ID   XYN5_MAGO7              Reviewed;         405 AA.
AC   G4MLU0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Endo-1,4-beta-xylanase 5;
DE            Short=Xylanase 5;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 5;
DE   Flags: Precursor;
GN   Name=XYL5; ORFNames=MGG_05464;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}. Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; CM001231; EHA57718.1; -; Genomic_DNA.
DR   RefSeq; XP_003710330.1; XM_003710282.1.
DR   AlphaFoldDB; G4MLU0; -.
DR   SMR; G4MLU0; -.
DR   STRING; 318829.MGG_05464T0; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblFungi; MGG_05464T0; MGG_05464T0; MGG_05464.
DR   GeneID; 2675881; -.
DR   KEGG; mgr:MGG_05464; -.
DR   VEuPathDB; FungiDB:MGG_05464; -.
DR   eggNOG; ENOG502QR4K; Eukaryota.
DR   HOGENOM; CLU_020161_12_1_1; -.
DR   InParanoid; G4MLU0; -.
DR   OMA; DSDSWIP; -.
DR   OrthoDB; 829814at2759; -.
DR   UniPathway; UPA00114; -.
DR   PHI-base; PHI:2208; -.
DR   Proteomes; UP000009058; Chromosome 1.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Disulfide bond; Glycoprotein;
KW   Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..380
FT                   /note="Endo-1,4-beta-xylanase 5"
FT                   /id="PRO_0000429625"
FT   PROPEP          381..405
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429626"
FT   DOMAIN          32..352
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        166
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        273
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   LIPID           380
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        302..308
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  43247 MW;  3B41DEFAB55501EC CRC64;
     MTRLATLITL AGLLAVSPGA YAQRNRNDTG GSTGAEGLNS LAVKAGLLYF GTASDTRNFA
     DEPYMSVVNN TNEFGMIVPE NSMKWEATEK EPGRFSFANA DRVRALTKAN GQMLRCHALT
     WHSQLPNFVK TTAWTRDTLT AAIESHISNE VGHFAGDCYA WDVVNEAVNE NGSFRDSPFH
     RTLGTDFLAI SFRAAAAADP NAKLYYNDFN IETPGPKANA AMGIVRLLKE QGVRIDGVGF
     QGHLTVGSTP SRAQLASQLQ RFADLGVEVT YTELDIRHKS LPVSSRAAQD QARDYVSVIG
     SCLDVTACVG VMVWQPTDKY SWIPETFPGT GDACLFDANM NPKPAYTSVS SLLAAAAATA
     PASVVPPASV TTSKTPIQAG AGRETVSIAG LTLALSSLAF GMFML