 |
InterPro: IPR012341 Six-hairpin glycosidase
Protein matches
|
UniProtKB Matches: 4490 proteins |
|
Accession
|
IPR012341 6hp_glycosidase |
Type
|
Domain |
Signatures
|
|
InterPro Relationships
|
|
Children
|
IPR000556 Glycoside hydrolase, 48F
IPR005195 Glycoside hydrolase family 65, central catalytic
IPR011613 Glycoside hydrolase 15-related
|
|
Found in
|
IPR001701 Glycoside hydrolase, family 9
IPR002037 Glycoside hydrolase, family 8
IPR008928 Six-hairpin glycosidase-like
IPR010819 N-acylglucosamine 2-epimerase
IPR010905 Glycosyl hydrolase, family 88
|
|
Contains
|
IPR018221 Glycoside hydrolase, family 9, active site
IPR019834 Glycoside hydrolase, family 8, conserved site
|
GO Term annotation
|
|
Function
|
GO:0003824 catalytic activity
|
|
InterPro annotation
|
|
Entry Details in BioMart
|
Abstract
|
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 (EC:2.4.1.-) and related proteins into distinct sequence based families has been described [1]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [2]. 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'.
The six-hairpin glycoside transferase domain contains up to seven alpha-hairpins arranged in closed circular array. Protein families that contain domains with this structure include glucoamylases, various endocellulases and exocellulases (catalytic domain), N-acyl-D-glucosamine 2-epimerases, bacterial maltose phosphorylase (central domain), and bacterial glucoamylases (C-terminal domain).
|
Structural links
|
|
Database links
|
|
Additional Reading
|
|
Itoh T, Ochiai A, Mikami B, Hashimoto W, Murata K.
A novel glycoside hydrolase family 105: the structure of family 105 unsaturated rhamnogalacturonyl hydrolase complexed with a disaccharide in comparison with family 88 enzyme complexed with the disaccharide.
J. Mol. Biol. 360 2006 573-85
[PubMed: 16781735]
http://dx.doi.org/10.1016/j.jmb.2006.04.047
|
|
Itoh T, Hashimoto W, Mikami B, Murata K.
Crystal structure of unsaturated glucuronyl hydrolase complexed with substrate: molecular insights into its catalytic reaction mechanism.
J. Biol. Chem. 281 2006 29807-16
[PubMed: 16893885]
http://dx.doi.org/10.1074/jbc.M604975200
|
|
Parsiegla G, Reverbel C, Tardif C, Driguez H, Haser R.
Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action.
J. Mol. Biol. 375 2008 499-510
[PubMed: 18035374]
http://dx.doi.org/10.1016/j.jmb.2007.10.039
|
|
Yasutake Y, Kawano S, Tajima K, Yao M, Satoh Y, Munekata M, Tanaka I.
Structural characterization of the Acetobacter xylinum endo-beta-1,4-glucanase CMCax required for cellulose biosynthesis.
Proteins 64 2006 1069-77
[PubMed: 16804941]
http://dx.doi.org/10.1002/prot.21052
|
|
De Vos D, Collins T, Nerinckx W, Savvides SN, Claeyssens M, Gerday C, Feller G, Van Beeumen J.
Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product.
Biochemistry 45 2006 4797-807
[PubMed: 16605248]
http://dx.doi.org/10.1021/bi052193e
|
|
|
InterPro 23.1
|