ID A0A128ATN2_9ACTN Unreviewed; 5234 AA. AC A0A128ATN2; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 24-JUL-2024, entry version 40. DE SubName: Full=Type I polyketide synthase {ECO:0000313|EMBL:CUW01174.1}; GN Name=gonP4 {ECO:0000313|EMBL:CUW01174.1}; OS Streptomyces caniferus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=285557 {ECO:0000313|EMBL:CUW01174.1}; RN [1] {ECO:0000313|EMBL:CUW01174.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GUA-06-06-006A {ECO:0000313|EMBL:CUW01174.1}; RX DOI=10.1186/s12934-016-0443-5; RA Garcia-Salcedo R., Olano C., Gomez C., Fernandez R., Brana A.F., Mendez C., RA De la Calle F., Salas J.A.; RT "Characterization and engineering of the biosynthesis gene cluster for RT antitumor macrolides PM100117 and PM100118 from a marine actinobacteria: RT generation of a novel improved derivative."; RL Microb. Cell Fact. 15:44-44(2016). 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; LN997801; CUW01174.1; -; Genomic_DNA. 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:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion 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; cd05195; enoyl_red; 1. DR CDD; cd08952; KR_1_SDR_x; 2. DR CDD; cd08956; KR_3_FAS_SDR_x; 1. DR CDD; cd00833; PKS; 3. DR Gene3D; 3.30.70.3290; -; 3. DR Gene3D; 3.40.47.10; -; 3. DR Gene3D; 3.40.50.11460; -; 1. DR Gene3D; 1.10.1200.10; ACP-like; 3. DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3. DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013154; ADH-like_N. DR InterPro; IPR011032; GroES-like_sf. 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; IPR042104; PKS_dehydratase_sf. DR InterPro; IPR020807; PKS_DH. DR InterPro; IPR049551; PKS_DH_C. DR InterPro; IPR049552; PKS_DH_N. DR InterPro; IPR020843; PKS_ER. 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; IPR002364; Quin_OxRdtase/zeta-crystal_CS. 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; 3. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF13602; ADH_zinc_N_2; 1. DR Pfam; PF08990; Docking; 1. DR Pfam; PF16197; KAsynt_C_assoc; 3. DR Pfam; PF00109; ketoacyl-synt; 3. DR Pfam; PF02801; Ketoacyl-synt_C; 3. DR Pfam; PF08659; KR; 3. DR Pfam; PF18369; PKS_DE; 2. DR Pfam; PF21089; PKS_DH_N; 1. DR Pfam; PF00550; PP-binding; 3. DR Pfam; PF14765; PS-DH; 1. DR SMART; SM00827; PKS_AT; 3. DR SMART; SM00826; PKS_DH; 1. DR SMART; SM00829; PKS_ER; 1. DR SMART; SM00822; PKS_KR; 3. DR SMART; SM00825; PKS_KS; 3. DR SMART; SM00823; PKS_PP; 3. DR SMART; SM01294; PKS_PP_betabranch; 3. DR SUPFAM; SSF47336; ACP-like; 3. