HAMAP rule MF_01446
General rule information
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PURL | https://purl.expasy.org/hamap/rule/MF_01446 |
Accession | MF_01446 |
Dates | 13-AUG-2007 (Created)
8-OCT-2024 (Last updated, Version 25) |
Name | Kae1 |
Scope(s) |
Archaea |
Template(s) | Q9UXT7 (KAE1_PYRAB); P36132 (KAE1_YEAST); [ Recover all ] |
Triggered by |
case c? <OC:Archaea>
HAMAP; MF_01446 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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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 | Name=kae1; |
Comments
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case <OC:Methanobacteriati> | |
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 | Reaction=L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L- threonylcarbamoyladenosine(37) in tRNA + AMP + H(+); 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=2.3.1.234; |
COFACTOR | Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Note=Binds 1 Fe(2+) ion per subunit.; |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the KAE1 / TsaD family. |
Keywords
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Gene Ontology
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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
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PROSITE | PS01016; GLYCOPROTEASE; 1; |
Pfam | PF00814; Peptidase_M22; 1; |
PRINTS | PR00789; OSIALOPTASE; 1; |
NCBIfam | TIGR03722; Arch_KAE1; 1; |
NCBIfam | TIGR00329; Gcp_kae1; 1; |
Features
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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 | 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 | 172 | 172 | /ligand="substrate" | G | ||||||||
BINDING | 176 | 176 | /ligand="substrate" | [ED] | ||||||||
BINDING | 257 | 257 | /ligand="substrate" | [NS] |
Additional information
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Size range | 314-363 amino acids |
Related rules |
MF_01447 |
Fusion | Nter: None Cter: 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. |