Detail Information for IndEnz0008000578
IED ID IndEnz0008000578
Enzyme Type ID cellulase000578
Protein Name Endo-1,4-beta-xylanase S20
Xylanase S20
EC 3.2.1.8
1,4-beta-D-xylan xylanohydrolase S20
Gene Name xynS20
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 MLRKLVTGALAAALLLSGQSNAQNACQQTQQLSGGRTINNKNETGNGNGNYKYEIWRDGNGGSLTLYPKDAAFKASWNNSGDFLGRVGLTFNKPAATNLGGDLIANYNYKKSGSDGGTYSYIGIYGWMDNPQIEYYVVDDWMHNRGAPGGSYMGSQKGTITVDGGTYKVWSGQRTGASKWGTSTFTQIFSIRTSPRQCGSINVSEHFRQWQKLGLRLGGLMEAQLLAESGGGSGYVDFTYATITIGGSSSNASAPSNNNNNNNNNNDNNGNWNNWNNNNNNNNNNNNNNNNNNNNQGGGNCAAIWGQCGGSGYNGPKCCKQGSCKQINQWYSQCQ
Enzyme Length 335
Uniprot Accession Number A8TGA1
Absorption
Active Site ACT_SITE 134; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 228; /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; Evidence={ECO:0000269|PubMed:18415096};
DNA Binding
EC Number 3.2.1.8
Enzyme Function FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. {ECO:0000269|PubMed:18415096}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius.;
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0.;
Pathway PATHWAY: Glycan degradation; xylan degradation.
nucleotide Binding
Features Active site (2); Chain (1); Domain (2); Glycosylation (4); Region (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18415096}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 36,094
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.9 mg/ml for oat spelt xylan; Vmax=3.886 umol/min/mg enzyme toward oat spelt xylan;
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.8;