ID   PVHD_TALVA              Reviewed;         360 AA.
AC   A0A3Q9U4A9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Methyltransferase pvhD {ECO:0000303|PubMed:30609896};
DE            EC=2.1.1.- {ECO:0000269|PubMed:30609896};
DE   AltName: Full=Varicidin biosynthesis cluster protein D {ECO:0000303|PubMed:30609896};
GN   Name=pvhD {ECO:0000303|PubMed:30609896};
OS   Talaromyces variabilis (Penicillium variabile).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=28576;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=HXQ-H-1;
RX   PubMed=30609896; DOI=10.1021/jacs.8b12010;
RA   Tan D., Jamieson C.S., Ohashi M., Tang M.C., Houk K.N., Tang Y.;
RT   "Genome-mined Diels-Alderase catalyzes formation of the cis-
RT   octahydrodecalins of varicidin A and B.";
RL   J. Am. Chem. Soc. 141:769-773(2019).
CC   -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of varicidin A, an antifungal natural product containing a
CC       cis-octahydrodecalin core (PubMed:30609896). The PKS module of pvhA
CC       together with the enoylreductase pvhC catalyze the formation of the
CC       polyketide unit which is then conjugated to L-isoleucine by the
CC       condensation domain of the NRPS module (PubMed:30609896). Activity of
CC       the Dieckmann cyclase domain (RED) of pvhA results in release of an
CC       acyclic tetramate (PubMed:30609896). The cytochrome P450 monooxygenase
CC       pvhE then catalyzes the oxidation of the C21 methyl group to a to
CC       carboxylate group (PubMed:30609896). The methyltransferase pvhD then
CC       further methylates the pvhE product (PubMed:30609896). The Diels-
CC       Alderase pvhB is able to catalyzes Diels-Alder cycloaddition using both
CC       pvhE and pvhD products as substrates to form the decalin ring, yielding
CC       varicidin B and A, respectively (PubMed:30609896).
CC       {ECO:0000269|PubMed:30609896}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:30609896}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; MK376933; AZZ09611.1; -; Genomic_DNA.
DR   SMR; A0A3Q9U4A9; -.
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   PIRSF; PIRSF005739; O-mtase; 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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..360
FT                   /note="Methyltransferase pvhD"
FT                   /id="PRO_0000453343"
FT   BINDING         201..202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         251..252
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         267
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         268
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   360 AA;  40389 MW;  9C100ADC008772E4 CRC64;
     MPPSLPCRCQ EAPTPVFGYL YQIVELGVMR LFVEKRVFNE IPDEGILIAD LATKTGIEFN
     LLERLVNFLI SSRIFTSSSP GYVHHTPTSK YFTERRAQLW YPHIFDTFLT SAVKWPEYFD
     INGMQEPQCS SKSPFGFGSG YSDKSVYEIF DLMPKRSSDF NATMALSMGE MPILGMYDFS
     WIGEYGKRPE VKDRTLFVDV SGGKGQALQA ILEAFPSIIP EQCVLEDQEK VIEEAKLATG
     PLETVKKVPI DLFGEQPVKG ALVYYIRRVL NDWSDAEVVQ ILRSIRDACA PDSKVLISEN
     LLPDEPPLKL AAIDVWMLNF GGKRRNKGNF GALARRAGFE LSSIAEDDKT KSAVLELVVA