Summary: Glycosyl hydrolase family 48
This is the Wikipedia entry entitled "Glycoside hydrolase family 48". More...
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Glycoside hydrolase family 48 Edit Wikipedia article
x-tal structure of the mutant e44q of the cellulase cel48f in complex with a thiooligosaccharide
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. This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
An example of an enzyme containing a domain belonging to this family is one of the cellulases (celA) from the genome of the thermophilic anaerobic bacterium Caldocellum saccharolyticum. The celA gene product is a polypeptide of 1751 amino acids; this has a multidomain structure comprising two catalytic domains and two cellulose-binding domains, linked by Pro-Thr-rich regions. The N-terminal domain encodes an endoglucanase activity on carboxymethylcellulose, consistent with its similarity to several endo-1, 4-beta-D-glucanase sequences, and is a member of the glycoside hydrolase family 9. The C-terminal domain belongs to this family shows similarity to a cellulase from Clostridium thermocellum (CelS), which acts synergistically with a second component to hydrolyse crystalline cellulose.
- 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.
- 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.
- Saul DJ, Bergquist PL, Te o VS (1995). "celA, another gene coding for a multidomain cellulase from the extreme thermophile Caldocellum saccharolyticum". Appl. Microbiol. Biotechnol. 43 (2): 291–296. doi:10.1007/BF00172827. PMID 7612247.
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Glycosyl hydrolase family 48 Provide feedback
Members of this family are endoglucanase EC:22.214.171.124 and exoglucanase EC:126.96.36.199 enzymes that cleave cellulose or related substrate.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000556
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.
The largest cellulase gene sequenced to date is one of the cellulases (celA) from the genome of the thermophilic anaerobic bacterium Caldocellum saccharolyticum. The celA gene product is a polypeptide of 1751 amino acids; this has a multidomain structure comprising two catalytic domains and two cellulose-binding domains, linked by Pro-Thr-rich regions. The N-terminal domain encodes an endoglucanase activity on carboxymethylcellulose, consistent with its similarity to several endo-1, 4-beta-D-glucanase sequences. The C-terminal domain shows similarity to a cellulase from Clostridium thermocellum (CelS), which acts synergistically with a second component to hydrolyse crystalline cellulose [PUBMED:7612247].
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)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This Clan includes CAZy clans GH-L, GH-M and GH-G. The members of this clan share a common structure composed of 6 helical hairpins. Most members of this superfamily are glycosyl hydrolase enzymes.
The clan contains the following 28 members:A2M_comp Bac_rhamnosid C5-epim_C Cobalamin_bind DUF1237 DUF1680 DUF2807 DUF4097 DUF4098 DUF608 GDE_C GlcNAc_2-epim Glyco_hydro_100 Glyco_hydro_15 Glyco_hydro_47 Glyco_hydro_48 Glyco_hydro_63 Glyco_hydro_65m Glyco_hydro_76 Glyco_hydro_8 Glyco_hydro_88 Glyco_hydro_9 Glycoamylase Pec_lyase Prenyltrans Prenyltrans_1 Prenyltrans_2 Trehalase
We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Number in seed:||7|
|Number in full:||213|
|Average length of the domain:||485.10 aa|
|Average identity of full alignment:||49 %|
|Average coverage of the sequence by the domain:||70.58 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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_48 domain has been found. There are 21 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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