Protein Family Models

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 199. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This HMM describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases.

Gene:

iadA

Date:

2024-07-08