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Non-reducing polyketide synthase ptaA (EC 2.3.1.-) (Pestheic acid biosynthesis cluster protein A)

 PTAA_PESFW              Reviewed;        1746 AA.
A0A067XNI2; W3WSW2;
31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
01-OCT-2014, sequence version 1.
28-FEB-2018, entry version 24.
RecName: Full=Non-reducing polyketide synthase ptaA {ECO:0000303|PubMed:24302702};
EC=2.3.1.- {ECO:0000305|PubMed:24302702};
AltName: Full=Pestheic acid biosynthesis cluster protein A {ECO:0000303|PubMed:24302702};
Name=ptaA {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10824;
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: Non-reducing polyketide synthase; 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: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}.
-!- DOMAIN: Multidomain protein; including a starter unit:ACP
transacylase (SAT) that selects the starter unit; a ketosynthase
(KS) that catalyzes repeated decarboxylative condensation to
elongate the polyketide backbone; a malonyl-CoA:ACP transacylase
(MAT) that selects and transfers the extender unit malonyl-CoA; a
product template (PT) domain that controls the immediate
cyclization regioselectivity of the reactive polyketide backbone;
and an acyl-carrier protein (ACP) that serves as the tether of the
growing and completed polyketide via its phosphopantetheinyl arm
(By similarity). {ECO:0000250|UniProtKB:Q5B0D0}.
-!- DISRUPTION PHENOTYPE: Totally abolishes the production of pestheic
acid but does not affect the production iso-A82775C, another
precursor of chloropupukeananes (PubMed:24302702).
{ECO:0000269|PubMed:24302702}.
-!- SEQUENCE CAUTION:
Sequence=ETS76950.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; KC145148; AGO59040.1; -; Genomic_DNA.
EMBL; KI912116; ETS76950.1; ALT_SEQ; Genomic_DNA.
RefSeq; XP_007837596.1; XM_007839405.1.
SMR; A0A067XNI2; -.
EnsemblFungi; ETS76950; ETS76950; PFICI_10824.
GeneID; 19275837; -.
KEGG; pfy:PFICI_10824; -.
Proteomes; UP000030651; Unassembled WGS sequence.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.40.366.10; -; 1.
Gene3D; 3.40.47.10; -; 1.
InterPro; IPR001227; Ac_transferase_dom_sf.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020807; PKS_dehydratase.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR030918; PT_fungal_PKS.
InterPro; IPR032088; SAT.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
Pfam; PF16073; SAT; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
2: Evidence at transcript level;
Complete proteome; Multifunctional enzyme; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1746 Non-reducing polyketide synthase ptaA.
/FTId=PRO_0000443038.
DOMAIN 1671 1745 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 4 227 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255}.
REGION 364 799 Ketosynthase (KS) domain. {ECO:0000255}.
REGION 898 1218 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255}.
REGION 1286 1605 Product template (PT) domain.
{ECO:0000255}.
ACT_SITE 534 534 {ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 1705 1705 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 1746 AA; 190191 MW; A975511650CD6C28 CRC64;
MSDNSGSGTS PWGSLNTPVG PPKVTLAYFS NEFPPDDLNF IVRKLFDRTS KGPFCSIDGV
LLCAIQFANL IGHYETTDHL FPFGSSIASV AGLGIGLVAA AAVSVTPSLA DLPVAGAEAV
RIAFRLGVLV DGVSQNLQPR DRSTTGTPDS WAYVIPDVSP EVVQKELDEI HSREKTPIPS
KIFVSALSRT SVTISGPPAR LRSLFRLSDF FRDRKFVALP VYGGLCHAGH IYEQRHVQEV
VEKSVLDETH VRYSPSVRLF STSTGKPFLS TSVTNLFEQV VGEILTQKIQ WDKVVKGVLE
RIQELSATEV EVLVFRDSLP VHELVKALKS ADSGLQTTTE DLLQWLHQSR ERLQGPRGSL
QSKIAIVGMS CRMPSGATDT EKFWELLEKG LDVHRKIPAD RFDVETHHDP TGKRVNTSIT
PYGCFIDEPG LFDAGFFNMS PREAQQTDPM QRLALVTAYE ALERAGYVAN RTSATNLHRI
GTFYGQASDD YREVNTAQEI STYFIPGGCR AFGPGRINYF FKFSGPSYSI DTACSSSLAT
IQAACTSLWN GDTDTVVAGG MNVLTNSDAF AGLGNGHFLS KTPNACKTWD CEADGYCRAD
GIGSIVMKRL EDAEADNDNI LGVILGAGTN HSADAISITH PHAPSQAFLY RQILRDAALD
PFDVSFVEMH GTGTQAGDSE EMQSVTEVFA PIANKRRTSK QPLHIGAVKS NVGHGEAVAG
VTALIKVLLM FQKEAIPPHA GIKNSINPGF PKDLDKRNIN IPYQKTAWPR STDRKRIAVV
NNFSAAGGNT TIAIEEGPLR QTIGHDPRTT HLIPISAKSK VSLKGNIQRL IDYLEVSPDV
SLADLSYSLT ARRYHHSHRV AITTSDVAHL KKQLRSQLDS ADSHKPIVAA AGPPPVAFAF
TGQGASYGTM DLELYHESKY FRDQILQLDS FAQGQGFPSF VPAIDGSFPK EHTHRPVVTQ
LALLCTEIAL AKYWASLGVK PDVVIGHSLG EYAALHVAGV LSASDAIFLV GQRALMLEKK
CQAGSHKMLA VRASLAQVQE AAGELPYEVA CINGQKDTVL SAAKDDIDKL ASVLESAGYK
CFSLDVAFAF HSAQTDPILD DFESVSRTGV LFQAPNLPVI SPLLGKVVFN DKTINANYVR
RATRESVDFL SALEAAQKIS IIDESTTWIE IGPHPVCMGF IRSAVPSIKV ASPSIRRGEN
NWQTLVQTLG ALHLAGIPVD WNEYHRPFEQ ALRLLDLPTY SWNDKTYWIQ YNGDWALTKG
NTFYDAEKAA KAPRVGGDLP PSPISTSTVH RVIGETFDGT AGTVDIQSDL MQQDFHDAAY
GHKMNNCGVV TSSIHADIVY TIGRYLHTKL KPGVKDIHMN ISNLEVVKGL VAQKNRDVPQ
LIQVSISTED ISSGTAQVTW FNVLPDGGLD EPFATATLFY GKANDWLQSW IPTTHLVLGR
VHELERLAEQ GVANRFSRNM AYGLFARNLV DYADKYRGMQ SVVLHGLEAF ADVELTKEKG
GTWTVPPFFI DSVAHLAGFI MNVSDAVDTA NNFCVTPGWE SMRFARPLLA GARYRSYVKM
IPTEEDAGVF LGDVYIFQDN KIIGQVRGIK FRRYPRLLLD RFFSAPDAAK HGGKHAPAVK
AAIPPALEKK SAVVVAQVPV VDKPPPTKEN AVAAPAAKSP EPVAAAAVNE DSITVKAMAL
VAAEAALDVS ELEDDVQFAN IGVDSLMSLV IAEKFRETLG VTISGSLFLE YPAVGDLRAW
LLEYYG


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