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Oxidoreductase ptaE (EC 1.-.-.-) (Dihydrogeodin oxidase) (DHGO) (Pestheic acid biosynthesis cluster protein E)

 PTAE_PESFW              Reviewed;         610 AA.
A0A067XMP0; W3WT07;
31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
31-JAN-2018, sequence version 2.
28-FEB-2018, entry version 7.
RecName: Full=Oxidoreductase ptaE {ECO:0000303|PubMed:24302702};
EC=1.-.-.- {ECO:0000305|PubMed:24302702};
AltName: Full=Dihydrogeodin oxidase {ECO:0000303|PubMed:24302702};
Short=DHGO {ECO:0000303|PubMed:24302702};
AltName: Full=Pestheic acid biosynthesis cluster protein E {ECO:0000303|PubMed:24302702};
Flags: Precursor;
Name=ptaE {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10828;
Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Xylariomycetidae; Xylariales; Sporocadaceae;
Pestalotiopsis.
NCBI_TaxID=1229662;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
INDUCTION.
STRAIN=W106-1 / CGMCC3.15140;
PubMed=24302702; DOI=10.1002/cbic.201300626;
Xu X., Liu L., Zhang F., Wang W., Li J., Guo L., Che Y., Liu G.;
"Identification of the first diphenyl ether gene cluster for pestheic
acid biosynthesis in plant endophyte Pestalotiopsis fici.";
ChemBioChem 15:284-292(2014).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
STRAIN=W106-1 / CGMCC3.15140;
PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
"Genomic and transcriptomic analysis of the endophytic fungus
Pestalotiopsis fici reveals its lifestyle and high potential for
synthesis of natural products.";
BMC Genomics 16:28-28(2015).
-!- FUNCTION: Oxidoreductase; part of the gene cluster that mediates
the biosynthesis of pestheic acid, a diphenyl ether which is a
biosynthetic precursor of the unique chloropupukeananes
(PubMed:24302702). The biosynthesis initiates from condensation of
acetate and malonate units catalyzed by the non-reducing PKS ptaA
(PubMed:24302702). As the ptaA protein is TE/CLC domain-deficient,
hydrolysis and Claisen cyclization of the polyketide could be
catalyzed by ptaB containing a beta-lactamase domain
(PubMed:24302702). The ptaB protein might hydrolyze the thioester
bond between the ACP of ptaA and the intermediate to release
atrochrysone carboxylic acid, which is spontaneously dehydrated to
form endocrocin anthrone (PubMed:24302702). Endocrocin anthrone is
then converted to endocrocin, catalyzed by the anthrone oxygenase
ptaC (PubMed:24302702). Spontaneous decarboxylation of endocrocin
occurs to generate emodin (PubMed:24302702). An O-
methyltransferase (ptaH or ptaI) could methylate emodin to form
physcion (PubMed:24302702). PtaJ could then catalyze the oxidative
cleavage of physcion, and rotation of the intermediate could then
afford desmethylisosulochrin (PubMed:24302702). PtaF, a putative
NADH-dependent oxidoreductase, might also participate in the
oxidative cleavage step (PubMed:24302702). Desmethylisosulochrin
is then transformed by another O-methyltransferase (ptaH or ptaJ)
to form isosulochrin (PubMed:24302702). Chlorination of
isosulochrin by ptaM in the cyclohexadienone B ring then produces
chloroisosulochrin (PubMed:24302702). PtaE is responsible for the
oxidative coupling reactions of both benzophenones isosulouchrin
and chloroisosulochrin to RES-1214-1 and pestheic acid
respectively, regardless of chlorination.
{ECO:0000269|PubMed:24302702}.
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:24302702}.
-!- INDUCTION: The cluster is expressed in rice fermentation medium
(PubMed:25623211). Expression is correlated with the production of
pestheic acid (PubMed:24302702). Three regulators are located in
the cluster (ptaR1, ptaR2 and ptaR3), suggesting that the
production of pestheic acid is controlled by a complex regulatory
mechanism (PubMed:24302702). {ECO:0000269|PubMed:24302702,
ECO:0000269|PubMed:25623211}.
-!- DISRUPTION PHENOTYPE: Abolishes the production of pestheic acid
and RES-1214-1, but accumulates isosulochrin and
chloroisosulochrin (PubMed:24302702).
{ECO:0000269|PubMed:24302702}.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AGO59042.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; KC145148; AGO59042.1; ALT_SEQ; Genomic_DNA.
EMBL; KI912116; ETS76954.1; -; Genomic_DNA.
RefSeq; XP_007837600.1; XM_007839409.1.
EnsemblFungi; ETS76954; ETS76954; PFICI_10828.
GeneID; 19275841; -.
KEGG; pfy:PFICI_10828; -.
Proteomes; UP000030651; Unassembled WGS sequence.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
Gene3D; 2.60.40.420; -; 3.
InterPro; IPR001117; Cu-oxidase.
InterPro; IPR011706; Cu-oxidase_2.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR008972; Cupredoxin.
Pfam; PF00394; Cu-oxidase; 1.
Pfam; PF07731; Cu-oxidase_2; 1.
Pfam; PF07732; Cu-oxidase_3; 1.
SUPFAM; SSF49503; SSF49503; 3.
2: Evidence at transcript level;
Complete proteome; Copper; Glycoprotein; Metal-binding;
Oxidoreductase; Reference proteome; Repeat; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 610 Oxidoreductase ptaE.
/FTId=PRO_0000443050.
DOMAIN 67 181 Plastocyanin-like 1. {ECO:0000255}.
DOMAIN 191 344 Plastocyanin-like 2. {ECO:0000255}.
DOMAIN 425 568 Plastocyanin-like 3. {ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 602 602 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
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


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