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Database: UniProt
Entry: F9U9E1_9GAMM
LinkDB: F9U9E1_9GAMM
Original site: F9U9E1_9GAMM 
ID   F9U9E1_9GAMM            Unreviewed;      1848 AA.
AC   F9U9E1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=6-deoxyerythronolide-B synthase {ECO:0000313|EMBL:EGV19399.1};
DE            EC=2.3.1.94 {ECO:0000313|EMBL:EGV19399.1};
GN   ORFNames=ThimaDRAFT_1543 {ECO:0000313|EMBL:EGV19399.1};
OS   Thiocapsa marina 5811.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocapsa.
OX   NCBI_TaxID=768671 {ECO:0000313|EMBL:EGV19399.1, ECO:0000313|Proteomes:UP000005459};
RN   [1] {ECO:0000313|EMBL:EGV19399.1, ECO:0000313|Proteomes:UP000005459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5811 {ECO:0000313|EMBL:EGV19399.1,
RC   ECO:0000313|Proteomes:UP000005459};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA   Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V., Frigaard N.-U.,
RA   Bryant D., Woyke T.J.;
RT   "The draft genome of Thiocapsa marina 5811.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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DR   EMBL; AFWV01000004; EGV19399.1; -; Genomic_DNA.
DR   STRING; 768671.ThimaDRAFT_1543; -.
DR   PATRIC; fig|768671.3.peg.1642; -.
DR   eggNOG; COG3321; Bacteria.
DR   OrthoDB; 9778690at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000005459; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
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:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 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; PF00550; PP-binding; 2.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:EGV19399.1};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005459};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGV19399.1}.
FT   DOMAIN          381..459
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          483..905
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1747..1826
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          338..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1848 AA;  197207 MW;  66CA4B3B76F67F99 CRC64;
     MRLNLGNRIY YRDAGGLEEP GRVAVLFPGF GHRDTGLARQ LCGLSPAVDA WYGSVAGPRP
     FGLASGDSGS ELAGMLDDVL MADLAMWVLL RDLGLSCDLL VGHSFGEHAA LVASGMVPSL
     ADLSPLFASV ASLDAEGDPL GMLAITEAAV DLIAPEMQRD PPSVFMALDN CRQQKVFWGQ
     PEVLGRVEAQ VKAQGLLAYR LAGLACPVHT PAFPVGGEQL RRDYAALALS APRIPVWSCS
     RLRPLPEERT AATEVLAAQW HEPVRFRESI LALFDAGFRT FVEVGPGERL SGFVRETLRG
     KGVSAVPTHR EGHPPLQTIH VALAQLYLLG QAIAPDRLSP RPSVSEERFD GRGITSSGPP
     ETRGESGPPP AVQQPASTDR QRFRDLVEVI QGEVAGLLDL ADPESLDSET GFFDLGLGSL
     GCVELSERLG RVLGRSLPQT LAFDYPDITR LARALASAPG TSPECAGSDA GRATAASESA
     SENEPIAIVG IGCRFPGGVD SPDAFWQLLR EGRDAISEVP PERWDPGVYE GWIDADQREA
     ARFGGFLADA LGFDADFFGI SPREAKTLDP QQRMLLEVSW ESLEDACIDP KGLGGSRTGV
     FVGISSADYV QRLSPTQRLE VGGYLATGNA PSTAAGRIAF ALGLNGPAMA VDTACSSSLV
     AVHLACASLR RGESDLALAG GVNLMLNPET TVFLANAHAL SRSGRCRTFD AGADGYVRAE
     GCGVVVLKRL SDALAAGDAV VAVVLGSAVN HDGRTSGLTV PSGPAQNALI RDCLHSAGVE
     PSEVGYLEAH GTGTPLGDPI ELQALGEVFR STRAVPLRLG SVKSNIGHLE AAAGIAGLIK
     AALQLRRRRL VPSLHFRTPN PRSNWASLPF EVNRDDRDWD SVGRRIAGVS SFGISGTNAH
     VILAEAQSTR SAIEQNAESD GADTGRAHLL VLSARTPEAL RTAALRMVDR LEESPVDRSM
     DPGAVEPGAF TTLVGCPAST LVDCASLVHP TPLVHPTPLV QPTAPIGDVA GFIGDAVEPL
     SALCRTSWLG RHHWRYRIGV VARSRLEARD RLRERMASAA VDRAGAEARA PRVAFLFTGQ
     GSHEPGMGRE LYATEPVFRR AFDRCCEGLA PDLEAPLAEV VLDPRDRRLE QTAWAQPGLF
     ALEYALVETW RSRGIVPDVV MGHSLGEYVA ACVAGVMSLE DALRLVAVRA RLMQSLPAGG
     GMLSVAASPE GLESVVSLAS LGLDLAAVNG PASLVVAGPV GALDRAERRL MEAGIGCRRL
     PVSHAFHSRL VEPILAEFGR YVAACRLSEP RIEMVSNLTG ERVRHEVTDP AYWVDHLRRT
     VRFEAGMRTL STLGCDAYVE IGPKPVLTAL GRESADDARG VLWLASMQPP VDPSLTLLNA
     LGQLYERGAD PEWTGLEPAA AKRPRARLPT TPFERRSFWI EIAEGRHDAV APSDAPPRLP
     GLLLNLPGNT GALRFEARTG VGLTPELDGY PALAERALPP GLLLYAALRA ARRAAPGIEM
     WLEALRLVDV QRLADPCVIL HTLVKTPNAD PGVVEIYGRA EGVEDAPWSL LIQARLRAVS
     GSPQPEPRPM SGRTRDADES LLARLRSAHS AIEKAAFYRA GEQLGFRYGP DLQVLREIRL
     GMHAASAVLD LQTGGGVDPS PLPDLPLAAI EGGLQLLGGL DAGATPPRVR QLRAIDRIDV
     AAPLPREVLV LVWRAEDHAS ATIRLLDARS FLLCAELSGI QSDAMEITRV STAEGEIRDR
     LERVPREEWP PLIVGFVNRI AGLIIDGSPD YRIDPSRPLT ELGLDSLMAL RIAIELKADL
     GVEIPVSQIV SGATIETLAA VSVEQVMDGD LTTEVSQRLD GFFQEGEL
//
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