ID F8QPG2_9ACTN Unreviewed; 3533 AA. AC F8QPG2; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-NOV-2024, entry version 60. DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:ADM46360.1}; GN Name=natE {ECO:0000313|EMBL:ADM46360.1}; OS Streptomyces sp. CS. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=876169 {ECO:0000313|EMBL:ADM46360.1}; RN [1] {ECO:0000313|EMBL:ADM46360.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS {ECO:0000313|EMBL:ADM46360.1}; RA Wu Y.Y., Kang Q.J., Shen Y.M., Bai L.Q., Deng Z.X.; RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADM46360.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CS {ECO:0000313|EMBL:ADM46360.1}; RX PubMed=21614382; DOI=10.1039/c1mb05036b; RA Wu Y., Kang Q., Shen Y., Su W., Bai L.; RT "Cloning and functional analysis of the naphthomycin biosynthetic gene RT cluster in Streptomyces sp. CS."; RL Mol. Biosyst. 0:0-0(2011). CC -!- COFACTOR: CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; CC Evidence={ECO:0000256|ARBA:ARBA00001957}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GQ452266; ADM46360.1; -; Genomic_DNA. DR BioCyc; MetaCyc:MONOMER-20758; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0004312; F:fatty acid synthase activity; IEA:TreeGrafter. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IEA:TreeGrafter. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro. DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt. DR CDD; cd08956; KR_3_FAS_SDR_x; 2. DR CDD; cd00833; PKS; 2. DR FunFam; 3.40.47.10:FF:000019; Polyketide synthase type I; 2. DR FunFam; 3.40.366.10:FF:000002; Probable polyketide synthase 2; 1. DR FunFam; 1.10.1200.10:FF:000007; Probable polyketide synthase pks17; 1. DR Gene3D; 3.30.70.3290; -; 2. DR Gene3D; 3.40.47.10; -; 2. DR Gene3D; 1.10.1200.10; ACP-like; 2. DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2. DR InterPro; IPR001227; Ac_transferase_dom_sf. DR InterPro; IPR036736; ACP-like_sf. DR InterPro; IPR014043; Acyl_transferase_dom. 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; IPR042104; PKS_dehydratase_sf. DR InterPro; IPR020807; PKS_DH. DR InterPro; IPR049551; PKS_DH_C. DR InterPro; IPR049552; PKS_DH_N. DR InterPro; IPR013968; PKS_KR. DR InterPro; IPR049900; PKS_mFAS_DH. DR InterPro; IPR050091; PKS_NRPS_Biosynth_Enz. 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; IPR055123; SpnB-like_Rossmann. 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; 2. DR Pfam; PF08990; Docking; 1. DR Pfam; PF16197; KAsynt_C_assoc; 2. DR Pfam; PF00109; ketoacyl-synt; 2. DR Pfam; PF02801; Ketoacyl-synt_C; 2. DR Pfam; PF08659; KR; 2. DR Pfam; PF21089; PKS_DH_N; 2. DR Pfam; PF00550; PP-binding; 2. DR Pfam; PF14765; PS-DH; 2. DR Pfam; PF22953; SpnB_Rossmann; 2. DR SMART; SM00827; PKS_AT; 2. DR SMART; SM00826; PKS_DH; 2. DR SMART; SM00822; PKS_KR; 2. DR SMART; SM00825; PKS_KS; 2. DR SMART; SM00823; PKS_PP; 2. DR SMART; SM01294; PKS_PP_betabranch; 1. DR SUPFAM; SSF47336; ACP-like; 2. