PKS1_ZYMTI
ID PKS1_ZYMTI Reviewed; 2175 AA.
AC F9XMW3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Non-reducing polyketide synthase PKS1 {ECO:0000303|PubMed:25360032};
DE EC=2.3.1.- {ECO:0000305|PubMed:25360032};
DE AltName: Full=Conidial pigment biosynthesis cluster 29 protein PKS1 {ECO:0000303|PubMed:28818040};
GN Name=PKS1 {ECO:0000303|PubMed:25360032}; ORFNames=MYCGRDRAFT_96592;
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323;
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=25360032; DOI=10.1534/g3.114.015289;
RA Lendenmann M.H., Croll D., Stewart E.L., McDonald B.A.;
RT "Quantitative trait locus mapping of melanization in the plant pathogenic
RT fungus Zymoseptoria tritici.";
RL G3 (Bethesda) 4:2519-2533(2014).
RN [3]
RP FUNCTION, AND PATHWAY.
RX PubMed=28818040; DOI=10.1186/s12864-017-3969-y;
RA Cairns T., Meyer V.;
RT "In silico prediction and characterization of secondary metabolite
RT biosynthetic gene clusters in the wheat pathogen Zymoseptoria tritici.";
RL BMC Genomics 18:631-631(2017).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster 29
CC that mediates the biosynthesis of mediates the biosynthesis of
CC dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a
CC structural component of the conidial wall (PubMed:25360032,
CC PubMed:28818040). The first step of the pathway is the production of
CC the heptaketide naphtopyrone YWA1 by the polyketide synthase PKS1
CC though condensation of acetyl-CoA with malonyl-CoA (By similarity).
CC {ECO:0000250|UniProtKB:W3X7U2, ECO:0000269|PubMed:25360032,
CC ECO:0000269|PubMed:28818040}.
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:0000250|UniProtKB:W3X7U2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653;
CC Evidence={ECO:0000250|UniProtKB:W3X7U2};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:Q9Y8A5};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:Q9Y8A5};
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000305|PubMed:28818040}.
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. {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}.
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DR EMBL; CM001206; EGP83620.1; -; Genomic_DNA.
DR RefSeq; XP_003848644.1; XM_003848596.1.
DR AlphaFoldDB; F9XMW3; -.
DR SMR; F9XMW3; -.
DR STRING; 1047171.Mycgr3P96592; -.
DR EnsemblFungi; Mycgr3T96592; Mycgr3P96592; Mycgr3G96592.
DR GeneID; 13396530; -.
DR KEGG; ztr:MYCGRDRAFT_96592; -.
DR VEuPathDB; FungiDB:ZTRI_11.184; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR InParanoid; F9XMW3; -.
DR UniPathway; UPA00785; -.
DR PHI-base; PHI:8593; -.
DR Proteomes; UP000008062; Chromosome 11.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0042438; P:melanin biosynthetic process; IMP:PHI-base.
DR Gene3D; 1.10.1200.10; -; 2.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; 2.
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 SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
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; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Melanin biosynthesis; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..2175
FT /note="Non-reducing polyketide synthase PKS1"
FT /id="PRO_0000451090"
FT DOMAIN 1666..1743
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1801..1878
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 5..242
