ID   PRL3_FUNXX              Reviewed;         408 AA.
AC   A0A089GT80;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   26-NOV-2014, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Diels-Alderase gNR600 {ECO:0000303|PubMed:25226362};
DE            EC=5.5.1.- {ECO:0000305|PubMed:25226362};
DE   AltName: Full=Pyrrolocin biosynthesis protein gNR600 {ECO:0000303|PubMed:25226362};
GN   ORFNames=gNR600 {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: Diels-Alderase; part of the gene cluster that mediates the
CC       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:0000305|PubMed:25226362}.
CC   -!- SIMILARITY: Belongs to the Diels-Alderase family. {ECO:0000305}.
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DR   EMBL; KM107910; AIP87501.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A089GT80; -.
DR   SMR; A0A089GT80; -.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..408
FT                   /note="Diels-Alderase gNR600"
FT                   /id="PRO_0000441294"
SQ   SEQUENCE   408 AA;  43397 MW;  F91031340FA42AF3 CRC64;
     MAGTFVSVLD ISGDSVVTGP VPVEPFVPGS ANLFPKMTSR INDTAWELWE FEGFSAGGEA
     AVGVSLYRDA RGVDKGGFHA EVNAIWPDGR KWGQTLYFAE SIVTAEGASP DEGRIHGFWR
     SNSNTAGGAP AAARSITFSI SEDLGVATVC FSVPDQVTGT IELRSSGSNR KSCLPATEEA
     ALLYPSVYYM FPMGPVDANA DLTFSFSATA GGEIEEERKL SVQSRGGGHG GMVRGWSTEA
     WPQFMNDAYY VVAKVGSYML QMLRVVGSAA AGHRPYAVAR LYLNKELVCA ANQAVDAQSA
     AEGSTATTQP RDMVAVEKVL SEPKSQEQVV SGAFSDKNIG YVIEFISGQQ KRWRFDARHK
     RAWWSEPTSA PGPGCTGKSG WIEGFLGGSD GETFEGAGVG GQLQIPVP