gltX

UniProt ID: Q88LF6
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Review Status: DRAFT
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Gene Description

GltX is the class I glutamate--tRNA ligase of Pseudomonas putida KT2440. It uses ATP to attach L-glutamate to tRNA(Glu), producing Glu-tRNA(Glu) for translation. It is not known whether it also misacylates tRNA(Gln) in this GlnRS-containing strain.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0000049 tRNA binding
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: tRNA binding is inherent to the documented GltX reaction but is less informative than catalysis.
Reason: The reaction explicitly uses tRNA(Glu); GO:0004818 captures the core activity.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
Reaction=tRNA(Glu) + L-glutamate + ATP
GO:0000166 nucleotide binding
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: Nucleotide binding is true but uninformative beside the separately annotated ATP binding activity.
Reason: The exact reaction and annotated binding site identify ATP, which is already captured by GO:0005524.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
Reaction=tRNA(Glu) + L-glutamate + ATP
GO:0004812 aminoacyl-tRNA ligase activity
IEA
GO_REF:0000120
MARK AS OVER ANNOTATED
Summary: Generic aminoacyl-tRNA ligase activity is true but uninformative beside the substrate-specific annotation.
Reason: GO:0004818 already captures the EC 6.1.1.17 reaction specifically.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
RecName: Full=Glutamate--tRNA ligase
GO:0004818 glutamate-tRNA ligase activity
IEA
GO_REF:0000120
ACCEPT
Summary: This is the substrate-specific catalytic activity of GltX.
Reason: The reviewed record directly assigns tRNA(Glu), L-glutamate, and ATP as substrates.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
Reaction=tRNA(Glu) + L-glutamate + ATP
GO:0005524 ATP binding
IEA
GO_REF:0000120
ACCEPT
Summary: ATP is the activating substrate for glutamyl-tRNA formation.
Reason: UniProt records both ATP consumption and a specific ATP-binding site.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
Reaction=tRNA(Glu) + L-glutamate + ATP
GO:0005737 cytoplasm
IEA
GO_REF:0000120
KEEP AS NON CORE
Summary: Cytoplasm is correct but broader than the separately annotated cytosol location for this soluble enzyme.
Reason: The reviewed entry assigns GltX to the cytoplasm, while GO:0005829 more precisely captures the soluble compartment used in the core function.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm
GO:0005829 cytosol
IEA
GO_REF:0000118
ACCEPT
Summary: Cytosol is consistent with the reviewed cytoplasmic localization.
Reason: The protein is a soluble monomer with no membrane or export feature.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm
GO:0006418 tRNA aminoacylation for protein translation
IEA
GO_REF:0000120
MARK AS OVER ANNOTATED
Summary: The broad translational charging term is true but uninformative beside the substrate-specific process annotation.
Reason: GO:0006424 already captures the defined glutamate and tRNA(Glu) substrates.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
Catalyzes the attachment of glutamate to tRNA(Glu)
GO:0006424 glutamyl-tRNA aminoacylation
IEA
GO_REF:0000120
ACCEPT
Summary: GltX directly produces Glu-tRNA(Glu).
Reason: The assigned reaction exactly matches glutamyl-tRNA aminoacylation.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
Catalyzes the attachment of glutamate to tRNA(Glu)
GO:0008270 zinc ion binding
IEA
GO_REF:0000002
REMOVE
Summary: The zinc-binding call is contradicted by loss of the conserved four-cysteine zinc-binding cluster.
Reason: Alignment to zinc-binding Escherichia coli GluRS P04805 shows that Q88LF6 retains the first Cys pair but lacks the downstream cysteine needed to preserve the four-cysteine zinc-binding cluster. The InterPro-derived zinc-binding transfer is therefore not appropriate for this protein.
Supporting Evidence:
file:PSEPK/gltX/gltX-bioinformatics/RESULTS.md
Q88LF6 therefore does not preserve the four-cysteine zinc-binding cluster present in P04805.
GO:0043039 tRNA aminoacylation
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: The broad tRNA aminoacylation term is true but uninformative beside the substrate-specific process annotation.
Reason: GO:0006424 already captures the direct GltX process specifically.
Supporting Evidence:
file:PSEPK/gltX/gltX-uniprot.txt
Catalyzes the attachment of glutamate to tRNA(Glu)

Core Functions

Direct ATP-dependent production of Glu-tRNA(Glu) for translation.

Directly Involved In:
Cellular Locations:
Supporting Evidence:
  • file:PSEPK/gltX/gltX-uniprot.txt
    Catalyzes the attachment of glutamate to tRNA(Glu)

References

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Suggested Questions for Experts

Q: Does Q88LF6 also recognize tRNA(Gln) and generate Glu-tRNA(Gln) under any physiological condition despite the presence of GlnS?

Suggested Experiments

Experiment: Compare purified GltX aminoacylation kinetics with native KT2440 tRNA(Glu) and tRNA(Gln), and identify charged products by acid-urea electrophoresis or LC-MS.

Hypothesis: Q88LF6 may discriminate strongly against tRNA(Gln) in this GlnRS-containing strain.

πŸ“š Additional Documentation

Notes

(gltX-notes.md)

gltX curation notes

  • Q88LF6 is a reviewed class I glutamate--tRNA ligase that directly charges
    tRNA(Glu) [file:PSEPK/gltX/gltX-uniprot.txt, "Catalyzes the attachment of
    glutamate to tRNA(Glu)"].
  • The exact record does not establish tRNA(Gln) misacylation. That route remains
    a PSEPK-specific knowledge gap because KT2440 also encodes GlnS.
  • The InterPro-derived zinc-binding annotation was removed after a reproducible
    alignment to zinc-binding E. coli GluRS P04805 showed that Q88LF6 lacks the
    complete four-cysteine cluster [file:PSEPK/gltX/gltX-bioinformatics/RESULTS.md,
    "Q88LF6 therefore does not preserve the four-cysteine zinc-binding cluster present in P04805."].

Bioinformatics Results

(RESULTS.md)

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