ID D9WAX8_9ACTN Unreviewed; 1193 AA.
AC D9WAX8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:EFL20772.1};
GN ORFNames=SSOG_00484 {ECO:0000313|EMBL:EFL20772.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL20772.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL20772.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL20772.1,
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.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; GG657754; EFL20772.1; -; Genomic_DNA.
DR RefSeq; WP_009712594.1; NZ_GG657754.1.
DR AlphaFoldDB; D9WAX8; -.
DR STRING; 457427.SSOG_00484; -.
DR HOGENOM; CLU_000022_35_7_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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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 Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
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; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 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 Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 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..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 459..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 124901 MW; DAF1CD98A5B4E49C CRC64;
MANEDKLREY LKRAIADARD AHLRLSEAEA KAHEPIAIVG MGCRYPGGVA SPEDLWQLVS
SAGDGITPFP TDRGWDLETL FDPDTDRPGT SHVHEGGFLH DAAEFDAELF GISPREALAM
DPQQRLLLET SWEALERAGI NPHSLRGSAT GVFAGLMYHD YASRLSGVPK DVEGFLANGN
AGSVFSGRIS YVFGFEGPAV TLDTACSSSL VSLHLACHAL RTGECGIALA GGVTVMAAPT
TFVEFSRQRG LAADGRCKPF AEAADGTAWA EGAGVLVLER LSEAQRLGHQ VLAVISGSAV
NQDGASNGLS APNGPSQQRV IRQALKAARI PASEVDVVEA HGTGTRLGDP IEAQALLATY
GQGREGAEPL WLGSVKSNFG HTQAAAGVAG VIKMVMALRA GELPRTLHVG EPSSHVDWDA
GSVRLLTEER PWPRADHPRR AGISSFGISG TNAHVILEEP PAASGGDSGD GDGQENGTAS
GEATTDLSAM PVVPWVLSGR NAQSVRAQTE RLAAFLGERD HSPVDVGFSL ATTRAVLEHR
TVVLGTDGAA PLTGLTDPAG GDAVISGAVT DGRTGWMFTG QGSQRLGMGR GLYDRFPVFA
RVLDEVCGHL EAELAGGPGF GVPVREVLFA AEGSAEAVLL EGTGYAQSAL FAVQVALVEL
LRSWGMGPDV VLGHSIGEFV AAYVAGVFGL GDAARLVAGR ARLMQGLPSG GAMAAVEGTE
SEVTDILGGV PEGERATVAA VNGPTAVVVS GDEDAVERVM AVARERGRRV SRLRVSHAFH
SPLMEPMLAE FAEIAAGVAY RQPVLPAVST VSGQLVGAAD WATPEYWVRQ IHEPVRFHRA
LETTTTEQGV TRLLEIGPDP VLTALAQTAV DSMVASTLRK GRGEPETVLS AVAEMFVRGS
QVDWPAMFAG TGARRVDLPT YAFQRQRYWL DAARPVTDAR GLGLGVAEHP LLGAAVSVAG
SDAVLLTSRL SVRSHPWLAD HVVAGSVLVP GTAFVELAVQ AGDRVGCDRV EELTLQAPLV
LPEDGAVQVQ LSIDGAEDGR RALWVYSRPE EAGAEQPWTV HATGVLVAGV PAGGWDLRVW
PPVGAEAVVV DGLYERLSGA GLAYGPAFRG LREVWKQGED LLVEAALPEA VAEDGAGFGL
HPALLDTVLH ALGLQEPDAG ADTAFAAIHV VGCVAVRRGR LRRAGTSVST RHR
//
