NEC1_MAGO7
ID NEC1_MAGO7 Reviewed; 2758 AA.
AC G4NEB1;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Highly reducing polyketide synthase NEC1 {ECO:0000303|PubMed:30443971};
DE EC=2.3.1.- {ECO:0000269|PubMed:30443971};
DE AltName: Full=Nectriapyrone biosynthesis cluster protein 1 {ECO:0000303|PubMed:30443971};
GN Name=NEC1 {ECO:0000303|PubMed:30443971}; ORFNames=MGG_00806;
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 CATALYTIC
RP ACTIVITY.
RX PubMed=30443971; DOI=10.1002/cbic.201800620;
RA Motoyama T., Nogawa T., Hayashi T., Hirota H., Osada H.;
RT "Induction of nectriapyrone biosynthesis in the rice blast fungus
RT Pyricularia oryzae by disturbance of the two-component signal transduction
RT system.";
RL ChemBioChem 20:693-700(2019).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of nectriapyrone and its analogs
CC phomopyrone A, acropyrone and zaepyrone (PubMed:30443971). The
CC nectriapyrone biosynthetic gene cluster consists of two genes, the
CC highly reducing polyketide synthase NEC1 that produces a demethylated
CC analog of nectriapyrone from one unit of acetyl-CoA and one unit of
CC malonyl-CoA; and the O-methyltransferase NEC2 that further methylates
CC the NEC1 product to yield nectriapyrone (PubMed:30443971).
CC Nectriapyrone is further hydrolyzed to nectriapyrone D, also known as
CC gulypyrone B, by an unidentified hydrolase localized outside the
CC nectriapyrone cluster (PubMed:30443971). {ECO:0000269|PubMed:30443971}.
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:30443971}.
CC -!- DISRUPTION PHENOTYPE: Completely abolishes the production of
CC nectriapyrones. {ECO:0000269|PubMed:30443971}.
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DR EMBL; CM001235; EHA48594.1; -; Genomic_DNA.
DR RefSeq; XP_003718178.1; XM_003718130.1.
DR SMR; G4NEB1; -.
DR EnsemblFungi; MGG_00806T0; MGG_00806T0; MGG_00806.
DR GeneID; 2675225; -.
DR KEGG; mgr:MGG_00806; -.
DR VEuPathDB; FungiDB:MGG_00806; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; G4NEB1; -.
DR OMA; IHQYGVD; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000009058; Chromosome 5.
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; -; 2.
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; 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; 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; 2.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..2758
FT /note="Highly reducing polyketide synthase NEC1"
FT /id="PRO_0000446265"
FT DOMAIN 2673..2750
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:30443971"
FT REGION 38..495
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30443971"
FT REGION 512..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..1044
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30443971"
FT REGION 1124..1442
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30443971"
FT REGION 1622..1727
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30443971"
FT REGION 2031..2344
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30443971"
FT REGION 2372..2553
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30443971"
FT COMPBIAS 512..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 790
