ID D9WQ65_9ACTN Unreviewed; 2049 AA.
AC D9WQ65;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:EFL26025.1};
GN ORFNames=SSOG_05739 {ECO:0000313|EMBL:EFL26025.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL26025.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL26025.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL26025.1,
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; EFL26025.1; -; Genomic_DNA.
DR STRING; 457427.SSOG_05739; -.
DR HOGENOM; CLU_000022_35_2_11; -.
DR Proteomes; UP000003963; Unassembled WGS sequence.
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; 3.40.50.11460; -; 1.
DR Gene3D; 6.10.140.1830; -; 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; 2.
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 336..411
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 432..858
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1890..1965
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2049 AA; 214141 MW; A182601DD7AA8BF8 CRC64;
MSARWHGWRR CWPPEPRPGP GPGGEDQVAV RASGVFGRRL VRASAPASAD GSWRPGTGSV
LVTGGTGALG ARVARWLVEN GAEHVVLTSR RGLDAPGAAE LRDELAASGA RVTVAACDAA
DRDALARLLA GLPDELPLTG VVHTAGVLDD GVLDALTPER FTTVLRAKVA AAAHLDELTR
ELDLSAFVLF SSISGTFGAA GQGNYAAANA YLDALAERRR AEGLPATSIA WGPWAEGGMA
ADDALEQRLR RGGLPPMDAE RAMAALQRAL DLDDAAVVVA DIDWARFAPD FTAVRPSRLI
ADFAEVAEPE ADSDTVSPGQ GLAARLAGVG EAERDRLLLD LVRTHVAAVL GHDGTESVGA
ERAFGELGFD SLTAVELRNR LGAASGVKLP ATLVFDYPTA TALAGYLRAE LVDSEPAATP
SAPATVAVAT DDDPIAIVAM SCRFPGGVTT PEELWQLLTA GGDAIAGFPA DRGWDLDALY
DPDPDKRGTF YAREGGFLYD AGRFDAAFFG ISPREALAMD PQQRLLLETS WEAFERAGID
PATLRGTSAG VFVGSNGQDY DASLHTVPEG VEGYLGTGNA ASVVSGRLAY TFGLEGPAVT
VDTACSSSLV ALHWAIQALR QGECSLALAG GVTVMSSPGA YIEFSRQRGL AADGRCKAFA
AGADGTGWGE GVGMLLVERL SDARANGHPV LAVVRGSAIN QDGASNGLTA PNGPAQQRVI
RQALATAGLS AAEVDAVEAH GTGTRLGDPI EAQALLATYG QERDPERPLW LGAIKSNIGH
TQAAAGVAGI IKMVLAMRHG VLPQTLHVDE PSPHVDWSAG AVSLLTHEQA WPETGRPRRA
GVSSFGFSGT NAHTVLEQAP EPAAVDGTEP SAVRPDVLAW PLSAKSGDAL REQAERLRAH
VAADPALDAV DVAYSLATTR SALDHRAVVL GPDRDRLLAG LAALARGESA AQLVQGSPAE
GRTAVLFTGQ GSQRLGMGRE LYEASPVFAE ALDAVCAELD RHLERPLYDV LFGAEKADKE
LLDRTAFTQP ALFAVGVALF RLAEAAGLRP DVLAGHSIGE LAAAHVAGVL SLADAATLVA
ARGRLMQELP AGGAMIAVQA SEDEAAPLLT ERVSIAAVNG PTSVVIAGDE DATVEIAADF
EARGRKTKRL TVSHAFHSPH MDGMLAGFRK VAEGLTYGAP RIPILSTVTG QPVTDELGMG
SDYWVRHVRQ SVRFLDGIRA LEAQGVTTYV ELGPDGVLTA MAQDCVTGEG PDDVAFVPVL
RGGRPEPETL AGALATLHVR GVALDWEALF AGTGAHRVDL PTYAFQRRHY WLDGTPRHTT
PDTTTDVAGE RFWAAVESDD LGALADTAGI DVDQPLSALL PALSAWRRRE REQSAIEGWR
YRVSWKPLEE PRLAAAPGVW LVAEPDGHAD TVRTLLDALA ERGADLRRIA PTGTDLDREA
LADRIRRAAA GDPVHGVLSL LALDEHPHPA HGAAPTGLLR TGVLVQALGD AGVDAPLWCA
TTGAVSTAAS EPPRSAAQAQ VWGLGRVVAL EHPERWGGLI DLPASLTDLP ATLDERAADR
LAGVLGGHGD DAHEDQFAIR TAGVLARRLA HAERATAAGE PWRPHGTVLV TGGTGALGAH
VARWLAAGGA EHLVLTSRRG PDAPGASQLD AELTALGARV TVAACDVTDR EAVAGLLARI
RDEHPDHPLT AVVHTAGAGQ FAPLADTAPA DVADVVAAKV AGANHLDALL ADTDLDAFVL
FSSIAGVWGS GGQGAYAAAN AHLDALAEQR RARGAAATSV AWGPWADGGL VADDEAAEQL
RRRGLPVMAP HSAIAALQQA LDGSETTITV ADVDWDRFAP AFTAARPRPL IADLPEVRNA
DTAADVVSDD DPAEALRERL SGLTESEADR VLLDLVRAEV AAVLGHDDTT AIEAGRAFKE
LGFDSLTAVE LRNRLNAATG LQLTATLVFD HPTPGVLAGE LRAEILGEDT TPELPALAEI
DKLEFTLSHV PDDKAERERV TARLEALLRT WHETENETGA DGADDDDLDI ESASAEDIFD
LINNEFGRS
//