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 3. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 7. DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 3. DR SUPFAM; SSF53901; Thiolase-like; 3. DR PROSITE; PS50075; CARRIER; 3. DR PROSITE; PS00606; KS3_1; 3. DR PROSITE; PS52004; KS3_2; 3. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2. DR PROSITE; PS52019; PKS_MFAS_DH; 1. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 34..452 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" FT DOMAIN 1480..1555 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT DOMAIN 1575..2001 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" FT DOMAIN 2478..2753 FT /note="PKS/mFAS DH" FT /evidence="ECO:0000259|PROSITE:PS52019" FT DOMAIN 3547..3622 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT DOMAIN 3644..4071 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" FT DOMAIN 5079..5154 FT /note="Carrier" FT /evidence="ECO:0000259|PROSITE:PS50075" FT REGION 450..479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2478..2605 FT /note="N-terminal hotdog fold" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT REGION 2617..2753 FT /note="C-terminal hotdog fold" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT COILED 5..32 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 456..471 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 2510 FT /note="Proton acceptor; for dehydratase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" FT ACT_SITE 2676 FT /note="Proton donor; for dehydratase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01363" SQ SEQUENCE 5234 AA; 549932 MW; 69962C5D5F30A53C CRC64; MATSADQIVE ALRASLREND RLRKENQQLV DAAGEPLAIV AMSCRFPGGV QTPEDYWQLL AGGVDALSEF PADRGWDLSA LGVATTRGGF VHTADAFDPQ FFGMSPREAL ATDPQQRLLL EVSWEALERA GLDPMTLRGS RTAVFAGCSN QEYGAGLRGN VPEGVAGHVL TGTTGSVVSG RVAYALGLEG PAVTVDTACS SSLVTLHLAA QSLRAGECDL ALAGGVAVMS TPAAFVEFDR QGGLAADGRC KPFSDDADGT GWGEGAGMLL VERLSDARRN GHPVLALLRG SALNQDGASN GLTAPNGPAQ QRVIRSALTG AGLTAADVDA VEAHGTGTTL GDPIEAQALL ATYGQDRPAD RPLWLGSVKS NIGHTQAAAG VAGVIKMVLA LRHGVLPQSL HTTRPATHVD WSAGHVRLLT EPVAWPDGSR PRRAAVSSFS ISGTNAHTIL EQAPEDRAPS PDHRKAAAES REQAVEAAPH PTAARLPYIP WVLSARSADA LRAQAGRLHA HLDSHPDVDP YDLAYSLATS RSAFEHRAVL LGTDLADLHG KLTALAEEGP HTAAAVSGSP LRGKTAFLFT GQGAQRLGMG RELHETFPVF ADAFDAAGAH LDPELSQPLA DVVFGQDAAA LDRTGFTQPA LFAFEVALFR LLTSWGIQPD IMMGHSIGEL AAAHCAGVLS LPDACRLVAA RGRLMQALPP