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT),"
FT /evidence="ECO:0000255"
FT REGION 372..804
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 900..1212
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1285..1604
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1640..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1879..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..2158
FT /note="Claisen cyclase domain"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT COMPBIAS 1766..1798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 541
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 988
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2002
FT /note="For Claisen cyclase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1703
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1838
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2175 AA; 235713 MW; FBC387368E22C265 CRC64;
MSNILLFGDQ TAEQYPLLHR IVLRKDNVLL LSFVERCALA LREETRTLSR SQREVMPDFL
TLSNLIEAYY QKGEKVLMLE SAFLTIAQLG HYIGYFSENP SELPAVSDTR VLGLCTGLLA
ASAVVSAKTV EELAIVGVDF VRIAFRSGAV VDNVRSMLGQ SSQDKSTWST IISGPSEVDV
KDALTSFHEA SGIPRSNQAY VSAVSTMALT VSGPPITVER FFQESSLIIN HRVSIPIYGP
YHAGHLFGEA ECERILSGEV GQELRKHMPA SLVHSAATGK PIVSENAYEL AKLALGEIHQ
YPVRWDYLLE ETVAQIGHYP CGAKIFALGA SNIATSLSSA LKAGGQADVM IVDEASFVET
KKYTGRTQTD KIAIVGMAGR FPNSANHEAL WDLLMKGLDV HRKVPADRFD ADAHCDPSGK
GKNKSHTPFG CFIDEPGLFD PRFFNMSPRE AAQTDPMGRL ALVTAYEALE MSGYVPNRST
STKLNRIGTF YGQTSDDWRE INAAENVDTY YITGGVRAFA PGRINYYFKF SGPSYSIDTA
CSSSLAAIQL ACTSLWAGDC DTACAGGLNV LTNPDIFSGL SKGQFLSKTG GCKTYDNDAD
GYCRGDACGT VILKRYQDAV ADKDNILGCI LGAATNHSAE AVSITHPHAG AQEFLYKQVL
ANAGIDAHEI SYVEMHGTGT QAGDGIEMTS VTNVFAPRRR QRKPEQTVHL GAIKANVGHA
EAASGINSLV KVLMMMKNNK IPANVGVKGE LNKTFPADLK DRNVHISLKQ VDWPRKTEAP
RKVFLNNFSA AGGNTALLIE DGPVHKMPNG VDPRSTLPIT VTARSIGSLK RNLMNLQKYV
AENGSTTLPS FSYTLTARRI QHNYRVAFPL ADISKVADAL EAQAKDSYSP VPMVTTKTAF
CFTGQGSQYT GLGQKLYQDL KSFRDDIDQL DQMARIQGLP SFLELLDGTD VQTLSPVKVQ
LGMACIQVAL SRMWASWGVT PTAVIGHSLG EYAALHVAGV ISASDMVLLV GRRAELLVRE
CTPHTHGMLA VKGGVEAIRN ALGINMTEIA CINGPEETVL CGSSDVVAAA NDTLGKNGFK
ATKLNVPFAF HSAQVDPILD EFRKVASSVT FNKPSVPILS PLVGIVIRDG GIITADYLAR
HARETVNFSS ALLSGQKEAV FDEKTAWLEV GAHPVCSGMV KASIGTTITA PSLRRGEDAW
KTISTSICHL FTAGVNFNFD EFHREFNDAQ ELLTLPTYSF DNKKYWLDYH NNWTLTKGEV
QKTKEVIVEK EIVAPVIEVP AKRLSTSCQN VISEEFDGNR ATVVIRSNLA DSKLYPVVCG
HMVNNAALCP SSLYADMALT VGDYIYKELQ PGVETPGMNV CNMEVPKPFI ANIPQPAEGQ
HLEMEATADL DLGTVSLKFR SVHPDGKKIQ DHAFCTIRYE DKAVWASEWT RYNYMVKAQI
DMLTARTMTG GAHKVQRGMA YKLFKALVNY DDKYRAMAEV VLDGANTEAS AAIDFPTKPD
DGDFYCPPYH IDGACHISGF IVNASDLLDS EQNVYVSHGW GAMKFSRPLV AGMKLRNYVR
MVPQPNNISK GDVYIMEGDE IVAVCEGIKF QQIPRKVLNV FLPPNKGSAV QAKPSPIAQR
PAPVRASVAA PVKRMLAPAP VRKSAGPAKA AAAPSMPKPS KVAAKKPAGS MVDKVLTILS
KETEVDVAEL VDDAHFENLG VDSLLSLTIS AIFREDLSME ISPSLFTDYP TVGEMKKYFS
QFNNVESTTE SEDDSDTDSL ATTDVATPFD EMSTPASSAP SVPQSDAGKP SPDSPTGDSL
SDDVGDVSIA RHIIAQEMGV DISEVTDDAE LAEMGMDSLM SLTILGELRE KTGIDLPGTF
LMTNPTLVDI ENALGMRPKP KAVGPKLSKP STKTDMNEVS SRLTAINKTD ISQYPSATSV
LLQGNPKTAT KKVFFLPDGS GSATSYVSIP NIGPHVAAFG LNCPFMKDPE QWQCGIEVSS
LIYLAEIRRR QPKGPYIIGG WSAGGVIAYA VAQALLAAGE KVEKLLLLDS PCPVNLAPLP
TRLHVFFNEI GLLGTGDPAK TPKWLLPHFS AAIRSLSAYD PKPTIAELPT YAVWCKDGVA
GNPGDPRPPP AEEEDPAPMK WLLNHRTDFS DNGWAQLCGQ NMKFGVMGGH HFSMMKDPHA
SELGQLIKEG IEWKA
