{
    "accession": "MITE0000440",
    "status": "active",
    "changelog": [
        {
            "version": "1",
            "date": "2026-06-01",
            "contributors": [
                "0009-0008-8086-5325"
            ],
            "reviewers": [
                "0000-0002-4540-6501"
            ],
            "comment": "New entry."
        }
    ],
    "enzyme": {
        "name": "SlnF",
        "description": "Cytochrome P450",
        "references": [
            "doi:10.1128/AEM.06701-11"
        ],
        "auxiliaryEnzymes": [
            {
                "name": "SlnE",
                "description": "Ferridoxin protein",
                "databaseIds": {
                    "uniprot": "UPI000247F57A",
                    "genpept": "AEZ53957.1"
                }
            }
        ],
        "databaseIds": {
            "uniprot": "UPI00024E0A7A",
            "genpept": "AEZ53958.1"
        },
        "cofactors": {
            "organic": [
                "Heme"
            ],
            "inorganic": [
                "Fe"
            ]
        }
    },
    "reactions": [
        {
            "tailoring": [
                "Hydroxylation",
                "Oxidation"
            ],
            "description": "The P450 monooxygenase SlnF performs the hydroxylation at C-20 in cognate with ferredoxin SlnE",
            "reactionSMARTS": "[#6:1]-[#6:2]-[#6:3](-[#6:25](-[#6:51](-[#6:52])-[#6:50]-[#6:48](-[#6:49])-[#6:27]1-[#8:47]-[#6:31]2(-[#8:46]-[#6:34](-[#6:36]3-[#8:45]-[#6:43](-[#6:44])-[#6:39](-[#6:41]-[#6:42])(-[#8:40])-[#6:38]-[#6:37]-3)(-[#6:35])-[#6:33]-[#6:32]-2)-[#6:30]-[#6:29](-[#8:53])-[#6:28]=1)-[#8:26])-[#6:4](-[#6:6](-[#6:8](-[#6:10](-[#6:12]1-[#6:23](-[#6:24])-[#6:22]-[#6:21]-[#6:14](-[#6:15](-[#6:18](-[*])=[#8:19])-[#6:16]-[#6:17])-[#8:13]-1)-[#6:11])-[#8:9])-[#6:7])=[#8:5]>>[#6:1]-[#6:2]-[#6:3](-[#6:25](-[#6:51](-[#6:52])-[#6:50]-[#6:48](-[#6:49])-[#6:27]1-[#8:47]-[#6:31]2(-[#8:46]-[#6:34](-[#6:36]3-[#8:45]-[#6:43](-[#6:44])-[#6:39](-[#6:41]-[#6:42])(-[#8:40])-[#6:38]-[#6:37]-3)(-[#6:35])-[#6:33]-[#6:32]-2)-[#6:30](-[#8])-[#6:29](-[#8:53])-[#6:28]=1)-[#8:26])-[#6:4](-[#6:6](-[#6:8](-[#6:10](-[#6:12]1-[#6:23](-[#6:24])-[#6:22]-[#6:21]-[#6:14](-[#6:15](-[#6:18](-[*])=[#8:19])-[#6:16]-[#6:17])-[#8:13]-1)-[#6:11])-[#8:9])-[#6:7])=[#8:5]",
            "reactions": [
                {
                    "substrate": "*C(=O)C(CC)C1CCC(C)C(C(C)C(O)C(C)C(=O)C(CC)C(O)C(C)CC(C)C2=CC(O)CC3(CCC(C)(C4CCC(O)(CC)C(C)O4)O3)O2)O1",
                    "products": [
                        "*C(=O)C(CC)C1CCC(C)C(C(C)C(O)C(C)C(=O)C(CC)C(O)C(C)CC(C)C2=CC(O)C(O)C3(CCC(C)(C4CCC(O)(CC)C(C)O4)O3)O2)O1"
                    ],
                    "isIntermediate": true,
                    "description": "The final steps of salinomycin assembly involve C-20 hydroxylation by SlnE/SlnF followed by polyether chain release from the PKS by thioesterases SlnDI/SlnDII. Lastly, the methyltransferase-like enzyme SlnM catalyzes the spirocyclization-coupled dehydration of OH-19 and forms the final product salinomycin."
                }
            ],
            "evidence": {
                "evidenceCode": [
                    "Inference from genomic data and chemical structure",
                    "Knock-out studies"
                ],
                "references": [
                    "doi:10.1128/AEM.06701-11",
                    "doi:10.3390/md20060393"
                ]
            }
        }
    ]
}