ID   XYN3_MAGGR              Reviewed;         236 AA.
AC   Q92244;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Endo-1,4-beta-xylanase 3;
DE            Short=Xylanase 3;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 3;
DE   Flags: Precursor;
GN   Name=XYL3;
OS   Magnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=148305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CP987;
RA   Wu S.-C., Darvill A.G., Albersheim P.;
RT   "Three differentially expressed xylanases from the rice blast fungus are
RT   required for pathogenicity.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 46-62, SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=CP987;
RX   DOI=10.1094/MPMI.1997.10.6.700;
RA   Wu S.C., Ham K.S., Darvill A.G., Albersheim P.;
RT   "Deletion of two endo-beta-1,4-xylanase genes reveals additional isozymes
RT   secreted by the rice blast fungus.";
RL   Mol. Plant Microbe Interact. 10:700-708(1997).
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:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000269|Ref.2};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; AY144350; AAB06572.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q92244; -.
DR   SMR; Q92244; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   OMA; DYWQNWT; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000515153; Genome assembly.
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; 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; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..45
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..236
FT                   /note="Endo-1,4-beta-xylanase 3"
FT                   /id="PRO_0000429622"
FT   DOMAIN          46..236
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        131
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        223
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   236 AA;  25555 MW;  317AF862291B17E2 CRC64;
     MQILTWALAA LAAIPAVTAA PVETVEASSM DELVERSPNV TLVARGTPSS TGTHNGFYYS
     HWTDNAGADV TYSMGGGGQF SYTWRNSGNF VGGKGWNPGN AGRVINYSGS YSPQGNSYLA
     VYGWTRNPLI EYYVVESFGS YNPSSGATNR GSFTSDGSTY DILVSTRYNQ PSIDGTKTFQ
     QFWSVRRNKR ASGTVTFANH VNAWRNAGLN LGNQWNYQIL AVEGYHSSGS ASMTVR