| IED ID | IndEnz0004000057 |
| Enzyme Type ID | xylanase000057 |
| Protein Name |
Reducing end xylose-releasing exo-oligoxylanase Rex EC 3.2.1.156 |
| Gene Name | BH2105 |
| Organism | Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Alkalihalobacillus Alkalihalobacillus halodurans (Bacillus halodurans) Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans) |
| Enzyme Sequence | MKKTTEGAFYTREYRNLFKEFGYSEAEIQERVKDTWEQLFGDNPETKIYYEVGDDLGYLLDTGNLDVRTEGMSYGMMMAVQMDRKDIFDRIWNWTMKNMYMTEGVHAGYFAWSCQPDGTKNSWGPAPDGEEYFALALFFASHRWGDGDEQPFNYSEQARKLLHTCVHNGEGGPGHPMWNRDNKLIKFIPEVEFSDPSYHLPHFYELFSLWANEEDRVFWKEAAEASREYLKIACHPETGLAPEYAYYDGTPNDEKGYGHFFSDSYRVAANIGLDAEWFGGSEWSAEEINKIQAFFADKEPEDYRRYKIDGEPFEEKSLHPVGLIATNAMGSLASVDGPYAKANVDLFWNTPVRTGNRRYYDNCLYLFAMLALSGNFKIWFPEGQEEEH |
| Enzyme Length | 388 |
| Uniprot Accession Number | Q9KB30 |
| Absorption | |
| Active Site | ACT_SITE 70; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:A0A0S2UQQ5; ACT_SITE 263; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:A0A0S2UQQ5 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides.; EC=3.2.1.156; Evidence={ECO:0000269|PubMed:15491996}; |
| DNA Binding | |
| EC Number | 3.2.1.156 |
| Enzyme Function | FUNCTION: Hydrolyzes xylooligosaccharides with a degree of polymerization of greater than or equal to 3, releasing xylose from the reducing end. Only hydrolyzes the beta anomers of xylooligosaccharides, with inversion of anomeric configuration. Hydrolyzes the glucose and xylose-based trisaccharides where xylose is located at the -1 subsite, GXX, XXG and GXG. Does not hydrolyze xylan, chitosan, lichenan, curdlan or carboxymethylcellulose. {ECO:0000269|PubMed:15491996}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Stable up to 40 degrees Celsius. {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.2-7.3. Stable between pH 5.0 and 9.8 for 30 min at 30 degrees Celsius. {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (12); Chain (1); Helix (19); Mutagenesis (6); Sequence conflict (1); Turn (6) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 1WU4; 1WU5; 1WU6; 2DRO; 2DRQ; 2DRR; 2DRS; 3A3V; |
| Mapped Pubmed ID | 16511021; 19819900; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,010 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.4 mM for X3 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312}; KM=5.0 mM for X4 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312}; KM=4.4 mM for X5 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312}; KM=18.5 mM for X6 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312}; KM=4.3 mM for X3 (in 0.1 M MOPS, pH 7.0, 30 degrees Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.156; |