ID A0A0B5EGY4_STRA4 Unreviewed; 3727 AA.
AC A0A0B5EGY4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:AJE80649.1};
GN ORFNames=SLNWT_0273 {ECO:0000313|EMBL:AJE80649.1};
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:AJE80649.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE80649.1, 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.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP010519; AJE80649.1; -; Genomic_DNA.
DR KEGG; sals:SLNWT_0273; -.
DR Proteomes; UP000031523; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; cd05195; enoyl_red; 1.
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; 3.40.50.11460; -; 1.
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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
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; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR036299; Polyketide_synth_docking_sf.
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; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
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; SM00829; PKS_ER; 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; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 5.
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; 1.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000031523};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..463
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 1574..1999
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3569..3644
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2562..2582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..36
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3727 AA; 388855 MW; DFFFD906DA622054 CRC64;
MTELSNTNED KLREYLKRAT TDLRNARRRV RELEEPEPVA VVRMACRFPG EVASPEELWD
LVAEGREGIS GFPEDRGWDL EALYDPDPDR AGTSYTQRGG FLQEVPQFDA QLFGISPREA
LAMDPQQRLL LETAWEVLER AGIDPHSLKG SSTGVFVGAS SSSYGGDLEE VPEGVEGYLG
TGSAAAVVSG RLAYTFGLEG PAVTVDTACS SSLVALHLAV QALRQNECGL ALAAGVTVMS
TPGLFVEFSR QRGLASDGRC KAFGDTADGT GFAEGVGVLL LERLSDARRN GHEVLAVIRG
SAVNQDGASN GLTAPNGPSQ RRVIKQALAN ARLEAAEIDA VEAHGTGTTL GDPIEAQALI
ATYGKGRAPE RPLWLGSVKS NIGHTQAAAG MAGVMKMIMA MRHGVLPRTL HADSPSTKID
WSAGTVRLLQ EDTPWERRED APRRAGVSAF GVGGTNAHVI LEQDTPAEPA PEAPAAEPAP
RVLDTRLLPW LVSGKNPGAL RAQADRLHGF ATASEAAPAD IALSLATTRA ALEQRGAVVA
ADRAALASGL TALADGTSSP AVVQGTTLPG AGVVFVFPGQ GSQWPGMAVE LLDSSPVFAA
RLRECAEALA PYVDWSLLDV LRQADGAPGF DRVDVVQPAL WAVMVSLAEL WRASGVRPAA
VIGHSQGEIA AAAVSGALSL GDAAKVSALR AKALLALAGK GGMVSVAAPA AEVTTRIAAW
GERLAVASVN GPQSTVVSGE PGALDELLAA CERDGVRARR INVDYASHGP QVETIREQVL
TALDGIRPGR TGVPFLSTVT GEFVTGTELD AAYWYTNLRN TVRFEDAVRT LLAEGHGLFI
EASAHPVLTV GVQETLDDAG QPAATLGSLR REEGGPGRFL TSLAEAWTRG APVDWPRLLG
GPGTRTVELP TYAFQQERYW LESDPAAESA GGLPADEIEA RFWDAVERED LEELAGTLDV
DEDGDHGLSR LLPALASWRR RRREGAEIDR WRYRVEFTRL GDPGQARLDG TWLLVVPEGA
DTLAASCAGA LERHGADTLT LPAATADRTA LAETLGALAG TPLAGVLSLT GLAAEDPALL
