Summary: Glycosyl hydrolase family 65, N-terminal domain
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Glycoside hydrolase family 65 Edit Wikipedia article
|Glycosyl hydrolase family 65, N-terminal domain|
maltose phosphorylase from lactobacillus brevis
|Glycosyl hydrolase family 65 central catalytic domain|
maltose phosphorylase from lactobacillus brevis
|Glycosyl hydrolase family 65, C-terminal domain|
maltose phosphorylase from lactobacillus brevis
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.
This family of glycosyl hydrolases (CAZY GH_65) includes vacuolar acid trehalase and maltose phosphorylases. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose.
It consists of three structural domains. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerisation interface. The N-terminal domain is believed to be essential for catalytic activity although its precise function remains unknown.
- 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.
- van Tilbeurgh H, Egloff MP, Uppenberg J, Haalck L (2001). "Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases". Structure 9 (8): 689–697. doi:10.1016/S0969-2126(01)00626-8. PMID 11587643.
Glycosyl hydrolase family 65, N-terminal domain Provide feedback
This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain.
Internal database links
External database links
- 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
- the number of residues in the sequence
- the Pfam graphic itself.
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This clan is composed of a beta-sandwich that was first observed in domain 5 of beta-galactosidase, then as the central domain of copper amine oxidase, the C-terminal domain of chondroitinase, the C-terminal domain of hyaluronate lyase, the N-terminal domain of maltose phosphorylase and in Galactose Mutarotase . All these enzymes act on a sugar substrate.
The clan contains the following 11 members:Aldose_epim Bgal_small_N DUF4432 Gal_mutarotas_2 Glyco_hyd_65N_2 Glyco_hydro_38C Glyco_hydro_65N Lyase_8 MdoG Rhamnogal_lyase YidC_periplas
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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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:||45|
|Number in full:||2684|
|Average length of the domain:||220.30 aa|
|Average identity of full alignment:||28 %|
|Average coverage of the sequence by the domain:||29.45 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||2|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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_hyd_65N_2 domain has been found. There are 9 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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