ID D9WQN1_9ACTN Unreviewed; 512 AA.
AC D9WQN1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Polyketide synthase type I {ECO:0000313|EMBL:EFL28164.1};
GN ORFNames=SSOG_07878 {ECO:0000313|EMBL:EFL28164.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL28164.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL28164.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL28164.1,
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};
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|RuleBase:RU003694}.
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DR EMBL; GG657754; EFL28164.1; -; Genomic_DNA.
DR AlphaFoldDB; D9WQN1; -.
DR STRING; 457427.SSOG_07878; -.
DR HOGENOM; CLU_000022_16_2_11; -.
DR Proteomes; UP000003963; 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; 3.40.47.10; -; 1.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 16..427
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 381..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 52850 MW; 297A87508C7816B7 CRC64;
MREALATMTS DLVHGTDAIA ITGVSCRLPQ ASDPGAFWEL LRAGRSAITE VPPDRWDPDA
VLPDEDERHR DGLRHGGFLD RVDAFDAAFF GISPREAVAI DPQQRLFAEL AWEALEDAGI
VPETLRSTAT GVMVGAIAAD YAALAQRGGA ITQHSLPGLN RGVIANRVSY ALGLRGPSLA
VDTAQSSSLV AVHLAVESLR KGECTLALAG GVALNFAPES AEVAGRFGGL SPDGRCFTFD
ARANGYVRGE GGGVVVLKPL VDAVRDGDTV YGVILGSALN NDGATDGLTV PSAEAQAAVA
RQACDDAGVD PAQVRYVELH GTGTPTGDPL EAAGVGAAYG SARPAGSPVL VGSAKTNVGH
LEGAAGIVGL IKTALSIRAP GDPGEPELRA AAPPHRPRGA EPARPDRVRP VAGRAAAGRG
ELLRRGRDEL PRRARRGTGR GCAGGFGERR AGDPAGAVAG VRTYRGGPAR PGRTAAGAAD
GRRGRRRVRH RLVAGPYPHP LRAPRRGPRA RP
//