GGAMASLQAT EAEVRPLLGE TADRVSIAAV NGPEATVIAG DEATVDTLAG HFRDLGRKVA RLRVSHAFHS PLMDPMLADL RATARDLTYR PPRTPVVSNV TGRLATPDEL CSPDYWVRHA RQGVRFADGV RTLAERHVTR LVELGPDGTL TALAAACLPD ADTLVTPLLR KDTPEAESLL TAIGGLHLSG TPLDWAALLP GARRVDLPTY AFQRTRYWLN DTPPGDAPGS RPAHSAFWTA VEQQNVPELA DSLSLDRSLL EPVVPALAAF HHDQQQHSTA RSWRYTEHWE PVEPHATTTA PAHWLLVVPA EGPEDHQPVV DALTTALAGH GATVTTVNLP PDADDLAQRI EEAGGRDPDG INVLSLLGLG TARDPHHPEA PAALVLTSAL LQVLVGADTP VRLWSATRGA VSIGRSDRLS APGQAALWGL GRSAAIEHPD HWTGLVDLPE RLDARALERL CAVLHSPRHD TGNGKEFALR ASGLFARRLV RAPRPEQPGR STTWTPAGTT LITGGTGTIG SALARRLARE GSDHLLLISR RGPDAPGAQN LVAELAAHGT RTTLAACDPA DRDALAELLA ALPEDRPLTS VFHTAGVLDD GTLAAMDAER FATVLRPKTE AAANLHELTR AHDLTAFVLF SSIAGTLGAA GQANYAAANA GLDALARHRR AHGLPATSVA WGPWAHDGMA ADPTLRAKLS RAGLPPMEPD TALVALHQAL DHDETHLVIA DIDWNTFPAS HNPLFGKLPE AAAHHPGQDT GTEGVRSLLA TQRTPAEQEQ HLLGLVRRTT ATVLGYPGSE SVGTTRTFQE LGTDSLTAVE LRNALSAAVS LPLSPTLVFD HPTPLALARH LHTELLGDLG EQHTAALAHP VQADGEPIAI VGMACRYPGD IRSPEDLWKL IADGGDAITP FPEDRGWNID AVYDPDSGCP GTSYVREGGF VRSAGDFDPG FFGISPREAL AMDPQQRMLL EIAWEAVERA GIAPLSLRGS RSGLFVGCGY QGYGSGAGDM PDDLLGHLLT GSSGAVVSGR VAYALGLEGP ALTVDTACSS SLVALHLAVQ SLRSGDCDLA LAGGVTVMST PGAFIEFSRQ RGLAADARCK AFAETADGTI WSEGAGIVLV ERLSDARRNG HRVLAVVRGS AVNQDGASNG LTAPNGPSQQ RVIRQALAGA GLSASDVDAV EGHGTGTTLG DPIEAQALLA TYGQDREADR PLWLGSVKSN IGHTQVAAGV AGVIKMVEAF RHGVLPRTLY VDEPSSHVNW SAGHVRLLTD DMQWPADDRP RRAGVSSFGL SGTNAHVILE QPPADEPQDA LSRTPAPPLL PWVLSGRSEA ALRAQAARLS AHLKDRPELD PWDVGRSLAT TRSSFEHRAV VLGEDREALL DGLTALDRGE PRGNLVAGMA GSEGGLAFLF TGQGAQRPGM GRELYEGFPV FAEAFDAVCA HFDGALAAPL RDVVFGTDEG DADVERLHRT EFTQPALFAV EVALFRLVES FGVRPDYLMG HSIGELVAAH VAGVLSLGDA CRLVAARGRL MQALPVGGAM VSVQATESEV LSLLEGQETR VSVAAVNGPE AVVVSGVESV VAEIAGRFES EGRKVRRLQV SHAFHSPLME PMLDAFRLVA ESVTYAEPRI PVVSNVTGEL ATARELTSAD YWVRHVREAV RFADGIRWLE EHEVTRFLEI GPDGTLTAMA QGCLDGPADH LLVPALRKDR PEVTGLLTAL GHAHARGVTV DWATFFAGTG ARHTDLPTYA FQHQRYWLRL AHTNATNLGA AGLQGAEHPL LAATMTLADS HSVVFTGRLC AQDHPWLADH VVDGSLLVPG TAFLELALRA ADQAGCDHVE SLTIEAPLVL PAHEAVQLQM RLQEPDLHGA RTLTLHSCRI GSTGVAEEPW VRHATGVLGA DRHRETFDFA VWPPEGARPV PTDGLYEAFA DAGIAYGPAF RGLRAVWRRD GDLFATVEIP EAAEASSFGL HPALLDTVLH ALALDADETA ALGQQPLSWQ NVKLYALGAT VLRARMSTRA DGGVSLQLAD AVGQPVAEVA SLTRQPMTAE LFGRARQGGT HSDALYRVDW ARVPETAAEA VDLVDLDELG SAPGDDIPSF VALRLDTATG ESAATAEAAR AVTYRALAGL QQWTDSERYS AARLVVVTRN AVPAELQHPD PAQATVWGLV RAARVEHPDR FVLVDVDGTE ASLAALPTAL ASGEPELALR EGTAYLPRLS MNIRRDELSP PCLPQDGWCL ENAAEGTLEN LRLVQRPEAV DQLETGQVRI