ID   XYN1_MAGGR              Reviewed;         233 AA.
AC   P0CT48; 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 32.
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;
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], SUBCELLULAR LOCATION, CATALYTIC
RP   ACTIVITY, AND INDUCTION.
RC   STRAIN=KEN60-19;
RX   PubMed=8589407; DOI=10.1094/mpmi-8-0506;
RA   Wu S.C., Kaufman S., Darvill A.G., Albersheim P.;
RT   "Purification, cloning and characterization of two xylanases from
RT   Magnaporthe grisea, the rice blast fungus.";
RL   Mol. Plant Microbe Interact. 8:506-514(1995).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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. Accounts for approximately 70 percent of the
CC       endoxylanase activity in the culture filtrate. {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|PubMed:8589407};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8589407}.
CC   -!- INDUCTION: Expressed in presence of rice cell walls or on oat spelt
CC       xylan, but not when grown on sucrose. {ECO:0000269|PubMed:8589407}.
CC   -!- DISRUPTION PHENOTYPE: Retains 88 percent of the catalytic activity.
CC       Double xyl1/xyl2 deletion mutant retains 19 percent of the activity and
CC       exhibits a 50 percent reduction in accumulation of total mycelial mass.
CC       {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000303|PubMed:8589407}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L37529; AAC41683.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CT48; -.
DR   SMR; P0CT48; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_MAGGR; -.
DR   OMA; VENHGEY; -.
DR   UniPathway; UPA00114; -.
DR   PHI-base; PHI:567; -.
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; 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   1: Evidence at protein level;
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_0000429857"
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