Reviewed,
UniProtKB/Swiss-Prot Q2LQN4 (SYE1_SYNAS)
Last modified
June 16, 2009.
Version 22.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutamyl-tRNA synthetase 1 EC=6.1.1.17 Alternative name(s): Glutamate--tRNA ligase 1 Short name=GluRS 1 | ||||||
| Gene names |
| ||||||
| Organism | Syntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 56780 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Deltaproteobacteria › Syntrophobacterales › Syntrophaceae › Syntrophus |
Protein attributes
| Sequence length | 472 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. |
| Catalytic activity | ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the class-I aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Metal-binding Nucleotide-binding Zinc |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-tRNA ligase activityInferred from electronic annotation. Source: HAMAP 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 – 472 | 472 | Glutamyl-tRNA synthetase 1 HAMAP MF_00022 | PRO_0000237413 | |||||
Regions | |||||||||
| Motif | 13 – 23 | 11 | "HIGH" region HAMAP MF_00022 | ||||||
| Motif | 239 – 243 | 5 | "KMSKS" region HAMAP MF_00022 | ||||||
Sites | |||||||||
| Metal binding | 102 | 1 | Zinc By similarity | ||||||
| Metal binding | 104 | 1 | Zinc By similarity | ||||||
| Metal binding | 129 | 1 | Zinc By similarity | ||||||
| Metal binding | 131 | 1 | Zinc By similarity | ||||||
| Binding site | 242 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential." Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000252 Genomic DNA. Translation: ABC76071.1. | |
| RefSeq | YP_460239.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3884491. |
| GenomeReviews | Gene locus SYNAS_01920 in contig CP000252_GR. |
| KEGG | sat:SYN_02557. |
| NMPDR | fig|56780.10.peg.190. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q2LQN4. |
| OMA | Q2LQN4. MAHIPLI. |
Enzyme and pathway databases | |
| BioCyc | SACI56780:SYN_02557-MON. |
Family and domain databases | |
| HAMAP | MF_00022. [Tree] |
| InterPro | IPR008925. aa-tRNA-synth_I_codon-bd. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-synth_Ic_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ic. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit. |
| PANTHER | PTHR10119. Glu_tRNA-synt_1c. 1 hit. |
| TIGRFAMs | TIGR00464. gltX_bact. 1 hit. |
| PROSITE | PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYE1_SYNAS | ||||||||
| Accession | Primary (citable) accession number: Q2LQN4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


