"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"
"IPR002708"	"{'subfamilies': 0, 'domain_architectures': 9, 'interactions': 0, 'matches': 1326, 'pathways': 0, 'proteins': 1324, 'proteomes': 663, 'sets': 0, 'structural_models': {'alphafold': 1169, 'bfvd': 0}, 'structures': 0, 'taxa': 1995}"	"{}"	"[{'text': ""<p>This presumed domain (used to be named as DUF39) is about is about 360 residues long. The function of this domain is not clear. It is found at N terminus in some proteins that have two C-terminal cystathionine beta-synthase (CBS) domains, such as MJ0100 from Methanocaldococcus jannaschii. This domain can also be found in proteins that contain two C-terminal inserted Fe4S domains [[cite:PUB00093781]].</p>\n\n<p>In Methanocaldococcus jannaschii, MJ0100 and its ortholog MA1821 from Methanosarcina acetivorans are involved in Hcy (homocysteine) biosynthesis. MJ0100 CBS domains bind S-adenosyl-l-methionine (SAM) and 5'-methylthioadenosine (MTA), which induce a conformational change consistent with regulatory function. Another protein in the homocysteine biosynthesis pathway, MJ0099 and its ortholog MA1822, is involved in the reduction of the disulfide formed in MJ0100/MA1821 during the conversion of Asa (aspartate semialdehyde) to Hcy [[cite:PUB00078766], [cite:PUB00093781]].</p>\n\n<p>The DUF39-CBS and DUF39-ferredoxin architectures repeatedly occur together in the genomes of methanogenic Archaea, suggesting they may be of diverged function. This is consistent with a phylogenetic reconstruction of the DUF39 family, which clearly distinguishes the CBS-associated and ferredoxin-associated DUF39s [[cite:PUB00078766]].</p>"", 'llm': False, 'checked': False, 'updated': False}]"	""	""	"{'accession': 'IPR002708', 'name': 'Homocysteine biosynthesis enzyme, sulfur-incorporation', 'type': 'Domain', 'children': []}"	""	False	False	False	"{'PUB00078766': {'PMID': 25315403, 'ISBN': None, 'volume': '94', 'issue': '6', 'year': 2014, 'title': 'Novel proteins for homocysteine biosynthesis in anaerobic microorganisms.', 'URL': None, 'raw_pages': '1330-42', 'medline_journal': 'Mol Microbiol', 'ISO_journal': 'Mol. Microbiol.', 'authors': ['Rauch BJ', 'Gustafson A', 'Perona JJ.'], 'DOI_URL': 'http://dx.doi.org/10.1111/mmi.12832'}, 'PUB00093781': {'PMID': 25938369, 'ISBN': None, 'volume': '54', 'issue': '20', 'year': 2015, 'title': 'Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea.', 'URL': None, 'raw_pages': '3129-32', 'medline_journal': 'Biochemistry', 'ISO_journal': 'Biochemistry', 'authors': ['Allen KD', 'Miller DV', 'Rauch BJ', 'Perona JJ', 'White RH.'], 'DOI_URL': None}, 'PUB00158972': {'PMID': 30932481, 'ISBN': None, 'volume': '58', 'issue': '15', 'year': 2019, 'title': 'Identification of an Enzyme Catalyzing the Conversion of Sulfoacetaldehyde to 2-Mercaptoethanesulfonic Acid in Methanogens.', 'URL': None, 'raw_pages': '1958-1962', 'medline_journal': 'Biochemistry', 'ISO_journal': 'Biochemistry', 'authors': ['White RH.'], 'DOI_URL': 'https://doi.org/10.1021/acs.biochem.9b00176'}}"	"{'pfam': {'PF01837': 'Homocysteine biosynthesis enzyme, sulfur-incorporation'}}"	"{'name': 'Homocysteine biosynthesis enzyme, sulfur-incorporation', 'short': 'HcyBio'}"	""	""	""	"interpro"	"domain"	""