HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"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
}
}
