| IED ID | IndEnz0004000199 |
| Enzyme Type ID | xylanase000199 |
| Protein Name |
Endo-1,4-beta-xylanase A Xylanase A EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase A Endoxylanase |
| Gene Name | xynA |
| Organism | Thermotoga neapolitana |
| Taxonomic Lineage | cellular organisms Bacteria Thermotogae Thermotogae Thermotogales Thermotogaceae Thermotoga Thermotoga neapolitana |
| Enzyme Sequence | MRKKRRGFLNASTAVLVGILAGFLGVVLAATGALGFAVRESLLLKQFLFLSFEGNTDGASPFGKDVVVTASQDVAADGEYSLKVENRTSVWDGVEIDLTGKVNTGTDYLLSFHVYQTSDSPQLFSVLARTEDEKGERYKILADKVVVPNYWKEILVPFSPTFEGTPAKFSLIITSPKKTDFVFYVDNVQVLTPKEAGPKVVYETSFEKGIGDWQPRGSDVKISISPKVAHSGKKSLFVSNRQKGWHGAQISLKGILKTGKTYAFEAWVYQESGQDQTIIMTMQRKYSSDSSTKYEWIKAATVPSGQWVQLSGTYTIPAGVTVEDLTLYFESQNPTLEFYVDDVKVVDTTSAEIKLEMNPEEEIPALKDVLKDYFRVGVALPSKVFINQKDIALISKHSNSSTAENEMKPDSLLAGIENGKLKFRFETADKYIEFAQQNGMVVRGHTLVWHNQTPEWFFKDENGNLLSKEEMTERLREYIHTVVGHFKGKVYAWDVVNEAVDPNQPDGLRRSTWYQIMGPDYIELAFKFAREADPNAKLFYNDYNTFEPKKRDIIYNLVKSLKEKGLIDGIGMQCHISLATDIRQIEEAIKKFSTIPGIEIHITELDISVYRDSTSNYSEAPRTALIEQAHKMAQLFKIFKKYSNVITNVTFWGLKDDYSWRATRRNDWPLIFDKDYQAKLAYWAIVAPEVLPPLPKESKISEGEAVVVGMMDDSYMMSKPIEIYDEEGNVKATIRAIWKDSTIYVYGEVQDATKKPAEDGVAIFINPNNERTPYLQPDDTYVVLWTNWKSEVNREDVEVKKFVGPGFRRYSFEMSITIPGVEFKKDSYIGFDVAVIDDGKWYSWSDTTNSQKTNTMNYGTLKLEGVMVATAKYGTPVIDGEIDDIWNTTEEIETKSVAMGSLEKNATAKVRVLWDEENLYVLAIVKDPVLNKDNSNPWEQDSVEIFIDENNHKTGYYEDDDAQFRVNYMNEQSFGTGASAARFKTAVKLIEGGYIVEAAIKWKTIKPSPNTVIGFNVQVNDANEKGQRVGIISWSDPTNNSWRDPSKFGNLRLIK |
| Enzyme Length | 1055 |
| Uniprot Accession Number | Q60042 |
| Absorption | |
| Active Site | ACT_SITE 498; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 604; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10061 |
| 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; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 102 degrees Celsius. Thermostable.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (3); Region (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 119,323 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |