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{
    "metadata": {
        "accession": "IPR004372",
        "entry_id": null,
        "type": "family",
        "go_terms": [
            {
                "identifier": "GO:0016301",
                "name": "kinase activity",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            },
            {
                "identifier": "GO:0016774",
                "name": "phosphotransferase activity, carboxyl group as acceptor",
                "category": {
                    "code": "F",
                    "name": "molecular_function"
                }
            },
            {
                "identifier": "GO:0006082",
                "name": "organic acid metabolic process",
                "category": {
                    "code": "P",
                    "name": "biological_process"
                }
            }
        ],
        "source_database": "interpro",
        "member_databases": {
            "hamap": {
                "MF_00020": "Acetate kinase [ackA]"
            },
            "pirsf": {
                "PIRSF000722": "Acetate/propionate kinase"
            },
            "ncbifam": {
                "TIGR00016": "acetate/propionate family kinase"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR000890",
            "name": "Aliphatic acid kinase, short-chain",
            "type": "Family",
            "children": [
                {
                    "accession": "IPR004372",
                    "name": "Acetate/propionate kinase",
                    "type": "Family",
                    "children": [
                        {
                            "accession": "IPR024896",
                            "name": "Propionate kinase PduW",
                            "type": "Family",
                            "children": []
                        },
                        {
                            "accession": "IPR024917",
                            "name": "Propionate kinase",
                            "type": "Family",
                            "children": []
                        }
                    ]
                },
                {
                    "accession": "IPR011245",
                    "name": "Butyrate kinase",
                    "type": "Family",
                    "children": []
                }
            ]
        },
        "name": {
            "name": "Acetate/propionate kinase",
            "short": "Ac/propionate_kinase"
        },
        "description": [
            {
                "text": "<p>This entry represents proteins which transfer phosphate from ATP to a short chain aliphatic acid. For example, Acetate kinase catalyses the reaction  ATP + acetate = ADP + acetyl phosphate and propionate kinase which utilizes propionate as substrate [[cite:PUB00016056], [cite:PUB00065155]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00016056": {
                "PMID": 9484901,
                "ISBN": null,
                "volume": "27",
                "issue": "2",
                "year": 1998,
                "title": "Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate.",
                "URL": null,
                "raw_pages": "477-92",
                "medline_journal": "Mol Microbiol",
                "ISO_journal": "Mol. Microbiol.",
                "authors": [
                    "Hesslinger C",
                    "Fairhurst SA",
                    "Sawers G."
                ],
                "DOI_URL": "http://dx.doi.org/10.1046/j.1365-2958.1998.00696.x"
            },
            "PUB00065155": {
                "PMID": 23031654,
                "ISBN": null,
                "volume": "12",
                "issue": null,
                "year": 2012,
                "title": "Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface.",
                "URL": null,
                "raw_pages": "24",
                "medline_journal": "BMC Struct Biol",
                "ISO_journal": "BMC Struct. Biol.",
                "authors": [
                    "Chittori S",
                    "Savithri HS",
                    "Murthy MR."
                ],
                "DOI_URL": "http://dx.doi.org/10.1186/1472-6807-12-24"
            }
        },
        "set_info": null,
        "overlaps_with": [
            {
                "accession": "IPR043129",
                "name": "ATPase, nucleotide binding domain",
                "type": "homologous_superfamily"
            }
        ],
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 25660,
            "pathways": 7,
            "proteins": 25660,
            "proteomes": 14084,
            "sets": 0,
            "structural_models": {
                "alphafold": 20315,
                "bfvd": 0
            },
            "structures": 39,
            "taxa": 24428
        },
        "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": "GenProp1267",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1267"
                    },
                    {
                        "accession": "GenProp1749",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1749"
                    },
                    {
                        "accession": "GenProp0478",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0478"
                    },
                    {
                        "accession": "GenProp1762",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1762"
                    },
                    {
                        "accession": "GenProp0754",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0754"
                    },
                    {
                        "accession": "GenProp1345",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1345"
                    },
                    {
                        "accession": "GenProp1543",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1543"
                    }
                ]
            },
            "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": "2.7.2.1",
                        "url": "https://enzyme.expasy.org/EC/2.7.2.1"
                    }
                ]
            }
        },
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "4ijn",
            "name": "Crystal structure of an acetate kinase from Mycobacterium smegmatis bound to AMP and sulfate"
        }
    }
}