From 4e8db09da3b5bf5db8ab58ee8f92d8c7bce9450d Mon Sep 17 00:00:00 2001 From: mite-bot Date: Sun, 30 Aug 2026 17:53:33 +0200 Subject: [PATCH 1/2] Add submission UUID file --- .../846545fe-a48a-11f1-a881-7d5f8d37e7b5.json | 44 +++++++++++++++++++ 1 file changed, 44 insertions(+) create mode 100644 mite_data/data/846545fe-a48a-11f1-a881-7d5f8d37e7b5.json diff --git a/mite_data/data/846545fe-a48a-11f1-a881-7d5f8d37e7b5.json b/mite_data/data/846545fe-a48a-11f1-a881-7d5f8d37e7b5.json new file mode 100644 index 00000000..3f8b0a66 --- /dev/null +++ b/mite_data/data/846545fe-a48a-11f1-a881-7d5f8d37e7b5.json @@ -0,0 +1,44 @@ +{ + "accession": "MITE9999999", + "status": "pending", + "changelog": [ + { + "version": "1", + "date": "2026-08-30", + "contributors": [ + "0009-0008-8086-5325" + ], + "reviewers": [ + "BBBBBBBBBBBBBBBBBBBBBBBB" + ], + "comment": "New entry." + } + ], + "enzyme": { + "name": "AoiQ", + "databaseIds": { + "uniprot": "UPI0001F2A4ED", + "genpept": "" + }, + "references": [ + "doi:" + ] + }, + "reactions": [ + { + "evidence": { + "evidenceCode": [], + "references": [ + "doi:" + ] + }, + "reactions": [ + { + "products": [ + "" + ] + } + ] + } + ] +} \ No newline at end of file From 5de49b1aec16573c214a72fc727a379ee3e9e8b1 Mon Sep 17 00:00:00 2001 From: mite-bot Date: Sun, 30 Aug 2026 19:32:24 +0200 Subject: [PATCH 2/2] Update submission --- .../846545fe-a48a-11f1-a881-7d5f8d37e7b5.json | 90 ++++++++++++++++--- 1 file changed, 80 insertions(+), 10 deletions(-) diff --git a/mite_data/data/846545fe-a48a-11f1-a881-7d5f8d37e7b5.json b/mite_data/data/846545fe-a48a-11f1-a881-7d5f8d37e7b5.json index 3f8b0a66..943d87e8 100644 --- a/mite_data/data/846545fe-a48a-11f1-a881-7d5f8d37e7b5.json +++ b/mite_data/data/846545fe-a48a-11f1-a881-7d5f8d37e7b5.json @@ -1,6 +1,7 @@ { "accession": "MITE9999999", "status": "pending", + "comment": "AoiQ is a bifunctional methyltransferase (MT) and flavin-dependent halogenase (FDH) that catalyzes dimethylation and gem-dichlorination in the biosynthesis of 8-methyldichlorodiaporthin", "changelog": [ { "version": "1", @@ -16,29 +17,98 @@ ], "enzyme": { "name": "AoiQ", + "description": "bifunctional methyltransferase-halogenase", + "references": [ + "doi:10.1021/jacs.1c02868", + "doi:10.1002/anie.201604516" + ], "databaseIds": { "uniprot": "UPI0001F2A4ED", - "genpept": "" + "mibig": "BGC0002237" }, - "references": [ - "doi:" - ] + "cofactors": { + "organic": [ + "FAD", + "SAM" + ] + } }, "reactions": [ { + "tailoring": [ + "Halogenation", + "Methylation" + ], + "description": "AoiQ catalyzes dimethylation and gem-dichlorination of 1,3-diketone substrates to produce 