| IED ID | IndEnz0010000509 |
| Enzyme Type ID | esterase000509 |
| Protein Name |
Peptidoglycan deacetylase PG deacetylase EC 3.5.1.- Acetylxylan esterase EC 3.1.1.72 |
| Gene Name | pgdA HPG27_289 |
| Organism | Helicobacter pylori (strain G27) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter Helicobacter pylori (Campylobacter pylori) Helicobacter pylori (strain G27) |
| Enzyme Sequence | MAKEILVAYGVDIDAVAGWLGSYGGEDSPDDISRGLFAGEVGIPRLLKLFKKYHLPATWFVPGHSIETFPEQMKMIVDAGHEVGAHGYSHENPIAMSTKQEEDVLLKSVELIKDLTGKAPTGYVAPWWEFSNITNELLLKHGFKYDHSLMHNDFTPYYVRVGDSWSKIDYSLEAKDWMKPLIRGVETNLVEIPANWYLDDLPPMMFIKKSPNSFGFVSPRDIGQMWIDQFDWVYREMDYAVFSMTIHPDVSARPQVLLMHEKIIEHINKHEGVRWVTFNEIADDFLKRNPRKK |
| Enzyme Length | 293 |
| Uniprot Accession Number | B5ZA76 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Deacetylation of xylans and xylo-oligosaccharides.; EC=3.1.1.72; |
| DNA Binding | |
| EC Number | 3.5.1.-; 3.1.1.72 |
| Enzyme Function | FUNCTION: Catalyzes the N-deacetylation of peptidoglycan (PG), an important mechanism that appears to confer lysozyme resistance and to mitigate host immune detection; this likely contributes to pathogen persistence in the host. The exact nature of the residue in PG that is deacetylated has not been determined. Is also able to catalyze the deacetylation of acetylated xylan, and, to a lesser extent, that of chitin and chitosan. Therefore, this enzyme might play a role during infection, considering that xylan-containing carbohydrate structures are among those commonly consumed by humans (By similarity). In vitro, does not show activity on N-acetylglucosamine (GlcNAc), chitotriose (GlcNAc3), some N-acetyl-dipeptides and allantoinase. {ECO:0000250, ECO:0000269|PubMed:21559431}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (8); Chain (1); Domain (1); Helix (16); Initiator methionine (1); Metal binding (3); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Cell wall biogenesis/degradation;Hydrolase;Metal-binding;Polysaccharide degradation;Xylan degradation;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3QBU; 4LY4; |
| Mapped Pubmed ID | 24346839; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,734 |
| Kinetics | |
| Metal Binding | METAL 14; /note=Zinc; /evidence=ECO:0000269|PubMed:21559431; METAL 86; /note=Zinc; via tele nitrogen; /evidence=ECO:0000269|PubMed:21559431; METAL 90; /note=Zinc; via tele nitrogen; /evidence=ECO:0000269|PubMed:21559431 |
| Rhea ID | |
| Cross Reference Brenda | 3.5.1.104; |