Summary: Alpha-L-fucosidase
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 "Alpha-L-fucosidase". More...
Alpha-L-fucosidase Edit Wikipedia article
| crystal structure of thermotoga maritima alpha-fucosidase | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Alpha_L_fucos | ||||||||
| Pfam | PF01120 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR000933 | ||||||||
| PROSITE | PDOC00324 | ||||||||
| SCOP | 1hl9 | ||||||||
| SUPERFAMILY | 1hl9 | ||||||||
| CAZy | GH29 | ||||||||
|
|||||||||
| alpha-L-fucosidase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 3.2.1.51 | ||||||
| CAS number | 9037-65-4 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
|
|||||||
In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction
- an alpha-L-fucoside + H2O
L-fucose + an alcohol
Thus, the two substrates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is alpha-L-fucoside fucohydrolase. This enzyme is also called alpha-fucosidase. This enzyme participates in n-glycan degradation and glycan structures - degradation.
Defiiciency of this enzyme is called Fucosidosis.
In CAZy, alpha-L-fucosidases are found in glycoside hydrolase family 29 and glycoside hydrolase family 95.
Contents |
[edit] Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1HL8, 1HL9, and 1ODU.
[edit] See also
[edit] References
[edit] Further reading
- Levvy GA and McAllan A (1961). "Mammalian fucosidases. 2. ?-l-Fucosidase". Biochem. J. 80 (2): 435439. PMC 1244021. PMID 13761578. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1244021.
- Reglero A, Cabezas JA (1976). "Glycosidases of molluscs. Purification and properties of alpha-L-fucosidase from Chamelea gallina L". Eur. J. Biochem. 66 (2): 37987. doi:10.1111/j.1432-1033.1976.tb10527.x. PMID 7458.
- Tanaka K, Nakano T, Noguchi S, Pigman W (1968). "Purification of alpha-L-fucosidase of abalone livers". Arch. Biochem. Biophys. 126 (2): 62433. doi:10.1016/0003-9861(68)90449-9. PMID 5672520.
[edit] External links
| This hydrolase article is a stub. You can help Wikipedia by expanding it. |
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This is the Wikipedia entry entitled "Glycoside hydrolase family 29". More...
Glycoside hydrolase family 29 Edit Wikipedia article
| crystal structure of thermotoga maritima alpha-fucosidase | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Alpha_L_fucos | ||||||||
| Pfam | PF01120 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR000933 | ||||||||
| PROSITE | PDOC00324 | ||||||||
| SCOP | 1hl9 | ||||||||
| SUPERFAMILY | 1hl9 | ||||||||
| CAZy | GH29 | ||||||||
|
|||||||||
In molecular biology, glycoside hydrolase family 29 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of over 100 different families.[1][2][3] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes. [5]
Glycoside hydrolase family 29 includes alpha-L-fucosidases,[6] They are lysosomal enzymes responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Fucosylated glycoconjugates are involved in numerous biological events, making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. Deficiency in alpha-l-fucosidase activity is associated with fucosidosis, a lysosomal storage disorder characterised by rapid neurodegeneration, resulting in severe mental and motor deterioration.[7] The enzyme is a hexamer and displays a two-domain fold, composed of a catalytic (beta/alpha)(8)-like domain and a C-terminal beta-sandwich domain.[7]
Drosophila melanogaster spermatozoa contains an alpha-l-fucosidase that might be involved in fertilisation by interacting with alpha-l-fucose residues on the micropyle of the eggshell.[8] In human sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by membrane domains and compartmentalisation. These help preserve protein integrity.[9]
[edit] References
- ^ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 70907094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41477.
- ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- ^ Fisher KJ, Aronson NN (December 1989). "Isolation and sequence analysis of a cDNA encoding rat liver alpha-L-fucosidase". Biochem. J. 264 (3): 695701. PMC 1133642. PMID 2482732. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1133642.
- ^ a b Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y (March 2004). "Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis". J. Biol. Chem. 279 (13): 1311928. doi:10.1074/jbc.M313783200. PMID 14715651.
- ^ Pasini ME, Intra J, Pavesi G (August 2008). "Expression study of an alpha-l-fucosidase gene in the Drosophilidae family". Gene 420 (1): 2333. doi:10.1016/j.gene.2008.04.021. PMID 18556148.
