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Database: UniProt
Entry: A0A263CVC1_9PSEU
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ID   A0A263CVC1_9PSEU        Unreviewed;      1557 AA.
AC   A0A263CVC1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OZM69919.1};
GN   ORFNames=CFN78_28050 {ECO:0000313|EMBL:OZM69919.1};
OS   Amycolatopsis antarctica.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1854586 {ECO:0000313|EMBL:OZM69919.1, ECO:0000313|Proteomes:UP000242444};
RN   [1] {ECO:0000313|EMBL:OZM69919.1, ECO:0000313|Proteomes:UP000242444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU-G6 {ECO:0000313|EMBL:OZM69919.1,
RC   ECO:0000313|Proteomes:UP000242444};
RA   Wang J., Leiva S., Huang J., Huang Y.;
RT   "Amycolatopsis antarcticus sp. nov., isolated from the surface of an
RT   Antarcticus brown macroalga.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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:OZM69919.1}.
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DR   EMBL; NKYE01000031; OZM69919.1; -; Genomic_DNA.
DR   InParanoid; A0A263CVC1; -.
DR   Proteomes; UP000242444; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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; 6.10.140.1830; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; IPR041618; PKS_DE.
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; 2.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF18369; PKS_DE; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00827; PKS_AT; 2.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
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:UP000242444};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          23..97
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          113..534
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1444..1519
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1557 AA;  163106 MW;  A0341C50EF7F282B CRC64;
     MPFVRSRSGD DENEVGRVRA GPRECLEGVR DAVATVLGVE PDSVAVHVPL RELGIDSVGL
     TRLTAAIGER LDAEVPSWAV WQCPTVATLA EFLSDGSPRA PAGRASRSAN PATEPVAIVG
     MGCRLPGGID SPERLWAALR SEVDAVGTVP ADRWNAGEWY DPDQSAPGKT TTDRGGFLDD
     ITGFDAAFFR VSPAEAERMD PQQRIALEVV WAALEDARIV PAALSGTRTG VFFGTMWQEY
     HLATGADPAG IGPHSAVGWD TSIVPSRIAY VLGLQGPVLS VGSACSSSLG AVHLAAHSLR
     RGESDIALAG GVSLMLHPHT TVAMTKFGGL NPDGQCRAFD ADAAGYVRSE GCGVVVLRRL
     SDALRDGDRI YAVLRGSAVN NDGASNGLTA PNPRAQVDVL RTAWAEAGVR TDQVSYVEAH
     GTGTPLGDLI EASALGEVFG PGRTEPLRIG SAKTNFGHLE PAAGVLGVLK TALALHHGEL
     PASLHFDRPN PEIDFVGQKL AVVTERQSWP VGPRYAGVSA FGFGGTNVHV ALEQAPHRRR
     RLLAVAADTE PALRARLAAV STAGDIPMSP GPGHHRAVAW LDGCGDPAAT ARVAQVGDRP
     KVVFCFSGHG AQWLGMGAGL LAEPVFRAAI EDVDRALAPV TGWSVLDELL APRLDRADVV
     QPALFAVQVA LTRLLAAWGV SPDVVFGQSV GEVAAAVATG ALFLDQGAEL IGRWSRLVAE
     RASGSGSMIV CDLPAAAADR ISRGRLSIAA AVAEDWTCLS GSTGALVEVE RDLAQAGATV
     RRVAIDYPAH STELAAITPD LVAELAGLRA GQGTIPFLST VTGGPLPGTR LDAGYWARNT
     CQPMRLTEVA AALPADAQVV EIGPHPVLAQ PMRRLLAPGS RVLAACHRDV PARQTVEDLL
     AELWLSGVEV DWAAATGVPA PTVEPVPLTV SSATRTGLRA QAAAMREHLA AHPEQSLAEV
     GHSLVATRSM FDHRAVVLAA DRDQATSGLD ALAAGVPHPG LVTAATEPVR DTAGPVLVFP
     GQGSQWTGMA RELLADSPVF AARFAECAAA LDEFVEWSLI DVLADEAALA RADVVQPALW
     AVMVSLARLW EAHGLRPTAV VGHSQGEIAA ACVGGALSLR DAARVVASRA RVIADTLSGS
     GGMVSVALPR DEAAERAGGW DRRLSVAAEL GPRSTVLAGP DDALEGLMTR CAEAAVVARR
     VAIDYPSHSP GVDPARAEVL AALTGVEPQP AELTHVSTVT GKPLAGVELD ADYWYRNLRE
     PVELRAVVDL LLDRGHRVFV EASPHPVLSP GIEETAAARG LDVVAVASVR RGDGGLSRFL
     TSVTEAHVRG VDLDWALVLS SAGPVDLPTY QFQRRDYWPR VDRRSGAADP ADAEFWGAVE
     RGDLGALRDT LNLPADATLA DLLPALARWR RERIQPEVPE PAPEPAPAAL VELLAGQPPA
     RRLELVTDVV LRNAAAVLGY RGDEPAAPER AFRELGFDSV SGLDLRNRLA AELGLALPPT
     LVYDQPTPAA LAGHLLAELD LDSSAPDPDT AVSASIADAA DDELFDLIDS LTSRRTS
//
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