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Database: UniProt
Entry: F8JLQ6_STREN
LinkDB: F8JLQ6_STREN
Original site: F8JLQ6_STREN 
ID   F8JLQ6_STREN            Unreviewed;       972 AA.
AC   F8JLQ6; G8XFQ3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:AEW99514.1};
GN   OrderedLocusNames=SCATT_p13210 {ECO:0000313|EMBL:AEW99514.1};
OS   Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS   / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OG   Plasmid pSCATT {ECO:0000313|EMBL:AEW99514.1,
OG   ECO:0000313|Proteomes:UP000007842}.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptantibioticus.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW99514.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RC   PLASMID=Plasmid pSCATT {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003229; AEW99514.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8JLQ6; -.
DR   KEGG; scy:SCATT_p13210; -.
DR   PATRIC; fig|1003195.11.peg.403; -.
DR   HOGENOM; CLU_000022_16_6_11; -.
DR   Proteomes; UP000007842; Plasmid pSCATT.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 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   InterPro; IPR001227; Ac_transferase_dom_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; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR   PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 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   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; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Plasmid {ECO:0000313|EMBL:AEW99514.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007842}.
FT   DOMAIN          11..465
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          937..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        942..972
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   972 AA;  102157 MW;  85ADF7A120DA598D CRC64;
     MVDSHAYQPS GHPVAIVGLA AMFPQAHDVR EFWDNVVTGR DCVTDVPETS WSVADHYDPD
     MRAPDKTYAR RGGFLPPVVF DPVEFAMPPA TLDSIGLVQL LSLRVAREVL RDAGCPGAAW
     YDPGRTGVVL GVCGQNSTMV PLASRLRAPA VRRAALSCGL SPRDADEIAR RFLAESPEWT
     EDSFPGILAN VVAGRIANRF GLGAANCVVD AACASSLAAL RMAVSELVEH RADLMITGGC
     DADNSVTTFL CFSKTPALSP SGAVRPFDRE ADGTLLGEGI GMLALKRLAD AERDGDRVYA
     VLRGLGGSSD GRTGSIYAPS ADGQVTAMRR AYADAGVPAA SVELIEAHGT GTRVGDTVEL
     GALRTVLGPA PDRPRIAVGS VKSQIGHTKA AAGAAGLIKA ALALHHRLLP PTINVTEPND
     ALRDSALYVN TRARPWIRDP ARPVRRAGVS SFGFGGVNFH AVLEEHPPTP PRTLHRTPRA
     LVWHAPDPAA LLALVRDGAD PADGGPVPPH HARLGVLVHD AADREALLAA ATARLSDTPD
     ADGWTLAGRA HYRRSGLPPD ARAAVLFAGQ GSQYVGMGAD ALLAVPPVRR AFDDANALWE
     GEEETLAQVV HPEPGRRDPA ADTARLRRTA YAQPAIGALA MGHYAYLAEL GFAPAAALGH
     SCGEVTALWS AGSLSDADCL LLTRRRGQAM RPAPGGTDRD AGAMAAVRLS AEEWRQRAQN
     FPQLALCNIN APDEIVVGGP TPAVEELAAA CLRDGGPAVR RLPVAAAFHT PLMAHAVPVF
     AEAVSRTEVR PPAHPVLACT PGARYGTDPE ADRRVLAEQI TRPVDFAGRV RELYDDGCRV
     FVECGPKGIL SRLVRRTLGD ATVETVPADT GPGTDSAAAL KNAALRLAVL GFGIRHINRY
     DAPDPPPPAP PSPVARRLAG PVFAMRARRA AYEAGLAVPY RCTPTGPPPD RSAAPGPADA
     PQPPTSPPPR PL
//
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