BGLG_ASPOR
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 25-MAY-2022, entry version 81.
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}.
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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 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 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; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 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 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; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 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
