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Database: UniProt
Entry: Q826K7_STRAW
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Original site: Q826K7_STRAW 
ID   Q826K7_STRAW            Unreviewed;      1517 AA.
AC   Q826K7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:BAC74895.1};
GN   Name=pks4 {ECO:0000313|EMBL:BAC74895.1};
GN   ORFNames=SAVERM_7184 {ECO:0000313|EMBL:BAC74895.1};
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC74895.1, ECO:0000313|Proteomes:UP000000428};
RN   [1] {ECO:0000313|EMBL:BAC74895.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2] {ECO:0000313|EMBL:BAC74895.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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DR   EMBL; BA000030; BAC74895.1; -; Genomic_DNA.
DR   KEGG; sma:SAVERM_7184; -.
DR   eggNOG; COG1028; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_35_4_11; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000000428; 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; cd08955; KR_2_FAS_SDR_x; 1.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR013968; PKS_KR.
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; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000000428};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          34..461
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1431..1506
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1517 AA;  164169 MW;  43B0D4C75D48E962 CRC64;
     MPDSSVPVEE RLRSALDTVE EQQQTISKLL REKHEPIAVV GIGLRFPGGS NTPDEFAEFL
     REGRSGIGPF PTDRFDTDTY VADGSGEDDE PGRIRTIGGG FLDRIDQFDA PFFNISPKEA
     QYMDPQQRLL LETAWEALEH ANIDPTPLRR ANGGVYIGAS SIDYALELDS LPYEELDGHL
     ASGITFFPLS GRLSYFLGWR GPCMSLDTAC ASSLTALHSA AEGLRRGECD IALAGAVNAL
     HHPRIPVIFS AANMLAPDAQ CKTFDESADG YVRAEGCAVA VLKRLSDAQR DGDTVLGLIR
     GSAVGQDGDS AGLTVPNGPA QEAVMRAAIQ RASLQPSDIQ YVEAHGTGTP LGDPIEMGAI
     SDVFATSHDK ERPLTVGSVK TNLGHMEPVA GLVGVIKTLL QMREQTIFPH LNFTTPSGRI
     PWDSYPVTVP TENRPWKADT RRAVVNSFGF GGTIAAVVLE EPPVPEQPAT APAAVQADRT
     DSASAVEQHV FTVSAKNHRS LKQLIERYQR HLDDSPSTDL GSLCYTGNVG RAHHPLRLAG
     VVGGREDLDA LLKKGLGQIE KRSIAAERAR KTAFLFTGQG SQHAGMGRPL YERFVVFREH
     LDECDRLFAP LLGRSIRALV LGEDDDPDAI HQTRFTQPAL FSLEYSLAQL WLSWGARPSV
     LIGHSIGEVV AAAVAGLFSL EDAVTLVAAR ARLMQSVSAP GGMAAVPEAA EQVAPLLESY
     PDLTMAAVNS PRQCVISGGT DSLAEVSETL RGRGLDVKQL RVSHAFHSPL MAEVLDEFRE
     ALKDITFRQP QLTLVSNITG KVARVAEISK PEYWVRHIVE PVNFEAGMRA IERRGRHVFV
     EIGPSIALTG LARSCVDAGE HRWLNSLHPK EKQGLTILQA VAKLYSAGVR VDWNGFHDGR
     PGRRVDLPLY AFDRKRYWLP NGTGPSAQDE AAGPRSAFLH EPRWVEQPPT ARTVAGPRHV
     LVVNRAAQDV TGLVEQAAGQ DVRLSFAADP EQALDVVRAG EPTDVCWFWQ SDDGPVSAES
     LRAECEHNYR DLLTLLGLLE QEEGGLARRL WLVTEAAQVL PGDEPGSGAH LAAATLWGFG
     HVLLNEYPSY RVTLVDLPAG GGRTAEEMLL GEWLAADTGE FQVAYRDRTG RHVHRLLPSA
     FDSPEQPAEP GTAPVRPDRN YLITGGLGAL GLLTAHRLVD EGARYLTLVS RRAEPAADAA
     GLWERLRDRA EVTVLRGDVG DSGDVHRIVE SLHAAPQPLG GIVHTAGGLD DAPVAAQTWE
     SIDALFSAKV YGSWMLHEAA QGFDELDFFV AYSSAAAVVG GASQSNYAAA NAYLDQLLHW
     RAAQNLPALG VNWGPWSEAG MSARLNARHI EALEREGIVF IPPRQALDTM VSLLGEPVTQ
     VLAGECDWDR FSAAKPVVNA FYQELVGADG TSSRTLDLDA LLASPDGERV EKITDFIRHR
     VADVLHIDDA DDISPYTEFV QLGLDSLVAV ELKNALEAAF RIPLPLTMAF DYPSAAVLGE
     FIGKRLEQAR PTAPAGS
//
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