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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR004229",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0052876",
"name": "methylamine dehydrogenase (amicyanin) activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0030288",
"name": "outer membrane-bounded periplasmic space",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"ncbifam": {
"TIGR02659": "methylamine dehydrogenase (amicyanin) small subunit"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR016008",
"name": "Amine dehydrogenase light chain",
"type": "Family",
"children": [
{
"accession": "IPR004229",
"name": "Methylamine dehydrogenase light chain",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Methylamine dehydrogenase light chain",
"short": "MeN_DH_Ltc"
},
"description": [
{
"text": "<p>This family consists of the light chain (small subunit) of methylamine dehydrogenase, a periplasmic enzyme. This subunit contains a tryptophan tryptophylquinone (TTQ) prosthetic group derived from Trp-114 and Trp-165 of the precursor, numbered according to the sequence from Paracoccus denitrificans [[cite:PUB00021028], [cite:PUB00065256]]. The enzyme forms a complex with the type I blue copper protein amicyanin and cytochrome. Electron transfer proceeds from TQQ to the copper and then to the heme group of the cytochrome.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00065256": {
"PMID": 23487750,
"ISBN": null,
"volume": "110",
"issue": "12",
"year": 2013,
"title": "Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis.",
"URL": null,
"raw_pages": "4569-73",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Yukl ET",
"Liu F",
"Krzystek J",
"Shin S",
"Jensen LM",
"Davidson VL",
"Wilmot CM",
"Liu A."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.1215011110"
},
"PUB00021028": {
"PMID": 15734739,
"ISBN": null,
"volume": "280",
"issue": "17",
"year": 2005,
"title": "Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.",
"URL": null,
"raw_pages": "17392-6",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Jones LH",
"Pearson AR",
"Tang Y",
"Wilmot CM",
"Davidson VL."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M500943200"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036560",
"name": "Methylamine/Aralkylamine dehydrogenase light chain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 135,
"pathways": 1,
"proteins": 135,
"proteomes": 91,
"sets": 0,
"structural_models": {
"alphafold": 106,
"bfvd": 0
},
"structures": 42,
"taxa": 204
},
"entry_annotations": {},
"cross_references": {
"gp": {
"displayName": "Genome Properties",
"description": "Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.",
"rank": 45,
"accessions": [
{
"accession": "GenProp0860",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0860"
}
]
},
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "1.4.9.1",
"url": "https://enzyme.expasy.org/EC/1.4.9.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2bbk",
"name": "CRYSTAL STRUCTURE OF THE QUINOPROTEIN METHYLAMINE DEHYDROGENASE FROM PARACOCCUS DENITRIFICANS AT 1.75 ANGSTROMS"
}
}
}
