ID L7UED9_MYXSD Unreviewed; 1834 AA.
AC L7UED9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AGC47286.1};
GN OrderedLocusNames=MYSTI_06013 {ECO:0000313|EMBL:AGC47286.1};
OS Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC47286.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC47286.1, ECO:0000313|Proteomes:UP000011131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC {ECO:0000313|Proteomes:UP000011131};
RX PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT fruiting myxobacterium.";
RL Genome Announc. 1:E0010013-E0010013(2013).
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DR EMBL; CP004025; AGC47286.1; -; Genomic_DNA.
DR RefSeq; WP_015351541.1; NC_020126.1.
DR STRING; 1278073.MYSTI_06013; -.
DR KEGG; msd:MYSTI_06013; -.
DR PATRIC; fig|1278073.3.peg.6096; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_7; -.
DR OrthoDB; 7617297at2; -.
DR Proteomes; UP000011131; 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; cd08955; KR_2_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 Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; 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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
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; 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; 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; 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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..457
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1714..1789
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1834 AA; 196848 MW; 95971439CD123218 CRC64;
MSAPGEYGDL MKRALLKLQE AQSQLDAHAR ERHEGLAIVG MGCRFPGGAS TPGRYWRLLL
DGTDAISEVP PERWDVDALY HPDPDQPGKV SCRFGSFLED IDQFEPRFFG ISPREAARMD
PQHRLLLEVT WEALESSGRN PASLHGTRTG VFVGMMGQDY TQLATQSPEL IDAHTGAGNS
ASVASGRLSY TFGFQGPSLT VDTACSSSLV ALHLALRSLR QREVDFAVVG GVNLVLSPVA
TLMESRAHML SADGRCKTFD AAANGIGRGE GCGVLVLRRL SDALADEDPI VAVIRGSAVN
QDGRTSGLTV PNGLAQRQVI QDALRDARVE ASRVGYVEAH GTGTALGDPI ELEALGAVYG
DRTAREQPLR VGSVKTNLGH LEGAAGIAGV LKAALCLANE EIPPHLHLRT PTPHVDWSRL
FVEVPTERRG WKAEAPRFAA VSSFGFSGTN AHVILESAPR LARAPARSTA RPLDLLTLSA
RSAGSLHRLA ESFADALSGP CKDSLADVCH TARVSRGSME ERAAFVASTS EEMVAALRAF
AHGETGTRGR REAESPRVAW LFTGQGAQYA GMGRELFETE PGFRRDLLRF EELLGPHLDR
PLTEVLFRDD SGALNETRYT QPATVALELA VAGLLRSWGV QPDAVLGHSV GEYAAAIFAG
ALTPEVGLPL VAERARLMQA LPERGGMLAL FTDEARALRA LAGHDRVTLA ALNGPRNTVV
SGAESSLDAI ARELAAEGIG SQRLKVSHAF HSPLMQPMLE AFARVAGAVR LQAPEVPLIS
NLDGAEAGAA LLRPDYWVRH VREPVRFEQG LRTLLQRGVS VFVEVGPKAV LSNLARDGVA
PEGSVWLETL HPRRSACAGL LRTLAELFVR GARVDGARLA GDAGVRRISL PTYPFERQRH
WLDVPAPWAR PTRPSTHPLL GARWESPALR EGTTVFSREL DARSLPLLSD HRVFGKGVVP
AAAFVEMVAS AVSQVVGAES MSLEAVTLHQ PLVLPEQRTR VVQTLLEEQG AAGFTCTVMS
QEEARGARAS WTTHLTCRVS SQGTLPSPPR LELDAWRRSC PSPVDIGDFS EAIRQRGLDY
GPSLSVLSSL HRGPHAALSS SEVAEGGVSY RAHPALLDAC LRTAAAVTPL SPEDEGLLLP
VAIQRLDLHR RLPERLWTYA TQRPEAEAAG HPITDMTLCA EDGTVVASLT GLSVRGADRD
VLLRGLEVDW REWLYRVTWS PCASPEAERV SDPHWVLFTD EAGFGEEVAA LLEQRGARVT
RVRQGSEFLQ GPTGFQVDPA RPAHFEQLFS TWDGASPQGL LYLWGLDAGD SLESAQRSGC
VGALHLVRAL AQRSWAPAPR LVIATRGTQA LPADVQGPRI AQAPLWGFGQ AVSTELPELR
CLRVDLPGEP VPTDAEALLR ACALPEQECQ VAVRTGALHT ARLEHARPRA MSRKLEVSPA
ASYLIAGGLG GLGLRLAGWL ADRGAKHLLL LGRRGPSPEA QRRIEALEAR GVHVRVAQAD
LASRDAVAAA LSEARGAPPL RGLFHVAGVL HDGTLVHQTA EQLHEVLAPK VQGAWNLHEL
SAGLPLDFFI CFSSAASLLG TPGQSNYVAA NAFLDALAHL RHAQGLPALT LNWGSWAETG
MAARLGSAAE GTSSAMGFET IPVERGLEVL ERLMGGAGAS LGVFPVDWRR LGEKWPGLSR
QAFFQGLLGT TPHAPRAPVF RAQLEAAAPT RRLELLRQHV SSQVSRTLGL AESERLSGHE
RLFDLGFDSL LAVELKNRLA SSLGRNLRST LVFDFPSVAG LVSHLAGELG LGGEAPKRVE
GPARDDSLAA EIQTLSEQEL TSLIDQELMS ALTR
//