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{
    "metadata": {
        "accession": "IPR013346",
        "entry_id": null,
        "type": "domain",
        "go_terms": null,
        "source_database": "interpro",
        "member_databases": {
            "prosite": {
                "PS00089": "Ribonucleotide reductase large subunit signature"
            },
            "ncbifam": {
                "TIGR02506": "ribonucleoside-diphosphate reductase subunit alpha"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR000788",
            "name": "Ribonucleotide reductase large subunit, C-terminal",
            "type": "Domain",
            "children": [
                {
                    "accession": "IPR013346",
                    "name": "Ribonucleotide reductase, class I, alpha subunit, C-terminal",
                    "type": "Domain",
                    "children": []
                }
            ]
        },
        "name": {
            "name": "Ribonucleotide reductase, class I, alpha subunit, C-terminal",
            "short": "NrdE_NrdA_C"
        },
        "description": [
            {
                "text": "<p>This entry represents the C-terminal region of the alpha (large) chain of the class I ribonucleotide reductase (RNR). RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. Class I RNR's generate the required radical (on tyrosine) via a \"non-heme\" iron cofactor which resides in the beta (small) subunit. The alpha subunit contains the catalytic and allosteric regulatory sites. The mechanism of this enzyme requires molecular oxygen [[cite:PUB00020744]]. Escherichia coli contains two versions of this enzyme which are regulated independently (NrdAB and NrdEF, where NrdA and NrdE are the large chains [[cite:PUB00005954], [cite:PUB00020990]]). Most organisms contain only one, but the application of the gene symbols NrdA and NrdE are somewhat arbitrary. Members of this group are found in diverse clades of bacteria, eukaryotes as well as numerous DNA viruses and phage.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00020744": {
                "PMID": 11807048,
                "ISBN": null,
                "volume": "184",
                "issue": "4",
                "year": 2002,
                "title": "Aerobic-type ribonucleotide reductase in the anaerobe Bacteroides fragilis.",
                "URL": null,
                "raw_pages": "895-903",
                "medline_journal": "J Bacteriol",
                "ISO_journal": "J. Bacteriol.",
                "authors": [
                    "Smalley D",
                    "Rocha ER",
                    "Smith CJ."
                ],
                "DOI_URL": "http://dx.doi.org/10.1128/jb.184.4.895-903.2002"
            },
            "PUB00005954": {
                "PMID": 8052308,
                "ISBN": null,
                "volume": "370",
                "issue": "6490",
                "year": 1994,
                "title": "Structure of ribonucleotide reductase protein R1.",
                "URL": null,
                "raw_pages": "533-9",
                "medline_journal": "Nature",
                "ISO_journal": "Nature",
                "authors": [
                    "Uhlin U",
                    "Eklund H."
                ],
                "DOI_URL": "http://dx.doi.org/10.1038/370533a0"
            },
            "PUB00020990": {
                "PMID": 8820648,
                "ISBN": null,
                "volume": "19",
                "issue": "4",
                "year": 1996,
                "title": "Promoter identification and expression analysis of Salmonella typhimurium and Escherichia coli nrdEF operons encoding one of two class I ribonucleotide reductases present in both bacteria.",
                "URL": null,
                "raw_pages": "777-90",
                "medline_journal": "Mol Microbiol",
                "ISO_journal": "Mol. Microbiol.",
                "authors": [
                    "Jordan A",
                    "Aragall E",
                    "Gibert I",
                    "Barbe J."
                ],
                "DOI_URL": "http://dx.doi.org/10.1046/j.1365-2958.1996.424950.x"
            }
        },
        "set_info": null,
        "overlaps_with": null,
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 30479,
            "pathways": 20,
            "proteins": 30309,
            "proteomes": 16535,
            "sets": 0,
            "structural_models": {
                "alphafold": 22262,
                "bfvd": 27
            },
            "structures": 129,
            "taxa": 32623
        },
        "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": "GenProp1191",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1191"
                    },
                    {
                        "accession": "GenProp0289",
                        "url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0289"
                    }
                ]
            },
            "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": "1.17.4.1",
                        "url": "https://enzyme.expasy.org/EC/1.17.4.1"
                    }
                ]
            }
        },
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "6l3r",
            "name": "Crystal structure of Ribonucleotide reductase R1 subunit, RRM1 in complex with 4-bromo-N-((1S,2R)-2-(naphthalen-1-yl)-1-(5-oxo-4,5-dihydro-1,3,4-oxadiazol-2-yl)propyl)benzenesulfonamide"
        }
    }
}