AC   MF_01446;
DC   Protein; auto
c?   <OC:Archaea>
TR   HAMAP; MF_01446; -; 1; level=0
XX
Names: Kae1
XX
ID   KAE1
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 Kae1;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1;
GN   Name=kae1;
XX
case <OC:Euryarchaeota>
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 a component of the KEOPS complex that is probably
CC       involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely
CC       plays a direct catalytic role in this reaction, but requires other
CC       protein(s) of the complex to fulfill this activity.
CC   -!- SUBUNIT: Monomer. Component of the KEOPS complex that consists of Kae1,
CC       Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
else
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 probably involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC       group of A37.
end case
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; TIGR03722; Arch_KAE1; 1; trigger=no
DR   NCBIfam; TIGR00329; Gcp_kae1; 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: KAE1_PYRAB (Q9UXT7)
FT   BINDING         127..131
FT                   /ligand="substrate"
FT   Condition: x-x-[SA]-G-[GA]
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: H
FT   BINDING         111
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: H
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Optional; Condition: Y
FT   BINDING         285
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   Condition: D
FT   BINDING         159
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         172
FT                   /ligand="substrate"
FT   Optional; Condition: G
FT   BINDING         176
FT                   /ligand="substrate"
FT   Condition: [ED]
FT   BINDING         257
FT                   /ligand="substrate"
FT   Condition: [NS]
XX
Size: 314-363;
Related: MF_01447!;
Template: Q9UXT7; P36132;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Was originally (PubMed:17766251) thought to have endonuclease activity, but it
 could not be confirmed with orthologs purified from M. jannaschii (PubMed:18951093) and
 S. cerevisiae (PubMed:21183954).
 Some Archaea contain a kinase domain in the C-terminus. These sequences are represented in the
 MF_01447 family rule.
XX
# Revision 1.23 2023/06/01
//