Protein Family Models

This entry represents the cupin domain, with a conserved jelly roll-like beta-barrel fold capable of homodimerisation found in bacteria, plant and fungi. It is present in EutQ family from the eut operon, involved in ethanolamine degradation. EutQ is essential during anoxic growth and has acetate kinase activity [1]. The cupin domain from EutQ does not possess the His residues responsible for metal coordination in other classes of cupins [2]. This domain is also found in (S)-ureidoglycine aminohydrolase (UGlyAH) from E.coli, which is involved in the anaerobic nitrogen utilisation via the assimilation of allantoin. It catalyses the deamination of allantoin to produce S-ureidoglycolate and ammonia from S-ureidoglycine [3,4]. [1]. 26448059. The EutQ and EutP proteins are novel acetate kinases involved in ethanolamine catabolism: physiological implications for the function of the ethanolamine metabolosome in Salmonella enterica. Moore TC, Escalante-Semerena JC;. Mol Microbiol. 2016;99:497-511. [2]. 23144756. Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment. Pitts AC, Tuck LR, Faulds-Pain A, Lewis RJ, Marles-Wright J;. PLoS One. 2012;7:e48360. [3]. 19935661. Ureide catabolism in Arabidopsis thaliana and Escherichia coli. Werner AK, Romeis T, Witte CP;. Nat Chem Biol. 2010;6:19-21. [4]. 20038185. Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria. Serventi F, Ramazzina I, Lamberto I, Puggioni V, Gatti R, Percudani R;. ACS Chem Biol. 2010;5:203-214. (from Pfam)

Date:

2024-10-16

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

Date:

2024-11-08