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InterPro: IPR005027 Glycosyl transferase, family 43
Protein matches
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UniProtKB Matches: 323 proteins |
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Accession
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IPR005027 Glyco_trans_43 |
Type
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Family |
Signatures
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GO Term annotation
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Function
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GO:0015018 galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
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Component
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GO:0016020 membrane
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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'.
Glycosyltransferase family 43 GT43 comprises enzymes with only one known activities; beta-glucuronyltransferase(EC:2.4.1);.
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Structural links
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Database links
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Pfam Clan: CL0110.8
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Additional Reading
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Kakuda S, Shiba T, Ishiguro M, Tagawa H, Oka S, Kajihara Y, Kawasaki T, Wakatsuki S, Kato R.
Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1.
J. Biol. Chem. 279 2004 22693-703
[PubMed: 14993226]
http://dx.doi.org/10.1074/jbc.M400622200
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Tone Y, Pedersen LC, Yamamoto T, Izumikawa T, Kitagawa H, Nishihara J, Tamura J, Negishi M, Sugahara K.
2-o-phosphorylation of xylose and 6-o-sulfation of galactose in the protein linkage region of glycosaminoglycans influence the glucuronyltransferase-I activity involved in the linkage region synthesis.
J. Biol. Chem. 283 2008 16801-7
[PubMed: 18400750]
http://dx.doi.org/10.1074/jbc.M709556200
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Pedersen LC, Tsuchida K, Kitagawa H, Sugahara K, Darden TA, Negishi M.
Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I.
J. Biol. Chem. 275 2000 34580-5
[PubMed: 10946001]
http://dx.doi.org/10.1074/jbc.M007399200
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Terayama K, Seiki T, Nakamura A, Matsumori K, Ohta S, Oka S, Sugita M, Kawasaki T.
Purification and characterization of a glucuronyltransferase involved in the biosynthesis of the HNK-1 epitope on glycoproteins from rat brain.
J. Biol. Chem. 273 1998 30295-300
[PubMed: 9804790]
http://dx.doi.org/10.1074/jbc.273.46.30295
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Pedersen LC, Darden TA, Negishi M.
Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA.
J. Biol. Chem. 277 2002 21869-73
[PubMed: 11950836]
http://dx.doi.org/10.1074/jbc.M112343200
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Wei G, Bai X, Sarkar AK, Esko JD.
Formation of HNK-1 determinants and the glycosaminoglycan tetrasaccharide linkage region by UDP-GlcUA:Galactose beta1, 3-glucuronosyltransferases.
J. Biol. Chem. 274 1999 7857-64
[PubMed: 10075678]
http://dx.doi.org/10.1074/jbc.274.12.7857
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InterPro 23.1
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