ID   XYN6_MAGGR              Reviewed;         380 AA.
AC   Q8NJ73;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Endo-1,4-beta-xylanase 6;
DE            Short=Xylanase 6;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 6;
DE   Flags: Precursor;
GN   Name=XYL6;
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], PROTEIN SEQUENCE OF 22-33, SUBCELLULAR
RP   LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=CP987;
RX   PubMed=16461639; DOI=10.1128/aem.72.2.986-993.2006;
RA   Wu S.C., Halley J.E., Luttig C., Fernekes L.M., Gutierrez-Sanchez G.,
RA   Darvill A.G., Albersheim P.;
RT   "Identification of an endo-beta-1,4-D-xylanase from Magnaporthe grisea by
RT   gene knockout analysis, purification, and heterologous expression.";
RL   Appl. Environ. Microbiol. 72:986-993(2006).
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|PubMed:16461639}.
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:16461639};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16461639}.
CC   -!- INDUCTION: Highly expressed both in culture with rice cell walls (RCWs)
CC       as a carbon source and in infected rice leaves.
CC       {ECO:0000269|PubMed:16461639}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; AY124591; AAM95237.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NJ73; -.
DR   SMR; Q8NJ73; -.
DR   CLAE; XYN10F_MAGGR; -.
DR   PRIDE; Q8NJ73; -.
DR   OMA; PENQMKW; -.
DR   BRENDA; 3.2.1.8; 3152.
DR   UniPathway; UPA00114; -.
DR   PHI-base; PHI:2043; -.
DR   Proteomes; UP000515153; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00236; fCBD; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:16461639"
FT   CHAIN           22..380
FT                   /note="Endo-1,4-beta-xylanase 6"
FT                   /id="PRO_0000429630"
FT   DOMAIN          22..53
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   DOMAIN          74..379
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   REGION          53..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        316
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        334..340
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  40868 MW;  5723E7A41998CB6D CRC64;
     MRTPAIVLAL APAAAFGQAA LWGQCGGQGW TGAKTCVSGA VCQAQNEWYS QCVPGSGGGN
     PPTPQPTQPS NPPPSTGSGL NAKFKNKGKL YFGTSMDHYD LNKAQLTNIV KAQFGQITNE
     NSMKWDAIEP SRNSFSWTNA DAVVNFATAN GKLMRGHTLL WHSQLPAWVS NINDRNTLTQ
     VIQNHVTAMV TRYRGKILQW DVVNEIFAED GSLRSSVFSR VLGEDFVGIA FRAARAADPN
     AKLYINDYNL DIANYAKVTR GMVEKVNKWV SQGIPIDGIG SQAHLAQPGG WNPASGVPAA
     LRALAAANVK EIAITELDIA GASANDYVTV VNACLQISKC VGITVWGVSD AISWRPNDNP
     LLYDRNYQPK AAYTAIMNAL