BGLF_ASPFC
ID BGLF_ASPFC Reviewed; 869 AA.
AC B0Y7Q8;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 52.
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=AFUB_074660;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP49439.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS499599; EDP49439.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B0Y7Q8; -.
DR SMR; B0Y7Q8; -.
DR VEuPathDB; FungiDB:AFUB_074660; -.
DR PhylomeDB; B0Y7Q8; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000001699; 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..869
FT /note="Probable beta-glucosidase F"
FT /id="PRO_0000394109"
FT REGION 677..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 728
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 869 AA; 93060 MW; 31B560B5A3F5F87D CRC64;
MRVLSAIALV ASLASSALSA PASESRVSTQ LRSRDAEGYS SPPYYPAPNG GWLSSWADAY
EKAQRVVRDM TLAEKVNLTT GTGIFMGPCV GQTGSALRFG IPNLCLQDSP LGVRNSDHNT
AFPAGITVGA TFDKDLMYAR GVELGKEFRG KGINVLLGPS VGPIGRKPRG GRNWEGFGAD
PSLQAIGGAQ TIKGIQSQGV IATIKHYIGN EQEMYRMSNV GQRAYSSNID DRTLHEVYLW
PFAEGIRAGV GAVMTAYNEV NSSACSQNSK LLNEILKDEL GFQGFVMTDW LGQYGGVSSA
LAGLDMAMPG DGAIPLLGTA YWGSELSRSI LNGSVPVSRL NDMVTRIVAA WYKMGQDGDF
PLPNFSSNTQ DATGPLYPGA LFSPSGVVNQ YVNVQADHNI TARAIARDAI TLLKNDDNIL
PLKKDDALKV FGTDAGPNPD GLNSCADMGC NKGVLTMGWG SGTSRLPYLV TPQEAIANIS
SNAAFFITDK FPSNVAVSSG DVAVVFISAD SGENYITVEG NPGDRTSAGL NAWHNGDKLV
KDAAAKFSKV VVVVHTVGPI LMEEWIDLPS VKAVLVAHLP GQEAGWSLTD VLFGDYSPSG
HLPYTIPRAE SDYPSSVGLL SQPIVQIQDT YTEGLYIDYR HFLKANITPR YPFGHGLSYT
TFSFSQPTLS VRTALDSTYP PTRPPKGPTP TYPTAIPDPS EVAWPKNFDR IWRYLYPYLD
DPASAAKNSS KTYPYPAGYT TVPKPAPRAG GAEGGNPALF DVAFAVSVTV TNTGSRPGRA
VAQLYVELPD SLGETPSRQL RQFAKTKTLA PGTSETLTME ITRKDISVWD VVVQDWKAPV
RGEGVKIWLG ESVLDMRAVC EVGGACRVI
