ID E3S0T1_PYRTT Unreviewed; 817 AA.
AC E3S0T1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=PTT_15710 {ECO:0000313|EMBL:EFQ88412.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ88412.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ88412.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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}.
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DR EMBL; GL536389; EFQ88412.1; -; Genomic_DNA.
DR RefSeq; XP_003303486.1; XM_003303438.1.
DR AlphaFoldDB; E3S0T1; -.
DR STRING; 861557.E3S0T1; -.
DR EnsemblFungi; EFQ88412; EFQ88412; PTT_15710.
DR KEGG; pte:PTT_15710; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_3_1; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000001067; 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:UP000001067};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..817
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003179598"
FT DOMAIN 733..804
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 817 AA; 87961 MW; 530F1B994F18E453 CRC64;
MAPSVLSAVL SGSTLLAAVN AQNFAGSGRG DDAFTYVQPL NTTILNEYGS SPPVYPSPNI
TGAGGWEMGL EKAKAFVAQL TLEEKADMVT GQAGPCVGNI VAIPRLGFPG LCLQDGPLAI
RVADYASVFS AGVSAGATWD KKIMYERGHA MGEEFRAKGA QIMLGPVAGP LGRSAYAGRN
WEGFSSDPYL SGIAMEETII GAQDAGVQAC AKHWIGNEQE IQRNPTYSTG VDNTQHTSAA
LSSNIDDRTM HELYMWPFAN AVKARAASFM CSYQRINGSY GCQNSKTQNG LLKTELGFQG
YVMSDWGATH TGVAAIEAGL DMNMPGGLGA YGVNFGLTSF FGGNVTAASK NGSLEMSRID
DMVIRIMTPY FQLGQDKDFP SIDPSSGGLN TFSPPSTWTR EYNFTGETSR DVRGNHAELI
RRHGAAGTVL LKNVESALPL KAPRNVAVFG NDASEPARSS VINQKDYEYG SLFAGGGSGT
GQFTYMISPL RALQDRVTAD GGIVQSFLNN THIITNNVST LVIPRRQPDV CIVMLKTWAE
EGADRAHLAS DWDGDDVVAS VAAFCNNTVV VTHSAGINTL AWSDHPNVTA IVAAHFPGQE
SGNSLVDILY GHVNPSGHLP YTIAMDGNDY NAPPTTNINT TGFYDWQSWF DEKLEIDYRH
FDMHNISVRY EFGFGLSYTT FDIKDITAEA CASDITSMPE QLPIQPGGNP ALWETVYNVT
VTVSNTGSVA GAAVPQLYVG LPSSAPAGTP VRQLRGFEKV YLEKGESQSV SFELMRRDLS
YWDIVSQQWV IPEGEFTVWV GHSSRDLKVM KSFTVVQ
//
