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UniProt functional annotation for P27000 | ||
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| UniProt code: P27000. |
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| Organism: | |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). |
| Taxonomy: | |
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. |
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| Function: | |
Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). {ECO:0000255|HAMAP- Rule:MF_00022, ECO:0000269|PubMed:11224561, ECO:0000269|PubMed:17161369}. |
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| Catalytic activity: | |
Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L- glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000255|HAMAP- Rule:MF_00022}; |
| Activity regulation: | |
In the absence of bound tRNA, ATP is bound in a non-productive mode, and the enzyme cannot activate amino acids. {ECO:0000269|PubMed:17161369}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=4.7 uM for tRNA-Glu {ECO:0000269|PubMed:11224561}; |
| Subunit: | |
Monomer. {ECO:0000255|HAMAP-Rule:MF_00022, ECO:0000269|PubMed:11224561}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}. |
| Similarity: | |
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP- Rule:MF_00022}. |
Annotations taken from UniProtKB at the EBI.