Molecular Cloning of a Novel Glucuronokinase/Putative Pyrophosphorylase from Zebrafish Acting in an UDP-Glucuronic Acid Salvage Pathway
Figure 9
Sequence alignment of two bacterial nucleotidyltransferase with known crystal structure (1H5T [33]; 2PA4 [51]) and the pyrophosphorylase domain from zebrafish DrGKUP.
Note that some of the residues identified in the E. coli enzyme to bind the substrate are conserved in the zebrafish sequence (e.g. Gly11; Asp91; Asp118; Lys163; Arg220; numbers refer to the E. coli sequence 1H5T).