SerS is the cytoplasmic class II seryl-tRNA synthetase of Pseudomonas putida KT2440. It uses ATP to esterify L-serine onto tRNA(Ser) for translation and also charges the specialized tRNA(Sec), generating Ser-tRNA(Sec), the immediate substrate for SelA in the bacterial selenocysteinyl-tRNA(Sec) biosynthetic route.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000166 nucleotide binding | IEA GO_REF:0000002 | MODIFY | Summary: SerS binds ATP rather than an unspecified nucleotide during aminoacylation. Reason: The reviewed UniProt entry identifies ATP as the nucleotide substrate and annotates multiple ATP-contacting residues. GO:0005524 is therefore more informative than the generic nucleotide-binding parent. Proposed replacements: ATP binding Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Ser) + L-serine + ATP |
| GO:0004812 aminoacyl-tRNA ligase activity | IEA GO_REF:0000002 | MODIFY | Summary: The generic ligase call is correct but can be replaced by the substrate-specific activity. Reason: UniProt and the PANTHER subfamily both identify this protein specifically as serine--tRNA ligase, so GO:0004828 captures the known amino-acid specificity without retaining the broad parent. Proposed replacements: serine-tRNA ligase activity Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt RecName: Full=Serine--tRNA ligase |
| GO:0004828 serine-tRNA ligase activity | IEA GO_REF:0000120 | ACCEPT | Summary: This is the specific catalytic activity of SerS. Reason: The reviewed entry assigns EC 6.1.1.11 and explicitly records aminoacylation of both tRNA(Ser) and tRNA(Sec) with L-serine. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt DE EC=6.1.1.11 |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: ATP is the activating substrate for both documented SerS aminoacylation reactions. Reason: Both UniProt reaction records consume ATP and produce AMP plus diphosphate, and predicted ATP-binding residues are present. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Sec) + L-serine + ATP |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: A cytoplasmic location is appropriate for this soluble bacterial aminoacyl-tRNA synthetase. Reason: The reviewed UniProt entry explicitly assigns SerS to the cytoplasm and contains no secretion or membrane-topology features. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006418 tRNA aminoacylation for protein translation | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: The broad translational aminoacylation process is less informative than seryl-tRNA aminoacylation. Reason: GO:0006434 already captures the defining substrate-specific process. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Catalyzes the attachment of serine to tRNA(Ser). |
| GO:0006434 seryl-tRNA aminoacylation | IEA GO_REF:0000120 | ACCEPT | Summary: SerS directly produces Ser-tRNA(Ser) for translation. Reason: The assigned reaction attaches L-serine to tRNA(Ser), which is exactly the process represented by this term. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Catalyzes the attachment of serine to tRNA(Ser). |
| GO:0016260 L-selenocysteine biosynthetic process | IEA GO_REF:0000104 | ACCEPT | Summary: SerS supplies Ser-tRNA(Sec), the first charged-tRNA intermediate in bacterial Sec-tRNA synthesis. Reason: UniProt explicitly records aminoacylation of tRNA(Sec) with serine. SerS therefore participates in L-selenocysteine biosynthesis, but this annotation does not imply that SerS synthesizes or functions as the downstream selenoprotein. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt to aminoacylate tRNA(Sec) with serine |
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Download this section (compressed HTML)Experiment: Purify SerS and compare steady-state aminoacylation kinetics with the two cognate tRNA classes; verify Ser-tRNA products by acid-urea electrophoresis or LC-MS.
Hypothesis: Q88FT2 aminoacylates both KT2440 tRNA(Ser) and tRNA(Sec).
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