IED ID | IndEnz0004000158 |
Enzyme Type ID | xylanase000158 |
Protein Name |
Endo-1,4-beta-xylanase S20 Xylanase S20 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase S20 |
Gene Name | xynS20 |
Organism | Neocallimastix patriciarum (Rumen fungus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Chytridiomycota Chytridiomycota incertae sedis Neocallimastigomycetes Neocallimastigales Neocallimastigaceae Neocallimastix Neocallimastix patriciarum (Rumen fungus) |
Enzyme Sequence | MLRKLVTGALAAALLLSGQSNAQNACQQTQQLSGGRTINNKNETGNGNGNYKYEIWRDGNGGSLTLYPKDAAFKASWNNSGDFLGRVGLTFNKPAATNLGGDLIANYNYKKSGSDGGTYSYIGIYGWMDNPQIEYYVVDDWMHNRGAPGGSYMGSQKGTITVDGGTYKVWSGQRTGASKWGTSTFTQIFSIRTSPRQCGSINVSEHFRQWQKLGLRLGGLMEAQLLAESGGGSGYVDFTYATITIGGSSSNASAPSNNNNNNNNNNDNNGNWNNWNNNNNNNNNNNNNNNNNNNNQGGGNCAAIWGQCGGSGYNGPKCCKQGSCKQINQWYSQCQ |
Enzyme Length | 335 |
Uniprot Accession Number | A8TGA1 |
Absorption | |
Active Site | ACT_SITE 134; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 228; /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:18415096}; |
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:18415096}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius.; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0.; |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (2); Glycosylation (4); Region (1); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18415096}. |
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 | 36,094 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.9 mg/ml for oat spelt xylan; Vmax=3.886 umol/min/mg enzyme toward oat spelt xylan; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.8; |