BGLD_ASPOR
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 25-MAY-2022, entry version 73.
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 EnsemblFungi; BAE56805; BAE56805; AO090001000266.
DR VEuPathDB; FungiDB:AO090001000266; -.
DR HOGENOM; CLU_004542_2_1_1; -.
DR OMA; IWSTSTM; -.
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; 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..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
