HAMAP rule MF_01852
General rule information
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| Accession | MF_01852 |
| Dates | 23-SEP-2008 (Created)
1-JUN-2023 (Last updated, Version 14) |
| Name | TsaC |
| Scope(s) |
Bacteria Betaproteobacteria Gammaproteobacteria |
| Template(s) | P45748 (TSAC_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_01852 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | TSAC |
| Protein name | RecName: Full=Threonylcarbamoyl-AMP synthase; Short=TC-AMP synthase; EC=2.7.7.87; AltName: Full=L-threonylcarbamoyladenylate synthase; AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC; AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC; |
| Gene name | Name=tsaC; |
Comments
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| FUNCTION | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. |
| CATALYTIC ACTIVITY | Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L- threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87; |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the SUA5 family. TsaC subfamily. |
Keywords
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Gene Ontology
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| GO:0005524; Molecular function:ATP binding |
| GO:0016779; Molecular function:nucleotidyltransferase activity |
| GO:0002949; Biological process:tRNA threonylcarbamoyladenosine modification |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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Features
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Additional information
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| Size range | 175-214 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in E.coli, B.subtilis and many other species including fungi and plants (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by TcdA. |