ID A0A2K8P9Y8_STRLA Unreviewed; 3491 AA.
AC A0A2K8P9Y8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Erythronolide synthase, modules 1 and 2 {ECO:0000313|EMBL:ATZ23551.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:ATZ23551.1};
GN Name=eryA9 {ECO:0000313|EMBL:ATZ23551.1};
GN ORFNames=SLAV_08355 {ECO:0000313|EMBL:ATZ23551.1}, SLLC_06385
GN {ECO:0000313|EMBL:QUQ53382.1};
OS Streptomyces lavendulae subsp. lavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ23551.1, ECO:0000313|Proteomes:UP000231791};
RN [1] {ECO:0000313|EMBL:ATZ23551.1, ECO:0000313|Proteomes:UP000231791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ23551.1,
RC ECO:0000313|Proteomes:UP000231791};
RA Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT 3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT angucycline-type antibiotic auricin.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QUQ53382.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Del-LP {ECO:0000313|EMBL:QUQ53382.1};
RA Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA Kalinowski J., Kormanec J.;
RT "The linear plasmid pSA3239 is essential for the replication of the
RT Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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; CP024985; ATZ23551.1; -; Genomic_DNA.
DR EMBL; CP073778; QUQ53382.1; -; Genomic_DNA.
DR KEGG; slx:SLAV_08355; -.
DR Proteomes; UP000231791; Chromosome.
DR Proteomes; UP000676025; Chromosome.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd08952; KR_1_SDR_x; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 6.10.140.1830; -; 1.
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; 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; 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; IPR013968; PKS_KR.
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; 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; PF18369; PKS_DE; 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; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 2.
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; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ATZ23551.1};
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:UP000231791};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ATZ23551.1}.
FT DOMAIN 35..461
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1750..1825
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1846..2271
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3308..3383
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 464..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3471..3491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3491 AA; 359630 MW; 9164DC1A152FE117 CRC64;
MAGANEEKLL ENLKWMTTEL RRSRRRLQEV EQDAREPLAI VAMSCRFPGG VRSPEDLWRL
VSEGGDAITG FPDDRGWDIA SLADPDPDRK GTFYNTGGGF LTDATRFDPA FFGISPREAL
AMDPQQRQIL ETSWEVFERA GIDPATVRGS RTGVYIGAGA MGYGADLREV PEGLEGLLLT
GGATSVLSGR VSYVLGLEGP AATIDTACSS SLVALHLAGQ ALRQRECSLA LVGGVCVMPT
PDVFVEFSRQ RGLAADGRCK SFAAAADGTG WSEGVGVLLV ERLSDAQRNG HPVLAVVRGS
AVNQDGASNG LTAPNGPAQQ RVIRQALENA RLSAAEVDAV EAHGTGTRLG DPIEAQALLA
TYGQDRPEDR PLRLGSLKSN LGHTQAAAGV AGIIKTVMAI RHGVLPQTLH VDEPTPDVDW
SAGAVSLLTE AMPWPETGAP RRAAVSAFGV SGTNAHTIIE QAPEADTAEQ PPHGAQPGGA
SGTGTGSAAP VTASATASVR PTLLPWTLSG RSAAALRAQA ARLVAARTAD AAAGSALDLG
LSLATTRAAL EHRAVLIGRT GDDLDSALAA LAAGEEAAGL VTDTAAEGRT AFLFTGQGSQ
RPGMGRELYA SQPVFAAALD ALCARLDIRL ELPLKEILFG SDAALLDRTE YTQPALFAVE
VALFRLLESW GLKPDFVSGH SIGEIAAAHV AGVLSLDDAC TLVAARARLM QELPASGVMI
AVQASEDEVL PLLTDRVSIA AVNGPASVVI AGDEDAATAI VEAFPDRKSK RLTVSHAFHS
PHMDGMLADF RRVAEGLTYE SPRIPVVSNL TGALVTDEMG SAEFWVRHVR EAVRFLDGVR
ALEAAGVTTY VEIGPEGVLT ALAQDCVSGE GAAFVPALRA GRPEPETVLA ALARVHAHGG
TVDWAAYFAG TGARTVDLPT YAFQHERYWL EPGADTAGDV SVAGLDPAGH PLLGAAVTLA
GSDRLLCTGR LSVRGHAWLA DHTVAGAAVL PGAAFVELAV RAGDQADCGH IEELVLDAPL
ALPADGGVRI QVLVEDADER GRRTFTVSAE RAGGTAEDSG WTRHAHGVLA PAAAAGSAGP
AASFDLAEWP PAGADAVDLS RLYDADTAGG LRRGPVRGPL FQAVEAAWKR DGEYFAQVRL
PEGAAQEAGF GLHPILLDTA AHLATVLADT DADADTDTDT APDGGNGVGP GSVWSDVALH
AVGAGALRVR VRPAGEGAFA LDLADDLGDP VATIGRLAPR PHTPAATDAT DPVPAVVREA
LFRLDWTPLA VPATATAPAG GWAVLGDTGF GPAVRYAGLA ELGEAVDAGT PVPAYVLAPF
PRQADGPDAL SGAAQRALAL VRAWLADSRF ETARLVLVTS GAVAGPGEGA EDLPHAAVRG
LLRSAETENP GRFVLADIRD LGEAAGSAEA AGSAGSADLA VLAAALDSGE PELLLRDGAV
HVPRLRRAAT AATVTADATA GAVIDPDGTA LITGGSGTLA GIVARHLAGT HGVRNLLLLS
RRGADAPGTA ERTAELDALG ARVTWAACDA ADRDALATVL AAIPAEHPLT TVVHTAGVLD
DGVIGSLTPE RLDTVLRPKA LAAHHLHELT RDLPVTAFVL YSAIAGTLGA AGQSNYACAN
AYLDALAELR HHQGLPATSL AWGLWAEAGG MIGTLDEAQL RRMEQHGMGA LTAADGMALL
DAALASGRSV LVPARLNLPA LRAAAAPGPV APVFRELLGR AGRRTARTRD DAGTSLTDRL
TSLTRSERDR VLLDLVRAQV ASVLGHASAE RVEPGKAFKD LGFDSLTAVE LRNRLGAATG
LRLATTLVFD HPSPVALARL LYCELLGDEE TGSGAEGVRS AEAAEDDPIA IVAMSCRYPG
GVRNPEELWR LVAAGGDAIG GLPGNRGWDT AELYAGQGGD GRAFEGGFLY DADSFDAEFF
GISPREALAM DPQQRLLLEA SWEAIEGAGI DPSSLRGSRA GVFVGASYTG YDAQLERSAD
ADGVLGHVMT GNAGSVMSGR VSYALGLEGP AVTVDTACSS SLVALHWAIQ ALRNGECTLA
LAGGVTVMST PGTFSEFSHQ GGLSPDGRCK AFAAGADGTG WGEGVGMLLV ERLSDARRNG
HPVLAVIRGS AVNQDGASNG LTAPNGPSQQ RVIRAALANA GLSAAEVDVV EAHGTGTRLG
DPIEAQALLA TYGQERAEGQ PLLLGSIKSN IGHTQAAAGV AGVIKMVLAM RHGVLPQTLH
VDAPTPHVDW TAGEVTLLTE PTPWPQTRRA RRAAVSSFGI SGTNAHTIIE AAPDAPEDPT
PTTPATGPVP YVLSARNPSA LRDQAARLLP VAEAGDCALV DLAHSLATGR AGLEHRAAFA
AADREGVLRA LAALAADEPA PGLFRGTVSG GGLAFLFTGQ GSQRPGMAHG LYETQPVFAT
ALDGVCARFS LELPLKDVLF GSDAEVLDRT EYAQPALFAV EVALFRLLES WGVRPDFVSG
HSVGEIAAAH VAGVFSLEDA CTLVAARGRL MQALPAGGVM IAVQASEDEV LPLLTDRVSI
AAVNGPTSVV VAGDEDAAVK VAEAFPDRKT KRLTVSHAFH SPHMDGMLDG FRKVAEGITF
AAPRIPVVSN LTGALVSDEM GSAGFWVRHV REAVRFLDGM RALEAAGVTT YLELGPDGVL
SALAQDCVTE DAATFAPLLR KGRGEAEALA GALAQVHTRG VTVDWTAFYA GSGARRVDLP
TYAFQPVRYW PEPTAPRGVA PAAGAGSEAD ARFWEVVERA DLTAFADEFA VDGEQPFRSV
LPALAAWRRD RQAQAEADAL LYRVSWQPFA GQDRGALTGT WLVAVPAAQA EDPWVRALTD
RIGAEGARVL PLPLDVADGD PAVLRTGLDG LLREAATDPG TGAVTGVLSL LALDERPHPE
HPGVPVGLAL TAALTSVLTS EPAGPGAELA DAPLWCVTRE AVAAAPGDTL GGATQAQVWG
LGRVFALEHP DRWGGLLDLP AVCDERVLSR LPAALTAAGD EDQLALRATG TLVRRLVRGT
TAADADGTRT GSGWNPCGTV LITGGTGALG RHVARRLAER GAEHLVLVSR SGARAPGASE
TRTELEALGA AVTLAACDVT DRDALAALVA GLAADGTPVR SVVHAAGISQ PPGTGTDLPG
FARVVTAKTA GAVHLDALFD TPDSLDAFVL FSSIAGVWGS GGQAAYAAAN TFLDTLAERR
AARGLAATAV AWGPWAEAGM ATEGDATEQL TRRGLPPVAP ATNLTALDRA LAGRDAAVTV
ADVDWARFAP VFAAARPRPL VGDLPEVREA LRGETADGAT PTGDGTAADA GATLLRRLGE
LSGEDRDSAL LDLVREHAAA ALGHPSADAV APDRAFKDLG FDSLTAVELR NRLGAACGLR
LPSSLVFDYP NPQALTRHLL RTLLPEGSGG GAAAAAVADL DSDPLDAELR RTLAAIPMGR
IREAGLLDTL LGLAGSGSDT TAASGPGARA ADAGESIDTM DLQDLLDLAL DGGGLDDDGP
TGDTTTSNSN F
//
