BGLA_ASPNC
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 25-MAY-2022, entry version 77.
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 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; 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 PaxDb; A2RAL4; -.
DR EnsemblFungi; CAK48740; CAK48740; An18g03570.
DR GeneID; 4989921; -.
DR KEGG; ang:ANI_1_456164; -.
DR VEuPathDB; FungiDB:An18g03570; -.
DR HOGENOM; CLU_004542_2_0_1; -.
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:0044275; P:cellular carbohydrate catabolic process; IDA:AspGD.
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 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.
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
