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Galactose-1-phosphate uridyl transferase, C-terminal domain
SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding. [1]. 7669762. Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution. Wedekind JE, Frey PA, Rayment I;. Biochemistry 1995;34:11049-11061. (from Pfam)
Galactose-1-phosphate uridyl transferase, N-terminal domain
SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding. [1]. 7669762. Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution. Wedekind JE, Frey PA, Rayment I;. Biochemistry 1995;34:11049-11061. (from Pfam)
UDP-glucose--hexose-1-phosphate uridylyltransferase
galactose-1-phosphate uridylyltransferase
galactose-1-phosphate uridylyltransferase catalyzes the reversible transfer of the uridine 5'-monophosphoryl moiety of UDP-glucose to the phosphate group of galactose 1-phosphate to form UDP-galactose in the third step of the Leloir pathway
This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model PF01087 from PFAM.
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