Notes for DANRE bdh2

• The UniProt record supports two distinct Bdh2 activities: 4-oxoproline reductase chemistry described as ketoproline detoxification [file:DANRE/bdh2/bdh2-uniprot.txt "detoxification mechanism for ketoprolines"] and separate 2,5-DHBA-associated siderophore formation [file:DANRE/bdh2/bdh2-uniprot.txt "formation of 2,5-dihydroxybenzoate (2,5-DHBA)"].
• The siderophore/heme branch is retained as a separate core role because bdh2 inactivation affects zebrafish heme biology and erythroid maturation PMID:26929344.
• 3-hydroxybutyrate dehydrogenase activity is kept as non-core because UniProt phrases it as a possible by-similarity activity, while zebrafish evidence focuses on siderophore/heme biology.
• Hemoglobin and erythrocyte maturation terms are real phenotypic consequences, but not the molecular core.