ID   PKS1_COCH4              Reviewed;        2528 AA.
AC   N4WHE3; Q92217;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Reducing polyketide synthase PKS1 {ECO:0000303|PubMed:8953776};
DE            EC=2.3.1.- {ECO:0000305|PubMed:8953776};
DE   AltName: Full=T-toxin biosynthesis protein PKS1 {ECO:0000305};
GN   Name=PKS1 {ECO:0000303|PubMed:8953776}; ORFNames=COCC4DRAFT_45906;
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.
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   [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, AND DISRUPTION PHENOTYPE.
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   [5]
RP   FUNCTION.
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   [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:8953776}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the loss of T-Toxin production,
CC       resulting in low virulence for maize (PubMed:8953776, PubMed:12236595).
CC       {ECO:0000269|PubMed:12236595, ECO:0000269|PubMed:8953776}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U68040; AAB08104.3; -; Genomic_DNA.
DR   EMBL; KB733517; ENH98624.1; -; Genomic_DNA.
DR   RefSeq; XP_014072534.1; XM_014217059.1.
DR   AlphaFoldDB; N4WHE3; -.
DR   SMR; N4WHE3; -.
DR   PRIDE; N4WHE3; -.
DR   EnsemblFungi; ENH98624; ENH98624; COCC4DRAFT_45906.
DR   GeneID; 25845241; -.
DR   HOGENOM; CLU_000022_31_1_1; -.
DR   OrthoDB; 19161at2759; -.
DR   PHI-base; PHI:55; -.
DR   Proteomes; UP000012338; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase 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: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; 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; 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; 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; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW   Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..2528
FT                   /note="Reducing polyketide synthase PKS1"
FT                   /id="PRO_0000437634"
FT   DOMAIN          2442..2519
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          14..439
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          573..868
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000255"
FT   REGION          956..1277
FT                   /note="Dehydratase (DH) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1827..2139
FT                   /note="Enoyl reductase (ER) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          2164..2341
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2479
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2528 AA;  275297 MW;  AC6429AF6734E3C3 CRC64;
     MTVRDSKTGG ITPIAVVGMS FRGPGDATNV EKLLNMISEG RESRAEVQAK KWDPEGFYHP
     DSSRHGTHNV EYGHWFQQDV YNFDAPFFNV SPAEAAALDP QQRMLLECSY EAFENSGTPM
