| IED ID | IndEnz0004000009 |
| Enzyme Type ID | xylanase000009 |
| Protein Name |
Beta-1,3-xylanase EC 3.2.1.32 |
| Gene Name | txyA 3xynAlc |
| Organism | Alcaligenes sp. |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Alcaligenaceae Alcaligenes unclassified Alcaligenes Alcaligenes sp. |
| Enzyme Sequence | MKKLAKMISIATLGACAFSAHALDGKLVPNEGVLVSVGQDVDSVNDYSSAMSTTPAGVTNYVGIVNLDGLASNADAGAGRNNVVELANLYPTSALIVGVSMNGQIQNVAQGQYNANIDTLIQTLGELDRPVYLRWAYEVDGPWNGHNTEDLKQSFRNVYQRIRELGYGDNISMIWQVASYCPTAPGQLSSWWPGDDVVDWVGLSYFAPQDCNWDRVNEAAQWARSHNKPLFINESSPQRYQLADRTYSSDPAKGTNRQSKTEQQIWSEWFAPYFQFMEDNKDILKGFTYINADWDSQWRWAAPYNEGYWGDSRVQVLPYIKQQWQDTLENPKFINHSSDLFAKLGYVADGGDNGGDNGGDNGGDNGGDNGGDNGGTEPPENCQDDFNFNYVSDQEIEVYHVDKGWSAGWNYVCLNDYCLPGNKSNGAFRKTFNAVLGQDYKLTFKVEDRYGQGQQILDRNITFTTQVCN |
| Enzyme Length | 469 |
| Uniprot Accession Number | Q8RS40 |
| 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 CuCl(2), FeCl(3), HgCl(2) and N-bromosuccinimide. Moderately inhibited by AgCl, AlCl(3), Pb(CH(3)COO)(2) and dithiothreitol. BaCl(2), CaCl(2), KCl, MgCl(2), MnCl(2), NaCl, ZnCl(2), ethylenediaminetetraacetic acid, N-ethylmaleimide, iodoacetic acid and p-chloromercuribenzoic acid have little or no effect on activity. {ECO:0000269|PubMed:12501421}. |
| 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:11948152, ECO:0000269|PubMed:12501421}; |
| DNA Binding | |
| EC Number | 3.2.1.32 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, carboxymethylcellulose, curdlan, glucomannan or beta-1,4-mannan. {ECO:0000269|PubMed:11948152, ECO:0000269|PubMed:12501421}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Stable below 40 degrees Celsius. Loses 70% and 99% of activity respectively when incubated for 10 minutes at 50 and 60 degrees Celsius. {ECO:0000269|PubMed:11948152, ECO:0000269|PubMed:12501421}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. Stable from pH 5.0-11.0. Retains 65% and 70% of activity respectively when incubated at pH 4.0 and 12.0 for 24 hours. {ECO:0000269|PubMed:11948152, ECO:0000269|PubMed:12501421}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (8); Chain (1); Disulfide bond (2); Domain (1); Helix (1); Region (2); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: By beta-1,3-xylan. {ECO:0000269|PubMed:12501421}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000269|PubMed:12501421 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2COV; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,257 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.32; |