| IED ID | IndEnz0008000474 |
| Enzyme Type ID | cellulase000474 |
| Protein Name |
Bifunctional xylanase/deacetylase Includes: Endo-1,4-beta-xylanase 11A EC 3.2.1.8 Xylanase XynT Xylanase xyn11A ; Acetylated xylan deacetylase EC 3.5.1.- |
| Gene Name | xyn11A xynT |
| Organism | Pseudobutyrivibrio xylanivorans |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Lachnospiraceae Pseudobutyrivibrio Pseudobutyrivibrio xylanivorans |
| Enzyme Sequence | MSATLLVPSMTVKAADTIYNNKTGNQDGYDYELWKDTGNTSMTLNAGGTFDCSWSNINNALFRKGKKFDSTQTYQQIGNITFDYGCDYRPNGNSYLCVYGWTVDPLVEYYIVDSWGTWRPPGGTPKGQIQVDGGTYDVYETTRYNAPSIQGDTTFKQYFSVRTSKRTSGTISVSEHFKAWERMGMRCGNFMKPALNIEGYQSSGSASVYKNNMTIGGSSSSSGNQGGNQGGNTGNENAGNNLVTVADADKIQCETMTKSGQYTGNISSPFNGVALYANNDAVKYTQYFASGTHDFTLRGCSNNNKMARVDLKIGGQNKGTFYYGDSYPAEYTIKNVSHGTGNQTIELVVTADDGQWDAYLDYFNNSVEPGCSLVPGAVVVLVALGSSSNTGNNSGTNTQNQKLIALTFDDGPSSTTSQVLDMLEKYNVKATFFLIGQNVNSNTASIVQRQVKMGCELACHSYTHEDMTKMNASQIRNQIDWTASAIKNTAGVDVKFFRPPYISVNNTMYQNIDLPFIQGSMHNDWESSTSASQRVNSVLSSAKDGDIILLHDFQGNSQTVSALPQIIEGLKNQGYTFVTVSELFEMKGVNPNVEYKIWSNVK |
| Enzyme Length | 602 |
| Uniprot Accession Number | P83513 |
| Absorption | |
| Active Site | ACT_SITE 108; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 198; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063 |
| 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|Ref.2}; |
| DNA Binding | |
| EC Number | 3.2.1.8; 3.5.1.- |
| Enzyme Function | FUNCTION: Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is also probably able, via its C-terminal domain, to remove acetyl groups from acetylated xylan, and thus it is probably capable of hydrolyzing acetylated xylan. {ECO:0000269|Ref.2}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 38 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.6. Active from pH 4.0 to 8.0.; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (3); Region (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Multifunctional enzyme;Polysaccharide degradation;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2, ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: In the later growth phases, seems to undergo a proteolytic cleavage into a 30 kDa protein possessing xylanolytic activity. |
| Signal Peptide | SIGNAL 1..14; /evidence=ECO:0000269|Ref.2 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 65,923 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |