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A6SX06 (SYE_JANMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:mma_1113
OrganismJanthinobacterium sp. (strain Marseille) (Minibacterium massiliensis) [Complete proteome] [HAMAP]
Taxonomic identifier375286 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeJanthinobacterium

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330976

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif241 – 2455"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2441ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6SX06 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: F6FA1D2BD88EC633

FASTA46351,793
        10         20         30         40         50         60 
MTVRTRFAPS PTGYLHVGGA RTALFSWAYA RHFGGTFVLR IEDTDLERST PEAVQAIIEG 

        70         80         90        100        110        120 
MEWLGLHHDE GPFYQMQRMD RYREVIGQML AAGTAYHCYS SPEEVEAMRE RQRAAGEKPR 

       130        140        150        160        170        180 
YDGTWRPEAG KTLPAIPEGR KPVVRFRNPT EGDVTWLDVV KGSITISNRE LDDLVIARPD 

       190        200        210        220        230        240 
GTPTYNFCVA VDDSDMKITH VIRGDDHVNN TPRQINILQA LGATLPHYGH LPMILGTDGE 

       250        260        270        280        290        300 
KLSKRHGAVS VMDYPAQGYL PEAMLNYLAR LGWSHGDDEV FSMEQFTQWF DLDHLTKSPA 

       310        320        330        340        350        360 
QFNPEKLDWL NNHYIKQADN TRLAGLVRPM MEGLGAQFEN APDLAAVIAL MKERVNTLNE 

       370        380        390        400        410        420 
LAVAAMLFYR QPAADAALLA QHLTDAIRPA LAQYVEQLKT VAWSKEALSA TLKEVLAAHK 

       430        440        450        460 
LKMPQLAMPL RLLITGQLQT PSIDAVVELF GREVVLARLG KNL 

« Hide

References

[1]"Genome analysis of Minibacterium massiliensis highlights the convergent evolution of water-living bacteria."
Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 3:1454-1463(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Marseille.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000269 Genomic DNA. Translation: ABR88734.1.
RefSeqYP_001352803.1. NC_009659.1.

3D structure databases

ProteinModelPortalA6SX06.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING375286.mma_1113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR88734; ABR88734; mma_1113.
GeneID5351703.
KEGGmms:mma_1113.
PATRIC22154659. VBIJanSp106498_1116.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycJSP375286:GJ8U-1132-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_JANMA
AccessionPrimary (citable) accession number: A6SX06
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries