IPR000766 Galactose-1-phosphate uridyl transferase, class II
IPR001937 Galactose-1-phosphate uridyl transferase, class I
IPR011151 Histidine triad motif
Contains
IPR019779 Galactose-1-phosphate uridyl transferase, class I His-active site
Galactose-1-phosphate uridyl transferase catalyses the conversion of UDP-glucose and alpha-D-galactose 1-phosphate to alpha-D-glucose 1-phosphate and UDP-galactose during galactose metabolism. The enzyme is present
in prokaryotes and eukaryotes. Defects in GalT in humans is the cause of galactosemia, an
inherited disorder of galactose metabolism that leads to jaundice, cataracts and mental retardation.
This domain describes the C-terminal of Galactose-1-phosphate uridyl transferase. SCOP reports fold duplication of the C-terminal with the N-terminal domain. Both are involved in Zn and Fe binding
Wedekind JE, Frey PA, Rayment I.
Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution.
Biochemistry 34 1995 11049-61
[PubMed: 7669762] http://dx.doi.org/10.1021/bi00035a010
Thoden JB, Ruzicka FJ, Frey PA, Rayment I, Holden HM.
Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site.
Biochemistry 36 1997 1212-22
[PubMed: 9063869] http://dx.doi.org/10.1021/bi9626517
Wedekind JE, Frey PA, Rayment I.
The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer.
Biochemistry 35 1996 11560-9
[PubMed: 8794735] http://dx.doi.org/10.1021/bi9612677
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