ID H0EC87_GLAL7 Unreviewed; 528 AA.
AC H0EC87;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN ORFNames=M7I_0020 {ECO:0000313|EMBL:EHL03830.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL03830.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHL03830.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
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.
CC {ECO:0000256|ARBA:ARBA00024983}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHL03830.1}.
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DR EMBL; AGUE01000001; EHL03830.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EC87; -.
DR HOGENOM; CLU_515843_0_0_1; -.
DR InParanoid; H0EC87; -.
DR Proteomes; UP000005446; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:SF19; BETA-GLUCOSIDASE G-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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446}.
FT DOMAIN 426..497
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 528 AA; 57191 MW; 56186154CF7AB5D0 CRC64;
MVTGQPGPCI GNIVGIPRLN FSGLCLQDGP ASLRIANYAS SFPSGVTIAS SWDKKMLYER
GLAMGREFKG KGAHVALAPV AGPLGRSAYC GLNWEGFSPD PYLTGIAMQE SVLGLQDAGV
QATAKHFILN EQEILRNAFS FPNGSVQYEA ISSNVDDRTL REITEGPINQ DIFEFGTLAV
GGGSGAAQFS YLISPLQAIK ERALETGAIV EAWLNNTYVS QVTETAITGA GGILLANTPD
VCLVFLKGWA SEGVDRETLD LDWSANEVVE AVAGACNNTV VITHSSGIND LPWADHPNVT
AILVAHYPGQ ESGNSIVDVL YGDVNPSGHL PYTIAFNGSD YNSPVVTSIN TTGSDDWQSY
FTERLEIDYR FLTPKILMFA MNLADGQITS HAEELETQPG GNPALWEVIY TANVVVYNTG
DVRGNVVPQL YVSFPSSTPA GTPLRQLRGF EKVELTSGQR ASVDFELMRR DLSYWDINSQ
QWLIPEGEFT LHVGLSSRDL HGSTIAGRIE RAQRLLLLDE TMKVRNFV
//
