ID A0A1V4CWE8_9ACTN Unreviewed; 3264 AA.
AC A0A1V4CWE8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Polyketide synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=VT50_0232360 {ECO:0000313|EMBL:OPF71888.1};
OS Streptomyces antioxidans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF71888.1, ECO:0000313|Proteomes:UP000033615};
RN [1] {ECO:0000313|EMBL:OPF71888.1, ECO:0000313|Proteomes:UP000033615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC164 {ECO:0000313|Proteomes:UP000033615};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces antioxidans MUSC 164.";
RL Submitted (DEC-2016) 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:OPF71888.1}.
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DR EMBL; LAKD02000117; OPF71888.1; -; Genomic_DNA.
DR Proteomes; UP000033615; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
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; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.40.50.720; 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; 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; 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; 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 3.
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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..263
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1422..1497
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1514..1938
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3105..3180
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 3264 AA; 337909 MW; A3950CCAA9396282 CRC64;
MEGPALTVDT ACSSSLVALH LAVGALREGE CSLALAGGVT VMSTPMAFVE FSRQGGLAVD
GRCKAFSDGA DGTNWGEGVG VVVLERLSDA RRHGHEVLAV VRGSAVNQDG ASNGLTAPNG
PSQERVIRAA LASGGLSASD VDVVEAHGTG TRLGDPIEAQ ALLATYGQDR DAPLLLGSVK
SNIGHTQAAA GVAGVIKMVL AMRHGVLPRT LHVDEPSSQV DWSSGAVELL GEARAWEAGD
GPRRAGVSAF GVSGTNAHVI LEEGTEPATS APKVRDHGPV AWVVSGRGAE GLSRQVARLA
DHAAATGDLS AADVGFSLAT SRARLSHRVA VVGSSVDELL RGLRAVSGGV AAATDGRLGV
VFTGQGAQRM GMGRGLYGVL PVFTETLDRV ASGFEGLLDR SLLNVVFDDA GALEDTLYAQ
AGLFAVEVAL FEQLRVWGVV PDFVAGHSVG EVSAAYAAGV VSLEDGCRLV AARGQAMRRA
RSDGAMLAVG AAEADVVELL GDGVGLAAVN GPASVVVSGD ADRVAVLEGV CRERGWKVSR
LRVSRAFHSH HMDGVLGKFA AAIDQLTFAQ PRMPLVSTVT GQLMDERVTT PAYWVEQVRA
TVRFGDAVEY MAEQGGVTAF LEVGPDAALS ATVTEAGHDA VPTLRSGHDD ETCVVSAVAQ
LHVHGFDVDW AAIFAPYRPQ RVALPTYAFR QERFWLSTGP AGLLADAVEL PRGGAVVSGR
LSLGSMAWLA GHAVGGEVVV PGTGLADMAV RAGHHVGCEL VEELTLQAPL VVPASGGVAV
RVVTTPPAAD GRCGVEVHSR PEGPSEEWTC HASGTLAPGG PVAAEPVSWP PADAVEVPVV
GLYDELAARG FAYDGVFRGL RRAWRHDDEL FVEAAVDGDV SGFGVHPALL DAVLHGIAVS
