HAMAP rule MF_01428
General rule information
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| Accession | MF_01428 |
| Dates | 14-SEP-2005 (Created)
1-JUN-2023 (Last updated, Version 22) |
| Name | Glu_Q_tRNA_synth |
| Scope(s) |
Bacteria |
| Template(s) | P27305 (GLUQ_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_01428 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | GLUQ |
| Protein name | RecName: Full=Glutamyl-Q tRNA(Asp) synthetase; Short=Glu-Q-RSs; EC=6.1.1.-; |
| Gene name | Name=gluQ; |
Comments
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| FUNCTION | Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon. |
| case <FTGroup:1> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| end case | |
| SIMILARITY | Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. |
Keywords
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| Aminoacyl-tRNA synthetase | |
| ATP-binding | |
| Ligase | |
| Nucleotide-binding | |
| case <FTGroup:1> | |
| Metal-binding | |
| Zinc | |
| end case | |
Gene Ontology
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| GO:0004812; Molecular function:aminoacyl-tRNA ligase activity | |
| case <FTGroup:1> | |
| GO:0008270; Molecular function:zinc ion binding | |
| end case | |
Cross-references
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| PROSITE | PS00178; AA_TRNA_LIGASE_I; 1; |
| Pfam | PF00749; tRNA-synt_1c; 1; |
| PRINTS | PR00987; TRNASYNTHGLU; 1; |
| NCBIfam | TIGR03838; queuosine_YadB; 1; |
Features
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| From: GLUQ_ECOLI (P27305) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 19 | 23 | /ligand="L-glutamate" /ligand_id="ChEBI:CHEBI:29985" |
R-[FLY]-[AS]-P-[ST] | ||||||||
| MOTIF | 22 | 32 | /note="'HIGH' region" | |||||||||
| MOTIF | 238 | 242 | /note="'KMSKS' region" | |||||||||
| BINDING | 111 | 111 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
| BINDING | 113 | 113 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
| BINDING | 125 | 125 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
Y | 1 | |||||||
| BINDING | 129 | 129 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
| BINDING | 55 | 55 | /ligand="L-glutamate" /ligand_id="ChEBI:CHEBI:29985" |
[ED] | ||||||||
| BINDING | 182 | 182 | /ligand="L-glutamate" /ligand_id="ChEBI:CHEBI:29985" |
Y | ||||||||
| BINDING | 200 | 200 | /ligand="L-glutamate" /ligand_id="ChEBI:CHEBI:29985" |
R | ||||||||
| BINDING | 241 | 241 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
K | ||||||||
Additional information
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| Size range | 283-347 amino acids |
| Related rules |
MF_00022 |
| Fusion | Nter: None Cter: None |
| Comments | See: PubMed=16164993; Blaise M., Becker H.D., Lapointe J., Cambillau C., Giege R., Kern D.; "Glu-Q-tRNA(Asp) synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNA(Asp) anticodon."; Biochimie 87:847-861(2005). |