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{
    "metadata": {
        "accession": "IPR049023",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "interpro",
        "member_databases": {
            "pfam": {
                "PF21405": "Phosphoacetylglucosamine mutase AMG1, domain II"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR049023",
            "name": "Phosphoacetylglucosamine mutase AMG1, domain II",
            "type": "Domain",
            "children": []
        },
        "name": {
            "name": "Phosphoacetylglucosamine mutase AMG1, domain II",
            "short": "AMG1_II"
        },
        "description": [
            {
                "text": "<p>Phosphoacetylglucosamine mutase (AMG1) catalyses the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc. It consists of four domains, the first three have the same fold of four β-strands between two α-helices.</p>\n\n<p>This entry represents domain II of eukaryotic AMG1, which contains the metal-binding loop [[cite:PUB00040263], [cite:PUB00151789]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00040263": {
                "PMID": 16651269,
                "ISBN": null,
                "volume": "281",
                "issue": "28",
                "year": 2006,
                "title": "Crystal structures of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, and its substrate and product complexes.",
                "URL": null,
                "raw_pages": "19740-7",
                "medline_journal": "J Biol Chem",
                "ISO_journal": "J. Biol. Chem.",
                "authors": [
                    "Nishitani Y",
                    "Maruyama D",
                    "Nonaka T",
                    "Kita A",
                    "Fukami TA",
                    "Mio T",
                    "Yamada-Okabe H",
                    "Yamada-Okabe T",
                    "Miki K."
                ],
                "DOI_URL": "http://dx.doi.org/10.1074/jbc.M600801200"
            },
            "PUB00151789": {
                "PMID": 29967067,
                "ISBN": null,
                "volume": "475",
                "issue": "15",
                "year": 2018,
                "title": "Evidence for substrate-assisted catalysis in <i>N</i>-acetylphosphoglucosamine mutase.",
                "URL": null,
                "raw_pages": "2547-2557",
                "medline_journal": "Biochem J",
                "ISO_journal": "Biochem J",
                "authors": [
                    "Raimi OG",
                    "Hurtado-Guerrero R",
                    "van Aalten DMF."
                ],
                "DOI_URL": null
            }
        },
        "set_info": null,
        "overlaps_with": [
            {
                "accession": "IPR016055",
                "name": "Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III",
                "type": "homologous_superfamily"
            }
        ],
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 71,
            "interactions": 0,
            "matches": 4316,
            "pathways": 7,
            "proteins": 4315,
            "proteomes": 2924,
            "sets": 0,
            "structural_models": {
                "alphafold": 3883,
                "bfvd": 0
            },
            "structures": 6,
            "taxa": 8253
        },
        "entry_annotations": {
            "alignment:seed": 1,
            "alignment:full": 2923
        },
        "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": "5.4.2.3",
                        "url": "https://enzyme.expasy.org/EC/5.4.2.3"
                    }
                ]
            }
        },
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}