Detail Information for IndEnz0004000127
IED ID IndEnz0004000127
Enzyme Type ID xylanase000127
Protein Name Endo-1,4-beta-xylanase A
Xylanase A
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase A
Gene Name xynA BSU18840
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MFKFKKNFLVGLSAALMSISLFSATASAASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTTGSPFRTINYNAGVWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKGTVKSDGGTYDIYTTTRYNAPSIDGDRTTFTQYWSVRQSKRPTGSNATITFSNHVNAWKSHGMNLGSNWAYQVMATEGYQSSGSSNVTVW
Enzyme Length 213
Uniprot Accession Number P18429
Absorption
Active Site ACT_SITE 106; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:7911679"; ACT_SITE 200; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
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
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Beta strand (13); Chain (1); Domain (1); Helix (1); Mutagenesis (2); Signal peptide (1); Turn (1)
Keywords 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Signal;Xylan degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..28
Structure 3D X-ray crystallography (15)
Cross Reference PDB 1AXK; 1XXN; 2B42; 2B45; 2B46; 2DCY; 2DCZ; 2QZ3; 2Z79; 3EXU; 3HD8; 5K9Y; 5TVV; 5TVY; 5TZO;
Mapped Pubmed ID 16289057; 16467302; 17983355; 19422059; 19769747; 28109807; 28925919; 9618460;
Motif
Gene Encoded By
Mass 23,345
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.8;