ID   EQXD_FUSHE              Reviewed;         359 AA.
AC   S4W780;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Methyltransferase eqxD {ECO:0000303|PubMed:23614392};
DE            EC=2.1.1.- {ECO:0000305|PubMed:23614392};
DE   AltName: Full=Equisetin biosynthesis protein D {ECO:0000303|PubMed:23614392};
GN   Name=eqxD {ECO:0000303|PubMed:23614392};
OS   Fusarium heterosporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium heterosporum species complex.
OX   NCBI_TaxID=42747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=ATCC 74349 / MF6069;
RX   PubMed=23614392; DOI=10.1021/cb400159f;
RA   Kakule T.B., Sardar D., Lin Z., Schmidt E.W.;
RT   "Two related pyrrolidinedione synthetase loci in Fusarium heterosporum ATCC
RT   74349 produce divergent metabolites.";
RL   ACS Chem. Biol. 8:1549-1557(2013).
RN   [2]
RP   FUNCTION.
RX   PubMed=18652469; DOI=10.1021/ja803078z;
RA   Sims J.W., Schmidt E.W.;
RT   "Thioesterase-like role for fungal PKS-NRPS hybrid reductive domains.";
RL   J. Am. Chem. Soc. 130:11149-11155(2008).
CC   -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of equisetin, a trans-fused decalin-containing tetramic
CC       acid with antimicrobial activity (PubMed:23614392). The PKS module of
CC       eqxS together with the enoylreductase eqxC catalyze the formation of
CC       the polyketide unit which is then conjugated to L-serine by the
CC       condensation domain of the eqxS NRPS module (PubMed:23614392). Activity
CC       of the Dieckmann cyclase domain (RED) results in release of the
CC       Dieckmann product intermediate (PubMed:23614392, PubMed:18652469).
CC       Diels-Alderase eqx3 is involved in endo-selective Diels-Alder
CC       cycloaddition to form the decalin ring, leading to the production of N-
CC       desmethylequisetin also called trichosetin (By similarity). Subsequent
CC       N-methylation is carried out by eqxD to give equisetin
CC       (PubMed:23614392). {ECO:0000250|UniProtKB:A0A0E4AZP0,
CC       ECO:0000269|PubMed:18652469, ECO:0000269|PubMed:23614392}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + trichosetin = equisetin + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:57648, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:142060,
CC         ChEBI:CHEBI:142061; Evidence={ECO:0000305|PubMed:23614392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57649;
CC         Evidence={ECO:0000305|PubMed:23614392};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:23614392}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of equisetin and
CC       accumulates the intermediate trichosetin (PubMed:23614392).
CC       {ECO:0000269|PubMed:23614392}.
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; KC439347; AGO86665.1; -; Genomic_DNA.
DR   AlphaFoldDB; S4W780; -.
DR   SMR; S4W780; -.
DR   BioCyc; MetaCyc:MON-19333; -.
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   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..359
FT                   /note="Methyltransferase eqxD"
FT                   /id="PRO_0000441300"
FT   BINDING         198..199
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         248..249
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         264
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
FT   BINDING         265
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   359 AA;  39735 MW;  6A8D6DCF52EB1C27 CRC64;
     MSSILSRYPE AETPVHGYFY SMVELAVVRV FVQHEIFDAI ADDGTSIEEL ATKTGMEMNL
     LERLSNFLIA SKVLSSPKPG FIGLPAETKM FQQRRAKLFY SHIFDAFMGS AVKWPQYLQT
     NGLAEPQKSN RSPFGLGAGY PDKSFYDVLD MMPERAQAFN STMAIGLGDM PITGIYDFSW
     VTAHAGTDPK RTLIVDVGGG KGQAIKAIIE ETPSIPASAC VLQDLPNVIK DTPEEDGILR
     KVQKVGSSFF DKQSTRGALV YYIRRVLNDW PDDECVTILK NIREACASDS RLLISENLLP
     DEPSVSLAAA DLWMMNFAGK RRNVRMFNDL ASRSGFEISS IAKDKMSNSA VIEMLPVQS