ID   FSDC_FUSHE              Reviewed;         381 AA.
AC   S0ASL9;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Trans-enoyl reductase fsdC {ECO:0000303|PubMed:15724180};
DE            EC=1.-.-.- {ECO:0000305|PubMed:15724180};
DE   AltName: Full=Fusaridione A biosynthesis protein C {ECO:0000303|PubMed:15724180};
GN   Name=fsdC {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: Trans-enoyl reductase; part of the gene cluster that mediates
CC       the 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:15724180}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AY700570; AGO65991.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0ASL9; -.
DR   SMR; S0ASL9; -.
DR   BioCyc; MetaCyc:MON-19335; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NADP; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..381
FT                   /note="Trans-enoyl reductase fsdC"
FT                   /id="PRO_0000441297"
FT   REGION          276..304
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255"
FT   BINDING         46..49
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         130..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         166..169
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         189..193
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         208
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         255..256
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         370..371
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ   SEQUENCE   381 AA;  42394 MW;  2D60A1C56A83E4A8 CRC64;
     MDRPNKAIYL YQTSKGNHEI RTIQEPYVPK DAQSLVDVQY SGINPADTRH VYMDMSNYVA
     GYEFAGTVKQ VGPKSPFKIG QEIFGISIPY NNRPNYLGAH QSFLLAENFM TFARPDHLDP
     ITAATLLAGG GTAMDGLLNV LGYGFPPAGI PGDDPTNVPI LIWGGAGGVG QAAVQLAKAA
     GFFPIITTAS QQNHDVMKQL GASHVFNYKS PSVVQDIRNL LESKGWSLKT VFDAVSTGLG
     VFDGLTEEQE KAVQQKYNQS SSAMARQCCD PNIPDSELRL TSVLPVKMDP NYVFCLNFRP
     VEILDIGGEV TKDTKEEEMT KWKEWQPRIE KCIEWLIENH EKHWQPPRTR VVKGVEEGLQ
     GIRDVWQGKM SREKLVIDHR V