Detail Information for IndEnz0008000446
IED ID IndEnz0008000446
Enzyme Type ID cellulase000446
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