ID   Q6TLJ8_9PSED            Unreviewed;      1739 AA.
AC   Q6TLJ8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Polyketide synthase type I {ECO:0000313|EMBL:AAQ90174.1};
GN   Name=pltC {ECO:0000313|EMBL:AAQ90174.1};
OS   Pseudomonas sp. M18.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=228095 {ECO:0000313|EMBL:AAQ90174.1};
RN   [1] {ECO:0000313|EMBL:AAQ90174.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M18 {ECO:0000313|EMBL:AAQ90174.1};
RX   PubMed=15033239; DOI=10.1016/S0378-1097(04)00074-6;
RA   Huang X., Zhu D., Ge Y., Hu H., Zhang X., Xu Y.;
RT   "Identification and characterization of pltZ, a gene involved in the
RT   repression of pyoluteorin biosynthesis in Pseudomonas sp. M18.";
RL   FEMS Microbiol. Lett. 232:197-202(2004).
RN   [2] {ECO:0000313|EMBL:AAQ90174.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M18 {ECO:0000313|EMBL:AAQ90174.1};
RX   PubMed=16581203; DOI=10.1016/j.gene.2006.02.009;
RA   Huang X., Yan A., Zhang X., Xu Y.;
RT   "Identification and characterization of a putative ABC transporter PltHIJKN
RT   required for pyoluteorin production in Pseudomonas sp. M18.";
RL   Gene 376:68-78(2006).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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DR   EMBL; AY394844; AAQ90174.1; -; Genomic_DNA.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd05274; KR_FAS_SDR_x; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
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; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-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; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          39..465
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          467..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1739 AA;  187251 MW;  9F42F4C9128FB1B2 CRC64;
     MENETSDVSK QQLEASLAQA IGTIRSLKEK LAGRTHSGAG PIAVVGLGCR LPGGADSPRR
     LWSLLKNATD ATGDMPAERR YATDYYDPDP DVPGKAYVMR GGFVEGVERF DAAFFGISPS
     EAEGMDPQQR IALEVAWEAL EHAAIDPFSL DGSKLGVFMG ASTNDYVRLR QQLGEVADVN
     AHQFYGETSF IAGRIAYTLG GQGPAMMIDT SCSSSLVALH QACQSLRSGE SDLALAGGVN
     LILSPYGFVL VSKLRAVASD GRCKTFDAAA DGYGRGEGCV VLVLKRLADA ERDRDPVLGV
     IQGSALNNDG SSSGITVPNI HAQQAVIAAA LRNAGAQASQ VDYIEAHGTG TPLGDPIELR
     ALDAVLGAQR PADRPLLVGS IKANIGHLEP VAGAAGLAKI LLALQHDELP GQVNFHTPNP
     RVEWRRMALR VVREATPWPR HQGQRLAGVS SFGVTGTNAH VLVGDATPRA RGTGRGNPWQ
     LFTASGRGET PRRQMCGRYE RYVAEHPQVP LEDLCYTVNA GRAHFEHRFA CVADDRERLR
     EQLAAYASRK LVGDTFEGVC RPGVPPASAW LFPGQGCQYP GMARTLYDSE LPFREALDEC
     LVALRGMGVE LSCALFESTP EAEALLAQTR YAQPAIFAVE YALARLWMAW GVLPGALFGH
     SFGEIGAACI AGALTLEDAL RMVEARGRLA QELMTAGGVM HAVNLGEAEL LGLLREQGLA
     GIELAAVNSP EDLVVAGPEA DVEVLLEKLA AMQVRTRKLA VSHAFHSAAA EPMLERFREV
     VREIRFSEPR IPLVSGVSGR LHTLESLSSA DYWCAHSRDS VRFSDGVRTL LEQGTELFLE
     VAPEAVLTPL VLRHQVDRSL LVVPSMRRGG DAAREIRLAA AQLYTGGVDL DWQRLHAHDG
     ALRQALPGYA FQRERYWFTP ARAQAGGRSQ IGGVGRLLGQ PINAPFPVFE ATLDADAMLA
     LGATASEELV RLEPGRLLSL LLEDVLDHLG LDDFELSLER LGEGLAIHPG DRLYLYTELE
     ALPEKCWSVT CSLRSEAECQ AGLGWREAVL AMVHALPASS ALSPLDGEGR SVELGGAASG
     CLFARLLDGK PASALESIRR MRGRRALLNQ TWRSLLMPAE DGVGFDCNLY DAGQELLGTL
     EGMSLGMALE DARLVERIAQ PDVLYRLDWP SRPRQPGNPC LGERGFAVLS SDIEAARQLA
     ALMQARGLRA QPFQPGQLQE ALDSVAPCDI VFLDERARGA GPTLDSLDTL RSRVLHPLLA
     LIQAILPLGD EAVGRLWLVT FGAQAAGLAS GVPVNVAGAP LWGLGKSMAL EHPEHWGGLV
     DLAPDDPDWC ANLLDELLLN DGENQVCLRR DGRRGHRLER DTGTGWPNSV FAPSKDGCYL
     ISGGMGGIGL GMADWLLAHG AGQVVITGRS PARAQGEKLA RFGAAVSRVR YVQADIASKA
     EMSALFEELS AMPGGLRGIF HAAGISIPQD LRDADRDSFD RVLRPKVDGA WLLHELSLGL
     ELEFFAMCST IACVWGSQHI ASYAAANQFL DGLAAYRHAL GLPALVVDWG LWAGGSHLFD
     EEVLGFLKSV GLKPLAPAQG IGLLARLLGS DVGHQVIAGV DWARFKALLE SRGAQPLLEH
     IEVEDTPTRP GDVAADQGLL RKLSAVEGRE RFQLVDDYVW GQYANLLGVK VEQVRAKLED
     GGSLMDYGLD SLLVMEMVAR CRRDLKVQIK AREFLECPGL MWPDFLARSI EQQGVLYAV
//