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0  structures 327  species 0  interactions 387  sequences 5  architectures

Family: LuxE (PF04443)

Summary: Acyl-protein synthetase, LuxE

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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 [1] 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 [2]. 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.

Literature references

  1. 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

  2. Soly RR, Meighen EA; , J Mol Biol 1991;219:69-77.: Identification of the acyl transfer site of fatty acyl-protein synthetase from bioluminescent bacteria. PUBMED:2023262 EPMC:2023262

  3. 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.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan ANL (CL0378), which has the following description:

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 [1]. 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 [1].

The clan contains the following 3 members:

AMP-binding GH3 LuxE

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(7)
Full
(387)
Representative proteomes NCBI
(413)
Meta
(321)
RP15
(47)
RP35
(90)
RP55
(108)
RP75
(124)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(7)
Full
(387)
Representative proteomes NCBI
(413)
Meta
(321)
RP15
(47)
RP35
(90)
RP55
(108)
RP75
(124)
Alignment:
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Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(7)
Full
(387)
Representative proteomes NCBI
(413)
Meta
(321)
RP15
(47)
RP35
(90)
RP55
(108)
RP75
(124)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: DOMO:DM04138;
Previous IDs: none
Type: Family
Author: Kerrison ND
Number in seed: 7
Number in full: 387
Average length of the domain: 321.20 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 83.12 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.1 20.1
Trusted cut-off 20.1 20.2
Noise cut-off 20.0 20.0
Model length: 366
Family (HMM) version: 7
Download: download the raw HMM for this family

Species distribution

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