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227  structures 4349  species 0  interactions 19731  sequences 545  architectures

Family: Glyco_hydro_31 (PF01055)

Summary: Glycosyl hydrolases family 31

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This is the Wikipedia entry entitled "Glycoside hydrolase family 31". More...

Glycoside hydrolase family 31 Edit Wikipedia article

Glycosyl hydrolases family 31
PDB 2f2h EBI.jpg
structure of the yici thiosugar michaelis complex
Identifiers
SymbolGlyco_hydro_31
PfamPF01055
Pfam clanCL0058
InterProIPR000322
PROSITEPDOC00120
CAZyGH31

In molecular biology, glycoside hydrolase family 31 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]

Glycoside hydrolase family 31 CAZY GH_31 comprises enzymes with several known activities; alpha-glucosidase (EC 3.2.1.20), alpha-galactosidase (EC 3.2.1.22); glucoamylase (EC 3.2.1.3), sucrase-isomaltase (EC 3.2.1.48) (EC 3.2.1.10); alpha-xylosidase (EC 3.2.1); alpha-glucan lyase (EC 4.2.2.13).

Glycoside hydrolase family 31 groups a number of glycosyl hydrolases on the basis of sequence similarities[6][7][8] An aspartic acid has been implicated[9] in the catalytic activity of sucrase, isomaltase, and lysosomal alpha-glucosidase.

References

  1. ^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ 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.
  3. ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
  4. ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
  5. ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
  6. ^ Cite error: The named reference PUB00000503 was invoked but never defined (see the help page).
  7. ^ Kinsella BT, Hogan S, Larkin A, Cantwell BA (1991). "Primary structure and processing of the Candida tsukubaensis alpha-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase". Eur. J. Biochem. 202 (2): 657–664. doi:10.1111/j.1432-1033.1991.tb16420.x. PMID 1761061.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ Niermann T, Naim HY, Kleinhans U, Hollenberg CP, Strasser AW (1991). "Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene". FEBS Lett. 294 (1): 109–112. doi:10.1016/0014-5793(91)81353-A. PMID 1743281.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  9. ^ van Beeumen J, Kroos MA, Oostra BA, Hermans MM, Reuser AJ (1991). "Human lysosomal alpha-glucosidase. Characterization of the catalytic site". J. Biol. Chem. 266 (21): 13507–13512. PMID 1856189.{{cite journal}}: CS1 maint: multiple names: authors list (link)
This article incorporates text from the public domain Pfam and InterPro: IPR000322

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.

Glycosyl hydrolases family 31 Provide feedback

Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.

Literature references

  1. Henrissat B; , Biochem J 1991;280:309-316.: A classification of glycosyl hydrolases based on amino acid sequence similarities. PUBMED:1747104 EPMC:1747104

  2. Henrissat B , Biochem Soc Trans 1998;26:153-156.: Glycosidase families PUBMED:9649738 EPMC:9649738


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000322

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 31 CAZY comprises enzymes with several known activities; alpha-glucosidase ( EC ), alpha-galactosidase ( EC ); glucoamylase ( EC ), sucrase-isomaltase ( EC ); isomaltase ( EC ); alpha-xylosidase ( EC ); alpha-glucan lyase ( EC ).

Glycoside hydrolase family 31 groups a number of glycosyl hydrolases on the basis of sequence similarities [ PUBMED:1747104 , PUBMED:1761061 , PUBMED:1743281 ]. An aspartic acid has been implicated [ PUBMED:1856189 ] in the catalytic activity of sucrase, isomaltase, and lysosomal alpha-glucosidase.

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...

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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...

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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
(659)
Full
(19731)
Representative proteomes UniProt
(53439)
RP15
(3206)
RP35
(8798)
RP55
(17112)
RP75
(25865)
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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
(659)
Full
(19731)
Representative proteomes UniProt
(53439)
RP15
(3206)
RP35
(8798)
RP55
(17112)
RP75
(25865)
Alignment:
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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
(659)
Full
(19731)
Representative proteomes UniProt
(53439)
RP15
(3206)
RP35
(8798)
RP55
(17112)
RP75
(25865)
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: Pfam-B_369 (release 3.0)
Previous IDs: Glycosyl_hydr15;
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD , Bateman A
Number in seed: 659
Number in full: 19731
Average length of the domain: 405.4 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 52.57 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null --hand HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 32.0 32.0
Trusted cut-off 32.0 32.0
Noise cut-off 31.9 31.9
Model length: 444
Family (HMM) version: 29
Download: download the raw HMM for this family

Species distribution

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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_31 domain has been found. There are 227 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.

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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
A0A044TPS6 View 3D Structure Click here
A0A044UFQ5 View 3D Structure Click here
A0A077YZY3 View 3D Structure Click here
A0A077Z0Q6 View 3D Structure Click here
A0A077Z0V5 View 3D Structure Click here
A0A077Z243 View 3D Structure Click here
A0A077Z405 View 3D Structure Click here
A0A077ZGG9 View 3D Structure Click here
A0A0D2DLF9 View 3D Structure Click here
A0A0D2DNT6 View 3D Structure Click here
A0A0D2E3W7 View 3D Structure Click here
A0A0D2F4P8 View 3D Structure Click here
A0A0D2G041 View 3D Structure Click here
A0A0D2H258 View 3D Structure Click here
A0A0D2HA85 View 3D Structure Click here
A0A0D2HLQ4 View 3D Structure Click here
A0A0G2KY72 View 3D Structure Click here
A0A0G2L1N0 View 3D Structure Click here
A0A0H3GUJ8 View 3D Structure Click here
A0A0H3GXH3 View 3D Structure Click here
A0A0K0DZI5 View 3D Structure Click here
A0A0K0DZJ0 View 3D Structure Click here
A0A0K0ECR7 View 3D Structure Click here
A0A0N4U8A0 View 3D Structure Click here
A0A0N4UK71 View 3D Structure Click here
A0A0N4UQN2 View 3D Structure Click here
A0A0P0X5N3 View 3D Structure Click here
A0A0R0G0B7 View 3D Structure Click here
A0A0R0I6Y6 View 3D Structure Click here
A0A0R0JT00 View 3D Structure Click here
A0A175VQS7 View 3D Structure Click here
A0A175VX48 View 3D Structure Click here
A0A175VZG2 View 3D Structure Click here
A0A175W239 View 3D Structure Click here
A0A175W4L4 View 3D Structure Click here
A0A175W942 View 3D Structure Click here
A0A175W9F4 View 3D Structure Click here
A0A1C1CAY5 View 3D Structure Click here
A0A1C1CDY8 View 3D Structure Click here
A0A1C1CME5 View 3D Structure Click here