"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PF03881"	"{'subfamilies': 0, 'domain_architectures': 159, 'interactions': 0, 'matches': 16168, 'pathways': 0, 'proteins': 15869, 'proteomes': 8623, 'sets': 1, 'structural_models': {'alphafold': 12591, 'bfvd': 0}, 'structures': 10, 'taxa': 17463}"	"{}"	"[{'text': '<p>This family includes eukaryotic fructosamine-3-kinase enzymes [[cite:PUB00008463]]. The family also includes bacterial members that have not been characterised but probably have a similar or identical function.</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR016477"	False	False	False	"{'PUB00008463': {'PMID': 11016445, 'ISBN': None, 'volume': '49', 'issue': '10', 'year': 2000, 'title': 'Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase.', 'URL': None, 'raw_pages': '1627-34', 'medline_journal': 'Diabetes', 'ISO_journal': 'Diabetes', 'authors': ['Delpierre G', 'Rider MH', 'Collard F', 'Stroobant V', 'Vanstapel F', 'Santos H', 'Van Schaftingen E.'], 'DOI_URL': 'http://intl-diabetes.diabetesjournals.org/cgi/content/abstract/49/10/1627'}}"	""	"{'name': 'Fructosamine kinase', 'short': 'Fructosamin_kin'}"	""	"{'accession': '9cx8', 'name': 'Crystal structure of Human FN3K in apo-state'}"	"{'accession': 'CL0016', 'name': 'PKinase'}"	"pfam"	"family"	"[{'title': 'Fructosamine_kinase_family', 'extract': '<p>In molecular biology the <b>fructosamine kinase family</b> is a family of enzymes. This family includes eukaryotic fructosamine-3-kinase enzymes which may initiate a process leading to the deglycation of fructoselysine and of glycated proteins and in the phosphorylation of 1-deoxy-1-morpholinofructose, fructoselysine, fructoseglycine, fructose and glycated lysozyme. The family also includes ketosamine-3-kinases (KT3K). Ketosamines derive from a non-enzymatic reaction between a sugar and a protein. Ketosamine-3-kinases (KT3K) catalyse the phosphorylation of the ketosamine moiety of glycated proteins. The instability of a phosphorylated ketosamine leads to its degradation, and KT3K is thus thought to be involved in protein repair.</p>', 'thumbnail': None}]"