ID   PTAF_PESFW              Reviewed;         261 AA.
AC   A0A067XNH7; W3WSW6;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Oxidoreductase ptaF {ECO:0000303|PubMed:24302702};
DE            EC=1.-.-.- {ECO:0000305|PubMed:24302702};
DE   AltName: Full=Pestheic acid biosynthesis cluster protein F {ECO:0000303|PubMed:24302702};
GN   Name=ptaF {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10829;
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: Oxidoreductase; part of the gene cluster that mediates the
CC       biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic
CC       precursor of the unique chloropupukeananes (PubMed:24302702). The
CC       biosynthesis initiates from condensation of acetate and malonate units
CC       catalyzed by the non-reducing PKS ptaA (PubMed:24302702). As the ptaA
CC       protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization
CC       of the polyketide could be catalyzed by ptaB containing a beta-
CC       lactamase domain (PubMed:24302702). The ptaB protein might hydrolyze
CC       the thioester bond between the ACP of ptaA and the intermediate to
CC       release atrochrysone carboxylic acid, which is spontaneously dehydrated
CC       to form endocrocin anthrone (PubMed:24302702). Endocrocin anthrone is
CC       then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC
CC       (PubMed:24302702). Spontaneous decarboxylation of endocrocin occurs to
CC       generate emodin (PubMed:24302702). An O-methyltransferase (ptaH or
CC       ptaI) could methylate emodin to form physcion (PubMed:24302702). PtaJ
CC       could then catalyze the oxidative cleavage of physcion, and rotation of
CC       the intermediate could then afford desmethylisosulochrin
CC       (PubMed:24302702). PtaF, a putative NADH-dependent oxidoreductase,
CC       might also participate in the oxidative cleavage step
CC       (PubMed:24302702). Desmethylisosulochrin is then transformed by another
CC       O-methyltransferase (ptaH or ptaI) to form isosulochrin
CC       (PubMed:24302702). Chlorination of isosulochrin by ptaM in the
CC       cyclohexadienone B ring then produces chloroisosulochrin
CC       (PubMed:24302702). PtaE is responsible for the oxidative coupling
CC       reactions of both benzophenones isosulouchrin 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 avfA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ETS76955.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; KC145148; AGO59035.1; -; Genomic_DNA.
DR   EMBL; KI912116; ETS76955.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_007837601.1; XM_007839410.1.
DR   AlphaFoldDB; A0A067XNH7; -.
DR   SMR; A0A067XNH7; -.
DR   STRING; 1229662.A0A067XNH7; -.
DR   EnsemblFungi; ETS76955; ETS76955; PFICI_10829.
DR   GeneID; 19275842; -.
DR   KEGG; pfy:PFICI_10829; -.
DR   eggNOG; ENOG502SM0C; Eukaryota.
DR   OrthoDB; 1166292at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF13460; NAD_binding_10; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..261
FT                   /note="Oxidoreductase ptaF"
FT                   /id="PRO_0000443042"
SQ   SEQUENCE   261 AA;  28284 MW;  7672C7D54F132460 CRC64;
     MSRYAILGST GNCGTALIEN VLDSSMTEVH AFCRNQEKLE RLVPRVISDA RVKVFVGGIG
     DTETLAACLH GCNAVFLCIT TNDNVPGCRV AQDTALGVVK VLERSRADGF LPMPKLVLLS
     SATIDDVLSR NTPWVLRSIL LKSASHVYED LRKTEILLRA EQDWLTTIFI KPGALSVDIQ
     RGHALSLTDE DSPVSYLDLA AAMIEAVNDP QGRYDMRNVG VVNTHGRANF PSGTPLCIAV
     GLLSHFAPFL HPYLPSGTGP R