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Oxydoreductase ptaK (EC 1.-.-.-) (Pestheic acid biosynthesis cluster protein K)

 PTAK_PESFW              Reviewed;         585 AA.
A0A067XMP2; W3WUZ4;
31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
31-JAN-2018, sequence version 2.
20-JUN-2018, entry version 9.
RecName: Full=Oxydoreductase ptaK {ECO:0000303|PubMed:24302702};
EC=1.-.-.- {ECO:0000305|PubMed:24302702};
AltName: Full=Pestheic acid biosynthesis cluster protein K {ECO:0000303|PubMed:24302702};
Flags: Precursor;
Name=ptaK {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10836;
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: Oxydoreductase; 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 isosulochrin
and chloroisosulochrin to RES-1214-1 and pestheic acid
respectively, regardless of chlorination.
{ECO:0000269|PubMed:24302702}.
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000305|PubMed:24302702}.
-!- INDUCTION: The cluster is expressed in rice fermentation medium
(PubMed:25623211). 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:25623211,
ECO:0000305|PubMed:24302702}.
-!- DISRUPTION PHENOTYPE: Does not affect the production of pestheic
acid (PubMed:24302702). {ECO:0000269|PubMed:24302702}.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AGO59052.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; KC145148; AGO59052.1; ALT_SEQ; Genomic_DNA.
EMBL; KI912116; ETS76962.1; -; Genomic_DNA.
RefSeq; XP_007837608.1; XM_007839417.1.
SMR; A0A067XMP2; -.
EnsemblFungi; ETS76962; ETS76962; PFICI_10836.
GeneID; 19275849; -.
KEGG; pfy:PFICI_10836; -.
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 21 585 Oxydoreductase ptaK. {ECO:0000255}.
/FTId=PRO_5001647983.
DOMAIN 71 184 Plastocyanin-like 1. {ECO:0000255}.
DOMAIN 195 355 Plastocyanin-like 2. {ECO:0000255}.
DOMAIN 431 551 Plastocyanin-like 3. {ECO:0000255}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 362 362 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 411 411 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 422 422 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 441 441 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 574 574 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
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


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