ID   XYN1_MAGO7              Reviewed;         233 AA.
AC   P0CT49; A4QZG4; G4N2U4; P55335; Q01171;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Endo-1,4-beta-xylanase 1;
DE            Short=Xylanase 1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   AltName: Full=Xylanase 22;
DE   Flags: Precursor;
GN   Name=XYL1; Synonyms=XYN22; ORFNames=MGG_07955;
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. Accounts for approximately 70 percent of the
CC       endoxylanase activity in the culture filtrate (By similarity).
CC       {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: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; CM001233; EHA53393.1; -; Genomic_DNA.
DR   RefSeq; XP_003713200.1; XM_003713152.1.
DR   AlphaFoldDB; P0CT49; -.
DR   SMR; P0CT49; -.
DR   STRING; 318829.MGG_07955T0; -.
DR   EnsemblFungi; MGG_07955T0; MGG_07955T0; MGG_07955.
DR   GeneID; 2683882; -.
DR   KEGG; mgr:MGG_07955; -.
DR   VEuPathDB; FungiDB:MGG_07955; -.
DR   eggNOG; ENOG502RXA7; Eukaryota.
DR   HOGENOM; CLU_052631_0_0_1; -.
DR   OMA; VENHGEY; -.
DR   OrthoDB; 1306131at2759; -.
DR   UniPathway; UPA00114; -.
DR   PHI-base; PHI:2213; -.
DR   Proteomes; UP000009058; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; 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   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..233
FT                   /note="Endo-1,4-beta-xylanase 1"
FT                   /id="PRO_0000008008"
FT   DOMAIN          40..230
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        217
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   233 AA;  25491 MW;  400963836F581F98 CRC64;
     MVSFTSIVTA VVALAGSALA IPAPDGNMTG FPFEQLMRRQ STPSSTGRHN GYYYSWWTDG
     ASPVQYQNGN GGSYSVQWQS GGNFVGGKGW MPGGSKSITY SGTFNPVNNG NAYLCIYGWT
     QNPLVEYYIL ENYGEYNPGN SAQSRGTLQA AGGTYTLHES TRVNQPSIEG TRTFQQYWAI
     RQQKRNSGTV NTGEFFQAWE RAGMRMGNHN YMIVATEGYR SAGNSNINVQ TPA