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Non-reducing polyketide synthase ZEA1 (EC 2.3.1.-) (Macrolactone megasynthetase) (Polyketide synthase 13) (PKS13) (Zearalenone biosynthesis polyketide synthase 1)

 ZEA1_GIBZE              Reviewed;        2038 AA.
A0A098D6U0; A0A0E0RTV4; I1RFC4; Q2VLJ3;
18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
07-JAN-2015, sequence version 1.
25-OCT-2017, entry version 25.
RecName: Full=Non-reducing polyketide synthase ZEA1 {ECO:0000305};
EC=2.3.1.- {ECO:0000269|PubMed:18427109};
AltName: Full=Macrolactone megasynthetase {ECO:0000303|PubMed:18427109};
AltName: Full=Polyketide synthase 13 {ECO:0000303|PubMed:16262793};
Short=PKS13 {ECO:0000303|PubMed:16262793};
AltName: Full=Zearalenone biosynthesis polyketide synthase 1 {ECO:0000303|PubMed:16517624};
Name=ZEA1 {ECO:0000303|PubMed:16517624};
Synonyms=PKS13 {ECO:0000303|PubMed:16262793};
ORFNames=FGRAMPH1_01T05749, FGSG_02395;
Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084)
(Wheat head blight fungus) (Fusarium graminearum).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
Fusarium.
NCBI_TaxID=229533;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
INDUCTION, AND PATHWAY.
STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
PubMed=16262793; DOI=10.1111/j.1365-2958.2005.04884.x;
Kim Y.T., Lee Y.R., Jin J., Han K.H., Kim H., Kim J.C., Lee T.,
Yun S.H., Lee Y.W.;
"Two different polyketide synthase genes are required for synthesis of
zearalenone in Gibberella zeae.";
Mol. Microbiol. 58:1102-1113(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
PubMed=17823352; DOI=10.1126/science.1143708;
Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
"The Fusarium graminearum genome reveals a link between localized
polymorphism and pathogen specialization.";
Science 317:1400-1402(2007).
[3]
GENOME REANNOTATION.
STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
PubMed=20237561; DOI=10.1038/nature08850;
Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J.,
Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M.,
Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C.,
Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A.,
Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M.,
Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S.,
Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K.,
Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M.,
Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y.,
Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S.,
Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O.,
Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C.,
Rep M.;
"Comparative genomics reveals mobile pathogenicity chromosomes in
Fusarium.";
Nature 464:367-373(2010).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084;
PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
Hammond-Kosack K.E.;
"The completed genome sequence of the pathogenic ascomycete fungus
Fusarium graminearum.";
BMC Genomics 16:544-544(2015).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16517624; DOI=10.1128/AEM.72.3.1793-1799.2006;
Gaffoor I., Trail F.;
"Characterization of two polyketide synthase genes involved in
zearalenone biosynthesis in Gibberella zeae.";
Appl. Environ. Microbiol. 72:1793-1799(2006).
[6]
FUNCTION.
PubMed=16751498; DOI=10.1128/AEM.00963-05;
Lysoee E., Klemsdal S.S., Bone K.R., Frandsen R.J., Johansen T.,
Thrane U., Giese H.;
"The PKS4 gene of Fusarium graminearum is essential for zearalenone
production.";
Appl. Environ. Microbiol. 72:3924-3932(2006).
[7]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18427109; DOI=10.1073/pnas.0800657105;
Zhou H., Zhan J., Watanabe K., Xie X., Tang Y.;
"A polyketide macrolactone synthase from the filamentous fungus
Gibberella zeae.";
Proc. Natl. Acad. Sci. U.S.A. 105:6249-6254(2008).
-!- FUNCTION: Non-reducing polyketide synthase; part of the gene
cluster that mediates the biosynthesis of zearalenone (ZEA), a
nonsteroid estrogen that is a contaminant of cereal grains and
causes estrogenic disorders in humans and animals
(PubMed:16262793, PubMed:16517624, PubMed:18427109). The ZEA
backbone is synthesized from a single acetyl-CoA molecule and
eight malonyl-CoA molecules (PubMed:16262793, PubMed:16517624,
PubMed:18427109). The reducing polyketide synthase ZEA2 is
proposed to synthesize a reduced hexaketide intermediate by using
different combinations of its reductive domains during each round
of condensation (PubMed:16262793, PubMed:16517624,
PubMed:16751498, PubMed:18427109). The hexaketide thioester is
then transacylated to the non-reducing polyketide synthase ZEA1
and is further condensed with three malonyl-CoAs without reductive
tailoring to yield a mixed reduced/unreduced nonaketide
(PubMed:16262793, PubMed:16517624, PubMed:18427109). ZEA1 must be
able to interact with ZEA2 to facilitate starter-unit acyltransfer
and initiate polyketide biosynthesis (PubMed:18427109). ZEA1 also
mediates the required C2-C7 cyclization to form the resorcylate
core and catalyzes the formation of the macrolactone
(PubMed:18427109). ZEA1 exhibits broad starter-unit specificities
toward fatty acyl-CoAs ranging in sizes between C6 and C16 and
displays the highest activity toward decanoyl-CoA
(PubMed:18427109). ZEB1 is then responsible for the chemical
conversion of beta-zearalenonol (beta-ZOL) to ZEA in the
biosynthetic pathway (PubMed:16262793).
{ECO:0000269|PubMed:16262793, ECO:0000269|PubMed:16751498,
ECO:0000269|PubMed:17823352, ECO:0000269|PubMed:18427109}.
-!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:16262793}.
-!- INDUCTION: Expression is positively regulated by the zearalenone
biosynthesis specific transcription factor ZEB2 (PubMed:16262793).
Conditions for carbon-, nitrogen-, or phosphorus-starvations lead
to very low expression (PubMed:16262793). Increase in pH results
in gradual reduction of the gene expression (PubMed:16262793).
{ECO:0000269|PubMed:16262793}.
-!- DOMAIN: Multidomain protein; including a starter unit:ACP
transacylase (SAT) that selects the starter unit; a ketosynthase
(KS) that catalyzes repeated decarboxylative condensation to
elongate the polyketide backbone; a malonyl-CoA:ACP transacylase
(MAT) that selects and transfers the extender unit malonyl-CoA; a
product template (PT) domain that controls the immediate
cyclization regioselectivity of the reactive polyketide backbone;
and an acyl-carrier protein (ACP) that serves as the tether of the
growing and completed polyketide via its phosphopantetheinyl arm
(By similarity). {ECO:0000250|UniProtKB:Q5B0D0}.
-!- DOMAIN: The release of the polyketide chain from the non-reducing
polyketide synthase is mediated by the thioesterase (TE) domain
localized at the C-ter of the protein (By similarity).
{ECO:0000250|UniProtKB:Q5ATJ7}.
-!- DISRUPTION PHENOTYPE: Results in the loss of zearalenone
production but still produces beta-zearalenonol (PubMed:16262793,
PubMed:16517624). {ECO:0000269|PubMed:16262793,
ECO:0000269|PubMed:16517624}.
-!- SEQUENCE CAUTION:
Sequence=ABB90282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=ESU07824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; DQ019316; ABB90282.1; ALT_SEQ; Genomic_DNA.
EMBL; DS231663; ESU07824.1; ALT_SEQ; Genomic_DNA.
EMBL; HG970332; CEF74679.1; -; Genomic_DNA.
RefSeq; XP_011318309.1; XM_011320007.1.
SMR; A0A098D6U0; -.
STRING; 229533.XP_382571.1; -.
ESTHER; gibze-q2vlj3; Thioesterase.
EnsemblFungi; CEF74679; CEF74679; FGRAMPH1_01T05749.
GeneID; 23549774; -.
KEGG; fgr:FGSG_02395; -.
eggNOG; KOG1202; Eukaryota.
eggNOG; COG3321; LUCA.
InParanoid; I1RFC4; -.
OrthoDB; EOG092C0220; -.
Proteomes; UP000070720; Chromosome 1.
GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.40.47.10; -; 2.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020807; PKS_dehydratase.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR006162; Ppantetheine_attach_site.
InterPro; IPR030918; PT_fungal_PKS.
InterPro; IPR032088; SAT.
InterPro; IPR001031; Thioesterase.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
Pfam; PF16073; SAT; 1.
Pfam; PF00975; Thioesterase; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53474; SSF53474; 2.
SUPFAM; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
1: Evidence at protein level;
Complete proteome; Multifunctional enzyme; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 2038 Non-reducing polyketide synthase ZEA1.
/FTId=PRO_0000438784.
DOMAIN 1616 1693 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258,
ECO:0000305|PubMed:18427109}.
REGION 9 246 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255,
ECO:0000305|PubMed:18427109}.
REGION 367 797 Ketosynthase (KS) domain. {ECO:0000255,
ECO:0000305|PubMed:18427109}.
REGION 888 1172 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255,
ECO:0000305|PubMed:18427109}.
REGION 1221 1572 Product template (PT) domain.
{ECO:0000255,
ECO:0000305|PubMed:18427109}.
REGION 1778 1882 Thioesterase (TE) domain. {ECO:0000255,
ECO:0000305|PubMed:18427109}.
COMPBIAS 419 422 Poly-Thr. {ECO:0000255}.
ACT_SITE 537 537 For beta-ketoacyl synthase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 979 979 For acyl/malonyl transferase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 2021 2021 For thioesterase activity.
{ECO:0000250|UniProtKB:Q5ATJ7}.
