ID   PRLC_FUNXX              Reviewed;         360 AA.
AC   A0A089FS99;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   26-NOV-2014, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Trans-enoyl reductase prlC {ECO:0000303|PubMed:25226362};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25226362};
DE   AltName: Full=Pyrrolocin biosynthesis protein C {ECO:0000303|PubMed:25226362};
GN   Name=prlC {ECO:0000303|PubMed:25226362};
OS   Fungal sp. (strain NRRL 50135).
OC   Eukaryota; Fungi.
OX   NCBI_TaxID=1547289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=25226362; DOI=10.1021/sb500296p;
RA   Kakule T.B., Jadulco R.C., Koch M., Janso J.E., Barrows L.R., Schmidt E.W.;
RT   "Native promoter strategy for high-yielding synthesis and engineering of
RT   fungal secondary metabolites.";
RL   ACS Synth. Biol. 4:625-633(2015).
RN   [2]
RP   FUNCTION.
RX   PubMed=25351193; DOI=10.1021/np500617u;
RA   Jadulco R.C., Koch M., Kakule T.B., Schmidt E.W., Orendt A., He H.,
RA   Janso J.E., Carter G.T., Larson E.C., Pond C., Matainaho T.K.,
RA   Barrows L.R.;
RT   "Isolation of pyrrolocins A-C: cis- and trans-decalin tetramic acid
RT   antibiotics from an endophytic fungal-derived pathway.";
RL   J. Nat. Prod. 77:2537-2544(2014).
CC   -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates
CC       the biosynthesis of pyrrolocin, a bright yellow trans-fused decalin-
CC       containing tetramic acid with antimicrobial activity (PubMed:25226362,
CC       PubMed:25351193). The PKS module of prlS together with the
CC       enoylreductase prlC catalyze the formation of the polyketide unit which
CC       is then conjugated to L-serine by the condensation domain of the prlS
CC       NRPS module (PubMed:25226362). Diels-Alderase gNR600 is involved in
CC       endo-selective Diels-Alder cycloaddition to form the decalin ring (By
CC       similarity). Subsequent methylation is carried leads to pyrrolocin A
CC       (PubMed:25226362). The methyltransferase involved in that last step has
CC       not been identified yet and is probably located outside of the prl
CC       cluster (PubMed:25226362). {ECO:0000250|UniProtKB:A0A0E4AZP0,
CC       ECO:0000269|PubMed:25226362, ECO:0000269|PubMed:25351193}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25226362}.
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; KM107910; AIP87505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A089FS99; -.
DR   SMR; A0A089FS99; -.
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..360
FT                   /note="Trans-enoyl reductase prlC"
FT                   /id="PRO_0000441298"
FT   BINDING         50..53
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         136..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         171..174
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         194..197
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         212
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         259..260
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         280..284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         349..350
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ   SEQUENCE   360 AA;  38112 MW;  443359E2D04615E4 CRC64;
     MGSLEKARRT QTAVVGNNQG GVQLSHDAPI PEAKGDIVVV RAEAVSVNPV DAKMRGQYVT
     SGAIGGCDFA GVVVEVGLDA AKYDIKVGDR VCAAIMGMNP LEPAHGAFSE YVGAHAFALV
     KIPPTVSFES AAALCTCFMT CGLALFRSLQ LPGHPLSPSS KPLPVLVYGG ATATGTAAIQ
     LLRLAGFTPV VTCSPHSYDL IKSYGAEAAF DYHDPDCAAQ IRAQTKNGLR FALDCITNTQ
     SMQICYAALG RAGGRYTALD PYPEAVAATR KIIKADWVIG PVMLGLDIGW PAPHGRKADP
     DLFEFGQRWK ATVQQLLNQG LIREHPLFVQ SGGLSRVIDS MEAILAKKVS GKKMVCKLSQ