BGLF_NEOFI
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 25-MAY-2022, entry version 75.
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 / NRRL 181
RC / 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; 36630.CADNFIAP00004621; -.
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; WHNGDKL; -.
DR OrthoDB; 559385at2759; -.
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; 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..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
