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BGLF_ASPTN
ID   BGLF_ASPTN              Reviewed;         867 AA.
AC   Q0CI67;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=ATEG_06617;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476602; EAU33161.1; -; Genomic_DNA.
DR   RefSeq; XP_001215795.1; XM_001215795.1.
DR   AlphaFoldDB; Q0CI67; -.
DR   SMR; Q0CI67; -.
DR   STRING; 341663.Q0CI67; -.
DR   EnsemblFungi; EAU33161; EAU33161; ATEG_06617.
DR   GeneID; 4322302; -.
DR   VEuPathDB; FungiDB:ATEG_06617; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   OMA; WHNGDKL; -.
DR   OrthoDB; 559385at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000007963; 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..867
FT                   /note="Probable beta-glucosidase F"
FT                   /id="PRO_0000394113"
FT   REGION          723..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        660
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        725
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   867 AA;  93551 MW;  9018187913DC563C CRC64;
     MAPSSLKWTL LCALPWTLAS PASYNVHHAR DSDAQAFSPP YYPTPHGGWI ADWAEAYEKA
     SQLVRNMTLA EKVNLTTGTG MYMGPCAGQT GSVPRFGIPN LCMHDGPLGV RNTDHNTAFP
     PGITVGATFD KDLMRSRGVA LGEEGRGKGV NVLLGPSVGP IGRKPRGGRN WEGFGADPSL
     QAIAGSLTIE GMQSTGLIAC IKHFIANEQE MHRMSSVVTQ GYSSNVDDRT LHELYLWPFA
     EGVRAGVGSL MAAYNDVNNS ASSQNSKMLN DILKDELGFQ GFVMSDWFGN YGGVSAALAG
     LDVSMPGDGA IPLLGDSYWG SELSRSILNG TVPVDRLNDM ATRILASWYK MGQDQDYPLP
     NFSANTEDAE GPLYPGAVFS PKGVVNKFVN VQGDHNVTAR AIARDAITLL KNNNNILPLH
     RNDSLKIFGT DAGTNPDGIN SCSDKGCNKG VLTMGWGSGS SKLPYLVTPQ EAIANISSHA
     EFHITDSFPS DVSAGPNDIA IVFINSDSGE NYITVEGNPG DRTSAGLNAW HNGDDLVKAA
     AEKFRQVVVV YHTVGPVLME EWIDLEPVKA VLVAHLPGQE AGWSLTDVLF GDYSPSGHLP
     YTIPRSESDY PDSVSLIQQP FGRIQDDYTE GLYIDYRHFA KAGITPRFPF GYGLSYTNFN
     FSRASISAQS SLDTAYPAPR SPKGSTPEYS TAIPPAAEAA WPKNFNRIWR YLYPYLDNPE
     GARANSSRKY PYPDGYSTVQ KPGPRAGGGE GGNPALFDVA FSVQVQVTNT GARKGRAVAQ
     LYVELPDSLG VDTPSRQLRQ FEKTKILAPG ESQVLTMEIT RKDLSVWDVV AQDWKAPVNG
     EGVKMWIGES VADMRVLCTV GEGCSTL
 
 
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