ID   PTAJ_PESFW              Reviewed;         444 AA.
AC   A0A067XMK8; W3WVT2;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Baeyer-Villiger oxidase ptaJ {ECO:0000303|PubMed:24302702};
DE            EC=1.-.-.- {ECO:0000305|PubMed:24302702};
DE   AltName: Full=Pestheic acid biosynthesis cluster protein J {ECO:0000303|PubMed:24302702};
GN   Name=ptaJ {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10835;
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: Baeyer-Villiger oxidase; 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 isosulouchrin and chloroisosulouchrin
CC       to RES-1214-1 and pestheic acid respectively, regardless of
CC       chlorination. {ECO:0000269|PubMed:24302702}.
CC   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC         Evidence={ECO:0000250|UniProtKB:Q0CCX5};
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 questin oxidase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KC145148; AGO59039.1; -; Genomic_DNA.
DR   EMBL; KI912116; ETS76961.1; -; Genomic_DNA.
DR   RefSeq; XP_007837607.1; XM_007839416.1.
DR   AlphaFoldDB; A0A067XMK8; -.
DR   EnsemblFungi; ETS76961; ETS76961; PFICI_10835.
DR   GeneID; 19275848; -.
DR   KEGG; pfy:PFICI_10835; -.
DR   eggNOG; ENOG502S69W; Eukaryota.
DR   OMA; IDFFYMH; -.
DR   OrthoDB; 614605at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR025337; Questin_oxidase-like.
DR   PANTHER; PTHR35870; PTHR35870; 1.
DR   Pfam; PF14027; Questin_oxidase; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..444
FT                   /note="Baeyer-Villiger oxidase ptaJ"
FT                   /id="PRO_0000443049"
SQ   SEQUENCE   444 AA;  48827 MW;  171BFF5FECABABCF CRC64;
     MAASTAAQVQ LSEEALGLAR IFENPKGSLE AASKLLQKNH DEFHVFWRDV GGHNHIPHSV
     LSILALGGGP AELQRAWDDG VAIQRPTPPL DEDVVKKLEN PAEFRARIGS IPNYTNFLHF
     FRNQMDKKGW QAVVSEYAFS RTPLAETIFA QLFEGAYHPF IHIGFGIEFN LPSIIAEGLA
     QAATHDSAGI EGFFLEAERQ AAQSKGPGKS LVQLLDEVRT TEKIKTAARL PDGPVRVRDG
     VIGRAGAEIA ALASQFRVPA DQLSRGAAES INISAYTAGA AQRAGKARKI DFFHMHNTTS
     SLFLTVFLNQ PWISTEDKVR IVEWKGRLDL VWYAACSAPD LNVDHVIGYK PAQSAGWGWK
     ELYEAINVAH DDGHLAKIVR ALKNGEEVSR PFESGEGAEA FPIKGDSWLK LAQMSYDTTL
     DLPDDDKWIW GAGFLPLWNK VPSL