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 [[cite:PUB00096913]]. The cupin domain from EutQ does not possess the His residues responsible for metal coordination in other classes of cupins [[cite:PUB00063996]]. 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 [[cite:PUB00078751],[cite:PUB00096858]].
","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Cupin_superfamily","extract":"The cupin superfamily is a diverse superfamily of proteins named after its conserved barrel domain. The superfamily includes a wide variety of enzymes as well as non-enzymatic seed storage proteins.
","thumbnail":null}],"literature":{"PUB00096913":{"PMID":26448059,"ISBN":null,"volume":"99","issue":"3","year":2016,"title":"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.","URL":null,"raw_pages":"497-511","medline_journal":"Mol Microbiol","ISO_journal":"Mol Microbiol","authors":["Moore TC","Escalante-Semerena JC."],"DOI_URL":null},"PUB00078751":{"PMID":19935661,"ISBN":null,"volume":"6","issue":"1","year":2010,"title":"Ureide catabolism in Arabidopsis thaliana and Escherichia coli.","URL":null,"raw_pages":"19-21","medline_journal":"Nat Chem Biol","ISO_journal":"Nat. Chem. Biol.","authors":["Werner AK","Romeis T","Witte CP."],"DOI_URL":"http://dx.doi.org/10.1038/nchembio.265"},"PUB00096858":{"PMID":20038185,"ISBN":null,"volume":"5","issue":"2","year":2010,"title":"Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria.","URL":null,"raw_pages":"203-14","medline_journal":"ACS Chem Biol","ISO_journal":"ACS Chem Biol","authors":["Serventi F","Ramazzina I","Lamberto I","Puggioni V","Gatti R","Percudani R."],"DOI_URL":null},"PUB00063996":{"PMID":23144756,"ISBN":null,"volume":"7","issue":"10","year":2012,"title":"Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.","URL":null,"raw_pages":"e48360","medline_journal":"PLoS One","ISO_journal":"PLoS ONE","authors":["Pitts AC","Tuck LR","Faulds-Pain A","Lewis RJ","Marles-Wright J."],"DOI_URL":"http://dx.doi.org/10.1371/journal.pone.0048360"}},"set_info":{"accession":"CL0029","name":"Cupin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":78,"interactions":0,"matches":11372,"pathways":0,"proteins":11191,"proteomes":5435,"sets":1,"structural_models":{"alphafold":7292},"structures":19,"taxa":8650},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":24,"alignment:full":5340},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1o5u","name":"Crystal structure of a duf861 family protein (tm1112) from thermotoga maritima at 1.83 A resolution"}}}