LuxE

• PFAM accession number: PF04443
• Interpro abstract (IPR007534):

  LuxE is an acyl-protein synthetase found in bioluminescent bacteria. LuxE catalyses the formation of an acyl-protein thiolester from a fatty acid and a protein. This is the second step in the bioluminescent fatty acid reduction system, which converts tetradecanoic acid to the aldehyde substrate of the luciferase-catalysed bioluminescence reaction [ (PUBMED:8941351) ]. A conserved cysteine found at position 364 in Photobacterium phosphoreum LuxE ( Q52100 ) is thought to be acylated during the transfer of the acyl group from the synthetase subunit to the reductase. The C-terminal of the synthetase is though to act as a flexible arm to transfer acyl groups between the sites of activation and reduction [ (PUBMED:2023262) ]. A LuxE domain is also found in the Vibrio cholerae RBFN protein ( Q06961 ), which is involved in the biosynthesis of the O-antigen component 3-deoxy-L-glycero-tetronic acid.

  This entry represents the LuxE domain, which is found in archaeal and bacterial proteins.

• GO process: bioluminescence (GO:0008218)
• GO function: long-chain fatty acid luciferin component ligase activity (GO:0047474)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry LuxE