ID S3DHT4_GLAL2 Unreviewed; 839 AA.
AC S3DHT4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=GLAREA_02050 {ECO:0000313|EMBL:EPE26138.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE26138.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE26138.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE145371; EPE26138.1; -; Genomic_DNA.
DR RefSeq; XP_008087457.1; XM_008089266.1.
DR AlphaFoldDB; S3DHT4; -.
DR STRING; 1116229.S3DHT4; -.
DR GeneID; 19461108; -.
DR KEGG; glz:GLAREA_02050; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; DMTMAGD; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..839
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004508197"
FT DOMAIN 761..829
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 711..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 90224 MW; 3DEAED4AF2831D55 CRC64;
MLWSSSLASI VVLAASASAQ LDGAQSPPSY PSPWMRGGNG WQDAYAKAQA FVSQLTLLEK
VNLTTGVGWE GEACVGNTGS IPRLGFRGFC LQDSPLGIRF ADQASAFPSG MNVAATWTTR
LFKSRGRAMG DEHRGKGIDV QLGPVAGPLG RVPAGGRNWE GFSPDPVLTG VAIGETIKGI
QDGGVIANAK HYIMNEQEHN REPSGSFAAY SANVDDKTMH ETYLWPFADA VHAGVASIMC
SYNQINNSYG SQNSYTLNYL LKNELDFQGF VVSDWWAQHT GVASALAGLD MTMAGDQGLA
SGNTYWGGNL TAAAINGTLP QWRLDDMVTR IMAAYYKVGR DTARVDVNFN SWSSETYGYI
HPQANEGYQQ INYHVNVQSD HAKLIREIGG ASTVMLKNVN NALPLKKPKS VAVIGEDAHD
NPGGPNACGD RGCNTGTLAM GWGSGTANFP YLIAPVTALR AQAAKDRTLF ANVSNNYDLD
AAAKAASNAS VAIVFANADS GEAYITVDGN SGDRNNLTLW GNGDALIKKV ASVNPNTIVV
LHTVGAVIVE DLKNNPNVTA ILWAGLPGQE SGNAITDIIY GYRNPSAKSV FTWGKKREDW
GVDVIYTPTS NPPQLNFNEG NFIDYRYFDA NNIEPSYEFG FGLSYTNYSY SNLQISKNDP
GPYQPTVGMT KAAPTLGTID KDPAHAEFPT GFRAVFKYIY PYLTGPVLTN QPESWPAKSQ
DGSPQPRVGA GGSAGGNRQL WDVMYTVSCT VTNTGGVKGT EIPQLYLSLG APTDPKIVLR
GFDDLILDPG ESNTFTYKLT RRDISNWDPV TQNWVISPYP KTVYVGASSR DLKLKGVLP
//
