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{
    "metadata": {
        "accession": "PF07837",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "pfam",
        "member_databases": null,
        "integrated": "IPR012886",
        "hierarchy": null,
        "name": {
            "name": "Formiminotransferase domain, N-terminal subdomain",
            "short": "FTCD_N"
        },
        "description": [
            {
                "text": "<p>The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This,  in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a  short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to  form a number of contacts with residues found in both the N-terminal and C-terminal subdomains [[cite:PUB00007432]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": [
            {
                "title": "Glutamate_formimidoyltransferase",
                "extract": "<p><b>Glutamate formimidoyltransferase</b> is a methyltransferase enzyme which uses tetrahydrofolate as part of histidine catabolism. It catalyses two reactions. In the first, N-formimidoyl-L-glutamate transfers its formimidoyl group to tetrahydrofolate.\n</p>\n",
                "thumbnail": null
            }
        ],
        "literature": {
            "PUB00007432": {
                "PMID": 10673422,
                "ISBN": null,
                "volume": "8",
                "issue": "1",
                "year": 2000,
                "title": "The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.",
                "URL": null,
                "raw_pages": "35-46",
                "medline_journal": "Structure",
                "ISO_journal": "Structure",
                "authors": [
                    "Kohls D",
                    "Sulea T",
                    "Purisima EO",
                    "MacKenzie RE",
                    "Vrielink A."
                ],
                "DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(00)00078-2"
            }
        },
        "set_info": null,
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 48,
            "interactions": 0,
            "matches": 5248,
            "pathways": 0,
            "proteins": 5179,
            "proteomes": 2204,
            "sets": 0,
            "structural_models": {
                "alphafold": 4594,
                "bfvd": 0
            },
            "structures": 3,
            "taxa": 6672
        },
        "entry_annotations": {
            "hmm": 0,
            "logo": 0,
            "alignment:seed": 114,
            "alignment:full": 3022
        },
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "1qd1",
            "name": "THE CRYSTAL STRUCTURE OF THE FORMIMINOTRANSFERASE DOMAIN OF FORMIMINOTRANSFERASE-CYCLODEAMINASE."
        }
    }
}