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Database: UniProt
Entry: A0A101PCW0_9ACTN
LinkDB: A0A101PCW0_9ACTN
Original site: A0A101PCW0_9ACTN 
ID   A0A101PCW0_9ACTN        Unreviewed;      1584 AA.
AC   A0A101PCW0;
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:KUN09175.1};
GN   ORFNames=AQI95_04815 {ECO:0000313|EMBL:KUN09175.1};
OS   Streptomyces yokosukanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67386 {ECO:0000313|EMBL:KUN09175.1, ECO:0000313|Proteomes:UP000053127};
RN   [1] {ECO:0000313|EMBL:KUN09175.1, ECO:0000313|Proteomes:UP000053127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40224 {ECO:0000313|EMBL:KUN09175.1,
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:KUN09175.1}.
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DR   EMBL; LMWN01000006; KUN09175.1; -; Genomic_DNA.
DR   RefSeq; WP_067117834.1; NZ_KQ948207.1.
DR   STRING; 67386.AQI95_04815; -.
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; cd08952; KR_1_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 6.10.140.1830; -; 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   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; IPR041618; PKS_DE.
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; PF18369; PKS_DE; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 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          36..449
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1430..1505
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1584 AA;  165401 MW;  7596933EB3A65B2B CRC64;
     MEDSATAGKL RDYLKRATTE LERSRRRVRE LEEQDREPVA IIGMGCRYPG GVRTPEDLWR
     IVDEGIDVVT EFPTDRGWDV EAIYDPEPGA PGKSYVRHGG FLHDAAECDP AFFGISPKDA
     PGTDPQQRML LEVTWEAFER AGIDPTTVKG SSTGVFVGLM HHDYIGGTIS GSIVSGRIAY
     TLGLEGPAVT MDTACSSSLV ALHSAIQSLR KGECSLALAG GAAVMASPEM FIEFSERRAL
     SPDGRCHSFS DDAAGAAWAE GAGMLLVERL SDALRNGHEV LAVVRGSAVN QDGASNGLTA
     PSGPAQIRVI EQALADARLA PHHIDAVEAH GTGTTLGDPI EAQSVIAAYG QDRPENQPIL
     LGSIKSNMGH PQAAAGVGAV IKMVMAMRHG TLPRTLHVEK PSTAVDWSAG DIELLTEPRA
     WHTPDGRPRR AGVSSFGISG TNAHTILEEA PAVEAEQPAP ERAALPVVPW VLSGKGSDAV
     QRQAERLLAA AADLDPYDVG FSLATTRTRF THRAAVTGRD RDELLAALRA VADGSQAAVV
     TPEPGRLGVL FSGQGSQRPG MGRTLHAAFP VFAAAFDEIC AAFDAHLERP LREVMFEEAA
     DPAASPLNQT VYTQAALFTF ETALYRLLEH WGVRPDLLAG HSIGEVVAAH VAGVLELKDA
     VALVAARGRL MQELPTGGAM VSLLASEAEV TPLLTDGVDI AAVNGPRAVV ISGDEEAVLA
     VAAQVEKTTR LKVSHAFHSH RMDPMLDAFR EVLEGLTFHE PALPVVSNVT GRMADALTSP
     EYWVRHVREA VRFHDGVTTL AAEGATRFLE VGPDSVLTNM AQDVVPDVIG AQRRDRDEDA
     TLVDAVSRLQ LTGSGPDWTA VFAGGRKVDL PTYPFRRDRH WEDAPILQAE RSAAARAGGD
     AADPFWELVR DQDVPAVAAT LGVADETSVA AVVPALAAWH EQRQANAAAD GWRYRVAWEP
     LAPAATPALG GHWLAVVPAD DDPWTLAVLT GLADRGVTID TLTVPLAADR AELAGLVAGR
     GDVDGVLSML APATDVTSTA ALVQALGDAE ITAPLWCATR DAVAHGTAAE VTGFAQAQVW
     GLGRVAALEH PDRWGGLIDL PAEIGPQTVA RLAALLGDAG GEDQVVIRES GAYGRRLEHA
     PARAGAPWKP SGTVLVTGAT GAVGTAVARW LAAEGADHLL LTSRRGTDAP GADDLVAELT
     GTGTEVTLAA CDVADREALA ALLDSVPEEH PLTAVLHLAG VLDDGVLDAL TPDRFAGVLA
     AKADSARHLH ELTAERDLSA FVLFSSLTAT VGGAGQANYA AANAYLDALA EHRQAAGLAG
     TSVAWGPWGG DGMAAHGTVR SAARAMGMSL LAPERALTAL GRALDGGDTT VTVADVDWSV
     FAPAFTSSRP SALLSALPEA RRGTGGGAEA GAADGFAEKL AGLTGGERDR ALQELVCGQA
     AAVLGYGSAD AIEATTAFRD LGFDSLTSVD LRNRISSAAG VPLPATLIFD YATPAALAKH
     LGTELAGADT SVDSVVAELD RVAARLGDLT AEDIEQGRIT TRLQSLLADL NKTLGQDAAA
     VAGRLEDASA DDVFAFIDNE LGSA
//
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