ID Q63LK6_BURPS Unreviewed; 1562 AA.
AC Q63LK6;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:CAH38470.1};
GN OrderedLocusNames=BPSS1009 {ECO:0000313|EMBL:CAH38470.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH38470.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH38470.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH38470.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|RuleBase:RU003694}.
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DR EMBL; BX571966; CAH38470.1; -; Genomic_DNA.
DR RefSeq; WP_011205501.1; NZ_CP009537.1.
DR RefSeq; YP_111015.1; NC_006351.1.
DR STRING; 272560.BPSS1009; -.
DR KEGG; bps:BPSS1009; -.
DR PATRIC; fig|272560.6.peg.5136; -.
DR eggNOG; COG3321; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR024320; LPG_synthase_C.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF09924; LPG_synthase_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 953..1382
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1562 AA; 168073 MW; 45BBAB0829898DF2 CRC64;
MQATFNPGEV ALAGDARRTD GDADRAAASP HGFRFVEKAR IADEPGLSAR LAARKGDAHQ
DGVFLDLWPS IFLSDEHGDH IHVLRDRGLL FVTRFVGAPQ REAALLSALL DRARGEGRAL
CYLDMSNRRK PDIERECGLL STPLGVVQTI DDIRRFTLDG PRMRKLRYLV SKFGRDPSCR
VVEYTEPDPA VDGEIRAVMA AWSREKGVVN KVDAILADMR VGNLLKRYRV YLTYLGDRLQ
NVVVLSHIGE GYITDQEYFV PDMPLGGTEY AYATIIERLA AEGHRKFSLG LTWGLFEPEA
GFSDAEGWAL VNRTEGQLAQ IFRRGVQNHQ YKNKYCPAEY PLYLYRSADS RPQIIKQCMG
QFFRNGVPYD EIARQIEADD ARALAAAGAA PPRATHGGDE AEARSAPGGA PDDASFDVPD
EAPIEVSDHA PGSTPPPRAA RNERGGERDG GKGGQAGQAD RSGKHDPADA RGRAASGTPD
AARAPAPADI PDAFFDATQA DPNAIRLDLV SDSWAHLGYP FIRERARRLL AGLASPHADP
AAPCGLFGVD HCVLTTSGRN AERVFFNLFP AKRKTILQNI PFFSTRHNAA KAGFASVEIP
DPRIFDPDCR EIFRGGIDFA RLREQLEARP DGVAMVLIEL CNNASGGYPV PLAQIADVSA
LCRARGVPFV MDVTRIVRNA ELIRRHEPGC ANVGLWDTVA RIVAHADVVF GSLCKDFGVS
AGGIVAANDG RLIGKARRYA EIEGALLDHV QTQVVCASLG ERDALERGVA AQLDVARRVS
DALDARRIPA LLPVVGHCAL VRAADMPGYA GRRYPRESLL RALLERHGVR AGIHLAGSGA
ERVIDRCIRI ALPIGLDDAR LASGLADALA GTAPGATDAP AALPDLLHAR APGAADTADT
VDTVDKVDTA DTADTADTAD TADTADTADT AAQAGVRRGE AHASRAPMRA SDDDAIAIVG
MAGRYPGADD LSAFWRNLVD GVNAITEIPA ERWDWRAHYH PDPEQAARLR KSYGKWGGFL
GEFDCFDPLF FWMAPRRIAM IDPQERLFLE ECWKALEDAG YPPSRLGDAL RERTGVFGGL
SKHGFSLYAS QYAGTQPHTS PASMVGRVSH FFDLKGPSVA IDNHCASSLV AVHEACEYLR
RGDGDLAIAG GVSLCLHPSS YVQLSLVRML SRDAHCAAFD EGGAGYVPGE GVGVVVLKRL
AQARAHGDPI HAVIRSGAVN HNGRMRYYGQ PDQAGQQAAI RAALARARID PRSISYIEAA
ASGVETTDAV EMAALTEVFG DRAGAAGAYT IGTVKPAIGH GEAASGMSQL MRVALSLKHA
TLTPTRLPRR PSPLIDFDRL PFRLAAEAAP WAPVSVDGRP VPRRAGVTAI GNGVNAHLVL
EEWPGAPADD SAAAPREPQV FVLSAQDGER LAAYVERWIA FLASGATPDF GRMLRTLQIA
REPMPARLAL VASDRDDLLR ALRAWRDGGG ASSRVHRGDA RRRAGQAALA EQACDPRACA
PDEAAAAWVQ GRTVRWEALH RGGPWRRVGG LPAYPFARER YRIADAASGA PAGREEASAR
PD
//
