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UniProt functional annotation for Q5SM28 | ||
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| UniProt code: Q5SM28. |
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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 proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine. {ECO:0000269|PubMed:12013438, ECO:0000269|PubMed:12130657}. |
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| Catalytic activity: | |
Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl- tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA- COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039, ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215; EC=6.1.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01571, ECO:0000269|PubMed:12013438, ECO:0000269|PubMed:12130657}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.15 mM for proline (at 60 degrees Celsius) {ECO:0000269|PubMed:12130657}; KM=0.02 mM for cysteine (at 60 degrees Celsius) {ECO:0000269|PubMed:12130657}; |
| Subunit: | |
Homodimer. Only one tRNA molecule binds per dimer. {ECO:0000269|PubMed:10970866, ECO:0000269|PubMed:11399074}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01571}. |
| Domain: | |
Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension. The C-terminal extension binds a zinc ion, which probably plays a non-essential structural role in stabilizing the fold of C-terminal domain. |
| Similarity: | |
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571, ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.