ID   XLNA_AGABI              Reviewed;         333 AA.
AC   O60206;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Endo-1,4-beta-xylanase;
DE            Short=Xylanase;
DE            EC=3.2.1.8;
DE   Flags: Precursor;
GN   Name=xlnA;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Horst H39, and Horst U1;
RX   PubMed=9514754; DOI=10.1006/jmbi.1997.1605;
RA   De Groot P.W.J., Basten D.E.J.W., Sonnenberg A.S.M.,
RA   van Griensven L.J.L.D., Visser J., Schaap P.J.;
RT   "An endo-1,4-beta-xylanase-encoding gene from Agaricus bisporus is
RT   regulated by compost-specific factors.";
RL   J. Mol. Biol. 277:273-284(1998).
CC   -!- FUNCTION: Has xylanase activity. Seems to be involved in the release of
CC       sugars from the hemicellulolytic fraction in the compost.
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.
CC   -!- INDUCTION: Repressed on glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; Z83310; CAB05886.1; -; Genomic_DNA.
DR   EMBL; Z83199; CAB05665.1; -; mRNA.
DR   AlphaFoldDB; O60206; -.
DR   SMR; O60206; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10A_AGABI; -.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..333
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /id="PRO_0000007962"
FT   DOMAIN          18..330
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   333 AA;  36847 MW;  CFAD93D81145E90A CRC64;
     MYLVAFMLLA ILPTGYCQLN TLAVRAGKKY FGTATDNPEL GDAPYVAQLG NTADFNQITA
     GNSMKWDATE PSRGTFTFSN GDTVANMARN RGQLLRGHTC VWHSQLPNWV TSGNFDNSTL
     LSIVQNHCST LVSHYRGQMY SWDVVNEPFN EDGSFRQSVF FQKTGTAYIA TALRAARNAD
     PNTKLYINDF NIEGTGAKST GMINLVRSLQ QQNVPIDGIG VQAHLIVGQI PSSIQQNLQN
     FANLGVEVAI TELDIRMTLP VTQQKLEQQQ EDYRTVIRAC KAVSRCVGVT VWDWTDRYSW
     VPGVFNGEGA ACPWDENLAK KPAYQGIVDG WSQ