| IED ID | IndEnz0008000525 |
| Enzyme Type ID | cellulase000525 |
| 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 | Paenibacillus barcinonensis |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus Paenibacillus barcinonensis |
| Enzyme Sequence | MRGKWLRLCLAAVLIVSLLPGLGAGEWKASAAKAGDILLSHSFEEGTTQGWTARGGVKVDVTAEQAYQGKQSLQTTGRTEAWNGPSLSLTDVVHKNEVVEISGYVKLVAGSAPPDLKFTVERRDRNGDTQYDQVNAAEQVTDQKWVKLQGQYSYEQGSSLLLYLESTDAKAAYLLDEFQIRLVKAAPENPGEPGEAGQALFKAYFEDGNIGNWRARGTEKLEVVSGIGHNSNRSLKTSSRSETYHGPLVEVLPYLQKGSTVHISFWAMYDEGPATQVINGSLEKEFNRDTANLEYAMFASTTLNKGQWKKIEADIIVPAESTGISGLRMYAETPWKQSSEVTETDTIPFYVDDVQITATEAIAIEKNIPDLAKKLGSSYALGAAIDQTALDPKDPHSELLTKHFNSITAGNFMKMDAMQPTEGKFVWSEADKLVNFAAANNMQVRGHTLLWHSQVPDWFFTDPNDPSKPATREQLMQRMKTHIQTIVSRYKGKVHTWDVVNEVISDGGGLRNQASGSKWRDIIGDVDGDGDDSDYIELAFRYAREADPDAVLVINDYGIEGSVSKMNDMVKLVEKLLAKGTPIDAIGFQMHVSMYGPDIKQIREAFNRAAALGVHIQVTELDMSIYSGNSEQEKPVTDEMMLEQAYRYRALFDLFKEFDDRGVMDSVTLWGLADDGTWLDDFPVKGRKDAPLLFDRKLKAKPAYWALVDPSTLPVYRNEWTASQAKVSLPDRKGQEDIIWGAVRALPFSHVIEGAVGTTGEVKTLWDGKQLNLRIEVKDATRLKGDQVEVFVSPEDMTAGKKNSTPKDGQYIFNRDGGKGKDQKLYQVKENKSGYVVYASLPLSSADLAAGKVLSLDFRITDKQPNGKTSIVVWNDVNNQQPQKTENRGKLKLGFDLKHAKVMYGTPTVDGKEDKLWKKAVTITTDVKVTGNSGAKAKAKLLWDEKYLYVLAEVKDPLLSKKSANAHEQDSIELFIDLNKNQTNSYEEDDAQYRVNFDNETSFGGSPRKELFKSATRLTKEGYIVEAAIPLENVRTKESKWIGFDLQVNDDGAGDGKRSSVFMWSDPSGNSYRDTSGFGSLLLMKK |
| Enzyme Length | 1086 |
| Uniprot Accession Number | O69230 |
| Absorption | |
| Active Site | ACT_SITE 502; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 556; /evidence=ECO:0000250; ACT_SITE 620; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10061 |
| 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:10463183}; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Endoxylanase with high hydrolytic activity on birchwood and oat spelt xylan. Xylotetraose, xylotriose, xylobiose and xylose are the main products from birchwood xylan hydrolysis. Shows increasing activity on xylo-oligosaccharides of increasing length. Displays very low hydrolytic activity on Avicel, carboxymethylcellulose (CMC) and p-nitrophenyl-beta-xylopyranoside. Also shows transxylosidase activity, allowing the formation of xylo-oligosaccharides of higher degree of polymerization than the starting substrate. {ECO:0000269|PubMed:10463183}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Is only stable at 55 degrees Celsius or lower temperatures. Retains more than 77% activity after 2 hours incubation at 55 degrees Celsius and pH 7. {ECO:0000269|PubMed:10463183}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. Retains at least 50% of its maximum activity between pH 4.5 and 8.0. Is not active at pH values below 4.5, while at least 35% of maximum activity is found in the pH range 8.5-11.0. {ECO:0000269|PubMed:10463183}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (39); Chain (1); Domain (3); Helix (21); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 4W8L; 4XUN; 4XUO; 4XUP; 4XUQ; 4XUR; 4XUT; |
| Mapped Pubmed ID | 25664784; 26001782; |
| Motif | |
| Gene Encoded By | |
| Mass | 120,586 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |