ID Q63HU1_BURPS Unreviewed; 544 AA.
AC Q63HU1;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Acyl transferase {ECO:0000313|EMBL:CAH39815.1};
GN OrderedLocusNames=BPSS2329 {ECO:0000313|EMBL:CAH39815.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH39815.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH39815.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH39815.1,
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).
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DR EMBL; BX571966; CAH39815.1; -; Genomic_DNA.
DR RefSeq; YP_112331.1; NC_006351.1.
DR AlphaFoldDB; Q63HU1; -.
DR STRING; 272560.BPSS2329; -.
DR KEGG; bps:BPSS2329; -.
DR PATRIC; fig|272560.6.peg.6787; -.
DR eggNOG; COG0331; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW Transferase {ECO:0000313|EMBL:CAH39815.1}.
FT DOMAIN 456..536
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 544 AA; 57218 MW; 92A112036FEC6222 CRC64;
MVGKGNLMAQ VAFLFPGQGA FYAGATRALS GAYPVVQRAM QAIDAVSVRR LRRPLLATVW
DGHIGAEDLL QHAPDLLQLA IYATSVSYFE ALRARGVRPD VLVGHSFGEI AALTCAGAFS
IETGAEIVCD RIDALRAAAP ADGRMAAVGA SPDAVRAHLA ACFRDARAGR VRIAVENHVS
QTVVSGACEY VDEFRAYCAR NNISAQVLNS PYAFHHEDLE NARIEFGRRL KAYKNKALEY
PVYSPILNRY YTAADDLGAC LARHLVLPVR FGDGVARLKA AGIGAFVECG ALNALSRISV
RALGPGAVKT FPGASSAGGE LAGLENVLAY FNGGSVMNDD IRASNLQLDF DEFWRNSGPG
IVDKIKGELK RFFDARGLQA TPAPQIVADH GVAAGFAGGL TAGAADYAPK VAAGVSSAAA
PVAAPIVAAA PAAPLAVAPA APVAQAAAVP AASARVPRDR LFVELVAIYA EAMEYPVEVF
TETVELEAEL GIDSVKQTEI IQRISARYGL PPLPANFRAG DFKAMGQIVD FVYEHQGEAA
LVTS
//
