ID A0A1V4D0E4_9ACTN Unreviewed; 921 AA.
AC A0A1V4D0E4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OPF75739.1};
DE Flags: Fragment;
GN ORFNames=VT50_0224345 {ECO:0000313|EMBL:OPF75739.1};
OS Streptomyces antioxidans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF75739.1, ECO:0000313|Proteomes:UP000033615};
RN [1] {ECO:0000313|EMBL:OPF75739.1, 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:OPF75739.1}.
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DR EMBL; LAKD02000065; OPF75739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4D0E4; -.
DR OrthoDB; 9778690at2; -.
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; 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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 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; SSF52151; FabD/lysophospholipase-like; 1.
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.
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 123..198
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 217..643
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OPF75739.1"
FT NON_TER 921
FT /evidence="ECO:0000313|EMBL:OPF75739.1"
SQ SEQUENCE 921 AA; 95270 MW; 4D721581D5000F5D CRC64;
DRRARGLAGT AVAWGPWAEG GMAAAEGMEA ELVRRGLAVI PPALALAALQ GAITGDDGVL
TVADVDWERF APVFTLERPS PLISDLPEVR RALDSAGPSA QTGDASTGLR ARLAGLTDAE
IDRTLLELVR SQAAAVLGFA GAEVVEPGRA FKELGFDSLT AVEFRNRLNV ETGLVLPATL
VFDYPSAAVL ADHLRAEVLG TQGAVAAPSA ALAPVDDDPI AIVGMSCRFP GGVGSPEDLW
RLVADGGDAI SDFPSNRGWD VDGMYDPDPE RLGTFYSSEG GFLHEAGEFD AAFFGISPRE
ALAMDPQQRL LLETSWEAFE RAGIAPLSVR GQQIGVFVGA ATSGYGVGHD GAAGELEGQI
LTGNATSVVS GRISYTLGLE GPALTVDTAC SSSLVALHQA AQALRQGECE MALAGGVTVM
ATPGAFVEFS RQRGLAPDGR CKPFADAADG TGWSEGVGML LVERLSDARR KGHQVLAVVR
GSAVNQDGAS NGLTAPNGPS QQRVIRQALA NAGVSAAEVD VVEAHGTGTT LGDPIEAQAL
LATYGRERPE GHPLWLGALK SNIGHTQAAA GVGGIIKMVM AMRHGVLPRT LHVDEPSREV
DWSAGEVRLL TEAAEWPETG HPRRAGVSAF GVSGTNAHTI IEQAPALDEE EPVPAAPAAG
RGVVPWALSA RSAEALRAQA ERLRSYLLER GELGALDVGY SLVASRSVHE HRAVISGTNR
VELLRGVEAV AAGDVAPGVV QGVATPSGPM AFLFSGQGAQ RLGMGRELYE VFPAFADAWD
EVCAHLDVVL DRPLRDVVFA AEGSADAGLL DQTAFTQPAL FAVEVALFRL LSAWGVTPDV
VIGHSIGEIA AAHVAGVFSL EDACALVAAR GRLMQALPEG GAMVAIEGSE EEVAASLAGR
EAEVSIAAVN GPAAVVVAGD E
//
