Protein Family Models

Date:

2024-08-14

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)

Date:

2024-10-16

Date:

2021-10-20

dihydroorotase catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis

Date:

2023-03-02

In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this HMM should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but the model excludes related proteins such as allantoinase.

Gene:

pyrC

Date:

2021-04-27