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Q1MBL0 (SYE_RHIL3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:RL4184
OrganismRhizobium leguminosarum bv. viciae (strain 3841) [Complete proteome] [HAMAP]
Taxonomic identifier216596 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length488 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 – 488488Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001947

Regions

Motif16 – 2611"HIGH" region HAMAP-Rule MF_00022
Motif257 – 2615"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2601ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1MBL0 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: D578ECDF275354D8

FASTA48854,802
        10         20         30         40         50         60 
MTVSGTATGV RVRIAPSPTG EPHVGTAYIA LFNYLFAKKH GGEFILRIED TDATRSTPEF 

        70         80         90        100        110        120 
ETKVLDALKW CGLEWKEGPD IGGPYGPYRQ SDRKDMYQPY AQELLEKGHA FRCFCTPARL 

       130        140        150        160        170        180 
EQMRETQRAA GKPPKYDGLC LNLAAEEVTS RMAAGETTVI RMKIPTEGSC DFTDGVYGEV 

       190        200        210        220        230        240 
SIPWDSVDMQ VLVKADGMPT YHMANVIDDH LMKITHVARG EEWLASVPKH ILLYRYFGWD 

       250        260        270        280        290        300 
QPVFMHLSLM RNADKSKLSK RKNPTSISYY SALGYIPEAL MNFLGLFFIQ IAEGEELLTM 

       310        320        330        340        350        360 
DELSEKFDPE NLSKAGAIFD IQKLDWLNGR WIREKLSEEE FQARVLTWAM ENDRLKEGLR 

       370        380        390        400        410        420 
LSQTRISKLG ELPDLAGFLL KSDLGLQPSD FAKIKSPPEE ILEILNTVQP DLEKILEWNV 

       430        440        450        460        470        480 
ETIEAELRAI ADRMGKKLKV VVSPLFVAVS GSSRSLPLFD SMAILGRSVV RQRLKLASQA 


VAALVGSK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM236080 Genomic DNA. Translation: CAK09673.1.
RefSeqYP_769759.1. NC_008380.1.

3D structure databases

ProteinModelPortalQ1MBL0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216596.RL4184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK09673; CAK09673; RL4184.
GeneID4402932.
KEGGrle:RL4184.
PATRIC23145201. VBIRhiLeg32091_5511.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycRLEG216596:GKE5-4252-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_RHIL3
AccessionPrimary (citable) accession number: Q1MBL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 61 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