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Q8YAB3 (SYE_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:lmo0237
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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_0000119594

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif254 – 2585"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1101Zinc By similarity
Metal binding1121Zinc By similarity
Metal binding1371Zinc By similarity
Metal binding1391Zinc By similarity
Binding site2571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YAB3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 7A1744ED14F62FE6

FASTA49156,036
        10         20         30         40         50         60 
MSETKRVRVR YAPSPTGFLH IGNARTALFN YLFARHNDGD FIIRIEDTDA KRNIADGEES 

        70         80         90        100        110        120 
QMTNLKWLGM DWDEGVDVPG KYGPYRQSER QSIYEPLIQE LLDKDLAYKC YCTEEELDAE 

       130        140        150        160        170        180 
REKQKANGEM PRYSGKCRHL TKEQQAEKEA QGFKPSIRFK VPANETITFN DMVKDDVSFE 

       190        200        210        220        230        240 
SNGIGDFVIA KKDGIPTYNF AVAVDDHLME ISHVLRGDDH ISNTPKQILI YNAFGWEPPI 

       250        260        270        280        290        300 
FGHMTLIVNE SRRKLSKRDG SIIQFIEQYR DLGYLPEALF NFIAMLGWSP EGEEEIFSKE 

       310        320        330        340        350        360 
EFIKMFDPKR LSKSPALFDN VKLTWVNNQY VKKLPLNDVV ELSLPHLQKA GVVSAELNQA 

       370        380        390        400        410        420 
ELDWVHKLVS LYHEQMSYGA EIVPLSEMFF ADAESITFDE EETAVLAEET VPTVISAFKK 

       430        440        450        460        470        480 
ELEALEVLEA AEVKAAIKRV QKETGVKGKG LFMPIRIVTT GEMHGPELPL AIEVLGREKV 

       490 
LNRLDTWLKN N 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591974 Genomic DNA. Translation: CAD00764.1.
PIRAF1104.
RefSeqNP_463768.1. NC_003210.1.

3D structure databases

ProteinModelPortalQ8YAB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo0237.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD00764; CAD00764; CAD00764.
GeneID987229.
KEGGlmo:lmo0237.
PATRIC20309518. VBILisMon69206_0245.

Organism-specific databases

GenoListLMO0237.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLMON169963:LMO0237-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_LISMO
AccessionPrimary (citable) accession number: Q8YAB3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 75 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