argJ

UniProt ID: P59612
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

ArgJ (PP_1346) is a bifunctional acetyltransferase in L-arginine biosynthesis. It can initiate the pathway by transferring an acetyl group from acetyl-CoA to L-glutamate and can close the cyclic acetyl route by transferring the acetyl group from N-acetyl-L-ornithine back to L-glutamate, releasing L-ornithine and regenerating N-acetyl-L-glutamate.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004042 L-glutamate N-acetyltransferase activity, acting on acetyl-CoA as donor
IEA
GO_REF:0000120
ACCEPT
Summary: ArgJ can catalyze acetyl-CoA-dependent formation of N-acetyl-L-glutamate.
Reason: Reviewed UniProt assigns EC 2.3.1.1 and RHEA:24292 to the bifunctional ArgJ protein.
Supporting Evidence:
file:PSEPK/argJ/argJ-uniprot.txt
Reaction=L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+);
file:PSEPK/argJ/argJ-deep-research-openscientist.md
L-glutamate + acetyl-CoA β†’ N-acetyl-L-glutamate + CoA + H⁺
GO:0004358 L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
IEA
GO_REF:0000120
ACCEPT
Summary: ArgJ transfers acetyl from N-acetyl-L-ornithine to glutamate, releasing ornithine.
Reason: Reviewed UniProt assigns EC 2.3.1.35 and RHEA:15349 as the second defining ArgJ activity.
Supporting Evidence:
file:PSEPK/argJ/argJ-uniprot.txt
Reaction=N(2)-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate +
file:PSEPK/argJ/argJ-deep-research-openscientist.md
NΒ²-acetyl-L-ornithine + L-glutamate β†’ N-acetyl-L-glutamate + L-ornithine
GO:0005737 cytoplasm
IEA
GO_REF:0000120
KEEP AS NON CORE
Summary: ArgJ is a soluble cytoplasmic biosynthetic enzyme.
Reason: The location is supported but is secondary to its two catalytic reactions.
GO:0006526 L-arginine biosynthetic process
IEA
GO_REF:0000120
ACCEPT
Summary: Both ArgJ acetyltransferase reactions operate in L-arginine biosynthesis.
Reason: The reviewed UniProt pathway assignments place ArgJ in initiation and cyclic ornithine release. A KT2440 argJ mutant remains arginine prototrophic, consistent with compensation by the ArgA/ArgE route rather than evidence against these activities.
GO:0006592 L-ornithine biosynthetic process
IEA
GO_REF:0000118
ACCEPT
Summary: ArgJ directly releases L-ornithine from N-acetyl-L-ornithine.
Reason: The EC 2.3.1.35 transacetylation reaction produces ornithine in the cyclic route.

Core Functions

Transfers acetyl from acetyl-CoA to L-glutamate to form N-acetyl-L-glutamate and initiate L-arginine biosynthesis.

Supporting Evidence:
  • file:PSEPK/argJ/argJ-uniprot.txt
    Reaction=L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+);
  • file:PSEPK/argJ/argJ-deep-research-openscientist.md
    L-glutamate + acetyl-CoA β†’ N-acetyl-L-glutamate + CoA + H⁺

Transfers acetyl from N-acetyl-L-ornithine to L-glutamate, releasing L-ornithine and regenerating N-acetyl-L-glutamate in the cyclic route.

Supporting Evidence:
  • file:PSEPK/argJ/argJ-uniprot.txt
    Reaction=N(2)-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate +
  • file:PSEPK/argJ/argJ-deep-research-openscientist.md
    NΒ²-acetyl-L-ornithine + L-glutamate β†’ N-acetyl-L-glutamate + L-ornithine

References

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Deep Research

OpenScientist

(argJ-deep-research-openscientist.md)

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