ID A0A1B4Z9A6_9ACTN Unreviewed; 2480 AA. AC A0A1B4Z9A6; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 31-JUL-2019, entry version 17. DE SubName: Full=PKS (KS-AT-DH-ER-KR-ACP-TE) {ECO:0000313|EMBL:BAV56012.1}; GN Name=flvP3 {ECO:0000313|EMBL:BAV56012.1}; OS Actinomadura fulva subsp. indica. OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae; OC Actinomadura. OX NCBI_TaxID=1752060 {ECO:0000313|EMBL:BAV56012.1}; RN [1] {ECO:0000313|EMBL:BAV56012.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 53714 {ECO:0000313|EMBL:BAV56012.1}; RX PubMed=26818633; DOI=10.1080/09168451.2015.1132155; RA Miyanaga A., Hayakawa Y., Numakura M., Hashimoto J., Teruya K., RA Hirano T., Shin-ya K., Kudo F., Eguchi T.; RT "Identification of the Fluvirucin B2 (Sch 38518) Biosynthetic Gene RT Cluster from Actinomadura fulva subsp. indica ATCC 53714: substrate RT Specificity of the ?-Amino Acid Selective Adenylating Enzyme FlvN."; RL Biosci. Biotechnol. Biochem. 80:935-941(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; LC095592; BAV56012.1; -; Genomic_DNA. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.1200.10; -; 1. DR Gene3D; 3.10.129.110; -; 1. DR Gene3D; 3.40.366.10; -; 1. DR Gene3D; 3.40.47.10; -; 1. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. 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_N. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR032821; KAsynt_C_assoc. 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; IPR020801; PKS_acyl_transferase. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR020807; PKS_dehydratase. DR InterPro; IPR042104; PKS_dehydratase_sf. DR InterPro; IPR020843; PKS_ER. DR InterPro; IPR013968; PKS_KR. DR InterPro; IPR020806; PKS_PP-bd. DR InterPro; IPR020802; PKS_thioesterase. DR InterPro; IPR015083; Polyketide_synth_docking. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS. DR InterPro; IPR001031; Thioesterase. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF00698; Acyl_transf_1; 1. DR Pfam; PF08240; ADH_N; 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; PF00550; PP-binding; 1. DR Pfam; PF14765; PS-DH; 1. DR Pfam; PF00975; Thioesterase; 1. DR SMART; SM00827; PKS_AT; 1. DR SMART; SM00826; PKS_DH; 1. DR SMART; SM00829; PKS_ER; 1. DR SMART; SM00825; PKS_KS; 1. DR SMART; SM00823; PKS_PP; 1. DR SMART; SM00824; PKS_TE; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 3. DR SUPFAM; SSF52151; SSF52151; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR SUPFAM; SSF53901; SSF53901; 1. DR SUPFAM; SSF55048; SSF55048; 1. