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 24-JAN-2024, entry version 7. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GL985060; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; P9WEU0; -. DR Proteomes; UP000008984; Unassembled WGS sequence. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR44068; ZGC:194242; 1. DR PANTHER; PTHR44068:SF1; ZGC:194242; 1. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. 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 //