ID   FSDK_FUSHE              Reviewed;         452 AA.
AC   Q5SBK7;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Prenyltransferase fsdK {ECO:0000305|PubMed:15724180};
DE            EC=2.5.1.- {ECO:0000305|PubMed:15724180};
DE   AltName: Full=Fusaridione A biosynthesis protein K {ECO:0000303|PubMed:23614392};
GN   Name=fsdK {ECO:0000303|PubMed:23614392};
GN   Synonyms=eqi3 {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: Prenyltransferase; 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 tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AY700570; AAV66102.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5SBK7; -.
DR   SMR; Q5SBK7; -.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   InterPro; IPR012148; DMATS-type_fun.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   PIRSF; PIRSF000509; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..452
FT                   /note="Prenyltransferase fsdK"
FT                   /id="PRO_0000441316"
SQ   SEQUENCE   452 AA;  50714 MW;  2ACF2D2F3E83D335 CRC64;
     MSLNSASTRE HPSEAWKSLA QYLPSRSTDL DYWWQRIGPS AALVLEKAGY SIKSQYDALL
     FLYHWVVPEL GPSLLSTDHK WKSLLQGDGS AFELSWKWNT NDSPPEVRYV VEPINQFSGT
     LLDPLNSQPS MVFRHRLASI LPNIDLTWCH HFAGSLFDHN KARLLREMMP EGHKMPAGYT
     VPSTLVALEF LQDGQVATKS YFIPRKHGQG VWLPIAQFEE SIAELDPVNE ARAAVVDFVS
     KDPESLTPIM LAVDDKDVSS ARIKWYFATA RTELSWAKEI MTLGGRITTK HLPHLEQQLD
     DLIELIKAVT GIASEYPQDV ELPFAPRFDP SKGAGNFVPL PIPIAGYQVH FNIAPGSEVP
     GVKLYIPMRR YARDDASVAK GITSFMESRG RNTYIKEYTE MLAGLLPDGK ELSSVHCLQT
     YVSCLFKKNG ELEITTYLGM APYGDNHKPM SI