PTAA_PESFW
ID PTAA_PESFW Reviewed; 1746 AA.
AC A0A067XNI2; W3WSW2;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Non-reducing polyketide synthase ptaA {ECO:0000303|PubMed:24302702};
DE EC=2.3.1.- {ECO:0000305|PubMed:24302702};
DE AltName: Full=Pestheic acid biosynthesis cluster protein A {ECO:0000303|PubMed:24302702};
GN Name=ptaA {ECO:0000303|PubMed:24302702}; ORFNames=PFICI_10824;
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: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of pestheic acid, a diphenyl ether which
CC is a biosynthetic precursor of the unique chloropupukeananes
CC (PubMed:24302702). The biosynthesis initiates from condensation of
CC acetate and malonate units catalyzed by the non-reducing PKS ptaA
CC (PubMed:24302702). As the ptaA protein is TE/CLC domain-deficient,
CC hydrolysis and Claisen cyclization of the polyketide could be catalyzed
CC by ptaB containing a beta-lactamase domain (PubMed:24302702). The ptaB
CC protein might hydrolyze the thioester bond between the ACP of ptaA and
CC the intermediate to release atrochrysone carboxylic acid, which is
CC spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702).
CC Endocrocin anthrone is then converted to endocrocin, catalyzed by the
CC anthrone oxygenase ptaC (PubMed:24302702). Spontaneous decarboxylation
CC of endocrocin occurs to generate emodin (PubMed:24302702). An O-
CC methyltransferase (ptaH or ptaI) could methylate emodin to form
CC physcion (PubMed:24302702). PtaJ could then catalyze the oxidative
CC cleavage of physcion, and rotation of the intermediate could then
CC afford desmethylisosulochrin (PubMed:24302702). PtaF, a putative NADH-
CC dependent oxidoreductase, might also participate in the oxidative
CC cleavage step (PubMed:24302702). Desmethylisosulochrin is then
CC transformed by another O-methyltransferase (ptaH or ptaI) to form
CC isosulochrin (PubMed:24302702). Chlorination of isosulochrin by ptaM in
CC the 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 -!- CATALYTIC ACTIVITY:
CC Reaction=8 H(+) + holo-[ACP] + 8 malonyl-CoA = atrochrysone carboxyl-
CC [ACP] + 8 CO2 + 8 CoA + 2 H2O; Xref=Rhea:RHEA:64232, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:149712;
CC Evidence={ECO:0000305|PubMed:24302702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64233;
CC Evidence={ECO:0000305|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 -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DISRUPTION PHENOTYPE: Totally abolishes the production of pestheic acid
CC but does not affect the production iso-A82775C, another precursor of
CC chloropupukeananes (PubMed:24302702). {ECO:0000269|PubMed:24302702}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ETS76950.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KC145148; AGO59040.1; -; Genomic_DNA.
DR EMBL; KI912116; ETS76950.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_007837596.1; XM_007839405.1.
DR AlphaFoldDB; A0A067XNI2; -.
DR SMR; A0A067XNI2; -.
DR STRING; 1229662.A0A067XNI2; -.
DR EnsemblFungi; ETS76950; ETS76950; PFICI_10824.
DR GeneID; 19275837; -.
DR KEGG; pfy:PFICI_10824; -.
DR eggNOG; KOG1202; Eukaryota.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..1746
FT /note="Non-reducing polyketide synthase ptaA"
FT /id="PRO_0000443038"
FT DOMAIN 1671..1745
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 4..227
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 364..799
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 898..1218
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1286..1605
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1705
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ 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
