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Q92F38 (SYE_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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:lin0269
OrganismListeria innocua serovar 6a (strain CLIP 11262) [Complete proteome] [HAMAP]
Taxonomic identifier272626 [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
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_0000119592

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
Q92F38 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: B94060A6A7AC9760

FASTA49156,004
        10         20         30         40         50         60 
MSETKRVRVR YAPSPTGFLH IGNARTALFN YLFARHNDGD FIIRIEDTDA KRNVADGEES 

        70         80         90        100        110        120 
QMKNLKWLGM DWDEGVDVPG KYGPYRQSER QSIYEPLIQQ LLDKGLAYKC YCTEEELEAE 

       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 GVVSADLDQA 

       370        380        390        400        410        420 
ELDWVHKLVS LYHEQMSYGA EIVPLSEMFF ADAESITFDE EEKAVLAEET VPKVISAFKK 

       430        440        450        460        470        480 
ELEALDVLEA AEVKSAIKRV QKETGVKGKG LFMPIRIVTT GEMHGPELPL AIEVLGLEKV 

       490 
LNRLDTWLQN N 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL596164 Genomic DNA. Translation: CAC95502.1.
PIRAF1466.
RefSeqNP_469614.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ92F38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272626.lin0269.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC95502; CAC95502; CAC95502.
GeneID1128683.
KEGGlin:lin0269.
PATRIC20297218. VBILisInn102668_0283.

Organism-specific databases

GenoListLIN0269.
CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAKHYDGDF.
OrthoDBEOG6DRPF7.

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_LISIN
AccessionPrimary (citable) accession number: Q92F38
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 77 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