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B1MWU1 (SYE_LEUCK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 43. 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:LCK_00160
OrganismLeuconostoc citreum (strain KM20) [Complete proteome] [HAMAP]
Taxonomic identifier349519 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeLeuconostoc

Protein attributes

Sequence length498 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 – 498498Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090085

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif260 – 2645"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2631ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1MWU1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: E0D092CA3BC44868

FASTA49857,008
        10         20         30         40         50         60 
MTEDIRVRYA PSPTGHLHIG NARTAIFNWL FARHYNGKFI IRIEDTDSAR NIADGEKSQL 

        70         80         90        100        110        120 
ENLAWLGLDW DESPEKPGEY GPYRQSERNE QGIYQPFIDK LLTEGLAYKS YKTSEQLASE 

       130        140        150        160        170        180 
REAQQAAKQA PHYVYEYEGL TREEREAKYA EFEAKGLKPV VRFRVPEEKT YAWDDIVKGH 

       190        200        210        220        230        240 
IEIGAKEVGG DWVIQKADGM PTYNFAVVVD DHMMKISHVL RGDDHVSNTP KQMMIFEALG 

       250        260        270        280        290        300 
WDIPQFGHMA LIINGETGKK LSKRDENVLQ FVEQYKALGY QPQAMVNFIG LLGWSPKGED 

       310        320        330        340        350        360 
EIFSLEEFKQ MFDETRLSKA NAKFDQKKLE WINNQWMRRD LEEIMPQLIQ ELVTANLVSP 

       370        380        390        400        410        420 
ADATAKADWL AQVIKVAGVE GISYTREIVD LVRQPFFELG DITDEMVAYL TSEEGRRVFD 

       430        440        450        460        470        480 
AWESAYIALP DDATAEDYLN AIRGIQNQLE IKGRNLWNPI RIATTHEVQG PNLPEMLVVL 

       490 
DKATVLQTMA DVKSNYLN 

« Hide

References

[1]"Complete genome sequence of Leuconostoc citreum KM20."
Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S., Lee S., Park H.-S., Park Y.-H., Oh T.K.
J. Bacteriol. 190:3093-3094(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KM20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ489736 Genomic DNA. Translation: ACA81993.1.
RefSeqYP_001727437.1. NC_010471.1.

3D structure databases

ProteinModelPortalB1MWU1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349519.LCK_00160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA81993; ACA81993; LCK_00160.
GeneID6063132.
KEGGlci:LCK_00160.
PATRIC32613549. VBILeuCit37309_0277.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAKLEWYNG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycLCIT349519:GHNF-163-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_LEUCK
AccessionPrimary (citable) accession number: B1MWU1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 43 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