ID A0A1V2RFT7_9ACTN Unreviewed; 2870 AA.
AC A0A1V2RFT7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Erythronolide synthase, modules 3 and 4 {ECO:0000313|EMBL:ONK11248.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:ONK11248.1};
GN ORFNames=STBA_19780 {ECO:0000313|EMBL:ONK11248.1};
OS Streptomyces sp. MP131-18.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK11248.1, ECO:0000313|Proteomes:UP000189065};
RN [1] {ECO:0000313|EMBL:ONK11248.1, ECO:0000313|Proteomes:UP000189065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP131-18 {ECO:0000313|EMBL:ONK11248.1,
RC ECO:0000313|Proteomes:UP000189065};
RA Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT "New natural products identified by combined genomics-metabolomics
RT profiling of marine Streptomyces sp. MP131-18.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ONK11248.1}.
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DR EMBL; LZNS01000001; ONK11248.1; -; Genomic_DNA.
DR RefSeq; WP_077058869.1; NZ_LZNS01000001.1.
DR STRING; 1857892.STBA_19780; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000189065; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 2.
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; 1.
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; 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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
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:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ONK11248.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000189065};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ONK11248.1}.
FT DOMAIN 6..436
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 976..1051
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1078..1487
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2733..2808
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2816..2848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2870 AA; 295362 MW; 1B505BCDA2DB5568 CRC64;
MRSDGDQAVA IVGAGCRFPG GGSGPEGLWR LLLRGTDVIT EVPRSRWDLE RYYDPDPDTP
GTMYTRWGGF LPDIERFDAA FFGIAPREAR QMDPQQRLLL EVAWEALEDA GIRPGDLSGT
RTSVFTGGLG VDYFLAHARD AGIAGIDPWY ATGKESSFTS GRLSYLLGLN GPSLSLNTAC
SSSLVAVHLA RQSLLTGESD AALVGGVNLL LSPELTVFMC KAGAMAPDGR CKVFDAGANG
IVRGDGCAVL VLKRLDDALA DGDDVLAVIR GSAVNHDGQS AGLTVPSATA QQRLITDALT
AARIHPHDVG YVEAHGTGTP LGDPIEAWAL GDVLARGRSA EDPLVIGSVK ANLGHTDGAA
GITGLLKAAL VVRHGRIPPH LHLKEPNPNI AWDQWPLRVP PTEGPVDWPG PAGRPRIAGV
SAFGLSGSNA HVLVESPPER ATAPGARAGG TDGRALVLPL SARSAAALRD LAAAHRDRLG
GQEAEEREGA DGFADVASFV RTAAVRRTHH AEHRLAVTGG SAAELAAALD AFTAQAPVVG
