Home  |  Contact
Annotation rule MF_01445
Send feedback

General rule information [?]

Accession MF_01445
Dates 13-AUG-2007 (Created)
19-NOV-2019 (Last updated, Version 19)
Name TsaD
Scope
Bacteria
Templates O05518 (TSAD_BACSU); P05852 (TSAD_ECOLI); P36175 (TSAD_MANHA); Q2FWL2 (TSAD_STAA8): [Recover all]
case <OC:Bacteria>
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
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 RHEA:37059: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
EC 2.3.1.234
Cofactor Fe(2+)
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: transferase activity, transferring acyl 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;
TIGRFAMs TIGR00329; Gcp_kae1; 1;
TIGR03723; T6A_YgjD; 1;

Features [?]

From: TSAD_BACSU (O05518)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     139     143       Substrate binding     x-x-S-G-x  
METAL     117     117       Iron     H  
METAL     121     121       Iron     H  
METAL     307     307       Iron     D  
BINDING     172     172       Substrate     D  
BINDING     185     185       Substrate; via amide nitrogen     G  
BINDING (Optional)     189     189       Substrate     [DE]  
BINDING     278     278       Substrate     N  

Additional information [?]

Size range 233-401 amino acids
Related rules None
Fusion 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.