Acyl-protein synthetase, LuxE (IPR007534)

Short name: LuxE

Overlapping homologous superfamilies


Domain relationships



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 [PMID: 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 [PMID: 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 terms

Biological Process

GO:0008218 bioluminescence

Molecular Function

GO:0047474 long-chain fatty acid luciferin component ligase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.