AC   MF_01445;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01445; -; 1; level=0
XX
Names: TsaD
XX
ID   TSAD
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase;
DE            EC=2.3.1.234;
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase;
DE            Short=t(6)A synthase;
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD;
GN   Name=tsaD;
XX
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC       with adenine. Is involved in the transfer of the threonylcarbamoyl
CC       moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC       together with TsaE and TsaB. TsaD likely plays a direct catalytic role
CC       in this reaction.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC         H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 1 Fe(2+) ion per subunit.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family.
XX
DR   PROSITE; PS01016; GLYCOPROTEASE; 1; trigger=no
DR   Pfam; PF00814; Peptidase_M22; 1; trigger=no
DR   PRINTS; PR00789; OSIALOPTASE; 1; trigger=no
DR   NCBIfam; TIGR00329; Gcp_kae1; 1; trigger=no
DR   NCBIfam; TIGR03723; T6A_YgjD; 1; trigger=no
XX
KW   Acyltransferase
KW   Cytoplasm
KW   Iron
KW   Metal-binding
KW   Transferase
KW   tRNA processing
XX
GO   GO:0005506; F:iron ion binding
GO   GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups
GO   GO:0002949; P:tRNA threonylcarbamoyladenosine modification
GO   GO:0005737; C:cytoplasm
XX
FT   From: TSAD_BACSU (O05518)
FT   BINDING         139..143
FT                   /ligand="substrate"
FT   Condition: x-x-S-G-x
FT   BINDING         117
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: H
FT   BINDING         121
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: H
FT   BINDING         307
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: D
FT   BINDING         172
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         185
FT                   /ligand="substrate"
FT   Condition: G
FT   BINDING         189
FT                   /ligand="substrate"
FT   Optional; Condition: [DE]
FT   BINDING         278
FT                   /ligand="substrate"
FT   Condition: N
XX
Size: 233-401;
Related: None;
Template: O05518; P05852; P36175; Q2FWL2;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.24 2023/06/01
//