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0  structures 335  species 0  interactions 2087  sequences 50  architectures

Family: Glyco_tran_10_N (PF17039)

Summary: Fucosyltransferase, N-terminal

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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

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 http://www.faqs.org/health/topics/33/Urinary-tract-infections.html".  External link in |title= (help)
  4. ^ Medscape.org. "Urinary Tract Infections What Factors Determine the Risk of UTI http://www.medscape.org/viewarticle/436592_4".  External link in |title= (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.

Fucosyltransferase, N-terminal Provide feedback

This is the N-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 N-terminal domain is the likely binding-region for the fucose-like substrate (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


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR031481

This is the N-terminal domain of a family of fucosyltransferases, known as glycosyltransferase family 10 [PUBMED:9334165, PUBMED:17251184]. This enzyme transfers fucose from GDP-Fucose to GlcNAc in an alpha1,3 linkage [PUBMED:9451017]. The N-terminal domain is the likely binding-region for the fucose-like substrate (manuscript in publication).

Domain organisation

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Alignments

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  Seed
(81)
Full
(2087)
Representative proteomes UniProt
(4162)
NCBI
(4690)
Meta
(0)
RP15
(852)
RP35
(1301)
RP55
(1723)
RP75
(1921)
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Key: ✓ available, x not generated, not available.

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  Seed
(81)
Full
(2087)
Representative proteomes UniProt
(4162)
NCBI
(4690)
Meta
(0)
RP15
(852)
RP35
(1301)
RP55
(1723)
RP75
(1921)
Alignment:
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  Seed
(81)
Full
(2087)
Representative proteomes UniProt
(4162)
NCBI
(4690)
Meta
(0)
RP15
(852)
RP35
(1301)
RP55
(1723)
RP75
(1921)
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.

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Curation and family details

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Curation View help on the curation process

Seed source: PF00852
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Coggill P
Number in seed: 81
Number in full: 2087
Average length of the domain: 106.70 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 25.84 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 28.7 28.7
Trusted cut-off 28.7 28.9
Noise cut-off 28.5 28.6
Model length: 111
Family (HMM) version: 5
Download: download the raw HMM for this family

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