ID G0X2F9_9EURO Unreviewed; 860 AA.
AC G0X2F9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN Name=bgl {ECO:0000313|EMBL:AEL79685.1};
OS Aspergillus saccharolyticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=979771 {ECO:0000313|EMBL:AEL79685.1};
RN [1] {ECO:0000313|EMBL:AEL79685.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22906186; DOI=10.1139/w2012-076;
RA Sorensen A., Ahring B.K., Lubeck M., Ubhayasekera W., Bruno K.S.,
RA Culley D.E., Lubeck P.S.;
RT "Identifying and characterizing the most significant beta-glucosidase of
RT the novel species Aspergillus saccharolyticus.";
RL Can. J. Microbiol. 58:1035-1046(2012).
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 Evidence={ECO:0000256|ARBA:ARBA00000448,
CC ECO:0000256|RuleBase:RU361161};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; HM853555; AEL79685.1; -; Genomic_DNA.
DR AlphaFoldDB; G0X2F9; -.
DR UniPathway; UPA00696; -.
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:SF12; BETA-GLUCOSIDASE A-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 {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361161};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361161}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..860
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003411410"
FT DOMAIN 779..847
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 860 AA; 93168 MW; 28793193E0C4E09F CRC64;
MRLSWLEAAA LTAASVVSAD ELAFASPFYP SPWANGQGEW ADAYKRAVDI VSQMTLDEKV
NLTTGTGWEL EKCVGQTGGV PRLDIGGMCL QDSPLGVRDS DYNSGFPAGV NVAATWDRKL
AYLRGQAMGQ EFSDKGVDVQ LGPAAGPLGR SPDGGRNWEG FSPDPALTGV LFAETIKGIQ
DAGVIATAKH YILNEQEHFR QVSEAAGYGF NISDTISSNI DDKTIHEMYL WPFADAVRAG
VGAVMCSYNQ INNSYACQNS YTLNKLLKSE LGFQGFVMSD WGAHHSGVGS ALAGLDMSMP
GDVSFDSATS FWGTNLTVAV LNGTVPQWRV DDMAVRIMAA YYKVGRDRLY QPPNFSSWTR
DEYGFKYYYS QEGPYEKVNQ YVNVQRNHSE VIRKVGADST VLLKNNNALP LTGKERKVAL
IGEDAGSNAY GANGCSDRGC DNGTLAMAWG SGTAEFPYLV TPEQAIQAEV LKNKGSTYTI
TDNWALSQVE ALAKTASVSL VFVNADSGEG YISVDGNEGD RNNLTLWKNG DNLIKATASN
CNNTIVVIHS VGAVLVDEWY DHPNVTAILW AGLPGQESGN SLADVLYGRV NPGGKTPFTW
GKTRASYGDY LVREPNNGHG APQDNFSEGV FIDYRGFDKR NETPIYEFGH GLSYTTFNYS
GLQVEVLNTS SSTPVATQTK PAPTFGEIGN ASDYLYPEGL DRITAFIYPW LNSTDLKESS
GDPDYGVDTA KYIPAGATNS SAQPVLPAGG GFGGNPRLYD ELIRVSVTVK NTGRVTGDAV
PQLYVSLGGP NEPKVVLRQF DRITLRPSEE TVWTTTLTRR DLSNWDVAAQ DWVITSYPKK
VHVGSSSRQL PLHAALPKVQ
//
