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.
83  structures 2323  species 0  interactions 8726  sequences 261  architectures

Family: Melibiase_2 (PF16499)

Summary: Alpha galactosidase A

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 27". More...

Glycoside hydrolase family 27 Edit Wikipedia article

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 galactosidase A Provide feedback

No Pfam abstract.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002241

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) website.

Glycoside hydrolase family 27 CAZY comprises enzymes with several known activities; alpha-galactosidase ( EC ); alpha-N-acetylgalactosaminidase ( EC ); isomalto-dextranase ( EC ).

Alpha-galactosidase (melibiase) catalyses the hydrolysis of melibiose into galactose and glucose [ PUBMED:7725791 ]. In man, deficiency in the enzyme results in Fabry's disease (X-linked sphingolipidosis). Alpha-N-acetylgalactosaminidase catalyses the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides [ PUBMED:2174888 ]. Two conserved Asp residues may be involved in the catalytic mechanism in these enzymes. Deficiency in this enzyme results in Schindler and Kanzaki diseases.

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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB 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
(10)
Full
(8726)
Representative proteomes UniProt
(19848)
RP15
(1382)
RP35
(4120)
RP55
(7793)
RP75
(11694)
Jalview View  View  View  View  View  View  View 
HTML View             
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
(10)
Full
(8726)
Representative proteomes UniProt
(19848)
RP15
(1382)
RP35
(4120)
RP55
(7793)
RP75
(11694)
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
(10)
Full
(8726)
Representative proteomes UniProt
(19848)
RP15
(1382)
RP35
(4120)
RP55
(7793)
RP75
(11694)
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: manual
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Coggill P
Number in seed: 10
Number in full: 8726
Average length of the domain: 216.60 aa
Average identity of full alignment: 30 %
Average coverage of the sequence by the domain: 52.66 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.0 23.0
Trusted cut-off 23.0 23.0
Noise cut-off 22.9 22.9
Model length: 284
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Hide

Weight segments by...


Change the size of the sunburst

Small
Large

Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

Align selected sequences to HMM

Generate a FASTA-format file

Clear selection

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.

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 Melibiase_2 domain has been found. There are 83 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.

Loading structure mapping...

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
A0A0P0X580 View 3D Structure Click here
A0A0P0XVP1 View 3D Structure Click here
A0A0R0FT50 View 3D Structure Click here
A0A0R0GL97 View 3D Structure Click here
A0A0R0HUR0 View 3D Structure Click here
A0A0R0KI41 View 3D Structure Click here
A0A0R0L8J4 View 3D Structure Click here
A0A0R4IJL2 View 3D Structure Click here
A0A1D6EFC8 View 3D Structure Click here
A0A1D6HYF2 View 3D Structure Click here
A0A1D6JPI1 View 3D Structure Click here
A0A1D6JWU1 View 3D Structure Click here
A0A1D6KS86 View 3D Structure Click here
A0A1D6KS92 View 3D Structure Click here
A0A1D6MYU4 View 3D Structure Click here
A0A1D6QBS8 View 3D Structure Click here
B4FA27 View 3D Structure Click here
C0PAL4 View 3D Structure Click here
D3ZJF9 View 3D Structure Click here
F1Q5G5 View 3D Structure Click here
F4JCI4 View 3D Structure Click here
I1K4F3 View 3D Structure Click here
I1KB92 View 3D Structure Click here
I1KSW9 View 3D Structure Click here
I1L3R4 View 3D Structure Click here
I1L6Y9 View 3D Structure Click here
I1LBZ8 View 3D Structure Click here
I1LNG1 View 3D Structure Click here
I1N3A6 View 3D Structure Click here
K7M508 View 3D Structure Click here
K7MJ32 View 3D Structure Click here
K7N4X3 View 3D Structure Click here
P06280 View 3D Structure Click here
P17050 View 3D Structure Click here
P51569 View 3D Structure Click here
Q21801 View 3D Structure Click here
Q54EG4 View 3D Structure Click here
Q55B10 View 3D Structure Click here
Q5QLK3 View 3D Structure Click here
Q66H12 View 3D Structure Click here