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220  structures 8905  species 0  interactions 99339  sequences 1125  architectures

Family: Glycos_transf_1 (PF00534)

Summary: Glycosyl transferases group 1

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

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

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.

Glycosyl transferases group 1 Provide feedback

Mutations in this domain of P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001296

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'.

Proteins containing this domain transfer UDP, ADP, GDP or CMP linked sugars to a variety of substrates, including glycogen, fructose-6-phosphate and lipopolysaccharides. The bacterial enzymes are involved in various biosynthetic processes that include exopolysaccharide biosynthesis, lipopolysaccharide core biosynthesis and the biosynthesis of the slime polysaccaride colanic acid. Mutations in this domain of the human N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein are the cause of paroxysmal nocturnal hemoglobinuria (PNH) [ PUBMED:12037021 ], an acquired hemolytic blood disorder characterised by venous thrombosis, erythrocyte hemolysis, infections and defective hematopoiesis.

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
(44)
Full
(99339)
Representative proteomes UniProt
(466859)
RP15
(13782)
RP35
(48730)
RP55
(100620)
RP75
(169792)
Jalview View  View  View  View  View  View  View 
HTML View             
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
(44)
Full
(99339)
Representative proteomes UniProt
(466859)
RP15
(13782)
RP35
(48730)
RP55
(100620)
RP75
(169792)
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
(44)
Full
(99339)
Representative proteomes UniProt
(466859)
RP15
(13782)
RP35
(48730)
RP55
(100620)
RP75
(169792)
Raw Stockholm Download   Download   Download   Download   Download      
Gzipped 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: MRC-LMB Genome group
Previous IDs: glycosyl_transf_1;
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 44
Number in full: 99339
Average length of the domain: 165.00 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 36.36 %

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 26.4 26.4
Trusted cut-off 26.4 26.4
Noise cut-off 26.3 26.3
Model length: 172
Family (HMM) version: 23
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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 Glycos_transf_1 domain has been found. There are 220 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
A0A0N7KUA0 View 3D Structure Click here
A0A0P0XCU3 View 3D Structure Click here
A0A0R0E7P7 View 3D Structure Click here
A0A0R0EIF9 View 3D Structure Click here
A0A0R0F4I7 View 3D Structure Click here
A0A0R0GH70 View 3D Structure Click here
A0A0R0GUJ0 View 3D Structure Click here
A0A0R0HW79 View 3D Structure Click here
A0A0R0J9M2 View 3D Structure Click here
A0A0R0K711 View 3D Structure Click here
A0A1D6DYQ3 View 3D Structure Click here
A0A1D6E1K2 View 3D Structure Click here
A0A1D6E268 View 3D Structure Click here
A0A1D6E340 View 3D Structure Click here
A0A1D6EBE4 View 3D Structure Click here
A0A1D6ENE0 View 3D Structure Click here
A0A1D6FE39 View 3D Structure Click here
A0A1D6FIB1 View 3D Structure Click here
A0A1D6FZL4 View 3D Structure Click here
A0A1D6FZN3 View 3D Structure Click here
A0A1D6GQA5 View 3D Structure Click here
A0A1D6H2R7 View 3D Structure Click here
A0A1D6HA27 View 3D Structure Click here
A0A1D6HKA3 View 3D Structure Click here
A0A1D6HXP2 View 3D Structure Click here
A0A1D6I4J1 View 3D Structure Click here
A0A1D6ICE7 View 3D Structure Click here
A0A1D6IX24 View 3D Structure Click here
A0A1D6JWU6 View 3D Structure Click here
A0A1D6JX85 View 3D Structure Click here
A0A1D6JXP7 View 3D Structure Click here
A0A1D6K2D7 View 3D Structure Click here
A0A1D6K2G3 View 3D Structure Click here
A0A1D6K4M5 View 3D Structure Click here
A0A1D6KEQ3 View 3D Structure Click here
A0A1D6L1M5 View 3D Structure Click here
A0A1D6LG94 View 3D Structure Click here
A0A1D6LQW1 View 3D Structure Click here
A0A1D6LVT8 View 3D Structure Click here
A0A1D6MQF7 View 3D Structure Click here