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InterPro: IPR008928 Six-hairpin glycosidase-like
Protein matches
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UniProtKB Matches: 10579 proteins |
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Accession
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IPR008928 6-hairpin_glycosidase-like |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR008902 Bacterial alpha-L-rhamnosidase
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Found in
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IPR001661 Glycoside hydrolase, family 37
IPR004888 Glycoside hydrolase, family 63
IPR005198 Glycoside hydrolase, family 76
IPR006421 Glycogen debranching enzyme
IPR006451 Glycogen debranching enzyme, archaeal type
IPR006775 Glucosylceramidase
IPR006937 Plant neutral invertase
IPR008313 Uncharacterised conserved protein UCP028846
IPR008734 Phosphorylase kinase alphabeta
IPR010401 Amylo-alpha-1,6-glucosidase
IPR012878 Protein of unknown function DUF1680
IPR014480 Mannan endo-1,6-alpha-mannosidase
IPR014512 Predicted O-glycosyl hydrolase
IPR014551 Beta-glucosidase, GBA2 type
IPR016518 Uncharacterised conserved protein UCP007663
IPR017045 Maltose phosphorylase/glycosyl hydrolase/vacuolar acid trehalase
IPR020429 LanC-like protein superfamily
IPR020464 LanC-like protein, eukaryotic
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Contains
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IPR005194 Glycoside hydrolase, family 65, C-terminal
IPR012341 Six-hairpin glycosidase
IPR018221 Glycoside hydrolase, family 9, active site
IPR018232 Glycoside hydrolase, family 37, conserved site
IPR019834 Glycoside hydrolase, family 8, conserved site
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GO Term annotation
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Function
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GO:0003824 catalytic activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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).
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Structural links
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Database links
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Additional Reading
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Gibson RP, Gloster TM, Roberts S, Warren RA, Storch de Gracia I, Garcia A, Chiara JL, Davies GJ.
Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors.
Angew. Chem. Int. Ed. Engl. 46 2007 4115-9
[PubMed: 17455176]
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Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH.
The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion.
J. Mol. Biol. 367 2007 895-908
[PubMed: 17292397]
http://dx.doi.org/10.1016/j.jmb.2006.11.001
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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
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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
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Sevcik J, Hostinova E, Solovicova A, Gasperik J, Dauter Z, Wilson KS.
Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain.
FEBS J. 273 2006 2161-71
[PubMed: 16649993]
http://dx.doi.org/10.1111/j.1742-4658.2006.05230.x
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InterPro 23.1
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