PTAE_PESFW
ID PTAE_PESFW Reviewed; 610 AA.
AC A0A067XMP0; W3WT07;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Oxidoreductase ptaE {ECO:0000303|PubMed:24302702};
DE EC=1.-.-.- {ECO:0000305|PubMed:24302702};
DE AltName: Full=Dihydrogeodin oxidase {ECO:0000303|PubMed:24302702};
DE Short=DHGO {ECO:0000303|PubMed:24302702};
DE AltName: Full=Pestheic acid biosynthesis cluster protein E {ECO:0000303|PubMed:24302702};
DE Flags: Precursor;
GN Name=ptaE {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10828;
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, DISRUPTION PHENOTYPE, AND
RP 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:0000269|PubMed:24302702}.
CC -!- INDUCTION: The cluster is expressed in rice fermentation medium
CC (PubMed:25623211). Expression is correlated with the production of
CC pestheic acid (PubMed:24302702). Three regulators are located in the
CC cluster (ptaR1, ptaR2 and ptaR3), suggesting that the production of
CC pestheic acid is controlled by a complex regulatory mechanism
CC (PubMed:24302702). {ECO:0000269|PubMed:24302702,
CC ECO:0000269|PubMed:25623211}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of pestheic acid and
CC RES-1214-1, but accumulates isosulochrin and chloroisosulochrin
CC (PubMed:24302702). {ECO:0000269|PubMed:24302702}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AGO59042.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KC145148; AGO59042.1; ALT_SEQ; Genomic_DNA.
DR EMBL; KI912116; ETS76954.1; -; Genomic_DNA.
DR RefSeq; XP_007837600.1; XM_007839409.1.
DR AlphaFoldDB; A0A067XMP0; -.
DR SMR; A0A067XMP0; -.
DR EnsemblFungi; ETS76954; ETS76954; PFICI_10828.
DR GeneID; 19275841; -.
DR KEGG; pfy:PFICI_10828; -.
DR eggNOG; KOG1263; Eukaryota.
DR OMA; TFWIDGH; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
PE 2: Evidence at transcript level;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..610
FT /note="Oxidoreductase ptaE"
FT /id="PRO_0000443050"
FT DOMAIN 67..181
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 191..344
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 425..568
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 610 AA; 68758 MW; F5F87BE6DDD38970 CRC64;
MFQSILFLAF YGRPVFGSAA ARDYACVNTA ESRDCWKDGF NIETDYYGKE EAPEGKLVEY
ELTLSQQIIS PDGYEMLGMV VNGQYPGPTI EADWGDTLRI TVKNNFTENY NGTAVHWHGI
RQKETNWLDG VPGVTQCPIT PGDSQVYEFR VTQYGTSWYH SHYSLQYSNG AYGPIVIHGP
SSANWDVDLG PWLLSDWYHD DAFALDHVGI TTNRAAIPKS SLINGKGYYE CDPTNDAKCT
GTRDYYEVVL KQGTKYKFGI INTSTILTYT FWIDGHNFTI IAIDFVPIEP LTVDTLNVGI
GQRYEIIIET NPDFDDDSSF WMHAQYCFIN QTDIVDDKVG IVRYESAGSS DPPYINKSDY
HLNFGCADPK PESLVPILKQ QVGAQANPLA AEDYFRVGLG NFTWPDATNS TGSVFLWFLQ
KLPLYVNWSE PSVKKLTIDE TADFPPNSRP IELDYETGQW VYFVIESDWD PAGAVDQYGQ
EIRVEPSVHP FHLHGHDFLI LAQGLGKFTS DIQPNLDNPP RRDTVDVEPL GYVWIAFQID
NPGAWLFHCH IAFHSSDGIA IQFLEQPSKL KPIMEEAGVL GDFADRCNKW DDWYQAVNIP
HNATQADSGV
