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9  structures 340  species 0  interactions 1458  sequences 27  architectures

Family: Glyco_transf_10 (PF00852)

Summary: Glycosyltransferase family 10 (fucosyltransferase)

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

Fucosyltransferase Edit Wikipedia article

Glycosyltransferase family 10 (fucosyltransferase)
Identifiers
Symbol Glyco_transf_10
Pfam PF00852
InterPro IPR001503

A fucosyltransferase is an enzyme that transfers an L-fucose sugar from a GDP-fucose (guanosine diphosphate-fucose) donor substrate to an acceptor substrate. The acceptor substrate can be another sugar such as the transfer of a fucose to a core GlcNAc (N-acetylglucosamine) sugar as in the case of N-linked glycosylation, or to a protein, as in the case of O-linked glycosylation produced by O-fucosyltransferase. There are various fucosyltransferases in mammals, the vast majority of which, are located in the Golgi apparatus. The O-fucosyltransferases have recently been shown to localize to the endoplasmic reticulum (ER).

Some of the proteins in this group are responsible for the molecular basis of the blood group antigens, surface markers on the outside of the red blood cell membrane. Most of these markers are proteins, but some are carbohydrates attached to lipids or proteins [Reid M.E., Lomas-Francis C. The Blood Group Antigen FactsBook Academic Press, London / San Diego, (1997)]. Galactoside 3(4)-L-fucosyltransferase (EC 2.4.1.65) belongs to the Lewis blood group system and is associated with Le(a/b) antigen.

Classification[edit]

Glycosyltransferase family 10 CAZY GT_10 comprises enzymes with two known activities; galactoside 3(4)-L-fucosyltransferase (EC 2.4.1.65) and galactoside 3-fucosyltransferase (EC 2.4.1.152). The galactoside 3-fucosyltransferases display similarities with the alpha-2 and alpha-6-fucosyltranferases.[1] The biosynthesis of the carbohydrate antigen sialyl Lewis X (sLe(x)) is dependent on the activity of an galactoside 3-fucosyltransferase. This enzyme catalyses the transfer of fucose from GDP-beta-fucose to the 3-OH of N-acetylglucosamine present in lactosamine acceptors.[2]

Human proteins containing this domain[edit]

FUT1; FUT2; FUT3; FUT4; FUT5; FUT6; FUT7; FUT8; FUT9; FUT10; FUT11;

See also[edit]

References[edit]

  1. ^ Breton C, Oriol R, Imberty A (1998). "Conserved structural features in eukaryotic and prokaryotic fucosyltransferases". Glycobiology 8 (1): 87–94. doi:10.1093/glycob/8.1.87. PMID 9451017. 
  2. ^ Britten CJ, Bird MI (1997). "Chemical modification of an alpha 3-fucosyltransferase; definition of amino acid residues essential for enzyme activity". Biochim. Biophys. Acta 1334 (1): 57–64. PMID 9042366. 

External links[edit]

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 10 (fucosyltransferase) Provide feedback

This family of Fucosyltransferases are the enzymes transferring fucose from GDP-Fucose to GlcNAc in an alpha1,3 linkage [1]. This family is know as glycosyltransferase family 10 [2].

Literature references

  1. Breton C, Oriol R, Imberty A; , Glycobiology 1998;8:87-94.: Conserved structural features in eukaryotic and prokaryotic fucosyltransferases. PUBMED:9451017 EPMC:9451017

  2. 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 IPR001503

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 (EC) 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 10 CAZY comprises enzymes with two known activities; galactoside 3(4)-L-fucosyltransferase (EC) and galactoside 3-fucosyltransferase (EC).

The galactoside 3-fucosyltransferases display similarities with the alpha-2 and alpha-6-fucosyltranferases [PUBMED:9451017]. The biosynthesis of the carbohydrate antigen sialyl Lewis X (sLe(x)) is dependent on the activity of an galactoside 3-fucosyltransferase. This enzyme catalyses the transfer of fucose from GDP-beta-fucose to the 3-OH of N-acetylglucosamine present in lactosamine acceptors [PUBMED:9042366].

Some of the proteins in this group are responsible for the molecular basis of the blood group antigens, surface markers on the outside of the red blood cell membrane. Most of these markers are proteins, but some are carbohydrates attached to lipids or proteins [Reid M.E., Lomas-Francis C. The Blood Group Antigen FactsBook Academic Press, London / San Diego, (1997)]. Galactoside 3(4)-L-fucosyltransferase (EC) belongs to the Lewis blood group system and is associated with Le(a/b) antigen.

Gene Ontology

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Domain organisation

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Alignments

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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
(49)
Full
(1458)
Representative proteomes NCBI
(1374)
Meta
(288)
RP15
(422)
RP35
(516)
RP55
(726)
RP75
(858)
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Format an alignment

  Seed
(49)
Full
(1458)
Representative proteomes NCBI
(1374)
Meta
(288)
RP15
(422)
RP35
(516)
RP55
(726)
RP75
(858)
Alignment:
Format:
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Sequence:
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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
(49)
Full
(1458)
Representative proteomes NCBI
(1374)
Meta
(288)
RP15
(422)
RP35
(516)
RP55
(726)
RP75
(858)
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.

Pfam alignments:

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Trees

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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_1677 (release 2.1)
Previous IDs: Fucosyl_transf;
Type: Family
Author: Bateman A
Number in seed: 49
Number in full: 1458
Average length of the domain: 287.80 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 74.46 %

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 21.0 21.0
Trusted cut-off 21.1 21.6
Noise cut-off 20.8 20.8
Model length: 350
Family (HMM) version: 14
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 Glyco_transf_10 domain has been found. There are 9 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 seqence.

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