PKS1_ELSFA
ID PKS1_ELSFA Reviewed; 2192 AA.
AC A7UMW1;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Non-reducing polyketide synthase 1 {ECO:0000303|PubMed:18321192};
DE EC=2.3.1.- {ECO:0000305|PubMed:18321192};
DE AltName: Full=Elsinochromes biosynthesis cluster protein PKS1 {ECO:0000303|PubMed:18321192};
GN Name=PKS1 {ECO:0000303|PubMed:18321192};
OS Elsinoe fawcettii (Citrus scab fungus) (Sphaceloma fawcettii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40997;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18957608; DOI=10.1099/mic.0.2008/019414-0;
RA Chung K.R., Liao H.L.;
RT "Determination of a transcriptional regulator-like gene involved in
RT biosynthesis of elsinochrome phytotoxin by the citrus scab fungus, Elsinoe
RT fawcettii.";
RL Microbiology 154:3556-3566(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18321192; DOI=10.1094/mpmi-21-4-0469;
RA Liao H.L., Chung K.R.;
RT "Genetic dissection defines the roles of elsinochrome phytotoxin for fungal
RT pathogenesis and conidiation of the citrus pathogen Elsinoe fawcettii.";
RL Mol. Plant Microbe Interact. 21:469-479(2008).
RN [3]
RP INDUCTION.
RX PubMed=20965063; DOI=10.1016/j.mycres.2009.10.007;
RA Yang S.L., Chung K.R.;
RT "Transcriptional regulation of elsinochrome phytotoxin biosynthesis by an
RT EfSTE12 activator in the citrus scab pathogen Elsinoe fawcettii.";
RL Fungal Biol. 114:64-73(2010).
RN [4]
RP REVIEW.
RX PubMed=21199563; DOI=10.1111/j.1364-3703.2010.00663.x;
RA Chung K.R.;
RT "Elsinoe fawcettii and Elsinoe australis: the fungal pathogens causing
RT citrus scab.";
RL Mol. Plant Pathol. 12:123-135(2011).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of elsinochromes, pigments consisting of
CC at least four interconvertible tautomers (A, B, C and D) that have a
CC core phenolic quinone to which various side chains are attached and
CC which play an important role in fungal pathogenesis (PubMed:18957608,
CC PubMed:18321192). The non-reducing polyketide synthase PKS1 was
CC proposed to iteratively catalyze decarboxylation between acetyl-CoA and
CC malonyl-CoA subunits for polyketide chain elongation. The released
CC polyketide undergoes cyclization to form an aromatic ring, and proceeds
CC via serial modification steps to produce the heptaketide back- bone of
CC elsinochrome. As elsinochrome has a symmetrical structure, two
CC identical heptaketides are fused to form a core 1,2-dihydrobenzo-
CC perylene ring structure, which can then be successively modified to
CC produce the various derivatives of elsinochrome. Some of these
CC reactions may be cooperatively carried out, at least in part, by the
CC products of RDT1, OXR1 and PKS1. PRF1, embedded within the elsinochrome
CC cluster possibly functions to stabilize some of the biosynthetic
CC enzymes required for elsinochrome production. As prefoldin is a hexamer
CC containing 2 a and 4 b subunits, additional prefoldin subunits, whose
CC coding genes may not immediately link to the elsinochrome biosynthetic
CC gene cluster, are required to fulfill the chaperone function. In
CC addition, no methyltransferase-coding gene exists within the
CC biosynthetic gene cluster, even though elsinochrome has four methyl
CC groups at positions C3, C7, C8 and C12. Apparently, the identified gene
CC cluster does not contain the entire entourage of genes responsible for
CC elsinochrome biosynthesis. Once elsinochrome is synthesized, it must be
CC exported outside the fungal cells, which is probably accomplished by
CC the ECT1 transporter, to avoid toxicity (PubMed:21199563).
CC {ECO:0000269|PubMed:18321192, ECO:0000269|PubMed:18957608,
CC ECO:0000303|PubMed:21199563}.
CC -!- INDUCTION: The promoter contains 4 ambient pH-regulated pacC-binding
CC consensus motifs (GCCARG) and multiple cAMP-inducible C/EBP-binding
CC motifs (CCAAT or CAAT). In addition, the promoter contains 3 MRAGGGR
CC and 2 CATTCY consensus motifs that have been shown to serve as binding
CC sites for the conidial formation-related brlA and abaA transcriptional
CC activators (PubMed:18321192). Expression is up-regulated on exposure to
CC light, in the presence of large amounts of glucose, during nitrogen
CC starvation or at alkaline pH, all conditions highly conducive to
CC elsinochrome accumulation (PubMed:18957608, PubMed:18321192,
CC PubMed:20965063). Expression is positively regulated by the cluster-
CC specific transcription factor TSF1 (PubMed:18957608). Expression is
CC also positively regulated by the STE12 transcription factor in a TSF1-
CC independent manner (PubMed:20965063). {ECO:0000269|PubMed:18321192,
CC ECO:0000269|PubMed:18957608, ECO:0000269|PubMed:20965063}.
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. {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DOMAIN: The release of the polyketide chain from the non-reducing
CC polyketide synthase is mediated by the thioesterase (TE) domain
CC localized at the C-ter of the protein. {ECO:0000250|UniProtKB:Q5ATJ7}.
CC -!- DISRUPTION PHENOTYPE: Blocks the expression of the elsinochrome cluster
CC genes RDT1, TSF1, PRF1 and ECT1 (PubMed:18957608). Abrogates
CC elsinochrome production, drastically reduces conidiation, and
CC significantly decreases lesion formation on rough lemon leaves
CC (PubMed:18321192). {ECO:0000269|PubMed:18321192,
CC ECO:0000269|PubMed:18957608}.
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DR EMBL; EU086466; ABU63483.1; -; Genomic_DNA.
DR AlphaFoldDB; A7UMW1; -.
DR SMR; A7UMW1; -.
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; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
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; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 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; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat;
KW Transferase; Virulence.
FT CHAIN 1..2192
FT /note="Non-reducing polyketide synthase 1"
FT /id="PRO_0000445818"
FT DOMAIN 1670..1747
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1798..1875
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 5..243
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 377..809
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 905..1218
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1293..1610
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1639..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..2164
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1764..1788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 546
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 993
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1707
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1835
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2192 AA; 238122 MW; D03C4182A088CC71 CRC64;
MSNVLLLGDQ TADQSPLLRK LVLRRNDALV TTFHEQVSVA LRDEVSKLPA RQRQDIPSFL
KLNTLVDLYY QGDKRLPILE STFVALTQLG HYIGYFSENP DRLPYAANTR VLGLCTGSLA
ATVIVSAKSL SELVSLAVEA VRIAFRAGAC VDAAKRVLQQ PGEEKEPWST IVMNLSEKDA
QKALDEFHSS TGTSGPSRAY ISAISTMAVT ISGPPSTTQK LFSESADLST KNRVSIPIYA
PYHAAHLHSE RDLQRIIPDS SRALLKKYQP HTLLHSSATG ECLVADNTCD LMSLALVDFL
REPVRWDRLL EESISQIIAT PKAPAKIFTI GVSNVANSMA AALKASGQAT VSITDHTSWI
VPDDYNSTRG RTQNDKIAIV GMSGRFPSAA SVDALWELLE KGLDVHRKIP ADRFDADAHC
DPSGKSKNKS HTPYGCFIDE PGLFDPRFFN MSPREAAQTD PMGRLALVTA YEALEESGYV
PNRTPSTKLH RIGTFYGQTS DDWREINAAE NVDTYFITGG VRAFAPGRIN YYFKFSGPSF
SIDTACSSSL AAIQLACTSL WAGDCDTACA GGLNVLTNPD IFSGLSKGQF LSKTGSCKTY
DNDADGYCRG DGCGSVILKR YEDAIADKDN ILGCILGAAT NHSAEAVSIT HPHAGNQEFL
FKKVLAEAGV DAHEISYVEM HGTGTQAGDG IEMTSVTNAF APPNRRRTPD EKLFLGAIKA
NVGHGEAASG INSLAKVLMM FKKNAIPANV GIKGVMNESF PKDLGERNVH IPLKQVEFPR
NGDAPRKIFL NNFSAAGGNT SLLLEDGPVR KPSTVKDPRS TLPITVTARS IASLKRNIDN
LKSYLSKTPE ASLTSLSYTS TARRIQHNYR IAFPATDINK VSEALDAQIK DSYSPVAITA
TRVAFCFTGQ GSQYTGLGQK LYQDLPSFKA DIDQLNQLAE SHNLPSFLEL FDGTDVATLS
PVKVQLGTAC IQVALSRMWE SWGIKPSAVI GHSLGEYAAL HVAGVISASD MVYLVGRRAE
LLVKDCTPHT HGMLAVKASV DAIRNALGSK MTEVACINGP EETVLCGSSE IVTAANEVLT
SKGMKSTKLN VPFAFHSAQV DPILESFRTT ASSVSFKKPA VPVLSPLSGD IITDVGVIGP
EYLAKHARET VNFSQALESG QKAKIFDGKT AWLEIGAHPV CLGMVKGSVE TTATAPSLRR
GEDAWKTLAN SMCALFLAGV YINFDEYHRA FNDAQELLHL PTYSFDDKKY WLDYHNNWTL
TKGEAPQPTK AIEAAPFEAA APVERTYKKL SDSCQKIIDE EFSANAGRVL VQSDVCQPNL
RRVAMGHQVN DTALCPSSLY FDMAMTVADY IYKALRPSAP KIGYNVAHME VPKPFIIKNV
APPEGQHLQL EAHADLEEGV AKLVFRSVTP NGKQLVVHAH CTVKFEDINT WQEGWENISF
MVKSQIENLQ RKTRTQEAHV IGRGLAYKLF KVFVNYAKPY RGMEEIILDN QTTEATASVH
FQTKPEDGEF FFPAYWCDSM AHLGGFIVNA TDLCDSDNYV SVSHGWGSIK VAKEMSANKK
YRNYVRMVEK PGNVTQGDVY IFDGDEIIAV VGALKFQKIP RKVLNTFLPP QKAGSAVSAP
VAPPAAARPA LKQAPRINTQ AQPAKAVPKQ VTVAAPTPKA APKKADLKKP AGPTIITRVM
HIIAAETDVD SSELVDQAAF ENLGVDSLMS LTISARFREE LDMDISSTLF TDFPTVGEMK
KFFSQYDGEV GTPEQDDSDS DSETSGDAST PMSEVGTPMT IPSSAVSESG KFDLDTAAPA
SGEVSIARQI VATEMGVEIA EVTDQADLAD MGMDSLMSLT ILSELREKTG IDLPSTFLMT
NPTIEDVENA LDMRPKARVA PVAVPAPSNR RPSSPQLDKV NEKLNASRSA DISKYPAATS
VLLQGNPKIA TKKIFFLPDG SGSATSYVSI PNIGSDVCAF GLNCPFMKSP EQWSCGIEIC
AMVYLKEIKR RKPTGPYIIG GWSAGGVIAY AVAQALLANN EEVEKLLLLD SPCPVNLDPL
PARLHIFFNE IGLLGTGDPS KTPKWLLPHF SAAIRSLSDY QPQPTIKPVK TYAIWCREGV
AGNPGDPRPP PAEDEDPAPM KWLLNHRTDF TDNGWGKLCG VENMKYGVMG GHHFSMMKPP
HVSIFDYSIV DDEANMRQAE DLGQLIKEGL SM
