IED ID | IndEnz0004000225 |
Enzyme Type ID | xylanase000225 |
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 | Caldicellulosiruptor sp. (strain Rt8B.4) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Caldicellulosiruptor unclassified Caldicellulosiruptor Caldicellulosiruptor sp. (strain Rt8B.4) |
Enzyme Sequence | MMRSLKSRKLVFILAMLFLINAIVSLKFITYSSANQLASKSKYIEYNFENKSVSPLAKYPSNVVLKVTNSTCAEGTFSVLVAGRKNANDGVIVDITKFLDFSREYEVSFYVLQTTKKLQRISVTLEILDSNDKNQVIAAEKVLLPNIWTKVSAKVQASNYKKAKRINLIVNMPTSKSDSFYIDLFTIKDLENAYVLKQENFENKNTGGFLPEDKNCKITLAKDRAYSSAYSLKVQPSQKTKNGKILFPIKGLLQKGGTYDFSLLVYQDSSKPVNFSAGIKLNDGKSTKEIVLAKQNVAPKKWTQLFATLDLDTRFSAKDVSFFVKPAAAISYYLDLYSISDENWGQPVPDYNLPSLCEKYKNYFKIGVAVPYRALTNPVDVEVIKRHFNSITPENEMKPESLQPYEGGFSFSIADEYVDFCKKDNISLRGHTLVWHQQTPSWFFTNPETGEKLTNSEKDKEILLDRLKKHIQTVVGRYKGKVYAWDVVNEAIDENQPDGYRRSDWYNILGPEYIEKAFIWAHEADPKAKLFYNDYSTEDPYKREFIYKLIKNLKAKGVPVHGVGLQCHISLDWPDVSEIEETVKLFSRIPGLEIHFTEIDISIAKNMTDDDAYNRYLLVQQAQKLKAIFDVLKKYRNVVTSVTFWGLKDDYSWLRGDMPLLSDKDYQPKFAFWSLIDPSVVPKE |
Enzyme Length | 684 |
Uniprot Accession Number | P40944 |
Absorption | |
Active Site | ACT_SITE 490; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 598; /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 | |
PH Dependency | |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (3); 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..34; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 78,354 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |