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Protein

Non-reducing polyketide synthase ptaA

Gene

ptaA

Organism
Pestalotiopsis fici (strain W106-1 / CGMCC3.15140)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

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.1 Publication

Pathwayi: Secondary metabolite biosynthesis

This protein is involved in Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei534PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMultifunctional enzyme, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Non-reducing polyketide synthase ptaA1 Publication (EC:2.3.1.-1 Publication)
Alternative name(s):
Pestheic acid biosynthesis cluster protein A1 Publication
Gene namesi
Name:ptaA1 Publication
ORF Names:PFICI_10824
OrganismiPestalotiopsis fici (strain W106-1 / CGMCC3.15140)
Taxonomic identifieri1229662 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesXylariomycetidaeXylarialesSporocadaceaePestalotiopsis
Proteomesi
  • UP000030651 Componenti: Unassembled WGS sequence

Pathology & Biotechi

Disruption phenotypei

Totally abolishes the production of pestheic acid but does not affect the production iso-A82775C, another precursor of chloropupukeananes (PubMed:24302702).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004430381 – 1746Non-reducing polyketide synthase ptaAAdd BLAST1746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1705O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Expressioni

Inductioni

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).2 Publications

Structurei

3D structure databases

SMRiA0A067XNI2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1671 – 1745CarrierPROSITE-ProRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 227N-terminal acylcarrier protein transacylase domain (SAT)Sequence analysisAdd BLAST224
Regioni364 – 799Ketosynthase (KS) domainSequence analysisAdd BLAST436
Regioni898 – 1218Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST321
Regioni1286 – 1605Product template (PT) domainSequence analysisAdd BLAST320

Domaini

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).By similarity

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
InterProiView protein in InterPro
IPR001227 Ac_transferase_dom_sf
IPR036736 ACP-like_sf
IPR014043 Acyl_transferase
IPR016035 Acyl_Trfase/lysoPLipase
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR030918 PT_fungal_PKS
IPR032088 SAT
IPR016039 Thiolase-like
PfamiView protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit
PF00550 PP-binding, 1 hit
PF14765 PS-DH, 1 hit
PF16073 SAT, 1 hit
SMARTiView protein in SMART
SM00827 PKS_AT, 1 hit
SM00825 PKS_KS, 1 hit
SM00823 PKS_PP, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF52151 SSF52151, 2 hits
SSF53901 SSF53901, 1 hit
SSF55048 SSF55048, 1 hit
TIGRFAMsiTIGR04532 PT_fungal_PKS, 1 hit
PROSITEiView protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 1 hit
PS50075 CARRIER, 1 hit

Sequencei

Sequence statusi: Complete.

A0A067XNI2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNSGSGTS PWGSLNTPVG PPKVTLAYFS NEFPPDDLNF IVRKLFDRTS
60 70 80 90 100
KGPFCSIDGV LLCAIQFANL IGHYETTDHL FPFGSSIASV AGLGIGLVAA
110 120 130 140 150
AAVSVTPSLA DLPVAGAEAV RIAFRLGVLV DGVSQNLQPR DRSTTGTPDS
160 170 180 190 200
WAYVIPDVSP EVVQKELDEI HSREKTPIPS KIFVSALSRT SVTISGPPAR
210 220 230 240 250
LRSLFRLSDF FRDRKFVALP VYGGLCHAGH IYEQRHVQEV VEKSVLDETH
260 270 280 290 300
VRYSPSVRLF STSTGKPFLS TSVTNLFEQV VGEILTQKIQ WDKVVKGVLE
310 320 330 340 350
RIQELSATEV EVLVFRDSLP VHELVKALKS ADSGLQTTTE DLLQWLHQSR
360 370 380 390 400
ERLQGPRGSL QSKIAIVGMS CRMPSGATDT EKFWELLEKG LDVHRKIPAD
410 420 430 440 450
RFDVETHHDP TGKRVNTSIT PYGCFIDEPG LFDAGFFNMS PREAQQTDPM
460 470 480 490 500
QRLALVTAYE ALERAGYVAN RTSATNLHRI GTFYGQASDD YREVNTAQEI
510 520 530 540 550
STYFIPGGCR AFGPGRINYF FKFSGPSYSI DTACSSSLAT IQAACTSLWN
560 570 580 590 600
GDTDTVVAGG MNVLTNSDAF AGLGNGHFLS KTPNACKTWD CEADGYCRAD
610 620 630 640 650
GIGSIVMKRL EDAEADNDNI LGVILGAGTN HSADAISITH PHAPSQAFLY
660 670 680 690 700
RQILRDAALD PFDVSFVEMH GTGTQAGDSE EMQSVTEVFA PIANKRRTSK
710 720 730 740 750
QPLHIGAVKS NVGHGEAVAG VTALIKVLLM FQKEAIPPHA GIKNSINPGF
760 770 780 790 800
PKDLDKRNIN IPYQKTAWPR STDRKRIAVV NNFSAAGGNT TIAIEEGPLR
810 820 830 840 850
QTIGHDPRTT HLIPISAKSK VSLKGNIQRL IDYLEVSPDV SLADLSYSLT
860 870 880 890 900
ARRYHHSHRV AITTSDVAHL KKQLRSQLDS ADSHKPIVAA AGPPPVAFAF
910 920 930 940 950
TGQGASYGTM DLELYHESKY FRDQILQLDS FAQGQGFPSF VPAIDGSFPK
960 970 980 990 1000
EHTHRPVVTQ LALLCTEIAL AKYWASLGVK PDVVIGHSLG EYAALHVAGV
1010 1020 1030 1040 1050
LSASDAIFLV GQRALMLEKK CQAGSHKMLA VRASLAQVQE AAGELPYEVA
1060 1070 1080 1090 1100
CINGQKDTVL SAAKDDIDKL ASVLESAGYK CFSLDVAFAF HSAQTDPILD
1110 1120 1130 1140 1150
DFESVSRTGV LFQAPNLPVI SPLLGKVVFN DKTINANYVR RATRESVDFL
1160 1170 1180 1190 1200
SALEAAQKIS IIDESTTWIE IGPHPVCMGF IRSAVPSIKV ASPSIRRGEN
1210 1220 1230 1240 1250
NWQTLVQTLG ALHLAGIPVD WNEYHRPFEQ ALRLLDLPTY SWNDKTYWIQ
1260 1270 1280 1290 1300
YNGDWALTKG NTFYDAEKAA KAPRVGGDLP PSPISTSTVH RVIGETFDGT
1310 1320 1330 1340 1350
AGTVDIQSDL MQQDFHDAAY GHKMNNCGVV TSSIHADIVY TIGRYLHTKL
1360 1370 1380 1390 1400
KPGVKDIHMN ISNLEVVKGL VAQKNRDVPQ LIQVSISTED ISSGTAQVTW
1410 1420 1430 1440 1450
FNVLPDGGLD EPFATATLFY GKANDWLQSW IPTTHLVLGR VHELERLAEQ
1460 1470 1480 1490 1500
GVANRFSRNM AYGLFARNLV DYADKYRGMQ SVVLHGLEAF ADVELTKEKG
1510 1520 1530 1540 1550
GTWTVPPFFI DSVAHLAGFI MNVSDAVDTA NNFCVTPGWE SMRFARPLLA
1560 1570 1580 1590 1600
GARYRSYVKM IPTEEDAGVF LGDVYIFQDN KIIGQVRGIK FRRYPRLLLD
1610 1620 1630 1640 1650
RFFSAPDAAK HGGKHAPAVK AAIPPALEKK SAVVVAQVPV VDKPPPTKEN
1660 1670 1680 1690 1700
AVAAPAAKSP EPVAAAAVNE DSITVKAMAL VAAEAALDVS ELEDDVQFAN
1710 1720 1730 1740
IGVDSLMSLV IAEKFRETLG VTISGSLFLE YPAVGDLRAW LLEYYG
Length:1,746
Mass (Da):190,191
Last modified:October 1, 2014 - v1
Checksum:iA975511650CD6C28
GO

Sequence cautioni

The sequence ETS76950 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KC145148 Genomic DNA Translation: AGO59040.1
KI912116 Genomic DNA Translation: ETS76950.1 Sequence problems.
RefSeqiXP_007837596.1, XM_007839405.1

Genome annotation databases

EnsemblFungiiETS76950; ETS76950; PFICI_10824
GeneIDi19275837
KEGGipfy:PFICI_10824

Similar proteinsi

Entry informationi

Entry nameiPTAA_PESFW
AccessioniPrimary (citable) accession number: A0A067XNI2
Secondary accession number(s): W3WSW2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 31, 2018
Last sequence update: October 1, 2014
Last modified: February 28, 2018
This is version 24 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

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