ID   FSDD_FUSHE              Reviewed;         284 AA.
AC   Q5SBL1;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 2.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Methyltransferase fsdD {ECO:0000303|PubMed:15724180};
DE            EC=2.1.1.- {ECO:0000305|PubMed:15724180};
DE   AltName: Full=Fusaridione A biosynthesis protein D {ECO:0000303|PubMed:15724180};
GN   Name=fsdD {ECO:0000303|PubMed:15724180};
GN   Synonyms=eqi4 {ECO:0000303|PubMed:15724180};
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].
RC   STRAIN=ATCC 74349 / MF6069;
RX   PubMed=15724180; DOI=10.1039/b413523g;
RA   Sims J.W., Fillmore J.P., Warner D.D., Schmidt E.W.;
RT   "Equisetin biosynthesis in Fusarium heterosporum.";
RL   Chem. Commun. (Camb.) 2:186-188(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND 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).
CC   -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of fusaridione A, a bright yellow trans-fused decalin-
CC       containing tetramic acid with antimicrobial activity (PubMed:23614392).
CC       The PKS module of fsdS catalyzes the formation of the polyketide unit
CC       which is then conjugated to L-tyrosine by the condensation domain of
CC       the fsdS NRPS module. Activity of the Dieckmann cyclase domain (RED)
CC       results in release of the intermediate fusaridione A (PubMed:23614392).
CC       The unstable pyrrolidinedione ring of fusaridione A is opened through a
CC       reverse-Dieckmann reaction to afford its ring-opened form
CC       (PubMed:23614392). {ECO:0000269|PubMed:23614392}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|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; AY700570; AAV66107.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q5SBL1; -.
DR   SMR; Q5SBL1; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..284
FT                   /note="Methyltransferase fsdD"
FT                   /id="PRO_0000441301"
FT   BINDING         197..198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:O04385"
SQ   SEQUENCE   284 AA;  30942 MW;  2662A6E385358274 CRC64;
     MGSAGDDYEY VFPDISVENE RLAGQHAGIK VGMGGRLCMA PLDLTRPNLR IFDGGTSDGY
     WLDDLKKELA HPETCDLIGG DVTGERFPTN PPPGVKLEVQ SSTGPFPSDW LQSFDLVHQR
     LTLAGLGNQS EHCVEQLMSL VKPGGWIQLV ELDNSSHEPN GPAVKTLGAL VARLAEGMGA
     DLKYRGGGME KWVRDKGFIR VGSILAPVCM GAECPVPNMR DQTTKAFSFT AEQLIKACKR
     FPGGLKVMTD EEAEGLVGRL EDELRTRGGY FPVRVVWGKR PVDQ