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Database: UniProt
Entry: A0A0K1EF47_CHOCO
LinkDB: A0A0K1EF47_CHOCO
Original site: A0A0K1EF47_CHOCO 
ID   A0A0K1EF47_CHOCO        Unreviewed;      1810 AA.
AC   A0A0K1EF47;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AKT39491.1};
GN   ORFNames=CMC5_036380 {ECO:0000313|EMBL:AKT39491.1};
OS   Chondromyces crocatus.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC   Chondromyces.
OX   NCBI_TaxID=52 {ECO:0000313|EMBL:AKT39491.1, ECO:0000313|Proteomes:UP000067626};
RN   [1] {ECO:0000313|EMBL:AKT39491.1, ECO:0000313|Proteomes:UP000067626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cm c5 {ECO:0000313|EMBL:AKT39491.1,
RC   ECO:0000313|Proteomes:UP000067626};
RA   Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT   "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT   high potential for natural compound synthesis and the genetic basis for the
RT   loss of fruiting body formation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012159; AKT39491.1; -; Genomic_DNA.
DR   RefSeq; WP_050431565.1; NZ_CP012159.1.
DR   STRING; 52.CMC5_036380; -.
DR   KEGG; ccro:CMC5_036380; -.
DR   PATRIC; fig|52.7.peg.4011; -.
DR   OrthoDB; 7617297at2; -.
DR   Proteomes; UP000067626; Chromosome.
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   CDD; cd08953; KR_2_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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; 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; IPR049490; C883_1060-like_KR_N.
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; 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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
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; PF21394; Beta-ketacyl_N; 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   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..439
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1450..1525
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1353..1382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1415..1447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1810 AA;  196428 MW;  015F9AB55C7B298F CRC64;
     MDPLEQPVPE DHIAIIGMAC NFPGARNAEA YWQNIRDGVE SIVPLSEQDL AAAGVPPEIA
     SDPSYVRARA VLDGVEWFDA AFFSMTPREA EILDPQHRIF LECTWEALEH AGYNPDGFNG
     SIGVYGGGSG HNTYFLSNLY PNHDLMRAME YQILLANDKD FLTTRTSYKL NLRGPSVTVQ
     TGCSTSLVAV HMACQALLTY QCDMALAGGV AINVPTRSGY LYRHGMILSP DGRCRAFDAE
     AQGTVVGNGA GVVVLRRLED ALDSGDHILA VIRGSAVNND GAAKIGFTAP GVEGQAQVIA
     QALAMAETNP ETISYVEAHG TGTRLGDPIE IAALTRAFRA RSEGRRNGWC AIGSVKTNIG
     HLDVAAGIAG LIKVIQALRN REIPPSLHYK RANPEIDFAS SPFKVSTELR AWESTGNPRR
     AGVSSFGIGG TNAHVVVEEA PHAAAAPGGR PWQLLLLSAR TRTALDSVSE NLVGYLRKWP
     DVSLPDVTFT LQVGRKAFPH RRMLICKDAE EAATLLSTLG DRRVLTQLEE SIDRPVVFMF
     SGQGTQYVGM AQELYEREPT FRAGIDLCAA MLQPELGLDL RDVLYPQPSR EAWAAEMLKQ
     TRLAQPALFV IEYALATLWM EWGLKPAAMI GHSLGEYVAA CIAGVFSLSD ALTLVAKRGH
     LMQEMPVGAM LSVPLPEADL KPFLGNLSLA AVNSPSACVV AGPIEEVRAL EDRLLVECDV
     ECQWLQTSHA FHSAMMEPVL EPFLAVLRRI PRLAPKIPIV SNVTGSWLSS GEAQSAEYWA
     RHLREPVRFL DGLGEVLVDP ARALLEIGPG RVLSTLARQH PSRGSGRVVL SSIRQPQHPQ
     SDVGFLLETL GQLWLSGIRI DWAGFHTHEP RRRVPLPTYP FERNRYWIEA PQPLSGAVRP
     PARPAPAMPG LLQLPAWKRS VLSGSVKRSA QPRDGRCCLL YADSHGLGAR MEMRLRRDGY
     EVILVRPGES FAAEGATAFT VDPTSASDHA SLLGALRRAG RVPSMILFLW GVTTPTRAPL
     DAARAEAAQV FGFHSLMALA QALGEVGARE EVRLGVVTSY MHKVTEGAAL CPEKTTVLGP
     CRALSREYGN VSCISIDVDL PEPRTLQEGR LIDQILAEVS LERTESIIAY RNGERWIRTY
     EPARMDRPDG LPSRIREGGV YLIIGGLGFL GSTFAEHLAR VARARLILTG RTVLPPRAMW
     EELASSEEEA SAQLRRKIRT VLQLERLGVE VVCMSADVTR IDDMREVVGR AVDHFGRIDG
     VIHAAGSTRT GSIQGTSREE AEAVLAPKLV GAVVVDDALR GLRPDFILLC ASRQAVLGGA
     RLASQSAAST FLGAFAQRQA AVGGPLTIAV EWDPWQRSES SDDRTPGDGV ESGHGVSSSA
     GHVLSREEVL DAWMRILTNP TPQVVVAKRE EVARQRQSAS SIAPPSKEVD SESIPRSVHP
     RPDLGTAYVA PRDPLERAIA ETWEKLFGIE RIGAHDNFFD LGGDSLLAVQ VISRLRGVVN
     MDLPGHSLLN APTVAALAEL IAQSDSPSST SLSRRRPARL LPDSLVLIKA GTTRPLFLMH
     PVGGHVYFYH DLASCLDSSQ PVYGLQAQGI DGKGPPLTRI EEMAARYLEA VRQIQPEGPY
     MLGGASFGGI IAFEMAHQLL SGGQRVSLLT MMDTPAPSAV LPQQHLDSTE RLAYLISGDP
     SLPIPSEEFR DLSPDEQLLH VLRRKKGVSR MFPKLALPEL ASFRKIVTAN LQAALSYAPR
     PYPGRVLFFQ ASERDTLSVS APSNGWVELA RGGVAFYEVP GNHITMNLPP NVAAIAQPLQ
     KSIAAIQDEE
//
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