PKS5_LEPMJ
ID PKS5_LEPMJ Reviewed; 2569 AA.
AC E5A7D9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Highly reducing polyketide synthase pks5 {ECO:0000303|PubMed:31034868};
DE Short=HR-PKS pks5 {ECO:0000303|PubMed:31034868};
DE EC=2.3.1.- {ECO:0000305|PubMed:31034868};
DE AltName: Full=Abscisic acid biosynthesis cluster protein pks5 {ECO:0000303|PubMed:31034868};
GN Name=pks5 {ECO:0000303|PubMed:31034868}; ORFNames=LEMA_P087730.1;
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, INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31034868; DOI=10.1016/j.fgb.2019.04.015;
RA Darma R., Lutz A., Elliott C.E., Idnurm A.;
RT "Identification of a gene cluster for the synthesis of the plant hormone
RT abscisic acid in the plant pathogen Leptosphaeria maculans.";
RL Fungal Genet. Biol. 130:62-71(2019).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of abscisic acid (ABA), a phytohormone
CC that acts antagonistically toward salicylic acid (SA), jasmonic acid
CC (JA) and ethylene (ETH) signaling, to impede plant defense responses
CC (PubMed:31034868). The first step of the pathway catalyzes the reaction
CC from farnesyl diphosphate to alpha-ionylideneethane performed by the
CC alpha-ionylideneethane synthase abl3 via a three-step reaction
CC mechanism involving 2 neutral intermediates, beta-farnesene and
CC allofarnesene (By similarity). The cytochrome P450 monooxygenase abl1
CC might then be involved in the conversion of alpha-ionylideneethane to
CC alpha-ionylideneacetic acid (By similarity). Alpha-ionylideneacetic
CC acid is further converted to abscisic acid in 2 steps involving the
CC cytochrome P450 monooxygenase abl2 and the short-chain
CC dehydrogenase/reductase abl4, via the intermediates 1'-deoxy-ABA or
CC 1',4'-trans-diol-ABA, depending on the order of action of these 2
CC enzymes (By similarity). Abl2 is responsible for the hydroxylation of
CC carbon atom C-1' and abl4 might be involved in the oxidation of the C-
CC 4' carbon atom (By similarity). Pks5 is clearly not involved in the
CC production of ABA. Nonetheless, the possibility cannot be excluded that
CC pks5 may modify ABA into another compound. It also cannot be excluded
CC the possibility that pks5 also has a function completely independent of
CC ABA synthesis (PubMed:31034868). Pks5 is not required for pathogenicity
CC on B.napus cotyledon (PubMed:31034868). {ECO:0000250|UniProtKB:Q6H9H9,
CC ECO:0000269|PubMed:31034868}.
CC -!- INDUCTION: Expression is induced during the early biotrophic stage of
CC development (PubMed:31034868). Expression is positively regulated by
CC the ABA cluster-specific transcription regulator abl7
CC (PubMed:31034868). {ECO:0000269|PubMed:31034868}.
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:31034868}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of abscisic acid
CC (ABA) but leads to the accumulation of unidentified compounds
CC (PubMed:31034868). Does not affect sporulation, pycnidiospore
CC germination nor fungal growth rates in vitro, and does not alter the
CC pathogenicity of L.maculans (PubMed:31034868).
CC {ECO:0000269|PubMed:31034868}.
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DR EMBL; FP929136; CBX99534.1; -; Genomic_DNA.
DR RefSeq; XP_003843013.1; XM_003842965.1.
DR AlphaFoldDB; E5A7D9; -.
DR SMR; E5A7D9; -.
DR STRING; 985895.E5A7D9; -.
DR EnsemblFungi; CBX99534; CBX99534; LEMA_P087730.1.
DR GeneID; 13289265; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; E5A7D9; -.
DR OMA; GYVEAHM; -.
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:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic 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; IPR013149; ADH-like_C.
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; IPR032821; PKS_assoc.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 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.
