ID   BGLA_ASPNC              Reviewed;         860 AA.
AC   A2RAL4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Probable beta-glucosidase A;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase A;
DE   AltName: Full=Cellobiase A;
DE   AltName: Full=Gentiobiase A;
DE   Flags: Precursor;
GN   Name=bglA; Synonyms=bgl1; ORFNames=An18g03570;
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}.
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DR   EMBL; AM270402; CAK48740.1; -; Genomic_DNA.
DR   RefSeq; XP_001398816.1; XM_001398779.2.
DR   AlphaFoldDB; A2RAL4; -.
DR   SMR; A2RAL4; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; A2RAL4; 14 sites, No reported glycans.
DR   EnsemblFungi; CAK48740; CAK48740; An18g03570.
DR   GeneID; 4989921; -.
DR   KEGG; ang:An18g03570; -.
DR   VEuPathDB; FungiDB:An18g03570; -.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006706; Chromosome 8L.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015926; F:glucosidase activity; IDA:AspGD.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic 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; IPR019800; Glyco_hydro_3_AS.
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:SF12; BETA-GLUCOSIDASE A-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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..860
FT                   /note="Probable beta-glucosidase A"
FT                   /id="PRO_5000221323"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        442
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        690
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        712
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   860 AA;  93229 MW;  087215D2E1F89643 CRC64;
     MRFTSIEAVA LTAVSLASAD ELAYSPPYYP SPWANGQGDW AEAYQRAVDI VSQMTLAEKV
     NLTTGTGWEL ELCVGQTGGV PRLGIPGMCA QDSPLGVRDS DYNSAFPAGV NVAATWDKNL
     AYLRGQAMGQ EFSDKGADIQ LGPAAGPLGR SPDGGRNWEG FSPDPALSGV LFAETIKGIQ
     DAGVVATAKH YIAYEQEHFR QAPEAQGYGF NITESGSANL DDKTMHELYL WPFADAIRAG
     AGAVMCSYNQ INNSYGCQNS YTLNKLLKAE LGFQGFVMSD WAAHHAGVSG ALAGLDMSMP
     GDVDYDSGTS YWGTNLTISV LNGTVPQWRV DDMAVRIMAA YYKVGRDRLW TPPNFSSWTR
     DEYGFKYYYV SEGPYEKVNQ FVNVQRNHSE LIRRIGADST VLLKNDGALP LTGKERLVAL
     IGEDAGSNPY GANGCSDRGC DNGTLAMGWG SGTANFPYLV TPEQAISNEV LKNKNGVFTA
     TDNWAIDQIE ALAKTASVSL VFVNADSGEG YINVDGNLGD RRNLTLWRNG DNVIKAAASN
     CNNTIVIIHS VGPVLVNEWY DNPNVTAILW GGLPGQESGN SLADVLYGRV NPGAKSPFTW
     GKTREAYQDY LYTEPNNGNG APQEDFVEGV FIDYRGFDKR NETPIYEFGY GLSYTTFNYS
     NLQVEVLSAP AYEPASGETE AAPTFGEVGN ASDYLYPDGL QRITKFIYPW LNSTDLEASS
     GDASYGQDAS DYLPEGATDG SAQPILPAGG GAGGNPRLYD ELIRVSVTIK NTGKVAGDEV
     PQLYVSLGGP NEPKIVLRQF ERITLQPSKE TQWSTTLTRR DLANWNVETQ DWEITSYPKM
     VFAGSSSRKL PLRASLPTVH
//