Summary: Glycosyl hydrolase family 92
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This is the Wikipedia entry entitled "Glycoside hydrolase family 92". More...
Glycoside hydrolase family 92
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Glyco_hydro_92 | ||||||||
| Pfam | PF07971 | ||||||||
| Pfam clan | CL0268 | ||||||||
| InterPro | IPR012939 | ||||||||
| CAZy | GH92 | ||||||||
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In molecular biology, glycoside hydrolase family 92 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]
This domain occurs within alpha-1,2-mannosidases, which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation.[6]
Glycoside hydrolase family 92 includes enzymes with mannosyl-oligosaccharide α-1,2-mannosidase EC 3.2.1.113, mannosyl-oligosaccharide α-1,3-mannosidase EC 3.2.1.-, mannosyl-oligosaccharide α-1,6-mannosidase EC 3.2.1.-, α-mannosidase EC 3.2.1.24, α-1,2-mannosidase EC 3.2.1.-, α-1,3-mannosidase EC 3.2.1.- and α-1,4-mannosidase EC 3.2.1.- activities. It includes enzymes critical for the maturation of N-linked oligosaccharides and ER-associated degradation.[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.
- ^ a b Liu Y, Choudhury P, Cabral CM, Sifers RN (February 1999). "Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome". J. Biol. Chem. 274 (9): 5861–7. PMID 10026209.
This article incorporates text from the public domain Pfam and InterPro IPR012939
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 hydrolase family 92
Members of this family are alpha-1,2-mannosidases, enzymes which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation [1].
Literature references
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Liu Y, Choudhury P, Cabral CM, Sifers RN; , J Biol Chem 1999;274:5861-5867.: Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. PUBMED:10026209
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Naumoff DG; , BMC Genomics. 2005;6:112.: GH97 is a new family of glycoside hydrolases, which is related to the alpha-galactosidase superfamily. PUBMED:16131397
Clan
This family is a member of clan Pec_lyase (CL0268), which has a total of 21 members.
External database links
| CAZY: | GH92 |
| PANDIT: | PF07971 |
| Pseudofam: | PF07971 |
| SYSTERS: | Glyco_hydro_92 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR012939
This domain occurs within alpha-1,2-mannosidases, which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation [PUBMED:10026209].
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 Pec_lyase (CL0268), which contains the following 21 members:
Adeno_E1B_55K Autotrns_rpt Beta_helix Chlam_PMP Disaggr_assoc DUF1565 DUF3737 Fil_haemagg Fil_haemagg_2 Glyco_hydro_28 Glyco_hydro_49 Glyco_hydro_80 Glyco_hydro_92 Haemagg_act NosD Pec_lyase_C Pectate_lyase Pectate_lyase_3 Pectinesterase Pertactin PhageP22-tailAlignments
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_1199 (release 16.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Mistry J |
| Number in seed: | 193 |
| Number in full: | 1628 |
| Average length of the domain: | 475.50 aa |
| Average identity of full alignment: | 31 % |
| Average coverage of the sequence by the domain: | 60.80 % |
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: | 502 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| 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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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_92 domain has been found. There are 32 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