| IED ID | IndEnz0004000002 |
| Enzyme Type ID | xylanase000002 |
| Protein Name |
Beta-1,3-xylanase XYL4 EC 3.2.1.32 Beta-1,3-xylanase |
| Gene Name | xyl4 |
| Organism | Vibrio sp. |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio unclassified Vibrio Vibrio sp. |
| Enzyme Sequence | MKRTYLSLIAAGVMSLSVSAWSLDGVLVPESGILVSVGQDVDSVNDYASALGTIPAGVTNYVGIVNLDGLNSDADAGAGRNNIAELANAYPTSALVVGVSMNGEVDAVASGRYNANIDTLLNTLAGYDRPVYLRWAYEVDGPWNGHSPSGIVTSFQYVHDRIIALGHQAKISLVWQVASYCPTPGGQLDQWWPGSEYVDWVGLSYFAPQDCNWDRVNEAAQFARSKGKPLFLNESTPQRYQVADLTYSADPAKGTNRQSKTSQQLWDEWFAPYFQFMSDNSDIVKGFTYINADWDSQWRWAAPYNEGYWGDSRVQANALIKSNWQQEIAKGQYINHSETLFETLGYGSTGGGDNGGGDNGGTNPPEPCNEEFGYRYVSDSTIEVFHKNNGWSAEWNYVCLNGLCLQGEIKNGEYVKQFDAQLGSTYGIEFKVADGESQFITDKSVTFENKQCGSTGTPGGGDNGSGGDNGGDNGSGGDNGSGGGTDPSQCSADFGYNYRSDTEIEVFHKDLGWSASWNYICLDDYCVPGDKSGDSYNRSFNATLGSDYKITFKVEDSASQFITEKNITFVNTSCAQ |
| Enzyme Length | 576 |
| Uniprot Accession Number | D5MP61 |
| Absorption | |
| Active Site | ACT_SITE 138; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01100; ACT_SITE 234; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01100 |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by Hg(2+), partially inhibited by Mn(2+), Cu(2+) and Pb(2+). Unaffected by Ca(2+), Mg(2+) and EDTA. {ECO:0000269|PubMed:15743273}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans.; EC=3.2.1.32; Evidence={ECO:0000269|PubMed:15743273}; |
| DNA Binding | |
| EC Number | 3.2.1.32 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylobiose, xylotriose and xylotetraose. Converts beta-1,3-xylotriose into xylose and xylobiose, converts beta-1,3-xylotetraose mainly into xylotriose and xylose, converts beta-1,3-xylopentaose into xylobiose and xylotriose. Does not hydrolyze beta-1,4-xylan, beta-1,4-mannan, beta-1,4-glucan, beta-1,3-xylobiose or p-nitrophenyl-beta-xyloside. {ECO:0000269|PubMed:15743273}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Inactive above 60 degrees Celsius. {ECO:0000269|PubMed:15743273}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:15743273}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (10); Chain (1); Disulfide bond (4); Domain (1); Helix (17); Mutagenesis (5); Region (4); Signal peptide (1); Turn (8) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2DDX; 3VPL; |
| Mapped Pubmed ID | 22296113; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,591 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.4 mM for beta-1,3-xylotetraose {ECO:0000269|PubMed:15743273}; KM=7.5 mM for beta-1,3-xylopentaose {ECO:0000269|PubMed:15743273}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.32; |