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};
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; 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
//