IED ID | IndEnz0004000076 |
Enzyme Type ID | xylanase000076 |
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 BH2120 |
Organism | Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Alkalihalobacillus Alkalihalobacillus halodurans (Bacillus halodurans) Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans) |
Enzyme Sequence | MITLFRKPFVAGLAISLLVGGGIGNVAAAQGGPPKSGVFGENEKRNDQPFAWQVASLSERYQEQFDIGAAVEPYQLEGRQAQILKHHYNSLVAENAMKPESLQPREGEWNWEGADKIVEFARKHNMELRFHTLVWHSQVPEWFFIDEDGNRMVDETDPDKREANKQLLLERMENHIKTVVERYKDDVTSWDVVNEVIDDGGGLRESEWYQITGTDYIKVAFETARKYGGEEAKLYINDYNTEVPSKRDDLYNLVKDLLEQGVPIDGVGHQSHIQIGWPSIEDTRASFEKFTSLGLDNQVTELDMSLYGWPPTGAYTSYDDIPAELLQAQADRYDQLFELYEELAADISSVTFWGIADNHTWLDGRAREYNNGVGIDAPFVFDHNYRVKPAYWRIID |
Enzyme Length | 396 |
Uniprot Accession Number | P07528 |
Absorption | |
Active Site | ACT_SITE 195; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 301; /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 | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active over a very broad pH range.; |
Pathway | PATHWAY: Glycan degradation; xylan degradation. |
nucleotide Binding | |
Features | Active site (2); Beta strand (13); Chain (1); Domain (1); Helix (18); Signal peptide (1); Turn (4) |
Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000269|Ref.1 |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 2UWF; 7CPK; 7CPL; |
Mapped Pubmed ID | 19567261; 33604642; |
Motif | |
Gene Encoded By | |
Mass | 45,294 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |