Detail Information for IndEnz0008000590
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;