     SKIVGTDTSV FVSSFATDYT DMLWRDPESV PMYQCTNSGF SRSNLANRIS YSFDLKGPSV
     LVDTACSGGL TALHLACQSL LVGDVRQALA AGSSLILGPE MMVTMSMMKF LSPDGRCYAF
     DERANGYARG EGVAVLLLKR LEDALADNDT IRAVIRGTGC NQDGKTPGIT MPNSVSQEAL
     IRSVYKKAAL DPLDTTYVEC HGTGTQAGDT TEASALSKVF SPGRRLPLLI GSVKTNIGHL
     EGASGLAGVV KSILMLEQGV ILPNRNFERP NTKIPLEKWN LRVPTTLECW NNVKTRRVSI
     NSFGYGGANV HAILESATDF LRDNSMGTDS TRFASRRSVV VGNVGQTKPA VSLVQDMSSN
     DRSHEDPTPL LFALSAFDSS AGDAWARSLS IYLSQRQGSD EKTILSSLAY TLSDRRTWHP
     WKAALSATTI QELITKLEKV RFVNMAPRHN IGFVFTGQGA QWCGMGRELI SIFPRFRQSL
     IACDIALQSF GADFHVIDEL EADVESSRIN KALYSQPLCT ALQIALVDLL VSWGIYAQSV
     TGHSSGEIAA AYAAGALSLS DAMLVAYARG CATANLAKKG AKGAMAAVSM ETQELSHILS
     ALENGKVGIA CFNSPTSCTV SGDKSALDEL QDVLRQKGVY NRRLIVDVAY HSHHMELIAD
     SYRSAISSIQ PLPGSDVKFF SSVTGELLDK NKLGVDYWVS NLVGQVKFAQ SLSSLVSSHH
     GTGTPQIQAL IEIGPHAALG GPISQVIDSE PLANPTGYFS ALVRKKNAVT TILSLAADLF
     LSGYPIQLSA VNQNCNSRHT PLVDLPSYSW NHSKAYTAES RISKTYRQRR YPRLDLIGVF
     DVHSSVLEPR WRQVIRLSEL PWLQDHKIQS SILYPVAGYI AMAIEAATQR NQMREMGNDI
     LGYQFRDVAI SSALTIPDMP GQVEVFITLR SFSESVRSPS NLWDEFSISS VNDENRWTEH
     CRGLISVLKS SKLSNLVNGK MQDASTIACQ HDLREVFATC CKTEWDVKDM YEHFWETGMQ
     YGPTFANLCD VRCTSNKCIG KVKVPDTAAV MPMKHEAPFI IHPGTLDSII QTYLPALVQA
     GHLKSATIPV AIESMFISRN VTRQAGDLLT SYASSTRKDY RYFSTSMSVF ADGPSSENQL
     VITIDDMTLV ALDRPNSSEE SGEALPLAFN LHWKPDVDML TEEQLVEMIN ASTKVKDHIA
     AKKMKQTAAQ LGKEILARVP FEQAQVVGES SRHLWKLLHA SLESLSTPDH RGALDEISSL
     KNVDSTLAQA ADRLSNVLTG RVAPSDVASM YDLMEAVRIP ELYDNNLPTA TYLHLLGHKK
     PSLRVLTVGP QSGPTSLNLL MLLAELGGGE IPFAVLHHSD AELNIDQTVR SRFPSWADSV
     GFRDVFNESG ASQQNPPIVN ETYDIVVAFN VLGSSPGFSK TLSAAAPLLN ARGKILLVDN
     SHKSPMAALV WGPLPSFLST WVDEKSADSP DVDCAVQSMG YDIYARLCPN VTVIQRAAQV
     QKAEKTIGLD VLVVTDGEPA GVDLQQLQTL CEDQYAEVHV ASLEHARPRP GQACIVLSEL
     SRPVLAAPTA AEWEAVKRIT DTCSGIVWVT RGAADNVCSN PQVSLIQGFA RTVRAEAGDK
     PITTLDLDND KVLSAQAAAA YIAAVFQRMM QGGEDIDVEL QERRGILHVA RLIEDGDAAK
     QLQGEATAME LRLDQAGPCR LFAGTPGLLD SLHFTVDDRV QESLETGQIE VQVHATGINF
     KDVMMAMGQI AVEDLGCECS GVVSAVGDGV VGLRVGDRVA CMGPGSFCTQ LRVDARLAHR
     IPHHMELETA AALPITYVTA YHSIHNIAHL RHGETILIHA AAGGLGQALV ELSQLVGARV
     LVTVGSTEKK RLIMQRFRLS EEDILFSRDT SFVHDVMRLT NGRGVDVIMN SLAGESLRQS
     WTCIAPNGRF VELGQRDITV NSRLDMAPFA RNVSFTAYNL AYMLRHDPQA AHEVLAEVLA
     LYDQGKLRGP EPLEKCTFSQ LGNAFRKIQT GRHMGKMVAV ANPDDMVWYK PPPASRRTLF
     RPDASYLLVG GVGGLGSATA LWMSTRGARH LLLLNRSGAD TEAARTTLAT LRANGCTATV
     LACDVADKAQ LSSVLAEARS NWPPIRGVIQ GAMVLRDSML ANMTLEDYMA VVRPKVQGTW
     NLQTHLPADL DFFILESSIS GIIGNPGQAA YAAANTFLDA FARWRRARCQ PATVIDIGAV
     HGIGYLERNV DVKLSMERQG FAFTDEQLLM RLLEFAISHS SREPHRAQIV TGLGPWHPDT
     SLPGLNAPLF SRYRMLSCQN STGSTDVDTL RGILAQSSSF DSAVTIVLSA LVDQVVSRTE
     IPIENVHTTK SLQDYGIDSL VAVELRNWLI KDMDSVVPML ELLGAESLSA LAVKIAARSQ
     LISTNNRG