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HAMAP rule MF_01446

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General rule information [?]

Accession MF_01446
Dates 13-AUG-2007 (Created)
19-NOV-2022 (Last updated, Version 22)
Name Kae1
Scope
Archaea
Templates Q9UXT7 (KAE1_PYRAB); P36132 (KAE1_YEAST): [Recover all]
case <OC:Archaea>
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
KAE1
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 Kae1;
AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1;
Gene name
kae1

Comments [?]

case <OC:Euryarchaeota>
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 a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity.
Subunit Monomer. Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
else
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 probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37.
end case
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: 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;
TIGRFAMs TIGR03722; Arch_KAE1; 1;
TIGR00329; Gcp_kae1; 1;

Features [?]

From: KAE1_PYRAB (Q9UXT7)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     127     131       /ligand="substrate     x-x-[SA]-G-[GA]  
BINDING     107     107       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875     H  
BINDING     111     111       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875     H  
BINDING (Optional)     127     127       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875     Y  
BINDING     285     285       /ligand="Fe cation" /ligand_id="ChEBI:CHEBI:24875     D  
BINDING     159     159       /ligand="substrate     D  
BINDING (Optional)     172     172       /ligand="substrate     G  
BINDING     176     176       /ligand="substrate     [ED]  
BINDING     257     257       /ligand="substrate     [NS]  

Additional information [?]

Size range 314-363 amino acids
Related rules MF_01447 (KAE1B supersedes the current rule)
Fusion 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.