| IED ID | IndEnz0008000458 |
| Enzyme Type ID | cellulase000458 |
| Protein Name |
Endo-1,4-beta-xylanase Xylanase EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase |
| Gene Name | XYLP |
| Organism | Penicillium chrysogenum (Penicillium notatum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium chrysogenum species complex Penicillium chrysogenum (Penicillium notatum) |
| Enzyme Sequence | MIPNITQLKTAALVMLFAGQALSGPVESRQASESIDAKFKAHGKKYLGNIADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKLYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGALNALASAGTEEVAVTELDIAGATSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNPKEAYNVSQLLSRQHAFDLYLKLGNLLLSRLHSD |
| Enzyme Length | 353 |
| Uniprot Accession Number | P29417 |
| Absorption | |
| Active Site | ACT_SITE 161; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 267; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10061 |
| 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 | FUNCTION: Hydrolyzes oat spelt and birchwood xylan randomly, yielding xylose and xylobiose as major end products. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 38,193 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |