ID   BGLD_ASPOR              Reviewed;         752 AA.
AC   Q2UNR0;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-MAY-2023, entry version 76.
DE   RecName: Full=Probable beta-glucosidase D;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase D;
DE   AltName: Full=Cellobiase D;
DE   AltName: Full=Gentiobiase D;
DE   Flags: Precursor;
GN   Name=bglD; ORFNames=AO090001000266;
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; AP007154; BAE56805.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UNR0; -.
DR   SMR; Q2UNR0; -.
DR   STRING; 510516.Q2UNR0; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; Q2UNR0; 12 sites, No reported glycans.
DR   EnsemblFungi; BAE56805; BAE56805; AO090001000266.
DR   VEuPathDB; FungiDB:AO090001000266; -.
DR   HOGENOM; CLU_004542_2_1_1; -.
DR   OMA; WVLNDTY; -.
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; 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:SF14; BETA-GLUCOSIDASE D-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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..752
FT                   /note="Probable beta-glucosidase D"
FT                   /id="PRO_0000394107"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
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        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        532
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        571
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        586
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        638
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        661
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        743
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   752 AA;  80223 MW;  1EFC3981368AF2B6 CRC64;
     MRFVSLAVGA ALLGAAGASS ISSNVGLLKA NGVALGNWEA AYEKASAFVS GLTTDQKLAL
     ITGSNVESAN GNFTPLYFLD GDMGLQDFYY VSAFSLSSAL AMTWDRDAIY EQAKAVGSEF
     YNKGVQVVAG PTSQPLGRTP WGGRGVEGFG PDPYLNGLAT GLTTKGYVDA GVIPGGKHFL
     LYEQETNRTS SFGSSGEGSP YSSNADDKTI HETYLWPFYD AVKNGAGAVM CAMTKVNGTM
     ACENSDLLMK MLKTELGFPG MVWPDMNGQN SAKGSALGGE DYGSSSIWST STMESFLSNG
     TLSEARLNDM AIRNLIGYYY VNLDNGRQPT RQTTDVYVDV RANHSKLIRE NGAKSMALLK
     NEGVLPLSKP HVMSIFGAHA GPIMGGPNSN VDVMGSGPTY QGHLATGSGS GMASMPYLIT
     PYDALTNKAA QDGTVLRWVL NDTYSSGGGS SLVPSSTSST AVEPSFENFA TGSDICLVFI
     NALAGEGADR TELYNADQDA MVNTVADNCN NTVAVVNTVG PRLLDQWIEH DNVTAVLYGS
     LLGQESGNSI VDLLYGDVNP SGRLVHTIAK NESDYNVGLC YTAQCNFTEG VYLDYRYFDA
     HNITPRYPFG HGLSYTTFHY SSLAIKAPSS ITKAPKGNLT VGGPSDLWDV VGTVSARIAN
     NGTLSGAEVP QLYLGFPDSA DQPVRQLRGF DRVELSAGQE AVVTFNLRRR DISYWNLKTQ
     QWMVAGGKYT VFVGGSSRDL RLNGTFFLWV GS
//