SerS is a cytoplasmic class II seryl-tRNA synthetase that charges tRNA(Ser) for translation and is predicted to charge tRNA(Sec), supplying the serine-bearing intermediate for selenocysteinyl-tRNA formation. It acts in the cytoplasm of Pseudomonas putida KT2440, using ATP to form the aminoacyl-tRNA substrate for protein synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000166 nucleotide binding | IEA GO_REF:0000002 | MODIFY | Summary: ATP is the nucleotide used to activate serine by serS. Reason: The MF_00176 reaction consumes ATP during formation of the aminoacyl adenylate and releases AMP plus diphosphate. Refine generic nucleotide binding to its supported ATP-binding descendant, without implying that all nucleotides bind equally. Proposed replacements: ATP binding Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Sec) + L-serine + ATP |
| GO:0004812 aminoacyl-tRNA ligase activity | IEA GO_REF:0000002 | MODIFY | Summary: The broad ligase annotation can specify serine and tRNA(Ser). Reason: HAMAP MF_00176 specifies both tRNA(Ser) and tRNA(Sec) reactions and a homodimer spanning the tRNA-binding surface. Current GO:0004828 explicitly includes the tRNA(Sec) reaction, so no extra MF proposal is required. GO:0004828 is the supported amino-acid-specific descendant of GO:0004812; the parent is biologically correct, not over-annotation. Proposed replacements: serine-tRNA ligase activity Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Sec) + L-serine + ATP |
| GO:0004828 serine-tRNA ligase activity | IEA GO_REF:0000120 | ACCEPT | Summary: serS supplies serine-charged tRNA(Ser) through ATP-dependent aminoacylation. Reason: HAMAP MF_00176 specifies both tRNA(Ser) and tRNA(Sec) reactions and a homodimer spanning the tRNA-binding surface. Current GO:0004828 explicitly includes the tRNA(Sec) reaction, so no extra MF proposal is required. The independently curated MF_00176 reaction supports this specific MF; electronic provenance does not make a central catalytic function peripheral. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Sec) + L-serine + ATP |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: ATP binding is integral to serS-catalysed serine activation. Reason: The curated MF_00176 reaction specifically consumes ATP, and the target retains the corresponding synthetase architecture. This is an essential biochemical property of the charging activity, even though direct KT2440 binding constants have not been measured in the retrieved sources. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Sec) + L-serine + ATP |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: serS is assigned to the bacterial cytoplasm for translational tRNA charging. Reason: The MF_00176 subcellular-location statement supports this native compartment as a conserved functional inference. No finer localization is established in the inspected record; this is the core cellular setting rather than a peripheral process. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006418 tRNA aminoacylation for protein translation | IEA GO_REF:0000002 | ACCEPT | Summary: serS catalyses the charging step that supplies serine to ribosomal protein synthesis. Reason: The MF_00176 reaction directly performs aminoacylation, rather than merely affecting translation through a downstream phenotype. Live QuickGO verifies GO:0006418 as current; the old amino-acid-specific biological-process term is obsolete and is not a reason to mark this correct process as over-annotated. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Sec) + L-serine + ATP |
| GO:0006434 seryl-tRNA aminoacylation | IEA GO_REF:0000120 | MODIFY | Summary: The serine-specific charging chemistry remains supported, but this biological-process ID is obsolete. Reason: The live QuickGO snapshot verifies GO:0006434 as obsolete. Preserve the original machine-sourced ID and label and represent the biological process with current GO:0006418; retain serine specificity in GO:0004828. This is ontology maintenance, not a rejection of the MF_00176 reaction. Proposed replacements: tRNA aminoacylation for protein translation Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Sec) + L-serine + ATP |
| GO:0016260 L-selenocysteine biosynthetic process | IEA GO_REF:0000104 | ACCEPT | Summary: SerS supplies Ser-tRNA(Sec), the first charged intermediate in the bacterial selenocysteine route. Reason: HAMAP MF_00176 independently assigns the tRNA(Sec) reaction and its pathway step. SerS catalyses formation of this intermediate itself, satisfying process participation; SelA performs the subsequent chemical conversion to Sec-tRNA. Exact KT2440 flux and physiological conditions remain unmeasured in the retrieved evidence. Supporting Evidence: file:PSEPK/serS/serS-uniprot.txt Reaction=tRNA(Sec) + L-serine + ATP |
Loading supporting content…
Download this section (compressed HTML)Q: Can purified KT2440 SerS charge both native tRNA(Ser) and tRNA(Sec), and which conditions support flux through the downstream Sec-tRNA route?
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).
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)