PKS12_GIBZE
ID PKS12_GIBZE Reviewed; 2067 AA.
AC I1RF58; A0A098D9G9;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Non-reducing polyketide synthase PKS12 {ECO:0000303|PubMed:15811992};
DE EC=2.3.1.- {ECO:0000269|PubMed:23557488};
DE AltName: Full=Aurofusarin biosynthesis cluster protein PKS12 {ECO:0000303|PubMed:15811992};
GN Name=PKS12 {ECO:0000303|PubMed:15811992};
GN Synonyms=AUR1 {ECO:0000303|PubMed:16278459};
GN ORFNames=FG12040, FGRAMPH1_01T05593;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15811992; DOI=10.1128/aem.71.4.1701-1708.2005;
RA Kim J.E., Han K.H., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT "Putative polyketide synthase and laccase genes for biosynthesis of
RT aurofusarin in Gibberella zeae.";
RL Appl. Environ. Microbiol. 71:1701-1708(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16278459; DOI=10.1128/ec.4.11.1926-1933.2005;
RA Gaffoor I., Brown D.W., Plattner R., Proctor R.H., Qi W., Trail F.;
RT "Functional analysis of the polyketide synthase genes in the filamentous
RT fungus Gibberella zeae (anamorph Fusarium graminearum).";
RL Eukaryot. Cell 4:1926-1933(2005).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=15809006; DOI=10.1016/j.fgb.2005.01.010;
RA Malz S., Grell M.N., Thrane C., Maier F.J., Rosager P., Felk A.,
RA Albertsen K.S., Salomon S., Bohn L., Schaefer W., Giese H.;
RT "Identification of a gene cluster responsible for the biosynthesis of
RT aurofusarin in the Fusarium graminearum species complex.";
RL Fungal Genet. Biol. 42:420-433(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15780665; DOI=10.1016/j.femsyr.2004.12.008;
RA Maier F.J., Malz S., Losch A.P., Lacour T., Schafer W.;
RT "Development of a highly efficient gene targeting system for Fusarium
RT graminearum using the disruption of a polyketide synthase gene as a visible
RT marker.";
RL FEMS Yeast Res. 5:653-662(2005).
RN [8]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=16879655; DOI=10.1111/j.1365-2958.2006.05295.x;
RA Frandsen R.J., Nielsen N.J., Maolanon N., Soerensen J.C., Olsson S.,
RA Nielsen J., Giese H.;
RT "The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a
RT close link between the naphthoquinones and naphthopyrones.";
RL Mol. Microbiol. 61:1069-1080(2006).
RN [9]
RP INDUCTION.
RX PubMed=16461721; DOI=10.1128/aem.72.2.1645-1652.2006;
RA Kim J.E., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT "GIP2, a putative transcription factor that regulates the aurofusarin
RT biosynthetic gene cluster in Gibberella zeae.";
RL Appl. Environ. Microbiol. 72:1645-1652(2006).
RN [10]
RP INDUCTION.
RX PubMed=17897620; DOI=10.1016/j.bbrc.2007.09.027;
RA Ochiai N., Tokai T., Nishiuchi T., Takahashi-Ando N., Fujimura M.,
RA Kimura M.;
RT "Involvement of the osmosensor histidine kinase and osmotic stress-
RT activated protein kinases in the regulation of secondary metabolism in
RT Fusarium graminearum.";
RL Biochem. Biophys. Res. Commun. 363:639-644(2007).
RN [11]
RP INDUCTION.
RX PubMed=19909822; DOI=10.1016/j.fgb.2009.11.001;
RA Zhou X., Heyer C., Choi Y.E., Mehrabi R., Xu J.R.;
RT "The CID1 cyclin C-like gene is important for plant infection in Fusarium
RT graminearum.";
RL Fungal Genet. Biol. 47:143-151(2010).
RN [12]
RP FUNCTION.
RX PubMed=21296881; DOI=10.1074/jbc.m110.179853;
RA Frandsen R.J., Schuett C., Lund B.W., Staerk D., Nielsen J., Olsson S.,
RA Giese H.;
RT "Two novel classes of enzymes are required for the biosynthesis of
RT aurofusarin in Fusarium graminearum.";
RL J. Biol. Chem. 286:10419-10428(2011).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23557488; DOI=10.1186/1475-2859-12-31;
RA Rugbjerg P., Naesby M., Mortensen U.H., Frandsen R.J.;
RT "Reconstruction of the biosynthetic pathway for the core fungal polyketide
RT scaffold rubrofusarin in Saccharomyces cerevisiae.";
RL Microb. Cell Fact. 12:31-31(2013).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of aurofusarin, a red mycelium pigment
CC which is acting as a mycotoxin (PubMed:15811992, PubMed:16278459,
CC PubMed:15809006, PubMed:15780665, PubMed:16879655). The first step is
CC performed by the polyketide synthase which condenses one acetyl-CoA and
CC 6 malonyl-CoA units to form the first intermediate, the cyclic
CC heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488).
CC The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed
CC during ring closure by an aldol-type cyclization reaction
CC (PubMed:21296881). The dehydratase aurZ then acts as the first
CC tailoring enzyme in the aurofusarin biosynthetic pathway by converting
CC YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488). Nor-
CC rubrofusarin is then methylated to rubrofusarin by the O-
CC methyltransferase aurJ (PubMed:21296881, PubMed:23557488). Rubrofusarin
CC is then transported across the plasma membrane by the rubrofusarin-
CC specific pump aurT for further enzymatic processing by the
CC extracellular complex composed of GIP1, aurF, aurO and aurS to yield
CC aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15780665,
CC ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:15811992,
CC ECO:0000269|PubMed:16278459, ECO:0000269|PubMed:16879655,
CC ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + H2O +
CC YWA1; Xref=Rhea:RHEA:62652, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:133763;
CC Evidence={ECO:0000269|PubMed:23557488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653;
CC Evidence={ECO:0000269|PubMed:23557488};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006,
CC ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:23557488}.
CC -!- INDUCTION: Expression is regulated by the aurofusarin biosynthesis
CC cluster-specific transcription factor aurR1/GIP2 (PubMed:16879655,
CC PubMed:16461721). Expression is negatively regulated by the MAPK-
CC mediated osmotic stress-signaling pathway (PubMed:17897620). Expression
CC is also regulated by the CID1 cyclin C-like protein (PubMed:19909822).
CC {ECO:0000269|PubMed:16461721, ECO:0000269|PubMed:16879655,
CC ECO:0000269|PubMed:17897620, ECO:0000269|PubMed:19909822}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DOMAIN: The C-terminal region is involved in Claisen-type cyclization
CC of the second ring of naphthopyrone. {ECO:0000250|UniProtKB:Q03149}.
CC -!- DISRUPTION PHENOTYPE: Leads to a albinos phanotype and affects
CC conidiation (PubMed:15811992, PubMed:16278459, PubMed:15809006,
CC PubMed:15780665). {ECO:0000269|PubMed:15780665,
CC ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:15811992,
CC ECO:0000269|PubMed:16278459}.
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DR EMBL; HG970332; CEF74601.1; -; Genomic_DNA.
DR RefSeq; XP_011318233.1; XM_011319931.1.
DR AlphaFoldDB; I1RF58; -.
DR SMR; I1RF58; -.
DR STRING; 5518.FGSG_02324P0; -.
DR GeneID; 23549706; -.
DR KEGG; fgr:FGSG_02324; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G05593; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR InParanoid; I1RF58; -.
