LeuC is the catalytic large subunit of the LeuC-LeuD 3-isopropylmalate dehydratase. The iron-sulfur enzyme reversibly isomerizes 2-isopropylmalate to 3-isopropylmalate through a dehydration/rehydration sequence in L-leucine biosynthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003861 3-isopropylmalate dehydratase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This is the specific activity of the LeuC-LeuD enzyme, to which LeuC contributes the catalytic iron-sulfur core. Reason: EC 4.2.1.33, HAMAP, and LeuC-specific family assignments agree. Because the functional enzyme is a LeuC-LeuD heterodimer, `contributes_to` is a better qualifier than the machine-sourced `enables` for this subunit. Supporting Evidence: file:PSEPK/leuC/leuC-uniprot.txt Full=3-isopropylmalate dehydratase large subunit file:PSEPK/leuC/leuC-uniprot.txt Heterodimer of LeuC and LeuD. file:PSEPK/leuC/leuC-deep-research-openscientist.md The gene *leuC* (locus PP_1985; UniProt Q88LE8) of *Pseudomonas putida* KT2440 encodes the **large, catalytic subunit of 3-isopropylmalate dehydratase** |
| GO:0009098 L-leucine biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: LeuC participates in the second leucine-specific step. Reason: UniProt places the LeuC-LeuD activity at step 2 of 4. |
| GO:0009316 3-isopropylmalate dehydratase complex | IEA file:PSEPK/leuC/leuC-uniprot.txt | NEW | Summary: LeuC is the catalytic large subunit of the LeuC-LeuD heterodimer. Reason: The exact Q88LE8 record identifies the heterodimer, but the fetched GOA snapshot lacks the corresponding complex-membership annotation. Supporting Evidence: file:PSEPK/leuC/leuC-uniprot.txt Heterodimer of LeuC and LeuD. |
| GO:0043436 oxoacid metabolic process | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: This broad process adds no information beyond leucine biosynthesis. Reason: GO:0009098 captures the specific biological pathway. |
| GO:0051539 4 iron, 4 sulfur cluster binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: The LeuC catalytic subunit carries the 4Fe-4S cluster. Reason: The aconitase-family active-site architecture supports this cofactor assignment. |
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