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Database: UniProt
Entry: D9WMI7_9ACTN
LinkDB: D9WMI7_9ACTN
Original site: D9WMI7_9ACTN 
ID   D9WMI7_9ACTN            Unreviewed;       510 AA.
AC   D9WMI7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:EFL27853.1};
DE   Flags: Fragment;
GN   ORFNames=SSOG_07567 {ECO:0000313|EMBL:EFL27853.1};
OS   Streptomyces himastatinicus ATCC 53653.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL27853.1, ECO:0000313|Proteomes:UP000003963};
RN   [1] {ECO:0000313|EMBL:EFL27853.1, ECO:0000313|Proteomes:UP000003963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL27853.1,
RC   ECO:0000313|Proteomes:UP000003963};
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 hygroscopicus strain ATCC 53653.";
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; GG657754; EFL27853.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9WMI7; -.
DR   STRING; 457427.SSOG_07567; -.
DR   HOGENOM; CLU_534790_0_0_11; -.
DR   Proteomes; UP000003963; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
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; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049552; PKS_DH_N.
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; PF21089; PKS_DH_N; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE   4: Predicted;
FT   DOMAIN          1..309
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   DOMAIN          374..507
FT                   /note="Polyketide synthase dehydratase"
FT                   /evidence="ECO:0000259|SMART:SM00826"
FT   REGION          473..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFL27853.1"
FT   NON_TER         510
FT                   /evidence="ECO:0000313|EMBL:EFL27853.1"
SQ   SEQUENCE   510 AA;  53503 MW;  4BA59B274D2D44A9 CRC64;
     FSGQGSQRPG TGRELYERYP VFAEAFDAVC AAVDEQLDGY AEHPLRDVAF APEGSPLAPL
     LQQSMYTQTG LFALEVALLE LLKAWGVRPD HVMGHSLGEV TAVYAADALS LADACTLVAA
     RGRLMQALPE GGAMVAIAVA EQEAEAYIAE ASLQDAVGIA AVNGPRAVVV SGDEAAVVDV
     AEHFRAAGHR VRRLSVSHAF HSHRMDAMLD EFADVVAGLT FRAPRIPVVS NVTGGPIDTE
     RLCTPQHWVE HVRRGVRFAD GVRSLADQGV TAYLEVGPEA VVTPMVHATL DAVLGDDGYV
     AVAALKSGQG EALALTRALA RTFVAGTPVA WELLLPGGRR TELPGYPFAG HRYWQDASES
     TVGIRAAGLN ATRHPLLGAA VHLADGQAVL TGRVLPGAHP WLADHAVGGT VLLPGTAFLD
     LALHAGHEVG CPLVEELTLR TPLVLSAGTA VNLQVALGAP DETGRRSVTV YSSPAAVSGT
     EPLGPARDRH AVRGTPARRR SVDLGRLPTP
//
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