| IED ID | IndEnz0008000455 |
| Enzyme Type ID | cellulase000455 |
| Protein Name |
Endo-beta-1,4-xylanase Xyn10C Xylanase 10C EC 3.2.1.8 XYLF |
| Gene Name | xyn10C xynF |
| Organism | Cellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Cellvibrionales Cellvibrionaceae Cellvibrio Cellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa) |
| Enzyme Sequence | MKKIQQLLMLSLISSTLIACGGGGGGGSTPTTSSSPQSSSPASTPSSASSSSIISSSSLSSSLSSSSLSSSSLSSSSASSVSSSSVAASEGNVVIEVDMANGWRGNASGSTSHSGITYSADGVTFAALGDGVGAVFDIARPTTLEDAVIAMVVNVSAEFKASEANLQIFAQLKEDWSKGEWDCLAASSELTADTDLTLTCTIDEDDDKFNQTARDVQVGIQAKGTPAGTITIKSVTITLAQEAYSANVDHLRDLAPSDFPIGVAVSNTDSATYNLLTNSREQAVVKKHFNHLTAGNIMKMSYMQPTEGNFNFTNADAFVDWATENNMTVHGHALVWHSDYQVPNFMKNWAGSAEDFLAALDTHITTIVDHYEAKGNLVSWDVVNEAIDDNSPANFRTTDSAFYVKSGNSSVYIERAFQTARAADPAVILYYNDYNIEQNNAKTTKMVDMVKDFQARSIPIDGVGFQMHVCMNYPSIANISAAMKKVVDLGLLVKITELDVAVNQPHCDAYPANKINPLTEAAQLAQKKRYCDVVKAYLDTVPVNQRGGISVWGTTDANTWLDGLYREQFEDEKISWPLLFDNNYNDKPALRGFADALIGTQCTNTH |
| Enzyme Length | 606 |
| Uniprot Accession Number | Q59675 |
| Absorption | |
| Active Site | ACT_SITE 385; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 497; /note=Nucleophile; /evidence=ECO:0000305|PubMed:14670951 |
| Activity Regulation | |
| Binding Site | BINDING 106; /note=Carbohydrate; BINDING 171; /note=Carbohydrate; BINDING 217; /note=Carbohydrate; BINDING 332; /note=Substrate; BINDING 384; /note=Substrate; BINDING 552; /note=Substrate |
| 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:14670951, ECO:0000269|PubMed:7492333}; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan, the arabinoxylans from wheat and rye, and glucuronoxylan. Also displays very low activity against xylooligosaccharides. During the xylan degradation process, Xyn10C may act on the soluble xylans and long xylooligosaccharides products released by the secreted xylanases Xyn11A, Xyn11B and Xyn10A. {ECO:0000269|PubMed:14670951, ECO:0000269|PubMed:7492333}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (28); Binding site (6); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (2); Helix (18); Lipidation (2); Mutagenesis (1); Region (2); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cell outer membrane;Disulfide bond;Glycosidase;Hydrolase;Lipoprotein;Membrane;Palmitate;Polysaccharide degradation;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Induced when the bacterium is cultured on xylan or beta-glucan but not on medium containing mannan. Is repressed by glucose. {ECO:0000269|PubMed:12107129}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305|PubMed:12107129}; Lipid-anchor {ECO:0000305|PubMed:12107129}. Note=Is predominantly associated with the cell membrane. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255|PROSITE-ProRule:PRU00303 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1GNY; 1US2; 1US3; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 64,884 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |