3.5.1.54	G559E/G572E	site-directed mutagenesis, crystal structure analysis, the mutant shows 14fold increaed Km for allophanate, and reduced substrate binding at the N-domain active site, but is catalytically active	734220	
3.5.1.54	G559E/G572E	site-directed mutagenesis, the mutant shows abolished activity	-, 744532	
3.5.1.54	H488A	site-directed mutagenesis	752542	
3.5.1.54	K91A	site-directed mutagenesis, inactive mutant	669098	
3.5.1.54	additional information	construction of the gene encoding C-terminally truncated AtzF mutant, AtzF467	733034	
3.5.1.54	additional information	generation of isolated domains	734220	
3.5.1.54	additional information	generation of the KlUADELTABCCP construct via insertion a stop codon after base pair 5223	-, 744532	
3.5.1.54	additional information	significantly higher concentrations of extracellular NH4-N are detected in the cultures along with overexpression of urea carboxylase (UC) and allophanate hydrolase (AH) genes. The bacterium forms biofilm, and displays swimming and swarming motilities in presence of urea. Additional glucose supply to urea boosts the colonization but ameliorates the media alkalization and ammonification through suppression of gene expressions encoding UC and AH	-, 774125	
3.5.1.54	R307A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	-, 733342	
3.5.1.54	R307M	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	-, 733342	
3.5.1.54	S165A	site-directed mutagenesis, inactive mutant	669098	
3.5.1.54	S177A	site-directed mutagenesis, crystal structure analysis	734220	
3.5.1.54	S177A	site-directed mutagenesis, the mutation inactivates the isolated KlAH	744532	
3.5.1.54	S179A	site-directed mutagenesis	-, 746393	
3.5.1.54	S189A	site-directed mutagenesis, inactive mutant	669098	
3.5.1.54	Y299A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	-, 733342	
3.5.1.54	Y299A/R307A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	733342	
3.5.1.54	Y299A/R307M	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	-, 733342	
3.5.1.54	Y299F	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	-, 733342	
3.5.1.54	Y299F/R307A	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	733342	
3.5.1.54	Y299F/R307M	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	733342