ID D9WG11_9ACTN Unreviewed; 880 AA.
AC D9WG11;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:EFL23227.1};
DE Flags: Fragment;
GN ORFNames=SSOG_02941 {ECO:0000313|EMBL:EFL23227.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL23227.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL23227.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL23227.1,
RC ECO:0000313|Proteomes:UP000003963};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657754; EFL23227.1; -; Genomic_DNA.
DR AlphaFoldDB; D9WG11; -.
DR STRING; 457427.SSOG_02941; -.
DR HOGENOM; CLU_000022_16_6_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000003963; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR001227; Ac_transferase_dom_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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR036299; Polyketide_synth_docking_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 33..462
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT NON_TER 880
FT /evidence="ECO:0000313|EMBL:EFL23227.1"
SQ SEQUENCE 880 AA; 91820 MW; 874B4BCA67C1E3E9 CRC64;
MANEEKLRAY LKRVTGDLHQ ARQRLQQLED GSAEPIAITA MSCRYPGGVE SPAELWNLVA
SGVDAVSGFP TNRGWDLDDL FDSDPDAKGK SYAREGGFLR DADQFDPAFF GISPREAMTM
DPQQRLLLET AWEALERAGI EPDSLRGSRT GVFAGVMYDD YGAARIYGGS ADEFEGYLVN
GSAGSIASGR VAYTLGLEGP AVTVDTACSS SLVSLHLAVQ ALRAGECSMA LAGGVTVLAT
PSLFVEFSRQ RGLSPDGRCR SFSDDADGTG WSEGAGMLLL ERLSDAQANG HPVLAVVRGS
AVNQDGASNG LTAPNGPSQQ RVIRAALANA RMSEAEVDAV EAHGTGTTLG DPIEAQALIA
TYGQGRAEGQ PLWLGSLKSN IGHAQAAAGV AGVIKMVEAM RHGVLPQTLH VGEPSSKVDW
DAGAVELLSE ARAWPEAEGR PRRAGVSAFG ASGTNAHVIL EQAPAVEPTS DAGDAVAAGV
VPWVVSGRGA DALRGQAARL LSRAEGDGGL APVDVGWSLA SGRAALEDRA VVVAPDREGL
IAGLGGLARG ESVPGLVTGS VVEGRVAFLF TGQGSQRLGM GRALYDAHPV FADALDEVCA
ELDRHLERPL KGVLFGEDAS VLDRTGFTQP ALFAVEVALF RLVQAWGVRP DFLSGHSIGE
LAAAHVAGVL SLADACTLVA ARGRLMQELP AGGAMVAVQA SEFEVAPLLT ERVSIAAVND
PTSVVISGDE DAVLELASGF AAQGRKTKRL AVSHAFHSPR MDGMLDAFRE VAEGLTYEAP
RIPIVSNLTG ELVSAEEIAT PGFWVRHARE AVRFLDGVRA LEAQGVTTYV ELGPDGVLTA
MAQECVTGDD AAFVPVLRAD RAEEQAFVEG VARAWTVGVA
//