This domain is present in bacterial ureases and corresponds to the gap region between the C-terminus of the beta-chain Urease beta subunit Pfam:PF00699 and the N-terminus of the alpha-chain Urease alpha-subunit, N-terminal domain Pfam:PF00449 [1]. It ...
This domain is present in bacterial ureases and corresponds to the gap region between the C-terminus of the beta-chain Urease beta subunit Pfam:PF00699 and the N-terminus of the alpha-chain Urease alpha-subunit, N-terminal domain Pfam:PF00449 [1]. It is suggested that this region is required for the stability of the putative transmembrane beta-barrel, and might be the reason for bacterial urease (B. pasteurii) not being lethal to insects [2].
The N-terminal domain is a composite domain and plays a major trimer stabilising role by contacting the catalytic domain of the symmetry related alpha-subunit.
This family of enzymes are a a large metal dependent hydrolase superfamily [1]. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisatio ...
This family of enzymes are a a large metal dependent hydrolase superfamily [1]. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source [2]. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyse the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit [3]. Dihydroorotases (EC:3.5.2.3) are also included [4-5].
