| IED ID | IndEnz0015000157 |
| Enzyme Type ID | laccase000157 |
| Protein Name |
O-methyltransferase VdtC EC 2.1.1.- Viriditoxin biosynthesis cluster protein C |
| Gene Name | VdtC C8Q69DRAFT_488617 |
| Organism | Byssochlamys spectabilis (Paecilomyces variotii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Thermoascaceae Paecilomyces Byssochlamys spectabilis (Paecilomyces variotii) |
| Enzyme Sequence | MAEEIKLTPLETFAQAISASAKTIATYCRDSGHPQLSDDNSSGLTGDVLPPSAPQAVTAARQTILEASYRLQQLVTEPSQYLPRLTVYPQHLAALRWLCHFRIPELIPVQGTRTYYELATEAKVPLHQLQSIARMAITGSFLREPEPNIVAHSRTSAHFVENPSLRDWTLFLAEDTAPMAMKLVEATEKWGDTRSKTETAFNLALGTDLAFFKYLSSNPQFTQKFSGYMKNVTASEGTSIKHLVNGFDWASLGNAIVVDVGGSTGHASIALAESFPDLKFIVQDLPMVTSTSKDNREKTPLPETVASRISFESHDFFKPQPVQNADVYLLRMILHDWSFKEAGEILANLVPSVKQGARILIMDTVLPRHGTVPVTEEALLRVRDMTMMETFNSHEREIDEWKDLIQGVHTGLRVQQVIQPAGSSMAIIEVVRG |
| Enzyme Length | 433 |
| Uniprot Accession Number | A0A443HJY8 |
| Absorption | |
| Active Site | ACT_SITE 335; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01020 |
| Activity Regulation | |
| Binding Site | BINDING 284; /note=S-adenosyl-L-methionine; /evidence=ECO:0000255|PROSITE-ProRule:PRU01020 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=7,9,10-trihydroxy-3-(2-oxopropyl)-1H-benzo[g]isochromen-1-one + S-adenosyl-L-methionine = 9,10-dihydroxy-7-methoxy-3-(2-oxopropyl)-1H-benzo[g]isochromen-1-one + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62864, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:146009, ChEBI:CHEBI:146010; Evidence={ECO:0000269|PubMed:31045362};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62865; Evidence={ECO:0000269|PubMed:31045362}; |
| DNA Binding | |
| EC Number | 2.1.1.- |
| Enzyme Function | FUNCTION: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity (PubMed:31304040, PubMed:31045362). The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin (PubMed:31304040). The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC (PubMed:31304040, PubMed:31045362). The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis (PubMed:31304040, PubMed:31045362). The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond (PubMed:31304040, PubMed:31045362). The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin (PubMed:31304040, PubMed:31045362). Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin (PubMed:31304040, PubMed:31045362). VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2 (PubMed:31304040, PubMed:31045362). The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling (PubMed:31304040, PubMed:31045362). The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet (PubMed:31304040, PubMed:31045362). {ECO:0000269|PubMed:31045362, ECO:0000269|PubMed:31304040}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:31045362, ECO:0000269|PubMed:31304040}. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (1); Chain (1) |
| Keywords | Methyltransferase;Reference proteome;S-adenosyl-L-methionine;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 48,046 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62864; RHEA:62865 |
| Cross Reference Brenda |