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Database: UniProt
Entry: A0A1C4KGR4_9ACTN
LinkDB: A0A1C4KGR4_9ACTN
Original site: A0A1C4KGR4_9ACTN 
ID   A0A1C4KGR4_9ACTN        Unreviewed;      1062 AA.
AC   A0A1C4KGR4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Enediyne polyketide synthase {ECO:0000313|EMBL:SCD60385.1};
DE   Flags: Fragment;
GN   ORFNames=GA0115251_114615 {ECO:0000313|EMBL:SCD60385.1};
OS   Streptomyces sp. TverLS-915.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839763 {ECO:0000313|EMBL:SCD60385.1, ECO:0000313|Proteomes:UP000198957};
RN   [1] {ECO:0000313|EMBL:SCD60385.1, ECO:0000313|Proteomes:UP000198957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TverLS-915 {ECO:0000313|EMBL:SCD60385.1,
RC   ECO:0000313|Proteomes:UP000198957};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMCE01000134; SCD60385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4KGR4; -.
DR   Proteomes; UP000198957; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd00833; PKS; 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   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; 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:SF37; FATTY ACID SYNTHASE; 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   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 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; PS52004; KS3_2; 1.
PE   4: Predicted;
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:UP000198957};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..465
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          945..1021
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          911..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1062
FT                   /evidence="ECO:0000313|EMBL:SCD60385.1"
SQ   SEQUENCE   1062 AA;  111558 MW;  1582342818261435 CRC64;
     MTTEPERIAV VGIACRYPDA DSPEELWQNV LAGRRAFRRL PDERMRREDY YSPDPAAPDR
     HYAQKAAVLE GFEFDRVKHR IAGSTFRSTD MTHWLALDTV GRALADAGYP EGKGLPSAGT
     GVVIGNSLTG EFSRANLMRL RWPYVRRTVG AALREQGWED EQLAAFLGSL EDRYKSPFPP
     IDEDSLAGGL ANTIAGRICN HFDLGGGGFT VDGACSSSLL SVATACDGLG AGHLDVAIAG
     GVDLSIDPFE VIGFAKTGAL ATSEMRVYDR GSNGFWPGEG CGAVVLMRDA DARAQGRFRY
     ATIAGWGYSS DGRGGITRPE AAGHRLALER AYHRAGFGLE TVPYLEGHGT GTAVGDSTEL
     RAFSEARRAA DPEAPPAALT SVKGNLGHTK AAAGIAGLLK AVLTVRHQII PPATGHYDPH
     PELTGERPAL RVPTEAEPWP EGASVRAGVS SMGFGGINAH VVVEHADGVR RTALPRSVVR
     LVRSRQDCEL LLVDADDTDA LRERLAGLAA LAGRLSYAEL GDLAATLQAE LAGRPLHAAV
     VASSPEQAEE RLLGLLHRVD GGADSLLEPA AGLFLGGRSA REPRIGFLFP GQGAGRRADG
     GALRRRFAEV DDLYREHRLP ADGDQVATEV AQPRIVTASV AGLRVLDALG IEATAAAGHS
     LGELTALHWG GAMDEAGLLR LAATRGRVMA RASDGGGTMA GIAAGPDDVA PLLAGEPVVI
     AGYNSPQQTV VSGPAAVVER VCARATERGI TAQRINVSHA FHSPAVAPAA RAFAEELADE
     EFQPLTRQVV STVTGGPLAE DADTAELLTR QVLAPVRFAE AVTEVARRSD LLLEVGPGRI
     LSGLAAQTAD DPVLALDTDG TSLAGLLNAV AAAWTLGARV RLDELFRDRF TRPLPLDKEF
     RFLANPCESA PDGELPAQEA RATAVAATPV PDASPAGERE PEQDADTLGV LLRLSAARAE
     LPLSALTPET NPLDELHLSS ITVGQIMNEA ARELGIDAPA TTSAFATSTL RELAGLLDEL
     SDTELPRETG RPDAVAGVAP WVRAFAVDLV EAGPPAAPSP AE
//
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