ID Q0B1F1_BURCM Unreviewed; 1474 AA.
AC Q0B1F1;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ABI92022.1};
GN OrderedLocusNames=Bamb_6478 {ECO:0000313|EMBL:ABI92022.1};
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI92022.1, ECO:0000313|Proteomes:UP000000662};
RN [1] {ECO:0000313|Proteomes:UP000000662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000442; ABI92022.1; -; Genomic_DNA.
DR KEGG; bam:Bamb_6478; -.
DR PATRIC; fig|339670.21.peg.6378; -.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR Proteomes; UP000000662; Chromosome 3.
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; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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 SMART; SM01294; PKS_PP_betabranch; 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 588..665
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 679..1087
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1474 AA; 157443 MW; D6ADFA050759E7F9 CRC64;
MLPDTKFRTV TEIFIFRGKV EPEKRAFIFL ENGESERARL TFGDLDKRAR GIAARLQGMA
QPGDRVLLVY PPGLEFICAW VGCLYAGLIG VPAYPPRRHR PADRLKAIVA DASPVVALTD
AATLDGIAHR ADGYSDTLEL KILATDQGFD APAEQWRAPD ITPQTLALLQ YTSGSTGTPK
GVMISHANIL SNMAVIAEAS DADASTVFVS WLPVFHDMGF FGKVLLPIYL GVPAVLMAPA
AFVQKPIRWL QAITKYRGTH CAAPDFAYDL CARKISDEAR ALLDLSSWRV AFNGAEPVRA
ESVARFSRAF AACGFHAHTM RPVYGMAEAT LFISGQPARS LPLVADYDAD GLARGVATRS
DGGKRHALVS CGRAWAEHRL QIVNPDTGER CPPDRIGEIW VTGPSVGVGY WNRVDETEHT
FRAKLDGDDA HYLRTGDLGF VDGENLFVTG RLKDLIIVAG RNHYPQDLEQ SAEGSHPALA
PNASAAFSIN VDDVERVVIA CEVRREALNT LDAEAVAAEI RRKLAEAHDV DLYAAILLKP
ATILRTSSGK IQRSRIRQAF LDEQGLAIAG EWRRSFSATY APSTAALRDT QTLVQWCVER
VSRLSGIDAG KIDPDAPFSI YGLDSKDAIM LSGELQDWLG LPVSPTVVYD FPSISLLARH
LSGTGNAVPD HAPGSAAARA DIAIVGMGCR FPGAGHPDAF WQLLLEGRDA VGASKKRAGD
LPPTGLLDQV DLFDAAFFGI SAREAEAMDP QQRLLLEVAW ETLEHAGIAP GRLAGGRTAV
IVGISNSDYI RLAQEEVADV GPYVATGNAL SVAANRISYT LDLRGPSWAV DTACSSSLVA
VHHACRALQR GEADAALAGG VNLILAPQLS DSFTQAGMLS PDGRCKAFDA AANGYVRGEG
AGMVLLKRLD DALEHGDTVY AVIRGSAVNQ DGRSNGLTAP NGPAQQAVIR GALHDAGVRA
QDIGFVEAHG TGTPLGDPIE LNALAAVLGE SRRPDDHCWI GSVKTNIGHL ESAAGIASLI
KTALALHHRA IPPNLHFRSI NPEIALDGTP FRIPQQVTPW HSEHGPRMAG VSSFGFGGTN
AHMILSEAPR PGEIEADPAA PAARVVTLSA RTPEALQALA ASYAAYLDAH PGIRVRDVAF
TANTGRTHFT RRAAIVASSL DTLRSQLDAV SAGEPADTPP AVTFHFCADH GGSDDAVRQL
RSACPAFGAL MQRQSAVSDA PAVDSAAAGF TAFQRALAQL WMSFGITPGA VSSTGDGHRA
AAAFADVPQA PDGAAAGSHG IVIEIGAHTA AWDTILRTLA ELYVRGASID WDAVEQDAPR
RRLALPTYPF ERRAFWISPR APRHPLLGRL MEQHAHAPAT WIWQSRLDAP ATTFLSGHRV
KGSPVLPYSA YVEMALAATS EIGAASHTTL KDLALHAPLP LHPHASHSVQ TVLSRRSWGP
FSFAVYHRIE DTRAAASWQI CASAEIHESD RSHA
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