ID XYN5_ASPNC Reviewed; 211 AA. AC A2R4D1; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Probable endo-1,4-beta-xylanase 5; DE Short=Xylanase 5; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase 5; DE Flags: Precursor; GN Name=XYN5; ORFNames=An14g07390; OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=425011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513; RX PubMed=17259976; DOI=10.1038/nbt1282; RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M., RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory Aspergillus RT niger CBS 513.88."; RL Nat. Biotechnol. 25:221-231(2007). 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:0000250}. 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 11 (cellulase G) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM270327; CAK46731.1; -; Genomic_DNA. DR RefSeq; XP_001401361.1; XM_001401324.1. DR AlphaFoldDB; A2R4D1; -. DR SMR; A2R4D1; -. DR EnsemblFungi; CAK46731; CAK46731; An14g07390. DR GeneID; 4987596; -. DR KEGG; ang:An14g07390; -. DR VEuPathDB; FungiDB:An14g07390; -. DR HOGENOM; CLU_052631_3_2_1; -. DR OrthoDB; 1778490at2759; -. DR UniPathway; UPA00114; -. DR Proteomes; UP000006706; Chromosome 1R. 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 PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1. DR PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1. DR Pfam; PF00457; Glyco_hydro_11; 1. DR PRINTS; PR00911; GLHYDRLASE11. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00776; GH11_1; 1. DR PROSITE; PS51761; GH11_3; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Glycosidase; Hydrolase; KW Polysaccharide degradation; Reference proteome; Secreted; Signal; KW Xylan degradation. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT CHAIN 17..211 FT /note="Probable endo-1,4-beta-xylanase 5" FT /id="PRO_5000220988" FT DOMAIN 19..210 FT /note="GH11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097" FT ACT_SITE 106 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062" FT ACT_SITE 197 FT /note="Proton donor" FT /evidence="ECO:0000250" SQ SEQUENCE 211 AA; 22639 MW; DECA078B58E362F0 CRC64; MKVTAAFASL LLTAFAAPAP EPVLVSRSAG INYVQNYNGN LGDFTYDEST GTFSMYWEDG VSSDFVVGLG WTTGSSKSIT YSAQYSASSS SSYLAVYGWV NSPQAEYYIV EDYGDYNPCS SATSLGTVYS DGSTYQVCTD TRTNAPSITG TSTFTQYFSV RESTRTSGTV TIANHFNFWA QHGFGNSNFN YQVMAVEAWN GAGSASVTIS S //