ID   PTAD_PESFW              Reviewed;         138 AA.
AC   A0A067XML2; W3WSV4;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Probable decarboxylase ptaD {ECO:0000303|PubMed:24302702};
DE            EC=1.-.-.- {ECO:0000305|PubMed:24302702};
DE   AltName: Full=Pestheic acid biosynthesis cluster protein D {ECO:0000303|PubMed:24302702};
GN   Name=ptaD {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10827;
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX   NCBI_TaxID=1229662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=W106-1 / CGMCC3.15140;
RX   PubMed=24302702; DOI=10.1002/cbic.201300626;
RA   Xu X., Liu L., Zhang F., Wang W., Li J., Guo L., Che Y., Liu G.;
RT   "Identification of the first diphenyl ether gene cluster for pestheic acid
RT   biosynthesis in plant endophyte Pestalotiopsis fici.";
RL   ChemBioChem 15:284-292(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC   STRAIN=W106-1 / CGMCC3.15140;
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT   of natural products.";
RL   BMC Genomics 16:28-28(2015).
CC   -!- FUNCTION: Probable decarboxylase; part of the gene cluster that
CC       mediates the biosynthesis of pestheic acid, a diphenyl ether which is a
CC       biosynthetic precursor of the unique chloropupukeananes
CC       (PubMed:24302702). The biosynthesis initiates from condensation of
CC       acetate and malonate units catalyzed by the non-reducing PKS ptaA
CC       (PubMed:24302702). As the ptaA protein is TE/CLC domain-deficient,
CC       hydrolysis and Claisen cyclization of the polyketide could be catalyzed
CC       by ptaB containing a beta-lactamase domain (PubMed:24302702). The ptaB
CC       protein might hydrolyze the thioester bond between the ACP of ptaA and
CC       the intermediate to release atrochrysone carboxylic acid, which is
CC       spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702).
CC       Endocrocin anthrone is then converted to endocrocin, catalyzed by the
CC       anthrone oxygenase ptaC (PubMed:24302702). Spontaneous decarboxylation
CC       of endocrocin occurs to generate emodin (PubMed:24302702). An O-
CC       methyltransferase (ptaH or ptaI) could methylate emodin to form
CC       physcion (PubMed:24302702). PtaJ could then catalyze the oxidative
CC       cleavage of physcion, and rotation of the intermediate could then
CC       afford desmethylisosulochrin (PubMed:24302702). PtaF, a putative NADH-
CC       dependent oxidoreductase, might also participate in the oxidative
CC       cleavage step (PubMed:24302702). Desmethylisosulochrin is then
CC       transformed by another O-methyltransferase (ptaH or ptaI) to form
CC       isosulochrin (PubMed:24302702). Chlorination of isosulochrin by ptaM in
CC       the cyclohexadienone B ring then produces chloroisosulochrin
CC       (PubMed:24302702). PtaE is responsible for the oxidative coupling
CC       reactions of both benzophenones isosulochrin and chloroisosulochrin to
CC       RES-1214-1 and pestheic acid respectively, regardless of chlorination.
CC       {ECO:0000269|PubMed:24302702}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:24302702}.
CC   -!- INDUCTION: The cluster is expressed in rice fermentation medium
CC       (PubMed:25623211). Three regulators are located in the cluster (ptaR1,
CC       ptaR2 and ptaR3), suggesting that the production of pestheic acid is
CC       controlled by a complex regulatory mechanism (PubMed:24302702).
CC       {ECO:0000269|PubMed:25623211, ECO:0000305|PubMed:24302702}.
CC   -!- SIMILARITY: Belongs to the tpcK family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ETS76953.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; KC145148; AGO59044.1; -; Genomic_DNA.
DR   EMBL; KI912116; ETS76953.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_007837599.1; XM_007839408.1.
DR   AlphaFoldDB; A0A067XML2; -.
DR   SMR; A0A067XML2; -.
DR   EnsemblFungi; ETS76953; ETS76953; PFICI_10827.
DR   GeneID; 19275840; -.
DR   KEGG; pfy:PFICI_10827; -.
DR   eggNOG; ENOG502SJ0E; Eukaryota.
DR   OrthoDB; 1621831at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR009799; EthD_dom.
DR   Pfam; PF07110; EthD; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
PE   2: Evidence at transcript level;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..138
FT                   /note="Probable decarboxylase ptaD"
FT                   /id="PRO_0000443041"
FT   DOMAIN          28..111
FT                   /note="EthD"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   138 AA;  16244 MW;  361EF9EF40E6D399 CRC64;
     MAEMSKNPAS TLKPSRYLCL TICGYRKPGM SEEDYRYHMT QVSAPMTKDL MAKYGVKRWT
     MNYMIRRWPS CPTLTASAKL CLRTLEDYKR MKQDPWYKEH LIGDHEKFAD TKRSKMTIGW
     IEEWISDGKP VDGLEFKS