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Database: UniProt
Entry: E3RV08_PYRTT
LinkDB: E3RV08_PYRTT
Original site: E3RV08_PYRTT 
ID   E3RV08_PYRTT            Unreviewed;       331 AA.
AC   E3RV08;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Beta-xylosidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PTT_12980 {ECO:0000313|EMBL:EFQ90448.1};
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:EFQ90448.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ90448.1,
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; GL535228; EFQ90448.1; -; Genomic_DNA.
DR   RefSeq; XP_003301463.1; XM_003301415.1.
DR   AlphaFoldDB; E3RV08; -.
DR   EnsemblFungi; EFQ90448; EFQ90448; PTT_12980.
DR   KEGG; pte:PTT_12980; -.
DR   eggNOG; ENOG502QTYK; Eukaryota.
DR   HOGENOM; CLU_009397_4_1_1; -.
DR   OrthoDB; 1849815at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT   SITE            138
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   331 AA;  37160 MW;  7EC672643CE58D74 CRC64;
     MSVAVYDPPV INTFHQCDPA AHVWKHDPNT VYVYGSHDWN STRVPPVQYD MKDYYVLIQV
     DINKPAKVGS KILDLPDIPW AEQQLWAPDA TEKNGKYYLY FPAKDKDGVF RIGVAKSDKP
     DGKFKAEPSY IPGAYSIDPA ILADDDGCYY MYFGGLWGGQ LQAWPNNTLN TSAFGNISPS
     SGPALGPRFA KLSANMTHLA TEPKELVIYD EDGQVMQANS KRRYFEGPSV NKVGNLYYLQ
     YSTGTSHTIE IAVGKKPDGP FYWKSTLLQP VKGWTTHQSI VKFKGDWLLY YADASLSGRD
     DLRNTKVRKL NFQNGTFVLA QPQPDTPFPS F
//
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