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.
0  structures 910  species 0  interactions 6528  sequences 91  architectures

Family: Glucan_synthase (PF02364)

Summary: 1,3-beta-glucan synthase component

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 "1,3-beta-glucan synthase". More...

1,3-beta-glucan synthase Edit Wikipedia article

  • From other capitalisation: This is a redirect from a title with another method of capitalisation. It leads to the title in accordance with the Wikipedia naming conventions for capitalisation, or it leads to a title that is associated in some way with the conventional capitalisation of this redirect title. This may help writing, searching and international language issues.
    • If this redirect is an incorrect capitalisation, then {{R from miscapitalisation}} should be used instead, and pages that use this link should be updated to link directly to the target. Miscapitalisations can be tagged in any namespace.
    • Use this rcat to tag only mainspace redirects; when other capitalisations are in other namespaces, use {{R from modification}} instead.

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.

1,3-beta-glucan synthase component Provide feedback

This family consists of various 1,3-beta-glucan synthase components including Gls1, Gls2 and Gls3 from yeast. 1,3-beta-glucan synthase EC:2.4.1.34 also known as callose synthase catalyses the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall [1]. The reaction catalysed is:- UDP-glucose + {(1,3)-beta-D-glucosyl}(N) <=> UDP + {(1,3)-beta-D-glucosyl}(N+1).

Literature references

  1. Mio T, Adachi-Shimizu M, Tachibana Y, Tabuchi H, Inoue SB, Yabe T, Yamada-Okabe T, Arisawa M, Watanabe T, Yamada-Okabe H; , J Bacteriol 1997;179:4096-4105.: Cloning of the Candida albicans homolog of Saccharomyces cerevisiae GSC1/FKS1 and its involvement in beta-1,3-glucan synthesis. PUBMED:9209021 EPMC:9209021

  2. Inoue SB, Takewaki N, Takasuka T, Mio T, Adachi M, Fujii Y, Miyamoto C, Arisawa M, Furuichi Y, Watanabe T; , Eur. J. Biochem 1995;231:845-854.: Characterization and gene cloning of 1,3-beta-D-glucan synthase from Saccharomyces cerevisiae. PUBMED:7649185 EPMC:7649185


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003440

The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates ([intenz:2.4.1.-]) and related proteins into distinct sequence based families has been described [ PUBMED:9334165 ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. The same three-dimensional fold is expected to occur within each of the families. Because 3-D structures are better conserved than sequences, several of the families defined on the basis of sequence similarities may have similar 3-D structures and therefore form 'clans'.

This is the glycosyltransferase 48 family CAZY , which consists of various 1,3-beta-glucan synthase components including Gls1, Gls2 and Gls3 from yeast. 1,3-beta-glucan synthase ( EC ) also known as callose synthase catalyses the formation of a beta-1,3-glucan polymer that is a major component of the fungal cell wall [ PUBMED:9209021 ]. The reaction catalysed is:-

UDP-glucose + {1,3-beta-D-glucosyl}(N) = UDP + {1,3-beta-D-glucosyl}(N+1).

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...

Pfam Clan

This family is a member of clan GT-C (CL0111), which has the following description:

This is the GT-C clan that contains diverse glycosyltransferases that possess 8-13 predicted transmembrane segments [1].

The clan contains the following 19 members:

ALG3 Alg6_Alg8 Arabinose_trans DIE2_ALG10 DUF2079 DUF2142 DUF2723 EpsG Glucan_synthase Glyco_transf_22 GT87 Mannosyl_trans Mannosyl_trans2 PIG-U PMT PMT_2 PTPS_related STT3 YfhO

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
(63)
Full
(6528)
Representative proteomes UniProt
(10890)
RP15
(675)
RP35
(2941)
RP55
(5301)
RP75
(6908)
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
(63)
Full
(6528)
Representative proteomes UniProt
(10890)
RP15
(675)
RP35
(2941)
RP55
(5301)
RP75
(6908)
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
(63)
Full
(6528)
Representative proteomes UniProt
(10890)
RP15
(675)
RP35
(2941)
RP55
(5301)
RP75
(6908)
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_686 (release 5.2)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bashton M , Bateman A
Number in seed: 63
Number in full: 6528
Average length of the domain: 484.90 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 44.39 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 37.2 37.2
Trusted cut-off 37.3 37.2
Noise cut-off 37.0 37.0
Model length: 819
Family (HMM) version: 17
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.

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
A0A0P0V3J9 View 3D Structure Click here
A0A0P0VRP0 View 3D Structure Click here
A0A0P0X182 View 3D Structure Click here
A0A0R0F7F5 View 3D Structure Click here
A0A0R0F7F5 View 3D Structure Click here
A0A0R0H5N5 View 3D Structure Click here
A0A0R0IMN2 View 3D Structure Click here
A0A0R0IMN2 View 3D Structure Click here
A0A0R0ISM0 View 3D Structure Click here
A0A0R0IV27 View 3D Structure Click here
A0A0R0IV27 View 3D Structure Click here
A0A0R0JH80 View 3D Structure Click here
A0A0R0JH80 View 3D Structure Click here
A0A0R0JH80 View 3D Structure Click here
A0A0R0JPR5 View 3D Structure Click here
A0A0R0K4H8 View 3D Structure Click here
A0A0R0K4H8 View 3D Structure Click here
A0A0R0KAY0 View 3D Structure Click here
A0A1D6GWW5 View 3D Structure Click here
A0A1D6GWW7 View 3D Structure Click here
A0A1D6GWW7 View 3D Structure Click here
A0A1D6H5N6 View 3D Structure Click here
A0A1D6H5N6 View 3D Structure Click here
A0A1D6HQB8 View 3D Structure Click here
A0A1D6HQB8 View 3D Structure Click here
A0A1D6HQC5 View 3D Structure Click here
A0A1D6IXP2 View 3D Structure Click here
A0A1D6JLH1 View 3D Structure Click here
A0A1D6JST4 View 3D Structure Click here
A0A1D6KBF1 View 3D Structure Click here
A0A1D6LIZ1 View 3D Structure Click here
A0A1D6LIZ1 View 3D Structure Click here
A0A1D6LMB0 View 3D Structure Click here
A0A1D6LMB0 View 3D Structure Click here
A0A1D6NBN0 View 3D Structure Click here
A0A1D6NBN0 View 3D Structure Click here
A0A1D6NG47 View 3D Structure Click here
A0A1D6NNC6 View 3D Structure Click here
A0A1D6NNC6 View 3D Structure Click here
A0A1D6NNZ3 View 3D Structure Click here
A0A1D6NNZ3 View 3D Structure Click here
A0A1D6P7A8 View 3D Structure Click here
A0A1D6Q188 View 3D Structure Click here
A0A1D8PCT0 View 3D Structure Click here
A0A1D8PDL5 View 3D Structure Click here
A0A1D8PRT5 View 3D Structure Click here
A0A1R3LAC8 View 3D Structure Click here
A0A1R3LAC8 View 3D Structure Click here
A0A368UHD0 View 3D Structure Click here
A0A368UHV8 View 3D Structure Click here
A0A368UHV8 View 3D Structure Click here
A0A368UI93 View 3D Structure Click here
I1KZH4 View 3D Structure Click here
I1LFH9 View 3D Structure Click here
I1M2S4 View 3D Structure Click here
I1M2S4 View 3D Structure Click here
I1MEJ0 View 3D Structure Click here
I1N0X8 View 3D Structure Click here
I1N0X8 View 3D Structure Click here
I1NJA0 View 3D Structure Click here
K7KY34 View 3D Structure Click here
K7M2P2 View 3D Structure Click here
K7MDN8 View 3D Structure Click here
K7ME49 View 3D Structure Click here
K7ME49 View 3D Structure Click here
K7MVL3 View 3D Structure Click here
O13967 View 3D Structure Click here
O74475 View 3D Structure Click here
P38631 View 3D Structure Click here
P40989 View 3D Structure Click here
Q04952 View 3D Structure Click here
Q0DE26 View 3D Structure Click here
Q0DF63 View 3D Structure Click here
Q0DVI7 View 3D Structure Click here
Q0DVP5 View 3D Structure Click here
Q0JKI5 View 3D Structure Click here
Q10287 View 3D Structure Click here
Q3B724 View 3D Structure Click here
Q5JLH4 View 3D Structure Click here
Q8HCN4 View 3D Structure Click here
Q8S1X0 View 3D Structure Click here
Q9AUE0 View 3D Structure Click here
Q9AUE0 View 3D Structure Click here
Q9LTG5 View 3D Structure Click here
Q9LUD7 View 3D Structure Click here
Q9LXT9 View 3D Structure Click here
Q9LYS6 View 3D Structure Click here
Q9LYS6 View 3D Structure Click here
Q9P377 View 3D Structure Click here
Q9S9U0 View 3D Structure Click here
Q9SFU6 View 3D Structure Click here
Q9SHJ3 View 3D Structure Click here
Q9SHJ3 View 3D Structure Click here
Q9SJM0 View 3D Structure Click here
Q9SL03 View 3D Structure Click here
Q9ZT82 View 3D Structure Click here

trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;