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Database: UniProt
Entry: G2XV83_BOTF4
LinkDB: G2XV83_BOTF4
Original site: G2XV83_BOTF4 
ID   G2XV83_BOTF4            Unreviewed;      2545 AA.
AC   G2XV83;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=BcPKS11, polyketide synthase {ECO:0000313|EMBL:CCD44403.1};
GN   ORFNames=BofuT4_P059830.1 {ECO:0000313|EMBL:CCD44403.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD44403.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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DR   EMBL; FQ790270; CCD44403.1; -; Genomic_DNA.
DR   STRING; 999810.G2XV83; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_1_1; -.
DR   InParanoid; G2XV83; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR011032; GroES-like_sf.
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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
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   PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 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; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          35..460
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2445..2522
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2545 AA;  277762 MW;  9F59ADEEA66BF43F CRC64;
     MGSLGPTRVT NGNPVNNGSA AVNGDSPTAA HGGHLEPIAV VGMSCRLSGD ASDTQKLWEL
     LIKGRSAWSK VPKDRFNQEA FHDPSAEGKP GRTSTDGGHF LKDDIKAFDA SFFGINPIEA
     TAMDPQQRLL LEIAYEAFEN AGLTLEQLSG SNTGVYVGQW ASDYQEMLLR DIDFPPIYQA
     SGVGAAISSN RISYCFNLHG PSLTLDTGCS ASLVALHQAV HSLRAGETDK CFVAGVNLQL
     DPQRYGYQNK LSMFSKQGKS FTFDHRAKTA SGYGRGEGCS GVVLMPLSQA QKQGFPIRAV
     VQNSVANQDG KTNGITVPSA EAQSAAIEKA YSQVGLVPYA DYVEAHGTGT AVGDPIEARA
     IAKVLGAGRE SDSPLPIGSL KANIGHTESA AGLTGLIKAV LMLEHNMIPP QVNFEKANPE
     IDLDALNLRI PITLESRPLK RISVNSFGYG GTNAHVVVDA AREIATVKPT SQNNGISTTY
     DHHVPEDASR AKERLFVLSA ASEKSCQDMS SKVAKYLESK ADSPDADTLL SRLAYTLSRR
     SVMANRVGVI ASDLNDLIAQ LTSLSTEAIP RADHQTTPRI GFVFSGQGAQ YPRMGQSLLG
     TWPTFTASMK RAAACIKACG SSWDLLEELL KKPAESRMED PRIAQPISTA VQISLVDTLK
     DLGVFPSAVI GHSSGEIAAA YCAEAISFED AMTVAYHRGR LTGDLRKENK GKAGAMIAVG
     ASATTVKQSI DQLGAAVSSR IAIACFNSPE SVTVSGDEDV INSLKQRLDE RDIWNRILRT
     GGAAYHSPQM LQVAEKYHEA LKDLSGGVPV SNISMVSSVT GEDHADKPIT RDYWVHNLVS
     PVRFTDALKK TCVGESGTRK VDLLLELGSH FQLEGPIKQT LRTFTGQPAK IHYAGSLKRG
     ENAQRRLLEM LRSLYLERFP VAFWKANAGF VETAPELLTD LPPYPFDHSK TYWHESRVSK
     AYKHRTFLPH ELLGSLVHDN NPQEPRWRCF LNLKDVPWLS GHIIQGQTIF PATAYLAMVF
     QAARQDTAMR NPQATINRFI LRNVNMSQAL VMENNKPDLE ISLSLRPQAV SARKSSQLWQ
     EFRIFSTSAE DIWTEHCRGL VQVVLKSESA TQDDGIVPTR VTLPPHAHHI QAKQFYHRAR
     DIGVNWSAPF DNLTDIKIAS GSCIADSSFV PGAGASETDY TIHPGVMDAV LYHGMMGVLI
     FDENDKSPVV PTFIEKMIVA EQDRAKPVQE VTCHATRTDN ALTFDIGIFE KQNEENMVLQ
     AWGVVATKLP DVSIGEGRKR DLCHVPDWVT YMPKTTQKHI DDLCKKSLEE RSIIPEIKAL
     EALTVNYVKR ALASTPADEV AEGYQRNWFK WMKTLADQEP DPVFLKAGEE DGSVSAEVAR
     RLGPRLSEIL RGTTHPLDIL NEDNLLSGLY LEGGNARCIA QIAAYMGELG RLNPNMKIIE
     VGAGTGSATL PVLQALQAPN RVLASEYDFT DISPGFFPAA RELLSDFENI MQYKTLNVEK
     TAEENGFEPN SYDVLIASNV LHATPCIDVV LENVRSLLRP GGKLILMEPT ENLPHYGLVF
     GSLAGWWAGV DEGRTLSPML SRSAWIQKLS KNGFVHNEAV FEDYPVADGG SISVFVSEVP
     VPAPSAAPLD VEIVSYSGDG VYSSFTEKLQ KNLWDRSVEA CVASPSVSED KISIIMPDIC
     ERVAWNMDGP LFESIKARVA NSKVIVFVMC TAKGKEQRPS GDWIYGFCRS IRYEYVSVRL
     VSLELESGLD AGVEALSTIL NSPTADMSLP IDEVELEYMD RDGQLYVSRV RSEPNLDSYV
     SRDLGRSVSE EAPFFNDRAM SAELGIPGVL DTLRWADNPE ISGPVDPDCV RLQLSAASIN
     FKDVLVASGQ LEGITQMRND CSGIVLEVGA NMTSKFKPGD RVCSLYSQSF TNYPMVHGLC
     CHVIPQDMDF ADAASIPLVW CTVYYCLITI ARLQKGESIL IHSAAGAVGQ ASIMLARHLG
     AEIFVTCGNE AKVELLNTEF NIPKDHIFSS RTTAFRDKIH AMTKGKGVDV VLNSLGGEMF
     RESCNTLAAH GRFVEIGRKD LMENALMPME FLLNNITFTY VDFAHILATK TWLASQLLGD
     VMKLFASGAV QHVRQIKYSI SEMAAAFRLI QAGKHTGKVV LTVDPEVKVQ VVPSKPTSVQ
     LNPEATYIVV GGLGGLGKRL VDWTTEKGAR HICIFSRTAQ PDSDTQSFLD KLKSMGVKVR
     VEKCDVSSEE SLKKAVAMIQ KTMPPIRGLF QAAMVLHDVL LEDMTVEQWC KVTAPKVQGT
     WNLHKLLPDD MDFFIMLSSV VSMVGTVGAS NYASSCAFQD GIARYRRRLG LPAYAINIGA
     IVEAGYVSEN PDVAVNLRKN GLGSVAISEF LSHLADVIQY KTEYTQSSLG ILPNGTERGL
     GEARWSNDKR LAQIFGSESQ AGSKAVGSGA DNVGFVLQAA TTFHEAQDIV CKAIVKQLAT
     ILAIDASDII PARSLDSYGL DSLVGVELRN WIGAYLQVNL PLLVMWNTSS INELAEIVTK
     GSRLVKVKSE ETEEEKKDVE EAKEE
//
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