ID   ILID_HYPJQ              Reviewed;         305 AA.
AC   P9WEU0;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=S-adenosyl-L-methionine-dependent Diels-Alderase iliD {ECO:0000303|PubMed:34947016};
DE            EC=2.1.-.- {ECO:0000269|PubMed:34947016};
DE   AltName: Full=C-methyltransferase iliD {ECO:0000303|PubMed:34947016};
DE   AltName: Full=Ilicicolin H biosynthesis cluster protein D {ECO:0000303|PubMed:34947016};
DE   AltName: Full=Pericyclase iliD {ECO:0000303|PubMed:34947016};
GN   Name=iliD {ECO:0000303|PubMed:34947016};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a;
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND PATHWAY.
RX   PubMed=34947016; DOI=10.3390/jof7121034;
RA   Shenouda M.L., Ambilika M., Cox R.J.;
RT   "Trichoderma reesei Contains a Biosynthetic Gene Cluster That Encodes the
RT   Antifungal Agent Ilicicolin H.";
RL   J. Fungi 7:0-0(2021).
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:34947016). IliD catalyzes the Diels-Alder reaction that
CC       converts the acyclic 2-pyridone intermediate to 8-epi-ilicicolin H
CC       (PubMed:34947016). 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:34947016) (Probable). {ECO:0000269|PubMed:34947016,
CC       ECO:0000305|PubMed:34947016}.
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:34947016};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64569;
CC         Evidence={ECO:0000269|PubMed:34947016};
CC   -!- COFACTOR:
CC       Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000305|PubMed:34947016};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:34947016}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Erg6/SMT family. {ECO:0000305}.
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DR   EMBL; GL985060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..305
FT                   /note="S-adenosyl-L-methionine-dependent Diels-Alderase
FT                   iliD"
FT                   /id="PRO_0000455714"
SQ   SEQUENCE   305 AA;  34700 MW;  5FB02C2F1DA40120 CRC64;
     MSSTQTTAAE PIMTDNVALR AYYESWDSRV VYQIIMGGTQ HFGYWDKDTY WPFPLGSKLR
     RSMEQKLMEI LALPKGSRVL DAGCGVGHVA RYMAQHGMRV FGIDIIDWAI EDARKAAKDA
     GLSKEMMSVE KMDYHHLDSL ASESFDGVYT MQAFGHAVDP QKAMAGFFRV VRPGGRIAMV
     EVERKTAAKH DDPNDRLTQE LKMVNDYTVM PTNEAASEDY FKNLLEEAGF VDVVVRDWQP
     NILPILRLFY SLVMIPYLFF RLFGNEKSFI NMICARSGYA GRSRWRFVAI TATKAGEKLE
     DHKSK