IED ID | IndEnz0004000131 |
Enzyme Type ID | xylanase000131 |
Protein Name |
Endo-1,4-beta-xylanase UM03411 Xylanase UM03411 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase UM03411 |
Gene Name | UMAG_03411 |
Organism | Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Ustilaginomycotina Ustilaginomycetes Ustilaginales Ustilaginaceae Ustilago Ustilago maydis (Corn smut fungus) Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) |
Enzyme Sequence | MKTNFLVLLSALLAASSAVTATLIPAKCKHEAFSQRAGSSLNAAIKSDGRKYFGTCADPGTLGNWQISNIIKAEMGQVTPENSMKWDATQPQRGTFNFGNADRLVDFATSNGKLIRGHTLVWHSQLPSWVSSITDANDLTNVIQNRIATVVGRYKGKVYAWDVVNEMFNENGSFRESVFYKLLGEDFVKIAFEAARKADPNAKLYINDYNLDDPDYPKLKSLVANVKKWRSQGVPIDGIGSQSHLQAAGHFLDASKVGGAMQALCAAASECAMTELDIAQASPDQYTKATEACLNQKNCVGITVWGVSDNTSWRKNANPLLWNSSYQKKPAYNAVLSTLNSYQA |
Enzyme Length | 344 |
Uniprot Accession Number | Q4P902 |
Absorption | |
Active Site | ACT_SITE 166; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 275; /note=Nucleophile; /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; |
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. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Signal peptide (1) |
Keywords | Carbohydrate metabolism;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation |
Interact With | |
Induction | INDUCTION: Induced in presence of Zea mays leaves and by xylan, and repressed by glucose. SNF1 acts as a positive regulator through the release of glucose repression. {ECO:0000269|PubMed:10882531, ECO:0000269|PubMed:21062173}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22300648}. |
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 | 37,592 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |