ID   D6AT80_STRFL            Unreviewed;       903 AA.
AC   D6AT80;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:EFE78157.2};
DE   Flags: Fragment;
GN   ORFNames=SSGG_05524 {ECO:0000313|EMBL:EFE78157.2};
OS   Streptomyces filamentosus NRRL 15998.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE78157.2, ECO:0000313|Proteomes:UP000003986};
RN   [1] {ECO:0000313|Proteomes:UP000003986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RA   Molnar K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000003986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA   Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces roseosporus strain NRRL 15998.";
RL   Submitted (DEC-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; DS999644; EFE78157.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6AT80; -.
DR   Proteomes; UP000003986; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   CDD; cd08956; KR_3_FAS_SDR_x; 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   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   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; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE   4: Predicted;
FT   DOMAIN          1..162
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   DOMAIN          238..413
FT                   /note="Polyketide synthase dehydratase"
FT                   /evidence="ECO:0000259|SMART:SM00826"
FT   REGION          354..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         903
FT                   /evidence="ECO:0000313|EMBL:EFE78157.2"
SQ   SEQUENCE   903 AA;  93879 MW;  D48177FC09F7898D CRC64;
     MMVAVEASEE EVLPFLGGGV SLAAVNGPSS VVLSGVEGVV DEVVGVFVGR GRRSKRLVVS
     HAFHSVLMEP MLEEFRGVVE GLVFREPVLG LVVGGDVCDP GFWVSHVREP VRFLETVRLM
     ERRGVSGFVE VGPDAVLSVM GPACVVGGVD EVVFVPSVVR GRDEVRGVVG ALGGLWVRGF
     DVDWGAVFDG LGVTGGAGAG GVVDLPTYPF ERRRYWLDPG GVGGSGDVGV SGQVGAGHPL
     LAAVLDHVDG GGVTLTGRLS LATHPWLADH AVHGAVLVPG TALVEMVLRA GQETGTPTID
     ELMLEAPLVL PERDAVDVRV DVGEAEENGR RPVRVHSRDG EGEWLRHATG YLTPEAPEAP
     EAPEAPEASD GTTDGAAHLE VWPPAGAEQL DVAGAYDELA DRGYAYGTAF QGLLAAWRRG
     AETYAEVALP AQTAQAAESD ARTFGIHPAL LDACWHALLL GDPEGSPMIP FAWTGVALQA
     EGVSHVRVRI APAGPDTTAM TVADQAGKPV ASVAGLVARP VSAQQLSAAP RSLYRVTQTA
     LPGAVGGIGD TDGWAVLGAD VHDLGHRVYA EPGVVPDPVP RFVTYDCPAI DGTVPEAVRT
     ATCDLLVLLA GWLEEPRFAE AHLVLTVGEH LTQAPLAGLV RAAQAEHPGR ITLVRTTGSP
     VNAGLLADAA ATGEPELAIA DGEIHAPRLT RITDLEPSGE SALLGPVLIT GGTGGLGALV
     ARHLAVRHGI REFVLLSRRG PQAPEAGRIQ EELAQLGATA AIVACDAADR AELAEVLERH
     PVRSVVHAAG VVDNAVLTSL TPERVAAVLR PKVDAAWNLH ELTAGHDLAA FVLFSSSAGI
     LLGAGQSNYA TANVFLDELA AYRRANGLPA LSLAWGLWDE GSGMAGGLDE MGRQRMRRLG
     MPA
//