PKS2_COCH4
ID PKS2_COCH4 Reviewed; 2144 AA.
AC N4WHA7; Q2XW08;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Reducing polyketide synthase PKS2 {ECO:0000303|PubMed:16529376};
DE EC=2.3.1.- {ECO:0000305|PubMed:16529376};
DE AltName: Full=T-toxin biosynthesis protein PKS2 {ECO:0000305};
GN Name=PKS2 {ECO:0000303|PubMed:16529376}; ORFNames=COCC4DRAFT_45941;
OS Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665024;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16529376; DOI=10.1094/mpmi-19-0139;
RA Baker S.E., Kroken S., Inderbitzin P., Asvarak T., Li B.Y., Shi L.,
RA Yoder O.C., Turgeon B.G.;
RT "Two polyketide synthase-encoding genes are required for biosynthesis of
RT the polyketide virulence factor, T-toxin, by Cochliobolus heterostrophus.";
RL Mol. Plant Microbe Interact. 19:139-149(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
RN [4]
RP FUNCTION.
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=8953776; DOI=10.2307/3870419;
RA Yang G., Rose M.S., Turgeon B.G., Yoder O.C.;
RT "A polyketide synthase is required for fungal virulence and production of
RT the polyketide T-toxin.";
RL Plant Cell 8:2139-2150(1996).
RN [5]
RP FUNCTION.
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=12236595; DOI=10.1094/mpmi.2002.15.9.883;
RA Rose M.S., Yun S.-H., Asvarak T., Lu S.-W., Yoder O.C., Turgeon B.G.;
RT "A decarboxylase encoded at the Cochliobolus heterostrophus translocation-
RT associated Tox1B locus is required for polyketide (T-toxin) biosynthesis
RT and high virulence on T-cytoplasm maize.";
RL Mol. Plant Microbe Interact. 15:883-893(2002).
RN [6]
RP FUNCTION.
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=20192833; DOI=10.1094/mpmi-23-4-0458;
RA Inderbitzin P., Asvarak T., Turgeon B.G.;
RT "Six new genes required for production of T-toxin, a polyketide determinant
RT of high virulence of Cochliobolus heterostrophus to maize.";
RL Mol. Plant Microbe Interact. 23:458-472(2010).
CC -!- FUNCTION: Reducing polyketide synthase (PKS); part of the Tox1A locus,
CC one of the 2 loci that mediate the biosynthesis of T-toxin, a family of
CC linear polyketides 37 to 45 carbons in length, of which the major
CC component is 41 carbons, and which leads to high virulence to maize
CC (PubMed:8953776, PubMed:20192833). One of the PKSs (PKS1 or PKS2) could
CC synthesize a precursor, used subsequently by the other PKS as starter
CC unit, to add additional carbons (PubMed:16529376). Variability in the
CC length of the final carbon backbone C35-47 could be achieved by varying
CC the number of condensation cycles, or use of different starter or
CC extender units or might be due to decarboxylation of the penultimate
CC product, catalyzed by DEC1 (PubMed:12236595). Additional proteins are
CC required for the biosynthesis of T-toxin, including oxidoreductases
CC RED1, RED2, RED3, LAM1 and OXI1, as well as esterase TOX9
CC (PubMed:20192833). {ECO:0000269|PubMed:12236595,
CC ECO:0000269|PubMed:16529376, ECO:0000269|PubMed:20192833,
CC ECO:0000269|PubMed:8953776}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:16529376}.
CC -!- DISRUPTION PHENOTYPE: Leads to the loss of T-Toxin production,
CC resulting in low virulence for maize (PubMed:16529376).
CC {ECO:0000269|PubMed:16529376}.
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DR EMBL; DQ186598; ABB76806.1; -; Genomic_DNA.
DR EMBL; KB733526; ENH98579.1; -; Genomic_DNA.
DR RefSeq; XP_014072489.1; XM_014217014.1.
DR AlphaFoldDB; N4WHA7; -.
DR SMR; N4WHA7; -.
DR EnsemblFungi; ENH98579; ENH98579; COCC4DRAFT_45941.
DR GeneID; 25845246; -.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000012338; Unassembled WGS sequence.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
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; IPR020806; PKS_PP-bd.