PE 2: Evidence at transcript level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2569
FT /note="Highly reducing polyketide synthase pks5"
FT /id="PRO_0000448425"
FT DOMAIN 2485..2562
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..455
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 572..892
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 960..1268
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1457..1567
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255"
FT REGION 1855..2170
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 2195..2371
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2522
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2569 AA; 282196 MW; D3B06252505FB0A0 CRC64;
MVVKFANGVR NRGNGDEGQR GTQRPLSTPI AIVGMSCRFA GGATSPSNLW GLLSEGKDAW
SPVPTDRFDA SSLYHPDQQR TDRHHIQGGY FLDGDVTRFD APFFNLSAEA ASSMDPQLRL
SMEGVFEALE NAGIPLGKIA GTNTSVFSGT FGRDYTDRLV KDPETLPPSY FTGNGAAMYS
NRISHFFDLK GQSVTTDTGC SGSMAALHLA AQTIRTGESD MSIVAVAQFM MNPDLYIALS
NLGVLSPQGK CLPWDHRANG YGRGEGMAVV ILKRLDLALK DGDHIHSVIR ESAMNQDGKT
STITTPAKEA QQTLIRDCYS RAGLSLSETA YIEAHMTGTP TGDPIEAESL AKTFGAARAA
GDSVYVGSIK ANIGHTEPVS GLASIIKTAL VLQHQQIPPH LNYEKSNPAI PLQDWNLKLP
LSLIGWPEGA PLRASVNNFG YGGTNVHVIM EAAPVSTAKT LHTSEFNTIN EVESQQIGPT
EASPSYVYII SSRHSAGGLE MGESLALHIR DSIMRDQKPR AIDLAYTLAE RRTRFAWTTV
VKATSIEELA DKLEETLRKP IRATTIPRLG FIFNGQGAQW YAMGRELLAR YPVFQSAVRH
CDHILTQIYQ APWSLYEELS RDEASSRIHD AEISQPANVA IQLCLVDLLT SWNVMPTAVV
SHSSGEIAAA YAAGILSFKE ALGVAYYRGF LLAAHCTGDA LQGGMMAVRL SVDDVQGYIK
STSSGKVVIA CVNSPSSVTL SGDIDALTEL ASMLEDDAVP ARKLNVPLAY HSHHMNPIAK
SYQNRLDVLL DTGKVPKILV ASPVTGELVS HGETLDSKHW VKNLVSPVLF SEALESMVFG
SKNVDRHSSS GTQSMNVDIL IEVGAHSTLS GAVRETLGNA QLPYLSCLRR NIDAVSTMQD
VACDLLVRGY PVSLAGVNFL EGQELNFVHD LPTYAWDHST SYLVEPRASR QNRYRRFPSH
ELLGSSVPGA SSLTPTWRNF LRVQDLEWLA DHQLESKIVF PAAGYISMAI EAVRRLKLSS
GAREEPTSYR LRDIDFMTAL LISSGQSGTE VVFTLRDCSD KELDYRGWYE FELFSISPSD
AWIRHCTGYV SAEDSSKNLK ATRALSSDVE RVAVADRVRH VRPDAMFAGL RKTGIYHGPA
FQNLIGSKIT GSSSDTSFML SPKALAKDEE YVLHPTTLDS IFQTCYFSLP EEAQDRAMMV
PKSIGSLTVP RDFGRQNDNK LQSRVRLLHC TSRDAAFKGT VVQAKMSEEA DVPLLMHNLR
LQKIQAEDDN AGKLFRVHSQ GRWEPDILHD VPAKTKASMQ IVLSDSGLSD EKDFREAAYH
LMFECLAQLQ HEESKGWQPF HKRYHHWLQT IVKSVETGQL AHAAALEAHE WLDRSEAAKR
SILEKVAAMN AGGELLVKIG RHLTQIIRGD ITPLELMMEN GLLQRYYTEL PQFNNTYQQL
RKVLEHYAIK EPGAKILEVG AGTGGATLHA LQAFAAMDET NSSKTLLGHY DYTDVSADFF
PEAKKKFASW EGRMNFARLN IEIDPIQQGF TAGSYDLIIA SQVLHATVSL ANTLSNVRKL
LKPKGKLIFL EGTQHSIDLE LIFGTLPGWW LGEEPERQMS AIADVPTWDR FLKSSGFSGV
DMNIGNCEQP EVQVSSVLIA TAAAEPSYPS SISIIWGRNA PLAWRKELAT AIAAKTGTAP
RHETLKDVCP DETTLYLVAI ELEYDLVSSM NQVTFEKLRH LLVSSMGIFW VSGGGLIDSQ
KPLWGLTPGL LRTFRREDMN KRCVHLDFDV SKDLWNAETT NHIMHVFEEG FDYSLENSNM
DWEYAVKNSE LHVLRYYPDV ELDMRCSGIK PMPEHRLWYD DERDLQYQVP EGSGDLLNKI
EFLEVPRLVD DVPFGMVEIE TKAFGLNFQD LMLALGFVKD VLTLTHEGAG FVKRLGPGTE
RSGLRIGDRI CGAFRGSFAS TSMAWWTNIV KIPDEMSWEE AAAFSVAYLT VHVGLDHVAR
LQKEERILIH SAAGGVGQAA IMWAQHVGAE IFATCGTETK RQFLMDTYNI SADHIFSSRD
ACFASEIIDR TGEQGVDVVL NSLGGPLLKA SWGCLADFGR FVEIGKVDLH AAKRLDMTPF
GRNITMAGVD LVAYSELRGM VIHNALVALM KLYRSGHLRS LRPITRFNIS DMGAAMKHMQ
SGTHMGKIVL TIEPTAVVNV SPRITSLDLA NMNVTHLIVG GLRGVGHAIA LRMIEKGARN
VLAISRNASS HPNRLELQKT ADQHGCKLVI RDCDISSAEE LVEIVGSLGD LHMPPIGGVL
QAAMVLDDTV LERMSYEQWQ TAVRPKVAGT LNLHNNLPGL RYFIMLSSGT AITGNVSQAN
YAAGNTFQDT LARHRTLHGE PAISINLGPV DDVGYVAEQG EDVLKRVDKA VTSMSLSVNH
VMQLIEGGII DPLKKTGDKS QIITCFPRYE ALPDNQGVKD DKRFGTLRLG DEGVASTGGN
GLSASRVNEL TQELVSNGRS TGESAARKLV SELITEELSE LFSIDPNDID PGMPLTHHGV
DSLVAVRVRN WLISEVKARV AIFEILQSPS LTDFAALVAS RSSLITSCV
