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10  structures 3646  species 0  interactions 4400  sequences 17  architectures

# Summary: Tetraacyldisaccharide-1-P 4'-kinase

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This is the Wikipedia entry entitled "Tetraacyldisaccharide 4'-kinase". More...

# Tetraacyldisaccharide 4'-kinase

LpxK
Identifiers
SymbolLpxK
PfamPF02606
Pfam clanCL0023
InterProIPR003758
OPM superfamily124
OPM protein4ehx
tetraacyldisaccharide 4'-kinase
Identifiers
EC no.2.7.1.130
CAS no.107309-06-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Tetraacyldisaccharide 4'-kinase is an enzyme that phosphorylates the 4'-position of a tetraacyldisaccharide 1-phosphate precursor (DS-1-P) of lipopolysaccharide lipid A. This lipid forms outer membranes of Gram-negative bacteria.[1] This enzyme catalyzes the chemical reaction

ATP + [2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl]-(1->6)-[2- N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl phosphate] ${\displaystyle \rightleftharpoons }$ ADP + [2-N,3-O-bis(3-hydroxytetradecanoyl)-4-O-phosphono-beta-D- glucosaminyl]-(1->6)-[2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D- glucosaminyl phosphate]

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor.

## References

• Ray BL, Raetz CR (1987). "The biosynthesis of gram-negative endotoxin. A novel kinase in Escherichia coli membranes that incorporates the 4'-phosphate of lipid A". J. Biol. Chem. 262 (3): 1122â€“8. PMIDÂ 3027079.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

# Tetraacyldisaccharide-1-P 4'-kinase

This family consists of tetraacyldisaccharide-1-P 4'-kinase also known as Lipid-A 4'-kinase or Lipid A biosynthesis protein LpxK, EC:2.7.1.130. This enzyme catalyses the reaction: ATP + 2,3-bis(3-hydroxytetradecanoyl)-D -glucosaminyl-(beta-D-1,6)-2,3-bis(3-hydroxytetradecanoyl)-D-glucosam inyl beta-phosphate <=> ADP + 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D- glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate. This enzyme is involved in the synthesis of lipid A portion of the bacterial lipopolysaccharide layer (LPS) [1]. The family contains a P-loop motif at the N terminus.

## Literature references

1. Garrett TA, Que NL, Raetz CR; , J Biol Chem 1998;273:12457-12465.: Accumulation of a lipid A precursor lacking the 4'-phosphate following inactivation of the Escherichia coli lpxK gene. PUBMED:9575203 EPMC:9575203

This tab holds annotation information from the InterPro database.

# InterPro entry IPR003758

Tetraacyldisaccharide 4'-kinase phosphorylates the 4'-position of a tetraacyldisaccharide 1-phosphate precursor (DS-1-P) of lipid A, but the enzyme has not yet been purified because of instability [ PUBMED:9575203 ]. This enzyme is involved in the synthesis of lipid A portion of the bacterial lipopolysaccharide layer (LPS).

### 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...

# 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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

## View options

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
(97)
Full
(4400)
Representative proteomes UniProt
(25770)
RP15
(673)
RP35
(2114)
RP55
(4476)
RP75
(7945)
Jalview View  View  View  View  View  View  View
HTML View  View
PP/heatmap 1 View

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, not available.

## Format an alignment

Seed
(97)
Full
(4400)
Representative proteomes UniProt
(25770)
RP15
(673)
RP35
(2114)
RP55
(4476)
RP75
(7945)
Alignment:
Format:
Order:
Sequence:
Gaps:

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
(97)
Full
(4400)
Representative proteomes UniProt
(25770)
RP15
(673)
RP35
(2114)
RP55
(4476)
RP75
(7945)

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

# 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.

# 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

 Seed source: COG1663 Previous IDs: none Type: Family Sequence Ontology: SO:0100021 Author: Bashton M , Bateman A Number in seed: 97 Number in full: 4400 Average length of the domain: 309.70 aa Average identity of full alignment: 30 % Average coverage of the sequence by the domain: 91.61 %

## HMM information

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.5 27.0
Noise cut-off 26.9 26.7
Model length: 327
Family (HMM) version: 17

# Species distribution

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### Colour assignments

 Archea Eukaryota Bacteria Other sequences Viruses Unclassified Viroids Unclassified sequence

### Selections

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# Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the LpxK domain has been found. There are 10 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

# AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information