| IED ID | IndEnz0009000269 |
| Enzyme Type ID | chitinase000269 |
| Protein Name |
Lytic chitin monooxygenase EC 1.14.99.53 EfCBM33A Lytic polysaccharide monooxygenase LPMO |
| Gene Name | EF_0362 |
| Organism | Enterococcus faecalis (strain ATCC 700802 / V583) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Enterococcaceae Enterococcus Enterococcus faecalis (Streptococcus faecalis) Enterococcus faecalis (strain ATCC 700802 / V583) |
| Enzyme Sequence | MKKSLLTIVLAFSFVLGGAALAPTVSEAHGYVASPGSRAFFGSSAGGNLNTNVGRAQWEPQSIEAPKNTFITGKLASAGVSGFEPLDEQTATRWHKTNITTGPLDITWNLTAQHRTASWDYYITKNGWNPNQPLDIKNFDKIASIDGKQEVPNKVVKQTINIPTDRKGYHVIYAVWGIGDTVNAFYQAIDVNIQ |
| Enzyme Length | 194 |
| Uniprot Accession Number | Q838S1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=((1->4)-N-acetyl-beta-D-glucosaminyl)(n+m) + reduced acceptor + O(2) = ((1->4)-N-acetyl-beta-D-glucosaminyl)(m-1)-(1->4)-2-(acetylamino)-2-deoxy-D-glucono-1,5-lactone + ((1->4)-N-acetyl-beta-D-glucosaminyl)(n) + acceptor + H(2)O.; EC=1.14.99.53; Evidence={ECO:0000269|PubMed:22210154}; |
| DNA Binding | |
| EC Number | 1.14.99.53 |
| Enzyme Function | FUNCTION: Involved in chitin degradation. Catalyzes the oxidative cleavage of glycosidic bonds in both alpha- and beta-chitin via a copper-dependent mechanism, leading to oxidized chitooligosaccharides with a dominance of even-numbered products. Acts synergistically with the chitinase EfChi18A, and combining the two enzymes leads to rapid and complete depolymerization of crystalline chitin, especially with beta-chitin as a substrate. Is likely involved in a chitin degradation pathway that allows E.faecalis V583 to grow on chitin as a carbon source. {ECO:0000269|PubMed:22210154}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; chitin degradation. {ECO:0000269|PubMed:22210154}. |
| nucleotide Binding | |
| Features | Beta strand (9); Chain (1); Domain (1); Helix (6); Metal binding (2); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Copper;Metal-binding;Oxidoreductase;Polysaccharide degradation;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22210154}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 4A02; 4ALC; 4ALE; 4ALQ; 4ALR; 4ALS; 4ALT; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,138 |
| Kinetics | |
| Metal Binding | METAL 29; /note="Copper; via pros nitrogen"; /evidence="ECO:0000269|PubMed:24828494, ECO:0007744|PDB:4ALE, ECO:0007744|PDB:4ALR, ECO:0007744|PDB:4ALS, ECO:0007744|PDB:4ALT"; METAL 114; /note="Copper; via tele nitrogen"; /evidence="ECO:0000269|PubMed:24828494, ECO:0007744|PDB:4ALE, ECO:0007744|PDB:4ALR, ECO:0007744|PDB:4ALS, ECO:0007744|PDB:4ALT" |
| Rhea ID | |
| Cross Reference Brenda | 1.14.99.53; |