| IED ID | IndEnz0015000148 |
| Enzyme Type ID | laccase000148 |
| Protein Name |
FAD-binding monooxygenase VdtE EC 1.14.13.- Viriditoxin biosynthesis cluster protein E |
| Gene Name | VdtE C8Q69DRAFT_480056 |
| 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 | MASMQEVDALVVGAGFGGLWMTNRLKEAGLNVLCVEKAPQAGGVWYWNCYPGARVDSRYPVYQYSDESLCKDWNWSELFPGYEEIRKYLSYAVDKWQLNSHIRYNTTVTGARFDESDHKWTVEGINGSHGTIRIRCRWYILALGFASKPYIPDFEGLNRFQGPCFHSSAWPQEGIDLKGRRVAVVGTGASAVQIIQTISKEVGHLTVYQRTPCTAMPMRQQSLTPEYQDNFKASGEMAATMRRTKYERFGGQDVQFVSRRWHEDTPEQRRAVFEQAWQKGGFHLLLSTYFEVFDDVEVNHAAWRFWAEKSRERIHNTKYKDILAPLEAVHAFGGKRTPFEQDYFEAFNRRNVDLIDMKASPILSFAEKGIITQNEGLQEFDVIILATGFDTNTGALTSIHIQDTDGILLKDRWSYDGVMTTFGMSTSKFPNMFFFYGPQAPTAFSNGPSCIELQGEFVEELILDMIGKGVTRVDTTSEAEKRWKESTLSLWNQFVFSSTKGFYTGENIPGKKAEPLNWFGGFPRYRKALTECRDGGYKEYSLRSLPKVPDPEHRGLIDKVAVVTSAQPVGA |
| Enzyme Length | 571 |
| Uniprot Accession Number | A0A443HK11 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 62; /note=FAD; /evidence=ECO:0000250|UniProtKB:H3JQW0 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=9,10-dihydroxy-7-methoxy-3-(2-oxopropyl)-1H-benzo[g]isochromen-1-one + H(+) + NADPH + O2 = H2O + methyl 2-[(3S)-9,10-dihydroxy-7-methoxy-1-oxo-1H,3H,4H-naphtho[2,3-c]pyran-3-yl]acetate + NADP(+); Xref=Rhea:RHEA:62868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:146010, ChEBI:CHEBI:146012; Evidence={ECO:0000269|PubMed:31045362};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62869; Evidence={ECO:0000269|PubMed:31045362}; CATALYTIC ACTIVITY: Reaction=(3S)-9,10-dihydroxy-7-methoxy-3-(2-oxopropyl)-1H,3H,4H-naphtho[2,3-c]pyran-1-one + H(+) + NADPH + O2 = H2O + NADP(+) + semiviriditoxin; Xref=Rhea:RHEA:62872, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:146008, ChEBI:CHEBI:146011; Evidence={ECO:0000269|PubMed:31045362};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62873; Evidence={ECO:0000269|PubMed:31045362}; |
| DNA Binding | |
| EC Number | 1.14.13.- |
| Enzyme Function | FUNCTION: FAD-binding monooxygenase; 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 | NP_BIND 44..47; /note=FAD; /evidence=ECO:0000250|UniProtKB:H3JQW0; NP_BIND 54..56; /note=NADP; /evidence=ECO:0000250|UniProtKB:H3JQW0; NP_BIND 56..57; /note=FAD; /evidence=ECO:0000250|UniProtKB:H3JQW0; NP_BIND 187..193; /note=NADP; /evidence=ECO:0000250|UniProtKB:H3JQW0; NP_BIND 210..211; /note=NADP; /evidence=ECO:0000250|UniProtKB:H3JQW0 |
| Features | Binding site (1); Chain (1); Nucleotide binding (5); Site (1) |
| Keywords | FAD;Flavoprotein;Monooxygenase;NADP;Oxidoreductase;Reference proteome |
| 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 | 64,947 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62868; RHEA:62869; RHEA:62872; RHEA:62873 |
| Cross Reference Brenda |