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UniProt functional annotation for O67323 | ||
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| UniProt code: O67323. |
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| Organism: | |
Aquifex aeolicus (strain VF5). |
| Taxonomy: | |
Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. |
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| Function: | |
Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. {ECO:0000255|HAMAP-Rule:MF_00036}. |
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| Catalytic activity: | |
Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl- tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA- COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00036}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00036}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00036}; |
| Subcellular location: | |
Cytoplasm. |
| Domain: | |
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The Aquifex aeolicus domain can be used in vitro to replace the corresponding domain in E.coli. {ECO:0000255|HAMAP- Rule:MF_00036, ECO:0000269|PubMed:19661429}. |
| Similarity: | |
Belongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000255|HAMAP-Rule:MF_00036}. |
Annotations taken from UniProtKB at the EBI.