Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7N6Y2 (SYE_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:plu1401
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length472 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 – 472472Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119620

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif238 – 2425"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding991Zinc By similarity
Metal binding1011Zinc By similarity
Metal binding1261Zinc By similarity
Metal binding1281Zinc By similarity
Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N6Y2 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 9BD312D42D52E319

FASTA47253,783
        10         20         30         40         50         60 
MSKIKTRFAP SPTGYLHVGG ARTALYSWLY SRHNKGEFVL RIEDTDLERS TQEAINAIMD 

        70         80         90        100        110        120 
GMNWLNLNWD EGPYYQTKRF DRYNQAIDQM LEQGNAYRCY CSKEHLEALR ETQMANGEKP 

       130        140        150        160        170        180 
RYDGRCRDNP CQHDPAQPHV VRFRNPQEGS VIFNDQIRGP IEFSNQELDD LIIRRTDGSP 

       190        200        210        220        230        240 
TYNFCVVIDD WDMEITHVIR GEDHINNTPR QINILKALGA PVPEYAHVSM ILGDDGKKLS 

       250        260        270        280        290        300 
KRHGAVSVMQ YRDDGYLPEA LLNYLVRLGW SHGDQEIFSI EEMTELFSLD AINKSASAFN 

       310        320        330        340        350        360 
TEKLQWLNHH YINTLPPEKV AVHLAWHIEQ QGIDSRNGPQ LVDLIKLLGE RCKTLKEMAE 

       370        380        390        400        410        420 
SCRYFYEDFA EFDADAAKKH LRPVARQPLE VVHAKLASIT DWTPENVHHA IQSTADELEV 

       430        440        450        460        470 
GMGKVGMPLR VAATGAGQSP GVDVTIHAIG QPRTLSRINQ ALEFIAQRET QS 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571863 Genomic DNA. Translation: CAE13694.1.
RefSeqNP_928701.1. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N6Y2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243265.plu1401.

Proteomic databases

PRIDEQ7N6Y2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE13694; CAE13694; plu1401.
GeneID2801381.
KEGGplu:plu1401.
PATRIC20506593. VBIPhoLum48522_1554.

Organism-specific databases

GenoListplu1401.
CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

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_PHOLL
AccessionPrimary (citable) accession number: Q7N6Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 70 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