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 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; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..2144
FT /note="Reducing polyketide synthase PKS2"
FT /id="PRO_0000437635"
FT DOMAIN 2059..2136
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 13..439
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 538..855
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000255"
FT REGION 924..1214
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1461..1747
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 1771..1948
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2096
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 1359
FT /note="R -> W (in Ref. 1; ABB76806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2144 AA; 231806 MW; 2B6B1F50574B5773 CRC64;
MTSRQNTNTP MPLAIIGMSC RFPGKVASLE DFWDMLSNSK HGYRQFPRER FNWEAFYHPN
QSRKDCIDVN CGYFLDGDIA EFDAQFFKMN GTDAASFDPQ GRMILECVYE ALENAGVPKE
SIVGSKVGVF STSNTSDYTL SLKDDIYSMP ALVGVLGHAC MLSNIVSNTF DLKGPSVSID
TACSSAFYAL QLASQSLRSG ETEMCIVSGC ALNISPWRWT MLSNLTMLNP DGLSKSFDPQ
ADAGYVRGEG AASIIVKPLD AAIRDNDRVH CVLSDIGVNH NGRTNGYTLP DARMQASLMR
ELQVRLDIKP DEFGFVEAHA PGTRVGDPIE ISALQEVFST SARTLEDPLL IGSVKANVGH
LESSSGFPSL IKAAMMLKKG LVVPNANFEN ESMNSHLKEK NMRVPISTQP WPKGKTYIAI
NNYGFGGSNS HCIVRAPPIP QGLVSQKETR NVESDYLFVL SANDEVALRR TREQLVEFLE
SVDASSTTMQ NTAYTLGQRR SLLSWRATVV ASNIDDLIIQ AASPQVIPRR VTRQPTLVFA
FTGQGAQYFG VGRELLQYPV FSTTLKMASA CAESFGANFS LQDELYGNEA TSRINDADVS
QPASTAIQIA LVDLLRSWGI QPSAVVGHSS GEVAAAYAAG LLSLPGAMRI AYARGQMAIR
IKKVQPDFKG GMLAVAAGPA DVLPLLDIVT SGKVVIACEN SPKSVTVSGD EAGLVELESL
LEEDGLPHRR LAVDFPYHST FLDPFIDDYE EAICTDDTFS NLQPTAEYFS AMAGRKVEPV
TVQKPSYWAS SAKFRVRFTS AAKALLRSKP SPNVVVEIGP NPTLVGSLKS ILSEIKKEIP
HPIEVVPSLH RGQNARTAML KLGASLVSFG QRIDMEQVNF ASGHISGQPP TLVDGIKPYP
WTRSHHWIKS RVRDDDLHRP FPHHDLLGSI NSSWGSKELV WKNNLDVENV PWLRDYQVAS
SITYPLAGYV CAAIEASKQF AMTRNLFLDR AFKGFTVRDM IIDESLVMKE GIPVELVTKL
RSLPGTNFEE FEVLSWDEGQ RAWKRCCRAL VKCEATTDGV EQVEEMKWAE SRAACHSCVG
SPLLYQRLSK VGPRRTGKFR NVVDLRYGAG KTTAEVVVSD TKASMPQHYE SDMTVHPTTI
DGLFQCGSCI PFLDESSSVV GGSSNIWVPR SIKEFTIQTR PGEALKPEMV FRTVARVDKN
ERHDRSYSID GTTDNAPICQ IRIRGLKLAV EATLAPQWPA PHYGCYKIAW QNATELRSQA
AQWHVLQGPG DVKNLAGSVS KKIGGTVRPL CEGVPSEASF CVVVDVGEGL LASVERESFN
HIKQALTTCE GVLWVTCGAF GVSYDSTHPN AGMVTGLLRT IRSEMRASVA SLDLDANASS
DIEAQAALVK RVADHLAAAA QNADVQAEME FTEKQGQLMV SRVVHDTQLD NVVHAVTGVI
APRTEPFDPE VRGFFTLQRP GMPDSLYLQR TDVPDPLDES EVEVRIAAIA LDADDIHGLQ
GRALSGTVVR CGSTVTRVQP GDRVFGLANI DGAVRTFARA PETCLARTPA NIPIDAAAAL
PATLGAAYHA LVDLGRLVAG ESVLIVAVGS ALGQAAIQVA LAKGALVFAL AHSQEERDAA
IVAGASIDRV VTTLVGLPPI QILFNPVSDA NANLSMLGAL APLGRIVQVG EPSHQYPALA
VGHSFSIAHL DAVADALPAQ MAAILDAVVG LVDSKFVHSP PVRTVGLEYL SEALSNISET
DSKKLLLVPG KNEMVKATPS CPAPPTFDPA AVYLLVGGSG GLGRVIAKWM LNNGARKIGL
LSRSTSMSPD VRTLVDDAAG IGAEVFLLPC DVTSQHHLQR VIDQCVIEKG QIKGVINAAM
VFKGGVFTSV SFDDFTSVVQ PKVCGTWNLH HALREATLDF FILISSVAGI MGTPGHSAYA
SANTFLDSFA MYRMQQGLPA TSLALTAVVD AGYMAENASK LQKLKYVSEF EGEILLTADV
LALLGAAVTG SIASSCKGFS IIGAGFGTAL KLPSYAQDPR FSTLTSNHSQ DRKSKPRTTT
AANTDTLVYA VDQADTKEEA TQLLLAAIRD KIAQLQLIPV SDIVDDQTIT ELGLDSLTVM
ELYSWVGRLF RLRFGIQEYA RLDTLEKIVD SVIVKREAAK VEAP
