Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
84  structures 589  species 1  interaction 1151  sequences 52  architectures

Family: Glyco_hydro_30 (PF02055)

Summary: O-Glycosyl hydrolase family 30

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 "Glycoside hydrolase family 30". More...

Glycoside hydrolase family 30 Edit Wikipedia article

O-Glycosyl hydrolase family 30
PDB 1nof EBI.jpg
Structure of a xylanase from glycoside hydrolase family 5.[1]
Identifiers
Symbol Glyco_hydro_30
Pfam PF02055
Pfam clan CL0058
InterPro IPR001139
SCOP 1nof
SUPERFAMILY 1nof
OPM superfamily 125
OPM protein 1ogs

In molecular biology, glycoside hydrolase family 30 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 >100 different families.[2][3][4] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6]

Glycoside hydrolase family 30 CAZY GH_30 includes the mammalian glucosylceramidases. Human acid beta-glucosidase (D-glucosyl-N-acylsphingosine glucohydrolase), cleaves the glucosidic bonds of glucosylceramide and synthetic beta-glucosides.[7] Any one of over 50 different mutations in the gene of glucocerebrosidase have been found to affect activity of this hydrolase, producing variants of Gaucher disease, the most prevalent lysosomal storage disease.[7][8]

References[edit]

  1. ^ Larson SB, Day J, Barba de la Rosa AP, Keen NT, McPherson A (July 2003). "First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis". Biochemistry 42 (28): 8411–22. doi:10.1021/bi034144c. PMID 12859186. 
  2. ^ 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): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375. 
  3. ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779. 
  4. ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
  5. ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
  6. ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
  7. ^ a b Legler G, Desnick RJ, Dinur T, Osiecki KM, Gatt S, Grabowski GA (1986). "Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site". Proc. Natl. Acad. Sci. U.S.A. 83 (6): 1660–1664. doi:10.1073/pnas.83.6.1660. PMC 323143. PMID 3456607. 
  8. ^ Iwasawa K, Ida H, Eto Y (1997). "Differences in origin of the 1448C mutation in patients with Gaucher disease". Acta Paediatr. Jpn. Overseas Ed. 39 (4): 451–453. PMID 9316290. 

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.

O-Glycosyl hydrolase family 30 Provide feedback

No Pfam abstract.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001139

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.

Glycoside hydrolase family 30 CAZY comprises enzymes with only one known activity; glucosylceramidase (EC).

Family 30 encompasses the mammalian glucosylceramidases. Human acid beta-glucosidase (D-glucosyl-N-acylsphingosine glucohydrolase), cleaves the glucosidic bonds of glucosylceramide and synthetic beta-glucosides [PUBMED:3456607]. Any one of over 50 different mutations in the gene of glucocerebrosidase have been found to affect activity of this hydrolase, producing variants of Gaucher disease, the most prevalent lysosomal storage disease [PUBMED:3456607, PUBMED:9316290].

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...

Loading domain graphics...

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 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
(3)
Full
(1151)
Representative proteomes NCBI
(1057)
Meta
(187)
RP15
(224)
RP35
(348)
RP55
(456)
RP75
(517)
Jalview View  View  View  View  View  View  View  View 
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(3)
Full
(1151)
Representative proteomes NCBI
(1057)
Meta
(187)
RP15
(224)
RP35
(348)
RP55
(456)
RP75
(517)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

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
(3)
Full
(1151)
Representative proteomes NCBI
(1057)
Meta
(187)
RP15
(224)
RP35
(348)
RP55
(456)
RP75
(517)
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:

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: IPR001139
Previous IDs: none
Type: Family
Author: Mian N, Bateman A
Number in seed: 3
Number in full: 1151
Average length of the domain: 328.70 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 77.79 %

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 20.2 20.2
Trusted cut-off 20.5 20.2
Noise cut-off 20.1 20.1
Model length: 496
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

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...

Loading sunburst data...

Tree controls

Hide

The 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.

Interactions

There is 1 interaction for this family. More...

Glyco_hydro_30

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_hydro_30 domain has been found. There are 84 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...