ID A0A1Y2X8G6_9PEZI Unreviewed; 769 AA.
AC A0A1Y2X8G6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=K445DRAFT_328844 {ECO:0000313|EMBL:OTB17767.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB17767.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB17767.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB17767.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KZ112932; OTB17767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2X8G6; -.
DR STRING; 1001832.A0A1Y2X8G6; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000243732; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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:SF5; BETA-GLUCOSIDASE M-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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OTB17767.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000243732};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..769
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013254676"
FT DOMAIN 692..758
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 769 AA; 83220 MW; 542B61A224EAE7D1 CRC64;
MLSPLLAALF TSSLVASAPF DPAGNYAQSP PVFPSPPGKG AGRWADAYDS ARDLVSQMTL
EEKVNITRGF TVHDNVCAGN TGTIPRLDWP GMCLHDAGNG VRATDLVNSY PSAIHAGASW
DKNLTYQRAY YIGYEFKAKG VNIVLGPNAG PLGRTPLGGR NWEGFSVDPY LSGQLNAETI
MGHQDAGVIA NIKHFIANEQ ETYRRPYFGV EAVSANIDDK TLHELYLWPF MDGIRAGVAS
VMCSYNRINN TYGCENSKLM NGILKTELAF DGFVLLDWNA QHNLESANAG LDMLMPGGGF
WGNNLTEAVR NGSVSEDRVT DMATRILAAW YHVGQDGSNF PVPGIGMKNL TLPHEQVDAR
TPDANPVILE GAIAGHVLVK NNGALPFKEC PTMLSVYGYD ATVPATKNTD ILFQLGYTSS
EEMGQAVLGT ERHFDQAAKG GTIVTGGRAG ANGPAYIDDP LSAIQQRAKD DGTWVNWDLT
SPNPDVNAAS DACLVFINAI ATEGWDRDGL HDDFSDGLVL NVASKCSNTI VVIHAAGIRL
VDQWIEHPNV TATIIAHLPG QDSGEALVKL FYGEAEFSGK LPYTLARNES DYAVYAPCGR
GPSNRTDPQC DFTEGVYVDY RHFDENNITP RYEFGYGLSY TTFNYSALAI EPLDITPERQ
GSSTPSNDEA LWDIVATVNA TIINAGEVSG AEVAQLYVGI PNSPPKQLRG FEKVPLAPGE
SAEVTFELTR RDLSIWDVVT QGWVIQAGQY ELYVGASSRD IRLMGTIDV
//