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4. DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2. DR SUPFAM; SSF53901; Thiolase-like; 2. DR PROSITE; PS50075; CARRIER; 2. DR PROSITE; PS00606; KS3_1; 2. DR PROSITE; PS52004; KS3_2; 2. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2. DR PROSITE; PS52019; PKS_MFAS_DH; 2. PE 4: Predicted; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW NADP {ECO:0000256|ARBA:ARBA00022857}; KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 34..457 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" FT DOMAIN 919..1207 FT /note="PKS/mFAS DH" FT /evidence="ECO:0000259|PROSITE:PS52019" FT DOMAIN 1666..1741 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT DOMAIN 1759..2184 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" FT DOMAIN 2678..2957 FT /note="PKS/mFAS DH" FT /evidence="ECO:0000259|PROSITE:PS52019" FT DOMAIN 3445..3520 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT REGION 919..1047 FT /note="N-terminal hotdog fold" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT REGION 1060..1207 FT /note="C-terminal hotdog fold" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT REGION 2678..2803 FT /note="N-terminal hotdog fold" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT REGION 2818..2957 FT /note="C-terminal hotdog fold" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT ACT_SITE 951 FT /note="Proton acceptor; for dehydratase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT ACT_SITE 1121 FT /note="Proton donor; for dehydratase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT ACT_SITE 2710 FT /note="Proton acceptor; for dehydratase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT ACT_SITE 2881 FT /note="Proton donor; for dehydratase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" SQ SEQUENCE 3533 AA; 364617 MW; 9ADC9D7FB658B7CA CRC64; MSASYEKLVE ALRKSLEEVG TLKKRNQQLL AASREPIAIV GMACRLPGGV DTPEGLWELV AEGRDGVSGF PADRGWDLDT LLDTDPEKTG TSYVDQGGFL QGAGRFDAEF FGISPREALA MDPQQRLLLE TSWEALEGAG IDPLSLKGTD TGVFNGIMGV DYFAGGSVPP ELEGFTGTGA ASSVASGRIS YVFGFEGPAV TLDTACSSSL VAIHLAAQAL RRGECSMALA GGATVMATPG LFIDFSRQRG LAADGRCKAY SATADGTGWA EGAGVVVLER LSEAKRKGHR VLAVVRGSAV NQDGASNGLT APNGPSQQRV IRKALAAAGL NPGDVDAVEG HGTGTVLGDP IEAQALLATY GKDREEPLWL GSLKSNVGHT QAAAGVAGVI KMVQAMRHAV LPATLHVDEP SPRVDWDAGA VRLLTEAREW PHVDRPRRAG VSGFGVSGTN AHVILEQAPE ETDAEGPVPS ADGMVPVIVS ARGAGALAGQ AGRLAAFVGD TDVSLGAVAG ALVSRRAVLS ERAVVLAGSV DEAVSGLGSL AAGEVSPVVV TGSDVDGKSV FVFPGQGSQR VGMGRELYAE FPVFARALDG ACAVLDAELG AGESLRGVIF AGGGLLDQTV FTQAALFAVE LALFRLVESW GVRPDVVAGH SIGEVVAAHV AGVLSLEDAA ALVAARGRLM QALAPGGAMV AVAATEAEIE DYLGAGVDLA AVNAPGSLVL SGDEGAVLAV AEKLREQGRR VKRLSVSHAF HSSLMEPMLS GFAEALAGLT WNEPSLPVVS NVTGKLAEPG QLSDPAYWVE HVRRPVRFAE GIAASGGSVF LELGPGGALS GAITESAGED AVSVSALRDD RGEAQTLLLS VAELFVRGAK VDWTAVLPEG VAEAHVDLPT