Automated artifact update

mite_data/fasta/MITE0000463.fasta

@@ -0,0 +1,10 @@
+>MITE0000463 A8W2Z0
+MNKPIKNIVIVGGGTAGWMAASYLVRALQQQANITLIESAAIPRIGVGEATIPSLQKVFF
+DFLGIPEREWMPQVNGAFKAAIKFVNWRKSPDHSRDDHFYHLFGNVPNCDGVPLTHYWLR
+KREQGFRQPMEYACYPQPGALDGKLAPCLADGTRQMSHAWHFDAHLVADFLKRWAVERGV
+NRVVDEVVEVRLNDRGYISTLLTKEGRTLEADLFIDCSGMRGLLINQALKEPFIDMSDYL
+LCDSAVASAVPNDDAREGVEPYTSAIAMNSGWTWKIPMLGRFGSGYVFSSKFTSRDQATA
+DFLNLWGLSDNQPLNQIKFRVGRNKRAWVNNCVSIGLSSCFLEPLESTGIYFIYAALYQL
+VKHFPDTSFDPRLSDAFNAEIVHMFDDCRDFVQAHYFTASREDTPFWLANRHELRLSDAI
+KEKVQRYKAGLPLTTTSFDDSTYYETFDYEFKNFWLNGNYYCIFAGLGMLPDRSLPLLQH
+RPESIEKAEAMFASIQREAERLRTSLPTNYDYLRSLRDGDAGLSRSQPGPTLAAREIL

mite_data/metadata/artifact_metadata.json

@@ -1,9 +1,9 @@
 {
   "version": "1.30",
-  "hash_mite_prot_acc": "fc0cc4607d5a27865fc3b4744d76c4c86b5bdbd250a9c30bda4c32dc1b357548",
-  "hash_general_summary": "f253648f32b8934d54d6e2c2af4815c421546b212e733387614f430aa782092d",
-  "summary": "5a230e263cb6773438555dcc2536df5b684e5ad357fa87bbc8865f7827c72b42",
-  "hash_mibig_summary": "e719547c42d9df4e4800c60d3cdcf211f9af9d925e9c8ebecc426d1f5f5d082f",
-  "smarts": "99366640461a6393edcf2e65d8da1cdf45a72eb3fd32e1118398c7a3311ce141",
-  "smiles": "3a893a4ed2812d7b5292f4ea1abd7ca3f288ed50dd8f4e737e43b01813ccdb78"
+  "hash_mite_prot_acc": "3fdca0a4ca423d0e022cd77b9fdf02869518eb496eec40e6930671e07261c16b",
+  "hash_general_summary": "78be176d13c6be982f667ae7e1eb107eda457a12757d8e2f49a72f4831c4b9b7",
+  "summary": "3661997d05f916c0c74a54afc1649f577d84daa1d7921469a17348468fe801e7",
+  "hash_mibig_summary": "1445d39956a63de0b79c62020af186681c49601eb56c2af7cacc7942b0d729b2",
+  "smarts": "7cc98d590d1ecd932d220241f42a330a3dbc7c95e053c9322cad45c21208e0f2",
+  "smiles": "32d7a2c1599211e20fc06576715c9a05fae67c94aeb08a74d5a2f9016da6ab37"
 }

mite_data/metadata/dump_smiles.csv

@@ -615,3 +615,4 @@
 613,MITE0000461.reaction1.example1,CC[C@H]1OC(=O)[C@H](C)C(=O)[C@H](C)[C@@H](O[C@@H]2O[C@H](C)C[C@H](N(C)C)[C@H]2O)[C@@H](C)C[C@@H](C)C(=O)C=C[C@H]1C,CC[C@H]1OC(=O)[C@H](C)C(=O)[C@H](C)[C@@H](O[C@@H]2O[C@H](C)C[C@H](N(C)C)[C@H]2O)[C@@H](C)C[C@@H](C)C(=O)C=C[C@]1(C)O
 614,MITE0000461.reaction2.example1,CC[C@H]1OC(=O)[C@H](C)[C@@H](O[C@@H]2O[C@H](C)C[C@H](N(C)C)[C@H]2O)[C@@H](C)C[C@@H](C)C(=O)C=C[C@H]1C,CC[C@H]1OC(=O)[C@H](C)[C@@H](O[C@@H]2O[C@H](C)C[C@H](N(C)C)[C@H]2O)[C@@H](C)C[C@@H](C)C(=O)C=C[C@]1(C)O
 615,MITE0000462.reaction1.example1,C[N+](C)(C)[C@@H](Cc1c[nH]cn1)C(=O)O.N[C@@H](CCC(=O)N[C@@H](CS)C(=O)O)C(=O)O,C[N+](C)(C)[C@@H](Cc1c[nH]c(S(=O)C[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O)n1)C(=O)O
+616,MITE0000463.reaction1.example1,[NH3+][C@H](Cc1c[nH]c2ccccc12)C(=O)[O-],[NH3+][C@H](Cc1c[nH]c2c(Cl)cccc12)C(=O)[O-]

