| IED ID | IndEnz0004000059 |
| Enzyme Type ID | xylanase000059 |
| 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; |