ID XYNA_ASPNG Reviewed; 211 AA. AC P55329; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 22-FEB-2023, entry version 107. DE RecName: Full=Endo-1,4-beta-xylanase A; DE Short=Xylanase A; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase A; DE AltName: Full=Endo-1,4-beta-xylanase I; DE Short=Xylanase I; DE Flags: Precursor; GN Name=xynA; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Hessing J.G.M., van Gorcom R.F.M., Verbakel J.M.A., Roza M., Maat J.; RT "Xylanase production."; RL Patent number WO9119782, 26-DEC-1991. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=8890913; DOI=10.1006/jmbi.1996.0556; RA Krengel U., Dijkstra B.W.; RT "Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus RT niger: molecular basis for its low pH optimum."; RL J. Mol. Biol. 263:70-78(1996). 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. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 3.0.; 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; A19535; CAA01470.1; -; Unassigned_DNA. DR PDB; 1T6G; X-ray; 1.80 A; C/D=28-211. DR PDB; 1UKR; X-ray; 2.40 A; A/B/C/D=28-211. DR PDB; 2QZ2; X-ray; 2.80 A; A=28-211. DR PDB; 6QE8; X-ray; 1.79 A; A=1-211. DR PDBsum; 1T6G; -. DR PDBsum; 1UKR; -. DR PDBsum; 2QZ2; -. DR PDBsum; 6QE8; -. DR AlphaFoldDB; P55329; -. DR SMR; P55329; -. DR Allergome; 980; Asp n Hemicellulase. DR CAZy; GH11; Glycoside Hydrolase Family 11. DR VEuPathDB; FungiDB:An14g07390; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1101058; -. DR VEuPathDB; FungiDB:ATCC64974_22790; -. DR VEuPathDB; FungiDB:M747DRAFT_300402; -. DR BRENDA; 3.2.1.8; 518. DR UniPathway; UPA00114; -. DR EvolutionaryTrace; P55329; -. 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; IPR033119; GH11_AS_2. 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; PS00777; GH11_2; 1. DR PROSITE; PS51761; GH11_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Disulfide bond; Glycosidase; KW Hydrolase; Polysaccharide degradation; Secreted; Signal; Xylan degradation. FT SIGNAL 1..27 FT CHAIN 28..211 FT /note="Endo-1,4-beta-xylanase A" FT /id="PRO_0000007992" FT DOMAIN 28..210 FT /note="GH11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097" FT ACT_SITE 106 FT /note="Nucleophile" FT ACT_SITE 197 FT /note="Proton donor" FT DISULFID 119..138 FT STRAND 33..38 FT /evidence="ECO:0007829|PDB:6QE8" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:6QE8" FT TURN 48..51 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 52..56 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 65..73 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 79..86 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 90..100 FT /evidence="ECO:0007829|PDB:6QE8" FT TURN 101..104 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 105..115 FT /evidence="ECO:0007829|PDB:6QE8" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 122..130 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 133..147 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 150..163 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:6QE8" FT HELIX 172..180 FT /evidence="ECO:0007829|PDB:6QE8" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 187..201 FT /evidence="ECO:0007829|PDB:6QE8" FT STRAND 204..209 FT /evidence="ECO:0007829|PDB:6QE8" SQ SEQUENCE 211 AA; 22642 MW; 82BEBEE12ED79303 CRC64; MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG VSSDFVVGLG WTTGSSKAIT YSAEYSASGS SSYLAVYGWV NYPQAEYYIV EDYGDYNPCS SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA QHGFGNSDFN YQVMAVEAWS GAGSASVTIS S //