Summary: Acyl-protein synthetase, LuxE
Acyl-protein synthetase, LuxE Provide feedback
LuxE is an acyl-protein synthetase found in bioluminescent bacteria. LuxE catalyses the formation of an acyl-protein thioester 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  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 carboxyl terminal of the synthetase is though to act as a flexible arm to transfer acyl groups between the sites of activation and reduction . This family also includes Vibrio cholerae RBFN protein (Q06961), which is involved in the biosynthesis of the O-antigen component 3-deoxy-L-glycero-tetronic acid.
Lin JW, Chao YF, Weng SF; , Biochem Biophys Res Commun 1996;228:764-773.: Nucleotide sequence and functional analysis of the luxE gene encoding acyl-protein synthetase of the lux operon from Photobacterium leiognathi. PUBMED:8941351 EPMC:8941351
Morona R, Stroeher UH, Karageorgos LE, Brown MH, Manning PA; , Gene 1995;166:19-31.: A putative pathway for biosynthesis of the O-antigen component, 3-deoxy-L-glycero-tetronic acid, based on the sequence of the Vibrio cholerae O1 rfb region. PUBMED:8529890 EPMC:8529890
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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 (SWISSPROT) 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 (SWISSPROT), 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.
|Molecular function||long-chain fatty acid luciferin component ligase activity (GO:0047474)|
|Biological process||bioluminescence (GO:0008218)|
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This superfamily consists of enzymes including luciferase, long chain fatty acid Co-A ligase, acetyl-CoA synthetase and various other closely-related synthetases as well as a plant auxin-responsive promoter family. The name ANL derives from from three of the subfamilies - Acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes . Members of this superfamily catalyse the initial adenylation of a carboxylate to form an acyl-AMP intermediate, followed by a second partial reaction, most commonly the formation of a thioester .
The clan contains the following 3 members:AMP-binding GH3 LuxE
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Curation and family details
|Number in seed:||2|
|Number in full:||774|
|Average length of the domain:||320.30 aa|
|Average identity of full alignment:||26 %|
|Average coverage of the sequence by the domain:||78.17 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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