GWDGVGGVPF AWSGVRVLAV GAEWVRARLV RMADGGISIT AVDDTGMPVA TVEALQLRPL
SDWRSATRRH TGPLYTVAWT EVERADGAEA DAPEAIEITG PADLAEPPVG APATAVFHAA
SGDGADPERA DEAVAEALAV VQAWLSDERW AATTLLVVTR NAVACADGDP APDVVGAAVA
GLVRSAQSEH PNRIVLADVD EPGGAADLLR IPWREPQLAV RGGRVLVPRL TRMPVPTDPE
SPWTGDGTVV VTGATGGLGA VVARHLVVEH GVRHLMLLSR SGPAAPGAEA LVSELSERGA
DVRVVACDVA DRADLAAALA QVEHPVTGVV HAAGVLDDGV VSALTPHRVS AVLRPKAIGA
WHLHELTQDM PVRAFVLFSS VAGVLGGAGQ ANYAAANAFL DALAGQRRRH GLPATSLAWG
LWSTETGMTG RLDGASRARV ARGGIAALST EEGLGLFDAA CATDTAQVVP VRLALDALRA
RAERNDLPAL FRGLVADRPK AIATAAASHD PLVGLSGADR HGYLLDLVRG RVAIVLGHAD
ASAIDPHRVF QELGFDSLTA VELRTGLSEA TGLRLPATLV FDHPTPAALA ARLDELLGGT
ERSAAEEEPV AAADEPIAIV GMACRYPGGV RGPEDLWRLV DGGRDAIAAF PDDRGWDLDG
VFDSVVEEQR ARFRPEGGFL YEAAEFDPGF FGISPREAVA MDPQQRLLLE TTWEAFEHAG
MDAGSVRGSR TGVFTGVMYY DYATRLPAVP EHLQAFVDTG NAGSVLSGRL AYTFGLEGPT
LTVDTACSSS LVALHLAAQS LRQGECSLAL AGGVTVMFTP KVFTNFARQG GLAADGRCKS
FSDEADGTGW GEGVGMLVLE RLSDARRHGH EVLAVVRGSA VNQDGASNGL TAPNGPSQER
VIRAALASGG LSTSDVDVVE AHGTGTALGD PIEAQALLAT YGSDRDRPLW LGSIKSNIGH
TQAAAGVAGV IKMVQAMRHG VLPRTLHVGE PSSQVDWSSG AVELLGEARA WKAGSGLRRA
GVSSFGISGT NAHVIVEEAE PSPVAERGES VGVPVVWSVS GRGVEGLRAQ AARLAEFLGE
RSDVSPVDVG FSLAMSRARL SHRAVVVGSS VDELVGGLRA VSGGVAAVAG ARLGVVFTGQ
GAQRVGMGRG LYGVLPVFTE TLDRVASGFE GLLDRSLLDV VFDDAGALED TLYAQAGLFA
VEVALFEQLR VWGVVPDFVA GHSVGEVSAA YAAGVVSLED GCRLVAARGQ AMRRARSDGA
MLAVGAAEAD VVELLGDGVG LAAVNGPASV VVSGDADRVA QVEGVCRERG WKVSRLRVSR
AFHSHHMDEV LGEFAAAIDQ LTFAQPRMPL VSTVTGQLVD ERVATPAYWV EQVRATVRFA
DAVEYMAGQG GVSAFLELGP DAALTPVIDS AVAVPTLREG HGEHRALLAA LGRLHTHGVE
PDWAAVYAPY APRRVDLPTY AFQHERYWLN AATGTGDVRS IGVAGVRHWL LGGAVALPEG
GTVLTGRLSA GQADWLSGHL VGGEMVVPGT VLVDLASCAG DEVGCDVVEE LSLRTPLVVP
DSGDIELRVV VGPVDTEGRG AVSVYSRSAG SDGSWTCHAT GTLAVGPDVA SEPAVTWPPA
DAEDVSVAGL YDALADAGLS YDGVFRAVTS VWRHDDDLYV EAGLDGDLVA GFALHPALLD
AVLHGIAVSG WDGVGGVPFV WSGVRVFAVG AARVRARLTR TADGGVSVSV VDDTGNPVAT
VDSLLLRPIP RGQPAAMADD SLFELDWTTI EAGPRTEPVT AVVGSAAGLS HVERAPDVVV
YRVDGAPAEV TDAVSATLAV LQQWIADDRW VSSRMVVVTR NAVSCPGDQR TDLVGAAVTG
LVRSAQSEHP DRIVLVDVGD TDDTDDIAAL GWTSGIGEPQ LAIRCGRVLV PRLRKTTSPP
SAEPGWAGDG TVVVTGATGG LGALVTRHLV DEHGVRRLLL LSRSGMAAPG VEALVAELGE
RGADVRVAAC DVADRDALAG VLAALPPGAE VTGIVHAAGV LDDGVLASLT PERVAGVLAP
KAVGAWHLHE LTRDMPVRAF VLFSSIGGVL GSAGQANYAA ANAFLDGLAH HRHQLGLPAT
SLAWGLWAGE QGMGAGPGPK RPVRGGVAPL SEAEGLALFD LLATADRPFV VPARLQPGEL
RDRADTGYLP AVLRRLVRTA PRRRTVRGQE APADFAALDD AARARALTDL VRDRVATVLG
YASGGEVALE KGYLDMGFDS LTALELRNDL SAAVGLRLPA TLLFDHPTPA TTVRRLGELL
APGTPEPISA ESSEPEIRRA LAALPLDRLR ELGLLETLLG LTAPNGDGAT ASDGTDHVKD
INELDVDGLV ARALGSDQAG LGGH
//
