Summary: Lipid-A-disaccharide synthetase
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Lipid-A-disaccharide synthetase Provide feedback
This is a family of lipid-A-disaccharide synthetases, EC:2.4.2.128. These enzymes catalyse the reaction: UDP-2,3-bis(3-hydroxytetradecanoyl) glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate <=> UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6 -beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. These enzymes catalyse the fist disaccharide step in the synthesis of lipid-A-disaccharide.
Literature references
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Servos S, Khan S, Maskell D; , Gene 1996;175:137-141.: Cloning and expression of genes encoding lipid A biosynthesis from Haemophilus influenzae type b. PUBMED:8917090 EPMC:8917090
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Crowell DN, Reznikoff WS, Raetz CR; , J Bacteriol 1987;169:5727-5734.: Nucleotide sequence of the Escherichia coli gene for lipid A disaccharide synthase. PUBMED:2824445 EPMC:2824445
Internal database links
SCOOP: | DUF354 Epimerase_2 Glyco_tran_28_C Glyco_transf_28 Glyco_transf_4 Glycos_transf_1 Glyphos_transf |
Similarity to PfamA using HHSearch: | Glycos_transf_1 |
External database links
CAZY: | GT19 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003835
The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates ([intenz:2.4.1.-]) and related proteins into distinct sequence based families has been described [ PUBMED:9334165 ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. The same three-dimensional fold is expected to occur within each of the families. Because 3-D structures are better conserved than sequences, several of the families defined on the basis of sequence similarities may have similar 3-D structures and therefore form 'clans'.
These enzymes belong to the glycosyltransferase family 19 CAZY . Lipid-A-disaccharide synthetase EC is involved with acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase EC and tetraacyldisaccharide 4'-kinase EC in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli and other bacteria. These enzymes catalyse the first disaccharide step in the synthesis of lipid-A-disaccharide.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | lipid-A-disaccharide synthase activity (GO:0008915) |
Biological process | lipid A biosynthetic process (GO:0009245) |
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 GT-B (CL0113), which has the following description:
This is the GT-B clan that contains diverse glycosyltransferases that possess a Rossmann like fold [1].
The clan contains the following 51 members:
A-2_8-polyST AGT ALG11_N Alg14 Asp1 Capsule_synth DUF1205 DUF1972 DUF2827 DUF3492 DUF354 DUF6716 Epimerase_2 FucT_N FUT8_N_cat Glyco_tran_28_C Glyco_trans_1_2 Glyco_trans_1_3 Glyco_trans_1_4 Glyco_trans_4_2 Glyco_trans_4_3 Glyco_trans_4_4 Glyco_trans_4_5 Glyco_transf_10 Glyco_transf_11 Glyco_transf_20 Glyco_transf_28 Glyco_transf_4 Glyco_transf_41 Glyco_transf_5 Glyco_transf_52 Glyco_transf_56 Glyco_transf_9 Glyco_transf_90 Glycogen_syn Glycos_transf_1 Glycos_transf_N Glyphos_transf LpxB MGDG_synth Mito_fiss_Elm1 NodZ O-FucT Phosphorylase PIGA PM0188 PS_pyruv_trans Sua5_C Sucrose_synth T4-Gluco-transf UDPGTAlignments
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...
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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 (4721) |
Representative proteomes | UniProt (26390) |
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RP15 (714) |
RP35 (2247) |
RP55 (4758) |
RP75 (8391) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
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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 (4721) |
Representative proteomes | UniProt (26390) |
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RP15 (714) |
RP35 (2247) |
RP55 (4758) |
RP75 (8391) |
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Raw Stockholm | |||||||
Gzipped |
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.
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
Seed source: | COG0763 |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Bashton M |
Number in seed: | 7 |
Number in full: | 4721 |
Average length of the domain: | 347.4 aa |
Average identity of full alignment: | 31 % |
Average coverage of the sequence by the domain: | 93.64 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 374 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 LpxB domain has been found. There are 3 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.
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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.