ID XYN3_ASPKW Reviewed; 211 AA. AC P33557; G7XQI2; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2012, sequence version 2. DT 24-JAN-2024, entry version 123. DE RecName: Full=Endo-1,4-beta-xylanase 3; DE Short=Xylanase 3; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase 3; DE AltName: Full=Xylanase C; DE Flags: Precursor; GN Name=xynC; ORFNames=AKAW_07136; OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus OS awamori var. kawachi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=1033177; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-34. RC STRAIN=NBRC 4308; RX PubMed=1368843; DOI=10.1271/bbb.56.1338; RA Ito K., Iwashita K., Iwano K.; RT "Cloning and sequencing of the xynC gene encoding acid xylanase of RT Aspergillus kawachii."; RL Biosci. Biotechnol. Biochem. 56:1338-1340(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 4308; RX PubMed=22045919; DOI=10.1128/ec.05224-11; RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H., RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.; RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used RT for brewing the Japanese distilled spirit shochu."; RL Eukaryot. Cell 10:1586-1587(2011). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-210. RC STRAIN=NBRC 4308; RX PubMed=9930661; DOI=10.1093/protein/11.12.1121; RA Fushinobu S., Ito K., Konno M., Wakagi T., Matsuzawa H.; RT "Crystallographic and mutational analyses of an extremely acidophilic and RT acid-stable xylanase: biased distribution of acidic residues and importance RT of Asp-37 for catalysis at low pH."; RL Protein Eng. 11:1121-1128(1998). 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 -!- 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; S45138; AAC60542.1; -; Genomic_DNA. DR EMBL; D14848; BAA03576.1; -; Genomic_DNA. DR EMBL; DF126466; GAA89022.1; -; Genomic_DNA. DR PDB; 1BK1; X-ray; 2.00 A; A=28-211. DR PDB; 3RI8; X-ray; 2.00 A; A=28-211. DR PDB; 3RI9; X-ray; 2.00 A; A=28-211. DR PDBsum; 1BK1; -. DR PDBsum; 3RI8; -. DR PDBsum; 3RI9; -. DR AlphaFoldDB; P33557; -. DR SMR; P33557; -. DR STRING; 1033177.P33557; -. DR CAZy; GH11; Glycoside Hydrolase Family 11. DR VEuPathDB; FungiDB:AKAW_07136; -. DR eggNOG; ENOG502RXA7; Eukaryota. DR InParanoid; P33557; -. DR BRENDA; 3.2.1.8; 514. DR UniPathway; UPA00114; -. DR EvolutionaryTrace; P33557; -. DR Proteomes; UP000006812; Unassembled WGS sequence. 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; Direct protein sequencing; KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; KW Secreted; Signal; Xylan degradation. FT SIGNAL 1..27 FT /evidence="ECO:0000269|PubMed:1368843" FT CHAIN 28..211 FT /note="Endo-1,4-beta-xylanase 3" FT /id="PRO_0000007991" FT DOMAIN 28..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 DISULFID 119..138 FT CONFLICT 7 FT /note="F -> S (in Ref. 1; AAC60542/BAA03576)" FT /evidence="ECO:0000305" FT CONFLICT 12..13 FT /note="VT -> GH (in Ref. 1; AAC60542/BAA03576)" FT /evidence="ECO:0000305" FT CONFLICT 21 FT /note="E -> Q (in Ref. 1; AAC60542/BAA03576)" FT /evidence="ECO:0000305" FT CONFLICT 42 FT /note="G -> A (in Ref. 1; AAC60542/BAA03576)" FT /evidence="ECO:0000305" FT CONFLICT 80 FT /note="T -> S (in Ref. 1; AAC60542/BAA03576)" FT /evidence="ECO:0000305" FT STRAND 33..38 FT /evidence="ECO:0007829|PDB:1BK1" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:1BK1" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 52..63 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 65..73 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 79..86 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 90..100 FT /evidence="ECO:0007829|PDB:1BK1" FT TURN 101..104 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 105..115 FT /evidence="ECO:0007829|PDB:1BK1" FT TURN 118..121 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 122..130 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 133..147 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 150..163 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:1BK1" FT HELIX 172..179 FT /evidence="ECO:0007829|PDB:1BK1" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:1BK1" FT STRAND 187..210 FT /evidence="ECO:0007829|PDB:1BK1" SQ SEQUENCE 211 AA; 22627 MW; 86EFBEE12A869022 CRC64; MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG VSSDFVVGLG WTTGSSNAIT YSAEYSASGS SSYLAVYGWV NYPQAEYYIV EDYGDYNPCS SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA QHGFGNSDFN YQVMAVEAWS GAGSASVTIS S //