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 27-MAR-2024, entry version 70.
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 GlyCosmos; Q0CI67; 10 sites, No reported glycans.
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; PAPYGGW; -.
DR OrthoDB; 5486783at2759; -.
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; 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..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
//
