Molecular Cloning of a Novel Glucuronokinase/Putative Pyrophosphorylase from Zebrafish Acting in an UDP-Glucuronic Acid Salvage Pathway
Figure 2
Sequence and Phylogenetic Analysis of DrGKUP.
(A) shows a bifunctional enzyme comprised of a putative kinase domain (DrGK; 357 amino acids; 40 kDa) at the C-terminal end and a putative pyrophosphorylase domain (DrUP; 260 amino acids; 30 kDa) at the N-terminal end. For the pyrophosphorylase domain analysis Danio rerio (XP_005157584.1), Xenopus tropicalis (XP_002940431.1), Ruminococcus_sp. (WP_021925996.1) and Firmicutes_bacterium (WP_022231022.1) were aligned and for glucuronokinase domain analysis Danio rerio (NP_001107088.1), Xenopus tropicalis (AAI55522.1), Arabidopsis thaliana (AAV74231.1) and Glycine max (NP_001242154.1) were aligned and with the pairwise method using Clustal Omega. (C) Identity and Similarity were calculated with GENEDOC and (B) phylogenetic distance trees were calculated with JalView. Neither a homologous glucuronokinase nor a pyrophosphorylase sequence could be found in higher animals or humans.