Reviewed,
UniProtKB/Swiss-Prot Q8G4X3 (GLUQ_BIFLO)
Last modified
January 19, 2010.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutamyl-Q tRNA(Asp) synthetase Short name=Glu-Q-RSs EC=6.1.1.- | ||||
| Gene names |
| ||||
| Organism | Bifidobacterium longum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216816 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium |
Protein attributes
| Sequence length | 379 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| 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 By similarity. HAMAP MF_01428 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_01428 |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | tRNA aminoacylation for protein translation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW aminoacyl-tRNA ligase activityInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 379 | 379 | Glutamyl-Q tRNA(Asp) synthetase HAMAP MF_01428 | PRO_0000208287 | |||||
Regions | |||||||||
| Region | 14 – 18 | 5 | Glutamate binding By similarity | ||||||
| Motif | 17 – 27 | 11 | "HIGH" region HAMAP MF_01428 | ||||||
| Motif | 300 – 304 | 5 | "KMSKS" region HAMAP MF_01428 | ||||||
Sites | |||||||||
| Metal binding | 106 | 1 | Zinc By similarity | ||||||
| Metal binding | 108 | 1 | Zinc By similarity | ||||||
| Metal binding | 128 | 1 | Zinc By similarity | ||||||
| Metal binding | 132 | 1 | Zinc By similarity | ||||||
| Binding site | 50 | 1 | Glutamate By similarity | ||||||
| Binding site | 229 | 1 | Glutamate By similarity | ||||||
| Binding site | 247 | 1 | Glutamate By similarity | ||||||
| Binding site | 303 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014295 Genomic DNA. Translation: AAN25052.1. |
| RefSeq | NP_696416.1. |
3D structure databases | |
| SMR | Q8G4X3. Positions 10-324, 11-353. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1022750. |
| GenomeReviews | Gene locus BL1251 in contig AE014295_GR. |
| KEGG | blo:BL1251. |
| NMPDR | fig|206672.1.peg.1183. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG628189. |
| OMA | DAPSSYH. |
| PhylomeDB | Q8G4X3. |
Enzyme and pathway databases | |
| BioCyc | BLON206672:BL1251-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01428. Glu_Q_tRNA_synth. Divergent sequence. [Tree] |
| InterPro | IPR000924. Glu/Gln-tRNA-synth_Ic. IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom. IPR020060. Glu/Gln-tRNA-synth_Ic_N. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| PANTHER | PTHR10119. Glu_tRNA-synt_1c. 1 hit. |
| Pfam | PF00749. tRNA-synt_1c. 2 hits. [Graphical view] |
| PRINTS | PR00987. TRNASYNTHGLU. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLUQ_BIFLO | ||||||||
| Accession | Primary (citable) accession number: Q8G4X3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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