ID A0A0B5EY37_STRA4 Unreviewed; 4385 AA.
AC A0A0B5EY37;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Type I modular polyketide synthase {ECO:0000313|EMBL:AJE87703.1};
GN ORFNames=SLNWT_7327 {ECO:0000313|EMBL:AJE87703.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE87703.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE87703.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP010519; AJE87703.1; -; Genomic_DNA.
DR KEGG; sals:SLNWT_7327; -.
DR Proteomes; UP000031523; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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; cd08952; KR_1_SDR_x; 1.
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; 6.10.140.1830; -; 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; 3.40.50.720; 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.
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; 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:SF51; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 3.
DR Pfam; PF16197; KAsynt_C_assoc; 3.
DR Pfam; PF00109; ketoacyl-synt; 3.
DR Pfam; PF02801; Ketoacyl-synt_C; 3.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF18369; PKS_DE; 1.
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; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 3.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
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; 2.
DR PROSITE; PS52004; KS3_2; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:UP000031523};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..419
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 903..978
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 998..1424
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2666..2741
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2761..3187
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 4230..4305
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1427..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4385 AA; 460145 MW; 120D411DD87D4093 CRC64;
MRDEHIAVIG MACRVPGAST PDEFWQLLRE GVSAITEIPA DRHAAELEDA GIRFGGFLDA
VDEFDPEFFG ISPREALAMD PQQRLALELC WEALESTGTD PAALRESRTG VFIGAIADDY
AALARRERTS VTQHTLTGLN RGIIANRLSY ALGLRGPSVA VDTGQSSSLT AVHLACESLR
RGESETAVAG GVQLNLAPDS FLAASAFGAL SPDGRCFTFD ARANGYVRGE GGGLVVLKRL
ADAERDGDPV LCVIRGSQTN NDGGGDSLTT PARQGQESML RAACAQAGIA PGAVQYVELH
GTGTRAGDPV EARALGEVLG AGRPAETPLR VGSVKTNVGH LEGAAGITGL IKTVLSLVHR
ALPPSLNHES PHPAIPLDEL GLRVQTAHED WTPPTGLPRL AGISSFGMGG TNVHVVLEEA
PGGETAEAAP ERPVPPRQVA WPLAGRSEAA LRAQAARLHT HLLSRPELHP LDVGYSLATS
RTAFAHRAVL TGSDRDTLLA DLHHLASGTT PAATALHGRT AFLFTGQGAQ RLGMGQELYE
TFPAFAAAFD AVCAELDQHL DVPVRDVVFG QDADALDRTV STQSALFALE VALFRLIESF
GVAPDFVMGH SIGEISAAHI AGVFSLEDAA ALTAARGRLM QALPEGGAMV SLQLPEADLL
PHLDGYEDRV SIAAINGPTA TVISGDEASV LEIAEATGAK TKRLRVSHAF HSPLMEPMLA
EFGAVASSLT YRTPRIPVVS NVTGGLADEE IATPDYWVRH VRQAVRFADG IEELAAREVT
RFVEVGPGGV LTAMAREGLP RTATDTGTDT GTGAAFVSLL RKDRPEAEAL FAALGQLHAH
GGDLDWHKLY QGRGAQRVEL PTYAFQRRRY WLDSPLPGAA EEAAPVSWRD RYLALGEEAE
RDRAALELVR AQTARVLGHD GPEAVPTEQV FKDLGFDSLM SVELCDLLST ATGSRLAGAV
LFDHPTPAAL ARHVQQVVTG TRGARTARPV VRRSASAEEP IAIVAMSCRL PGGVRSPEEL
WRLVSEGEDA IAAFPTGRGW DLEGLYDPDP GRHGTSYVRE GGFLYEADRF DAAFFGISPR
EAQAMDPQQR LLLETAWEAF ERAGIDPAVL KGSEAGVFVG AMPQDYGPRM DEAAEGQEGY
LLTGGTTSVA SGRIAYTFGL QGPAVTVDTA CSSSLVALHL ACQSLRQGEC TMALAGGATV
MSSPGIFVEL SRQKALSPDG RCKAFSSDAD GTGWGEGVGM VLLERLSDAR RNGHQVLALV
RGSATNQDGA SNGLTAPSGP AQQRVIRQAL ADAGLSGEEV DAVEAHGTGT SLGDPIEAGA
LLATYGQDHS PQRPLWLGSL KSNVGHPQAA AGVAGVIKMV MALRHGVLPR TLHVREPSPH
VDWSSGAVAL LTEAQAWPEA GRPRRAGVSS FGISGTNAHA ILEQAPLEPQ ESPEPKPEPQ
APEQEQAEAA EAGAFVLPWV LSGRTEQALR ERAEQLLTHL SASPGTDPAD SESADAESAD
ADLADVAFSL ATGRAAFDHR AALVGRDREE MLAGLAALAQ GGSAPQLAQG AGGGGRGAVF
VFPGQGSQWI GMASALWDSS PVFAAQLEAC LEALEPFLDW SLRDVLRGEE GAPSLSRIDV
VQPALFTVMV SLAALWRAHG VEPVAVVGHS QGEIAAAYVA GGLSLQDAAR VVARRSQAWY
ELSGKGGMLS VLDSAEAVAE RLEQWSERLG IAAVNSPGAV TVSGDPEALD AFMAELSADG
VKSRRIPGVD TAGHSPQVDA LRERLLREVA GVAPVASRIA YYSTVTGGAL ETTALTAEYW
YRNMREPVDF ERTCRALLAD GHTAFVECSP HPMLALPLQQ TIEAAGADAV VVGTLRREEG
GRERFAGAFA EAYAQGVRPE WGAVFAGRGA RRIALPTYPF QRQRYWLDKP VAAGEVAAAG
LDAAGHPLLG AVVALAGGQE YLLTGRLLAQ GQPWLAEGAE SGTAVVPGSV FAELAVQAGD
RCGCPRIDEL SLSAPLLLPA RGAVLLQVRV GAPDEQGRRD VSVHARAQGA DADEPWTAHA
TAVLTTDGGA HVDAAGGEFG DGAAVWPPAG AVPVAGAVGA WRLGQEVFAE VALNEAESAE
AAAYALHPVL LESVLAGLEL PDVPGGLRLA SQWRGLVLHA GGASALRVRL SPVGAGAFAL
AAQDTEGRAV VTAESVTLRA LDEGELAGNS GRHPSLFRLG WPVLRAEGGQ EARLAVLGED
TLALGAATGA QVFEESEQAP QAVLVPLTAG GDQVAEAAHE AAHRALALIQ RWIAEEQLAD
TRLVFVTRGA LAAVEGEEVP DVAHAAVWGL VRSAQSEHPG RFVLVDLDGH PGSAPALRAA
LASGEEQCAI RAGEIRVPRL ARTAANAEAA EAASRALDPE GTVLITGATG TLGGLLARHL
VTVHGVRRLL LISRRGPAAE GMDELRTELG ASGATVTVAA CDAADREALA RLLAEIPAAH
PLTGVFHAAG VLDDGVVDAL TPERLDAVLR PKADAAQNLH ELTAEADLAA FVLYSSVVAT
IGNAGQANYA AANAFLDALA QHRRARGLSG QSLAWGLWEQ ASGMSGHLAE ADVQRMARSG
VRPLPSTLGM ELFDAARTAG DATLVPVLLD LTELRRRAAG GETPPAWLRG LVHTPPRRLV
RARTGQEQDT SFGATLAALA PAMRESFLLD LVREHAAAVL GLASPEDIAA GRAFREVGFD
SLTAVELRNR LNAATGLRLP ATLLFDYPTP AVLVGHLRTE ALGEEAATVE VSAPVRGADA
DDPIAIVAMS CRLPGGARTP EELWELVAEG RDVISGFPGD RGWDVEELYD PNPGTPGRSY
AKEGGFLYDA YDFDADFFGI SPREALAMDP QQRLLLETSW EALERAGIDP HSTRGTAAGV
FIGSTGQDYA SQLREIPEEM EGYLLTGKAA SVVSGRIAYS LGWEGPALTL DTACSSSLVA
IHQAAQALRQ GECTLALAGG TTMMSTPSLF VEFSRQRGLA PDGRSKAFSS DTDGTSWGEG
VSMVLLERLS DARRNGHEVL ALVRGSAVNQ DGASNGLTAP NGPSQQRVIR QALAHAGLSA
DEVDAVEAHG TGTRLGDPIE AQAILATYGQ GRESERPLWL GALKSNIGHT QGAAGGAGVI
KMVMAMRHGL LPRTLHVKAP TPHVDWSAGE VELLTEARPW PRSERVRRAG VSAFGISGTN
AHLILEEAPP AEPVEVITPE EATTEEGSLN GASWPLTWPL SGHTAAALRA QAARLHTHLQ
NRPELHPLDI GYSLATSRAA LDHRAVLVGT DREQLLAELG QLATGMTPGT TAQEGRTAFL
FTGQGAQRLG MGAELYETFP VFAAAFDAVC AELDRHLDIP VRDVVFGQDA DALDRTVSTQ
SGLFALEVAL YRLVESWGVA PDFVMGHSIG EIAAAHIAGV LSLEDAATLT AARGRLMQAL
PQGGAMVSLQ LPEAEVLPHL EGFEDRVSIA AINGPASTVI SGDEASVLQI AEATGAKPKR
LRVSHAFHSP LMEPMLAEFG KLAATLTYHT PHTPVVSNVT GTLADDDIAT PDYWVRHVRQ
AVRFADGVRY LHGQDVARFV EVGPAGVLAA MARESLPDTG TGNGTGAGAG TGTGAGAAFV
PLLRKDRPEA EALFAALGQL HAHGGDLDWH KLYQGRGAQR VELPTYAFQR KRYWFAAPEE
TGSEAAAGAG SVEARFWDAV EREDLAELTA ALQVDERTRL GELVPALSSW RRGQSDRAVL
DSWRYRVSWY PVADSGQSSL SGGWLVAVPA AQAASEPVEW ALSGLRERGA RVVPFPVAGQ
EPAELAGRLR EAAAEGRFAG VLSLLALDET PYPEHPSLSA GLVGNLALVQ ALGEAGIAAP
LWLATRGAVS VGPSDPLNGW TQAATWGMGR VVALEHPQRW GGLVDLGAHL DARAADRLCA
ILSGLEGPSG VEDQLALRDG GVLVRRLVKA PVRDTGEKGF TPHGTVLITG GTGGLGAQVA
RRLARGGAGH LVLTSRRGEA APGAAELREE LLALGADRVT VAACDMAERS EVAALIEQVT
ADGEAVRAVF HAAGVVEFAQ LAQSAPADFA RMADGKVRGA GYLDELLDPE RLEAFVLFSS
IAATWGSGGQ SAYAAANAQL DALAEHRRAR GLPATSVAWG PWADEGMIEQ GEVAEHLSRR
GLPAMEPRLA VAALTEALEG RETSLVVADV RWERFVPGFT SARSRPLLGE LAEVRAVLAA
PAAGESEWAE EEAHGFLEGL AGLPAQEVER ALRDLVHAQT AAVLGHSSPE VVATGRAFKE
LGIDSLTSVE LRNRLGALTG LELPATLVFD YPAPAPLAGY LREELLRGRP DEALSVFEDL
DKWESALPEL LADEAVRDRL AGRLHALVAK LGAPPEQGAG SVDSSLISAT ADEVFDFIDN
EFGAS
//