BGLA_ASPFN
ID BGLA_ASPFN Reviewed; 861 AA.
AC B8NRX2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=AFLA_051140;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963483; EED47060.1; -; Genomic_DNA.
DR RefSeq; XP_002383240.1; XM_002383199.1.
DR AlphaFoldDB; B8NRX2; -.
DR SMR; B8NRX2; -.
DR STRING; 5059.CADAFLAP00011105; -.
DR EnsemblFungi; EED47060; EED47060; AFLA_051140.
DR VEuPathDB; FungiDB:AFLA_051140; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; EAQGYGF; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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 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; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..861
FT /note="Probable beta-glucosidase A"
FT /id="PRO_0000394094"
FT ACT_SITE 281
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
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 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 861 AA; 93415 MW; 5AD246CD78881B27 CRC64;
MKLGWIEVAA LAAASVVSAK DDLAYSPPFY PSPWADGQGE WAEVYKRAVD IVSQMTLTEK
VNLTTGTGWQ LERCVGQTGS VPRLNIPSLC LQDSPLGIRF SDYNSAFPAG VNVAATWDKT
LAYLRGQAMG EEFSDKGIDV QLGPAAGPLG AHPDGGRNWE GFSPDPALTG VLFAETIRGI
QDAGVIATAK HYIMNEQEHF RQQPEAAGYG FNVSDSLSSN VDDKTMHELY LWPFADAVRA
GVGAVMCSYN QINNSYGCEN SETLNKLLKA ELGFQGFVMS DWTAHHSGVG AALAGLDMSM
PGDVTFDSGT SFWGANLTVG VLNGTIPQWR VDDMAVRIMA AYYKVGRDTK YTPPNFSSWT
RDEYGFAHNH VSEGAYERVN EFVDVQRDHA DLIRRIGAQS TVLLKNKGAL PLSRKEKLVA
LLGEDAGSNS WGANGCDDRG CDNGTLAMAW GSGTANFPYL VTPEQAIQNE VLQGRGNVFA
VTDSWALDKI AAAARQASVS LVFVNSDSGE GYLSVDGNEG DRNNITLWKN GDNVVKTAAE
NCNNTVVIIH SVGPVLIDEW YDHPNVTGIL WAGLPGQESG NSIADVLYGR VNPGAKSPFT
WGKTRESYGS PLVKDANNGN GAPQSDFTQG VFIDYRHFDK FNETPIYEFG YGLSYTTFEL
SDLHVQPLNA SRYTPTSGMT EAAKNFGEIG DASEYVYPEG LERIHEFIYP WINSTDLKAS
SDDSNYGWED SKYIPEGATD GSAQPLLPAS GGAGGNPGLY EDLFRVSVKV KNTGNVAGDE
VPQLYVSLGG PNEPKVVLRK FERIHLAPSQ EAVWTTTLTR RDLANWDVSA QDWTVTPYPK
TIYVGNSSRK LPLQASLPKA Q
