ID   XLNA_AGABI     STANDARD;      PRT;   333 AA.
AC   O60206;
DT   28-FEB-2003 (Rel. 41, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Endo-1,4-beta-xylanase precursor (EC 3.2.1.8) (Xylanase).
GN   Name=xlnA;
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Horst H39, and Horst U1;
RX   MEDLINE=98181027; 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
CC       release of sugars from the hemicellulolytic fraction in the
CC       compost.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of 1,4-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- PATHWAY: Xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: Repressed on glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
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CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; Z83310; CAB05886.1; -.
DR   EMBL; Z83199; CAB05665.1; -.
DR   HSSP; Q59277; 1FH9.
DR   InterPro; IPR001000; Glyco_hydro_10.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   PROSITE; PS00591; GLYCOSYL_HYDROL_F10; 1.
KW   Glycosidase; Hydrolase; Signal; Xylan degradation.
FT   SIGNAL        1     17       Potential.
FT   CHAIN        18    333       Endo-1,4-beta-xylanase.
FT   ACT_SITE    147    147       Proton donor (By similarity).
FT   ACT_SITE    252    252       Nucleophile (By similarity).
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
//