ilvE

UniProt ID: Q88H54
Organism: Pseudomonas putida KT2440
Review Status: DRAFT
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Gene Description

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.

Existing Annotations Review

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.

Core Functions

Reversible branched-chain amino-acid aminotransferase supplying the terminal transamination in leucine, valine, and isoleucine biosynthesis.

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
    L-valine biosynthesis; L-valine from

References

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Deep Research

OpenScientist

(ilvE-deep-research-openscientist.md)

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