ID Q0B244_BURCM Unreviewed; 1303 AA.
AC Q0B244;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ABI91779.1};
GN OrderedLocusNames=Bamb_6235 {ECO:0000313|EMBL:ABI91779.1};
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:ABI91779.1, 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; ABI91779.1; -; Genomic_DNA.
DR RefSeq; WP_011661108.1; NZ_CP009800.1.
DR ESTHER; 9burk-q3fit9; Thioesterase.
DR GeneID; 69549187; -.
DR KEGG; bam:Bamb_6235; -.
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; 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; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
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; 1.
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; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 924..1000
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 898..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1303 AA; 138654 MW; FF0B0181F5214F31 CRC64;
MQGTSLPVSR IAITGTAYRF PGDAACHESY WALLESGRTA VRETPMARFD IQPFFSEDAS
VPGTTYVRNG GYVEGAFEFD AGFFRISESE ALAMDPQQRW MLELCWAALE NAGIAPGTVR
GQSIGVFLGS GEVDYGRRTV WAGDMSKLTT YARLGASRPT LAGRVAYFLG VHGPAVFVDT
ACSSSLTAVH LAAQSLRAGD CDIAIAGGIN LILSPEETIL GARLQAMSPS EMCRPFDARA
DGYLRGEGGG VVVLKRIDDA VRDGDRIDAV LAGSAINNDG ASNGLTAPNG AAQESAIRVA
LRRAGVGPAS VAYVEAHGTG TQLGDPIELT ALRNAYTAGV ERARPLLVGS VKAQIGHLEA
GAGIAGLIKA MLILSRRRVP VQANFDDPTP RFRWDDSQIC VPRTGEDALD ENGMVGVNGF
GISGTNVHLV LAGAGAREVA MDEERIPRVL PLSARSPEAV VRLAHAYRKM LHTAGPAAGD
ICYTASVRRD HWPHRAAVVG DSREQLLESL DDFLAGNAEG NWHSASVAKS RRLVFLFPGQ
GAWKPGVGAQ LYDDNPVFHR FVDECLAYLD PALAADVMAA IRGHHPETVR HRQGQLAHFV
ILHSLARTWI ESGNRPDAVV GHSLGEHVAA TLAGVMTLED GLKAVEARGR LFDTATPRGA
MLAVAAGVTE LQRLFEFGEV LFVAGINGPE QTVVSGTAAA IEEVHATMVA MGRRASMLGT
YDTPGHSPLL APMRPAFAQA LSALRFMPPR ITLISTLTGK PAGAEIAGIE HWLDLVERPV
LFADALGQFA DQDCVFLEVG PGAALSNLAR AATQKWESVV SSLADAPGDD ATESMNFAHA
CAHLYCLGFM RDWAALYPRP PRPAQVPTYP FERVHLELPM TLRAAASVDT EVEGTATGRD
AGISHDASNT GPTSVEATSG DLSRERAHVL DAIRRIARSV SSGAAAIDDD VPLAASGFDS
LALTELRSRM QHMFGHTVPM AVLARGASIS RLAELMAAAP IAKDSAARTS QTVPADMREA
LPARGAPEDR GMRAPPAEEP LIVLRHGEGE MVALIHPIGG DVLCYQALAD AWPGDPTIVG
LRHPDVDRPT LPFHRPLAEL ASGYRDVLER EFGRLPDRVG GWSFGGLVAL EMAAQWESEG
KVAPPLMLVD SPFPTGDFAL RLKEIVGSTT ALPSLADIDA LAKDARFVAL LDRDLGLLEM
RARLDPPEFA RISRLYASSV VSIVSRSFTA LRAPIHYALA ANGGNGRCRD DVWPHLARLT
TGAIEVDVFD DDHNSIVGGA SVRRLAARLG RRIAEMQAAA SGD
//