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1156
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2710
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2758 AA; 298817 MW; 46635CB20141A393 CRC64;
MFLKQQQQQP VEADFVDCQS TPRAGGPVAG TTFYTVPVRT FGVELGEYWY PGGSRGPVAF
VETEKLATFP TRFCASDYAG SSHSSPQPTA VGVSRERLDR GRFLGKHGEM PTLPLDSIAS
CGVHRIPEYR WIGKWAEQVD DGASAVNIRR LFEASSPIIG LDARFPGDGD TAERFYDFLL
AGRSARSEIP PERYNADAFW HPDGNRSGAT RARAAHFLKG SISAFDAPLF SITPTEAAAM
DPQQRGILES VYRALENGKF PLAVVGGCNL IISPEFALLL DAAGVLGPDG KSYSFDHRGN
GYSRGEGFGV VVLKRLPDAL RDGDVIRAVI RNSGSNSDGR SPGITQPTKA AQAALIKQVY
ANAGLDPSVT RFFEAHGTGT AVGDPIEASA IAEVFATHRS HKSPLWVGAL KSNIGHLEGA
AGVAAVIKGV LTLENGVIPP NTWFERKNPK ILDSWNLQFP TEPVVWPQTG LRRMSINSFG
VGGSNAHVVM DDALHFLQSY GLVGNHRTVA LPRLPGSSSS RRVVSQADSG VEFTDSDSEL
KTPDGTHSPD STAEHSKDMN FDSSCTNTDT LQTTDTNKQP KLSAIACPEV LSSSLSRLAV
SDEEGRQSQI FVFSSSDKDG VSRVVNELAD YLAKKAKQYK PNMRDQSKFL RDLSYTLACK
RTRHAWRSFV VAKTQSSLSA LLQAKSLATR AASEPQLAFV FTGQGAQWPT MGRGLMAYPT
FRESLHEAEE YMTQTLRCPW SLTYELCKEA GASRINDAEF SQPVCTALQV ALVDLLRTWK
VRPHAVVGHS SGEIAAAYAA GQLSRQSSWR IAYYRGKLAT KLIRSLRRRE NSQDAHVKKT
GMVAVGLDKE QTLAAISRVD SLVGEGSLEI ACMNSQESHT VSGDMAKLDA LVEVLKSENV
FARKLSVGIG YHSRHMLPIA DEYVRLIGDI GSDLPPSQGQ SLPRYFSSLE GSEITLDRLQ
SPDYWANNLT SPVRFHEAVE LMLRADLGCN SQGESSTVGK KTVTDLLEIG PHAALRGPIR
SIVKQVHQTA EWKIGYATVL KRGDGAIENA LGAAGSLFCR GFDVDLAAVN QHQVESSRQS
IALNGGNNVL MLTDLPGYPF NHKKEYWAES RLSRNYRFRS APRHELLGAP VPDWDKNDAV
WRNYIRITEN PWVEHHKVSG EILYPAAGML VMAIEASRQL VDKDQQVAGF RFKDVSFHLA
LLIPTNDVGV ETRFRLRSVS AGKLAGWSEF QLSTSENDDW KEHCRGFVRT EYSQTGSNTE
SDSSRLVHSQ CEQEIVQAKK SCTSMVHADK VYRKLSNIGL DFGTTFRTLK DVKFDGTSRI
LARAESQVSH IKKSMPAEYL HSHLVHPSML DAVLQANLIP IALGSSSRDS LVPVFASDFW
VSAATKEGVD FHNSAYLISS HAKLTPGTAD AEAALFGIHA DTGEPLVTSS GLVFKTIPNT
ASSGQRNHHR PALNLDWKPD PNYLTEEDAL RMFGAPAITQ SSDEVSDDIG DCEILCLLYI
RRFLASLDDT VVEKLDWHHL RYVSWMRHVV QTTTVKPAVD NISVMEARIA AAGTPEGKLI
MAVGRNLANI LVTGDVDPLD VIFGDKVAEN VYREGLGSRR CYAQMCAYLD ALAHVNPSMK
ILEVGGGTGG ATGSIMETLM ANGARRFDHY DFTDISPSFF EHAKEAFKQT AEHMSFRVLN
IEKEPTDQGY DGQSYNLVLA ANVLHATKSM ERTLANVRKL LKPGGKLIVF ELTNPAVLLG
GFCFGVLPGW WLSDEADREW GPLMVVDTWR AYLERAGFSG VDAVFDDFPD AAHQTSSILV
STALPVADAS KPVTAVDNLT RYCVLMGERP SVFQRQVADA LLPALARTGS VETSTITASA
GRDLKGSCCI VLSELDSPTL IDMTTDVFVA LQGVLNSCRR IIWLSRSGDD IVAAPDRELV
TGLARVVRAE REPPFSFVTV SFAEAERSET IVDKTLQVLD RGQETAENSF RVFNGVVHVP
RLVEAGYLTD HISAEANPTS TQATTQEVKL GADPRDFVAQ VQSTGLLQGA GTADVCFSED
HSRQQPLADD EVEFKVMACG VGAHDVAAED SAAGESSLSD MGIQMAGFVT RLGSTAASKF
SVGDRVTGIS LEGAIKTRAR TQAGLLAKIS DKLAWNQAAQ IPMAYFTACA IIQYMGVGDS
DDILLVHRAA ASAAGLAAVQ VARSNGAKIF ATVANAQERT ALQGVGGLLT DQILDLDQNT
TLSTIVKSKT GNRGVSMIID SLPQSDVDHA ASLVDCLAPF GRFVSLGDGP MPGISSRRNI
CLERFNGAEL MALDYEKAQR IFLRAARFIL DEPLAANAQV PVYKFSEVSE AFAQLGKGED
AVVLEPHDED VVKVVTSQQS HTDFTSRFDP GASYMVVGGL GGLGRSVSRW MASKGAKSLV
LVSRKGAVTP EAQVLVAELQ DLGVKVTTPA CDATDKMALR RALDQCVAHM PPIKGVIQCS
MVLKDKRFFE MSLEEWNTAI RPKVDVSVNL HDALDTASLD FFIMLSSTVG LTGSVEQANY
AAGGTFQDAF ARSLAASQTA SSGPVAVSLD LPVILDVGFV AEKPELMDQL RAAGWAYMEE
EEFHAALGYH CFQRRQLDLP TSVLRAQVAP RLWLAQDTAD EGTEPPAWVR DPLFSHLRPQ
SSETTGNGAA GGEAGKKEMK HTALLAAATS AAEAQAVVLD ALLAKLSRVL SVELSDLDPA
CPLSRYGVDS LVAVSLRAWI GKELGAELSV FEMTDKPSIR ALAAAVAGRS RLVSKALS
