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FUJ1_GIBF5
ID   FUJ1_GIBF5              Reviewed;        2492 AA.
AC   S0EET5;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Polyketide synthase 19 {ECO:0000303|PubMed:23825955};
DE            Short=PKS19 {ECO:0000303|PubMed:23825955};
DE            EC=2.3.1.- {ECO:0000269|PubMed:26192387};
DE   AltName: Full=Fujikurins biosynthesis cluster protein PKS19 {ECO:0000303|PubMed:26192387};
GN   Name=PKS19 {ECO:0000303|PubMed:23825955}; ORFNames=FFUJ_12239;
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, FUNCTION,
RP   AND INDUCTION.
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
RN   [2]
RP   FUNCTION.
RX   PubMed=26192387; DOI=10.1021/np5008137;
RA   von Bargen K.W., Niehaus E.M., Krug I., Bergander K., Wuerthwein E.U.,
RA   Tudzynski B., Humpf H.U.;
RT   "Isolation and structure elucidation of fujikurins A-D: products of the
RT   PKS19 gene cluster in Fusarium fujikuroi.";
RL   J. Nat. Prod. 78:1809-1815(2015).
CC   -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of fujikurins A-D, secondary metabolites
CC       playing a role during rice infection (PubMed:23825955,
CC       PubMed:26192387). The polyketide synthase PKS19 acts with the trans-
CC       enoyl reductase FFUJ_12240 and the polyketide transferase FFUJ_12241 to
CC       produce fujikurins, however, the biosynthesis pathway has not been
CC       identified yet (PubMed:23825955, PubMed:26192387).
CC       {ECO:0000269|PubMed:23825955, ECO:0000269|PubMed:26192387}.
CC   -!- INDUCTION: The fujikurins gene cluster is specifically expressed during
CC       rice infection (PubMed:23825955). {ECO:0000269|PubMed:23825955}.
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DR   EMBL; HF679030; CCT72377.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EET5; -.
DR   SMR; S0EET5; -.
DR   STRING; 5127.CCT72377; -.
DR   EnsemblFungi; CCT72377; CCT72377; FFUJ_12239.
DR   VEuPathDB; FungiDB:FFUJ_12239; -.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   Proteomes; UP000016800; Chromosome 8.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 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; IPR013217; Methyltransf_12.
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; 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; 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; PF08242; Methyltransf_12; 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; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..2492
FT                   /note="Polyketide synthase 19"
FT                   /id="PRO_0000442008"
FT   DOMAIN          2404..2479
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          15..466
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          571..866
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          967..1270
FT                   /note="Dehydrogenase (DH) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1431..1604
FT                   /note="C-methyltransferase (CMeT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          2118..2293
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2438
