ID E4W4U8_9BURK Unreviewed; 1475 AA.
AC E4W4U8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Putative beta-ketoacyl synthetase {ECO:0000313|EMBL:ADT64846.1};
OS Burkholderia contaminans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=488447 {ECO:0000313|EMBL:ADT64846.1};
RN [1] {ECO:0000313|EMBL:ADT64846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MS14 {ECO:0000313|EMBL:ADT64846.1};
RX PubMed=19167363; DOI=10.1016/j.bbrc.2009.01.073;
RA Gu G., Smith L., Wang N., Wang H., Lu S.E.;
RT "Biosynthesis of an antifungal oligopeptide in Burkholderia contaminans
RT strain MS14.";
RL Biochem. Biophys. Res. Commun. 380:328-332(2009).
RN [2] {ECO:0000313|EMBL:ADT64846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MS14 {ECO:0000313|EMBL:ADT64846.1};
RX PubMed=19500142; DOI=10.1111/j.1574-6968.2009.01653.x;
RA Gu G., Wang N., Chaney N., Smith L., Lu S.E.;
RT "AmbR1 is a key transcriptional regulator for production of antifungal
RT activity of Burkholderia contaminans strain MS14.";
RL FEMS Microbiol. Lett. 297:54-60(2009).
RN [3] {ECO:0000313|EMBL:ADT64846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MS14 {ECO:0000313|EMBL:ADT64846.1};
RA Gu G., Smith L., Wang N., Wang H., Lu S.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; EU938698; ADT64846.1; -; Genomic_DNA.
DR KEGG; bcon:NL30_34420; -.
DR PATRIC; fig|488447.4.peg.7507; -.
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; cd05931; FAAL; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR040097; FAAL/FAAC.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049552; PKS_DH_N.
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:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 589..666
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 680..1088
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1475 AA; 157681 MW; CF55748734B70AA8 CRC64;
MLPDTKFRTV TEILLFRGKV EPEKTAFIFL ENGEAELTRL TFGDLDKRAR GIAARLQAIA
QPGDRVLLVY PPGLEFICAW VGCLYAGLIG VPAYPPRRHR PADRLKAIVA DATPVVALTD
AATLDGIAHH ADGYSDTLEL KILATDQRFD APAEQWRAPD ITPQTLALLQ YTSGSTGTPK
GVMISHANIL SNMAVIAEAS DADASTVFVS WLPVFHDMGF FGKVLLPIYL GVLSVLMAPA
AFVQKPVRWL QAITKYRGTH CAAPDFAYDL CARKIADEAR AQLDLSSWRV AFNGAEPVRA
ESVARFSRAF AACGFHAHTM RPVYGMAEAT LFISGQPARS LPRVADYDAD ALAQGVATRN
DSGKRHALVS CGRTWAEHRV RIVNPDTGER CAPGRIGEIW LTGPSVGVGY WNRIDETERT
FRAKLDGDDA RYLRTGDLGF VDGEDLFVTG RLKDLIIVAG RNHYPQDLEQ SAEGSHPALA
PNASAAFSIH VDNVERVVVA CEVRREALNT LDAEAVAAEI RHTLAEVHDV DLYAAVLLKP
ATILRTSSGK IQRSRIRQAF LDEQGLAIAG EWRRAFSAPP APPQTAEPRD TQALVQWCIE
RVSRLSGIAS GKIDPDAPFS VHGLDSKDAI MLSGELQDWL GRPVSPTVVY DFPSISLLAR
HLSGTGSAMP DQAPGSAEAR ADIAIVGMGC RFPGAGNPDA FWQLLLEGRD AVGAATQRAA
DLPLAGLLDQ VDQFDAAFFG ISAREAESMD PQQRLLLEVA WETLEHAGIA PRSLAGGRTA
VIVGISNSDY IRLAQDEVAD VGPYVATGNA LSVAANRISY ALDLRGPSWA VDTACSSSLV
AVHQACRALQ RGESDAALAG GVNLILAPQL SASFTQAGML SPDGRCKAFD AAANGYVRGE
GVGMVLLKRL DDALENGDTV FAVIRGSAVN QDGRSNGLTA PNGPAQQAVI HGALRDAGVR
AQDIGFVETH GTGTPLGDPI ELNSLAAVLN ESRRPDDLCW IGSVKTNIGH LESAAGIASL
IKTALALHHR AIPPNLHFRS INPQIALDGT PFRIPRQVTP WHSEHGPRLA GVSSFGFGGT
NAHLILSEAP GLPEIEAEPV APAARVVTLS ARTPDALQAL AASYAAYLDA HPEAGVRDVA
FTANTGRTHF TQRAAIVAPS RDSLRAQLDS VSSGEPAETP PAVTFHFCAD DGASADAVRQ
LRAASPAFDA LMQRQSDASG APALAPDEAG FTRFQRALAQ LWMSFGIAPD AVSSTGDGQR
AAAAWAGVPQ APDSGAAGHP GIVIDIGAHT AAWDAILHTL AALYVRGASI DWDAVEQGAP
HRRLALPTYP FERRGFWIRP HARRHPLLGR LMEQHAHAPA TWIWQSRLDA PATNFLDGHR
VKGSPVLPYS AFVEMALSAT SEIGAAGHTT LKDLALHAPL PLHPHESHTV QTVLSRRSWG
PFSFAVYHRI DDTRAAATWQ MCASAEIHES DRSHA
//
