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{
"metadata": {
"accession": "cd04614",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "cdd",
"member_databases": null,
"integrated": null,
"hierarchy": null,
"name": {
"name": "Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2",
"short": "CBS_pair_arch2_repeat2"
},
"description": [
{
"text": "<p>This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). [[cite:PUB00043686], [cite:PUB00005461], [cite:PUB00003445], [cite:PUB00114595], [cite:PUB00000457], [cite:PUB00114596], [cite:PUB00019266], [cite:PUB00014845]]</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00000457": {
"PMID": 10200156,
"ISBN": null,
"volume": "38",
"issue": "15",
"year": 1999,
"title": "Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.",
"URL": null,
"raw_pages": "4691-700",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Zhang R",
"Evans G",
"Rotella FJ",
"Westbrook EM",
"Beno D",
"Huberman E",
"Joachimiak A",
"Collart FR."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi982858v"
},
"PUB00005461": {
"PMID": 9020585,
"ISBN": null,
"volume": "22",
"issue": "1",
"year": 1997,
"title": "The structure of a domain common to archaebacteria and the homocystinuria disease protein.",
"URL": null,
"raw_pages": "12-3",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Bateman A."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0968-0004(96)30046-7"
},
"PUB00003445": {
"PMID": 9106071,
"ISBN": null,
"volume": "75",
"issue": "3",
"year": 1997,
"title": "CBS domains in CIC chloride channels implicated in myotonia and nephrolithiasis (kidney stones).",
"URL": null,
"raw_pages": "160-3",
"medline_journal": "J Mol Med",
"ISO_journal": "J. Mol. Med.",
"authors": [
"Ponting CP."
],
"DOI_URL": null
},
"PUB00043686": {
"PMID": 16275737,
"ISBN": null,
"volume": "289",
"issue": "6",
"year": 2005,
"title": "CBS domains: structure, function, and pathology in human proteins.",
"URL": null,
"raw_pages": "C1369-78",
"medline_journal": "Am J Physiol Cell Physiol",
"ISO_journal": "Am. J. Physiol., Cell Physiol.",
"authors": [
"Ignoul S",
"Eggermont J."
],
"DOI_URL": "http://dx.doi.org/10.1152/ajpcell.00282.2005"
},
"PUB00114595": {
"PMID": 9590298,
"ISBN": null,
"volume": "19",
"issue": "1",
"year": 1998,
"title": "Correction of disease-causing CBS mutations in yeast.",
"URL": null,
"raw_pages": "91-3",
"medline_journal": "Nat Genet",
"ISO_journal": "Nat Genet",
"authors": [
"Shan X",
"Kruger WD."
],
"DOI_URL": null
},
"PUB00014845": {
"PMID": 14722619,
"ISBN": null,
"volume": "113",
"issue": "2",
"year": 2004,
"title": "CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations.",
"URL": null,
"raw_pages": "274-84",
"medline_journal": "J Clin Invest",
"ISO_journal": "J. Clin. Invest.",
"authors": [
"Scott JW",
"Hawley SA",
"Green KA",
"Anis M",
"Stewart G",
"Scullion GA",
"Norman DG",
"Hardie DG."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=14722619&action=stream&blobtype=pdf"
},
"PUB00114596": {
"PMID": 11230183,
"ISBN": null,
"volume": "10",
"issue": "6",
"year": 2001,
"title": "Mutations in the regulatory domain of cystathionine beta synthase can functionally suppress patient-derived mutations in cis.",
"URL": null,
"raw_pages": "635-43",
"medline_journal": "Hum Mol Genet",
"ISO_journal": "Hum Mol Genet",
"authors": [
"Shan X",
"Dunbrack RL Jr",
"Christopher SA",
"Kruger WD."
],
"DOI_URL": null
},
"PUB00019266": {
"PMID": 11524006,
"ISBN": null,
"volume": "40",
"issue": "35",
"year": 2001,
"title": "Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region.",
"URL": null,
"raw_pages": "10625-33",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Janosik M",
"Kery V",
"Gaustadnes M",
"Maclean KN",
"Kraus JP."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi010711p"
}
},
"set_info": {
"accession": "cl15354",
"name": "CBS_pair_SF"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 433,
"pathways": 0,
"proteins": 433,
"proteomes": 344,
"sets": 1,
"structural_models": {
"alphafold": 415,
"bfvd": 0
},
"structures": 1,
"taxa": 658
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2yzq",
"name": "Crystal structure of uncharacterized conserved protein from Pyrococcus horikoshii"
}
}
}
