ID B2WML4_PYRTR Unreviewed; 817 AA.
AC B2WML4;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=PTRG_11224 {ECO:0000313|EMBL:EDU44274.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU44274.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231630; EDU44274.1; -; Genomic_DNA.
DR RefSeq; XP_001941555.1; XM_001941520.1.
DR AlphaFoldDB; B2WML4; -.
DR STRING; 426418.B2WML4; -.
DR EnsemblFungi; EDU44274; EDU44274; PTRG_11224.
DR GeneID; 6349537; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_3_1; -.
DR InParanoid; B2WML4; -.
DR OMA; YERGYAM; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000001471; 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:UP000001471};
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_5002782960"
FT DOMAIN 733..804
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 817 AA; 88152 MW; C9D268BF8D30C9DE CRC64;
MAPSVLSAVL SGSALLAAVN AQNFAGGDRA EDAFVYYQPL NTTILTEYGS SPPVYPSPKI
TGAGGWEMGL EKAKAFVAQL TLEEKADMVT GQAGPCVGNI VAIPRLGFPG LCLQDGPLAI
RVADYASVFS AGVSAGATWD KKIMYERGHA MGEEFRAKGS QIMLGPVAGP LGRSAYAGRN
WEGFSSDPYL SGIAMEETIH GAQDAGVQAC AKHWIGNEQE IQRNPSYSTG VDKTAHSAAA
LSSNIDDRTM HELYMWPFAN AVKARAASFM CSYQRINGSY GCQNSKSQNG LLKTELGFQG
YVMSDWGATH TGVAAIEAGL DMNMPGGLGA YGQGFGFTSY FGGNVTAAAK NGSLEMSRID
DMVIRIMTPY FQLGQDKDFP SIDPSTGDLN TFSPPSTWTR EYNLTGEASR DVRGNHGELI
RRHGAAGTVL LKNVDHALPL KTPRNVAVFG NDASEPVRSS VINQQNYEYG TLFAGGGSGT
GQFTYMKSPL RAIQDRVTAD GGIVQSFLNN THIATNNVST LVIPKRQPDV CIVMLKTWAE
EGNDRAHLGS DWDGDKVVTS VAAFCNNTVV VTHSAGINTL NWSDHPNITA IVAAHFPGQE
SGNSLVDILY GHVNPSGHLP YTIAMNGNDY NAPPTTNINT TGFYDWQSWF DEKLEIDYRH
FDMHNISVRY EFGFGLSYTT FDIKDISAEA SASDITSMPE QLPIQPGGNP ALWETLYNVT
VTVSNTGDVA GAAVPQLYVG LPSSAPAGTP VRQLRGFEKV YLEKGESQSV SFELMRRDLS
YWDIVSQQWV IPEGEFTVWV GHSSRDLKVT KSFTVVQ
//