8-methyldichlorodiaporthin", + "reactionSMARTS": "[#8:1]-[#6:2]1:[#6:7]:[#6:6]2:[#6:8]:[#6:9](-[#6:13]-[#6:14](=[#8])-[#6:15]-[#6](=[#8])-[#6]):[#8:10]:[#6:11](=[#8:12]):[#6:5]:2:[#6:4](-[#8:17]):[#6:3]:1>>[#8:1](-[#6])-[#6:2]1:[#6:7]:[#6:6]2:[#6:8]:[#6:9](-[#6:13]-[#6@@:14](/[#8])-[#6:15](-[Cl])-[Cl]):[#8:10]:[#6:11](=[#8:12]):[#6:5]:2:[#6:4](-[#8:17]-[#6]):[#6:3]:1", + "reactions": [ + { + "substrate": "CC(=O)CC(=O)Cc1cc2cc(O)cc(O)c2c(=O)o1", + "products": [ + "COc1cc(OC)c2c(=O)oc(C[C@@H](O)C(Cl)Cl)cc2c1" + ], + "isIntermediate": true, + "description": "AoiQ is a bifunctional enzyme, first performs an unusual geminal \u03b1,\u03b1-dichlorination of the 1,3-diketone substrate. The resulting dichlorinated intermediate undergoes nonenzymatic deacetylation, followed by C10 ketoreduction catalyzed by the SDR enzyme DiaC, or catalyzed by heterologous host endogenous ketoreductases. The resulting dichlorinated diaporthin scaffold is subsequently O-methylated by the MT domain of AoiQ to produce 8-methyldichlorodiaporthin." + } + ], "evidence": { - "evidenceCode": [], + "evidenceCode": [ + "Heterologous expression" + ], "references": [ - "doi:" + "doi:10.1021/jacs.1c02868" ] - }, + } + }, + { + "tailoring": [ + "Halogenation" + ], + "description": "AoiQ-FDH domain catalyzes dichlorination of 1,3-diketone substrate", + "reactionSMARTS": "[#8:1]-[#6:2]1:[#6:7]:[#6:6]2:[#6:8]:[#6:9](-[#6:13]-[#6:14](=[#8:16])-[#6:15]-[#6](=[#8])-[#6]):[#8:10]:[#6:11](=[#8:12]):[#6:5]:2:[#6:4](-[#8:17]):[#6:3]:1>>[#8:1]-[#6:2]1:[#6:7]:[#6:6]2:[#6:8]:[#6:9](-[#6:13]-[#6:14](=[#8:16])-[#6:15](-[Cl])-[Cl]):[#8:10]:[#6:11](=[#8:12]):[#6:5]:2:[#6:4](-[#8:17]):[#6:3]:1", "reactions": [ { + "substrate": "CC(=O)CC(=O)Cc1cc2cc(O)cc(O)c2c(=O)o1", "products": [ - "" - ] + "O=C(Cc1cc2cc(O)cc(O)c2c(=O)o1)C(Cl)Cl" + ], + "isIntermediate": true } - ] + ], + "evidence": { + "evidenceCode": [ + "Heterologous expression", + "In vitro assay" + ], + "references": [ + "doi:10.1021/jacs.1c02868" + ] + } + }, + { + "tailoring": [ + "Methylation" + ], + "description": "AoiQ-MT domain catalyzes dimethylation on dichlorinated diaporthin scaffold", + "reactionSMARTS": "[#8:1]-[#6:2]1:[#6:19]:[#6:17](-[#8:18]):[#6:16]2:[#6:4](:[#6:5]:[#6:6](:[#8:13]:[#6:14]:2=[#8:15])-[#6:7]-[#6@@:8](-[#6:10](-[Cl:12])-[Cl:11])/[#8:9]):[#6:3]:1>>[#8:1](-[#6])-[#6:2]1:[#6:19]:[#6:17](-[#8:18]-[#6]):[#6:16]2:[#6:4](:[#6:5]:[#6:6](:[#8:13]:[#6:14]:2=[#8:15])-[#6:7]-[#6@@:8](-[#6:10](-[Cl:12])-[Cl:11])/[#8:9]):[#6:3]:1", + "reactions": [ + { + "substrate": "O=c1oc(C[C@H](O)C(Cl)Cl)cc2cc(O)cc(O)c12", + "products": [ + "COc1cc(OC)c2c(=O)oc(C[C@H](O)C(Cl)Cl)cc2c1" + ], + "isIntermediate": false + } + ], + "evidence": { + "evidenceCode": [ + "Heterologous expression", + "In vitro assay" + ], + "references": [ + "doi:10.1021/jacs.1c02868" + ] + } } ] } \ No newline at end of file