ID   BGLD_ASPNC              Reviewed;         754 AA.
AC   A2QPK4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   13-SEP-2023, entry version 71.
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=An07g09760;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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=CAK39741.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM270153; CAK39741.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A2QPK4; -.
DR   SMR; A2QPK4; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; A2QPK4; 13 sites, No reported glycans.
DR   EnsemblFungi; CAK39741; CAK39741; An07g09760.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006706; Chromosome 4L.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..754
FT                   /note="Probable beta-glucosidase D"
FT                   /id="PRO_5000220231"
FT   REGION          186..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        573
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        588
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        655
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        745
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   754 AA;  80738 MW;  6D106BFA5464A759 CRC64;
     MKVLSFIVAA ALLGLTGASS NSSPGLLKSD GVVLGDWESA YQKASSFVAG LTTDQKLALI
     TGSSVNSTNG SFSGLTFLDG DMGLQNFFYV SAFSLSSALA MTWDRDAIYA QAKAVGSEFY
     NKGIQVVAGP TSQPLGRTPW GGRIVEGFGP DPYLNGLASG LTAKGYIDAG VIPGAKHFLL
     YEQETNRTGG GGGGGGDSGS APYSSNADDK TLHETYLWPF YDAVKHGLGA VMCAMTKVNG
     TLSCQNSDLL MKHLKTELGF PGLVWPDTNG QSSALESAVN GEDYGSSSIW STSTMETLLS
     NGSLSEARLD DMAVRNLMGY YYVNLDNGLQ PEEQSEDAYV DVRGNHSKLI RENGAKSMAL
     LKNKNALPLR KPRVMSVFGA HAGPVLGGPN TAMDIEGSGP TYQGHLATGT GSAQASLPYL
     VPPYVALTNR IIEDGTMMRW VLNDTYSSSS TSGLITEGTD STAVDPSFAD YATNSDACLV
     FLNALSGEGA DRTELYNDDQ DTMVNTVADN CNNTIVIINT VGPRLMDQWI EHDNVTAVLY
     GSLLGQESGN SIVDILYGDV NPSGRLIHTI AKNESDYNVK ICYTAQCNFT EGVYLDYRYF
     DAHNVTPRYP FGHGLSYTTF SYSDLNIEKP STLSKYPTGE KAVGGNSDLW DIVGNVSVKV
     ANTGSLDGAE VPQLYLGFPT AAQQPVRQLR GFERVEIASG KQSQVTFQLR RRDISYWDVP
     AQQWLVASGD YKVYVGASSR DLKLNGTFTV QTSS
//