MOD_RES 1653 1653 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 2038 AA; 222411 MW; 843ED0E45BFFCEA9 CRC64;
MAPNKKTILL FGDQTDSWVD GIDRLYQDAA SIPWLQSFLD DLTHTFKTHT VGMDAVLRNS
LGDFANLQEL AEKYRYTTDD VGMAQAFLIY AVRAGILLKW AKYEPSLLST DENQPEWVGI
SGGLISLSVL AVAETFEKLY EACLEVAGLL ARLCRFTSVK SRSMEDRSGA WGWTVLGIGA
NELRNALDQY QQSMGIPPIK RAQVAVTGHR WNTIVGPPSI LQLIVKECPA IRSLPKNELN
IHALQHTVVT SRADLDYIVG DSTLLSQPLS LTFTLWGMDD PRAHYTTWGD MLRAICSQAL
SRPLDITHVV DQLSSKLRSF PQLDVKSIGP CSHLSYLTNV LKSAGRTVSV ADDHPPSTPP
KQLPGRIAIV GMAGRGPGSD NVEEFWNVIM SKLDLCEEIP EDRFNLSEFY RSKHDSGCTT
TTKFGCFMDK PGHFDNRFFH ISPREALLMD PGHRQFLMTT YEALEMAGYS DGATRAVDPA
RIATFFGQCN DDWHDVSHHT LGCDAYTLQG VQRAFGAGRI AFQFKWEGPT YSLDSACAST
ASSIHLACTS LLAKETDMAV AGAANVVGYP HSWTSLSKSG VLSDTGNCKT FRDDADGYCR
ADFVGTVVLK RLEDAIAHND NILAVVAASG RNHSGNSSSI TTSDAKAQEK LYRKMMHNAR
VSPNDISYVE MHGTGTKVGD PAEMGALASL FSHRRTPKPV VVGGVKANVG HSESKQAAGV
ASLLKCIMMF QKNILPPQAG MPHALNPNFP PLSEINIEIP SEPSTFESPV SQPRRILLNN
FDAAGGNACI LLEDFGNNMV KKSDPRVHHT VVTSSRTQAS YHGNKAKLLQ WLRQNPGARI
EDVAYTTTAR RTHHPIRFAV TASSTQELIS KLEADTADSP AAKESPVVFV FTGQGSHYAG
MGSELYETSP VFRETVNLCA TICEEQNFPP FLDLITQSDS EMSDKTTLEV QLAVLTLEIG
LAALWRSIGI QPSVVIGHSL GEYAALHVSG VLSLADVLYL VGQRALLILQ RCEVNTSAML
SVAMPVTDTH AFLEAQADPS CEIACVNSTN ASVISGSIEN ITELQAGLKA RSKMLSVPYG
FHSSQMDPIL ADYAALAGGV TFSEPKIPVA STLLASLVDT SGTFHAGYMA RQCRQPVNFV
GALEAIQSNY SDPIWLEIGP SQVCSSFVRA TLSPPPSKIL STLDKGTNAW LSLGKCMSSL
YKHGATIDWL ALHQPYVDNL SLLNLPTYAW DLKEFWIRYT ETKDQLPTST TNGHETFKAN
ISTCAQQVVE HISPPNMKVT FRASLSDPGF KALIDGHRLR DRSVCPGSVF SEAGLAAVTY
VLQLHHSKSL KLPALVLRNL SLKRPLTYDL VGPDGELITV VAPGGSSNDT FKVAWKASKG
NVSYSLGDCM VAACDGQLIQ ARWDKVSYFI RSRVDEIVAS SKSGISHRLQ PQILYGLFAN
TVKYDAAFKC IQEAYISSDF QEAAAVIVLN SDPVGTKFVA SPYWGESLVH LAGFVVNSNP
SRQSHDTTFM MDGFESFEQT VIPEPGKPYH TYVRVTGNES ASVVCDVYIF DDDKLIMHCA
GLHFHEVENA VLDQLLGGTN TSNTTRDQPA PIMSRKEVPK PVDTTEKVEA VSNDSQSDAH
VLDSILKIIS KETGSDLADF QDDTLIADLG VDSIMAIEIA SQVTEETGMD LLPSFIIDYP
AIGDLRRVFA PKSTHISLDN DLSRPSLVDD TSQALQSSGS ESFDQPPTSV TSTSDSGSIV
KIDLGPDVDS PAPKIKITLL QGRPGNGRTP FYLIADGTGT IATYIHLPQF KSQIPIYGID
SPFLRCPTRF TTDVGITGAA RFITEALMKA QPEGTFVLGG FSGGAMLAYE VCRQLAAANR
KVDSLMLIDM CSPRSKTVED KNDIGWAIFE SISRQNGLWR STDMTRQHLQ AIFAAVATYH
PQPLKASERP KRTAIIWAEK GMIDRCAGDS ELMQKLAKRG IPTEPYPKFM EDSELGPVAW
GLPHKTKNDL GPNGWERYVG DALCLSMPAD HLEMPMPGHV HLLHEKMTRA FEFFNEAG


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