Detail Information for IndEnz0008000543
IED ID IndEnz0008000543
Enzyme Type ID cellulase000543
Protein Name Bifunctional endo-1,4-beta-xylanase A
XYLA
EC 3.2.1.8
Gene Name XYNA
Organism Neocallimastix patriciarum (Rumen fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Fungi incertae sedis Chytridiomycota Chytridiomycota incertae sedis Neocallimastigomycetes Neocallimastigales Neocallimastigaceae Neocallimastix Neocallimastix patriciarum (Rumen fungus)
Enzyme Sequence MRTIKFFFAVAIATVAKAQWGGGGASAGQRLTVGNGQTQHKGVADGYSYEIWLDNTGGSGSMTLGSGATFKAEWNASVNRGNFLARRGLDFGSQKKATDYSYIGLDYTATYRQTGSASGNSRLCVYGWFQNRGVQGVPLVEYYIIEDWVDWVSDAQGRMVTIDGAQYKIFQMDHTGPTINGGSETFKQYFSVRQQKRTSGHITVSDHFKEWAKQGWGIGNLYEVALNAEGWQSSGIADVTKLDVYTTQKGSNPAPTSTGTVPSSSAGGSTANGKKFTVGNGQNQHKGVNDGFSYEIWLDNTGGNGSMTLGSGATFKAEWNAAVNRGNFLARRGLDFGSQKKATDYDYIGLDYAATYKQTASASGNSRLCVYGWFQNRGLNGVPLVEYYIIEDWVDWVPDAQGKMVTIDGAQYKIFQMDHTGPTINGGSETFKQYFSVRQQKRTSGHITVSDHFKEWAKQGWGIGNLYEVALNAEGWQSSGVADVTLLDVYTTPKGSSPATSAAPRTTTRTTTRTKSLPTNYNKCSARITAQGYKCCSDPNCVVYYTDEDGTWGVENNDWCGCGVEQCSSKITSQGYKCCSDPNCVVFYTDDDGKWGVENNDWCGCGF
Enzyme Length 607
Uniprot Accession Number P29127
Absorption
Active Site ACT_SITE 141; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 223; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063; ACT_SITE 386; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 474; /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 FUNCTION: Hydrolyzes xylans into xylobiose and xylose.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (4); Beta strand (13); Chain (1); Domain (4); Helix (2); Region (2); Signal peptide (1); Turn (1)
Keywords 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Repeat;Signal;Xylan degradation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D X-ray crystallography (2)
Cross Reference PDB 2C1F; 2VG9;
Mapped Pubmed ID 18078955;
Motif
Gene Encoded By
Mass 66,175
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.8;