| IED ID | IndEnz0008000594 |
| Enzyme Type ID | cellulase000594 |
| 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 | Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium funiculosum) |
| Enzyme Sequence | MKLFLAAIVLCATAATAFPSELAQRAAGDLSKRQSITTSQTGTNNGYYYSFWTNGGGEVTYTNGDNGEYSVTWVDCGDFTSGKGWNPANAQTVTYSGEFNPSGNAYLAVYGWTTDPLVEYYILESYGTYNPSSGLTSLGQVTSDGGTYDIYSTQRVNQPSIEGTSTFNQYWSVRTEKRVGGTVTTANHFAAWKALGLEMGTYNYMIVSTEGYESSGSSTITVS |
| Enzyme Length | 223 |
| Uniprot Accession Number | Q9HFH0 |
| Absorption | |
| Active Site | ACT_SITE 119; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 210; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by wheat xylanase inhibiting protein I (XIP-I), and by proteinaceous endoxylanase Triticum aestivum xylanase inhibitors I and II (TAXI-I and TAXI-II). {ECO:0000269|PubMed:12147340, ECO:0000269|PubMed:17216454}. |
| 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:12147340, ECO:0000269|PubMed:17216454}; |
| 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. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:12147340, ECO:0000269|PubMed:17216454}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:12147340, ECO:0000269|PubMed:17216454}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (13); Chain (1); Domain (1); Helix (1); Region (4); Signal peptide (1); Site (3); Turn (2) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12147340}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1TE1; 3WP3; |
| Mapped Pubmed ID | 25138599; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,045 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=2540 umol/min/mg enzyme toward birchwood xylan at pH 5.5 and 30 degrees Celsius {ECO:0000269|PubMed:12147340, ECO:0000269|PubMed:17216454}; Vmax=7190 umol/min/mg enzyme toward soluble wheat arabinoxylans at pH 5.5 and 30 degrees Celsius {ECO:0000269|PubMed:12147340, ECO:0000269|PubMed:17216454}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |