Mitochondrial lipoyl synthase that inserts sulfur atoms into octanoylated lipoyl domains during endogenous protein lipoylation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0009107 lipoate biosynthetic process | IBA GO_REF:0000033 | MODIFY | Summary: Lipoate biosynthetic process described the core process for LIP1, but GO:0009107 was obsoleted (2026-08-22) in favor of protein lipoylation. Reason: LIP1 catalyzes the sulfur-insertion step of endogenous protein lipoylation; GO:0009107 is now obsolete (replaced_by GO:0009249 protein lipoylation, per GO, obsoleted because term usage was inconsistent), so the annotation should move to the replacement term. Propagation Review Root cause: NO FAILURE CORE Sources checked: MGI:MGI:1934604 · mouse lipoyl synthase Lias SUPPORTS TRANSFER PANTHER:PTN000101947 SUPPORTS TRANSFER Propagation of the lipoate-synthesis role is sound; the MODIFY is ontology maintenance only, because GO:0009107 was obsoleted (2026-08-22) with replaced_by GO:0009249 protein lipoylation. Proposed replacements: protein lipoylation Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes file:POPTR/LIP1/LIP1-uniprot.txt PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. |
| GO:0016992 lipoate synthase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Lipoate synthase activity is the specific molecular function of LIP1. Reason: The reviewed entry identifies LIP1 as lipoate synthase EC 2.8.1.8. Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes |
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MODIFY | Summary: Generic catalytic activity is correct but too broad for a characterized lipoate synthase. Reason: Use the specific lipoate synthase activity term. Proposed replacements: lipoate synthase activity Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes |
| GO:0005739 mitochondrion | IEA GO_REF:0000120 | ACCEPT | Summary: Mitochondrion is the supported localization for LIP1. Reason: The reviewed entry places LIP1 in mitochondria. Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion |
| GO:0009107 lipoate biosynthetic process | IEA GO_REF:0000120 | MODIFY | Summary: Lipoate biosynthetic process described the core process for LIP1, but GO:0009107 was obsoleted (2026-08-22) in favor of protein lipoylation. Reason: LIP1 catalyzes the sulfur-insertion step of endogenous protein lipoylation; GO:0009107 is now obsolete (replaced_by GO:0009249 protein lipoylation, per GO, obsoleted because term usage was inconsistent), so the annotation should move to the replacement term. Proposed replacements: protein lipoylation Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes file:POPTR/LIP1/LIP1-uniprot.txt PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. |
| GO:0009249 protein lipoylation | IEA GO_REF:0000104 | ACCEPT | Summary: Protein lipoylation is an appropriate process for LIP1. Reason: The pathway annotation describes endogenous protein lipoylation via lipoyl-lysine formation. Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. |
| GO:0016783 sulfurtransferase activity | IEA GO_REF:0000104 | MODIFY | Summary: Sulfurtransferase activity is a broad description of the lipoate synthase reaction. Reason: Use the specific lipoate synthase activity term for this radical SAM enzyme. Proposed replacements: lipoate synthase activity Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes |
| GO:0016992 lipoate synthase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Lipoate synthase activity is the specific molecular function of LIP1. Reason: The reviewed entry identifies LIP1 as lipoate synthase EC 2.8.1.8. Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes |
| GO:0051536 iron-sulfur cluster binding | IEA GO_REF:0000002 | MODIFY | Summary: Iron-sulfur cluster binding is correct but less specific than the 4Fe-4S cluster annotation. Reason: The reviewed entry specifies two 4Fe-4S clusters per subunit. Proposed replacements: 4 iron, 4 sulfur cluster binding Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt Binds 2 [4Fe-4S] clusters per subunit. |
| GO:0051539 4 iron, 4 sulfur cluster binding | IEA GO_REF:0000120 | ACCEPT | Summary: 4 iron, 4 sulfur cluster binding is a supported cofactor feature of LIP1. Reason: The reviewed entry states that LIP1 binds two 4Fe-4S clusters per subunit. Supporting Evidence: file:POPTR/LIP1/LIP1-uniprot.txt Binds 2 [4Fe-4S] clusters per subunit. |
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Download this section (compressed HTML)Q: Which mitochondrial lipoate-dependent enzyme complexes are most sensitive to LIP1 perturbation in Populus?
Experiment: Quantify lipoylated mitochondrial enzyme subunits and lipoate-dependent dehydrogenase activities in LIP1 knockdown or mutant tissue.
Type: targeted functional assay
LIP1-uniprot.txt and LIP1-goa.tsv.Loading supporting content…
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