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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR003190",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004068",
"name": "aspartate 1-decarboxylase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006523",
"name": "alanine biosynthetic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd06919": "Aspartate alpha-decarboxylase or L-aspartate 1-decarboxylase, a pyruvoyl group-dependent decarboxylase in beta-alanine production"
},
"hamap": {
"MF_00446": "Aspartate 1-decarboxylase [panD]"
},
"pfam": {
"PF02261": "Aspartate decarboxylase"
},
"pirsf": {
"PIRSF006246": "Aspartate 1-decarboxylase"
},
"ncbifam": {
"TIGR00223": "aspartate 1-decarboxylase"
},
"panther": {
"PTHR21012": "ASPARTATE 1-DECARBOXYLASE"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR003190",
"name": "Aspartate decarboxylase",
"type": "Family",
"children": []
},
"name": {
"name": "Aspartate decarboxylase",
"short": "Asp_decarbox"
},
"description": [
{
"text": "<p>Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalysed by the enzyme L-aspartate decarboxylase (ADC, [ec:4.1.1.11]). Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The enzyme is translated as an inactive proenzyme [[cite:PUB00070769]], and is cleaved via self-processing at Gly23-Ser24 to yield an alpha chain (C-terminal fragment) and beta chain (N-terminal fragment). This model spans the precursor (or both beta and alpha chains) of aspartate decarboxylase. A pyruvoyl cofactor, which is covalently bound to the enzyme, is required for activity. The active site of the tetrameric enzyme is located at the interface of two subunits, with a lysine and a histidine from the beta chain of one subunit forming the active site with residues from the alpha chain of the adjacent subunit [[cite:PUB00039881], [cite:PUB00031775], [cite:PUB00022472], [cite:PUB00019168], [cite:PUB00011777], [cite:PUB00079743]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00070769": {
"PMID": 9169598,
"ISBN": null,
"volume": "323 ( Pt 3)",
"issue": null,
"year": 1997,
"title": "Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry.",
"URL": null,
"raw_pages": "661-9",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem. J.",
"authors": [
"Ramjee MK",
"Genschel U",
"Abell C",
"Smith AG."
],
"DOI_URL": null
},
"PUB00039881": {
"PMID": 17001646,
"ISBN": null,
"volume": "65",
"issue": "4",
"year": 2006,
"title": "Crystal structure of uncleaved L-aspartate-alpha-decarboxylase from Mycobacterium tuberculosis.",
"URL": null,
"raw_pages": "796-802",
"medline_journal": "Proteins",
"ISO_journal": "Proteins",
"authors": [
"Gopalan G",
"Chopra S",
"Ranganathan A",
"Swaminathan K."
],
"DOI_URL": "http://dx.doi.org/10.1002/prot.21126"
},
"PUB00031775": {
"PMID": 15184017,
"ISBN": null,
"volume": "340",
"issue": "1",
"year": 2004,
"title": "Crystal structure of the schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase.",
"URL": null,
"raw_pages": "1-7",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Lee BI",
"Suh SW."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.jmb.2004.04.049"
},
"PUB00022472": {
"PMID": 14633979,
"ISBN": null,
"volume": "22",
"issue": "23",
"year": 2003,
"title": "Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase.",
"URL": null,
"raw_pages": "6193-204",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Schmitzberger F",
"Kilkenny ML",
"Lobley CM",
"Webb ME",
"Vinkovic M",
"Matak-Vinkovic D",
"Witty M",
"Chirgadze DY",
"Smith AG",
"Abell C",
"Blundell TL."
],
"DOI_URL": "http://dx.doi.org/10.1093/emboj/cdg575"
},
"PUB00019168": {
"PMID": 9546220,
"ISBN": null,
"volume": "5",
"issue": "4",
"year": 1998,
"title": "Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.",
"URL": null,
"raw_pages": "289-93",
"medline_journal": "Nat Struct Biol",
"ISO_journal": "Nat. Struct. Biol.",
"authors": [
"Albert A",
"Dhanaraj V",
"Genschel U",
"Khan G",
"Ramjee MK",
"Pulido R",
"Sibanda BL",
"von Delft F",
"Witty M",
"Blundell TL",
"Smith AG",
"Abell C."
],
"DOI_URL": "http://dx.doi.org/10.1038/nsb0498-289"
},
"PUB00011777": {
"PMID": 10368289,
"ISBN": null,
"volume": "7",
"issue": "2",
"year": 1999,
"title": "A six-stranded double-psi beta barrel is shared by several protein superfamilies.",
"URL": null,
"raw_pages": "227-36",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Castillo RM",
"Mizuguchi K",
"Dhanaraj V",
"Albert A",
"Blundell TL",
"Murzin AG."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(99)80028-8"
},
"PUB00079743": {
"PMID": 3003510,
"ISBN": null,
"volume": "113",
"issue": null,
"year": 1985,
"title": "L-Aspartate alpha-decarboxylase.",
"URL": null,
"raw_pages": "589-95",
"medline_journal": "Methods Enzymol",
"ISO_journal": "Meth. Enzymol.",
"authors": [
"Williamson JM."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0076-6879(85)13078-8"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR009010",
"name": "Aspartate decarboxylase-like domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 11,
"interactions": 0,
"matches": 14738,
"pathways": 1,
"proteins": 14737,
"proteomes": 10349,
"sets": 0,
"structural_models": {
"alphafold": 10916,
"bfvd": 0
},
"structures": 31,
"taxa": 17017
},
"entry_annotations": {
"alignment:seed": 266,
"alignment:full": 5597
},
"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": "GenProp0124",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0124"
},
{
"accession": "GenProp1601",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1601"
}
]
},
"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": "4.1.1.11",
"url": "https://enzyme.expasy.org/EC/4.1.1.11"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1pqh",
"name": "Serine 25 to Threonine mutation of aspartate decarboxylase"
}
}
}
