ID L8EY01_STRR1 Unreviewed; 1133 AA.
AC L8EY01;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Type I polyketide synthase {ECO:0000313|EMBL:QST85420.1};
GN ORFNames=SRIM_039620 {ECO:0000313|EMBL:QST85420.1};
OS Streptomyces rimosus subsp. rimosus (strain ATCC 10970 / DSM 40260 / JCM
OS 4667 / NRRL 2234).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1265868 {ECO:0000313|EMBL:QST85420.1, ECO:0000313|Proteomes:UP000011074};
RN [1] {ECO:0000313|EMBL:QST85420.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST85420.1};
RA Pethick F.E., MacFadyen A.C., Tang Z., Sangal V., Tze-Tze L., Chu J.,
RA Guo M., Kirby R., Hoskisson P.A., Herron P.R., Hunter I.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QST85420.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST85420.1};
RA Algora L., Schniete J.K., MacFadyen A., Hoskisson P.A., Hunter I.S.,
RA Herron P.R.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QST85420.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10970 {ECO:0000313|EMBL:QST85420.1};
RA Algora-Gallardo L., Schniete J.K., Mark D.R., Hunter I.S., Herron P.R.;
RT "Bilateral symmetry of linear streptomycete chromosomes.";
RL bioRxiv 0:0-0(2021).
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DR EMBL; CP048261; QST85420.1; -; Genomic_DNA.
DR RefSeq; WP_003980258.1; NZ_CP048261.1.
DR AlphaFoldDB; L8EY01; -.
DR GeneID; 66860227; -.
DR Proteomes; UP000011074; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 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; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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 Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 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; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..438
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 920..995
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1002..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 119917 MW; EDAE9F209411F1FC CRC64;
MNAPADARVA VIGMAFRFPG ADTPEEFWRA VRIGRDCVRR FTEAELEAAG VPAEKYRADD
FVGASGILHD IAGFDAPFFG MSVREARLTD PQHRMFLECA YHALEDSGYP RERDGLRTGV
FATTGYHLYT MENYLLNNVL KSPIGDDWLS RMQVMVGNYT DFTATRVSFR LDLTGPAVSV
QTGCSSSLVA LQTAAQSVVT GDSDIALAGA TAVHVPQVLG YEYVKGSILS KSGRLRAFDA
GADGTVGGTG VAAVVLKRLD RAVADGDTIH GVIRGWGVTN DGASKQAYTA PSAAGQRAAI
RRALEHAGIG ADTVGYLETH GTGTLKGDPI EFEGAVSAYR ADTDRTGYCA LGSIKANIGH
LDVASGLASF IKTLLVLKHG VIPPMANFSE PNPALDLDNS PFYIPETARP WPQGDTPRRA
GVTSLGVGGT NVHVIVEQAP EPAPRSATVA PPGIVVLSGQ SEAARTANAE ALRDHLTRHP
DMNLADLVTT AAGRIHHRHR LAVRGTDPAS LAAALDSWLA GTGAPAGPAA VTTGEAPREA
RAGIAFQFTG QGSPYPGMAQ PLYERFTVVR DLLNTCERHH QRLYGSSLLD VLLDPIADRA
TTENTRIAQP ALFALQYALT GLWRQAGIVP DAVAGHSVGE YAALCAAGAL SVEDGLRLTA
ERGRLMQEHC APGAMAAVSA DLRTAENLAA EIAGLELAVV NGEQRHVLAG PVTAVDRLSA
LLEERGIPGQ RLPVTRAFHT ALMDPVLDKF RELLDGVAFR PVTTGFVSGL DGRLHEPGWV
PDADYFVRQT REPVRYDAVL RTLGDTGPAA LVELGPHTTL SGLARTALPT VRAVPTLRRG
AGTGPFWDAV ARLHCTGADL AWPVLLAGTG GRRTALPGYR FQHTDHWTGP RPTVVPAGQQ
PLREPSREEE DVAQDEAVFG RVLAHVIELV AKHLGHDAAA VTGDTSFFDL GADSLQMISV
LRELEQEHRV KVAMRELFEE ASTPGQLTEL IVGRMVGGAG GSGMPGGSGA SGAWAGSGEA
VAEEPVRHEP PVAEEPVRYE PPITEEPVRH EPPVAAAPAE PVRAQESAPA VPPGPEHPVT
RAELTDLVRQ VQQLSQIQLQ MMSQIHQLSQ LLTAQATSAL TGGAVSNGKA GGQ
//