mite_data/metadata/metadata_general.json

@@ -9925,6 +9925,28 @@
       "reaction_description":"Iron-dependent sulfoxidation of trimethylhistidine.",
       "status":"active",
       "tailoring":"Oxidation"
+    },
+    "MITE0000463":{
+      "accession":"MITE0000463",
+      "class_name":"Gammaproteobacteria",
+      "cofactors_inorganic":"N/A",
+      "cofactors_organic":"FAD",
+      "domain":"Bacteria",
+      "enzyme_description":"Tryptophan 7-halogenase",
+      "enzyme_ids":{
+        "genpept":"ABW69174.1",
+        "mibig":"BGC0000924",
+        "uniprot":"A8W2Z0"
+      },
+      "enzyme_name":"PrnA",
+      "family":"Pseudomonadaceae",
+      "kingdom":"Pseudomonadati",
+      "order":"Pseudomonadales",
+      "organism":"Pseudomonas chlororaphis",
+      "phylum":"Pseudomonadota",
+      "reaction_description":"Chlorination of tryptophan at C7 position to yield 7-chloro-L-tryptophan in pyrrolnitrin biosynthesis",
+      "status":"active",
+      "tailoring":"Halogenation"
     }
   },
   "version_mite_data":"1.30"

mite_data/metadata/metadata_mibig.json

@@ -2432,6 +2432,22 @@
         "mite_accession":"MITE0000452",
         "mite_url":"https://bioregistry.io/mite:MITE0000452",
         "status":"active"
+      },
+      {
+        "enzyme_description":"Tryptophan 7-halogenase",
+        "enzyme_ids":{
+          "genpept":"ABW69174.1",
+          "mibig":"BGC0000924",
+          "uniprot":"A8W2Z0"
+        },
+        "enzyme_name":"PrnA",
+        "enzyme_refs":[
+          "doi:10.1126/science.1116510"
+        ],
+        "enzyme_tailoring":"Halogenation",
+        "mite_accession":"MITE0000463",
+        "mite_url":"https://bioregistry.io/mite:MITE0000463",
+        "status":"active"
       }
     ],
     "BGC0000932":[

mite_data/metadata/mite_prot_accessions.csv

@@ -447,3 +447,4 @@ MITE0000459,active,AIG62145.1,A0A075TMP8
 MITE0000460,active,CAJ20005.1,Q1EMV9
 MITE0000461,active,AAC64105.1,O87605
 MITE0000462,active,EHI13262.1,G7CFI3
+MITE0000463,active,ABW69174.1,A8W2Z0

mite_data/metadata/summary.csv

@@ -461,3 +461,4 @@ MITE0000459,active,PatI,Cytochrome P450,Hydroxylation,"Hydroxylation of m-hydrox
 MITE0000460,active,FlB,Purine nucleoside phosphorylase,Other,"Phosphate-dependent purine nucleoside phosphorylase that catalyzes the reversible phosphorolysis of 5′-fluoro-5′-deoxyadenosine (5′-FDA), yielding adenine and a fluorinated sugar phosphate. This reaction constitutes a key step in microbial organofluorine biosynthesis, channeling fluorinated intermediates toward fluoroacetate and 4-fluorothreonine production. Gene inactivation abolishes downstream fluorometabolite formation, supporting its essential role in pathway flux.",N/A,N/A,Streptantibioticus cattleyicolor,Bacteria,Bacillati,Actinomycetota,Actinomycetes,Kitasatosporales,Streptomycetaceae
 MITE0000461,active,PikC,Cytochrome P450,Hydroxylation,Hydroxylation of narbomycin to form pikromycin,Heme,Fe,Streptomyces venezuelae,Bacteria,Bacillati,Actinomycetota,Actinomycetes,Kitasatosporales,Streptomycetaceae
 MITE0000462,active,EgtB,Sulfoxide synthase,Oxidation,Iron-dependent sulfoxidation of trimethylhistidine.,N/A,Fe,Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316),Bacteria,Bacillati,Actinomycetota,Actinomycetes,Mycobacteriales,Mycobacteriaceae
+MITE0000463,active,PrnA,Tryptophan 7-halogenase,Halogenation,Chlorination of tryptophan at C7 position to yield 7-chloro-L-tryptophan in pyrrolnitrin biosynthesis,FAD,N/A,Pseudomonas chlororaphis,Bacteria,Pseudomonadati,Pseudomonadota,Gammaproteobacteria,Pseudomonadales,Pseudomonadaceae