dapC encodes the PLP-dependent N-succinyl-LL-diaminopimelate aminotransferase (EC 2.6.1.17) of the succinylated DAP route. It transfers an amino group from L-glutamate to N-succinyl-2-amino-6-oxopimelate, producing the substrate subsequently deprotected by DapE.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0009016 succinyldiaminopimelate:2-oxoglutarate transaminase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This is the defining DapC molecular function. Reason: EC 2.6.1.17 and the beta/gammaproteobacterial DapC-specific family support the reaction. No direct Q88MI3 assay was found, so the assignment remains a family-based inference. Supporting Evidence: file:PSEPK/dapC/dapC-uniprot.txt DR InterPro; IPR019878; DapC_beta/gammaproteobac. file:PSEPK/dapC/dapC-uniprot.txt DR NCBIfam; TIGR03538; DapC_gpp; 1. file:PSEPK/dapC/dapC-deep-research-openscientist.md No direct biochemical characterization of the *P. putida* enzyme. |
| GO:0009085 L-lysine biosynthetic process | IEA GO_REF:0000002 | ACCEPT | Summary: DapC supplies N-succinyl-LL-diaminopimelate in L-lysine biosynthesis. Reason: The DapC-specific family and pathway context place this transamination in the succinylated DAP route. |
| GO:0030170 pyridoxal phosphate binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: PLP binding is valid cofactor context for DapC. Reason: The aminotransferase family requires PLP, but binding is less informative than the substrate-specific reaction. |
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