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};
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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
//