IED ID | IndEnz0008000590 |
Enzyme Type ID | cellulase000590 |
Protein Name |
Endo-1,4-beta-xylanase Xylanase EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase |
Gene Name | XYNA |
Organism | Thermomyces lanuginosus (Humicola lanuginosa) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Thermomyces Thermomyces lanuginosus (Humicola lanuginosa) |
Enzyme Sequence | MVGFTPVALAALAATGALAFPAGNATELEKRQTTPNSEGWHDGYYYSWWSDGGAQATYTNLEGGTYEISWGDGGNLVGGKGWNPGLNARAIHFEGVYQPNGNSYLAVYGWTRNPLVEYYIVENFGTYDPSSGATDLGTVECDGSIYRLGKTTRVNAPSIDGTQTFDQYWSVRQDKRTSGTVQTGCHFDAWARAGLNVNGDHYYQIVATEGYFSSGYARITVADVG |
Enzyme Length | 225 |
Uniprot Accession Number | O43097 |
Absorption | |
Active Site | ACT_SITE 117; /note=Nucleophile; ACT_SITE 209; /note=Proton donor |
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|Ref.3}; |
DNA Binding | |
EC Number | 3.2.1.8 |
Enzyme Function | |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. Thermostable. {ECO:0000269|Ref.3}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|Ref.3}; |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Beta strand (14); Chain (1); Disulfide bond (1); Domain (1); Helix (1); Modified residue (1); Sequence conflict (2); Signal peptide (1); Turn (2) |
Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Polysaccharide degradation;Pyrrolidone carboxylic acid;Signal;Xylan degradation |
Interact With | |
Induction | INDUCTION: By xylan. {ECO:0000269|Ref.3}. |
Subcellular Location | |
Modified Residue | MOD_RES 32; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P36217 |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..31 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1YNA; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 24,356 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=2223.3 umol/min/mg enzyme {ECO:0000269|Ref.3}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.8; |