PKS19_MAGO7
ID PKS19_MAGO7 Reviewed; 2571 AA.
AC G4N296;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Highly reducing polyketide synthase 19 {ECO:0000303|PubMed:27902426};
DE EC=2.3.1.- {ECO:0000269|PubMed:27902426};
DE AltName: Full=Pyriculol/pyriculariol biosynthesis cluster protein PKS19 {ECO:0000303|PubMed:27902426};
GN Name=PKS19 {ECO:0000303|PubMed:27902426}; ORFNames=MGG_10912;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP IDENTIFICATION, INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, AND PATHWAY.
RX PubMed=27902426; DOI=10.1099/mic.0.000396;
RA Jacob S., Groetsch T., Foster A.J., Schueffler A., Rieger P.H.,
RA Sandjo L.P., Liermann J.C., Opatz T., Thines E.;
RT "Unravelling the biosynthesis of pyriculol in the rice blast fungus
RT Magnaporthe oryzae.";
RL Microbiology 163:541-553(2017).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of pyriculol and pyriculariol, two
CC heptaketides that induce lesion formation upon application on rice
CC leaves but are dispensable for pathogenicity (PubMed:27902426). The
CC highly reducing polyketide synthase synthesizes the heptaketide
CC backbone of pyriculol and pyriculariol (PubMed:27902426). Pyriculol and
CC pyriculariol contain several hydroxyl moieties and double bonds, so it
CC can be assumed that several reduction steps occur during biosynthesis.
CC These reactions could be executed by PKS19 itself or partly by the
CC tailoring enzymes OXR1, PXR2, RED1, RED2 or RED3, identified within the
CC cluster (Probable). The FAD-linked oxidoreductase OXR1 is the only
CC tailoring enzyme for which the function has been determined yet, and is
CC involved in the oxidation of dihydropyriculol and dihydropyriculariol
CC into pyriculol and pyriculariol, respectively (PubMed:27902426).
CC {ECO:0000269|PubMed:27902426, ECO:0000305|PubMed:27902426}.
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:27902426}.
CC -!- INDUCTION: Expression is increased by fivefold in rice-extract medium
CC (REM) and is correlated with the production of pyriculol
CC (PubMed:27902426). Expression is also increased during invasive growth
CC during rice infection (PubMed:27902426). Expression is negatively
CC regulated by the 2 cluster-specific transcription factors TRF1 and TRF2
CC (PubMed:27902426). {ECO:0000269|PubMed:27902426}.
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; an enoylreductase (ER)
CC domain that reduces enoyl groups to alkyl group; a ketoreductase (KR)
CC domain that catalyzes beta-ketoreduction steps; and an acyl-carrier
CC protein (ACP) that serves as the tether of the growing and completed
CC polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:27902426}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of pyriculol,
CC pyriculariol, as well as of their dihydro derivatives dihydropyriculol
CC and dihydropyriculariol. {ECO:0000269|PubMed:27902426}.
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DR EMBL; CM001233; EHA52508.1; -; Genomic_DNA.
DR RefSeq; XP_003712315.1; XM_003712267.1.
DR AlphaFoldDB; G4N296; -.
DR SMR; G4N296; -.
DR STRING; 318829.MGG_10912T0; -.
DR EnsemblFungi; MGG_10912T0; MGG_10912T0; MGG_10912.
DR GeneID; 5048915; -.
DR KEGG; mgr:MGG_10912; -.
DR VEuPathDB; FungiDB:MGG_10912; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_1_1; -.
DR InParanoid; G4N296; -.
DR OMA; KDVQHYT; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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 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; IPR011032; GroES-like_sf.
