ID D9X575_STRVT Unreviewed; 915 AA.
AC D9X575;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:EFL33838.1};
DE Flags: Fragment;
GN ORFNames=SSQG_04356 {ECO:0000313|EMBL:EFL33838.1};
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:EFL33838.1, 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; EFL33838.1; -; Genomic_DNA.
DR AlphaFoldDB; D9X575; -.
DR STRING; 591159.SSQG_04356; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_16_6_11; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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 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; IPR014030; Ketoacyl_synth_N.
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; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00827; PKS_AT; 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 Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000004184}.
FT DOMAIN 33..452
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT NON_TER 915
FT /evidence="ECO:0000313|EMBL:EFL33838.1"
SQ SEQUENCE 915 AA; 96248 MW; 25F9B9391051F816 CRC64;
MVVTRGDFQY WKGSRAKMTS ERHSAAIDPL DRREPIAVVG LSCRLPGAAG PEEFWRLLRE
GRDAVTQMPG HRWEPISADA HSEIRRGGFL DAVEEFDAAF FGISPREAVV MDPQQRLLLE
IAWEALEDAG IAAASLDGSP TAVFVGTARE DYTSLLYRQG SAAITQHTVA GTHRGIIAGR
VSYALGLNGP SLTVDTSQSS SLVAVHLACE SLRAEEAELA LAAGVNLNLL AEGVVGRRAV
RRALPGRALL HLRRPGQRLR ARRGRRHGRA QAAAGGAVAD GDRVHGVILG SAVNNDGATP
GLTVPSAAAQ EKVVRLAHRR AGVVPDAVQY VELHGTGTPV GDPIEAAALG AAVSALKAAG
DPLRVGSVKT NIGHLEGAAG IAGLIKTVLS VRHRMLPPSL NFRTPNPKIP LDSLNLSVND
RLGEWPHPER PLVAGVSSFG MGGTNCHVVV GEAPGTREPL TAPRTRPADA VLPVVVSARG
TQALRAQAGR LAEFVETHGD AEPASVGRSS VFTRSRLGHR GVVLAADRDE LVAGLRALAS
GLPAAGVVAG AEATGRLAMV FTGQGAQRIG MGSELRAAFP VFAAAFDTVC AHLDPLLERP
LREVVPTGEG LDETRYTQPA LFAVEVALFR LFASWGVRPD LLAGHSIGEV AAAHVAGVLS
LTDACALVAA RGRLMQELPA AGAMVAVQAA EDEVLPLLAG QEGEVAVAAV NGPAALVLSG
DTDAVLEIAA ALKDRGHKTK RLTVSHAFHS PHMDGMLDAF RRVVTGLTLH QPRIPVVSTV
TGEIAAPELL TSPEYWVEQV RRPVRFLRAA RTLEAEGVRT VLEMGPDGVC SAMVAESVLD
KDSVAAEPAL RPGRPEERTA WTALARAFVR GAAVDWEAVF EGAGGRRIDL PTYAFQRERY
WVTDPGRAEG AAAGV
//
