Detail Information for IndEnz0004000220
IED ID IndEnz0004000220
Enzyme Type ID xylanase000220
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