| IED ID | IndEnz0004000138 |
| Enzyme Type ID | xylanase000138 |
| Protein Name |
Glucuronoxylanase XynC EC 3.2.1.136 Endoxylanase XynC Glucuronoxylan xylanohydrolase |
| Gene Name | xynC ynfF |
| Organism | Bacillus subtilis |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis |
| Enzyme Sequence | MMSSVKKTICVLLVCFTMMSVMLLGPGVTEVSAASDAKVNISADRQVIRGFGGMNHPAWIGDLTAAQRETAFGNGQNQLGFSVLRIHVDENRNNWYKEVETAKSAIKHGAIVFASPWNPPNDMVETFNHNGDTSAKRLRYDKYAAYAQHLNDFVNFMKSNGVNLYAISMQNEPDYAHEWTWWTPQEILRFMRENAGSINARVIAPESFQYLKNISDPILNDPQALRNMDILGTHLYGTQVSQFPYPLFKQKGGGKELWMTEVYYPNSDNNSADRWPEALGVSEHIHHSMVEGDFQAYVWWYIRRSYGPMKEDGMISKRGYNMAHFSKFVRPGYVRIDATKNPEPNVYVSAYKGDNKVVIVAINKNNTGVNQNFVLQNGTASQVSRWITSSSSNLQPGTDLKVTDNHFWAHLPAQSVTTFVVKR |
| Enzyme Length | 423 |
| Uniprot Accession Number | Q6YK37 |
| Absorption | |
| Active Site | ACT_SITE 172; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 261; /note=Nucleophile; /evidence=ECO:0000250 |
| 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). 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) (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Frameshift (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,840 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |