ID D9W5N5_9ACTN Unreviewed; 1660 AA.
AC D9W5N5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:EFL20213.1};
GN ORFNames=SSNG_07465 {ECO:0000313|EMBL:EFL20213.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL20213.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL20213.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL20213.1,
RC ECO:0000313|Proteomes:UP000005763};
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 sp. strain C.";
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; GG657752; EFL20213.1; -; Genomic_DNA.
DR STRING; 253839.SSNG_07465; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd08952; KR_1_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 6.10.140.1830; -; 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 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; 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; IPR015083; Polyketide_synth_docking.
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; 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; PF08659; KR; 1.
DR Pfam; PF18369; PKS_DE; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 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; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
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 44..470
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1498..1573
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1660 AA; 173801 MW; 0A6D43F895955DB5 CRC64;
MPERHPRSSR QMDNEQKLLD HLRWVTAELK QTRQRLREVE ADEPEPIAVV GMACRYPGGV
RSPEDLWRLV RDGRDAVSGF PVNRGWDLDS LYDPDPDHLG TTYVREGGFV HDAGDFDADF
FGISPREALA MDPQQRLLLE TAWEAFERAS VDPTAVAGSR TGVYVGTTYT GYGSDREGAA
ENVEGHLMTG IATAVSSGRL SYAFGLEGPA VSVDTMCSSS LVAIHLAVQS LRQGECALAL
AGGAQIMSTP EVYVEFSRQR GLSPDGRCKP FAAAADGTGW SEGVGVLLLE KLSDARRAGH
RVLAVIRGSA VNQDGASNGL TAPNGPSQQR VIEEALANAR LSPHEVDLVE AHGTGTTLGD
PIEAQALLAT YGRSRPEGRP LHLGSIKSNI GHSAAAAGVA GVIKAVMSVR EGVLPRSLHI
DGPTPEVDWS SGAVELLTEE RPWPAAEGPR TAAVSSFGAS GTNAHVIVQH AGQDADAEPA
PRASEPNRPV LPAATLPWVL SGRTAEGLRG QAARLRAFAD EAGTGVSEAA IGLALATTRA
GLEWRGVVPA GSRTGLDALA AGLPAADVVD GAVVTGADRP VFVFPGQGSQ WAGMAVELYD
SSPVFAARLD ACAGALAPHT DWSLLDVLRQ EDGAPGFDRV DVVQPALWAV MVSLAELWRA
AGVVPAAVIG HSQGEIAAAA VSGALSLEDA AKVSALRARA IVALAGKGGM VSVADVADAV
AERISTWGNR LALASVNGPQ STVVSGDPEA LDELMAACEA DGVRARRINV DYASHGPQVE
SIRDEVIGLL AGIEPRTAEV PFFSTVTGEW ADGSELDAEY WYTNLRQTVR FQDAVSALLE
RGHGLFVEAS AHPVLTIGVQ ETIEAAGTSA VTQGTLRRDE GGAQRFLASL AEAWTHGAPV
DWQSVCDTPD APADLPTYAF QRRTYWLEGT PAADRTPVVD EAEAGFWNSV ESADVTALAD
TLALQDTGPL RELLPALSAW RRDRREASAL DARRYRITWK HLPDAAPARL HGDWLLLAPE
GAPEGTSAGP FAELLTAHGA RAHLLALDPA RADRDAWAGA LRTAQDGHEP FAGILSLLST
DEDAGLLGTL VATQALDDAG IEAPLWALTR GAVAAGPENA PRSAVQAQVW GLGLVAALER
PRGWGGLVDL PADLDEAAAA RLAGALAGRD GEDQIAIRTA GTYVRRLVRA ALPDGAPARD
WQPSGTTLLT GAAGPLGAEA ARRLAAAGAG HLLLTAAPAE LTPALEALAG ELAADGTEVT
LEEWDGADPA ALAALTARAE QAGRPVRTVV HAAAHVELTP LAATTARHLE EALAAKVTSA
RALDEVFGTD GPALDAFVLF SSVTSYWGGG EHAAFAAANA HLDALAQQRR ARGLPATAVG
WGVWDLFDAE AHPDEARELH ERSAQRGLPL LDPEAALNAL RRILGHDETA VAVADVDWDR
FLPLFTSART GRLTEDVPQA RRILAQAGRG GDEEAGDTGA ADALRHKLAE LSGEEQDRVL
TDLVCGHAAA VLGHASSGAV DAARAFKDLG FDSLTAVGLR NGLNAATGLT LPATMVFDYP
TPGALAGYLR GLLLDGGAAR REEATTDSVH GDLDRIESDL LSLAPGQEEG RNLTRRLEAL
LSRWKDAQAA ADGGSVSGKL DAASDEEIFA FIRKEFGRPE
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