HAMAP rule MF_01445
General rule information
[?]
Accession | MF_01445 |
Dates | 13-AUG-2007 (Created)
1-JUN-2023 (Last updated, Version 24) |
Name | TsaD |
Scope(s) |
Bacteria |
Template(s) | O05518 (TSAD_BACSU); P05852 (TSAD_ECOLI); P36175 (TSAD_MANHA); Q2FWL2 (TSAD_STAA8); [ Recover all ] |
Triggered by |
case c? <OC:Bacteria>
HAMAP; MF_01445 (Get profile general information and statistics) end case
|
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Identifier | TSAD |
Protein name | RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase; EC=2.3.1.234; AltName: Full=N6-L-threonylcarbamoyladenine synthase; Short=t(6)A synthase; AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD; AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD; |
Gene name | Name=tsaD; |
Comments
[?]
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. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. |
CATALYTIC ACTIVITY | Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; |
COFACTOR | Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Note=Binds 1 Fe(2+) ion per subunit.; |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the KAE1 / TsaD family. |
Keywords
[?]
Gene Ontology
[?]
GO:0005506; Molecular function:iron ion binding |
GO:0016747; Molecular function:acyltransferase activity, transferring groups other than amino-acyl groups |
GO:0002949; Biological process:tRNA threonylcarbamoyladenosine modification |
GO:0005737; Cellular component:cytoplasm |
Cross-references
[?]
PROSITE | PS01016; GLYCOPROTEASE; 1; |
Pfam | PF00814; Peptidase_M22; 1; |
PRINTS | PR00789; OSIALOPTASE; 1; |
NCBIfam | TIGR00329; Gcp_kae1; 1; |
NCBIfam | TIGR03723; T6A_YgjD; 1; |
Features
[?]
From: TSAD_BACSU (O05518) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 139 | 143 | /ligand="substrate" | x-x-S-G-x | ||||||||
BINDING | 117 | 117 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" |
H | ||||||||
BINDING | 121 | 121 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" |
H | ||||||||
BINDING | 307 | 307 | /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875" |
D | ||||||||
BINDING | 172 | 172 | /ligand="substrate" | D | ||||||||
BINDING | 185 | 185 | /ligand="substrate" | G | ||||||||
BINDING | 189 | 189 | /ligand="substrate" | [DE] | ||||||||
BINDING | 278 | 278 | /ligand="substrate" | N |
Additional information
[?]
Size range | 233-401 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. |