| IED ID | IndEnz0004000100 |
| Enzyme Type ID | xylanase000100 |
| Protein Name |
Endo-1,4-beta-xylanase A Xylanase A EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase A |
| Gene Name | xynA |
| Organism | Thermoclostridium stercorarium (Clostridium stercorarium) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Oscillospiraceae Thermoclostridium Thermoclostridium stercorarium (Clostridium stercorarium) |
| Enzyme Sequence | MKRKVKKMAAMATSIIMAIMIILHSIPVLAGRIIYDNETGTHGGYDYELWKDYGNTIMELNDGGTFSCQWSNIGNALFRKGRKFNSDKTYQELGDIVVEYGCDYNPNGNSYLCVYGWTRNPLVEYYIVESWGSWRPPGATPKGTITQWMAGTYEIYETTRVNQPSIDGTATFQQYWSVRTSKRTSGTISVTEHFKQWERMGMRMGKMYEVALTVEGYQSSGYANVYKNEIRIGANPTPAPSQSPIRRDAFSIIEAEEYNSTNSSTLQVIGTPNNGRGIGYIENGNTVTYSNIDFGSGATGFSATVATEVNTSIQIRSDSPTGTLLGTLYVSSTGSWNTYQTVSTNISKITGVHDIVLVFSGPVNVDNFIFSRSSPVPAPGDNTRDAYSIIQAEDYDSSYGPNLQIFSLPGGGSAIGYIENGYSTTYKNIDFGDGATSVTARVATQNATTIQVRLGSPSGTLLGTIYVGSTGSFDTYRDVSATISNTAGVKDIVLVFSGPVNVDWFVFSKSGT |
| Enzyme Length | 512 |
| Uniprot Accession Number | P33558 |
| Absorption | |
| Active Site | ACT_SITE 124; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 215; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063 |
| Activity Regulation | |
| Binding Site | BINDING 271; /note=Substrate 1; via carbonyl oxygen; /evidence=ECO:0000250; BINDING 280; /note=Substrate 1; via amide nitrogen; /evidence=ECO:0000250; BINDING 337; /note=Substrate 1; /evidence=ECO:0000250; BINDING 364; /note=Substrate 1; /evidence=ECO:0000250; BINDING 417; /note=Substrate 2; via amide nitrogen; /evidence=ECO:0000250; BINDING 474; /note=Substrate 2; /evidence=ECO:0000250; BINDING 501; /note=Substrate 2; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Thermostable.; |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Domain (3); Metal binding (8); Region (1); Repeat (2); Signal peptide (1) |
| Keywords | Calcium;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Polysaccharide degradation;Repeat;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,843 |
| Kinetics | |
| Metal Binding | METAL 254; /note=Calcium 1; /evidence=ECO:0000250; METAL 256; /note=Calcium 1; /evidence=ECO:0000250; METAL 276; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 366; /note=Calcium 1; /evidence=ECO:0000250; METAL 391; /note=Calcium 2; /evidence=ECO:0000250; METAL 393; /note=Calcium 2; /evidence=ECO:0000250; METAL 413; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 503; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |