Detail Information for IndEnz0004000087
IED ID IndEnz0004000087
Enzyme Type ID xylanase000087
Protein Name Endo-1,4-beta-xylanase A
Xylanase A
EC 3.2.1.8
Gene Name xynAS9
Organism Streptomyces sp.
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces unclassified Streptomyces Streptomyces sp.
Enzyme Sequence MFRHHPTRGRRTAGLLAAALATLSAGLTAVAPAHPARADTATLGELAEAKGRYFGSATDNPELPDTQYTQILGSEFSQITVGNTMKWQYTEPSRGRFDYTAAEEIVDLAESNGQSVRGHTLVWHNQLPSWVDDVPAGELLGVMRDHITHEVDHFKGRLIHWDVVNEAFEEDGSRRQSVFQQKIGDSYIAEAFKAARAADPDVKLYYNDYNIEGIGPKSDAVYEMVKSFKAQGIPIDGVGMQAHLIAGQVPASLQENIRRFADLGVDVALTELDIRMTLPRTAAKDAQQATDYGAVVEACLVVSRCVGITVWDYTDKYSWVPSVFPGQGAALPWDEDFAKKPAYHAIAAALNGGSPAPGGNCTATYRVTSQWQGGFTAEITVGNDHTAPITGWTVTWTLSSGQSISHMWNGNLTVNGQDVTVRDVGYNGTLGGNGSTTFGFQGEGVADTPADVTCTPGRPSGTSA
Enzyme Length 464
Uniprot Accession Number B4XVN1
Absorption
Active Site ACT_SITE 166; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 271; /note=Nucleophile; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Completely inhibited by Hg(2+), unaffected by EDTA. {ECO:0000269|PubMed:18521591}.
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 hydrolysis of hemicellulose, the major component of plant cell-walls. Hydrolyzes xylan to xylose and xylobiose. {ECO:0000269|PubMed:18521591}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius, more than 80% of activity remains after 1 hour at 60 degrees Celsius. {ECO:0000269|PubMed:18521591};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5, more than 80% active between pH 5.0 and 7.0. {ECO:0000269|PubMed:18521591};
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Beta strand (13); Chain (1); Domain (2); Helix (16); Signal peptide (1); Turn (2)
Keywords 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Signal;Xylan degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..33; /evidence=ECO:0000255
Structure 3D X-ray crystallography (4)
Cross Reference PDB 3WUB; 3WUE; 3WUF; 3WUG;
Mapped Pubmed ID 25193708;
Motif
Gene Encoded By
Mass 49,868
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=772.20 umol/min/mg enzyme for oat spelt xylan {ECO:0000269|PubMed:18521591}; Vmax=490.87 umol/min/mg enzyme for birchwood xylan {ECO:0000269|PubMed:18521591};
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.8;