Protein Family Models

This family represents the conserved barrel domain of the 'cupin' superfamily [1] ('cupa' is the Latin term for a small barrel). [1]. 9573603. Cupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins. Dunwell JM;. Biotechnol Genet Eng Rev 1998;15:1-32. (from Pfam)

Date:

2024-10-16

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

This model represents a protein containing a tandem arrangement of cupin domains (N-terminal part of PF07883 and C-terminal more distantly related to PF00190). This protein is found in the vicinity of genes involved in the catabolism of allantoin, a breakdown product of urate and sometimes of urate iteslf. Recent analysis shows that members in general behave as ureidoglycine aminohydrolase (EC 3.5.3.26). However, a branch within the family (see NF040771 ) has additional activity as allantoate amidohydrolase (AAH) at the same active site, and marks genomes that lack a separately encoded AAH enzyme.

Gene:

allE

Date:

2022-03-17

ura-cupin family protein

Date:

2017-03-02