IED ID | IndEnz0004000150 |
Enzyme Type ID | xylanase000150 |
Protein Name |
Endo-1,4-beta-xylanase Xylanase EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase |
Gene Name | |
Organism | Penicillium simplicissimum |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium simplicissimum |
Enzyme Sequence | QASVSIDAKFKAHGKKYLGTIGDQYTLTKNTKNPAIIKADFGQLTPENSMKWDATEPNRGQFTFSGSDYLVNFAQSNGKLIRGHTLVWHSQLPGWVSSITDKNTLISVLKNHITTVMTRYKGKIYAWDVLNEIFNEDGSLRNSVFYNVIGEDYVRIAFETARSVDPNAKLYINDYNLDSAGYSKVNGMVSHVKKWLAAGIPIDGIGSQTHLGAGAGSAVAGALNALASAGTKEIAITELDIAGASSTDYVNVVNACLNQAKCVGITVWGVADPDSWRSSSSPLLFDGNYNPKAAYNAIANAL |
Enzyme Length | 302 |
Uniprot Accession Number | P56588 |
Absorption | |
Active Site | ACT_SITE 132; /note=Proton donor; ACT_SITE 238; /note=Nucleophile |
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; |
DNA Binding | |
EC Number | 3.2.1.8 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Beta strand (12); Chain (1); Disulfide bond (1); Domain (1); Helix (16); Modified residue (1); Turn (2) |
Keywords | 3D-structure;Carbohydrate metabolism;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Secreted;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:9792094 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (8) |
Cross Reference PDB | 1B30; 1B31; 1B3V; 1B3W; 1B3X; 1B3Y; 1B3Z; 1BG4; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 32,551 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |