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36  structures 653  species 0  interactions 11071  sequences 87  architectures

Family: Glyco_transf_29 (PF00777)

Summary: Glycosyltransferase family 29 (sialyltransferase)

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Sialyltransferase". More...

Sialyltransferase Edit Wikipedia article

Enzymes that tranfer sialic acid to nascent oligosaccarides. Each sialyltransferase is specific for a particular sugar substrate.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Glycosyltransferase family 29 (sialyltransferase) Provide feedback

Members of this family belong to glycosyltransferase family 29 [1].

Literature references

  1. Campbell JA, Davies GJ, Bulone V, Henrissat B; , Biochem J 1997;326:929-939.: A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities PUBMED:9334165 EPMC:9334165


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001675

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'.

Glycosyltransferase family 29 ( CAZY ) comprises enzymes with a number of known activities; sialyltransferase ( EC ), beta-galactosamide alpha-2,6-sialyltransferase ( EC ), alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase ( EC ), beta-galactoside alpha-2,3-sialyltransferase ( EC ), N-acetyllactosaminide alpha-2,3-sialyltransferase ( EC ), alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase ( EC ); lactosylceramide alpha-2,3-sialyltransferase ( EC ). These enzymes use a nucleotide monophosphosugar as the donor (CMP-NeuA) instead of a nucleotide diphosphosugar.

Sialyltransferase may be responsible for the synthesis of the sequence NEUAC-Alpha-2,3-GAL-Beta-1,3-GALNAC-, found on sugar chains O-linked to thr or ser and also as a terminal sequenec on certain gagnliosides. These enzymes catalyse sialyltransfer reactions during glycosylation, and are type II membrane 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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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
(131)
Full
(11071)
Representative proteomes UniProt
(20232)
RP15
(1347)
RP35
(3509)
RP55
(8418)
RP75
(11428)
Jalview View  View  View  View  View  View  View 
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PP/heatmap 1            

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

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

Format an alignment

  Seed
(131)
Full
(11071)
Representative proteomes UniProt
(20232)
RP15
(1347)
RP35
(3509)
RP55
(8418)
RP75
(11428)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

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
(131)
Full
(11071)
Representative proteomes UniProt
(20232)
RP15
(1347)
RP35
(3509)
RP55
(8418)
RP75
(11428)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

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: Pfam-B_1020 (release 2.1)
Previous IDs: Sialyltransf;
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 131
Number in full: 11071
Average length of the domain: 219.6 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 63.43 %

HMM information View help on HMM parameters

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 23.0 23.0
Trusted cut-off 23.0 23.0
Noise cut-off 22.9 22.8
Model length: 274
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 Glyco_transf_29 domain has been found. There are 36 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.

Protein Predicted structure External Information
A0A0G2JWU8 View 3D Structure Click here
A0A0G2KIJ1 View 3D Structure Click here
A0A1D6E6H8 View 3D Structure Click here
A0A1D6JZ52 View 3D Structure Click here
A0A1D6N6Q2 View 3D Structure Click here
A0A1D6QHP5 View 3D Structure Click here
A0A1D6QKY0 View 3D Structure Click here
A0A2R8PVE1 View 3D Structure Click here
A0A2R8QCT7 View 3D Structure Click here
A0A2R8QQH2 View 3D Structure Click here
A1A5W4 View 3D Structure Click here
A1KQY6 View 3D Structure Click here
A2CE97 View 3D Structure Click here
A2WX64 View 3D Structure Click here
A2XVC2 View 3D Structure Click here
A2ZI41 View 3D Structure Click here
A5D7T4 View 3D Structure Click here
B0CN48 View 3D Structure Click here
B0S5A8 View 3D Structure Click here
B8K0C9 View 3D Structure Click here
C0P8W2 View 3D Structure Click here
D2U4T9 View 3D Structure Click here
E7FBG1 View 3D Structure Click here
E9PSJ1 View 3D Structure Click here
F1Q5Y4 View 3D Structure Click here
F1QFM7 View 3D Structure Click here
F1QMH5 View 3D Structure Click here
F1QXR5 View 3D Structure Click here
F1QXW9 View 3D Structure Click here
F1QZT7 View 3D Structure Click here
F1R0F8 View 3D Structure Click here
F1R1A7 View 3D Structure Click here
F1R8G8 View 3D Structure Click here
F1RCA6 View 3D Structure Click here
G3V7T2 View 3D Structure Click here
G3V8D0 View 3D Structure Click here
G3V9C4 View 3D Structure Click here
I1K5E8 View 3D Structure Click here
I1LKS8 View 3D Structure Click here
I1LRF2 View 3D Structure Click here