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HAMAP rule MF_01445

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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;
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 [?]

FUNCTIONRequired 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=;
COFACTOR Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Note=Binds 1 Fe(2+) ion per subunit.;
SIMILARITYBelongs 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 [?]

Pfam PF00814; Peptidase_M22; 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"
BINDING 121 121 /ligand="Fe cation"
BINDING 307 307 /ligand="Fe cation"
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.

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