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LOCUS WP_000163973 306 aa linear BCT 21-MAR-2023 ACCESSION WP_000163973 VERSION WP_000163973.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 306) AUTHORS Shindou,H., Hishikawa,D., Harayama,T., Yuki,K. and Shimizu,T. TITLE Recent progress on acyl CoA: lysophospholipid acyltransferase research JOURNAL J Lipid Res 50 Suppl (Suppl), S46-S51 (2009) PUBMED 18931347 REFERENCE 2 (residues 1 to 306) AUTHORS Shindou,H. and Shimizu,T. TITLE Acyl-CoA:lysophospholipid acyltransferases JOURNAL J Biol Chem 284 (1), 1-5 (2009) PUBMED 18718904 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10792834 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..306 /organism="Salmonella" /db_xref="taxon:590" Protein 1..306 /product="Kdo(2)-lipid IV(A) acyltransferase" /EC_number="2.3.1.241" /GO_function="GO:0016747 - acyltransferase activity, transferring groups other than amino-acyl groups [Evidence IEA]" /GO_process="GO:0036104 - Kdo2-lipid A biosynthetic process [Evidence IEA]" /calculated_mol_wt=35083 Region 1..306 /region_name="PRK06860" /note="lipid A biosynthesis lauroyl acyltransferase; Provisional" /db_xref="CDD:235880" Site order(132,135,137,153..156,201..203) /site_type="active" /note="putative acyl-acceptor binding pocket [active]" /db_xref="CDD:153246" ORIGIN 1 mtklpkfsva llhprywltw lgigalwlvv qlpypviykl gcalghlarr vmkrrakiay 61 rnlelcfpem saqerhtmvv knfesvgmgv metgmawfwp drrvnrwmea sglehirevk 121 aqglgfilvg ihfltlefga rmfgmhnpgi gvyrpndnpl ldwlqtwgrl rsnksmldrk 181 dlkgmvkalk sgeliwyapd hdygprasvf vplfavdqaa ttsgtwmlar mskaciipfv 241 prrkpdgkgy eliilpaeys pplesaeata awmnkiveqc immapeqymw lhrrfktrpe 301 gvpsry