| IED ID | IndEnz0008000539 |
| Enzyme Type ID | cellulase000539 |
| Protein Name |
Endo-1,4-beta-xylanase A EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase A Xylanase 11A Xyn11A |
| 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 | MKRKVKKMAAMATSIIMAIMIILHSIPVLAGRIIYDNETGTHGGYDYELWKDYGNTIMELNDGGTFSCQWSNIGNALFRKGRKFNSDKTYQELGDIVVEYGCDYNPNGNSYLCVYGWTRNPLVEYYIVESWGSWRPPGATPKGTITVDGGTYEIYETTRVNQPSIDGTATFQQYWSVRTSKRTSGTISVTEHFKQWERMGMRMGKMYEVALTVEGYQSSGYANVYKNEIRIGANPTPAPSQSPIRRDAFSIIEAEEYNSTNSSTLQVIGTPNNGRGIGYIENGNTVTYSNIDFGSGATGFSATVATEVNTSIQIRSDSPTGTLLGTLYVSSTGSWNTYQTVSTNISKITGVHDIVLVFSGPVNVDNFIFSRSSPVPAPGDNTRDAYSIIQAEDYDSSYGPNLQIFSLPGGGSAIGYIENGYSTTYNNVNFANGLSSITARVATQISTSIQVRAGGATGTLLGTIYVPSTNSWDSYQNVTANLSNITGVHDITLVFSGPVNVDYFVFTPANVNSGPTSPVGGTRSAFSNIQAEDYDSSYGPNLQIFSLPGGGSAIGYIENGYSTTYKNIDFGDGATSVTARVATQNATTIQVRLGSPSGTLLGTIYVGSTGSFDTYRDVSATISNTAGVKDIVLVFSGPVNVDWFVFSKSGT |
| Enzyme Length | 651 |
| Uniprot Accession Number | Q8GJ44 |
| Absorption | |
| Active Site | ACT_SITE 124; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 214; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063 |
| Activity Regulation | |
| Binding Site | BINDING 270; /note="D-xylotriose 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY3"; BINDING 279; /note="D-xylobiose; via amide nitrogen"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY2"; BINDING 279; /note="D-xylotriose 1; via amide nitrogen"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY3"; BINDING 336; /note="D-xylobiose"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY2"; BINDING 336; /note="D-xylotriose 1"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY3"; BINDING 363; /note="D-xylobiose"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY2"; BINDING 363; /note="D-xylotriose 1"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY2"; BINDING 556; /note="D-xylotriose 2; via amide nitrogen"; /evidence="ECO:0000269|PubMed:12634060, ECO:0007744|PDB:1NAE"; BINDING 613; /note="D-xylotriose 2"; /evidence="ECO:0000269|PubMed:12634060, ECO:0007744|PDB:1NAE"; BINDING 640; /note="D-xylotriose 2"; /evidence="ECO:0000269|PubMed:12634060, ECO:0007744|PDB:1NAE" |
| 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 | FUNCTION: Endoxylanase that degrades arabinoxylan and glucuronoxylan to xylobiose and xylotriose (in vitro). {ECO:0000269|PubMed:11849546, ECO:0000269|PubMed:15256568}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius. Thermostable. {ECO:0000269|PubMed:15256568}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:15256568}; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (21); Binding site (10); Chain (1); Domain (4); Metal binding (8); Region (1); Repeat (3); Sequence conflict (1); Signal peptide (1) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Metal-binding;Polysaccharide degradation;Repeat;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: Up-regulated by growth on xylan. {ECO:0000269|PubMed:15256568}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15256568}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 1NAE; 1O8P; 1O8S; 1OD3; 1UY1; 1UY2; 1UY3; 1UY4; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 70,151 |
| Kinetics | |
| Metal Binding | METAL 253; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2, ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4"; METAL 255; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2, ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4"; METAL 275; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2, ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4"; METAL 365; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:15223327, ECO:0007744|PDB:1UY1, ECO:0007744|PDB:1UY2, ECO:0007744|PDB:1UY3, ECO:0007744|PDB:1UY4"; METAL 530; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12634060, ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P, ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3"; METAL 532; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12634060, ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P, ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3"; METAL 552; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:12634060, ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P, ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3"; METAL 642; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:12634060, ECO:0007744|PDB:1NAE, ECO:0007744|PDB:1O8P, ECO:0007744|PDB:1O8S, ECO:0007744|PDB:1OD3" |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.8; |