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2492 AA;  272819 MW;  FE92F5EC321772ED CRC64;
     MGSQISEKYY AREPIAIVGT SCRFPGGASS PSKLWELLDN PRDVVQKIPP RRFSTEAFYN
     ADSQHHGVSP SDLIKGLRLT LQWSTNVKHA YLLDDDPRGF DRDFFAINPK EAEAMDPQQR
     ILLETVYESV ESAGYSIEQL RGSSTAVFVG CMSFDYQFAA IRGIDSTLPQ YHATGAAMSI
     LANRVSYFYD WKGPSVAIDT ACSSSLVALH QAVSALRSGD AKLAVAAGSN LILGPEPFIS
     ESKLNMLSPN GRSYMWDASA DGYTRGEGFS VLLLKTLTKA LADSDHIECV IRETGVNSDG
     KTPGITMPSS NAQAQLIRDT YAKCGLDPNR ESDRPQFFEA HGTGTQAGDP IEARAIQEVF
     FPDHTQPTDS KLLVGSVKTV IGHTEGTAGL AGVLKATLAI QHSQIPANLH FNELNPKIRP
     YYDNLRIPTE TTPWPTLSPG APRRVSVNSF GFGGTNAHAI VESWDGPYVR ERSPAPNAIG
     AGPFVLSANS SQALAANAGA LAEYLKEHPT TNLGQLGYTL FKRTNLPFRA AFSGSSVECL
     VEKLQAGKES LKSNSRITTL PESLPPRVLG VFTGQGAQWA KMGEGLYQTS MVFRNSVEQM
     QHSLDSLPES DRPNWTLAEQ LHAPKETSRV GQATVSQPLC TAIQVALVDV LHVVGVELSA
     VVGHSSGEIG AAYAAGYLSA GDAIRIAYYR GFHSHLAQGP GGKRGSMMAV GLSYDQALSF
     CNELSGGITV AASNSYTSCT LAGDAEVIEE AKSRLEENGT FARVLAVDTA YHSHHMKPCA
     TPYLESLKQC DIQVQKPKKG CAWYSSVWGS DGSSRSFNTE GELLQGQYWI ENLTHPVLFS
     QALARALNED QCFDCALEVG PHPALKGPSL EIIKTLTGVS LPYSGVLKRG EGAAEAFADA
     LGLLWKSFPS SRPTITFNGI CRAFSAVKPS SMTILKNLPN YSWDHATLFW KESRASRNFR
     TPKHAPHELL GRSVSHGEHS RREVHWRQVM RLRELPWLRG HKIQGEILFP ASGYLSMAYE
     AAIRLVDEQQ SVRIVEMQDM DIVRAMRLED DTSGLEVLFT IHVTSQSQSC INANVACYSG
     AVDAPQPLDA HQTELTAHFN GRIRLWLEQP SAYTLPLRSE PLLPMSELNM AQVYSSLSKE
     GFDYSGDFQA KSMLRRLGHT VVTLSSPSPV SWTHTLTHPA PIDTAVQGLL TAFSFPGDGR
     IGTTYLPTRI ESVRISTAPS ESDAPILKAD SVVTLTDVTT ITGDVDIFDA ASCHTQVQMR
     GVQMTAIGKP PDRWLYAGKI WARDIAYGLE PGSGTQFSDD DRLLYEQLVR TAYFYLRQLR
     SKIRPPELML MGKFRRHMMR WVTEHLFPQI ESGQHPDIRT EWKDDTLDTV QRWRNSRPAD
     NNDMNLLHAM GQSLIPIVRG TVPPLKVLVQ DGMLDRLYFE GIGFRDGNVD LGAIVKQLGH
     EHPRMRIVEV GAGTGGTTRT VLDALETRYA AYTYTDISTG FFENARSVFS QHASKLTFKT
     LNIENDPVDQ GFTEGSFDML IASNCLHATH SLENTLRQCR KLLRPGGRLV LLEITRDFLP
     IQMIMATLPG WFLGMDEGRL WAPTVTLDRW DEILKTTGFS GVDISSTPSY CSVIVSQAVD
     ETVSVLRNPL ASPDGVPSLS EIVIIGGVGS GLAPQIQSLL TSTIPVETRI ASSLEDVEVN
     RGSTVLCLGD LDSPSFCNMD QTRFEGLQKV FQAANAVLWV TSGATSGTNP EANITVGMGS
     TLMAERGDLK LQFLDVDDPT TIDPSMLARM LLRLAILDQS KSDETLWTIE PELTLKNGAL
     YIPRVQPLDV INRQSTARYR QVIEDIDLNS ASPVVDLVKY QDSWKLQSSP IDSTRVNGIE
     VRVTASSLHT LSCEGGKPEY IFMGRELLSG DNIIGLSASN SSIANITDDQ VLHRWQDSQT
     GAINVAQLSD LLAKALAENL LRNTTGPVWI HGAPSNLSEA IGEVTKEEGL DVFQTTSDLA
     QVAAFNFIHP YATRQDIQDK QPSGLRNFVD LEHSELRNEA LHTSVAASLP VSAISHRCMM
     DLTHGINRSY LAKLAARCLT EDRKSSEDHS QVILIDRIAS ESSKDLGPTT VIDWHAANTV
     TALVRPLEHR DLFFPSKSYL LFGMTGDLGI SVCKWMVDNG ARNVVLASRN PNVPSSVLNF
     MSRKSATVRA LSVDITDMES LCTAREDIES TMPPIGGVMN AAMVLRDRLF HDLTWEDFAA
     VLGPKVQGTQ NINNAFGQKE SALDFFVCFS SATSIIGTVG QSAYAAANHF MVSLVQQRKR
     RGLAGSIVHI SVLTGLGYIF RRGSEHTAVI DKALLPRLER QAETDLHEML AEAIVCGRPG
     SSQPPELITG IKAVFQGEWR DDPRLLGYLG QQQLGNDSAK DQAAGMVSVE TQLDAADDPA
     ECLPILEKRF AQALGNMLEI DPEKVDGSMP VASLGIDSLV AIRIREWFMK ELGVEVPVLK
     IMSVGHSLSR VCDDVLVDWR RVKKEGELED KK
 
 
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