DR PHI-base; PHI:720; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..2067
FT /note="Non-reducing polyketide synthase PKS12"
FT /id="PRO_0000441086"
FT DOMAIN 1660..1738
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 4..241
FT /note="N-terminal acylcarrier protein transacylase (SAT)
FT domain"
FT /evidence="ECO:0000255"
FT REGION 350..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..811
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 912..1199
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1329..1604
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1619..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1742..1779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1781..2065
FT /note="Claisen cyclase domain"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT COMPBIAS 352..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1742..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 545
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1001
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1875
FT /note="For Claisen cyclase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1698
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2067 AA; 225115 MW; F66729BC0A3DA919 CRC64;
MEVFVFGDQS TRFAPPLKDL LLKGNSPYLT HFVKQVHALL RREISSLPAV QQKLFPNFAD
IQELVSKSDW GSGNPALTSA LACFYHLCSF IHFYDGQGRT FPSENSRIIG LCVGSLAAAA
VSCSTSLSEL VSAGVDAVRV ALHVGLRVWR TTSLFDVPDR PSATWSIIVP EAVLPRESAQ
DRLDSFIIEM GLARSSVPYI SSVAHHNMTI SGPPSVLEKF IHSISTSPKD SLPVPIYAPY
HASHLYSMDD VDEVLSLSAP SFASESIIPL ISSSSGDELQ PLKYADLLRC CVSDMLIQPL
DLTKVSQAVA QLLEVSSSTR AIIKPIATSV SNSLVSALEP TLAERCAVDN SMGPKASTSH
SSAETQTESS SKNSKIAIVA MSGRFPDAAD LGEFWDLLYK GRDVHRQIPE DRFNAELHYD
ATGRRKNTSK VMNGCFIKEP GLFDARFFNM SPKEAEQSDP GQRMALETAY EALEMAGIVP
DRTPSTQRDR VGVFYGMTSD DWREVNSGQN VDTYFIPGGN RAFTPGRLNY FFKFSGPSAS
VDTACSSSLA ALHLACNSLW RNDCDTAIAG GTNVMTNPDN FAGLDRGHFL SRTGNCNTFD
DGADGYCRAD GVGTIILKRL EDAEADNDPI LGVILGAYTN HSAEAVSITR PHAGAQEYIF
SKLLRESGTD PYNVSYIEMH GTGTQAGDAT EMTSVLKTFA PTSGFGGRLP HQNLHLGSVK
ANVGHGESAS GIIALIKTLL MMEKNMIPPH CGIKTKINHH FPTDLTQRNV HIAKVPTSWT
RSGQANPRIA FVNNFSAAGG NSAVLLQDAP RPSVVSDVTD PRSSHVVTMS ARSADSLRKN
LANLKELVEG QGDSEVDFLS KLSYTTTARR MHHQFRASVT AQTREQLLKG LDSAIERQDV
KRIPAAAPSV GFVFSGQGAQ YRGMGKEYFT SFTAFRSEIM SYDSIAQAQG FPSILPLIRG
EVEADSLSPV EIQLGLTCLQ MALAKLWKSF GVEPGFVLGH SLGHYAALHV AGVLSANDTI
YLTGIRAQLL VDKCQAGTHS MLAVRASLLQ IQQFLDANIH EVACVNGPRE VVISGRVADI
DQLVGLLSAD NIKATRVKVP FAFHSAQVDP ILSDLDTAAS RVTFHSPQIP VLCALDSSVI
SPGNHGVIGP LHLQRHCRET VNFEGALHAA EREKIINKTS TLWIEIGPHV VCSTFLKSSL
GPSTPTIASL RRNDDCWKVL ADGLSSLYSS GLTIDWNEYH RDFKASHQVL RLPCYSWEHK
NYWIQYKYDW SLTKGDPPIA PNSSVEAVSA LSTPSVQKIL QETSLDQVLT IVAETDLASP
LLSEVAQGHR VNGVKVCTSS VYADVGLTLG KYILDNYRTD LEGYAVDVHG IEVHKPLLLK
EDMNGTPQAT PFRIEVRYPI QSTTALMSIS TTGPNGQHIK HANCELRLEH PSQWEAEWDR
QAYLINRSVN YLLQRSAQGL DSMLATGMVY KVFSSLVDYA DGYKGLQEVV LHSQELEGTA
KVRFQTPSGG FVCNPMWIDS CGQTTGFMMN CHQTTPNDYV YVNHGWKSMR LAKAFREDGT
YRTYIRMRPI DSTKFAGDLY ILDEDDTVVG VYGDITFQGL PRRVLNTVLP SANAVPVDAP
MGRRDVPPSR MDVPPVRSGE GPPTSAPTQQ AIALPFAADT SMDSRLRPLL RILSEEIGLG
LDVLSDDELD FADHGVDSLL SLTITGRMRE ELGLDVESTA FMNCPTLGSF KLFLGLVDQD
NKSSSGSDGS GRSSPAPGIE SGATTPPMSE EDQDKIVSSH SLHQFQASST LLQGSPSKAR
STLFLLPDGS GSATSYASLP PISPDGDVAV YGLNCPWLKD ASYLVEFGLK GLTELYVNEI
LRRKPQGPYN LGGWSAGGIC AYEAALILTR AGHQVDRLIL IDSPNPVGLE KLPPRLYDFL
NSQNVFGSDN PHSTAGTSVK APEWLLAHFL AFIDALDAYV AVPWDSGLVG LASPLPAPPQ
TYMLWAEDGV CKDSDSARPE YRDDDPREMR WLLENRTNFG PNGWEALLGG KEGLFMDRIA
EANHFSMLKR GRNAEYVSAF LARALDN
