ID A4X8M2_SALTO Unreviewed; 3033 AA.
AC A4X8M2;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ABP55222.1};
GN OrderedLocusNames=Strop_2780 {ECO:0000313|EMBL:ABP55222.1};
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS 105044 / CNB-440).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP55222.1, ECO:0000313|Proteomes:UP000000235};
RN [1] {ECO:0000313|Proteomes:UP000000235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC {ECO:0000313|Proteomes:UP000000235};
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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DR EMBL; CP000667; ABP55222.1; -; Genomic_DNA.
DR RefSeq; WP_012014003.1; NC_009380.1.
DR STRING; 369723.Strop_2780; -.
DR KEGG; stp:Strop_2780; -.
DR PATRIC; fig|369723.5.peg.2866; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_8_11; -.
DR Proteomes; UP000000235; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd08952; KR_1_SDR_x; 2.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR001995; Peptidase_A2_cat.
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; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR036299; Polyketide_synth_docking_sf.
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; 2.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF18369; PKS_DE; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000235};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..443
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1112..1167
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 1366..1441
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1460..1884
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2872..2947
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2321..2347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2326..2343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3033 AA; 316519 MW; A132F845A4FF3C50 CRC64;
MANDDKLRTF LKRATAELQQ ANRRLREVED RDQEPIAIVG MGCRYPGGVR SPEDLWQLVL
DGTDAISDFP TDRGWDVYGV YDPEPGKPGK SYTRHGGFLY DAADFDPGFF GMSPREAVET
DPQQRLVLEA SWEAFEHGGI DPVGLKGSTT GVFVGMMHHD YVDSTTSGSL VSGRVAYVLG
LEGPAITVDT ACSSSSVAVH LACQSLRREE CGLALAGGVA VMATPQLFVE FSRQRALSPD
GRCRSFGDGA DGAAWSEGVG VLVLERLSDA RRNGHRVYGV VRGSAVNQDG ASNGLTAPNG
PAQQRVIRAA LANARLSVSD VDVVEAHGTG TTLGDPIEAQ AIVATYGRDR DRPLWLGSVK
SNIGHAQAAA GVAGVIKMVM AMRHGVLPRT LHVETPSRQV DWSAGDVRLL TESVEWPAVD
RPRRAGVSSF GISGTNVHLI IEQASPVEDQ APVEDSATGP TPPVTLWPVS GRSLEGLAGQ
AGRVAGFCGG VGVRAVDVGL SLGVGRAGLE FRGVAVGREV SELSAGLEVV AAGGGVSGRV
SSGRTAVLFS GQGAQWVGMG RELAGAFPVF AGALAEVCGV FGPLLGGDLR EVMFVDGGGV
LDRTGWAQPA LFAVEVALFR LAESWGLVPD FVVGHSVGEL VAAYVSGVWS LEDACRVVAA
RGGLMEGLPG GAMLAVGGSV GELELGGVDV AAVNGPRSVV VSGTEEEIAG LEGSLGVWTR
RLRVSHAFHS RLMDPMVADF GRVVGGVRGR VGGVAVVSTV TGEVVTDEVL GSVGYWQGQV
RGTVRFADAV ATLVERGVTR FVEVGPDSVL TGLVAECVPE AAVVVGLQRR GGDQVRAFAA
GMGRVWAAGV DLDWAAVHPG GRQVDLPTYA FQHQHYWLHD TGADKDVSTA GWRYRVMWRA
TNVPTGRHLT GDWWVVTPSA LTDDPRAAAV ADALTARGAT VVRLTDAAPH DRDTPAGVVS
LLGLDDTSDT LNAGLSAGVT GTVRLVHALA AADFTGRLWC LTTGAVAVDP YEDLPHAAQA
GLWGLGTVLS LDYPGWWGGL ADVPADWTPD ILDRLVDVLT DGGEDQVALR NGGVLARRMV
HWPVSGTPDR RWRPTGTVLV TGGTGGIGTH LSEWLLDQGA DRVVLASRRG PAALGAADLA
ARLPAVQVVA CDVTDRDAVA TLLDGIGDDL TAVFHAAGVL RDAAPLDETD LDAFADVCRA
KVLGATHLDA LLADRPLDAF VLFASGAAVW GSAGQAAYGT GNAWLDALAH QRRRQGRTAT
SIAWGTWGGG GMVDDQATEQ LLRQGTPPME PRLALGALQQ VLDHDESHLV VADIDWARFA
PIYTLARPRP LLAALPEANP SVVATAPAPP RETSVLADLP DADRLPYLLD TVRTHVAVVL
GYDASTTVDV QRPFRELGFD SLTAVELRNA VGEAVGLRLP ATMVYDHPTP AVLARHLYDE
LVGTAAAPTV TSTTAGFAPD EPIAIIGMGC RYPGGVRSPE DLWQLVATGT DAISAFPVDR
GWDADALFDA DPDQPGTSYV RSGGFVYDAA KFDAEFFGIS PREAIAMDPQ QRLMLEVTWE
ACERAGLNPE ALRGSSVGVF VGSGAQDYGD LLGLAPAESE AYLSTGTSAS VISGRLSYAF
GFEGPSMTID TACSSSLVAL HLASQALRAG ECATAIASGV LVMSNPTPFV AFSRQRGLAP
DGRCKSFSDD ADGTGWSEGV GVLVLERLSD ARRNGHRVYG VVRGSAVNQD GASNGLTAPN
GPAQQRVIRA ALANARLSVS DVDVVEAHGT GTTLGDPIEA QAIVATYGRD RDRPLWLGSV
KSNIGHTQAA AGVAGVIKMV MAMRHGVLPR TLHVETPSRQ VDWSAGDVRL LTESVEWPAV
DRPRRAGVSS FGISGTNAHV VLEQAPLVGD EESVGLVEVV DPPVVLWPVS GRSLEGLAGQ
AGRVAGFCGG VGVRAVDVGL SLGVGRAGLE FRGVAVGREV SELSAGLEVV AAGGGVSGRV
SSGRTAVLFS GQGAQWVGMG RELAGAFPVF AGALAEVCGV FGPLLGGDLR EVMFVDGGGV
LDRTGWAQPA LFAVEVALFR LAESWGLVPD FVVGHSVGEL VAAYVSGVWS LEDACRVVAA
RGGLMEGLPG GAMLAVGGSV GELELGGVDV AAVNGPRSVV VSGTEEEIAG LEGSLGVWTR
RLRVSHAFHS RLMDPMVADF GRVVGGVRGR VGGVAVVSTV TGEVVTDEVL GSVGYWQGQV
RGTVRFADAV ATLVERGVTR FVEVGPDSVL TGLVAECVPE AAVVVGLQRR GGDQVRAFAA
GMGRVWAAGV DLDWAAVHPG GRQVDLPTYA FQHQHYWIEP DRTDGTATDG TATDGTATDG
TATDGTDGGF WDAVERADVD ALADGLGVAP DVVDEVLPGL AAWRSRHRDA STLDGWRYRV
VWRSTDLPVG GELSGAWWVV VPVTLAGDAR VRAVIEGLAA RGAEVVMVVG VDLPVGDIPA
GVVSLLALDD SRDDTGVGLS AGVVDTVRLI QALAVTGRMG RVWCVTSGGV AIDRFEPVID
LAQGALWGLG TVLSLDYPDW WGGLVDLPVD WTDAHVERFV DVLADGGEDQ VAVRTVGVLA
RRMVRWPAVG TSERRWRPSG TVLVTGGTGG VGEHVTEWLL AGGADRVVLA SRRGLDAPGA
ADLVARHRGV DVVVCDVADR DAVAALLADL GDDLTAVFHA AGVLRPEVPL GETGLDDFAD
VCRAKVLGAV HLDALLADRP LEAFVLFSSG AAVWGSAGQA GYATANAYLD ALAHRRRTRG
VVATSVAWGS WGGGGMAGGE VGAHLRRQGT PPMDPGLAVQ ALRQALDHDE SHLVVADIDW
ARFAPIYTLA RPRPLLTALP DAHPESEPAT PVAATADLAG QLAAMPTPDR LDTILALVRD
QVAAVLGYAS DADVEPERAF KEAGFDSLTA VELRNRLATE TALRLPATLV FDHPTPIELA
RHLLTELAPA DAGGVTLLND LDRLQATLST LDTDAVAALD ESIRAGVGER LKALLATWTA
DQRPAEVVSV TEDLDTASDD DLFEFIDSKF GTS
//
