EQXC_FUSHE
ID EQXC_FUSHE Reviewed; 353 AA.
AC S4W4F3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Trans-enoyl reductase eqxC {ECO:0000303|PubMed:23614392};
DE EC=1.-.-.- {ECO:0000305|PubMed:23614392};
DE AltName: Full=Equisetin biosynthesis protein C {ECO:0000303|PubMed:23614392};
GN Name=eqxC {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: Trans-enoyl reductase; part of the gene cluster that mediates
CC the biosynthesis of equisetin, a trans-fused decalin-containing
CC tetramic acid with antimicrobial activity (PubMed:23614392). The PKS
CC module of eqxS together with the enoylreductase eqxC catalyze the
CC formation of the polyketide unit which is then conjugated to L-serine
CC by the condensation domain of the eqxS NRPS module (PubMed:23614392).
CC Activity of the Dieckmann cyclase domain (RED) results in release of
CC the 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=acetyl-CoA + ATP + 11 H(+) + L-serine + 7 malonyl-CoA + 8
CC NADPH + 2 S-adenosyl-L-methionine = (5S)-3-[(2E,6R,8E,10E,12E)-2,6-
CC dimethyltetradeca-2,8,10,12-tetraenoyl]-5-(hydroxymethyl)pyrrolidine-
CC 2,4-dione + AMP + 7 CO2 + 8 CoA + diphosphate + 6 H2O + 8 NADP(+) + 2
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67324, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58349, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:169938, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000305|PubMed:23614392};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67325;
CC Evidence={ECO:0000305|PubMed:23614392};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:23614392}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
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 zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; KC439347; AGO86659.1; -; Genomic_DNA.
DR AlphaFoldDB; S4W4F3; -.
DR SMR; S4W4F3; -.
DR BioCyc; MetaCyc:MON-19332; -.
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; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
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..353
FT /note="Trans-enoyl reductase eqxC"
FT /id="PRO_0000441296"
FT BINDING 45..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 131..138
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..192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 254..255
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT BINDING 275..279
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 344..345
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ SEQUENCE 353 AA; 38056 MW; 699E63ECD9399C33 CRC64;
MVQRQQTALV GTHDGGIRLS STETIPDIAG DSVLIKTKAV SVNPVDTKMI GPYVTPGAVA
GFDFAGVVEM VGPDATKCDI RVGDRVCTAI MGMNPLDPTV GAFAEYTAAV EWILLKIPPS
LSFQEGASLG ISFMTTGLAL FKSLGLPGNP LSPATEKLPV LVYGGSSATG TAAIQLVRLA
GFAPITTCSP RNFELVKSYG ASAVFDYNDP NCISDIKKHT KNNIRYALDC ISTTQSMQFC
YQAIGRAGGK YTALEPYSEA VARTRKMVKP DWIMGPQMLG KEIRWPEPHW RPANAEMGEF
GVYWTAVLNK LLENDLIRPH AIVVREGGLE KVLDGIEDIR AKKISGKKLV FTL
