Mitochondrial manganese superoxide dismutase that detoxifies superoxide radicals in the mitochondrial matrix by converting superoxide to hydrogen peroxide and oxygen.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004784 superoxide dismutase activity | IEA GO_REF:0000120 | ACCEPT | Summary: The EC/RHEA-supported UniProt annotation matches the protein name, catalytic reaction, and MnSOD family assignment. Reason: Superoxide dismutase activity is the defining catalytic activity of MnSOD and is directly supported by the UniProt EC 1.15.1.1 reaction. Supporting Evidence: file:MISSI/MnSOD/MnSOD-uniprot.txt Reaction=2 superoxide + 2 H(+) = H2O2 + O2 |
| GO:0005739 mitochondrion | IEA GO_REF:0000118 | KEEP AS NON CORE | Summary: Mitochondrial localization is supported, but the matrix annotation is more specific for this MnSOD entry. Reason: The broader mitochondrion term is true but less informative than the mitochondrial matrix annotation. Supporting Evidence: file:MISSI/MnSOD/MnSOD-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location annotation places the protein in the mitochondrial matrix. Reason: The matrix is the specific mitochondrial compartment supported by the UniProt entry. Supporting Evidence: file:MISSI/MnSOD/MnSOD-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion matrix |
| GO:0006801 superoxide metabolic process | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Superoxide metabolism is supported by the SOD reaction, although the specific removal-of-superoxide-radicals annotation captures the core process more precisely. Reason: This broader process term is correct but less specific than GO:0019430 for MnSOD's core role. Supporting Evidence: file:MISSI/MnSOD/MnSOD-uniprot.txt Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. |
| GO:0006950 response to stress | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Oxidative radical detoxification contributes to stress response, but this term is broad and not the core biochemical function. Reason: Stress response is a downstream biological context for MnSOD activity rather than its defining molecular role. Supporting Evidence: file:MISSI/MnSOD/MnSOD-uniprot.txt Destroys radicals which are normally produced within the cells and which are toxic to biological systems. |
| GO:0019430 removal of superoxide radicals | IEA GO_REF:0000108 | ACCEPT | Summary: The GO term matches the catalytic SOD reaction converting superoxide radicals to hydrogen peroxide and oxygen. Reason: Removal of superoxide radicals is the direct biological process accomplished by MnSOD activity. Supporting Evidence: file:MISSI/MnSOD/MnSOD-uniprot.txt Reaction=2 superoxide + 2 H(+) = H2O2 + O2 |
| GO:0030145 manganese ion binding | IEA GO_REF:0000118 | ACCEPT | Summary: Mn(2+) cofactor binding is explicitly recorded in UniProt and is consistent with a manganese superoxide dismutase. Reason: Manganese binding is the specific metal cofactor association for MnSOD catalysis. Supporting Evidence: file:MISSI/MnSOD/MnSOD-uniprot.txt COFACTOR: Name=Mn(2+) |
| GO:0046872 metal ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Generic metal ion binding is true through the manganese cofactor but less specific than GO:0030145. Reason: The specific manganese ion binding annotation should represent the core cofactor-binding aspect; the parent metal-binding term is non-core. |
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Download this section (compressed HTML)Q: Is Miscanthus MnSOD activity dynamically regulated during drought, cold, or high-light oxidative stress?
Experiment: Measure mitochondrial SOD activity and ROS accumulation in Miscanthus stress treatments.
Type: targeted functional assay
mitochondrion, superoxide metabolic process, response to stress, metal ion binding) are retained as non-core because more specific annotations capture the core biology.Loading supporting contentβ¦
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