ID   D9XDQ7_STRVT            Unreviewed;       972 AA.
AC   D9XDQ7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Polyketide synthase type I {ECO:0000313|EMBL:EFL30436.1};
DE   Flags: Fragment;
GN   ORFNames=SSQG_00954 {ECO:0000313|EMBL:EFL30436.1};
OS   Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS   Tue 494).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL30436.1, ECO:0000313|Proteomes:UP000004184};
RN   [1] {ECO:0000313|Proteomes:UP000004184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC   {ECO:0000313|Proteomes:UP000004184};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL   Submitted (FEB-2009) 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; GG657757; EFL30436.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9XDQ7; -.
DR   STRING; 591159.SSQG_00954; -.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_35_7_11; -.
DR   Proteomes; UP000004184; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   CDD; cd00833; PKS; 1.
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   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; 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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
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; PF02801; Ketoacyl-synt_C; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000004184}.
FT   DOMAIN          1..169
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         972
FT                   /evidence="ECO:0000313|EMBL:EFL30436.1"
SQ   SEQUENCE   972 AA;  101278 MW;  278F15FBE81975D0 CRC64;
     MLGVVRGSAV NQDGASSGLT APNGPSQQRV IRAALDNAGL TAADVDAVEA HGTGTKLGDP
     IEAQALIATY GQDRPEGRPL WLGSMKSNIG HSVAAAGVAG VIKMVMALRQ GELPPSLYAG
     EPTPMVDWSA GSVSLLADGV AWARGERVRR AGVSSFGVSG TNAHVIVEEA PAEEPAAEPV
     GDGAGLVSWV LSGASAGGLR GQAERLVSFL EQRPEVGAGS VAAALAGRER LRHRLAVVGE
     SAEELVEGLE SFLSGDLSVG AAQGVVGTES KVVFVFPGQG WQWVEMGVEL LAASEVFARV
     VGECSAMVEE LAGWSVVEVL RQKPGTPGFD RVDVVQPVMF SVMVGLARLW ESVGVTPSAV
     VGHSQGEIAA AHVAGVLSLE DAVRVVVARS QALVEICGQG AMASVALGCA EVQERIAGLE
     SVSVAAVNGP SSTVVSGGAE EIAGLVAGLT GSGVRARRID VDYASHSAHV EQVRRRIEAD
     LASVRPRAGQ VPVYSTLRGE VLTGPEMDGH YWYANLRGRV EFEQAVRGLL ADGFTTLVEC
     SAHPVLTPGI GETVDTVPGA QVTVTGTLRR DDGGLRRFLT SAGTLWTAGV DVAWDSLLPE
     AEPVELPTYA FDRSRFWLER TNGTGDASGM GLGAVEHGLV SAVVEVAAGG TVVLCGRLSR
     SRQRWLADHA VSGQVLFPGT GFMDLVLRAA DQVGCQVVEE LVVQAPLLLP DSGDVDLQIV
     IEPAGDDGGR QVVVCSRPAG TDSVWTQHAQ AVIAHGSTSD VGPVGVWPPS GAEAIDVSCL
     YEELAGRGYA YGPVFRGVRA AWRQGQDVYG EIELPESAAE EAARFGLHPA LCDAAAHLLQ
     FSEVLDQDGV WLPFAWNGVR LLATGATRLR VRITPLGEGS VRMDLYDVTG EPVAVVEQLT
     ARRLDAAELQ PTSTAGARGL FALAWPDLPT PSQPTVTDTV VWTPHDTGTE DTWGLPTITD
     LDDLPASSRA VV
//