{"metadata":{"accession":"PF01837","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR002708","hierarchy":null,"name":{"name":"Homocysteine biosynthesis enzyme, sulfur-incorporation","short":"HcyBio"},"description":[{"text":"<p>This presumed domain 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]]. 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]]. 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}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":8,"interactions":0,"matches":827,"pathways":0,"proteins":825,"proteomes":684,"sets":0,"structural_models":{"alphafold":656},"structures":0,"taxa":1663},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":76,"alignment:full":544},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}