Detail Information for IndEnz0008000429
IED ID IndEnz0008000429
Enzyme Type ID cellulase000429
Protein Name Endo-1,4-beta-xylanase A
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase
Xylanase A
XYLA
Gene Name XYNA
Organism Piromyces sp.
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Chytridiomycota Chytridiomycota incertae sedis Neocallimastigomycetes Neocallimastigales Neocallimastigaceae Piromyces unclassified Piromyces Piromyces sp.
Enzyme Sequence MKLFQIFPLLLSLTSVTLAADDFCNATGFQGQSVVSTGHDVKKIGNIDYEQWADGGNNSATFYSDGSFKCNFSNTKDYLCRSGVAFSQAKYPSEIGHIEAEYRLVKKSASNVGYSYVGVYGWTLQSGISGVYEYYIVDNWLSQWRPGDWVGNTKFGDFTIDGGVYTVYKNVNGNLTQYFSLRKSERTCGTIDVTAHFAQWEKLGLKMPKITEIKVLAEAGNTGGGCSGSVEIPYAKIYINGKDQDGKSKGGSSSGGSNGQGLGNGQGNGQGQGNGQGQSATGSGKCPSTITSQGYKCCSSNCDIIYRDQSGDWGVENDEWCGCGSRVPKTTNCPSSIKNQGYKCCSDSCEIVLTDSDGDWGIENDEWCGCGIKNTTPTTTTKKSNNSQPTQGQSNNNSSTNTNFCSTSKHSGQSVTETSNKVGSIGGVGYELWADSGNNSATFYSDGSFSCSFRNAKDYLCRSGLSFDSTKTYQQLGHMYADFKLVKQNIQNVDYSYVGIYGWTRNPLVEFYVVDNWLSQWRPGDWVGNKKHGDFTIDGAKYTVYENTRTGPSIDGNTTFKQYFSIRQQARDCGTIDITAHFEQWEKLGMRMGKMHEAKVLGEAGSTGSGTSGTADFPYAKVYIK
Enzyme Length 625
Uniprot Accession Number Q12667
Absorption
Active Site ACT_SITE 510; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 603; /note=Proton donor; /evidence=ECO:0000250
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: Hydrolyzes 1,4-beta linked polysaccharide backbones of xylans, one of the major hemicellulose components in hardwoods and softwoods. It is more active against xylopentaose than xylotetraose, has trace activity against xylotriose. The major products released from hydrolysis of xylooligosaccharides are xylobiose and xylotriose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Chain (1); Compositional bias (1); Domain (4); Region (5); Repeat (2); Signal peptide (1)
Keywords Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Signal;Xylan degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 68,049
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda