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Database: UniProt
Entry: A0A0B5F0V6_STRA4
LinkDB: A0A0B5F0V6_STRA4
Original site: A0A0B5F0V6_STRA4 
ID   A0A0B5F0V6_STRA4        Unreviewed;      2086 AA.
AC   A0A0B5F0V6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:AJE87699.1};
GN   ORFNames=SLNWT_7323 {ECO:0000313|EMBL:AJE87699.1};
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:AJE87699.1, ECO:0000313|Proteomes:UP000031523};
RN   [1] {ECO:0000313|EMBL:AJE87699.1, 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; AJE87699.1; -; Genomic_DNA.
DR   KEGG; sals:SLNWT_7323; -.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR   CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; IPR029058; AB_hydrolase.
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; 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; IPR020802; PKS_thioesterase.
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; IPR001031; Thioesterase.
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; 1.
DR   Pfam; PF08990; Docking; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
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          32..459
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1709..1784
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2086 AA;  216866 MW;  813FC45F073521EF CRC64;
     MSEAKLRDYL KRVTTDLART RQRLKDSEDR AQEPIAVIGM ACRYPGGVAS PEDLWELVAG
     GHDAVSMFPG DRGWDLDALY DPDPDTPGTS YAREGGFLDE AAHFDPAFFG ISPREALAMD
     PQQRLLLETG WEAFERAGID PARLRGSRTG VFAGVMYQDY ATRLRQAPED VEGYVGSGGS
     GSIASGRIAY TFGLEGPAVT VDTACSSSLV ALHLAAQALR RGECSLALVG GSMVMSTPVA
     FVDFSRQRGL AADGRCKAFS AAADGTGWGE GVGMLLVERL SQARRNGHEV LAVLRGSATN
     QDGASSGLTA PNGPAQQRVI QQALADAGLG PAEVDAVEAH GTGTSLGDPI EAGALLATYG
     KDRDGGDPLW LGSLKSNIGH TQAAAGVGGV IKTVMALRHG ILPKTLHAEE PSPSVDWASG
     AVELLTEARP WPVVEGRPRR AAVSAFGFSG TNAHVILEQA PAEEAAGDTA APEGAAGGVG
     EAAAALPQDG TPATAVVPWL LSARSPEALR AQALRLAERV EAAPEASAAD IGYSLALTRS
     ALGHRVAVAG AGRDELLGRL RQIASGQAEG AVADAGRTAF LFAGQGAQRL GMGRELYEAF
     PVFAAAFDEV CAALDTHLAG HVPLPLREVV FGGDKELLDR TVYTQTALFA LEVSLFRLVE
     SFGLVPDFVV GHSVGELAAA QVAGVFSLED GCALAAARAR LMQQVAQGGA MVSLTASEEE
     VLAHLRGRED EVSLGAVNGP EATVISGAEE AVLEVAAAVG AKSKRLSVQV AAHSPLLEPV
     LAEFARIAGR VRYQAPRLPV VSNVTGETAG AELADAAYWV AHMRQAVRFA DGIAHLERQG
     VTRFVEIGPS GVLSAMGQSC LADAGAGVFV PLLRADRPEP EALLSGLGRA WAHGATVDWG
     GFFTGRGRRV DLPTYAFQRE RYWLDSPAGA GDLAAAGLGE AAHPLLGAAV ELPGSDALVL
     TGRLSLGAQP WLAGHAVANT VLLPGTAFLE LAVQAAEHVG CAQVEELTLG APLILAPRGA
     LTLRVRAGEA DADGRRELHI HSRPQDAGLG EPWTAHATGI LSPTATGGGE KLTSWPPADA
     EEIDVSEVYA RFAAGGFAYG EAFQGLHTAW RRGEEVYAEI RLPASQRSAA GAYGLHPALL
     DACLHTIALA PALQSEQSRL PFSFTGVSLH ATGAQDLRIR LTPTGEDSVA LDLADTTGAP
     VATVEGLLLR AMSGEQLGGA RAAASQALFR LDWPSRSTEA PAVTRAAMIG EDALELTEDL
     FAAGVHLESY ADLDALGAAA ESGTSVPAHT LLTCPPATGE LPGAVRQSLG GALAAAQSWL
     ADERFAASRL VFVTRGAAAT GPGEDIGDLA QAALWGLIRS AQSESPDRFV LVDLDEDEAS
     LRALPAALAT GEPQLALRAG QLHTPRLARA QADAEQQPAR ALDAEGTVLV TGATGGLGTL
     LARHLVTAHG VRHLLLASRR GPRAEGAEQL REELTALGAH VTLAACDVAD RQALEALIAA
     VPAAHPLTAV FHTAGVLDDK TLTSLTPEQV DTVLRPKADA AWNLHEATAH LDLAAFVLYS
     SAAGVLGGAG QGNYAAANAF LDALAQHRRV RQLPAHSLAW GLWAQPGSMT GATPATGTSR
     SGIAPLSAEQ GMELLDTSLA LGTAHLVPMR LDMAALRAGA SAGSVPLLLR HLVRTPATRR
     TTAAAAGSGA GGSELISRLA GLDEDEQTAL LVELVRTQVA VVLGHPDASA IGATHDFVDS
     GFDSLTAVEL RNRLAAATGL RLPATLVFDH QSPTELAQRL RTDLAAARTS APAGETTGAV
     AAPAGGESTT LSALYTQAFA TGKWKEIFDL LHATAALRDR FASPAELPQL PKPVRLSKGP
     AREHLFCFSS CLAVAGIHQY ARFAASLRGR RDVSALALPG FGRGEPLPET AAAVVAAQAE
     AVAEAADGAP IVLLGSSAGG WFAQAAAGHL ERMGHTPAAV VLVDTYVPKS SILNQFGLSL
     MDGMTEREGV FVTMDDDRLS AMGWYLNLFG TWEPDPIATP TLLVRATEPL STGSLQLADL
     PDWRSFWELP HETVDVRGNH FTMMEDFSSP TAQAIEDWLD SLPHRT
//
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