PTAK_PESFW
ID PTAK_PESFW Reviewed; 585 AA.
AC A0A067XMP2; W3WUZ4;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Oxydoreductase ptaK {ECO:0000303|PubMed:24302702};
DE EC=1.-.-.- {ECO:0000305|PubMed:24302702};
DE AltName: Full=Pestheic acid biosynthesis cluster protein K {ECO:0000303|PubMed:24302702};
DE Flags: Precursor;
GN Name=ptaK {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10836;
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: Oxydoreductase; 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 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 -!- DISRUPTION PHENOTYPE: Does not affect the production of pestheic acid
CC (PubMed:24302702). {ECO:0000269|PubMed:24302702}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AGO59052.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KC145148; AGO59052.1; ALT_SEQ; Genomic_DNA.
DR EMBL; KI912116; ETS76962.1; -; Genomic_DNA.
DR RefSeq; XP_007837608.1; XM_007839417.1.
DR AlphaFoldDB; A0A067XMP2; -.
DR SMR; A0A067XMP2; -.
DR EnsemblFungi; ETS76962; ETS76962; PFICI_10836.
DR GeneID; 19275849; -.
DR KEGG; pfy:PFICI_10836; -.
DR eggNOG; KOG1263; Eukaryota.
DR OMA; QAHYYGI; -.
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..585
FT /note="Oxydoreductase ptaK"
FT /evidence="ECO:0000255"
FT /id="PRO_5001647983"
FT DOMAIN 71..184
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 195..355
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 431..551
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 585 AA; 64792 MW; D2577A37F1BEBDB8 CRC64;
MKSLFLTGLL SALTWASEFA SYPDIPLDYL YTTEPVTPLP QGYPWGSKTA NDSHPEEPTL
TGVIRSYDFH IKAGQIAPDG YLKDVLLVND QYPGPLIEAN WGDTIQVTVH NDLEEGTALH
WHAFLQKETP WQDGVPGITQ CPIAPGACFT YTFVADSYGT SWYHSHYSAQ YADGILGPII
VHGHPTVPYD IDLGPIMLSD LYHVPYTTVL EHLFDEDFAV VTKPANNNLI NGRNSWNCTL
KDLGDDTPCQ SNAPLSEFRL TPGKKHRLRI LNVGGSAIQK FSLDGHKLQV IAHDFVPVLP
YEVEFLTLGV GQRADVIVEA LANGTGTYTM RATIPPAPCA NSVDHDATAL VHYGNTTSTF
SNSSSEAWPS FIEALGVCDG LPTEEITPWY AIPAPEAPAT TQIINVTLAQ NETGQYLFYM
DNSSFRVNYN HPVLLLSNLG NNSYPDDPEW NVYNFGSNNS IRIVMYNNAI RTHPIHLHGH
NFFVEAVGLG EWDGHVDHPE NPVRRDTAML PQGGYMVISF NADNPGAWPL HCHVAWHVSS
GFYVTVLERP DEIAEYKIPS VVGQTCRDWW GYTNHTIVNQ IDSGL
