ID H6D570_STRA4 Unreviewed; 3917 AA.
AC H6D570; A0A0B5EMQ8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AEZ53946.1, ECO:0000313|EMBL:AJE80655.1};
GN Name=slnA2 {ECO:0000313|EMBL:AEZ53946.1};
GN ORFNames=SLNWT_0279 {ECO:0000313|EMBL:AJE80655.1};
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:AEZ53946.1};
RN [1] {ECO:0000313|EMBL:AEZ53946.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XM211 {ECO:0000313|EMBL:AEZ53946.1};
RX PubMed=22156425; DOI=10.1128/AEM.06701-11;
RA Jiang C., Wang H., Kang Q., Liu J., Bai L.;
RT "Cloning and Characterization of the Polyether Salinomycin Biosynthesis
RT Gene Cluster of Streptomyces albus XM211.";
RL Appl. Environ. Microbiol. 78:994-1003(2012).
RN [2] {ECO:0000313|EMBL:AJE80655.1, 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}, and DSM 41398
RC {ECO:0000313|EMBL:AJE80655.1};
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; JN033543; AEZ53946.1; -; Genomic_DNA.
DR EMBL; CP010519; AJE80655.1; -; Genomic_DNA.
DR KEGG; sals:SLNWT_0279; -.
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; cd08956; KR_3_FAS_SDR_x; 2.
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; 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; 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; 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; 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; 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; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 2.
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; 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; 2.
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 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 33..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1681..1756
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1775..2201
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3754..3829
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 3882..3902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3917 AA; 407746 MW; 257400A973A9CAD1 CRC64;
MANEDKLVES LKRVAAELHD TRQRLTEAEN RTGEPIALVG MACRYPGGVR SPEDLWELVS
EGRDAISGFP DDRGWDLERL YHPDPDNPGT AYTRSGGFLH DATDFDPGLF GISPREALAM
DPQQRILMET SWEALERAGL DPLSLKGSQT GVYVGAATPA YIVGGHTQQG AEGYSLTGTS
GSVVSGRLSY HYGFEGPAVT VDTACSSSLV ALHWACQALR AGECSMALAG GVSVMSVPGL
FVEFSRQRGL SEDGRCKAFA QCADGTGWGE GVGVLVLERL SDARRNGHRV LAVVRGSATN
QDGASNGLAA PNGPSQQRVI RQALAHARLR PRDVDVVEAH GTGTTLGDPI EAQAVLATYG
KERPAEQPLW LGSLKTNIGH TAAAAGIAGV IKMTMALRKG VLPKTLHIDA PTPHVDWSAG
AVELLTDNQD WPALDRPRRA AVSAFGISGT NAHLILEQAA ESDERRPAPE APALPPFAAD
TAVAWPLAGH STEAVRGQAA RVHAHGTAHP ETTAAALGLG LATTRSALPY RAVSLGAATG
EHLDTLRRLA DGQSAAHLVE GLADIEGKTT FVFPGQGSQW PGMAVELLDS SPAFAARMAE
CDKALAPHAD WRLLDVLRGA EGAPGFDRVD VVQPVLWAVM VSLAALWRAC GVEPDAVVGH
SQGEIAAAVV AGALSLEDGA KVSALRAKAL LALAGKGGMM SVAEPAEAVR ARLTPFGERI
SLAAVNGPSS TVVSGEPEAL AELRAACEAD GVRARLVNVD YASHGPQVES IRTAVLGALA
GITPRKATVP FLSTVTGKAA EGTELDAEYW YTNLRGTVRF EDGIRALLER GHGFFLEASA
HPVLTVGVQE TIEAAGLPAV ALGTLRREEG GPRRFLASLS EAWVRGRTPD WSAVFSGHAV
TAPELPTYAF QRKRYWADPV GAAAGDVAAA GLGAVDHPLL GATVRVADGD EFLLTGRLSL
QSHPWLADHA VSGTVLLPGT AFVELALRAG DEAGCAQLSE LTLEAPLLLP AQGGVQIQLV
VGEPKEDGRR SLGIYARPAE DDQPDTPWTR HAVGFLTPEP PAAAPEPLTV WPPAGAEPLA
LDDFYARATE SGYGYGPVFQ GLKAAWQLGG ETWAEVALPE QQREDAEEFG LHPALLDAAL
HATLLGADDG AADGVRLPFA WSGVSLRAVG AASLRVRLAP TADGELSVSL YDSAGAPLAE
VAALGLLPVS AEQLRGTTGA ESLHRVEWTT LAPGAEAAPD PDRRELPALR AALDAGEAAP
AHVLVELTPE DGADSPALAA HTATRRTLAL LRDWFAEERL TASRLVLLTR GAVRTAPGEG
PADLALAAVR GLVHSAQTEN PDRIQLLDTD GTEASTAVLH RALLSEEPEL ALREGEFRAP
RLVRTAPGGE GSEWDPEGTV LITGGTGALG ALLARHLVTR HGVRHLLLTG RRGLDTPGAA
ELVAELAESG ARTAVAACDA ADREQLASLL ATVPADRPLR AVVHAAGVLD DATTATLSEE
QLTRVLRPKA DAAWHLHELT RELDLTAFVL FSSAAGAFGN PGQGNYAAAN SFLDALADHR
RAEGLPAVSL AYGLWQSEGM PGHLDSAELG WSARAGYLPL RPEQGLAALD AADSHRGEPL
LVTVPLDKAV LRARAASGVL PHLFRSLVRV PSRRAVENGA QGTGSALADR LATLDPEARQ
AELLDLVRGL VAAVLGHDEP EAIEPDKAFK ELGFDSLTAV ELRNRLAAAT GLKLPATLVF
DHPSPGALAR HLLTALLATG GPAATAPAAT ATGSDEPIAI VAMACRYPGG VSTPEELWQL
VAEGRDAVSG FPEDRGWDLE GLYDPEGNRP GSSYTRSGGF LYDAADFDPE LFGISPREAV
TMDPQQRLLL ETTWEAFERA GLDPLGLQGS RTGVFAGVMY HDYASHVEQA ADSAEGYLLT
GTSGSVISGR LSYAFGLEGP SVSVDTACSS SLVAMHLAAQ ALRAGECSLA LAGGVTVMAT
PNVFVEFSRQ RGLSSDGRCK SFSATADGTG WAEGAGVLLL ERLSDAERNG HRVLAVMRGS
AVNQDGASNG LTAPNGPSQQ RVIEQALAGA RLTPAEVDAV EAHGTGTTLG DPIEAQALLA
TYGQQRESDR PLWLGSIKSN MGHAQAAAGV AGVIKMVQAM RHGILPKTLH AEEPSPHIDW
SEGAVALLTE ATPWPETGRP RRAGVSSFGA SGTNAHVVLE AAPEPAETAE AAEDSAAGPY
LWPLSGRGES ALRAQAARLH AHVSARPALR PADVTLSLTT GRPALEHRAA VTAADREGLL
TALAALAEGT RAPGLTQSSP RGGKLAFLFS GQGAQRLGMG RELYAVQPVF AAAFDEVCAG
FGADFRERVF AAEGGELDRT GLTQPALFAI EVALFRLVES FGVRADFLAG HSIGELAAAH
VAGVLSLEDA CTLVAARGRL MEALPAGGAM VSIRAAEVEV RSRIGEFEGR VDIAAVNGPE
SVVVSGEEAA VLELAEALAE SGHKTKRLRV SHAFHSPLME PMLEEFRRVA SGLAYGSPSI
PVVSNLTGEL VTAFDAAYWV EHVRHAVRFA DAIGFLAAEG VTRFVELGPD GVLSAMARDC
LPETFDGLLV PVLRKDRPEA ETFLAALGEA WTKGIRPDWA ALTAGQAARP VELPTYAFQR
LRYWPKPARP AGDVAAAGLG AAGHPLLGAT VAAADGGQIL LTGRLSLSSH PWLADHAVAG
TVLLPGTAFV ELALRAGEEA GVPHLAELVL EAPLVLPARQ AVQIQVLVGP AEEDGGRAVS
VHSRAGAPGE SDALWVRNAA GRLTHPAPEA PAEPGNWPPA GAEPVDLDGF YAGLAAAGYG
YGPAFQGLAK AWRSGDGDQV FAEVELPESQ QDEAGRFALH PALLDAALHG LAAAGPATAE
GQVRLPFSWN GVRLHAVGAS RLRVRMATAG PDSLSLDIAD PEGHPVLGVE SLATRAVPVE
QLAAAATAST TEHLYRLDWS AVPAASAAEP PHLLRIGAGD APGAPYRASH PDVAALTAAL
DADATPPGAV VLDVPGATAS GAEAARETAA AVLGVLQEWL AAEQLADVRL FVRTRRAVAV
RSGEDVTALA QSPVWGLVRA AQAENPGRLV LVDTDADWDT PLPEAVFAAA EEPQLAVREG
ALLAPRLVRG SAPGAAPALP AGGAWTLDTT GGETLEDLAF LPCEADRIPL AEGEIRVAVR
AAGLNFRDVL IALGMYPGAA RMGNEGAGIV TEIGPGVTGL AVGDRVTGLI RGAFGPLAVV
DRRLVVRVPE GLSFEQAAAL PTVFLTAYYG LVDLAGLRRG EKVLVHAAAG GVGMAAVQLA
EHLGAEVFGT ASEGKWDTLR ALGLDERHLA SSRTAAFEET FSAATGGEGV DVVLDCLAGE
LVDASLRLLP RGGRFLEMGK TDVRDPAEIA ASYPGVDYRA FDMVEGAGPD RIGEMLAELA
ELFEAGVLKP LPVRSWDIRR AGEAFRFMSQ ARHVGKIVLT VPQVWDPSGT VLVTGGTGTL
GALVARHLVV EHGVRHLVLA ARRGPEAPGA AELVAELGEL GAQAEVVACD AADRGQLAKL
LDGIDGARPL RAVVHTAGVL DDAVLAAQTP QKLDRAMRPK VDAALNLHEL TRDLDLTAFV
LYSSVAGVLG GPGQSNYAAA NAFLDALAAH RRAQGLPGVS LAWGQWAEAS GMTEGLAGAD
LARMNRSGVL PLPSEQGLAL FDESARHDEP LLAAVRLDAA ALRNQAEAGR LPAPLRGLVR
TAVRRAAAGT AATAAGAAAL GQRLATLAEP ERADALLDLV RGHVATVIAH PDPAAIDTER
GFLDLGFDSL TAVELRNGLG AATGLRLPTT LIFDYPSPAA LAGHLLAELR PEGGEDGAAD
TAVLGAMSEW EAAIAALPAG SEGREKAVKR LRSLLWKFDR TENETDEEAQ GQEGGSTLTA
ATDDEMFALI ENELGLN
//