ID G2R744_THETT Unreviewed; 777 AA.
AC G2R744;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=THITE_2118136 {ECO:0000313|EMBL:AEO68568.1};
OS Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia
OS terrestris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides;
OC Thermothielavioides terrestris.
OX NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO68568.1, ECO:0000313|Proteomes:UP000008181};
RN [1] {ECO:0000313|EMBL:AEO68568.1, ECO:0000313|Proteomes:UP000008181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; CP003011; AEO68568.1; -; Genomic_DNA.
DR RefSeq; XP_003654904.1; XM_003654856.1.
DR AlphaFoldDB; G2R744; -.
DR STRING; 578455.G2R744; -.
DR GeneID; 11518998; -.
DR KEGG; ttt:THITE_2118136; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_1_1; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000008181; Chromosome 3.
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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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:AEO68568.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000008181};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..777
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003436250"
FT DOMAIN 696..765
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 777 AA; 83826 MW; 4675E87440AAA1E0 CRC64;
MRFLLSVPLL AAAALAADQG RPSLKNAVFK NPKAPVEARV ADLLSRMTIE EKTSQLLQGD
IRNWMNDTTG AFNQTGLAWS TQYRGGSFYV GVAVPNEWIS EQIKNAQDYI QNSTYLGIPA
FVQTEGIHGF LVFNATIFNS PIGQACSWNP ELVEEMAIAI GKEARAMGVN QLFAPLADLA
RELRHGRVEE MYGEDGFLAG ELARAYVKGV QSTGVSAMVK HFAAFGVTEQ GLNTGPVHGG
ERERRTTFLP SYKKAIIDGG AFAIMTAYHC YDGIPAVADA HLLTDILRDE WGYKYFTMTD
AGASDRLCND FKMCASNPID KAAIVQYILP AGGDTEMGGG SYSFEQIPAL VSSGKLDQKL
VDTAVSRVLR AKFELGLFEN PFPGLPSSQW NTTIHTAEHV ALAKKLDEES IVLLENHNKV
LPLRKNASVA VIGPMAHGFM NYGDYVIANS STRGVTPLDG IQAVSTGKVT YAKGCERWST
SQDGFPEAVA AAEAADVAVV VVGTWSRDQN ELWEGLNATT GEHVDVDNLD LVGAQEPLVR
AIVATGKPTV VVFSSGKPIT APWISENAAA LVQQFYPSEQ GGAALASVLF GDVNPSGKLA
VSFPRSVGDL PVYYDHLNSG RDAFPDAGVA YENGTLVFGH QYVLGNPTPL YEFGYGLSYS
TFVYSDVAAD KHTVSAEDTV TISVTVKNVS DRDGKEVVQL YVKDLIASVV VPNIQLKGFQ
KVSLKAGESK RVSIKVSMQD LGVWDVRMKY VVEPGDFLFI VGASSSDFRG NVTVTLK
//
