ID A0A1P8XMA4_9ACTN Unreviewed; 1893 AA.
AC A0A1P8XMA4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Polyketide synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BV401_00970 {ECO:0000313|EMBL:AQA09283.1};
OS Streptomyces autolyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA09283.1, ECO:0000313|Proteomes:UP000187851};
RN [1] {ECO:0000313|Proteomes:UP000187851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA Yin M., Jiang M., Lu T.;
RT "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP019458; AQA09283.1; -; Genomic_DNA.
DR STRING; 75293.BV401_00970; -.
DR KEGG; sauo:BV401_00970; -.
DR Proteomes; UP000187851; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd08952; KR_1_SDR_x; 2.
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; 2.
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; 2.
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; IPR041618; PKS_DE.
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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 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; 2.
DR Pfam; PF18369; PKS_DE; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
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 Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 280..355
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 376..797
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1744..1819
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1893 AA; 197022 MW; 389A304E3376958D CRC64;
MVTGGTGGLG VCVARWLVGC GAEHVVLVSR RGAGAVGVEG VRAELEGLGA RVSVVACDVA
DRDGLAGVIA GIGEEVPLRT VVHAAGVNTG TVALESLTRE RLHEELAVKV DGAWHLDALT
AGMELDAFVL FSSGAAAWGS GGQAGYAAAN ACLDSLAAHR RARGRTATSI AWGAWSGAGM
VGATPGQDAL LRRLGVVPMR PDLAVSALQQ ALDDDETAIV VADLDWPRFL PTFTATRPSP
LLSALPEAAR PAAPAEEESP AGDPGLSARL VDLSARERSV FLVELVLREA AEVLGHTSGQ
AIVADQTFRD IGFDSFTAVE LRDRIARTTG LTLPATTVFD HPSALRLAAH LGSLLDGTGT
NEDTAAPGAP VGPAAEDPVV IVGMACRYPG GVTGPEDLWR LIAEGTDAIT PFPADRGWDL
AALSAPGGSG FSTTRSGGFL HDAGGFDADF FGISPREALT MDPQQRLLLE TSWEALERAG
IDPRATRGSR TGVFAGVTDQ GYGPPLHQPA EDGDPYALTG TAASVASGRV SYVLGLEGPA
LSVDTACSSS LVAMHLAAQS LRRDECSLAL AGGVTVMATP GPFVAFTRQG GLSPDGRCKS
FSQEADGTGW SEGVGMLVLE RQSDARRNGH RILAVLRGSA VNQDGASNGL TAPNGLAQER
VIRQALADAG LRPAEVATVE AHGTGTRLGD PIEGRALLAT YGQDRPGEEP LWLGSLKSNI
GHAQAAAGVG GVIKMVKAME HGVLPRTLHA DRPSSEVDWA AGAVRLLAEA RPWDGPRRAG
VSSFGISGTN AHLILEAGPD TSVSAERRPG ADGPRGPVPW MVSGHTEGAL RDQARALLDR
TGEADVHDIG LSLATTRALL HHRAVVVARD AEGFRAGLAA LAAGDPAQPV VTTPPAPGGL
GFLFSGQGAQ LPGMGQELAA AFPAFASAFA EASAGVGGVR VDDAEVLRGT AMAQRALFAF
QVALYRLWES WGVVPDAVIG HSVGEVAAAH VAGVLSLEDA CRLVAARADL MERLAERGGV
MMSVRASEDE VTGTLADGVS LAAVNGPRSV VLSGDAEAVE AYAARWPGAR GLRVSHAFHS
HHMDGMLDAF AAVVRELTFH PPSLPMPAAG DVTDPDHWVR QVREPVRFLD GVRQLLARGV
RTFCEIGPDA VLTGLGEECA EDVPGVRFVP SARRGSPEEI RTVRALGELA AHGVTPRWDR
VFPGARPTDL PTYAFQRRRY WLGPRQPDGD FWALVRQQDL SALTESLRVD GDPRLSEVLP
ALARWHRRGE DSAALGRWRY ELTWHPVAAD PPAEVTGTWL VAPATAGDPL ADAVVMALAE
RGADPAVVRP EDVPARVARR PVAGVVVLLP AADGPDEADG GSPAVPGLDE AAATVELVRR
IAAEETGTPL WLITRGAVAV DGEVPLSGPG HSLLWGLGPV LRDERPELWG GVVDVPAEPS
TTAAELLVTA LTSGWDQLAV TGGGLRTRRL VRAPYDRTVW RPSGTVLVTG GTGALGRHVA
RWLAAEGAGH VVLAGRRGGD APGVAELCAE LTAGGVTATA VSCDIRDRAA LAELLDRCSP
DAVVHAAAVV DDTTLDGLTP HRVDQVLRTK ALPAWHLHQL TRDRPLSAFV LFSSVAGTLG
TAGQGNYAPG NAFLDALAAH RHALGLPATS IAWGPWAGDG LAAADAVAGA AGRHGFTPMD
PALAVRALAA TAVPFALVMD ADWERFPAER APSVVAGLVP DRAAEPAPGL LDRLSGLSEA
EQARLVRQTV RSALAAVLGH RDPGTLGEDR TLTELGLDSM TAVELRNRLR AQTGLHLSAT
LAYNHPTAEE LARHLHDRLR ERTAPAASSV TAELDRLEAA VAALPPGGDE RGAVAERLRA
LLGEIAPDPA HERDLDDVTQ DELLALIDDE FGR
//
