GlyS is the beta subunit of the bacterial alpha2-beta2 glycyl-tRNA synthetase, paired with GlyQ. Its multidomain architecture contributes tRNA recognition, assembly and stabilization of ATP coordination in the complete enzyme. Together the subunits attach glycine to tRNA(Gly); an ArgRS-like recognition domain does not confer arginine-activation activity.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000166 nucleotide binding | IEA GO_REF:0000002 | MODIFY | Summary: glyS binds ATP as part of its aminoacylation machinery. Reason: Nucleotide binding is true but broad. The curated glycine reaction and relevant subunit architecture support the more specific ATP-binding claim; this is integral substrate recognition, not a peripheral role. Proposed replacements: ATP binding Supporting Evidence: file:PSEPK/glyS/glyS-uniprot.txt Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP + diphosphate; Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA- COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255}; |
| GO:0004814 arginine-tRNA ligase activity | IEA GO_REF:0000002 | REMOVE | Summary: GlyS is the beta subunit of GlyRS, not an arginine-activating synthetase. Reason: The exact curated GlyS beta-subunit family and glycyl-tRNA reaction contradict the arginine-ligase transfer. Homology of an anticodon-binding domain to ArgRS does not supply the class-I arginine-activation catalytic architecture. Retain genuine GlyRS complex contributions. Supporting Evidence: file:PSEPK/glyS/glyS-uniprot.txt Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP + diphosphate; Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA- COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255}; file:PSEPK/glyS/glyS-uniprot.txt Belongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000255|HAMAP-Rule:MF_00255}. |
| GO:0004820 glycine-tRNA ligase activity | IEA GO_REF:0000120 | ACCEPT | Summary: glyS supports its substrate-specific tRNA-ligase activity. Reason: The exact native protein has the corresponding curated HAMAP family/domain and reaction assignment. This supports conserved catalytic capability by homology, not direct KT2440 purification. As an alpha/beta complex subunit, it contributes to the whole reaction; ordinary relationship metadata does not turn this into an unsupported isolated-subunit claim. Supporting Evidence: file:PSEPK/glyS/glyS-uniprot.txt Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP + diphosphate; Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA- COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255}; file:PSEPK/glyS/glyS-uniprot.txt Belongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000255|HAMAP-Rule:MF_00255}. file:PSEPK/glyS/glyS-uniprot.txt Tetramer of two alpha and two beta subunits. {ECO:0000255|HAMAP-Rule:MF_00255}. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: glyS contributes integral ATP recognition to its enzymatic reaction. Reason: ATP binding is an integral biochemical property, not a non-core activity merely because it is binding. The curated reaction/architecture supports it by homology for KT2440. Full EcGlyRS structure directly places beta-subunit Arg326 against the ATP-analogue gamma phosphate; the corresponding bacterial GlyS architecture supports the target inference, without claiming a KT2440 affinity measurement. Supporting Evidence: file:PSEPK/glyS/glyS-uniprot.txt Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP + diphosphate; Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA- COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255}; PMID:34390350 Importantly, Arg326 from the Ξ²-subunit B3 domain was observed to form direct charge interactions with the Ξ³-phosphate of AMP-PNP (Figure 2B and C) |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | MODIFY | Summary: glyS acts in the soluble intracellular tRNA-processing system. Reason: The soluble intracellular synthetase acts on cellular tRNAs; refine cytoplasm to the already retained cytosol term. This is a conserved biochemical/localization inference, not native microscopy. Proposed replacements: cytosol Supporting Evidence: file:PSEPK/glyS/glyS-uniprot.txt Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}. |
| GO:0005829 cytosol | IEA GO_REF:0000118 | ACCEPT | Summary: glyS acts in the bacterial cytosol. Reason: The conserved soluble enzyme architecture and curated intracellular localization support this core location. Direct KT2440 imaging is not claimed; lack of such an experiment does not make the supported core location peripheral. Supporting Evidence: file:PSEPK/glyS/glyS-uniprot.txt Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}. |
| GO:0006420 arginyl-tRNA aminoacylation | IEA GO_REF:0000002 | MODIFY | Summary: glyS contributes to translational tRNA aminoacylation; the old substrate-specific BP is obsolete. Reason: Current QuickGO marks this substrate-specific process obsolete because it restates a molecular function. Preserve the original GOA term while replacing it with GO:0006418; retain substrate specificity in the supported ligase molecular function. The historical arginyl-tRNA aminoacylation assignment also misstates this protein's substrate: the native curated classification supports glycine charging. The replacement does not endorse the former wrong-substrate label. Proposed replacements: tRNA aminoacylation for protein translation Supporting Evidence: file:PSEPK/glyS/glyS-uniprot.txt Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP + diphosphate; Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA- COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255}; |
| GO:0006426 glycyl-tRNA aminoacylation | IEA GO_REF:0000120 | MODIFY | Summary: glyS contributes to translational tRNA aminoacylation; the old substrate-specific BP is obsolete. Reason: Current QuickGO marks this substrate-specific process obsolete because it restates a molecular function. Preserve the original GOA term while replacing it with GO:0006418; retain substrate specificity in the supported ligase molecular function. Proposed replacements: tRNA aminoacylation for protein translation Supporting Evidence: file:PSEPK/glyS/glyS-uniprot.txt Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP + diphosphate; Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA- COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255}; |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Are the ATP-coordinating beta-subunit interactions observed in EcGlyRS retained quantitatively in KT2440?
Experiment: Map the corresponding GlyS interface residues, substitute them in the native complex and measure ATP binding, glycine activation and tRNA(Gly) charging separately.
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)