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{
"metadata": {
"accession": "IPR012302",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0051287",
"name": "NAD binding",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"smart": {
"SM00919": "Malic enzyme, NAD binding domain"
},
"pfam": {
"PF03949": "Malic enzyme, NAD binding domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR012302",
"name": "Malic enzyme, NAD-binding",
"type": "Domain",
"children": [
{
"accession": "IPR045213",
"name": "Malic enzyme, NAD-binding domain, bacterial type",
"type": "Domain",
"children": []
}
]
},
"name": {
"name": "Malic enzyme, NAD-binding",
"short": "Malic_NAD-bd"
},
"description": [
{
"text": "<p>This entry represents the NAD-binding domain of malic enzymes.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate, a reaction important in a number of metabolic pathways - e.g. carbon dioxide released from the reaction may be used in sugar production during the Calvin cycle of photosynthesis [[cite:PUB00002876]]. There are 3 forms of the enzyme [[cite:PUB00002681]]: an NAD-dependent form that decarboxylates oxaloacetate; an NAD-dependent form that does not decarboxylate oxalo-acetate; and an NADPH-dependent form [[cite:PUB00002876]]. Other proteins known to be similar to malic enzymes are the Escherichia coli scfA protein; an enzyme from Zea mays (Maize), formerly thought to be cinnamyl-alcohol dehydrogenase [[cite:PUB00004541]]; and the hypothetical Saccharomyces cerevisiae protein YKL029c.</p>\n\n<p>Studies on the duck liver malic enzyme reveals that it can be alkylated by bromopyruvate, resulting in the loss of oxidative decarboxylation and the subsequent enhancement of pyruvate reductase activity [[cite:PUB00000616]]. The alkylated form is able to bind NADPH but not L-malate, indicating impaired substrate or divalent metal ion-binding in the active site [[cite:PUB00000616]]. Sequence analysis has highlighted a cysteine residue as the point of alkylation, suggesting that it may play an important role in the activity of the enzyme [[cite:PUB00000616]], although it is absent in the sequences from some species.</p>\n\n<p>Malic enzyme is a tetramer comprised of subunits with four domains each [[cite:PUB00099681], [cite:PUB00022087], [cite:PUB00099683]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00002876": {
"PMID": 8300616,
"ISBN": null,
"volume": "269",
"issue": "4",
"year": 1994,
"title": "Cloning and analysis of the C4 photosynthetic NAD-dependent malic enzyme of amaranth mitochondria.",
"URL": null,
"raw_pages": "2827-33",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Long JJ",
"Wang JL",
"Berry JO."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/269/4/2827"
},
"PUB00002681": {
"PMID": 1993674,
"ISBN": null,
"volume": "266",
"issue": "5",
"year": 1991,
"title": "Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli.",
"URL": null,
"raw_pages": "3016-21",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Loeber G",
"Infante AA",
"Maurer-Fogy I",
"Krystek E",
"Dworkin MB."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/266/5/3016"
},
"PUB00004541": {
"PMID": 2103472,
"ISBN": null,
"volume": "15",
"issue": "3",
"year": 1990,
"title": "Extensive sequence similarity of the bean CAD4 (cinnamyl-alcohol dehydrogenase) to a maize malic enzyme.",
"URL": null,
"raw_pages": "525-6",
"medline_journal": "Plant Mol Biol",
"ISO_journal": "Plant Mol. Biol.",
"authors": [
"Walter MH",
"Grima-Pettenati J",
"Grand C",
"Boudet AM",
"Lamb CJ."
],
"DOI_URL": "http://dx.doi.org/10.1007/BF00019173"
},
"PUB00000616": {
"PMID": 1911848,
"ISBN": null,
"volume": "1079",
"issue": "3",
"year": 1991,
"title": "Duck liver malic enzyme: sequence of a tryptic peptide containing the cysteine residue labeled by the substrate analog bromopyruvate.",
"URL": null,
"raw_pages": "247-52",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Satterlee J",
"Hsu RY."
],
"DOI_URL": "http://dx.doi.org/10.1016/0167-4838(91)90065-8"
},
"PUB00022087": {
"PMID": 12033925,
"ISBN": null,
"volume": "41",
"issue": "22",
"year": 2002,
"title": "Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution.",
"URL": null,
"raw_pages": "6928-38",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Coleman DE",
"Rao GS",
"Goldsmith EJ",
"Cook PF",
"Harris BG."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi0255120"
},
"PUB00099681": {
"PMID": 10477256,
"ISBN": null,
"volume": "7",
"issue": "8",
"year": 1999,
"title": "Crystal structure of human mitochondrial NAD(P)+-dependent malic enzyme: a new class of oxidative decarboxylases.",
"URL": null,
"raw_pages": "R877-89",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Xu Y",
"Bhargava G",
"Wu H",
"Loeber G",
"Tong L."
],
"DOI_URL": null
},
"PUB00099683": {
"PMID": 1640469,
"ISBN": null,
"volume": "226",
"issue": "2",
"year": 1992,
"title": "Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum.",
"URL": null,
"raw_pages": "565-9",
"medline_journal": "J Mol Biol",
"ISO_journal": "J Mol Biol",
"authors": [
"Clancy LL",
"Rao GS",
"Finzel BC",
"Muchmore SW",
"Holland DR",
"Watenpaugh KD",
"Krishnamurthy HM",
"Sweet RM",
"Cook PF",
"Harris BG."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036291",
"name": "NAD(P)-binding domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 243,
"interactions": 0,
"matches": 52586,
"pathways": 15,
"proteins": 52515,
"proteomes": 19132,
"sets": 0,
"structural_models": {
"alphafold": 42009,
"bfvd": 0
},
"structures": 55,
"taxa": 35614
},
"entry_annotations": {
"alignment:seed": 30,
"alignment:full": 23212
},
"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": "GenProp1344",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1344"
},
{
"accession": "GenProp1722",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1722"
}
]
},
"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": "1.1.1",
"url": "https://enzyme.expasy.org/EC/1.1.1"
},
{
"accession": "1.1.1.38",
"url": "https://enzyme.expasy.org/EC/1.1.1.38"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "6zn7",
"name": "MaeB malic enzyme domain apoprotein"
}
}
}