YAFDHQHYWL PAPRPLMDAT ALGQGAADHP LLGAVVQLPH SGGLVFTSRL SLRTHPWLAD HAIGGVVLVP GTGLVELAVR AGDEVGCGVL DELVIEAPLV VPEQGAVRVQ VTVGGPDETG ARGVEVYSTR HDVDTESGPD AWTRHASGTL STVAATGGTF DFTAWPPPGA RQVDISDGYE KLTRAGYGYG PAFQCVRKVW RREGELFAEV VVPQEQRENA AGFGIHPALL DAALHTSILD AAAEVTEAAV AEEKPVVRLP FAWNGLTLHA SGAASIRVRL LRPDPDTLSL EAVDDTGGPV LTLDSLVSRA VSGEQLEAAA GVSGVDGLFR VEWVGLPSVS GAGEVPGARV VQARSGGGET PVALVGRVLA DVRAWLADEE AVGAGRLVVV TGGAVAAGGD EALTDPGGAA VWGLVRAAQA ENPDRIVLVD ADSDGDGDSD GDWGEVDLKS VLATGEPQVA VRGGALYVPR LARVAPAASA EPALDPRGTV LITGGTGSLA GLLARHLVTR HGIRHLALVS RRGLEADGAR ELVAELEALG AESVSVPACD VTDRDAVAAL LAELTGTGRR LTAVVHAAGL FDAGVVGEMD QDRLAPVFAP KVTAVRHLDE LTRELAPDLD AFVTYSSVSG VFLGAGTGSY GAANACMDGL MAGRRAAGFP AQSLAWGLWE QNTGMGADLD DLSRSRMSRR GGVLAIGPDE GMELFDAALG SGETLLVPVK LDLRGLRADA TAGATVPSLL RGLVRAGRRA ARGTGGESRE GLAGRLAGLA TAEQEALLLD LVRTHVANVL GHTGPERVRA EAAFKDAGFD SLTSVELRNR LREATGLNLP ATAVFDYPTP LALARHLHAE LEGVTPAASA PVAVPHDPDE PIAVVGMACR LPGGVGSPED LWRLVSAGRD GVTGFPTDRG WDLDAVFDDD PEHAGTSYVA QGGFLHEAPL FDPVFFGISP REAVAMDPQQ RLLLETSWEA LERAGIDPTA LKGTDVGVFS GIMGVDYYSG GDVPEEVGGF ALAGAGASVA SGRVSYVFGL EGPAVTVDTA CSSSLVALHL AAQALRNGEC SMALAGGSTV MAGPGMFMEF SRQRALASDG RCKSYADAAD GTGWAEGAGV IVLERLSKAR REGHPVLAVL RGSAVNQDGA SNGLTAPNGP SQQRVIRQAL AAAGLTTADV DLVEGHGTGT VLGDPIEAQA LLATYGRDRD PDQPLWLGSL KSNIGHAQAA AGVAGVIKAV QALRHREMPA TLHVDAPSSQ VDWSAGAVRL LTDTREWPDP GRPRRAAVSS FGLSGTNAHV VLEEAPEPAE ESASAPEPER PTAAVPLVVS ARGTTALAGG AARLAAFLDG GGDGDGGGDG GGDGDGDGHG GGATPAEVCA ALLTRRAVLP ERAVVLAETR AEAVAGLNAL AHGESSPAVV TGGVAAAGAG KVVFVFPGQG TQWTGMGREL LDTSPVFAER IAECARALEP WTDWRLADVL RGEADADLLA RVDVVQPASF AMMVGLSAVW AAAGVVPDAV LGHSQGEIAA ACVAGALPLE EAARIVALRS QAIAERLSGH GGMAAVTLSE TEAMARLAAW EGRVEVAAVN GPSSVVVAGD AEALDEVLAA LEADGVRVRR VAVDYPSHTR HVEAVEDALD EVLADIRGKA PVVPFLSTVT GEWVREAGVL DGGYWYRNLR GQVRFGPAVT DLLHSGHTVF VEVGAHPVLT PAISESADGA DVLVTGTLRR DEGGPRRLLA SQAELFVKGV PVDWSGLLPA PAHPVDLPTY AFDHQHYWLP APAAAGDAAS LGLAGAEHPL IGAVVEIPDT GGVLCTSRLS LRTHPWLADH AVGDVVLLPG TGLVELAVRA GDEADCATLD ELVIEAPLIL PARGGVRVQV SVGGADESGA RTVTIHSARD GATGADSWIR HATGVLTPTP RTRAAAHPDL TNWPPPGAER VEVTPEDLYA ELHEHDYRYG PVFRGLRAVW RRDGELFAEI ALPEEQHAAA TEFGIHPALL DAALHTKAFL TSGEHRTMLP FAWNGLTLHA SGAASLRVRV TQATPEALSL EAADETGSPV LSTDSLLFRP VAAEQLRTTG DDMLFDVDWA PLPRPEATKT PTWLRLSTAE EVATLAEDTA DGTGLPDAVV LDAVTTGPDD TPLAVTDRTL EVVQTWLDGG GLEDTRLVVL TRGAVPAGGD ATLTDPGGAA VWGLVRAAQA ENPDQIVLLD VDAEADTDDP DARPGTGSEP TELGSLLGAV LASGEAQVAA RGEGLYVPRL TRAVAAGGFA EPVLDSAGSV LITGGTGSLA GVLARHLVVR HGIRHLVLVS RRGVEADGAR ELVAELEALG AESVTVPACD TTDRDAVAAL LTGLTGPRLT AVVHAAGLYD AGVVGEIEPE RLARVFAPKV TAVRHLDELT RELVPDLDAF VAYSSVSAHF LGAGTGSYGA ANACMDGLLA RRRAAGFPAK SLAWGLWEQT TGMAARADDL VRGRLNRRGG LRAITPDEGM RLFDAALDSD RTLLVPAKLD LRGLRAEAST GTAVPPLLRG LVRAGRQSAQ AAATGDERRR LAERLAGLPA GERTEALLEV VRTQIAVSLG YAATHRVDAD QGLFEIGFDS LTALELRNRL VELTGAKIGA GLVFDHPTPA LIVAHLTERM YGEDTTGPVA LSV //