| IED ID | IndEnz0004000075 |
| Enzyme Type ID | xylanase000075 |
| Protein Name |
Endo-1,4-beta-xylanase 1 Xylanase 1 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 1 |
| Gene Name | Xyn1 |
| Organism | Leucoagaricus gongylophorus (Leaf-cutting ant fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Agaricaceae Leucoagaricus Leucoagaricus gongylophorus (Leaf-cutting ant fungus) |
| Enzyme Sequence | MVSFIFTRIILFAAAINGAVALPMNTTEPEDFSILSRSGTPSSTGYSNGYYYSWWTDGAAQATYANGGGGQYSLNWSGNNGNLVGGKGWNPGFNGRVIQYSGTYQPNGNSYLSVYGWTLNPLIEYYIVESYGSYNPSSAAARKGSVNCDGANYDILTTTRYNEPSINGTQTFQQFWSVRNPKKNPGGSISGSVSTGCHFTAWGNLGMNLGSTWNYQIVATEGYQSSGFSSITVA |
| Enzyme Length | 234 |
| Uniprot Accession Number | A6YAP7 |
| Absorption | |
| Active Site | ACT_SITE 124; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 221; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063 |
| 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:18307762}; |
| 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. {ECO:0000269|PubMed:18307762}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Glycosylation (3); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,156 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |