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Database: UniProt
Entry: A0A136PXG0_9ACTN
LinkDB: A0A136PXG0_9ACTN
Original site: A0A136PXG0_9ACTN 
ID   A0A136PXG0_9ACTN        Unreviewed;       998 AA.
AC   A0A136PXG0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Polyketide synthase subunit {ECO:0000313|EMBL:KXK63105.1};
GN   ORFNames=AWW66_04790 {ECO:0000313|EMBL:KXK63105.1};
OS   Micromonospora rosaria.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK63105.1, ECO:0000313|Proteomes:UP000070620};
RN   [1] {ECO:0000313|EMBL:KXK63105.1, ECO:0000313|Proteomes:UP000070620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 803 {ECO:0000313|EMBL:KXK63105.1,
RC   ECO:0000313|Proteomes:UP000070620};
RA   Yang H., He X., Zhu D.;
RT   "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT   which can produce antibacterial substance rosamicin.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXK63105.1}.
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DR   EMBL; LRQV01000009; KXK63105.1; -; Genomic_DNA.
DR   RefSeq; WP_067360280.1; NZ_LRQV01000009.1.
DR   AlphaFoldDB; A0A136PXG0; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000070620; Unassembled WGS sequence.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; IPR006162; Ppantetheine_attach_site.
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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070620};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..430
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          914..989
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          889..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  101988 MW;  E4F074A7D2F00A2D CRC64;
     MSRDRSLDIA VTGVHARLPG VTDLDDWWAA TLAGRVLTTR LDRADLLAAG VPAALVDDPD
     YVPARGHLAD ADRFDHTLLR VSARDAELMD PQHRLMLETA WAALEDAGTA GPAAAEHTTG
     VYASGSGSGY LRAMLANGPL DPLTLDQALH GTEPDFVASL ISYKLGLTGP ALGVQTACSS
     SLVGVHLAVQ ALLAGECDQA VVVAAGIDFP QAGHLHVPGG IQSVSGNCRP FDAAADGVVA
     GSGVVAVVLR RLADALDDGP EPYGVLLGTA VNNDGAAKAG YYAPSVTGQE AVIRAALASA
     DVGGESIGYL EAHATGTRVG DPIEWAAASA ALTTAGARPG QVAVGALKAA IGHLDSASGL
     AGLVRALWVV REGVVPPVAG FTALNPLLEA DGSPLYVPTE AAAWSGPQPR RAGVSSFGIG
     GTNAHVIVEQ PPAAPAVPPR PERERLVVLS AADGAALTRT AARLAEHLHR AGPDLADVAY
     TLAAGRAALP ERLAVTGRTA AEVADRLTGD AGALRGRAPV DGPAPVVYLL PGQGTQQPGM
     AAPLAGALPG FADHLDECLA AFDAELSARL RRALHDPDAP ADELAATALA QPALFAVGYA
     AGRALTALGV APAALVGHSL GELTAACLAG TFGLADAARF VAARGRAMQD CPPGAMLALG
     CDPDTARDLL AETGAELAVA TVNSADGCTV AGAVEEVRRF ADRLGDRVFH RVLRTSHAFH
     SALVEPALPA LDRALDGVRA HPPAVPYASN LTGRLVQPGE PVDARSYVAQ ARRPVRFADA
     LADTMARLPG CVAVEVGPGR VLTGLAEAAG LPAVPLCPLR TDRPEGEVLA ALGTLWTWGQ
     PVPAGLLGGA DGRLAHLPGY AFGGRRWLAP EATPPAARAP ADRAVADRAV SGRADTDPAV
     GERAGVDRPQ RSGAGGPDPA VLVPKLWAEV LGHTDLADDS DFFALGGDSL LITQLARRVH
     EELGLRVPLR EMLAGRTLGR QTAVVRDALR RDRARPES
//
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