Summary: Beta-galactosidase trimerisation domain
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This is the Wikipedia entry entitled "Glycoside hydrolase family 42". More...
Glycoside hydrolase family 42
| crystal structure of thermus thermophilus a4 beta-galactosidase | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Glyco_hydro_42 | ||||||||
| Pfam | PF02449 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR013529 | ||||||||
| SCOP | 1kwg | ||||||||
| SUPERFAMILY | 1kwg | ||||||||
| CAZy | GH42 | ||||||||
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| crystal structure of thermus thermophilus a4 beta-galactosidase | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Glyco_hydro_42M | ||||||||
| Pfam | PF08532 | ||||||||
| Pfam clan | CL0014 | ||||||||
| InterPro | IPR013738 | ||||||||
| SCOP | 1kwg | ||||||||
| SUPERFAMILY | 1kwg | ||||||||
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| crystal structure of thermus thermophilus a4 beta-galactosidase | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Glyco_hydro_42C | ||||||||
| Pfam | PF08533 | ||||||||
| Pfam clan | CL0369 | ||||||||
| InterPro | IPR013739 | ||||||||
| SCOP | 1kwg | ||||||||
| SUPERFAMILY | 1kwg | ||||||||
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In molecular biology, glycoside hydrolase family 42 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.[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]
The glycosyl hydrolase 42 family CAZY GH_42 comprises beta-galactosidase enzymes (EC 3.2.1.23). These enzyme catalyse the hydrolysis of terminal, non-reducing terminal beta-D-galactoside residues. The middle domain of these three-domain enzymes is involved in trimerisation.[6]
[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): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41477.
- ^ 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.
- ^ 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.
- ^ Shimizu T, Kobayashi T, Ba-Thein W, Ohtani K, Hayashi H (1995). "Sequence analysis of flanking regions of the pfoA gene of Clostridium perfringens: beta-galactosidase gene (pbg) is located in the 3'-flanking region.". Microbiol Immunol 39 (9): 677–86. PMID 8577281.
This article incorporates text from the public domain Pfam and InterPro IPR013529
This article incorporates text from the public domain Pfam and InterPro IPR013739
This article incorporates text from the public domain Pfam and InterPro IPR013738
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.
Beta-galactosidase trimerisation domain
This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerisation [1].
Literature references
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Shimizu T, Kobayashi T, Ba-Thein W, Ohtani K, Hayashi H; , Microbiol Immunol 1995;39:677-686.: Sequence analysis of flanking regions of the pfoA gene of Clostridium perfringens: beta-galactosidase gene (pbg) is located in the 3'-flanking region. PUBMED:8577281
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Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, Wakagi T; , J Mol Biol 2002;322:79-91.: Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose. PUBMED:12215416
Clan
This family is a member of clan Glutaminase_I (CL0014), which has a total of 13 members.
External database links
| PANDIT: | PF08532 |
| Pseudofam: | PF08532 |
| SCOP: | 1kwg |
| SYSTERS: | Glyco_hydro_42M |
This tab holds annotation information from the InterPro database.
InterPro entry IPR013738
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.
This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerisation.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | beta-galactosidase activity (GO:0004565) |
| 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...
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Pfam Clan
This family is a member of clan Glutaminase_I (CL0014), which contains the following 13 members:
BPL_N DJ-1_PfpI DUF1355 DUF4066 GATase GATase_3 GATase_5 Glyco_hydro_42M HTS Peptidase_C26 Peptidase_S51 SNO ThuAAlignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
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Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
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. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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: | Pfam-B_2131 (release 5.4) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 28 |
| Number in full: | 787 |
| Average length of the domain: | 198.00 aa |
| Average identity of full alignment: | 25 % |
| Average coverage of the sequence by the domain: | 29.41 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 207 | ||||||||||||
| Family (HMM) version: | 5 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Colour assignments
Archea
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Eukaryota
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Bacteria
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Other sequences
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Viruses
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Unclassified
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Viroids
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Unclassified sequence
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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 if you need to select sub-trees and view sequence alignments. More...
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Interactions
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_42M domain has been found. There are 2 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.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence