BGLF_ASPFN
ID BGLF_ASPFN Reviewed; 866 AA.
AC B8NP65;
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 F;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase F;
DE AltName: Full=Cellobiase F;
DE AltName: Full=Gentiobiase F;
DE Flags: Precursor;
GN Name=bglF; ORFNames=AFLA_128480;
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; EQ963481; EED48625.1; -; Genomic_DNA.
DR RefSeq; XP_002382041.1; XM_002382000.1.
DR AlphaFoldDB; B8NP65; -.
DR SMR; B8NP65; -.
DR STRING; 5059.CADAFLAP00009906; -.
DR EnsemblFungi; EED48625; EED48625; AFLA_128480.
DR VEuPathDB; FungiDB:AFLA_128480; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; WHNGDKL; -.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..866
FT /note="Probable beta-glucosidase F"
FT /id="PRO_0000394110"
FT REGION 725..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
FT /evidence="ECO:0000250"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 866 AA; 93066 MW; 02697819B5DDB341 CRC64;
MAAFPAYLAL LSYLVPGALS HPEAKTLTSR ASTEAYSPPY YPAPNGGWIS EWASAYEKAH
RVVSNMTLAE KVNLTSGTGI YMGPCAGQTG SVPRFGIPNL CLHDSPLGVR NSDHNTAFPA
GITVGATFDK DLMYERGVGL GEEARGKGIN VLLGPSVGPI GRKPRGGRNW EGFGADPSLQ
AFGGSLTIKG MQSTGAIASL KHLIGNEQEQ HRMSSVITQG YSSNIDDRTL HELYLWPFAE
SVRAGAGSVM IAYNDVNRSA CSQNSKLING ILKDELGFQG FVVTDWLAHI GGVSSALAGL
DMSMPGDGAI PLLGTSYWSW ELSRSVLNGS VPVERLNDMV TRIVATWYKM GQDKDYPLPN
FSSNTEDETG PLYPGALFSP SGIVNQYVNV QGNHNVTARA IARDAITLLK NNDNVLPLKR
NNTLKIFGTD AGTNSDGINS CTDKGCNKGV LTMGWGSGTS RLPYLITPQE AIANISSNAG
FHITDTFPSG VTAGPDDIAI VFINSDSGEN YITVDGNPGD RTLAGLHAWH NGDNLVKAAA
EKFSNVVVVV HTVGPILMEE WIDLDSVKAV LVAHLPGQEA GWSLTDILFG DYSPSGHLPY
TIPHSESDYP ESVGLIAQPF GQIQDDYTEG LYIDYRHFLK ANITPRYPFG HGLSYTTFNF
TEPNLSIIKA LDTAYPAARP PKGSTPTYPT AKPDASEVAW PKNFNRIWRY LYPYLDNPEG
AAANSSKTYP YPDGYTTEPK PAPRAGGAEG GNPALWDVTF SVQVKVTNTG SRDGRAVAQL
YVELPSSLGL DTPSRQLRQF EKTKILAAGE SEVLTLDVTR KDLSVWDVVV QDWKAPVNGE
GVKIWVGESV ADLRVGCVVG EGCSTL
