ID   BGLF_NEOFI              Reviewed;         869 AA.
AC   A1DMR8;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=NFIA_054350;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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}.
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DR   EMBL; DS027698; EAW16089.1; -; Genomic_DNA.
DR   RefSeq; XP_001257986.1; XM_001257985.1.
DR   AlphaFoldDB; A1DMR8; -.
DR   SMR; A1DMR8; -.
DR   STRING; 331117.A1DMR8; -.
DR   GlyCosmos; A1DMR8; 9 sites, No reported glycans.
DR   EnsemblFungi; EAW16089; EAW16089; NFIA_054350.
DR   GeneID; 4584501; -.
DR   KEGG; nfi:NFIA_054350; -.
DR   VEuPathDB; FungiDB:NFIA_054350; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OMA; PAPYGGW; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006702; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 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..869
FT                   /note="Probable beta-glucosidase F"
FT                   /id="PRO_0000394115"
FT   REGION          678..698
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        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        425
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;  93105 MW;  27CA34C3DABB498D CRC64;
     MRVLSAIALV ASLVPSALSA PASESRVSTQ LQSRDAAGYS SPPYYPAPNG GWLSSWADAY
     EKAQRVVRNM TLAEKVNLTT GTGIFMGPCV GQTGSALRFG IPNLCLQDSP LGVRNSDHNT
     AFPAGITVGA TFDKDLMYAR GVELGEEFRG KGINVFLGPS VGPIGRKPRG GRNWEGFGAD
     PSLQAIGGAQ TIKGIQSRGV IATIKHYIGN EQEMYRMSNI GQRAYSSNID DRTLHELYLW
     PFAEGIRAGV GAVMTAYNEV NSSACSQNSK LLNEILKDEL GFQGFVMTDW LGQYGGVSSA
     LAGLDMAMPG DGAIPLLGNA YWGSELSHSI LNGSVPVSRL NDMVTRIVAT WYKMGQDGDF
     PLPNFSSNTQ DATGPLYPGA LFSPSGVVNQ YVNVQADHNI TARAIARDAI TLLKNDDNIL
     PLKRNDSLKV FGTDAGPNPD GLNSCADMGC NKGVLTMGWG SGTSRLPYLV TPQEAIANIS
     SNAAFFITDN FPSNVAVSSG DVAVVFISAD SGENYITVEG NPGDRTSAGL NAWHNGDKLV
     KDAAAKFSKV VVVVHTVGPI LMEEWIDLPS VKAVLVAHLP GQEAGWSLTD VLFGDYSPSG
     HLPYTIPRAE SDYPSSVGLL SQPIVQIQDT HTEGLYIDYR HFLKSSITPR YPFGHGLSYT
     TFSFSQPTLS VRTALDSAYP PTRPPKGPTP TYPTTIPNPS EVAWPKNFDR IWRYLYPYLD
     DPAGAAKNSS KTYPYPAGYT TVPKPAPRAG GAEGGNPALF DVAFAVSVTV TNTGTRPGRA
     VAQLYVELPD SLGETPSRQL RQFAKTKTLA PGASETLTME FTRKDISVWD VVVQDWKAPV
     RGEGVKIWLG ESVLDMRAVC EVGGACRVI
//