ID Q9RC94_9BACI Unreviewed; 354 AA. AC Q9RC94; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 04-NOV-2026, entry version 122. DE RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|RuleBase:RU362015}; DE EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|RuleBase:RU362015}; DE Flags: Precursor; GN Name=xynJ {ECO:0000313|EMBL:BAA82316.1}; OS Bacillus sp. 41M-1. OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=98930 {ECO:0000313|EMBL:BAA82316.1}; RN [1] {ECO:0000313|EMBL:BAA82316.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=41M-1 {ECO:0000313|EMBL:BAA82316.1}; RA Nakai R., Wakabayashi K., Asano T., Aono R., Horikoshi K., Nakamura S.; RT "Nucleotide sequence and mutational analysis of the gene encoding the novel RT alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1."; RL Nucleic Acids Symp. Ser. 31:235-236(1994). RN [2] {ECO:0000313|EMBL:BAA82316.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=41M-1 {ECO:0000313|EMBL:BAA82316.1}; RA Kusuda J.; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:2DCK} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH CA(2+). RA Ihsanawati., Tanaka N., Nakamura S., Kumasaka T.; RT "A two-domain structure of alkaliphilic XynJ from Bacillus sp. 41M-1."; RL Submitted (JAN-2006) to the PDB data bank. RN [4] {ECO:0007829|PDB:6KJL, ECO:0007829|PDB:6KKA} RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 28-354 IN COMPLEX WITH CA(2+). RX PubMed=31421720; DOI=10.1016/j.enzmictec.2019.109363; RA Takita T., Nakatani K., Katano Y., Suzuki M., Kojima K., Saka N., RA Mikami B., Yatsunami R., Nakamura S., Yasukawa K.; RT "Increase in the thermostability of GH11 xylanase XynJ from Bacillus sp. RT strain 41M-1 using site saturation mutagenesis."; RL Enzyme Microb. Technol. 130:109363-109363(2019). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681, CC ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015}; CC -!- PATHWAY: Glycan degradation; xylan degradation. CC {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097, CC ECO:0000256|RuleBase:RU362015}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family. CC {ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015}. 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; AB029319; BAA82316.1; -; Genomic_DNA. DR PDB; 2DCJ; X-ray; 2.24 A; A/B=1-354. DR PDB; 2DCK; X-ray; 2.10 A; A=1-354. DR PDB; 6KJL; X-ray; 2.45 A; A/B=28-354. DR PDB; 6KKA; X-ray; 2.36 A; A/B=28-354. DR AlphaFoldDB; Q9RC94; -. DR MDposit; Q9RC94; -. DR SMR; Q9RC94; -. DR CAZy; CBM36; Carbohydrate-Binding Module Family 36. DR CAZy; GH11; Glycoside Hydrolase Family 11. DR BRENDA; 3.2.1.8; 11174. DR UniPathway; UPA00114; -. DR EvolutionaryTrace; Q9RC94; -. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd04078; CBM36_xylanase-like; 1. DR Gene3D; 2.60.120.180; -; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR InterPro; IPR005084; CBM6. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR008979; Galactose-bd-like_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; PF03422; CBM_6; 1. DR Pfam; PF00457; Glyco_hydro_11; 1. DR PRINTS; PR00911; GLHYDRLASE11. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR PROSITE; PS51175; CBM6; 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 {ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:2DCK}; KW Calcium {ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:2DCK}; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|PROSITE-ProRule:PRU01097}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE- KW ProRule:PRU01097}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01097}; KW Metal-binding {ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:2DCK}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326, KW ECO:0000256|PROSITE-ProRule:PRU01097}; Signal {ECO:0000256|SAM:SignalP}; KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE- KW ProRule:PRU01097}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..354 FT /note="Endo-1,4-beta-xylanase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004332952" FT DOMAIN 28..223 FT /note="GH11" FT /evidence="ECO:0000259|PROSITE:PS51761" FT DOMAIN 237..354 FT /note="CBM6" FT /evidence="ECO:0000259|PROSITE:PS51175" FT ACT_SITE 120 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097" FT ACT_SITE 210 FT /note="Proton donor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097" FT BINDING 71 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:6KKA" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:6KKA" FT BINDING 240 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2DCK, ECO:0007829|PDB:6KJL" FT BINDING 242 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:2DCK" FT BINDING 259 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2DCK, ECO:0007829|PDB:6KJL" FT BINDING 264 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:2DCK" FT BINDING 340 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:2DCK" FT BINDING 344 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:6KKA" FT BINDING 345 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:2DCK" FT BINDING 349 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2DCJ, ECO:0007829|PDB:6KJL" SQ SEQUENCE 354 AA; 39000 MW; 5F81EBB473151DC8 CRC64; MKQVKIMFLM TMFLGIGLLF FSENAEAAIT SNEIGTHDGY DYEFWKDSGG SGSMTLNSGG TFSAQWSNVN NILFRKGKKF DETQTHQQIG NMSINYGATY NPNGNSYLTV YGWTVDPLVE FYIVDSWGTW RPPGGTPKGT INVDGGTYQI YETTRYNQPS IKGTATFQQY WSVRTSKRTS GTISVSEHFR AWESLGMNMG NMYEVALTVE GYQSSGSANV YSNTLTIGGQ SGGEQATRVE AESMTKGGPY TSNITSPFNG VALYANGDNV SFNHSFTKAN SSFSLRGASN NSNMARVDLR IGGQNRGTFY FGDQYPAVYT INNINHGIGN QLVELIVTAD DGTWDAYLDY LEIR //