| IED ID | IndEnz0004000216 |
| Enzyme Type ID | xylanase000216 |
| Protein Name |
Endo-1,4-beta-xylanase 2 Xylanase 2 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 2 |
| Gene Name | xynII |
| Organism | Aureobasidium pullulans (Black yeast) (Pullularia pullulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Dothideomycetidae Dothideales Saccotheciaceae Aureobasidium Aureobasidium pullulans (Black yeast) (Pullularia pullulans) |
| Enzyme Sequence | MHFSTITAALALLGLGAATPTDYSTSSYSKNQGLAQAWTSKGRQYIGTALTIRDDPVEQGIIQSRTDFNSITPENAMKWESTEPQRNNFTFAGADAVADFADRYNKEMRCHTLVWHSQLPAWVSQGNFDNKTLISIMENHIKKVAGRYKNKCTHWDVVNEALNEDGTYRSSVFYNTIGEAFIPIAFRFAEKYAGSKTKLYYNDYNLEYGSAKALGAQRILKLVQSYGVQIDGVGLQAHLSSEATASTGGGVTPDVQTLTNVLKLYTDLGVEVAYTELDVRFTTPATDAKLKAQADAYARVVQSCINVKRCVGITVWGVSDKYSWIPGVFPTEGAALLWDENFNKKPAYSSVLKTIQSFRKS |
| Enzyme Length | 361 |
| Uniprot Accession Number | Q2PGV8 |
| Absorption | |
| Active Site | ACT_SITE 160; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 276; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:15988573}; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Hydrolyzes birch-wood xylan, with a similar activity toward oat-spelt xylan. Also shows weak activities toward pNP-beta-D-cellobioside and pNP-beta-D-xylopyranoside, but no detectable activity toward carboxymethyl cellulose and pNP-beta-L-arabinofuranoside.-. {ECO:0000269|PubMed:15988573}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:15988573}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:15988573}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15988573}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:15988573 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,938 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |