Protein: PTAA_PESFW
Sequence: MSDNSGSGTSPWGSLNTPVGPPKVTLAYFSNEFPPDDLNFIVRKLFDRTSKGPFCSIDGVLLCAIQFANLIGHYETTDHLFPFGSSIASVAGLGIGLVAAAAVSVTPSLADLPVAGAEAVRIAFRLGVLVDGVSQNLQPRDRSTTGTPDSWAYVIPDVSPEVVQKELDEIHSREKTPIPSKIFVSALSRTSVTISGPPARLRSLFRLSDFFRDRKFVALPVYGGLCHAGHIYEQRHVQEVVEKSVLDETHVRYSPSVRLFSTSTGKPFLSTSVTNLFEQVVGEILTQKIQWDKVVKGVLERIQELSATEVEVLVFRDSLPVHELVKALKSADSGLQTTTEDLLQWLHQSRERLQGPRGSLQSKIAIVGMSCRMPSGATDTEKFWELLEKGLDVHRKIPADRFDVETHHDPTGKRVNTSITPYGCFIDEPGLFDAGFFNMSPREAQQTDPMQRLALVTAYEALERAGYVANRTSATNLHRIGTFYGQASDDYREVNTAQEISTYFIPGGCRAFGPGRINYFFKFSGPSYSIDTACSSSLATIQAACTSLWNGDTDTVVAGGMNVLTNSDAFAGLGNGHFLSKTPNACKTWDCEADGYCRADGIGSIVMKRLEDAEADNDNILGVILGAGTNHSADAISITHPHAPSQAFLYRQILRDAALDPFDVSFVEMHGTGTQAGDSEEMQSVTEVFAPIANKRRTSKQPLHIGAVKSNVGHGEAVAGVTALIKVLLMFQKEAIPPHAGIKNSINPGFPKDLDKRNINIPYQKTAWPRSTDRKRIAVVNNFSAAGGNTTIAIEEGPLRQTIGHDPRTTHLIPISAKSKVSLKGNIQRLIDYLEVSPDVSLADLSYSLTARRYHHSHRVAITTSDVAHLKKQLRSQLDSADSHKPIVAAAGPPPVAFAFTGQGASYGTMDLELYHESKYFRDQILQLDSFAQGQGFPSFVPAIDGSFPKEHTHRPVVTQLALLCTEIALAKYWASLGVKPDVVIGHSLGEYAALHVAGVLSASDAIFLVGQRALMLEKKCQAGSHKMLAVRASLAQVQEAAGELPYEVACINGQKDTVLSAAKDDIDKLASVLESAGYKCFSLDVAFAFHSAQTDPILDDFESVSRTGVLFQAPNLPVISPLLGKVVFNDKTINANYVRRATRESVDFLSALEAAQKISIIDESTTWIEIGPHPVCMGFIRSAVPSIKVASPSIRRGENNWQTLVQTLGALHLAGIPVDWNEYHRPFEQALRLLDLPTYSWNDKTYWIQYNGDWALTKGNTFYDAEKAAKAPRVGGDLPPSPISTSTVHRVIGETFDGTAGTVDIQSDLMQQDFHDAAYGHKMNNCGVVTSSIHADIVYTIGRYLHTKLKPGVKDIHMNISNLEVVKGLVAQKNRDVPQLIQVSISTEDISSGTAQVTWFNVLPDGGLDEPFATATLFYGKANDWLQSWIPTTHLVLGRVHELERLAEQGVANRFSRNMAYGLFARNLVDYADKYRGMQSVVLHGLEAFADVELTKEKGGTWTVPPFFIDSVAHLAGFIMNVSDAVDTANNFCVTPGWESMRFARPLLAGARYRSYVKMIPTEEDAGVFLGDVYIFQDNKIIGQVRGIKFRRYPRLLLDRFFSAPDAAKHGGKHAPAVKAAIPPALEKKSAVVVAQVPVVDKPPPTKENAVAAPAAKSPEPVAAAAVNEDSITVKAMALVAAEAALDVSELEDDVQFANIGVDSLMSLVIAEKFRETLGVTISGSLFLEYPAVGDLRAWLLEYYG
What is the function of this protein?
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702).  The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA (PubMed:24302702).  As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain (PubMed:24302702).  The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702).  Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC (PubMed:24302702).  Spontaneous decarboxylation of endocrocin occurs to generate emodin (PubMed:24302702).  An O-methyltransferase (ptaH or ptaI) could methylate emodin to form physcion (PubMed:24302702).  PtaJ could then catalyze the oxidative cleavage of physcion, and rotation of the intermediate could then afford desmethylisosulochrin (PubMed:24302702).  PtaF, a putative NADH-dependent oxidoreductase, might also participate in the oxidative cleavage step (PubMed:24302702).  Desmethylisosulochrin is then transformed by another O-methyltransferase (ptaH or ptaI) to form isosulochrin (PubMed:24302702).  Chlorination of isosulochrin by ptaM in the cyclohexadienone B ring then produces chloroisosulochrin (PubMed:24302702).  PtaE is responsible for the oxidative coupling reactions of both benzophenones isosulochrin and chloroisosulochrin to RES-1214-1 and pestheic acid respectively, regardless of chlorination.
What are the official names of this protein?
Non-reducing polyketide synthase ptaA, Pestheic acid biosynthesis cluster protein A.