ID   XYN1_CLAPU              Reviewed;         216 AA.
AC   O74716;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 79.
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   Flags: Precursor;
GN   Name=xyl1;
OS   Claviceps purpurea (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=5111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION,
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=T5;
RX   PubMed=18944813; DOI=10.1094/phyto.1998.88.10.1020;
RA   Giesbert S., Lepping H.B., Tenberge K.B., Tudzynski P.;
RT   "The xylanolytic system of Claviceps purpurea: cytological evidence for
RT   secretion of xylanases in infected rye tissue and molecular
RT   characterization of two xylanase genes.";
RL   Phytopathology 88:1020-1030(1998).
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:18944813}.
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:0000269|PubMed:18944813}.
CC   -!- INDUCTION: Expressed throughout the entire infection process during in
CC       infection of rye tissue. {ECO:0000269|PubMed:18944813}.
CC   -!- DISRUPTION PHENOTYPE: Leads to significant reduced xylanase activity.
CC       {ECO:0000269|PubMed:18944813}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; Y16969; CAA76570.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74716; -.
DR   SMR; O74716; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_CLAPU; -.
DR   VEuPathDB; FungiDB:CPUR_03570; -.
DR   BRENDA; 3.2.1.8; 1445.
DR   UniPathway; UPA00114; -.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..216
FT                   /note="Endo-1,4-beta-xylanase 1"
FT                   /id="PRO_5000147292"
FT   DOMAIN          29..216
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        112
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  23339 MW;  012E874E939E7581 CRC64;
     MFLTSVVSLV VGAISCVSAA PAAASELMQM TPRNSCYGGG LYSSYWADYG NTRYSCGAGG
     HYDLSWGNGG NVVAGRGWKP ASPRAVTYSG SWQCNGNCYL SVYGWTINPL VEYYIVENYG
     NYNPSAGAQR RGQVTADGSI YDIYISTQHN QPSILGTNTF HQYWSIRRNK RVGGTVSTGV
     HFNAWRSLGM PLGTYDYMIV ATEGFRSSGS ASITVS