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{
"metadata": {
"accession": "PF01597",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "pfam",
"member_databases": null,
"integrated": "IPR033753",
"hierarchy": null,
"name": {
"name": "Glycine cleavage H-protein",
"short": "GCV_H"
},
"description": [
{
"text": "<p>This is a family of glycine cleavage H-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyses the catabolism of glycine in eukaryotes. A lipoyl group is attached to a completely conserved lysine residue. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": [
{
"title": "Glycine_cleavage_system",
"extract": "<p>The <b>glycine cleavage system</b> (<b>GCS</b>) is also known as the <b>glycine decarboxylase complex</b> or <b>GDC</b>. The system is a series of enzymes that are triggered in response to high concentrations of the amino acid glycine. The same set of enzymes is sometimes referred to as glycine synthase when it runs in the reverse direction to form glycine. The glycine cleavage system is composed of four proteins: the T-protein, P-protein, L-protein, and H-protein. They do not form a stable complex, so it is more appropriate to call it a \"system\" instead of a \"complex\". The H-protein is responsible for interacting with the three other proteins and acts as a shuttle for some of the intermediate products in glycine decarboxylation. In both animals and plants, the glycine cleavage system is loosely attached to the inner membrane of the mitochondria. Mutations in this enzymatic system are linked with glycine encephalopathy.</p>",
"thumbnail": null
}
],
"literature": {
"PUB00004842": {
"PMID": 8197146,
"ISBN": null,
"volume": "91",
"issue": "11",
"year": 1994,
"title": "X-ray structure determination at 2.6-A resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves.",
"URL": null,
"raw_pages": "4850-3",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Pares S",
"Cohen-Addad C",
"Sieker L",
"Neuburger M",
"Douce R."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8197146"
}
},
"set_info": {
"accession": "CL0105",
"name": "Hybrid"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 143,
"interactions": 0,
"matches": 32863,
"pathways": 0,
"proteins": 32796,
"proteomes": 18597,
"sets": 1,
"structural_models": {
"alphafold": 26050,
"bfvd": 1
},
"structures": 23,
"taxa": 33690
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 13,
"alignment:full": 14591
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3wdn",
"name": "High-resolution X-ray crystal structure of bovine H-protein using a high-pressure cryocooling method"
}
}
}