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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 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; 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 SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2571
FT /note="Highly reducing polyketide synthase 19"
FT /id="PRO_0000446267"
FT DOMAIN 2490..2568
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..488
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 609..932
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1019..1340
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1800..2140
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 2177..2355
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 21..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 701
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1051
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2527
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2571 AA; 271956 MW; 7003ADD0491E34DA CRC64;
MSPIFLGDSE DAATCRCGPP SSPSPELSGT ETALTSDSDG PELLNPGPQG PEPIAIIGMG
CRLPGGASTP SKLWELLEAG RSAQGRLPAD RYNMDAFYHP NGDRPGSMNT SGGYFIQEDV
RGFDNSMFGI NHLEAMYMDP QQRKLLEVTF EAFEAAGLSL DAVSGANVGC YVGNFVTDFI
TMQLKDAEYT HRYTATGSGT TILANRISHV FNLKGPSFVI DTACSSSLYS LHAACSALWQ
RECDAAVVAG ANLIQSPEQQ LATMKAGVLS GTSTCHTFDA SADGYGRADG IGVLLVKRLS
DAIRDNDPIR SVIRSTAVNS NGKTNGITLP SADGQEAVIR KAYALAGLGY GDTDYVECHG
TGTAVGDPIE VEALSRVFRR QPGSQPLLIG SVKTNLGHSE AASGISSLLK VAMALECGRI
PPTIGISSLN PKLKLDEWNM RIVTENTEWP QNRTPNGQQG GRALRRAGVN SFGYGGANAH
CILESPDSHV PRGYRERGAA TRLTNTTTGA PRTALLLPVS SKSASSLEQK SADIASYVAA
KTASSADLQA SELAYTLGVR RSHLSSRGFW IAAPDSLSED VVVGSDAASS KLHTRIPGRA
YGRHPLAFVF TGQGAQWAGM GRELMDEFPS FRRTVQMLDS TLQLLPHPPT WTLRGALLEP
PESSSINLAS RSQPVCTAVQ LALVRLLRDW GVAPGFAVGH SSGEIAAAYA AGRLTARQAI
AVAYYRGYAV ERSTTVGAMM AAGLSQDEAD GDIAALGLAG KIRVACVNSP ESVTISGDTD
GIDEYKAVLD GRGVFARLLK TDGRAYHSHH MAAIGGLYED LVVEALASPA VQNDLDDAGQ
QNSSPAQWIS SVTGQVVGDD MPTAEPSYWR ANLESPVLFA QVVEKLLSPG TPVHLVEIGP
HSALEMPIKQ TRTKVGIDAA KTPYNSALLR GKNSTTTMLT LAGELFLHGH PIAFGAVNNT
TTAHTHSRYP PTKPGMLLSA RQPQVLTDLP RHVWEYDGGA GFHEPRSSIE WRNRTHARHD
LLGSRVPGGD GITRQWRNVL RAADLAWLVG HKLDTTTVLP AAGYLAMAVE AACQSTGLSL
ERYGRGSPRC SFALRHVHVE KALMVPDDQQ SGIEVFTTLQ PTTAPRTATA GSGGWYKFIV
SSFVAGESTR HAHGLVKLTQ NEDRPPARRL PVEDEAMEQS APRTWYRRFV QEGLNFSGPL
QSLSRIETHR RRGEMHLLAQ TSLSPGLGGE SAYALHPIAI DALFQSGPIA CTRGVVRDFT
AKVPVYIKDM ELRMPSRSLL SGSFVSPSGD ESAEATAQQG SIRTICKSAG LGAISVDSQL
FDGDDLVLCV SGCRMVPYSS GTAVGAAAGD GYERHPMLHV AWKPDVERLA DAGIEHGASA
LTAYLSQFQG TTVIGDDADG VAGVLGAAKL AGGVLDLVVH KRPTLHVLLA SDSTQDDGAA
KHMRELLGVG TAFQRCLSLW KRSTDEDGAV HFQDLSAKED TTANGTATAA SSAPPSIFDV
LVILDLDTST KGSTSADLAS YSSLVDEKKG TLIWSGPPSS ASTASSGSIP AKLSPLGFSC
MEAQQSHGTP VLEVVLAQRG LPDKKQELGQ QEVLIVERNP DHKLNSELAL HVAELTNKPA
KRVTLDQLTP DLATAHATVI ATVELEDALL ADVKDGDFAQ IKTLTDHCTN LIWVTGGGLA
DGTRPEQAVV FGLSRALMME QPSLRFFVVG VDGECVAAET TARQVLGVAR QALLDDAEPD
FEFVQDGRAG GALQVSRFVP DDAMNSTFRQ RQPNATETLE MRLGDAHPCR LSLAGPVAAN
MSDAFVFTRD LTHKNNDHGI GQDEVEVQVL TVGLHARDLR AMTGETSDGD GDTQPHAVTS
QYVGRVVRVG SAVEGLGVDD SVLVMAPGRC ATVERIPASS CSVLRDGEDP AAMASIPLPA
CTALYALRDR ARLQPGETVL VCYREADAHG RDRSGPAAVH IARALGANVF AVVVVDDGDD
EAKQEQRSEI VGDLGLPETH VSFVKVGDGA GFGSDMLSSH GRVQVVANFC TDRWPLSNVA
ALCADDARIV HVGRGTVLGE LVTTDPTILR KNIALSTFDV NLLLTPVPSS PSTTRSGLLL
DDVLSLWRQG KLNGLLGTQP RLFDVANLAE AFRALSGSTT KAGHTTPRGA VSVSFEATSL
VRVAPPNYHT VFNPDKSYLL VGCLGGLGRS MSRWMLSRGA RKFTFLGRSG TDREPAARLV
QYLELCGASV TVVRGDVVDA SDVERAVAAS AAAGPIGGVV QAAMGLDEAL FTAMPAAYWR
KGLAPKVRGS LNLHAALAGR DADLDFFLMT SSVSGSVGTA TESNYCAANY FLDVFARHRR
GLGLPATSVG LGMISEVGYL HENPEIEAML LRKGIQAISE DEMLNMIDIS LSASSSSRTR
GSPAAAWRGT DHALAHTLTG LEPIGVRELR AQGFDVSSPV LGDPRASLLA AALAADENES
AGAGAGGAST SSGGLPAGLA QAVAGGSAGA VAAQALELVA DKFSNLVLVP RDRLDLLRPL
SDVGVDSMLA AEFRGWIYQQ LKVNVPYLTM LASTTTLTML SELIAGKLLE A
