ID   VDTC1_BYSSP             Reviewed;         433 AA.
AC   A0A443HJY8;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=O-methyltransferase VdtC {ECO:0000303|PubMed:31304040};
DE            EC=2.1.1.- {ECO:0000269|PubMed:31045362};
DE   AltName: Full=Viriditoxin biosynthesis cluster protein C {ECO:0000303|PubMed:31304040};
GN   Name=VdtC {ECO:0000303|PubMed:31304040}; ORFNames=C8Q69DRAFT_488617;
OS   Byssochlamys spectabilis (Paecilomyces variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=264951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101075;
RX   PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA   Urquhart A.S., Mondo S.J., Maekelae M.R., Hane J.K., Wiebenga A., He G.,
RA   Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA   Grigoriev I.V., Idnurm A.;
RT   "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT   variotii (Eurotiales).";
RL   Front. Microbiol. 9:3058-3058(2018).
RN   [2]
RP   IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=31304040; DOI=10.1186/s40694-019-0072-y;
RA   Urquhart A.S., Hu J., Chooi Y.H., Idnurm A.;
RT   "The fungal gene cluster for biosynthesis of the antibacterial agent
RT   viriditoxin.";
RL   Fungal Biol. Biotechnol. 6:2-2(2019).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=31045362; DOI=10.1021/jacs.9b03354;
RA   Hu J., Li H., Chooi Y.H.;
RT   "Fungal dirigent protein controls the stereoselectivity of multicopper
RT   oxidase-catalyzed phenol coupling in viriditoxin biosynthesis.";
RL   J. Am. Chem. Soc. 141:8068-8072(2019).
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of viriditoxin, one of the 'classical' secondary
CC       metabolites produced by fungi and that has antibacterial activity
CC       (PubMed:31304040, PubMed:31045362). The first step is performed by the
CC       polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-
CC       CoA units to form the heptaketide monomer backbone of viriditoxin
CC       (PubMed:31304040). The product of VdtA is then O-methylated on C7 by
CC       the O-methyltransferase VdtC (PubMed:31304040, PubMed:31045362). The O-
CC       methyl group is important for the stereoselective coupling of the
CC       monomers at the final step of viriditoxin biosynthesis
CC       (PubMed:31304040, PubMed:31045362). The short-chain
CC       dehydrogenase/reductase VdtF then acts as a stereospecific reductase
CC       converting the pyrone to dihydropyrone via the reduction of the C3-C4
CC       double bond (PubMed:31304040, PubMed:31045362). The FAD-binding
CC       monooxygenase VdtE then converts the ketone group into a methyl-ester
CC       group to yield semi-viriditoxin (PubMed:31304040, PubMed:31045362).
CC       Finally, the laccase VdtB is involved in dimerization of 2 semi-
CC       viriditoxin molecules to yield the final viriditoxin (PubMed:31304040,
CC       PubMed:31045362). VdtB is responsible for the regioselective 6,6'-
CC       coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-
CC       viriditoxin at a ratio of 1:2 (PubMed:31304040, PubMed:31045362). The
CC       non-catalytic carboxylesterase-like protein VdtD affects the
CC       stereochemistical outcome of the coupling (PubMed:31304040,
CC       PubMed:31045362). The highly reducing polyketide synthase VdtX is not
CC       involved in viriditoxin synthesis, but might possibly play a role in
CC       the production of additional metabolites not identified yet
CC       (PubMed:31304040, PubMed:31045362). {ECO:0000269|PubMed:31045362,
CC       ECO:0000269|PubMed:31304040}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,9,10-trihydroxy-3-(2-oxopropyl)-1H-benzo[g]isochromen-1-one
CC         + S-adenosyl-L-methionine = 9,10-dihydroxy-7-methoxy-3-(2-oxopropyl)-
CC         1H-benzo[g]isochromen-1-one + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:62864, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:146009, ChEBI:CHEBI:146010;
CC         Evidence={ECO:0000269|PubMed:31045362};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62865;
CC         Evidence={ECO:0000269|PubMed:31045362};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:31045362, ECO:0000269|PubMed:31304040}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the O-methylation of C7 of the
CC       heptaketide monomer. {ECO:0000269|PubMed:31304040}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000305}.
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DR   EMBL; RCNU01000014; RWQ92168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443HJY8; -.
DR   SMR; A0A443HJY8; -.
DR   Proteomes; UP000283841; Unassembled WGS sequence.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..433
FT                   /note="O-methyltransferase VdtC"
FT                   /id="PRO_0000448343"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         284
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   433 AA;  48046 MW;  C2C353C1E0B15693 CRC64;
     MAEEIKLTPL ETFAQAISAS AKTIATYCRD SGHPQLSDDN SSGLTGDVLP PSAPQAVTAA
     RQTILEASYR LQQLVTEPSQ YLPRLTVYPQ HLAALRWLCH FRIPELIPVQ GTRTYYELAT
     EAKVPLHQLQ SIARMAITGS FLREPEPNIV AHSRTSAHFV ENPSLRDWTL FLAEDTAPMA
     MKLVEATEKW GDTRSKTETA FNLALGTDLA FFKYLSSNPQ FTQKFSGYMK NVTASEGTSI
     KHLVNGFDWA SLGNAIVVDV GGSTGHASIA LAESFPDLKF IVQDLPMVTS TSKDNREKTP
     LPETVASRIS FESHDFFKPQ PVQNADVYLL RMILHDWSFK EAGEILANLV PSVKQGARIL
     IMDTVLPRHG TVPVTEEALL RVRDMTMMET FNSHEREIDE WKDLIQGVHT GLRVQQVIQP
     AGSSMAIIEV VRG