ID   ILID_NEOS2              Reviewed;         244 AA.
AC   P0DO33;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=S-adenosyl-L-methionine-dependent Diels-Alderase iliD {ECO:0000303|PubMed:31216742};
DE            EC=2.1.-.- {ECO:0000269|PubMed:31216742};
DE   AltName: Full=C-methyltransferase iliD {ECO:0000303|PubMed:31216742};
DE   AltName: Full=Ilicicolin H biosynthesis cluster protein D {ECO:0000303|PubMed:31216742};
DE   AltName: Full=Pericyclase iliD {ECO:0000250|UniProtKB:A0A482NB13};
GN   Name=iliD {ECO:0000303|PubMed:31216742};
OS   Neonectria sp. (strain DH2).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria;
OC   unclassified Neonectria.
OX   NCBI_TaxID=1735992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, CATALYTIC
RP   ACTIVITY, AND PATHWAY.
RX   PubMed=31216742; DOI=10.3390/molecules24122267;
RA   Lin X., Yuan S., Chen S., Chen B., Xu H., Liu L., Li H., Gao Z.;
RT   "Heterologous expression of ilicicolin H biosynthetic gene cluster and
RT   production of a new potent antifungal reagent, ilicicolin J.";
RL   Molecules 24:0-0(2019).
CC   -!- FUNCTION: S-adenosyl-l-methionine-dependent Diels-Alderase; part of the
CC       gene cluster that mediates the biosynthesis of ilicicolin H, a 4-
CC       hydroxy-2-pyridonealkaloid that has potent and broad antifungal
CC       activities by inhibiting the mitochondrial respiration chain
CC       (PubMed:31216742). IliD catalyzes the Diels-Alder reaction that
CC       converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H
CC       (PubMed:31216742). The biosynthesis of ilicicolin H starts with
CC       formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA
CC       with the partnering trans-enoyl reductase iliB since iliA lacks a
CC       designated enoylreductase (ER) domain. The cytochrome P450
CC       monooxygenase iliC then catalyzes the ring expansion of the tetramate
CC       to the acyclic 2-pyridone. The pericyclase iliD further converts the
CC       acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might
CC       then spontaneously convert to ilicicolin H since ilicicolin H is
CC       produced in the absence of the epimerase iliE, in contrast to what was
CC       observed for the Talaromyces variabilis ilicolin H biosynthetic pathway
CC       (PubMed:31216742) (Probable). {ECO:0000269|PubMed:31216742,
CC       ECO:0000305|PubMed:31216742}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-[(2E,4E,8S,10E,12Z)-4,8-dimethyltetradeca-2,4,10,12-
CC         tetraenoyl]-4-hydroxy-5-(4-hydroxyphenyl)-1,2-dihydropyridin-2-one =
CC         ilicicolin H; Xref=Rhea:RHEA:64568, ChEBI:CHEBI:77772,
CC         ChEBI:CHEBI:155889; Evidence={ECO:0000269|PubMed:31216742};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64569;
CC         Evidence={ECO:0000269|PubMed:31216742};
CC   -!- COFACTOR:
CC       Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000305|PubMed:31216742};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:31216742}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Erg6/SMT family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DO33; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..244
FT                   /note="S-adenosyl-L-methionine-dependent Diels-Alderase
FT                   iliD"
FT                   /id="PRO_0000453070"
SQ   SEQUENCE   244 AA;  27012 MW;  A4807B2AD1806B5F CRC64;
     MTSTEAAGTG KAPAIRANPA LQTYYESQES YLVYEVVLRG SHHFGFYEKD TYWPFPVGRS
     LERMEAKLLS ALALPSGSQI LDAGCGFGPV AISMAKKGMR VTAIDIIDHH VTKARRNVEK
     AGLPKGQVTV EKMDYQHLES IASESHDDAK AAATGFFRIL KPGGRIAFFE AQRSRTSGDY
     DEGDELAGHL KLVNEYTAMP TNELSREDYF KDLLEDAGFV DVEFTLPPGT REPREHWSYS
     ALKA