ID   B8XLW5_STRGR            Unreviewed;       465 AA.
AC   B8XLW5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:ACL97764.1};
DE   Flags: Fragment;
OS   Streptomyces griseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1911 {ECO:0000313|EMBL:ACL97764.1};
RN   [1] {ECO:0000313|EMBL:ACL97764.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FXJ175 {ECO:0000313|EMBL:ACL97764.1};
RA   Rong X.Y., Huang Y.;
RT   "Multilocus sequence analysis of Streptomyces griseus cluster based on
RT   housekeeping and ketosynthase genes.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; FJ406019; ACL97764.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8XLW5; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 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; 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; 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; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00827; PKS_AT; 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;
FT   DOMAIN          1..84
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          334..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACL97764.1"
FT   NON_TER         465
FT                   /evidence="ECO:0000313|EMBL:ACL97764.1"
SQ   SEQUENCE   465 AA;  49211 MW;  8161C5E309953C42 CRC64;
     KSNIGHTQAA AGVGGMIKMI MAMRHGTLPR TLHAETATTA IDWSSGAMAL LTERLPWPER
     DRPARAAVSS FGISGTNAHI ILEAPGTDDG TSATALPPSA DVPRPWLLAA RTPDALRGQA
     QRLYDLLSAR PELRDADIEL SLRTGRTPFD HRAVITGDDR ETRTGALAAL ARDERSPHVV
     TGQAVRGDAV FVFPGQGSQW IGMGLDLYET YPVFAEHLRA CEEALDPYVD WSLLSVLRGE
     ADAPSLDRVD VVQPALFAVM VSLAHLWRSL GVQPAAVIGH SQGEIAAAHV AGALSLEDAA
     RIVALRSRAL RGLSGRGAMA AVSMSAEEAA RRIENLRSTD NGGRGGEDGS AGTDRRTGTD
     RRTGDGGGAL SVAAVNGPAS TVVAGSPDAV DAFLDQAEAD GFQTRRLPVD YASHSAQMEE
     IQQGLLDILA DVTARPGTIP FYSTVTADVM DTAGLDTAYW YRNLR
//