ID   XYN2_MAGGR              Reviewed;         331 AA.
AC   Q01176;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
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;
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 39 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 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; L37530; AAC41684.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01176; -.
DR   SMR; Q01176; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10B_MAGGR; -.
DR   BRENDA; 3.2.1.8; 3152.
DR   UniPathway; UPA00114; -.
DR   PHI-base; PHI:568; -.
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   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   1: Evidence at protein level;
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_5000142624"
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;  35570 MW;  002C380713232AEE CRC64;
     MKASSVLLGL APLAALAAPT PEAELSARQA QQSIDALMKA KGKLYFGTAT DQGLLNTGKN
     SAIIKADFGQ VTPENSMKCQ SLENTRGQYN WAPADALVNF AVSNNKSIRG HTLIWHSQLP
     GWVNNINDRN QLTTVIQNHV ATVMGRWKGK IRAWDVVNEI FNEDGTMRQS VFSRVLGEDF
     VRIAFEAARK ADPNAKLYIN DYNLDRPNAG KLTKGMVGHV KKWVGAGVPI DGIGRQGHLQ
     SGQGNGLGQG IKGLGDSGVK EVGGNELDIQ GNNGNEFGGG NKACLPVPAC VGIPAWGVRD
     NDSWRPQGNP LLFDSNYNPK PAYNSVVQAL K