TLTLAQALAD AGLTAPLWCA TRGAVSAVRG DAPATPAQAQ VWGLGRVLAL EAPRTWGGLI
DLPAAPDERA LTRFVQALAA SGEEDQIAVR DTGLYGRRLV RARLADRESG HEWRPRGTVL
ITGGTGGVGA HAARRLASLG APHLLLTSRR GPQAPGAAEL IRELGELGAR ATVVACDAAD
REALAAALAS VPEDAPLTAV LHAAGVPQST PFDALTPEEF AEVTAGKVRG AEHLDALLGD
TPLDAFVLFS SNSGVWGAAG HTAYAAANAH LDALAEQRRA RGLRATSLAW GAWGGGGIMD
TEGARAYMAK RGVLEMEPAT ALTALLRAVD HEETFLAVAD VDWARFAPGF TSGRPSPLLD
GVPEAREALR AAQPGEGQEG TYASEFAERL AGATEAEREE ITLDLVRTEA AAVLGHTTLD
AVAPDRAFKD FGFDSLTAVD LRNRLTTATG LTLPATLVFD HPTPTALARF VRAEVLGTPD
RSAERAGTSN TATDEPLAIV AMSCRYPGGV LSPEDLWQLV AEGRDAISGF PTDRGWDLGS
LYDPDPDALG TSYVREGGFV DSATRFDPGF FGISPREALT MDPQQRLLLE TSWETFERAG
IDPETLKGSS TGVFIGAGYP GYGEGMEMPE GSEGHMLFGA SAAVVSGRVA YTFGLEGPAV
TVDTMCSSSL VALHLAAQAL RSGECSMALA GGAMVMCSPG VFIGFSQQRG LSPDGRCKSF
AEEADGTGWS EGVGVLLLER LSDAERNGHQ VLAVIRGSAT NQDGASNGLT APNGPAQQRV
IRQALANAGL TGDQVDVVEA HGTGTTLGDP IEAQALLATY GQDHSAQSPL LLGSVKSNMG
HAQAASGVAG VIKMVMAMRH GIVPRTLHID NPSTEVDWNS GAVELLAESR DWPETGRPRR
AAVSSFGGSG TNAHLVLEQA PAPAPAEPRP AAEAPRLPLP WLLSGRGTPG LRAQAARLRD
FFAADGTLDA TDLAYSLTTT RAALETRGAV LAEDREGLLT ALTALAEGSP APGVVSGTAK
PAKTAFLFSG QGSQRPGAGR QLHAAFPVFA EALDELCAEF DRHLDRPLRT LLFAEEGTED
AALLDATRYT QPALFTLEVA LFRQLAALGV RPGVLVGHSI GEIAAAHAAG VLSLADACAL
VAARGRLMQE LPAGGVMISL RATEEEVLPL LAEVADRVSV AAVNGPASVV ISGEAEAARE
VAARLAEQGR KTRELTVSHA FHSPLMEPML AEFRRVAEQL TYQAPTLPVV SNLTGEQLTE
FGADYWVRHV REAVRFADGV RTVFGLGANT LIELGPGGVL TAMAQECVED GGPAPLLVPA
LRKDRPEPEA FLGALAQAWA HGVDVDWSGL YEGRAARRVD LPTYAFQHER FWPEPRTAGA
ADASGLGLTD AGHPLLGAAT ELADGAGLLF TGRLSPETQP WLADHAVAGT VILPGTAFVE
LAVRAGDEAG TGRLEELTLE APLPLPERGG VQIQVRVGEA DSAGRRPVAV HSRPENAAGR
PWTRHASGEL APAAGESAPG LGAWPPPGAE ALDVGGFYAG AAEVGYGFGP SFQGLTAAWK
HPESGEVFAE VVLPEPQQAQ AGKYVLHPAL LDAALHGMRL GDFVEQTGEA RLPFLFNGVH
LHAAGASALR VRIAKAGTDT IAVTATDTAG HPVATLDSLV LRPVATASLQ QSAGEAEGLF
RLDWVPVPAP TTAAAGTWAV LGADTPGLAD TLRTAGAAAS YPDVAAMKAA LTAGDPLPDT
VLLPLGPQTG AQEAGADAVR ESTARLLGHL KDWFADTSLE DVRLAVLTRG AVATRTGEDV
TDLAHAPAWG LVRSAQTENP GRLVLLDLDP KAEAPAAALP GALAATAEAD EPGAALRGET
LLVPRLVTTA GSGSLTLPEE AAWTLDTRAR GTLDNLGLLP RPEAEAPLAE NTVRIAVHAA
GLNFRDVMIA LGMYPGEAFL GSEAAGVVTE TGPGVTSLAV GDRVMGMIPH AFGPLAVADH
RMVARIPAGW TFERAASVPA AFLTAAYALR DLADLKRGEK VLVHAAAGGV GMAAVQLAQH
LGAEVFATAS KGKWDALRAA GLDEAHIASS RDADFEEYFS ASSDGKGMDV VLDSLSGELV
DASLRLLAKG GRFIEMGKTD IRDPEQIARD HGGALYRAFD LAEAGPERTG EMLAELAALF
DSGALTPLPV RSWDIRRAPE AFRLMSRAQH IGKIVLTVPQ RWDPEGTVLI TGGTGTLGAL
LARHLVTAHG VRHLVLAGRR GPEAPGAAEL VAEIAELGGT AQVVACDAAD RERLAAVLAE
IPAERPLRAV VHTAGIVDDG VLGSLDAERL AAVLRPKADA ALNLHELTRD LELTDFVLYS
SAAGVSGNSG QANYAAANAF LDALAHHRRA QGLPARSLAW GMWEPAGGMT ADLAETDVAR
MTRGGVTPLT PETGLALFDA AARLDEALYV PVRLDPASLG GQSGGAVPAL YRALVRTPVR
RSAQAAAAAS EPEELLGRLA GRTAAQAAEI LLDLVRTHVC AVLGITDPRT VEADRAFKDI
GFDSLTAVEL RNRLNSATGL RLPATLIFDF PSPGELVDHL RTELAPEAAG AQDTGTGSEE
ADEQQIRRVL SSVPVRRLRE AGLLDALLEL GAAPVGETAA QQPQQAAAIA EMDVDALVSL
ALDNSNS
//
