General Handler

HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept

{
    "metadata": {
        "accession": "IPR038583",
        "entry_id": null,
        "type": "homologous_superfamily",
        "go_terms": null,
        "source_database": "interpro",
        "member_databases": {
            "cathgene3d": {
                "G3DSA:3.40.50.10940": "G3DSA:3.40.50.10940"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR038583",
            "name": "L-arabinose isomerase, N-terminal domain superfamily",
            "type": "Homologous_superfamily",
            "children": []
        },
        "name": {
            "name": "L-arabinose isomerase, N-terminal domain superfamily",
            "short": "AraA_N_sf"
        },
        "description": [
            {
                "text": "<p>This entry includes L-arabinose isomerases, AraA, ([ec:5.3.1.4]). These enzymes catalyse the reaction: L-arabinose => L-ribulose. This reaction is the first step in the pathway of L-arabinose utilisation as a carbon source after entering the cell L-arabinose is converted into L-ribulose by the L-arabinose isomerases enzyme [[cite:PUB00039308], [cite:PUB00008241]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00008241": {
                "PMID": 9084180,
                "ISBN": null,
                "volume": "143 ( Pt 3)",
                "issue": null,
                "year": 1997,
                "title": "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression.",
                "URL": null,
                "raw_pages": "957-69",
                "medline_journal": "Microbiology",
                "ISO_journal": "Microbiology (Reading, Engl.)",
                "authors": [
                    "Sa-Nogueira I",
                    "Nogueira TV",
                    "Soares S",
                    "de Lencastre H."
                ],
                "DOI_URL": null
            },
            "PUB00039308": {
                "PMID": 16756997,
                "ISBN": null,
                "volume": "360",
                "issue": "2",
                "year": 2006,
                "title": "Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production.",
                "URL": null,
                "raw_pages": "297-309",
                "medline_journal": "J Mol Biol",
                "ISO_journal": "J. Mol. Biol.",
                "authors": [
                    "Manjasetty BA",
                    "Chance MR."
                ],
                "DOI_URL": "http://dx.doi.org/10.1016/j.jmb.2006.04.040"
            }
        },
        "set_info": null,
        "overlaps_with": [
            {
                "accession": "IPR009015",
                "name": "L-fucose isomerase, N-terminal/central domain superfamily",
                "type": "homologous_superfamily"
            },
            {
                "accession": "IPR003762",
                "name": "L-arabinose isomerase",
                "type": "family"
            },
            {
                "accession": "IPR055389",
                "name": "L-arabinose isomerase, N-terminal domain",
                "type": "domain"
            }
        ],
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 7387,
            "pathways": 0,
            "proteins": 7383,
            "proteomes": 4395,
            "sets": 0,
            "structural_models": {
                "alphafold": 5521,
                "bfvd": 0
            },
            "structures": 13,
            "taxa": 7302
        },
        "entry_annotations": {},
        "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": "5.3.1.4",
                        "url": "https://enzyme.expasy.org/EC/5.3.1.4"
                    }
                ]
            }
        },
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}