ID XLNA_AGABI STANDARD; PRT; 333 AA. AC O60206; DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 16-MAY-2006, entry version 34. 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 [GENOMIC DNA / MRNA]. 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 protein. CC -!- INDUCTION: Repressed on glucose. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z83310; CAB05886.1; -; Genomic_DNA. DR EMBL; Z83199; CAB05665.1; -; mRNA. 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 /FTId=PRO_0000007962. 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 //