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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR015340",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0005509",
"name": "calcium ion binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0016052",
"name": "carbohydrate catabolic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF09260": "Alpha-amylase, domain C"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR015340",
"name": "Alpha-amylase, C domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Alpha-amylase, C domain",
"short": "A_amylase_C_dom"
},
"description": [
{
"text": "<p>This domain is found at the C-terminal of various fungal alpha-amylase proteins. It has been identified as a secondary binding site, which might be part of a starch interaction site [[cite:PUB00097489], [cite:PUB00097488]]. It has a β-sandwich fold comprising an antiparallel β-sheet with eight strands.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Alpha-amylase is classified as family 13 ([cazy:GH13]) of the glycosyl hydrolases and is present in archaea, bacteria, fungi, plants and animals. Alpha-amylase is an essential enzyme in alpha-glucan metabolism, acting to catalyse the hydrolysis of alpha-1,4-glucosidic bonds of glycogen, starch and related polysaccharides. Although all alpha-amylases possess the same catalytic function, they can vary with respect to sequence. In general, they are composed of three domains: a TIM barrel containing the active site residues and chloride ion-binding site (domain A), a long loop region inserted between the third β-strand and the α-helix of domain A that contains calcium-binding site(s) (domain B), and a C-terminal β-sheet domain that appears to show some variability in sequence and length between amylases (domain C) [[cite:PUB00027666]]. Amylases have at least one conserved calcium-binding site, as calcium is essential for the stability of the enzyme. The chloride-binding functions to activate the enzyme, which acts by a two-step mechanism involving a catalytic nucleophile base (usually an Asp) and a catalytic proton donor (usually a Glu) that are responsible for the formation of the beta-linked glycosyl-enzyme intermediate.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00027666": {
"PMID": 11141191,
"ISBN": null,
"volume": "18",
"issue": "1",
"year": 2001,
"title": "Evolution of alpha-amylases: architectural features and key residues in the stabilization of the (beta/alpha)(8) scaffold.",
"URL": null,
"raw_pages": "38-54",
"medline_journal": "Mol Biol Evol",
"ISO_journal": "Mol. Biol. Evol.",
"authors": [
"Pujadas G",
"Palau J."
],
"DOI_URL": "http://mbe.oxfordjournals.org/cgi/content/abstract/18/1/38.pdf"
},
"PUB00097489": {
"PMID": 31623309,
"ISBN": null,
"volume": "20",
"issue": "19",
"year": 2019,
"title": "Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance.",
"URL": null,
"raw_pages": null,
"medline_journal": "Int J Mol Sci",
"ISO_journal": "Int J Mol Sci",
"authors": [
"Roth C",
"Moroz OV",
"Turkenburg JP",
"Blagova E",
"Waterman J",
"Ariza A",
"Ming L",
"Tianqi S",
"Andersen C",
"Davies GJ",
"Wilson KS."
],
"DOI_URL": null
},
"PUB00097488": {
"PMID": 23536251,
"ISBN": null,
"volume": "170",
"issue": "2",
"year": 2013,
"title": "A novel multifunctional α-amylase from the thermophilic fungus Malbranchea cinnamomea: biochemical characterization and three-dimensional structure.",
"URL": null,
"raw_pages": "420-35",
"medline_journal": "Appl Biochem Biotechnol",
"ISO_journal": "Appl Biochem Biotechnol",
"authors": [
"Han P",
"Zhou P",
"Hu S",
"Yang S",
"Yan Q",
"Jiang Z."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR013780",
"name": "Glycosyl hydrolase, all-beta",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 38,
"interactions": 0,
"matches": 2577,
"pathways": 0,
"proteins": 2576,
"proteomes": 807,
"sets": 0,
"structural_models": {
"alphafold": 2253,
"bfvd": 0
},
"structures": 20,
"taxa": 1907
},
"entry_annotations": {
"alignment:seed": 20,
"alignment:full": 1707
},
"cross_references": {
"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": "3.2.1.1",
"url": "https://enzyme.expasy.org/EC/3.2.1.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
