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11  structures 1037  species 0  interactions 5072  sequences 109  architectures

Family: Glyco_transf_10 (PF00852)

Summary: Glycosyltransferase family 10 (fucosyltransferase) C-term

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 "Fucosyltransferase". More...

Fucosyltransferase Edit Wikipedia article

Glycosyltransferase family 10 (fucosyltransferase)
Identifiers
SymbolGlyco_transf_10
PfamPF00852
InterProIPR001503

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

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]

Role in preventing UTIs

Robust fucosyltransferase activity discourages bacterial adherence in the urethra of women.[3] This is also mediated by the presence of few bacterial adhesion sites in the bladder and urethra. Women with these receptors who do not have mucosal secretion of the fucosyltransferase enzyme to help block bacterial adherence are more likely to have colonization of E coli and other coliforms from the rectum and less likely to have lactobacilli in the periurethral area, resulting in frequent episodes of cystitis.[4]

Human proteins containing this domain

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

See also

References

  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. doi:10.1016/s0304-4165(96)00076-1. PMID 9042366.
  3. ^ FAQs.org. "Urinary Tract Infections". Cite journal requires |journal= (help)
  4. ^ Medscape.org. "Urinary Tract Infections What Factors Determine the Risk of UTI". Cite journal requires |journal= (help)

External links

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) C-term Provide feedback

This is the C-terminal domain of a family of fucosyltransferases. This enzyme transfers fucose from GDP-Fucose to GlcNAc in an alpha1,3 linkage [1]. This family is known as glycosyltransferase family 10 [2]. The C-terminal domain is the likely binding-region for ADP (manuscript in publication).

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

  3. Sun HY, Lin SW, Ko TP, Pan JF, Liu CL, Lin CN, Wang AH, Lin CH;, J Biol Chem. 2007;282:9973-9982.: Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design. PUBMED:17251184 EPMC:17251184


Internal database links

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 ([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 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

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...

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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
(82)
Full
(5072)
Representative proteomes UniProt
(11942)
RP15
(1792)
RP35
(3109)
RP55
(4807)
RP75
(5928)
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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
(82)
Full
(5072)
Representative proteomes UniProt
(11942)
RP15
(1792)
RP35
(3109)
RP55
(4807)
RP75
(5928)
Alignment:
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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
(82)
Full
(5072)
Representative proteomes UniProt
(11942)
RP15
(1792)
RP35
(3109)
RP55
(4807)
RP75
(5928)
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_1677 (release 2.1)
Previous IDs: Fucosyl_transf;
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A
Number in seed: 82
Number in full: 5072
Average length of the domain: 165.60 aa
Average identity of full alignment: 28 %
Average coverage of the sequence by the domain: 41.62 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.9 23.9
Trusted cut-off 23.9 23.9
Noise cut-off 23.8 23.8
Model length: 180
Family (HMM) version: 21
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 11 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
A0A0G2L3V0 View 3D Structure Click here
A0A0R4IUI3 View 3D Structure Click here
A0A0R4IWR0 View 3D Structure Click here
A0A1D6KBS9 View 3D Structure Click here
A0A1D6KLA3 View 3D Structure Click here
A0A1D6PZE1 View 3D Structure Click here
A0A2R8Q5J5 View 3D Structure Click here
A4HRN0 View 3D Structure Click here
B3DGK8 View 3D Structure Click here
B3DJZ1 View 3D Structure Click here
C0HGQ1 View 3D Structure Click here
F1Q797 View 3D Structure Click here
F1QKT5 View 3D Structure Click here
F1QMG7 View 3D Structure Click here
F1R5F5 View 3D Structure Click here
F6NWZ6 View 3D Structure Click here
G5EDR5 View 3D Structure Click here
G5EE06 View 3D Structure Click here
G5EEE1 View 3D Structure Click here
G5EEL7 View 3D Structure Click here
G5EFP5 View 3D Structure Click here
I1JD68 View 3D Structure Click here
I1JET8 View 3D Structure Click here
I1KM01 View 3D Structure Click here
I1LD89 View 3D Structure Click here
I1MNV8 View 3D Structure Click here
I1NH94 View 3D Structure Click here
O88819 View 3D Structure Click here
P21217 View 3D Structure Click here
P22083 View 3D Structure Click here
P51993 View 3D Structure Click here
P83088 View 3D Structure Click here
Q08C60 View 3D Structure Click here
Q0IPS4 View 3D Structure Click here
Q11127 View 3D Structure Click here
Q11128 View 3D Structure Click here
Q11130 View 3D Structure Click here
Q11131 View 3D Structure Click here
Q2VU44 View 3D Structure Click here
Q32WF4 View 3D Structure Click here
Q495W5 View 3D Structure Click here
Q4DTY6 View 3D Structure Click here
Q4DV88 View 3D Structure Click here
Q54BB7 View 3D Structure Click here
Q54L56 View 3D Structure Click here
Q54P60 View 3D Structure Click here
Q54PH9 View 3D Structure Click here
Q54PJ9 View 3D Structure Click here
Q54PK0 View 3D Structure Click here
Q54PK3 View 3D Structure Click here
Q54RA6 View 3D Structure Click here
Q55FA8 View 3D Structure Click here
Q5F2L1 View 3D Structure Click here
Q5F2L2 View 3D Structure Click here
Q5F2N3 View 3D Structure Click here
Q62994 View 3D Structure Click here
Q68FV3 View 3D Structure Click here
Q6P4F1 View 3D Structure Click here
Q6ZDE5 View 3D Structure Click here
Q712G6 View 3D Structure Click here
Q7XQP0 View 3D Structure Click here
Q86J24 View 3D Structure Click here
Q8BHC9 View 3D Structure Click here
Q99JB3 View 3D Structure Click here
Q9C8W3 View 3D Structure Click here
Q9FX97 View 3D Structure Click here
Q9LJK1 View 3D Structure Click here
Q9VLC1 View 3D Structure Click here
Q9VUL9 View 3D Structure Click here
Q9W0F6 View 3D Structure Click here
Q9Y231 View 3D Structure Click here
X1WBS2 View 3D Structure Click here
X1WCW8 View 3D Structure Click here