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PksPT catalyzes the first step of MonAzPs biosynthesis and forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The starter acyl transferase (SAT) domain of pigA selects an acetyl-CoA starter unit, and the ketoacyl synthase (KS)-acyl transferase (AT)-acyl carrier protein (ACP) domains extend this starter unit five times with malonyl-CoA in five successive decarboxylative Claisen condensation cycles. The methyltransferase (MT) domain conducts a single C-methylation at C-4, most likely at the pentaketide stage. The reactive hexaketide chain then undergoes a product template (PT) domain-mediated C-2 to C-7 aldol cyclization to afford the first aromatic ring, followed by reductive release of the first pathway intermediate by the NADPH-dependent reductive release (R) domain. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7) (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"pantetheine 4'-phosphate","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00258"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:47942"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41961403"}],"value":"Secondary metabolite biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30769930"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32220027"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32221575"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33576885"}],"value":"Expression is induced in the presence of NaCl (PubMed:30769930). Expression is stimulated by low-frequency magnetic field (PubMed:32220027). Expression is also controlled by the histone methyltransferase gene Ash2 (PubMed:32221575). Finally, expression is also stimulated in the presence of lanthanum(III) ion (PubMed:33576885)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A0A0S2CHA9"}],"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:0000269","source":"PubMed","id":"41961403"}],"value":"Abolishes the production of any kinds of Monascus pigments, resulting in a distinct albino phenotype"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16283302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16660141"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17191930"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20666456"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22562164"}],"value":"MonAzPs possess wide-ranging biological activities such as antibacterial activity, preventing hypertension, lowering cholesterol levels, causing hypolipidemic effects, and displaying antiobesity and antitumor activities"}],"commentType":"BIOTECHNOLOGY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":2742,"modifier":"EXACT"}},"description":"Non-reducing polyketide synthase 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