{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A0A1C8AX29","uniProtkbId":"PIGK_MONRU","entryAudit":{"firstPublicDate":"2024-05-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-11-30","entryVersion":40,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Monascus ruber","commonName":"Mold","taxonId":89489,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Monascus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28959415"}],"value":"Fatty acid synthase beta subunit pigK"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28959415"}],"value":"2.3.1.86"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"S-acyl fatty acid synthase thioesterase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"3.1.2.14"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"[Acyl-carrier-protein] malonyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"2.3.1.39"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"3-hydroxyacyl-[acyl-carrier-protein] dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"4.2.1.59"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"Enoyl-[acyl-carrier-protein] reductase [NADH]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"1.3.1.9"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"[Acyl-carrier-protein] acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}],"value":"2.3.1.38"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28959415"}],"value":"Azaphilone pigments biosynthesis cluster protein K"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28959415"}],"value":"pigK"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.1"}],"value":"fas2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26946170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28959415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34220766"}],"value":"Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants (PubMed:26946170, PubMed:28959415, PubMed:34220766). PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring (PubMed:28959415). The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. 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) (PubMed:28959415)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).","ecNumber":"2.3.1.86","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41788"},{"database":"Rhea","id":"RHEA-COMP:9621"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78446"}],"ecNumber":"2.3.1.38","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41792"},{"database":"Rhea","id":"RHEA-COMP:9623"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57384"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78449"}],"ecNumber":"2.3.1.39","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13097"},{"database":"Rhea","id":"RHEA-COMP:9925"},{"database":"Rhea","id":"RHEA-COMP:9945"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:78784"},{"database":"ChEBI","id":"CHEBI:78827"}],"ecNumber":"4.2.1.59","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10240"},{"database":"Rhea","id":"RHEA-COMP:9925"},{"database":"Rhea","id":"RHEA-COMP:9926"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:78784"},{"database":"ChEBI","id":"CHEBI:78785"}],"ecNumber":"1.3.1.9","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15057"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9924"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30823"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78783"}],"ecNumber":"3.1.2.14","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8TGA1"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26946170"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28959415"}],"value":"Secondary metabolite biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19097"}],"value":"[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34220766"}],"value":"Expression does not seem to be regulated by the azaphilone pigments (MonAzPs) gene cluster-specific transcription regulator pigB"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28959415"}],"value":"Leads to the accumulation of pyran intermediates devoid of the medium-chain fatty acyl moiety such as monascusone A"}],"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"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37087240"}],"value":"As colorants, MonAzPs are widely used in various food products for centuries (PubMed:37087240). Moreover, MonAzPs also possess wide-ranging biological activities such as antibacterial activity, preventing hypertension, lowering cholesterol levels, causing hypolipidemic effects, and displaying antiobesity and antitumor activities (PubMed:16283302, PubMed:16660141, PubMed:17191930, PubMed:20666456, PubMed:22562164)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the fungal fatty acid synthetase subunit beta family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":2014,"modifier":"EXACT"}},"description":"Fatty acid synthase beta subunit pigK","featureId":"PRO_0000460204"},{"type":"Domain","location":{"start":{"value":1514,"modifier":"EXACT"},"end":{"value":1627,"modifier":"EXACT"}},"description":"MaoC-like","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"Acetyltransferase (AT) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":570,"modifier":"EXACT"},"end":{"value":815,"modifier":"EXACT"}},"description":"Enoyl reductase (ER) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":1126,"modifier":"EXACT"},"end":{"value":1606,"modifier":"EXACT"}},"description":"Dehydratase (DH) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":1645,"modifier":"EXACT"},"end":{"value":2005,"modifier":"EXACT"}},"description":"Malonyl/palmitoyl transferase (MT/PT) domain","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Active site","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"For acetyltransferase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PIRSR","id":"PIRSR005562-1"}]},{"type":"Active site","location":{"start":{"value":1790,"modifier":"EXACT"},"end":{"value":1790,"modifier":"EXACT"}},"description":"For malonyltransferase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"PIRSR","id":"PIRSR005562-1"}]}],"keywords":[{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"id":"KW-0520","category":"Ligand","name":"NAD"},{"id":"KW-0521","category":"Ligand","name":"NADP"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0608","category":"Ligand","name":"Pigment"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-AOM2SJ05SAD1F","citationType":"submission","authors":["Xie N.","Liu Q.","Chen F."],"title":"Identification of fas2, encoding a fatty synthase responsible for Monascus pigments biosynthesis in Monascus ruber.","publicationDate":"SEP-2012","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"M7","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"16660141","citationType":"journal article","authors":["Wong H.C.","Bau Y.S."],"citationCrossReferences":[{"database":"PubMed","id":"16660141"},{"database":"DOI","id":"10.1104/pp.60.4.578"}],"title":"Pigmentation and antibacterial activity of fast neutron- and X-ray-induced strains of Monascus purpureus went.","publicationDate":"1977","journal":"Plant Physiol.","firstPage":"578","lastPage":"581","volume":"60"},"referencePositions":["BIOTECHNOLOGY"]},{"referenceNumber":3,"citation":{"id":"17191930","citationType":"journal article","authors":["Akihisa T.","Tokuda H.","Ukiya M.","Kiyota A.","Yasukawa K.","Sakamoto N.","Kimura Y.","Suzuki T.","Takayasu J.","Nishino H."],"citationCrossReferences":[{"database":"PubMed","id":"17191930"},{"database":"DOI","id":"10.1002/cbdv.200590101"}],"title":"Anti-tumor-initiating effects of monascin, an azaphilonoid pigment from the extract of Monascus pilosus fermented rice (red-mold rice).","publicationDate":"2005","journal":"Chem. 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