ID   XYN2_MAGO7              Reviewed;         331 AA.
AC   G4MTF8;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Endo-1,4-beta-xylanase 2;
DE            Short=Xylanase 2;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 2;
DE   Flags: Precursor;
GN   Name=XYL2; Synonyms=XYN33; ORFNames=MGG_01542;
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 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; CM001232; EHA54709.1; -; Genomic_DNA.
DR   RefSeq; XP_003714516.1; XM_003714468.1.
DR   AlphaFoldDB; G4MTF8; -.
DR   SMR; G4MTF8; -.
DR   STRING; 318829.MGG_01542T0; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblFungi; MGG_01542T0; MGG_01542T0; MGG_01542.
DR   GeneID; 2679400; -.
DR   KEGG; mgr:MGG_01542; -.
DR   VEuPathDB; FungiDB:MGG_01542; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   HOGENOM; CLU_020161_2_0_1; -.
DR   InParanoid; G4MTF8; -.
DR   OMA; YSWRASG; -.
DR   OrthoDB; 829814at2759; -.
DR   UniPathway; UPA00114; -.
DR   PHI-base; PHI:2204; -.
DR   Proteomes; UP000009058; Chromosome 2.
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   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; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..331
FT                   /note="Endo-1,4-beta-xylanase 2"
FT                   /id="PRO_0000429620"
FT   DOMAIN          31..329
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        159
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        284..290
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  35681 MW;  86377226930F8EF9 CRC64;
     MKASSVLLGL APLAALAAPT PEAELSARQA QQSIDALMKA KGKLYFGTAT DQGLLNTGKN
     SAIIKADFGQ VTPENSMKWQ SLENTRGQYN WAPADALVNF AVSNNKSIRG HTLIWHSQLP
     GWVNNINDRN QLTTVIQNHV ATVMGRWKGK IRAWDVVNEI FNEDGTMRQS VFSRVLGEDF
     VRIAFEAARK ADPNAKLYIN DYNLDSPNAA KLTKGMVAHV KKWLAAGVPI DGIGSQGHLQ
     SGQGNGLAQA IKALADSGVK EVAVTELDIQ GNNANDYAAV TKGCLAVPAC VGITAWGVRD
     NDSWRPQGNP LLFDSNYNPK AAYNSVVQAL K