| IED ID | IndEnz0008000459 |
| Enzyme Type ID | cellulase000459 |
| 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 | Thermoanaerobacterium saccharolyticum |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Thermoanaerobacterium Thermoanaerobacterium saccharolyticum |
| Enzyme Sequence | MMKNNVDRIVSIVTALIMIFGASLFSPPIRVFADDTNINLVSNGDFESGTIDGWIKQGNPTLAVTTEQAIGQYSMKVTGRTQTYEGPAYSFLGKMQKGESYSVSLKVRLVSGQNSSNPLITVTMFREDDNGKHYDTIVWQKQVSEDSWTTVSGTYTLDYIGTLKTLYMYVESPDPTLEYYIDDVVVTTQNPIQVGNVIANETFENGNTSGWIGTGSSVVKAVYGVAHSGDYSLLTTGRTANWNGPSYDLTGKIVPGQQYNVDFWVKFVNGNDTEQIKATVKATSDKDNYIQVNDFANVNKGEWTEIKGSFTLPVADYSGISIYVESQNPTLEFYIDDFSVIGEISNNQITIQNDIPDLYSVFKDYFPIGVAVDPSRLNDADPHAQLTAKHFNMLVAENAMKPESLQPTEGNFTFDNADKIVDYAIAHNMKMRGHTLLWHNQVPDWFFQDPSDPSKSASRDLLLQRLKTHITTVLDHFKTKYGSQNPIIGWDVVNEVLDDNGNLRNSKWLQIIGPDYIEKAFEYAHEADPSMKLFINDYNIENNGVKTQAMYDLVKKLKSEGVPIDGIGMQMHININSNIDNIKASIEKLASLGVEIQVTELDMNMNGNISNEALLKQARLYKQLFDLFKAEKQYITAVVFWGVSDDVTWLSKPNAPLLFDSKLQAKPAFWAVVDPSKAIPDIQSAKALEGSPTIGANVDSSWKLVKPLYVNTYVEGTVGATATVKSMWDTKNLYLLVQVSDNTPSNNDGIEIFVDKNDDKSTSYETDDERYTIKRDGTGSSDITKYVTSNADGYVAQLAIPIEDISPAVNDKIGFDIRINDDKGNGKIDAITVWNDYTNSQNTNTSYFGDIVLSKSAQIATAIYGTPVIDGKVDDIWNNVEPISTNTWILGSNGATATQKMMWDDKYLYVLADVTDSNLNKSSINPYEQDSVEVFVDQNNDKTTYYENDDGQYRVNYDNEQSFGGSTNSNGFKSATSLTQSGYIVEEAIPWTSITPSNGTIIGFDLQVNNADENGKRTGIVTWCDPSGNSWQDTSGFGNLLLTGKPSGALKKGVTFDDIKNSWAKDAIEVLASRHIVEGMTDTQYEPNKTVTRAEFTAMILRLLNIKEEQYSGEFSDVNSGDWYANAIEAAYKAGIIEGDGKNARPNDSITREEMTQ |
| Enzyme Length | 1157 |
| Uniprot Accession Number | P36917 |
| Absorption | |
| Active Site | ACT_SITE 495; /note="Proton donor"; /evidence="ECO:0000250"; ACT_SITE 537; /evidence="ECO:0000269|PubMed:8376336"; ACT_SITE 600; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10061, ECO:0000269|PubMed:8376336" |
| 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 | FUNCTION: Endo-acting enzyme that randomly cleaves the internal xylosidic linkages of the xylan backbone, yielding xylooligosaccharides of various lengths which are further hydrolyzed to xylose molecules by beta-xylosidase (EC 3.2.1.37). Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5.; |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (5); Mutagenesis (3); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Signal;Xylan degradation |
| Interact With | |
| Induction | INDUCTION: By xylan and xylose. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000269|PubMed:8215382 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 128,380 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |