ID   BGLI_ASPNC              Reviewed;         818 AA.
AC   A2R989;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Probable beta-glucosidase I;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase I;
DE   AltName: Full=Cellobiase I;
DE   AltName: Full=Gentiobiase I;
GN   Name=bglI; ORFNames=An17g00520;
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; AM270384; CAK97412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2R989; -.
DR   SMR; A2R989; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; A2R989; 3 sites, No reported glycans.
DR   EnsemblFungi; CAK97412; CAK97412; An17g00520.
DR   VEuPathDB; FungiDB:An17g00520; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006706; Chromosome 5L.
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; 2.60.120.260; Galactose-binding domain-like; 1.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted.
FT   CHAIN           1..818
FT                   /note="Probable beta-glucosidase I"
FT                   /id="PRO_0000394887"
FT   DOMAIN          374..534
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   818 AA;  90051 MW;  BC1BC84183EB5F30 CRC64;
     MARVDFWHTA SIPRLNIPAL RMSDGPNGVR GTRFFNGIPA ACFPCATALG ATWDAHLLHE
     VGQLMGDESI AKGSHIVLGP TINIQRSPLG GRGFESFAED GVLSGILAGN YCKGLQEKGV
     AATLKHFVCN DQEHERLAVS SIVTMRALRE IYLLPFQLAM RICPTACVMT AYNKVNGTHV
     SENKELITDI LRKEWNWDGL VMSDWFGTYT TSDAINAGLD LEMPGKTRWR GSALAHAVSS
     NKVAEFVLDD RVRNILNLVN WVEPLGIPEH APEKALNRPQ DRDLLRRAAA ESVVLMKNED
     NILPLRKDKP ILVIGPNAQI AAYCGGGSAS LDPYYTVSPF EGVTAKATSE VQFSQGVYSH
     KELPLLGPLL KTQDGKPGFT FRVYNEPPSH KDRTLVDELH LLRSSGFLMD YINPKIHSFT
     FFVDMEGYFT PTESGVYDFG VTVVGTGRLL IDNETVVDNT KNQRQGTAFF GNATVEERGS
     KHLNAGQTYK VVLEFGSAPT SDLDTRGIVV FGPGGFRFGA ARQVSQEELI SNAVSQASQA
     SQVIIFAGLT SEWETEGNDR EHMDLPPGTD EMISRVLDAN PDNTVVCLQS GTPVTMPWVH
     KAKALVHAWF GGNECGNGIA DVLFGDVNPS AKLPVTFPVR LQDNPSYLNF RSERGRVLYG
     EDVYVGYRYY EKTNVKPLYP FGHGLSYTTF SRSDLKITTS PEKSTLTDGE PITATVQVKN
     TGTVAGAEIV QLWVLPPKTE VNRPVRELKG FTKVFLQPGE EKQVEIVVEK KLATSWWDEQ
     RGKWASEKGT YGVSVTGTGE EELSGEFGVE RTRYWVGL
//