{"metadata":{"accession":"IPR002708","entry_id":null,"type":"domain","go_terms":null,"source_database":"interpro","member_databases":{"pfam":{"PF01837":"Homocysteine biosynthesis enzyme, sulfur-incorporation"}},"integrated":null,"hierarchy":{"accession":"IPR002708","name":"Homocysteine biosynthesis enzyme, sulfur-incorporation","type":"Domain","children":[]},"name":{"name":"Homocysteine biosynthesis enzyme, sulfur-incorporation","short":"HcyBio"},"description":[{"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}],"wikipedia":null,"literature":{"PUB00078766":{"PMID":25315403,"ISBN":null,"volume":"94","issue":"6","year":2014,"title":"Novel proteins for homocysteine biosynthesis in anaerobic microorganisms.","URL":null,"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":null,"volume":"54","issue":"20","year":2015,"title":"Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen sulfide in methanogenic archaea.","URL":null,"raw_pages":"3129-32","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Allen KD","Miller DV","Rauch BJ","Perona JJ","White RH."],"DOI_URL":null},"PUB00158972":{"PMID":30932481,"ISBN":null,"volume":"58","issue":"15","year":2019,"title":"Identification of an Enzyme Catalyzing the Conversion of Sulfoacetaldehyde to 2-Mercaptoethanesulfonic Acid in Methanogens.","URL":null,"raw_pages":"1958-1962","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["White RH."],"DOI_URL":"https://doi.org/10.1021/acs.biochem.9b00176"}},"set_info":null,"overlaps_with":null,"counters":{"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},"entry_annotations":{"alignment:seed":76,"alignment:full":544},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}