ERAGPGGVCF VFSGQGGQWA GMGLRLRAAE PAFREALDRC DALIREAAGW SVVEELSADG
DASRLADTEI AQPVVFAVQV ALAALWRSWG VEPSAVVGHS MGEIAAAHVA GALDLADAVR
IAVLRGRLLQ HAAGQGRMAA VALPEDETER RLAPYGERLC VAAANAPGST VVAGEPDAVE
EFTATLKAEG LTCRTLPGGY AFHSPQMAPF EPELVGLLDG LAPHEPRVRI VPTTPGDGRF
DAAHWGRNVR RPVRFAGAVA ELLDAGHRTF VELGPHPVLA QPLTQSLEAA GLDGTVVPSL
RRDTDDVDTA RASLAALFTA GADVAWDAVA PAGEGVDKRL PRYAWQGERL WFETPQAAGP
DAQVAAGGLA ALHGELRLYD AAGRVVAEAT GLRLGAPGDG APTAAAVPGA PAVPAVPAVP
AVSAAVETAG HRPDPAELAD LVARKAAAVL GLPQGGTPAR TQGFTELGMD SLGTVELARQ
LQQALGVRVP KTAALDHPTV ERLAAYLDTR LAAAPAARAQ APAAVPAPGP VAAGVTGHEP
IAVIGLGCRF PGGASGPDAY WRMLRAGTDA IRPAPEGRFG GSRVWHGGFM EGVDEFDAPF
FRIPPREARV MDPQQRMFLE VAWEALEHAG QPPAALAGTR TGVFLGMNST DYAGIVTAHP
GNVDAFYGTG NSFTAAAGRL SYLLGVHGPS LAVDTACSSS LVAVHLAVAS LRSGESELAV
AGGVNLILSD VIHRSTSAMG ALAADGRCKT FDASADGYTR GEGCGVVVLK PLSAARADGD
DVLAVLLGSA VNQDGPSSGL TVPNGPAQED LLRRALADAG VAPGEVGYVE AHGTGTPLGD
PIELQALGAV LGERDGSCLV GSVKTNVGHL EAASGVAGLI KTVLALHHRE IPPHLHFTEP
SPDIPWDELP LAVPVEPTPW APGAARRVAG VSAFGFSGTN AHVVLAEPPA GAEPERGAAP
GGAAAGERRV HALPLSAAGR NALLAQADAW GALLADGDDG AAPALEDLAY TAALRRTHLE
HRVVVVGDDR RQLAERLAAF GRGEDVPGVA AGQAGAEPRR GPVFVFSGHG SFWRGMCRDL
LRESPVFREA VERCDRALRP HLDWSIAEVL AQGHEPAAEL DQQFLLFGVQ YALTQVWRGL
GVEPAAVTGH SMGEVSAALC AGALDLGQAV EVMVHRTEVL KDLMGRGGMA VVGLDAERTA
EELTGYEDRL CVSIVNSHRS TVISGETAAL EEVGARLKAR NVFFRPVAAG APAHSPVAEP
MRRELVARLA GLRPAEPVVP IYSSVTGGPV DGPLDAEFWG RNLRHTVWYA DAVRALAADG
HTTFVELSPH SLQLAPTEHE LDAAGVADRL LVPSLTRDSD GPVALMTAFG TLHATGRPVD
WERLHPAGGR LAAAPRYPWQ HKRYWVEHEA APGAAPAFGG AAGGGARHPL LARELRAAGG
PRTRIVEADV DAELAAGTGA EPVGGHLRLP AAAWLEMALA AVAGEGGRVR RLEDVSLPGS
CLTDPAVGSV AQLTLTPEPG GAFAFAVHAR AAGDGEGPAR PLAAGRAVPG SGSAAPGAVP
APGVRGAPDA RVTEWFAARG GGGALRAVSA VRGADAVEVE VECAPTALRW RMRPDVLDAA
LRLPALLGNA DEAARDVLPW HIASAAVYGT PGQRLLIGAR RTPGADGELC ADVWVATPEG
GLIAEARGVR LAPPPGRLLD AAELRSVADS FYRVDWRERP HEAAGAAEAQ EPAEAAGGWL
LLADGGGVAQ ALAGLLEERG GTVEVLAGAR EEAEVTAALR ALHRGPGCRG VVHLAALDLP
EGAPAADGLA AAAAVAASVP AVAAAAQAVT GAAGGARVHY VTRGAVTVGA GEPPAPLHAP
VHRLAGVTGV ERPAVWGGVT DLDPFGDGPA QDASWLLAEL LAPDGEDHLA VRAGRRLGAR
IVRCAEPEPV LVPPAPRADR TYLVAGDDGG LAERLAAWLT ERGAGRVVAA GPLADPGTAR
DTAGALVKEA EQAGAPLAGV VWAGADWNLG PQGAAPPAAD EVGRLLAERA AGAWLLHDVC
TEAGLDLDLF AVFTSVAALW GAAGAGHQAA PDALLSALAA HRRALGLAAC ELAWAPWDGV
GRLDENSRSL LLRSGLEPLS PEAGTRLLDH ALAGAHDAVA AAAVDWSLLL PLYQQSLRWP
LFDEIAASAL AAPDGTDELL ARLAALPPGE RDDLLLDLVL AEVAVVLGMD GADDLEPRQG
FFEIGVSSIT AVELRIRLER RFACALPATL AFEQPTAEAV ARYLAADVLG LPAADATGTG
SGTGTGTAPQ PEEEAAAQPR PESAGDGDDL LALLDEQISA VNDLLGKGAF
//