IED ID | IndEnz0008000586 |
Enzyme Type ID | cellulase000586 |
Protein Name |
Endo-1,4-beta-xylanase C Xylanase C EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase C |
Gene Name | xynC |
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 | MKFLQIIPVLLSLTSTTLAQSFCSSASHSGQSVKETGNKVGTIGGVGYELWADSGNNSATFYSDGSFSCTFQNAGDYLCRSGLSFDSTKTPSQIGRMKADFKLVKQNISNVGYSYVGVYGWTRSPLVEYYIVDNWLSPSPPGDWVGNKKHGSFTIDGAQYTVYENTRTGPSIDGNTTFKQYFSIRQQARDCGTIDISAHFDQWEKLGMTMGKLHEAKVLGEAGNGNGGVSGTADFPYAKVYIGDGNGGGASPAPAGGAPAGGAPAGNDQPQGPQGQQPPQGQQPPQGQQPPQGQQPPQGQQPPQGNDQQGQQPPQGQQPPQGNDQHQGQHPPQPQGPQGGNPGGSDFNNWSQGGSPWGGNQGGSPWGGNQGGNPWGGNQGGSPWGGNQGGSPWGQGNQGGNPWGGNQGGSPWGGNQGGNPWGGNQWGAPQNAAAPQSAAAPQNASDGGNCASLWGQCGGQGYNGPSCCSEGSCKPINEYFHQCQK |
Enzyme Length | 485 |
Uniprot Accession Number | Q9UV68 |
Absorption | |
Active Site | ACT_SITE 128; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 221; /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:10588045}; |
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:10588045}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Beta strand (16); Chain (1); Compositional bias (2); Domain (2); Glycosylation (5); Helix (4); Region (3); Repeat (15); Signal peptide (1); Turn (1) |
Keywords | 3D-structure;Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Secreted;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 3WP4; 3WP5; 3WP6; |
Mapped Pubmed ID | 24619408; |
Motif | |
Gene Encoded By | |
Mass | 50,192 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.8; |