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Database: UniProt
Entry: J1RWK2_9ACTN
LinkDB: J1RWK2_9ACTN
Original site: J1RWK2_9ACTN 
ID   J1RWK2_9ACTN            Unreviewed;      1462 AA.
AC   J1RWK2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:EJJ02907.1};
DE   Flags: Fragment;
GN   ORFNames=SU9_31533 {ECO:0000313|EMBL:EJJ02907.1};
OS   Streptomyces auratus AGR0001.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ02907.1};
RN   [1] {ECO:0000313|EMBL:EJJ02907.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ02907.1};
RX   PubMed=22965094; DOI=10.1128/JB.01155-12;
RA   Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT   "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT   Producing Actinomycete.";
RL   J. Bacteriol. 194:5472-5473(2012).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJJ02907.1}.
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DR   EMBL; AJGV01000203; EJJ02907.1; -; Genomic_DNA.
DR   STRING; 1160718.SU9_31533; -.
DR   eggNOG; COG0300; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_16_10_11; -.
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; cd08952; KR_1_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 2.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.11460; -; 1.
DR   Gene3D; 6.10.140.1830; -; 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; IPR041618; PKS_DE.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
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   Pfam; PF08659; KR; 1.
DR   Pfam; PF18369; PKS_DE; 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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 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          854..929
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          952..1380
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          812..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1381..1410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1394..1410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1462
FT                   /evidence="ECO:0000313|EMBL:EJJ02907.1"
SQ   SEQUENCE   1462 AA;  152759 MW;  06E44709E34F923F CRC64;
     MEPAAVVGHS QGEIAAACVA GALSLADGAR VVALRSKAIR ALSGRGGMVS VALPSSDVSD
     LIKPWNGRVS VAAVNGPSSV VVSGDADALD ELMDGCKERE VRARRIEVDY ASHSAHVESI
     REELLEVLAP VVPRPAEVPL FSTVRGEWLD AAEMDAGYWF TNLRRTVEFA PAIEALVAAG
     HRTFVEVSPH PVLTVPLQET VEDEGADAVV TGTLRRDDGG LARLYTSLGV LYAHGVDVDW
     SPAFADRRPH RVELPTYAFQ RQRFWLEPDA PAVAASPEEE AFWTAVGDQD AATLAGTLGL
     PGAEALDEVL PALSSWHRNR RQRGTADGWR YRVVWRPLTE PAARQLDGEW LVVVPAGYED
     DALVHGAREA LAEAGARTHS LTVDDRAGLA DLLRPGPGPF AGVLSLLALD ERPDRTHPCV
     PTGLSLTLAL LQALGDAGID APLWCVTRGA VGIGTTAEAA TGGSAGEHDA PTNPDQAGIW
     GLGRVAALEH PERWGGLIDL PGRAGGQTAA EGRTAADGQE VALLARILAA GDDEDQLAVR
     GSALFGRRLL PAPVAGKPPR RSWRPRGTVL VTGGTGALGA HIARWLAADG AEHLVLTGRR
     GADVPGVAAL CSELRDQGVR VTVAGCDLAD RQAVAELVRQ IERDGEPVRA VVHAAGVSAL
     GSLAEAGPAD LAAALAGKVA GADHLSSALD PAQLDAVVYF SSISGTWGVA DHGAYAAANA
     LLDARAERGR ADGLPVLSVA WGPWAGGGMI ADSIHDVLRR RGVPVIDPDT ALTALQQALD
     HDDTSIAVAD VDWRRFHSVF TSVRPSRLLT EIPQLAADED GDGPGDDGSG TDRGSARSPL
     AEKLAGLDVR QRTAALLDLV REQVASVLGH DKTAPVDPER PFKELGFDSL TAVELRNRLS
     RATGLRLPRT VVFDHPSPAA LAGYVGTQLT GAEESAAKPA AAPAPLPAPA DDDPIAIVAM
     ACRYPGGVQS PEDLWRLVRE GVDAMSAFPT DRGWDLDGLY DPDADQPGRS YVRESGFLGD
     AADFDAEFFG ISPREALAMD PQQRLLLETS WEVFERAGID PKSLRGSGTG VYMGVTDQEY
     GNRLRMAAPE QIEGYLATGA ATSVASGRVA YTLGLEGPAV TVDTACSSSL VALHMAVRAL
     RSGECSLAVA GAAMIMADPG PFIGFSRQRG LARDGRCKPF SAAADGFALS EGVGVLLVER
     LSDARRNGHP VLAVVRGTAV NQDGASNGLT APNGPSQQRV IRAALADARL SAGEVDAVEA
     HGTGTSLGDP IEAQALLATY GQERDAERPL WLGSVKSNIG HTQTVSGVAG VMKMVLAMRH
     GELPATLHVD EPSPHVEWAS GAVELLTEAR PWTAEEDRPR RAGISSFGIS GTNAHVIVEQ
     AEESGRAEQS DQAESADGGE SASSSSASGV GPVVPWVVSG RSADALVAQA ERLASRVAGT
     GLSPVDVGWS LVASRSSFEH RA
//
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