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. DR PROSITE; PS50075; CARRIER; 1. DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Phosphopantetheine {ECO:0000256|PROSITE-ProRule:PRU00258}. FT DOMAIN 2103 2178 Carrier. {ECO:0000259|PROSITE:PS50075}. FT REGION 463 530 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COILED 11 31 {ECO:0000256|SAM:Coils}. FT COMPBIAS 490 530 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT MOD_RES 2138 2138 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000256|PROSITE-ProRule:PRU00258}. SQ SEQUENCE 2480 AA; 261632 MW; FE91EDE488158C28 CRC64; MADEEKLLAY LRRVTEDLQQ ANRRLRDVET KEREPIAIVS MACRYPGGVN SPEDLWNLVL NREQGIVPFP KDRGWDLEAL YDPDPDTSGT TYARAGGFLD GADEFDAAFF GISPREAVAM DPQQRVVLEV AWELMERAGL HPGSLRGTPT GVFIGAFAND YEVGRGPLPE GSEGYLGTGN SSSVISGRVA YTLGLEGPAV TVDTACSSSL VAIHLACQSL RNGESTLALA GGVTIMATPE LLVDFSHQRG LARDDRCKAF SDEADGTVLS EGVGVLLLER LSDALAGGRR VLGVIRGSAV NQDGASNGLT APNGPSQERV IRQALANAGV CAGEVDVVEA HGTGTALGDP IEAQALLATY GRDRDAGVPL WLGSVKSNIG HSQAAAGVAG VIKMVQAMRH GVLPQTLHVS APTSHVDWEG GGVRLLDRAR EWPRLGGRPR RAGVSSFGVS GTNAHVIVEQ APDPEPRQEQ APDAQPQQEQ APDGQPRQAF ELEPRQDVRP QEDTHEDLRE GAQEDVRAGA REDVRAGARE DVRAGAQEDL REGVRVGVPV VSGVVPWVVS GRGVAALRAQ AGRLVDFVEA RAGLPVAGVG LSLVRGRAVF EDRAVVLGGD RQELLTGLRS VAAGEPDTGP VPGPVSGVVS GVVSGSRDAV LVFPGQGAQW VGMGVELAQA SPVFAARLGE CFGEIGRWVE WDPAGVLADP AGAGLASIEV LQPVVFAVGV ALAALWESVG VRPAAVVGHS QGEVAAACVA GVLSLADAVR VVVLRSRLFA RRLQGRGAIA AVALPADVVR EEVAAWGGVL EVSADNGPTS CAVAGSLPAL EEFVERVRGR GVRARVIEAT VASHSSMVEP LRDELVGMLG GVAARQGRVP FYSTVTGGLV DGGGLGAEYW FANARRPVVF QQAVRALLAD GRTGFIEASP HPVLTMAVQD ILDESGASGV AVGTLRRDEG GAQRFARSVG EAFTAGIDVD WQRFFTGADS ARPVGLPTYA FQRRRYWLEA GPGGGLDAGG LGQSGVDHPL LGAVVELPGQ DGVVLTGRIC VGTHPWLADH AVGPAVVFPG TGFVELVLRA GDEVACPVLE ELTLETPLVI DGGESVQVQV AVTAAGQGGR RGVSVYARTG QQPWTRHATA TLTTTSTTDH GQWGQWPPAD AEAVDVSSHY ETLAAAGYGY GPAFQGLKRA WVRNDEVFAE VELGEREAAE ASRYGIHPAL LDACLHATGL TGERAEGVAL PFAWSGVELL ASGAQHVRVH VVPAEGGAEG GAAGIRIADG TGAPVAVVSS LVSRPLPADG LSSRARNGHE ALHRLQWVMP PSWNPPHVGG AIAVIGTVGE DDALTEALHR NGLKVRSYAD LQAASTDKDV TTLVIPCPTR QPDDQGPLED LRSELDRVVA VLGGWLADER LAGTRLVLVT TGAVTVDTGT LDAGGLVGAA VSGLVRSAQA ENPGRILLID LDHTPESLTA LATLLAVEDE PQIAIRSGRV LVPRLARADS GDDLPLPGGA GGWRLDCPAK GSIDGLKLIP APEADRDLAP GEVRVQVRAA GLNFRDVVVT LGMVPEQGGA IGGEFAGVVA EVGPEVEGLR VGDRVMGLGE GTFGPRLVAD RRMVARMPFG WGFARAASVP GAFATAWYGL VDLAGLARGE RVLIHSGAGG VGMAAIQIAR HLGAEVFATA SPGKHHILHA LGLPDDHIAS SRDLDFARTF PRVDVVLNSL AGPFTDASLN LLTEDGRFIE MGKTDRRDPD HVAATHPHAC YRSFDLMDAG HERIGQILNH LLHLFTEREL AALPVRCWPI QQARHAFRHM AQARHTGKIV LTVPHAMDRE GTVLVTGGTG GLGAILTRHL ADHHQIKHLL LASRRGEQAP NADQLRTDLE AAGASVDIVA CDLSDPSQIT TLLDRVPAEH PLTAVFHTAG VLDDGTITSL TPDKFDRVLS PKADAAWHLH HTTRHLDLAA FVLYSSSAGT LDSAGQGNYS AANAFLDALA IHRQTTGLPA QSLAWGLWHQ PSGMSAHLTT TDITRIQQAG YHPITTTQGN QLLDTALTTP QPHLLPLPIN TRTLTKRHDG IPPILRGLVH TPTRRTANTA TTATNQSALQ QHLAGLSPVE QVGELTMLVR ECAAKVIGYS EPEAIRSEQN FLEAGFDSLT AMELRNVLNK ATGLRMPATA VFDYGTAAAL ARYIADEISF DAEIARTPSS GAAGPDAGGM LASMLRDAAP AGKLREGLEM LEAAAKLRPS FRRLDDLDRS YRPLALASGP ALPKLFCFST PMALGGAAQF ARLAVHFQGV RDLYALQVPG YAPDDSLPDT VDVIVRMWAE SIQETAGDDP FVMIGYCGGG NFAHAAVTYL EQKGVRPQGL VLLDTFLPGS EVIDELGGQM LEGMFDRAET FGPFSDTRMT AMGRYYRLFR ETEVVDVETP VLFLRPDTPL PSGPDGERSR VGNWRASWHL EHDLCEVRGD HLTMLEGEAG SIAQAIEEWL KPSDGRSNGA //