| IED ID | IndEnz0004000068 |
| Enzyme Type ID | xylanase000068 |
| Protein Name |
Glucuronoxylanase XynC EC 3.2.1.136 Endoxylanase XynC Glucuronoxylan xylanohydrolase |
| Gene Name | xynC ynfF BSU18150 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MIPRIKKTICVLLVCFTMLSVMLGPGATEVLAASDVTVNVSAEKQVIRGFGGMNHPAWAGDLTAAQRETAFGNGQNQLGFSILRIHVDENRNNWYKEVETAKSAVKHGAIVFASPWNPPSDMVETFNRNGDTSAKRLKYNKYAAYAQHLNDFVTFMKNNGVNLYAISVQNEPDYAHEWTWWTPQEILRFMRENAGSINARVIAPESFQYLKNLSDPILNDPQALANMDILGTHLYGTQVSQFPYPLFKQKGAGKDLWMTEVYYPNSDTNSADRWPEALDVSQHIHNAMVEGDFQAYVWWYIRRSYGPMKEDGTISKRGYNMAHFSKFVRPGYVRIDATKNPNANVYVSAYKGDNKVVIVAINKSNTGVNQNFVLQNGSASNVSRWITSSSSNLQPGTNLTVSGNHFWAHLPAQSVTTFVVNR |
| Enzyme Length | 422 |
| Uniprot Accession Number | Q45070 |
| Absorption | |
| Active Site | ACT_SITE 171; /note=Proton donor; /evidence=ECO:0000269|PubMed:21256135; ACT_SITE 260; /note=Nucleophile; /evidence=ECO:0000269|PubMed:21256135 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.; EC=3.2.1.136; |
| DNA Binding | |
| EC Number | 3.2.1.136 |
| Enzyme Function | FUNCTION: Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA). {ECO:0000269|PubMed:17028274}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. Half the activity is retained for 25 hours at 40 degrees Celsius and for 5 hours at 50 degrees Celsius. {ECO:0000269|PubMed:17028274}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:17028274}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (22); Chain (1); Helix (16); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:17028274}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15187182}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 3GTN; 3KL0; 3KL3; 3KL5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,337 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=59.5 umol/min/mg enzyme with methylglucuronoxylan from sweetgum as substrate (at 37 degrees Celsius and pH 6) {ECO:0000269|PubMed:17028274}; Note=The Km value for methylglucuronoxylan from sweetgum is 1.63 mg/ml. The activity is directly correlated to the degree of substitution of the glucuronosyl moiety on the xylan chain.; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.136; |