"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"
"cd19367"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 3500, 'pathways': 0, 'proteins': 3500, 'proteomes': 2563, 'sets': 1, 'structural_models': {'alphafold': 2765, 'bfvd': 0}, 'structures': 2, 'taxa': 4910}"	"{}"	"[{'text': '<p>This TenA family belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal HMP kinase/HMP-P kinase (ThiD-like) domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). A majority of this family are single-domain TenA_C- like proteins; some however have additional domains such as a ThiD domain. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. [[cite:PUB00064918], [cite:PUB00108479], [cite:PUB00070662], [cite:PUB00108053], [cite:PUB00108054], [cite:PUB00074296], [cite:PUB00108480], [cite:PUB00074293]]</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	""	False	False	False	"{'PUB00108479': {'PMID': 21904031, 'ISBN': None, 'volume': '67', 'issue': 'Pt 9', 'year': 2011, 'title': 'Structure of trifunctional THI20 from yeast.', 'URL': None, 'raw_pages': '784-91', 'medline_journal': 'Acta Crystallogr D Biol Crystallogr', 'ISO_journal': 'Acta Crystallogr D Biol Crystallogr', 'authors': ['French JB', 'Begley TP', 'Ealick SE.'], 'DOI_URL': None}, 'PUB00108053': {'PMID': 17637774, 'ISBN': None, 'volume': '3', 'issue': '8', 'year': 2007, 'title': 'At the crossroad of thiamine degradation and biosynthesis.', 'URL': None, 'raw_pages': '454-5', 'medline_journal': 'Nat Chem Biol', 'ISO_journal': 'Nat Chem Biol', 'authors': ['Bettendorff L.'], 'DOI_URL': None}, 'PUB00064918': {'PMID': 18028398, 'ISBN': None, 'volume': '8', 'issue': '2', 'year': 2008, 'title': 'Involvement of thiaminase II encoded by the THI20 gene in thiamin salvage of Saccharomyces cerevisiae.', 'URL': None, 'raw_pages': '266-75', 'medline_journal': 'FEMS Yeast Res', 'ISO_journal': 'FEMS Yeast Res.', 'authors': ['Onozuka M', 'Konno H', 'Kawasaki Y', 'Akaji K', 'Nosaka K.'], 'DOI_URL': 'http://dx.doi.org/10.1111/j.1567-1364.2007.00333.x'}, 'PUB00108480': {'PMID': 10383756, 'ISBN': None, 'volume': '32', 'issue': '6', 'year': 1999, 'title': ""Genetic redundancy and gene fusion in the genome of the Baker's yeast Saccharomyces cerevisiae: functional characterization of a three-member gene family involved in the thiamine biosynthetic pathway."", 'URL': None, 'raw_pages': '1140-52', 'medline_journal': 'Mol Microbiol', 'ISO_journal': 'Mol Microbiol', 'authors': ['Llorente B', 'Fairhead C', 'Dujon B.'], 'DOI_URL': None}, 'PUB00108054': {'PMID': 29018119, 'ISBN': None, 'volume': '8', 'issue': '5', 'year': 2017, 'title': 'Globally Important Haptophyte Algae Use Exogenous Pyrimidine Compounds More Efficiently than Thiamin. ', 'URL': None, 'raw_pages': 'e01459-17', 'medline_journal': 'mBio', 'ISO_journal': 'mBio', 'authors': ['Gutowska MA', 'Shome B', 'Sudek S', 'McRose DL', 'Hamilton M', 'Giovannoni SJ', 'Begley TP', 'Worden AZ.'], 'DOI_URL': None}, 'PUB00070662': {'PMID': 17618314, 'ISBN': None, 'volume': '3', 'issue': '8', 'year': 2007, 'title': 'A new thiamin salvage pathway.', 'URL': None, 'raw_pages': '492-7', 'medline_journal': 'Nat Chem Biol', 'ISO_journal': 'Nat. Chem. Biol.', 'authors': ['Jenkins AH', 'Schyns G', 'Potot S', 'Sun G', 'Begley TP.'], 'DOI_URL': 'http://dx.doi.org/10.1038/nchembio.2007.13'}, 'PUB00074296': {'PMID': 25014715, 'ISBN': None, 'volume': '463', 'issue': '1', 'year': 2014, 'title': 'Salvage of the thiamin pyrimidine moiety by plant TenA proteins lacking an active-site cysteine.', 'URL': None, 'raw_pages': '145-55', 'medline_journal': 'Biochem J', 'ISO_journal': 'Biochem. J.', 'authors': ['Zallot R', 'Yazdani M', 'Goyer A', 'Ziemak MJ', 'Guan JC', 'McCarty DR', 'de Crecy-Lagard V', 'Gerdes S', 'Garrett TJ', 'Benach J', 'Hunt JF', 'Shintani DK', 'Hanson AD.'], 'DOI_URL': 'http://dx.doi.org/10.1042/BJ20140522'}, 'PUB00074293': {'PMID': 9419250, 'ISBN': None, 'volume': '45', 'issue': '6', 'year': 1997, 'title': 'ThiD-TenA: a gene pair fusion in eukaryotes.', 'URL': None, 'raw_pages': '708-11', 'medline_journal': 'J Mol Evol', 'ISO_journal': 'J. Mol. Evol.', 'authors': ['Ouzounis CA', 'Kyrpides NC.'], 'DOI_URL': 'http://dx.doi.org/10.1007/PL00013145'}}"	""	"{'name': 'TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 protein', 'short': 'TenA_C_ScTHI20-like'}"	""	"{'accession': '3mvu', 'name': 'Crystal structure of a TenA family transcription regulator (TM1040_3656) from SILICIBACTER SP. TM1040 at 1.80 A resolution'}"	"{'accession': 'cl38925', 'name': 'TenA_PqqC-like'}"	"cdd"	"domain"	""