Detail Information for IndEnz0004000204
IED ID IndEnz0004000204
Enzyme Type ID xylanase000204
Protein Name Endo-1,4-beta-xylanase A
Xylanase A
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase A
Gene Name xlnA
Organism Streptomyces lividans
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces lividans
Enzyme Sequence MGSYALPRSGVRRSIRVLLLALVVGVLGTATALIAPPGAHAAESTLGAAAAQSGRYFGTAIASGRLSDSTYTSIAGREFNMVTAENEMKIDATEPQRGQFNFSSADRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGSALRQAMIDHINGVMAHYKGKIVQWDVVNEAFADGSSGARRDSNLQRSGNDWIEVAFRTARAADPSAKLCYNDYNVENWTWAKTQAMYNMVRDFKQRGVPIDCVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGAPASTYANVTNDCLAVSRCLGITVWGVRDSDSWRSEQTPLLFNNDGSKKAAYTAVLDALNGGDSSEPPADGGQIKGVGSGRCLDVPDASTSDGTQLQLWDCHSGTNQQWAATDAGELRVYGDKCLDAAGTSNGSKVQIYSCWGGDNQKWRLNSDGSVVGVQSGLCLDAVGNGTANGTLIQLYTCSNGSNQRWTRT
Enzyme Length 477
Uniprot Accession Number P26514
Absorption
Active Site ACT_SITE 169; /note=Proton donor; ACT_SITE 277; /note=Nucleophile
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: Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Beta strand (23); Chain (1); Disulfide bond (3); Domain (2); Helix (20); Signal peptide (1); Turn (6)
Keywords 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Lectin;Polysaccharide degradation;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..41; /evidence=ECO:0000269|PubMed:1743521
Structure 3D X-ray crystallography (12)
Cross Reference PDB 1E0V; 1E0W; 1E0X; 1KNL; 1KNM; 1MC9; 1OD8; 1V0K; 1V0L; 1V0M; 1V0N; 1XAS;
Mapped Pubmed ID 10767281; 10930426; 12744311; 15306887;
Motif
Gene Encoded By
Mass 51,163
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.8;