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

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. [1]. 7754395. The crystal structure of urease from Klebsiella aerogenes. Jabri E, Carr MB, Hausinger RP, Karplus PA;. Science 1995;268:998-1004. (from Pfam)

Date:

2024-10-16

urease subunit alpha is a component of the heterotrimeric enzyme that catalyzes the hydrolysis of urea to form carbon dioxide and ammonia

Date:

2023-02-23

Catalyzes the hydrolysis of urea into ammonia and carbon dioxide; the ammonia released plays a key role in bacterial survival by neutralizing acids when colonizing the gastric mucosa

Date:

2020-10-26

Catalyzes the hydrolysis of urea into ammonia and carbon dioxide; the ammonia released plays a key role in bacterial survival by neutralizing acids when colonizing the gastric mucosa

Date:

2024-05-02

This HMM describes the urease alpha subunit UreC (designated beta or B chain, UreB in Helicobacter species). Accessory proteins for incorporation of the nickel cofactor are usually found in addition to the urease alpha, beta, and gamma subunits. The trusted cutoff is set above the scores of many reported fragments and of a putative second urease alpha chain in Streptomyces coelicolor.

Gene:

ureC

Date:

2021-04-27