ID A0A101NW34_9ACTN Unreviewed; 1864 AA.
AC A0A101NW34;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KUN00411.1};
GN ORFNames=AQI95_34960 {ECO:0000313|EMBL:KUN00411.1};
OS Streptomyces yokosukanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN00411.1, ECO:0000313|Proteomes:UP000053127};
RN [1] {ECO:0000313|EMBL:KUN00411.1, ECO:0000313|Proteomes:UP000053127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN00411.1,
RC ECO:0000313|Proteomes:UP000053127};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT strain for the species Streptomyces yokosukanensis.";
RL Submitted (OCT-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUN00411.1}.
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DR EMBL; LMWN01000050; KUN00411.1; -; Genomic_DNA.
DR RefSeq; WP_067133566.1; NZ_KQ948223.1.
DR STRING; 67386.AQI95_34960; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000053127; Unassembled WGS sequence.
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; 3.40.366.10; 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; 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; 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; 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 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 SUPFAM; SSF47336; ACP-like; 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:UP000053127};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..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 1864 AA; 192748 MW; A43E8DE90C6909F2 CRC64;
MADEAELRDY LKRAIADARN ARKRLREVQD QAREPIAIVS MACRYPGGVS SPEQLWQLVA
DGADAVGGFP EDRGWDLEAL FDADPDHAGT SYVTQGGFLK GAGLFDAGFF GISPREALAM
DPQQRLLLET SWEALERAGI DPVSLKGTDV GVFSGLSGQG YGAGAGVVTP ESEGFAGTGA
STSVASGRVS YVLGFEGPAV SLDTACSSSL VAIHLAAQAL RQGECSMALA GGAMVMATPG
NFVAFSRQRG LAADGRCKAF ADGADGMGLA EGVGVVLLER LSVARERGHK VLAVLRGSAV
NQDGASNGLT APNGPSQQRV IRKALSSAGL APADVDVVEA HGTGTALGDP IEAQALLATY
GKDRDPEKPL WLGSLKSNIG HTQAAAGVGS VIKMVQALRY GTLPSTLHVD EPTTEVDWSA
GAVQLLTEAR QWPREGRPRR AGVSSFGVSG TNAHLILEEA PAAESAAEGT APAGVVPLVV
SAHHAGSLAG QAERLVAFLE SGVGGASLTD VARTLVTGRA VLGERAVVVA DSDEEALSGL
RALARGESGA NLLAGSAGSS GPGRVVWVFP GQGSQWVGMG RELLESSPVF AERIAECAAA
LEPWIDWSLV GVLRGEEPEL LERVDVVQPA SFAVMVGLAA VWASVGVEPD AVVGHSQGEI
AAACVSGALS LEDAAKVVAL RSQAIRERLA GRGGMASVAL SEAEAVARLE SWSDRVEVAA
VNGPSSVVVA GDAQALDEAL QSLSDAGVRV RRVAVDYASH TRHVEDIREA LAETLTGIEA
QAPTIPFYST VTGGWVQDAG VLDGGYWYRN LRGQVGFGPA VAELIRQGHR AFVEVSAHPV
LVQPVTEILD DAESGAATVV TGSLRREEGG LRRLLASMAE LFVRGVPVDW SGVLPAGTAS
AGVDLPTYAF DHQLYWLQPT GTGGDATSLG LAAADHPLLG AMVRLPHSDG LVFTSRLSLK
SHPWLADHAI GGLALLPGTG LVELAVRAGD EAGCSVLEEL VIEAPLVVPE HGGVRMQVVL
GAPAENGSRT VEVYSQREDA PDDGEVWTRH ATGTLSASAP TPGTDFDFAA WPPPGAQQVE
VDAVGFYDEL RERGVGYGPA FQGVRAVWRR GEELFAEVAL PEELRKDAAG FGIHPALLDA
ALQTGTFRAM ADAQPQEGGG QPLLAFSWNG LVLHASGASA LRVRVAPSGP DALSVDAADE
TGALVVTMDS LVSRAVSAEQ LETAADSAVA DSLFRVDWSE LPTVWGAEPA PAWVPVATAA
EIETLARSAD APAVAVLEAV GGAGEAAVLA LTTRVLEVVQ AWLATDGLDQ SRLVVHTRGA
VPAGDGAVTD PAGAAVWGLV RAAQAENPDR FVLLDTDADT DTDTDTGIDA AAGIDADGLG
DVLGAALATG EPQIAARGTV LSLPRLARVP AQDTDAETVF AAGGTVLVSG GGSLGELAAR
HLVVRHGVRH LVLASRRGPA AEGVRELVAE LTEQGAAVSV VACDVSDREQ VEALLAAVPD
EHPLTGVVHT AGVFEAGLVE TLTPERLARV FAPKVDAVRH LDELTRGLEL DAFVVYSSAS
SVFLGAGSSG YAAANAFLDG LMAHRRAAGL PGLALSWGTW AYATNMTTHL GADDQASMSR
RTSRDGVVAL TPAEGMQLFD AAVASAQSLL VPVKLDLRGV RAAAAAGGTV PHLLRGLVPT
GRQQARAAAA KDGDLLRRLS SVSEPEQEAM LLDLVRTQAA VVLGHSGPDG IRPDTAFKDV
GFDSLTSVEL RNRLREATGL KLPATLVFDQ PTPLVLTGYL RGELGISDDV LSRVNARIED
VESLIAAVTL DESMRASIAL RLQGLVAKCN GVVEQTDGST VAEKLESASA DEVLDFIHEE
LGLV
//
