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Q5LXZ7 (SYE_STRT1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:str1814
OrganismStreptococcus thermophilus (strain CNRZ 1066) [Complete proteome] [HAMAP]
Taxonomic identifier299768 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length484 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 – 484484Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119671

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif255 – 2595"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LXZ7 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 9EEC854C0ECF93F1

FASTA48455,354
        10         20         30         40         50         60 
MAKDIRVRYA PSPTGLLHIG NARTALFNYL YARHHGGTFI IRIEDTDRKR HVEDGERSQL 

        70         80         90        100        110        120 
DNLRWLGIDW DESPETHENY RQSERLPLYQ KYIDQLLAEG KAYKSYVTEE ELAAERERQE 

       130        140        150        160        170        180 
AAGETPRYIN EFLGMTEEEK AAYIAEREAA GIIPTVRLAV NESGIYKWHD IVKGDIEFEG 

       190        200        210        220        230        240 
GNIGGDWVIQ KRDGYPTYNF AVVVDDHDMQ ISHVIRGDDH IANTPKQLMV YEALGWEAPE 

       250        260        270        280        290        300 
FGHMTLITNS ETGKKLSKRD TNTLQFIEDY RKKGYLPEAV FNFIALLGWN PGGEDEIFSR 

       310        320        330        340        350        360 
EELIKLFDEN RLSKSPAAFD QKKLDWMSND YIKHADFDKV FALCKPFLEE AGRLTDKAEK 

       370        380        390        400        410        420 
LVELYKPQMT AAEEIVPLTD LFFEDFPELT AAEKEVMAGE TVPTVLEAFK AKLEAMSDDE 

       430        440        450        460        470        480 
FVTENIFSQI KAVQKETGIK GKNLFMPIRI AVSGEMHGPE LPETIFLLGR EKSIKHIDQV 


LATL 

« Hide

References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNRZ 1066.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000024 Genomic DNA. Translation: AAV63330.1.
RefSeqYP_142145.1. NC_006449.1.

3D structure databases

ProteinModelPortalQ5LXZ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING299768.str1814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV63330; AAV63330; str1814.
GeneID3167194.
KEGGstc:str1814.
PATRIC19796707. VBIStrThe135799_1797.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSTHE299768:GHWB-1791-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_STRT1
AccessionPrimary (citable) accession number: Q5LXZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 63 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