AVRAAGVTFR DVLSVLGRYP GDAGALGIEG AGVITEVGPG VTGFAPGDRV MGLFPSAFGP VAVADERMVV RVPEGWSFAQ AASVPAVFLT AYHALVDLGG LEAGESVLVH AGAGGVGMAA VQLARHLGAE VFATASPGKW ATLRALDLDE AHIASSRDLD FERSFLAATA GRGVDVVLDS LAGEFVDASL RLLPRGGRFL EMGKTDVREP AEVAAEHEGV HYRAFDLFDA GPERIGEMLT ALVGLFEEGV LEPLPVTAWD VRKAPEAFRF LSQARHVGKV VLTMPVPLDA EGTVLVTGGT GGLGAVVARH LVAEHGARHL LLASRRGPQA PGVDALVDEL VGCGAEVEVV ACDVSDRGAL SGLLDAVPKQ HPLTAVVHTA GVLDDGTLSS LTPARLDAVL APKADALLLL DELTRAEDLA EFVVFSSVAG TFGSAGQGNY AAANAFADAL MHRRSGSGFP ARSLAWGAWA PGAGMTGALS EADLQRMARG GITPFTEERG VEAFDAARHT AVPVVVPVQL NHTMLREQHA AGVLPPLMRG LLGRSTRRTA VSSSAEVTPA DALRSRLSPL SQDERRTAVL ELVRTQAALV LGHPGPEAIE PTRDFRGLGV DSLTAVELRN QLQAATGLPM PATLVFDHPS PLRVAHHLEG EFSGGDEAVD AGATPSAPVD ADPDEPVAIV SMGCRFPGGV GSPEELWRLL VEGGDGVVPF PVDRGWDVEG LFDPEPGVPG KVSTRAGGFL PGVDGFDPAF FGISPREAVA MDPQQRLLLE VSWEAFERAG IVPGSLRGSR TGVFAGTNGQ DYTGLLVASG EEDLGGYIGT GNAASVVSGR LSYVFGFEGP AVTVDTACSA SLVALHLAVQ SLRAGECDVA LAGGVTVMST PGLFVDFSRQ RGLAADGRCK AFSDAADGAG FSEGVGVLVL ERLSDARRHG HRVLAVVAGS AVNQDGASNG LTAPNGPSQQ RVIRQALGAA GLSSSDVDVV EAHGTGTSLG DPIEAQALLA TYGQDRDADQ PLWLGSVKSN IGHTQAAAGV AGVMKMVLAL QHGVLPQTLH VDEPSSHVDW SAGDVRLLTE SVHWPETGRP RRAGVSSFGI SGTNAHTIIE EAPASEELLD SAETLKLPAV PWVISGRDEA GLQAQAQRLL THLDEFLLDP SDVGFSLATS REIFDHRAVL LVDGHESATQ GLTALAEGRK AAGVVRGTKQ QGPSVFLFAG QGAQRLGMGW ELYDTFPVFA DAFDAVCACF DAELESSLRG VVFGENAEEL NRTEFTQPAL FAVEVALFRL VESFGVRPDF LVGHSVGELV AAYVAGVWSL EDACRLVAAR GRLMQALPEG GAMVSLQAAE DEVLPLLEGQ GTRVSVAAVN GPQSVVVSGD ESVVAGIADR FESEGRKVKW LQVSHAFHSP LMEPMLDEFR AVAESVVYAE PRIPVVSNVT GELATPEELM SPGYWVRHVR EAVRFADGVR WLEERGVTRF LEIGPDGTLT AMAQACADSA DLLLLPALRK ERLESEALVA AVGGMFVNGA EVQWQALFPG SRRVDLPTYA FQRESFWPSS PGTGGRDAAA QPADDGTGWF WDAVERDDPD ALTGELAIPG DASWDEALSA LSSWRRQQRA RSVVDGWRYR VQWKPLGAGA GEKLSGRWLV VVPEGLADSD WASSVVEGLV ACGVQVERVG CGRDVDRVAL AERFAGFEGD AVAGVMVLSG GVEGESSGGA PTSVWWTAVV VQALGDAGVG GRVWCVTRGA VAVGRSDGGP DPVGSAVWGL GRVAALELPD RWGGLVDLPG TLDRRAFDRL VGVVADGDED QVAVRASGVF GRRLVHAPAP SGDVAGGWQP RGTVLITGGT GALGGRVARW VAERGAEHVV LTSRRGLEAP GAVELEAELS GLGVRVTVAA CDVADRGAVE ELLSGCSVDA VVHAAGVVDS VPLGDVDAEH FSQVMGAKVS GAVVLDEALG DRELDAFVVF SSIAGVWGSG GQGAYAAANA FVEGLVEGRR ARGVVGCAVA WGPWSGGGMA GVDGAEEHLL RRGLRALDPS LAVSALESAV GAGEGSVVVA DVEWERFAPA FTSARPSPLL EDLPEAADAV GGMSTEASEG KGQSFVDRFA GVSPVERAQA VLDLVRGHTA AVLGFRDRKA VEAVRAFRDL GFDSLTAVEL RNGLNADTGM RLPATLVFDY PTPQLLAEHV HDAVFGAADV EPEAAVLADL DRLAGAISGF SPENAARGLV EARLRSMLAE LGGEGEAKSA VSQQLDAASD DEIFDFINQE LGRS //