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amidohydrolase family protein
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]. [1]. 9144792. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Holm L, Sander C;. Proteins 1997;28:72-82. [2]. 8550522. Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis. Nygaard P, Duckert P, Saxild HH;. J Bacteriol 1996;178:846-853. [3]. 7754395. The crystal structure of urease from Klebsiella aerogenes. Jabri E, Carr MB, Hausinger RP, Karplus PA;. Science 1995;268:998-1004. [4]. 9878395. Novel organization and sequences of five genes encoding all six enzymes for de novo pyrimidine biosynthesis in Trypanosoma cruzi. Gao G, Nara T, Nakajima-Shimada J, Aoki T;. J Mol Biol 1999;285:149-161. [5]. 8590465. As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe. Lollier M, Jaquet L, Nedeva T, Lacroute F, Potier S, Souciet JL;. Curr Genet 1995;28:138-149. (from Pfam)
putative aminohydrolase SsnA
putative aminohydrolase SsnA is a putative selenium metabolism protein
putative selenium metabolism protein SsnA
Members of this protein family are found exclusively in genomes that contain putative set of labile selenium-dependent enzyme accessory proteins as well as homologs of a labile selenium-dependent purine hydroxylase. A mutant in this gene in Escherichia coli had improved stationary phase viability. The function is unknown.
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