Summary: Glycosyl hydrolase family 3 C-terminal domain
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This is the Wikipedia entry entitled "Glycoside hydrolase family 3". More...
Glycoside hydrolase family 3 Edit Wikipedia article
Glycosyl hydrolase family 3 N terminal domain | |||||||||
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Identifiers | |||||||||
Symbol | Glyco_hydro_3 | ||||||||
Pfam | PF00933 | ||||||||
Pfam clan | CL0058 | ||||||||
InterPro | IPR001764 | ||||||||
PROSITE | PDOC00621 | ||||||||
SCOP2 | 1ex1 / SCOPe / SUPFAM | ||||||||
CAZy | GH3 | ||||||||
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Glycosyl hydrolase family 3 C-terminal domain | |||||||||
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![]() crystal structure of barley beta-d-glucan glucohydrolase isoenzyme exo1 | |||||||||
Identifiers | |||||||||
Symbol | Glyco_hydro_3_C | ||||||||
Pfam | PF01915 | ||||||||
InterPro | IPR002772 | ||||||||
PROSITE | PDOC00621 | ||||||||
SCOP2 | 1ex1 / SCOPe / SUPFAM | ||||||||
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In molecular biology, glycoside hydrolase family 3 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 3 CAZY GH_3 comprises enzymes with a number of known activities; beta-glucosidase (EC 3.2.1.21); beta-xylosidase (EC 3.2.1.37); N-acetyl beta-glucosaminidase (EC 3.2.1.52); glucan beta-1,3-glucosidase (EC 3.2.1.58); cellodextrinase (EC 3.2.1.74); exo-1,3-1,4-glucanase (EC 3.2.1). These enzymes are two-domain globular proteins that are N-glycosylated at three sites.[6]
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.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ 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.
- ^ Varghese JN, Fincher GB, Hrmova M (1999). "Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase". Structure. 7 (2): 179–190. doi:10.1016/S0969-2126(99)80024-0. PMID 10368285.
{{cite journal}}
: CS1 maint: multiple names: authors list (link)
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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 hydrolase family 3 C-terminal domain Provide feedback
This domain is involved in catalysis and may be involved in binding beta-glucan [1]. This domain is found associated with PF00933.
Literature references
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Varghese JN, Hrmova M, Fincher GB; , Structure Fold Des 1999;7:179-190.: Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase. PUBMED:10368285 EPMC:10368285
Internal database links
SCOOP: | Fascin GLEYA Glyco_hydro_3 PA14 |
External database links
PROSITE: | PDOC00621 |
SCOP: | 1ex1 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002772
Glycoside hydrolase family 3 CAZY comprises enzymes with a number of known activities; beta-glucosidase ( EC ); beta-xylosidase ( EC ); N-acetyl beta-glucosaminidase ( EC ); glucan beta-1,3-glucosidase ( EC ); cellodextrinase( EC ); exo-1,3-1,4-glucanase ( EC ).
These enzymes are two-domain globular proteins that are N-glycosylated at three sites [ PUBMED:10368285 ]. This entry represents the C-terminal domain, involved in catalysis and may be involved in binding beta-glucan [ PUBMED:10368285 ]. It is found associated with .
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553) |
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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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 (116) |
Full (25133) |
Representative proteomes | UniProt (78635) |
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RP15 (2556) |
RP35 (10759) |
RP55 (22627) |
RP75 (38100) |
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HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (116) |
Full (25133) |
Representative proteomes | UniProt (78635) |
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RP15 (2556) |
RP35 (10759) |
RP55 (22627) |
RP75 (38100) |
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Raw Stockholm | |||||||
Gzipped |
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
Seed source: | Pfam-B_1151 (release 3.0) |
Previous IDs: | glycosyl_hydr14; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 116 |
Number in full: | 25133 |
Average length of the domain: | 257 aa |
Average identity of full alignment: | 26 % |
Average coverage of the sequence by the domain: | 33.22 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null --hand HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 204 | ||||||||||||
Family (HMM) version: | 25 | ||||||||||||
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_3_C domain has been found. There are 185 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.