ID   XYNA_ASPAC              Reviewed;         327 AA.
AC   O59859;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Endo-1,4-beta-xylanase;
DE            Short=Xylanase;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   AltName: Full=FIA-xylanase;
DE   Flags: Precursor;
GN   Name=xynIA;
OS   Aspergillus aculeatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Arai M., Kawaguchi T., Sumitani J.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; AB013110; BAA25847.1; -; Genomic_DNA.
DR   AlphaFoldDB; O59859; -.
DR   SMR; O59859; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10A_ASPAC; -.
DR   VEuPathDB; FungiDB:ASPACDRAFT_1855989; -.
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   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
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; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..25
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007963"
FT   CHAIN           26..327
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /id="PRO_0000007964"
FT   DOMAIN          55..326
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        157
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   MOD_RES         26
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        281..287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  35331 MW;  4ED731EDB6FF0A74 CRC64;
     MVQIKAAALA VLFASNVLAN PIEPRQASVS IDAKFKAHGK KYLGTIGDQY TLNKNAKTPA
     IIKADFGQLT PENSMKWDAT EPNRGQFSFS GSDYLVNFAQ SNGKLIRGHT LVWHSQLPSW
     VQSIYDKGTL IQVMQNHIAT VMQRYKGKVY AWDVVNEIFN EDGSLRQSHF YNVIGEDYVR
     IAFETARAVD PNAKLYINDY NLDSASYPKL TGLVNHVKKW VAAGVPIDGI GSQTHLSAGA
     GAAVSGALNA LAGAGTKEVA ITELDIAGAS STDYVNVVKA CLNQPKCVGI TVWGVADPDS
     WRSSSSPLLF DSNYNPKAAY TAIANAL