| IED ID | IndEnz0015000128 |
| Enzyme Type ID | laccase000128 |
| Protein Name |
Highly reducing polyketide synthase VdtX HR-PKS VdtX EC 2.3.1.- Viriditoxin biosynthesis cluster protein X |
| Gene Name | VdtX C8Q69DRAFT_515060 |
| 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 | MAICGIAVRLPGGISNDAQLWDFLLAKRDARSQVPGSRYNISGYHSDSGKHGTSKSKYGYFLDESVDLGTLDTSFFSFTKLELEYIDPCQRQLLEVVRECFESAGEVNYRGKDIGCFVGSFGDDWTENLTHDEQTSAKYPLMVGGDFATPNRVSYEYNLHGPSVSIRTACSSSLVALHSACLSIQNGDCSAAIVAGFNLILTPTMTMIMSSKGVLSADGSSKSFDADADGYGRGEAVNAVYIKPLHDAIRDGNPIRAVIRGTATNSDGKSAGFTVPSADAQEDVIRKAYKAAGISDLSQTAFVECHGTGTTVGDPIEVAAIANTFGGDMYIGSVKPNVGHSEGASGLTSLIKAVLAVENRTIPPNIKFNTPNPKIPFEAKKITVPVEATPWPWNRCVRASVNSFGMGGVNAHVIIESADNFTPPTSEVIEEHDSTPQLLLFSANTQDSLEAMIQRNLAYLRENTDSLRDLVYTMGARREHLSFRAASIVHSDMSVTTASFGKAPSSPPDIVMVFAGQGAQWPGMGVELFKSNATFRRSILEMDSVLQSLPDAPAWSIADEISKEHQTSMLYLSSYSQPICTALQVALVNTLFELNIRPYAVIGHSSGELAAAYAAGRLTASQAVTLAYYRGIVAGKVAQAGYYPFLRPGVVVACENSPSSVTISGDIDQVQYVMQEISLAHPEILCRQIKSDTAYHSHHMKSVGDTYHSFINPFFRGETEVNCQPVHFFSTVTGDELSDGDHVGPKYWQQNLESRVLFQGALENIISRQRSRHLLFLDVSPHSTLAGPIRQTLEQAEVAHPYVPCLIRFKNCAESFLSTIGQLYSHRQPLDFNMLTNPDRTAKVLTDVPTYPWQHGYSNLYTTRQNNEWLFRKQPKHELLGTRVVDSTDNEPCWRNVLYLEHVTWLRDHKVSGNIVFPAAGYVMMAGEAVRQIGSTASGFIVRQMVLDTAMVLNQSNPTEIVTSLRKHRRDRWYSFTISSHNGVKWIEHCYGEVAQENLSRDINVSNWYKTLSRGGVEFGPAFQCVESQSCSVTSNTVSGRIVSKLDSVLHIVYGAIYKGFDWQVESLPVPTSIGEIMIGECVSDLDVTMWADVSRNSNILVNGEAFGSDGCLLIRIKDIVLRPLGANQACFEEDESHAGARLLWKPSMQFLNLADLIQTPVNWTKQTMLLNDFTSLCIERALCLLHAQGDWLQRQPKPSSEQSMESLVEKILATSAAPCARAMIKVLDNIVPICKGEIDALEVLMGDDTLYELYNYLNEPQQRILEIGAGTGGTTAKILPRTKYSTYTFTDISAAFFPAAKDRFQCHANVVYRTLDITKDPLDQANVLHATPNLYETLSNLLLEELCGDAKFTNFIVGVLPGWWAGESDGRADEPYISPDRWDSILKAAAPPLHSLAFMLASPSCVPESPLKRNVTLLSDVTSSEIAVRMQKQLLSRGYSVGVQSLDQSLMDGEDVIILVDTVSPFFHNLDSRKLSTFQNLLRELQRSHSGALWVTRSIQIDCRDPRYSPTLGVARTVRSEFGLDFGTCEVDTLKYTSIGLVIDVFEAFHGRRHGQNAYPEYEYAIREDTADAGQQVQLLGDDEVELQVDTAGVNFLTVLINSASDGVGLAAIQISKMIGATIYATVIGEDKVEYLTASHGIPRDHIFNSRDSSFLDGIMRVTNGRGVDLVLTSLSADFIQASCDCVANFGKLVNLSKPTAANQGQFPIDSFHPNMSYASVDIIDYIKRRPKESKRLLEEIVELYKQGHIQPITPVKTFTATDIRQCFDYMQSGQHIGQLRLSLKSQDTFIEAVCSPKTMIFQSDASYLLVGGLGGLGAEIARWMAEHGARNLIFLSRSADAESNIRLFRELESQGCSVQAIKGSVCNASDVKRAISAARIKLKGIFNMSMVLQDASLLKMSSDEWNAATGPKIQGTWNLHDASLDQDLDFFLLFSSMGGILGIPGQANYASANTFMDAFVQFRHSSHLPASVIDIGEVQGIGHVANNPEILNRLKLLECARMSQKDLFHAITIAISHSLPPQTLDYSRYENPAQFITGLRDTTGMLDSTGGKSMLLDSRLAAYVGNSAAVTAPTETKTSANKLNNFVSSAATDSAILSEPSATQFVSLEIARWVFDLLMKPVDDDSEIDLSRSLVDVGLDSLAAVEMRSWLKSSLGLDISVLEIMASPSLAAMGEHVIRELVRKFGGDNKN |
| Enzyme Length | 2193 |
| Uniprot Accession Number | A0A443HK66 |
| Absorption | |
| Active Site | ACT_SITE 170; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 2.3.1.- |
| Enzyme Function | FUNCTION: Highly reducing polyketide synthase; 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). 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. The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis (PubMed:31304040). The short-chain dehydrogenase/reductase VdtF is involved in the reduction of the C3-C4 double bond (PubMed:31304040). The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin (PubMed:31304040). Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin. The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling (PubMed:31304040). 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). {ECO:0000269|PubMed:31304040}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Modified residue (1); Region (6) |
| Keywords | Acyltransferase;Methyltransferase;Multifunctional enzyme;NADP;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2143; /note=O-(pantetheine 4'-phosphoryl)serine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00258 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 240,602 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |