PKS2_LEPMJ
ID PKS2_LEPMJ Reviewed; 2543 AA.
AC E5AE40;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Highly reducing polyketide synthase PKS2 {ECO:0000303|PubMed:23396262};
DE Short=HR-PKS PKS2 {ECO:0000305|PubMed:23396262};
DE EC=2.3.1.- {ECO:0000305|PubMed:23396262};
DE AltName: Full=Phomenoic acid biosynthesis cluster protein PKS2 {ECO:0000303|PubMed:23396262};
GN Name=PKS2 {ECO:0000303|PubMed:23396262}; ORFNames=LEMA_P002660;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
RN [2]
RP IDENTIFICATION, DOMAIN, DISRUPTION PHENOTYPE, FUNCTION, INDUCTION, AND
RP PATHWAY.
RX PubMed=23396262; DOI=10.1016/j.fgb.2013.01.008;
RA Elliott C.E., Callahan D.L., Schwenk D., Nett M., Hoffmeister D.,
RA Howlett B.J.;
RT "A gene cluster responsible for biosynthesis of phomenoic acid in the plant
RT pathogenic fungus, Leptosphaeria maculans.";
RL Fungal Genet. Biol. 53:50-58(2013).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of phomenoic acid, a long chain
CC aliphatic carboxylic acid that does not appear to be essential for
CC pathogenicity but may play a role in allowing to outcompete other fungi
CC in the environmental niche via its antifungal properties
CC (PubMed:23396262). The polyketide synthase produces the long methylated
CC aliphatic carboxylic acid chain of phomenoic acid (Probable). The
CC cluster-specific cytochrome P450 monooxygenase may then hydroxylate the
CC methyl group of carbon 31 (Probable). The putative dehydrogenase YogA,
CC which has no obvious role in phomenoic acid biosynthesis, may further
CC modify phomenoic acid to produce a compound not identified yet
CC (Probable). {ECO:0000269|PubMed:23396262, ECO:0000305|PubMed:23396262}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23396262}.
CC -!- INDUCTION: Expression is positively regulated by the phomenoic acid
CC biosynthesis cluster-specific transcription regulator C6TF.
CC {ECO:0000269|PubMed:23396262}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a methyltransferase
CC (CMeT) domain responsible for the incorporation of methyl groups; an
CC enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a
CC ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC an acyl-carrier protein (ACP) that serves as the tether of the growing
CC and completed polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:23396262}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of phomenoic acid.
CC {ECO:0000269|PubMed:23396262}.
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DR EMBL; FP929139; CBY01479.1; -; Genomic_DNA.
DR RefSeq; XP_003844958.1; XM_003844910.1.
DR AlphaFoldDB; E5AE40; -.
DR SMR; E5AE40; -.
DR STRING; 5022.CBY01479; -.
DR EnsemblFungi; CBY01479; CBY01479; LEMA_P002660.1.
DR GeneID; 13290520; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_1_1; -.
DR InParanoid; E5AE40; -.
DR OMA; LDEMPWI; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..2543
FT /note="Highly reducing polyketide synthase PKS2"
FT /id="PRO_0000446532"
FT DOMAIN 2463..2540
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 7..455
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23396262"
FT REGION 573..902
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23396262"
FT REGION 969..1283
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23396262"
FT REGION 1438..1631
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23396262"
FT REGION 1847..2159
FT /note="Enoylreductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23396262"
FT REGION 2184..2359
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23396262"
FT ACT_SITE 174
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 662
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1001
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2500
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2543 AA; 278542 MW; ACD7866DFC8FE036 CRC64;
MAQEPRIAVI GLSYRAPGVK GKSLWEYLSQ ARSAWTSVPA DRYDQSAYYQ AGGQKSGVVG
TKGAHFIDSP FGFDAAFFNM RADEAKHADP QHRLMLEVAL EAAEDAGKTF PDLAGKKIGV
FVGSGQHEYA QRLGDDEHAI QTFSGTGAAP CMAANRVSYF FDIDGPSVVA DAACASSVYA
ADMAVRALRN GECDGAFVGS ASLNLSPAGW LVLEKTGALS EHGRSYSYDT KASGFGRGEG
AACLLLKRYD DAIRDGDPVQ ALILSSACNH SGRSDGITMP NGLAQQKLLW SVHNAAGVDP
SDTPVVEGHG TGTAVGDPIE AGAFTAVLAR NRTANNPIYL GSLKSNFGHL EGASGVLAMV
KAIMMVNKGI VLPTAGFEKI NPKIEGHEKI KIAEMPLPWP KNEPRRCIVT NFGFGGSNSA
ILLEGPPPKA VSDDHALNGA AGTNGHALNG TNGTNGHALN GANGTNGHAI NGANGTNGHH
ENGNGVATQN QRLYVFSAKT QKSLTSYLST FDEYLDEAPE SSEFAKDLSY TLGQRRNHYP
YRVAAVADSI ETLQEKLSAL KPSRTKERGV LFVFTGQGAQ HAEMASGLES FEIFNKTLQE
AEMQLQTMGA PWSLIEELRK PSSESRVDDA EISQPACTAV QLALVALLKE WGVTPAAVTG
HSSGEIAAAY AAGLITFQQA IAASYFRGQA AAQLAAKQQP EEKGAMLALG VSFEEASKLI
EEHAEAYATV AAVNSPNSVT ISGDQSAIDN VHKAAEAKGL FARKLKVQMA YHSRHMEAVA
ASYLEDIKPY FQEDAPFLDK KSTTNPAFVS SVTGRVVDRI EASYWVKNLV QPVMFMDAVH
GLLAPQHLGT GKAAQALPRV VIEVGPHAAL KNPIKQTAEL VQVQQNWTPA SFTYLPTLFR
GTDATQAVLE LASSLFTLGA RVELAAVNQT DKHNAEVLTE LPAYAWDKTD YELRPRSTND
KYFPGENYHP LLGRKISPNA SGERTYRQVF TLDEMPWIRD HVVGGATIFP MTGYMSCAIE
AARRTLSTPA AAFLVTDFHV VRSLEIHEEE TVDMTTKLRP AAIGEGAFST KVWSFEMTTW
AEESGWTKHS WGQIEAEMTD MSMDTPTFRA SLPLVNKTTG LKEHDINAEY QTAGLRATLY
GPSFRNNVKF YEGKGYTILE HRLRDLGEAL RDPYARGSPV STDPPTLDGF LQGGGPLQYD
EHGRRPAQMP NYISRFRVSN KIPSDPSHRF DVVMRRLDYD VRGGRMHVGV AAFSRGPNDE
LTPIAEWESC AFRNIGSAEE VIDPSATVPD NWSWEVLPRY DFVPQDQLRK KLCDAVGELG
VEEDIRIRKG EEAACYYIEK ALKETADLDY SKLPPHLARF VRWGYKTVAE YDLDYSRGEP
TALLNEVRTS DAQGELICIM GEHIVDILRG KIEPLEIMLT DGRLTRHYEA DVTNAHLSKV
LGYLTEYLAD LEPNQRILEI GGGTAGTTLP VLEGLSRGRD ELAVLDYTFT DISTGFFEMA
RKKLSDWSRR ITYKRLDITQ DPSDQGFEQQ DYDVVIAANV LHATADMVKT MTHVRSLLKP
GGKLILLEAM RHPASVLPFS LLPGWWEAED KYRDHEEGPM MPATVWNQLL LDSGFSGVDV
VLPSRYGTDK PFVSILCSTR IGKQDNSRPI TICGPFLDEN EVEFAQSVAD LISKELGYPT
EMKPYAEIDP EDDPYYVFID SPHESALQDM DQEKFKSLQT LLLHNTGLLW VTPEGASPDA
KIIQGMVRTL RMEVDLKNLI LFEDVPCTSQ GAAGIMKLAT KLRDSELSRD QDFDFAWQDG
AIHLPRMRQL KEVKEQFAVE EGVAYRKMQN LWDNNDRGLE MTIDAAGSPD TIYFQRTDVS
NIGEDEVVVR VEAAGVGHRD LEVILGSIPW APPSYEGAGK IIRTGSRISH LREGDDVFFL
TPDSSALATE VKLPSWLVGK IPQGITIHDA ATLPLAYSLA VLALIQTARL RKNETVLIHA
AAGAVGQACV ALAQNVGAHV YVTAGNEAKR EFLHEKFGIP KDRIFSSRTP EFRDQILSAT
ANKGIDVIVN SLGGELMTET WALTAPFGRF IEIGKKDAFQ NNNLPMKPFN RNVTYTGIDL
RDLYQFRRDD IKDVFTEVVT LLQRGNIQPI GPVTTTPISQ FASALRKLKS GEHMGKMVIT
LGKDDTVVAE TALRPLNVTL KPDATYLVAG GTRGIGLDLA YWMIDHGARY IVLLGRSGAS
GPEAQKILNR YKDTDVCVKI FSCNVGHRDE LAEVVEAIKD LPPVRGVVHS ALLLSDKLFV
NSTLEDWEII TTPRVKGAWN LHELMPDNLD FFVALSSFNG DTGNLGQAIY AGTAGFYNAF
SQYRNSRGQY TVSIALPVVL DVGYVADNNL SEILKESLGV AITMADIRAI FGGILLGPSS
PFVYNGRAQT FMVYIDGQPV QNGGWKYFHP VHTKVRLMSD RRRVKIASGG VDQHSASWTT
AEDPLIGLTE AMITKVSAMT MIEREEVLPD APLTSYNLDS LVSVELRNWI RRETAVELTL
SAIMQADSLR ALATEILSQR KAE
