ID   BGLG_ASPOR              Reviewed;         815 AA.
AC   Q2U325;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   22-FEB-2023, entry version 83.
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=AO090038000223;
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; AP007169; BAE64040.1; -; Genomic_DNA.
DR   RefSeq; XP_001825173.1; XM_001825121.1.
DR   AlphaFoldDB; Q2U325; -.
DR   SMR; Q2U325; -.
DR   STRING; 510516.Q2U325; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; Q2U325; 13 sites, No reported glycans.
DR   EnsemblFungi; BAE64040; BAE64040; AO090038000223.
DR   GeneID; 5997268; -.
DR   KEGG; aor:AO090038000223; -.
DR   VEuPathDB; FungiDB:AO090038000223; -.
DR   HOGENOM; CLU_004542_2_3_1; -.
DR   OMA; YERGYAM; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006564; Chromosome 6.
DR   GO; GO:0005615; C:extracellular space; IDA:AspGD.
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:0005975; P:carbohydrate metabolic process; IDA:AspGD.
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; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..815
FT                   /note="Probable beta-glucosidase G"
FT                   /id="PRO_0000394117"
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
//