BGLI_ASPNC
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 25-MAY-2022, entry version 76.
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 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=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
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 PaxDb; A2R989; -.
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; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 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 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; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 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
