{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"G0REX6","uniProtkbId":"ILIA_TRIR6","entryAudit":{"firstPublicDate":"2022-08-03","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-10-19","entryVersion":92,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Trichoderma reesei (strain QM6a)","commonName":"Filamentous fungus","synonyms":["Hypocrea jecorina"],"taxonId":431241,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Hypocreaceae","Trichoderma"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34947016"}],"value":"Hybrid PKS-NRPS synthetase iliA"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34947016"}],"value":"PKS-NRPS iliA"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34947016"}],"value":"2.3.1.-"},{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34947016"}],"value":"6.3.2.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34947016"}],"value":"Ilicicolin H biosynthesis cluster protein A"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"34947016"}],"value":"iliA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"40069746"}],"value":"triliA"}],"orfNames":[{"value":"TRIREDRAFT_58285"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34947016"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40069746"}],"value":"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:34947016, PubMed:40069746). IliA assembles the backbone of ilicicolin H (PubMed:34947016, PubMed:40069746). The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly (PubMed:34947016). The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate (PubMed:34947016). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain (PubMed:34947016). The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iliE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. 8-epi-ilicicolin H might also spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, albeit at a significantly lower level (PubMed:34947016, PubMed:40069746). Hypocrea jecorina strain QM6a produces also ilicicolin K that differs from ilicicolin H in its structure by a second hydroxylation of the tyrosine derived phenol and an additional ring formed by an intramolecular ether bridge of the hydroxyl group at the pyridone towards the tyrosine moiety of the molecule. The formation of this product is not merely a spontaneous side reaction but may be catalyzed by additional highly specific enzymes that still need to be identified (PubMed:40069746)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosine + holo-[ACP] + 7 malonyl-CoA + acetyl-CoA + 8 AH2 + 2 S-adenosyl-L-methionine + ATP + 4 H(+) = N-[(4E,6E,10S,12Z,14E)-6,10-dimethyl-3-oxohexadeca-4,6,12,14-tetraenoyl]-L-tyrosyl-[ACP] + 8 A + AMP + 2 S-adenosyl-L-homocysteine + 7 CO2 + diphosphate + 8 CoA + 6 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64544"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:16623"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57384"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:58315"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:155893"},{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34947016"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:64545"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34947016"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34947016"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40069746"}],"value":"Mycotoxin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40069746"}],"value":"Expression is silenced under common cultivation conditions and positively regulated by the cluster-specific transcription factor triliR"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"34947016"}],"value":"IliA has the following domain architecture: KS-MAT-DH-MT-KR-ACP-C-A-T-R. The PKS module (domains KS to ACP) is responsible for the biosynthesis of the polyketide chain and catalyzes three Claisen condensations, as well as beta-keto processing and methylation. The downstream NRPS module contains the condensation (C), adenylation (A), and thiolation (T) domains and catalyzes the formation of the L-tyrosinyl-thioester and the amide linkage between L-tyrosinyl-thioester and the tetraketide. The bimodular assembly line is terminated with a putative reductase (R) domain that facilitates formation and release of the tetramic acid product"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40069746"}],"value":"Abolishes the production of ilicicolin H"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23562597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24900384"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"40069746"}],"value":"Ilicicolin H and ilicicolin K exhibit antifungal activity against Sacharomyces cerevisiae as well as against fungal human pathogens such as Cryptococcus species, Aspergillus fumigatus or Candida auris"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the C-terminal section; belongs to the NRP synthetase 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