PRO_0000394104" FT ACT_SITE 341 FT /evidence="ECO:0000250" FT CARBOHYD 40 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 116 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 223 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 274 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 364 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 480 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 488 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 528 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 638 AA; 70451 MW; F070472F086BA6F1 CRC64; MKVLAPGYLA EASLTALASG CQALSTRPYV PRGYSLSRRN DSTPIYKDAS YCIDERVDDL LARMTIEEKA GQLFHTRLMD GPLDDEGSGN NAHNSTSNMI GEKHMTHFNL ASDITNATET AEFINRIQEL ALQTRLGIPV TVSTDPRHSF TENVGTGFKA GVFSQWPESI GLAALRDPYV VRKFAEVAKE EYIAVGIRAA LHPQVDLSTE PRWARISNTW GENSTLTSEL LVEYIKGFQG DKLGPQSVKT VTKHFPGGGP VENGEDSHFA YGKNQTYPGN NLEEHLKPFK AAIAAGATEI MPYYSRPIGT EYEPVAFSFN KRIVTELLRN ELGFDGIVLT DWGLITDGYI AGQYMPARAW GVENLTELQR AARILDAGCD QFGGEERPEL IVQLVQEGII SEDRIDVSVR RLLKEKFVLG LFDNPFVDAE AAGRVVGNDY FVRLGREAQR RSYTLLSNNE DIVPLKKIEK STKFYIEGFN ASFIESWNYT VVDSPEEAEY ALLRYNAPYE PRPGGFEANM HAGSLAFNDT EKARQAKIYS AVPTIVDIVM DRPAVIPEII EQAKAVFASY GSDSNAFLDV VFGVSAPEGK LPFDLPSSME AVEAQMEDVP FDTRNPVFKF GHGLSYANPC ASSSSKCS //