IlvE is the pyridoxal 5'-phosphate-dependent branched-chain amino-acid aminotransferase. It reversibly transfers amino groups between glutamate and the keto-acid precursors of valine, isoleucine, and leucine, supplying the terminal transamination in all three biosynthetic branches.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: This generic term is redundant with BCAT activity. Reason: GO:0004084 identifies the actual transaminase chemistry. |
| GO:0004084 branched-chain-amino-acid:2-oxoglutarate transaminase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This is the core reversible IlvE molecular function. Reason: Family-level support. Q88H54 matches the NCBIfam TIGR01123 ilvE_II model and the InterPro branched-chain amino-acid aminotransferase II family (IPR005786), and the RuleBase-backed UniProt reactions assign EC 2.6.1.42 transamination of leucine, isoleucine and valine with 2-oxoglutarate. The PLP-lysine (K183) is annotated by PIRSR. No direct biochemical characterization of Q88H54 is cached. Supporting Evidence: file:PSEPK/ilvE/ilvE-uniprot.txt TIGR01123; ilvE_II; 1. file:PSEPK/ilvE/ilvE-uniprot.txt IPR005786; B_amino_transII. file:PSEPK/ilvE/ilvE-uniprot.txt Reaction=L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L- |
| GO:0030170 pyridoxal phosphate binding | IEA file:PSEPK/ilvE/ilvE-uniprot.txt | NEW | Summary: PLP binding is valid cofactor information for this class-IV aminotransferase. Reason: The exact Q88H54 record assigns pyridoxal 5'-phosphate, but the fetched GOA snapshot lacks the corresponding cofactor-binding annotation. Supporting Evidence: file:PSEPK/ilvE/ilvE-uniprot.txt Name=pyridoxal 5'-phosphate; |
| GO:0009081 branched-chain amino acid metabolic process | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: This broad term reflects the reversible biosynthetic and catabolic reaction. Reason: The transamination is reversible, but no target-specific evidence shows that IlvE primarily serves branched-chain amino-acid catabolism in KT2440. The broad metabolic term is retained as context, while the three supported biosynthetic processes define the core role. |
| GO:0052654 L-leucine:2-oxoglutarate transaminase activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: IlvE acts on the leucine/2-oxoisocaproate pair. Reason: This substrate-specific Rhea mapping refines the accepted general BCAT activity. |
| GO:0052655 L-valine:2-oxoglutarate transaminase activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: IlvE acts on the valine/2-oxoisovalerate pair. Reason: This substrate-specific Rhea mapping refines the accepted general BCAT activity. |
| GO:0052656 L-isoleucine:2-oxoglutarate transaminase activity | IEA GO_REF:0000116 | KEEP AS NON CORE | Summary: IlvE acts on the isoleucine/3-methyl-2-oxopentanoate pair. Reason: This substrate-specific Rhea mapping refines the accepted general BCAT activity. |
| GO:0009098 L-leucine biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: IlvE performs the terminal leucine transamination. Reason: UniProt explicitly places Q88H54 in the terminal leucine step. |
| GO:0009099 L-valine biosynthetic process | IEA GO_REF:0000041 | ACCEPT | Summary: IlvE performs the terminal valine transamination. Reason: UniProt explicitly places Q88H54 in the terminal valine step. |
| GO:1901705 L-isoleucine biosynthetic process | IEA file:PSEPK/ilvE/ilvE-uniprot.txt | NEW | Summary: IlvE performs the terminal isoleucine transamination. Reason: UniProt explicitly places Q88H54 in the terminal isoleucine step. |
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