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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR019362",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0009235",
"name": "cobalamin metabolic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF10229": "Methylmalonic aciduria and homocystinuria type D protein"
},
"panther": {
"PTHR13192": "MY011 PROTEIN"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR019362",
"name": "Methylmalonic aciduria and homocystinuria type D protein",
"type": "Family",
"children": []
},
"name": {
"name": "Methylmalonic aciduria and homocystinuria type D protein",
"short": "MMADHC"
},
"description": [
{
"text": "<p>This entry represents methylmalonic aciduria and homocystinuria type D protein (also known as cobalamin trafficking protein CblD) and homologues. These proteins are involved in cobalamin (vitamin B12) metabolism and trafficking [[cite:PUB00059225], [cite:PUB00094236], [cite:PUB00094234], [cite:PUB00094235]] CblD plays a role in regulating the biosynthesis and the proportion of two coenzymes, methylcob(III)alamin (MeCbl) and 5'-deoxyadenosylcobalamin (AdoCbl) [[cite:PUB00059225], [cite:PUB00094236], [cite:PUB00094234]]. It also promotes the oxidation of cob(II)alamin bound to MMACHC [[cite:PUB00094235]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00059225": {
"PMID": 18385497,
"ISBN": null,
"volume": "358",
"issue": "14",
"year": 2008,
"title": "Gene identification for the cblD defect of vitamin B12 metabolism.",
"URL": null,
"raw_pages": "1454-64",
"medline_journal": "N Engl J Med",
"ISO_journal": "N. Engl. J. Med.",
"authors": [
"Coelho D",
"Suormala T",
"Stucki M",
"Lerner-Ellis JP",
"Rosenblatt DS",
"Newbold RF",
"Baumgartner MR",
"Fowler B."
],
"DOI_URL": "http://dx.doi.org/10.1056/NEJMoa072200"
},
"PUB00094235": {
"PMID": 26364851,
"ISBN": null,
"volume": "290",
"issue": "49",
"year": 2015,
"title": "Structure of Human B12 Trafficking Protein CblD Reveals Molecular Mimicry and Identifies a New Subfamily of Nitro-FMN Reductases.",
"URL": null,
"raw_pages": "29155-66",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Yamada K",
"Gherasim C",
"Banerjee R",
"Koutmos M."
],
"DOI_URL": null
},
"PUB00094234": {
"PMID": 24722857,
"ISBN": null,
"volume": "37",
"issue": "5",
"year": 2014,
"title": "Characterization of functional domains of the cblD (MMADHC) gene product.",
"URL": null,
"raw_pages": "841-9",
"medline_journal": "J Inherit Metab Dis",
"ISO_journal": "J. Inherit. Metab. Dis.",
"authors": [
"Jusufi J",
"Suormala T",
"Burda P",
"Fowler B",
"Froese DS",
"Baumgartner MR."
],
"DOI_URL": null
},
"PUB00094236": {
"PMID": 23415655,
"ISBN": null,
"volume": "95",
"issue": "5",
"year": 2013,
"title": "The C-terminal domain of CblD interacts with CblC and influences intracellular cobalamin partitioning.",
"URL": null,
"raw_pages": "1023-32",
"medline_journal": "Biochimie",
"ISO_journal": "Biochimie",
"authors": [
"Gherasim C",
"Hannibal L",
"Rajagopalan D",
"Jacobsen DW",
"Banerjee R."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 47,
"interactions": 0,
"matches": 2501,
"pathways": 5,
"proteins": 2424,
"proteomes": 1437,
"sets": 0,
"structural_models": {
"alphafold": 2205,
"bfvd": 0
},
"structures": 4,
"taxa": 4901
},
"entry_annotations": {
"alignment:seed": 17,
"alignment:full": 1749
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "5cv0",
"name": "Crystal structure of N-terminal truncated human B12-chaperone CblD (108-296)"
}
}
}
