| IED ID | IndEnz0004000192 |
| Enzyme Type ID | xylanase000192 |
| Protein Name |
Endo-1,4-beta-xylanase 1 Xylanase 1 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 1 |
| Gene Name | xynI |
| 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 | MKFFATIAALVVAAVAAPVAEADAEASSPMLIERAGPGGINYVQNYNGNLGQFTYNENAGTYSMYWTNGVSGDFVVGLGWSTGAARSITYSSSYTASGGSYLSVYGWINSPQAEYYIVESYGSYNPCGAGQSGVTQLGTVVSDGATYTVCTDERVNEPSITGTSTFKQYWSVRQTKRTSGTVTTGNHFAYWAKYGFGNSYNFQVMAVEAFSGTGSASVTVS |
| Enzyme Length | 221 |
| Uniprot Accession Number | Q96TR7 |
| Absorption | |
| Active Site | ACT_SITE 114; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 208; /note=Proton donor; /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:16233094}; |
| 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 xylans from oat spelt and birchwood at similar rates, but it has no detectable activity toward Avicel or carboxymethyl cellulose. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:16233094}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2.0. {ECO:0000269|PubMed:16233094}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16233094}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,374 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |