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Q6AEQ1 (SYE_LEIXX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. 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:Lxx13080
OrganismLeifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]
Taxonomic identifier281090 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia

Protein attributes

Sequence length491 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 – 491491Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119589

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AEQ1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 410F47F79DA30B02

FASTA49154,176
        10         20         30         40         50         60 
MDVRVRFCPS PTGTPHVGMI RTALFNWAYA RHTGGKFLFR IEDTDAARDS EESYGQIIDA 

        70         80         90        100        110        120 
LRWLRLDWDE GVEVGGPHAP YRQSQRSSIY RELIEKLTAS GHIYESFATG EEVEAHNIAL 

       130        140        150        160        170        180 
GRDPKLGYDN FERDLTDAQK AAHRAEGREP ALRLRVPDED LSFDDLVRGE ITFSAGSFSD 

       190        200        210        220        230        240 
FVVVRPNRQP LYTFVNPVDD ALMGVTHVLR GEDLLSSTPR QIALYHALIE TGVTTFVPRF 

       250        260        270        280        290        300 
GHLPYVMGEG NKKLSKRDPE SNLFHHRDRG FIPEGLVNYL TLLGWSLSHD RDVFSIDEMV 

       310        320        330        340        350        360 
AAFDVGDVNP NPARFDQKKA ESINGDHIRL LEVGDFAERT IPYLVAAGVL TEPITETQRA 

       370        380        390        400        410        420 
VLAEAAPLVQ ERVQLLGETP GMLGFLFAEA ASVTIEDDAR ASLPANAGEA LAASIGALEL 

       430        440        450        460        470        480 
VPEAEWAHEA IEATLRDALV ETLGFKPRIA FGPLRVALSG RRVSPPLFES MAILGKAETL 

       490 
ARLVRLSAAL G 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016822 Genomic DNA. Translation: AAT89145.1.
RefSeqYP_062250.1. NC_006087.1.

3D structure databases

ProteinModelPortalQ6AEQ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281090.Lxx13080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT89145; AAT89145; Lxx13080.
GeneID2938719.
KEGGlxx:Lxx13080.
PATRIC22336221. VBILeiXyl11655_1356.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPEGMLNY.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycLXYL281090:GH0X-1239-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_LEIXX
AccessionPrimary (citable) accession number: Q6AEQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: September 13, 2004
Last modified: June 11, 2014
This is version 67 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