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{
"metadata": {
"accession": "IPR044704",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd02211": "(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR044704",
"name": "(S)-ureidoglycine aminohydrolase, N-terminal cupin domain",
"type": "Domain",
"children": []
},
"name": {
"name": "(S)-ureidoglycine aminohydrolase, N-terminal cupin domain",
"short": "UGlyAH_cupin_N"
},
"description": [
{
"text": "<p>(S)-ureidoglycine aminohydrolase (UGHY or UGlyAH) is involved in the ureide pathway, a metabolic route of purine catabolism in plants, some bacteria and probably in some fungi where, uric acid is degraded into glyoxylate and ammonia [[cite:PUB00078751]]. This enzyme is involved in the anaerobic nitrogen utilization via the assimilation of allantoin. It catalyses the second step in the allantoin degradation pathway, the deamination of the allantoin producing S-ureidoglycolate and ammonia from S-ureidoglycine [[cite:PUB00078751], [cite:PUB00096858]].</p>\n\n<p>The structure of UGlyAH from Arabidopsis thaliana (AtUGlyAH) has been studied. It contains two structurally similar β-barrel domains, called N and C (cupin) domains. AtUGlyAH binds a Mn ion through its C-terminal domain which acts as a molecular anchor to bind (S)-ureidoglycine. Its structure showed a bi-cupin fold with a conserved jelly roll-like β-barrel fold and an octameric functional unit. Several structural homologues of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features [[cite:PUB00096859]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This entry represents the N-terminal cupin domain found in (S)-ureidoglycine aminohydrolases, including UGlyAH from E.coli and its homologues from plants and fungi [[cite:PUB00096860]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"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
},
"PUB00096859": {
"PMID": 22493446,
"ISBN": null,
"volume": "287",
"issue": "22",
"year": 2012,
"title": "Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana.",
"URL": null,
"raw_pages": "18796-805",
"medline_journal": "J Biol Chem",
"ISO_journal": "J Biol Chem",
"authors": [
"Shin I",
"Percudani R",
"Rhee S."
],
"DOI_URL": null
},
"PUB00096860": {
"PMID": 23940254,
"ISBN": null,
"volume": "163",
"issue": "2",
"year": 2013,
"title": "The ureide-degrading reactions of purine ring catabolism employ three amidohydrolases and one aminohydrolase in Arabidopsis, soybean, and rice.",
"URL": null,
"raw_pages": "672-81",
"medline_journal": "Plant Physiol",
"ISO_journal": "Plant Physiol",
"authors": [
"Werner AK",
"Medina-Escobar N",
"Zulawski M",
"Sparkes IA",
"Cao FQ",
"Witte CP."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR014710",
"name": "RmlC-like jelly roll fold",
"type": "homologous_superfamily"
},
{
"accession": "IPR011051",
"name": "RmlC-like cupin domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 4160,
"pathways": 2,
"proteins": 4160,
"proteomes": 2796,
"sets": 0,
"structural_models": {
"alphafold": 3266,
"bfvd": 0
},
"structures": 6,
"taxa": 5018
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "3.5.3.26",
"url": "https://enzyme.expasy.org/EC/3.5.3.26"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