- ^ Venditti JJ, Bean BS (October 2009). "Stabilization of membrane-associated alpha-L-fucosidase by the human sperm equatorial segment". Int. J. Androl. 32 (5): 55662. doi:10.1111/j.1365-2605.2008.00897.x. PMID 18522672.
This article incorporates text from the public domain Pfam and InterPro IPR000933
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.
Alpha-L-fucosidase Provide feedback
No Pfam abstract.
Internal database links
| Similarity to PfamA using HHSearch: | DUF4434 GHL6 |
External database links
| CAZY: | GH29 |
| PANDIT: | PF01120 |
| PROSITE: | PDOC00324 |
| Pseudofam: | PF01120 |
| SCOP: | 1hl9 |
| SYSTERS: | Alpha_L_fucos |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000933
O-Glycosyl hydrolases (EC) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [PUBMED:7624375, PUBMED:8535779]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.
Family 29 (CAZY) encompasses alpha-L-fucosidases (EC) [PUBMED:2482732], which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Fucosylated glycoconjugates are involved in numerous biological events, making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. Deficiency in alpha-l-fucosidase activity is associated with fucosidosis, a lysosomal storage disorder characterised by rapid neurodegeneration, resulting in severe mental and motor deterioration [PUBMED:14715651]. The enzyme is a hexamer and displays a two-domain fold, composed of a catalytic (beta/alpha)(8)-like domain and a C-terminal beta-sandwich domain [PUBMED:14715651].
Drosophila melanogaster spermatozoa contains an alpha-l-fucosidase that might be involved in fertilisation by interacting with alpha-l-fucose residues on the micropyle of the eggshell [PUBMED:18556148]. In human sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by membrane domains and compartmentalisation. These help preserve protein integrity [PUBMED:18522672].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | alpha-L-fucosidase activity (GO:0004560) |
| Biological process | carbohydrate metabolic process (GO:0005975) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Pfam Clan
This family is a member of clan Glyco_hydro_tim (CL0058), which contains the following 50 members:
Alpha-amylase Alpha_L_fucos Cellulase Cellulase-like DUF187 DUF4015 DUF4038 DUF4434 GHL1-3 GHL12 GHL13 GHL15 GHL5 GHL6 Glyco_hydr_30_2 Glyco_hydro_1 Glyco_hydro_10 Glyco_hydro_101 Glyco_hydro_114 Glyco_hydro_14 Glyco_hydro_17 Glyco_hydro_18 Glyco_hydro_20 Glyco_hydro_25 Glyco_hydro_26 Glyco_hydro_2_C Glyco_hydro_3 Glyco_hydro_30 Glyco_hydro_31 Glyco_hydro_35 Glyco_hydro_39 Glyco_hydro_42 Glyco_hydro_44 Glyco_hydro_53 Glyco_hydro_56 Glyco_hydro_59 Glyco_hydro_66 Glyco_hydro_70 Glyco_hydro_72 Glyco_hydro_77 Glyco_hydro_79n Glyco_hydro_97 Glyco_hydro_cc hDGE_amylase Lipid_bd Melibiase NAGidase NAGLU Raffinose_syn XylanaseAlignments
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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 (48) |
Full (2021) |
Representative proteomes | NCBI (1863) |
Meta (422) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (276) |
RP35 (488) |
RP55 (583) |
RP75 (664) |
|||||
| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
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 (48) |
Full (2021) |
Representative proteomes | NCBI (1863) |
Meta (422) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (276) |
RP35 (488) |
RP55 (583) |
RP75 (664) |
|||||
| Raw Stockholm | ||||||||
| Gzipped | ||||||||
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.
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
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Family |
| Author: | Finn RD, Bateman A |
| Number in seed: | 48 |
| Number in full: | 2021 |
| Average length of the domain: | 324.50 aa |
| Average identity of full alignment: | 24 % |
| Average coverage of the sequence by the domain: | 62.37 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
| Model details: |
|
||||||||||||
| Model length: | 347 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis 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...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
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 Alpha_L_fucos domain has been found. There are 58 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.
Loading structure mapping...

L-fucose + an alcohol
Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence