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The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). 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The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG (PubMed:30952781). On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring (PubMed:30952781, PubMed:35418536). Finally, ascofuranol is oxidized into ascofuranone by ascJ (PubMed:30952781, PubMed:35418536)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ilicicolin A + NADPH + O2 + H(+) = ilicicolin A epoxide + NADP(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:63092"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:146154"},{"database":"ChEBI","id":"CHEBI:146155"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35418536"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:63093"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35418536"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y8G7"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y8G7"}],"value":"Binds 1 FAD."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y8G7"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y8G7"}],"value":"Binds 1 FMN."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y8G7"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35418536"}],"value":"Secondary metabolite biosynthesis; terpenoid biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"}],"value":"Expression is induced on AF medium"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"}],"value":"Impairs the production of ascochlorin and ascofuranone, and leads to the accumulation of ilicicolin A"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12084465"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12798927"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20688188"}],"value":"Ascofuranone is a specific inhibitor of trypanosome alternative oxidase (TAO), and quickly kills African trypanosomes in vitro and cures infected mice. As an essential factor for trypanosome survival, TAO is a promising drug target due to the absence of alternative oxidases in the mammalian host"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the N-terminal section; belongs to the cytochrome P450 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1064,"modifier":"EXACT"}},"description":"Bifunctional cytochrome P450/NADPH--P450 reductase ascE","featureId":"PRO_0000448999"},{"type":"Domain","location":{"start":{"value":504,"modifier":"EXACT"},"end":{"value":644,"modifier":"EXACT"}},"description":"Flavodoxin-like","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00088"}]},{"type":"Domain","location":{"start":{"value":676,"modifier":"EXACT"},"end":{"value":905,"modifier":"EXACT"}},"description":"FAD-binding FR-type","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00716"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"Cytochrome P450","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y8G7"}]},{"type":"Region","location":{"start":{"value":485,"modifier":"EXACT"},"end":{"value":1064,"modifier":"EXACT"}},"description":"NADPH-P-450 reductase","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y8G7"}]},{"type":"Binding site","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14779"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":514,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00088"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":588,"modifier":"EXACT"},"end":{"value":620,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00088"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P14779"}]}],"keywords":[{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0274","category":"Ligand","name":"FAD"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0288","category":"Ligand","name":"FMN"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0521","category":"Ligand","name":"NADP"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"30952781","citationType":"journal article","authors":["Araki Y.","Awakawa T.","Matsuzaki M.","Cho R.","Matsuda Y.","Hoshino S.","Shinohara Y.","Yamamoto M.","Kido Y.","Inaoka D.K.","Nagamune K.","Ito K.","Abe I.","Kita K."],"citationCrossReferences":[{"database":"PubMed","id":"30952781"},{"database":"DOI","id":"10.1073/pnas.1819254116"}],"title":"Complete biosynthetic pathways of ascofuranone and ascochlorin in Acremonium egyptiacum.","publicationDate":"2019","journal":"Proc. 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The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG (PubMed:30952781, PubMed:35418536). On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring (PubMed:30952781). Finally, ascofuranol is oxidized into ascofuranone by ascJ (PubMed:30952781, PubMed:35418536)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3 malonyl-CoA + acetyl-CoA + 2 H(+) = orsellinate + 3 CO2 + 4 CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:62972"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16162"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57384"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35418536"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:62973"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35418536"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35418536"}],"value":"Secondary metabolite biosynthesis; terpenoid biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30952781"}],"value":"Expression is induced on AF medium"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30952781"}],"value":"Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5ATJ7"}],"value":"The release of the polyketide chain from the non-reducing polyketide synthase is mediated by the thioesterase (TE) domain localized at the C-ter of the protein"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12084465"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12798927"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20688188"}],"value":"Ascofuranone is a specific inhibitor of trypanosome alternative oxidase (TAO), and quickly kills African trypanosomes in vitro and cures infected mice. 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The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG (PubMed:30952781). On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring (PubMed:30952781, PubMed:35418536). 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part of the asc-1 gene cluster that mediates the biosynthesis of both ascochlorin and ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis (PubMed:30952781, PubMed:35418536). The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG (PubMed:30952781). On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring (PubMed:30952781, PubMed:35418536). 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The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). 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