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

A8YTD2 (SYE_LACH4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:lhv_0369
OrganismLactobacillus helveticus (strain DPC 4571) [Complete proteome] [HAMAP]
Taxonomic identifier405566 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length499 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 – 499499Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000070999

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8YTD2 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 961D72B0647745D4

FASTA49957,622
        10         20         30         40         50         60 
MAKEKIRVRY APSPTGHLHI GNARTALFNY LFARHNKGTM VLRIEDTDQK RNVKGGSKSQ 

        70         80         90        100        110        120 
MENLHWLGID WDEGPDKGGD YGPYRQSERK EIYQKYIDQL IDEGKAYYSY KTEEELEAQR 

       130        140        150        160        170        180 
EEQRAMGVAP HYTYEYEGMT ADEIKQAQDE AKAKGLKPVV RIHIPEMETY SWDDIVKGHL 

       190        200        210        220        230        240 
EFESDTIGGD FVIQKRDGMP TYNFAVVIDD HLMKITHVLR GDDHVSNTPK QLVVYEALGW 

       250        260        270        280        290        300 
EPPKFGHMTL IINSETGKKL SKRDESVLQF IEQYRDLGYL PEAMFNFITL LGWSPKGENE 

       310        320        330        340        350        360 
IFNKREFIKQ FDPARLSKSP AAFDQKKLEW INNQYIKKAD RDTLLDLALN NLQEAGLVDE 

       370        380        390        400        410        420 
HPTPEKMEWI RQLVNIYSIQ MSYTKQIVDM AKIFFEEAKD LSDEEIEEIK NDDGRGVIEE 

       430        440        450        460        470        480 
FKKQLDLIPR FTSVQIMNAI QATRKATGVK GRKLFMPIRI ATTRSMVGPG IGEAMELLGK 

       490 
KRVVEHIDLT LKQMSENNL 

« Hide

References

[1]"Genome sequence of Lactobacillus helveticus: an organism distinguished by selective gene loss and IS element expansion."
Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K., McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F., Beresford T., Ross R.P.
J. Bacteriol. 190:727-735(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DPC 4571.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000517 Genomic DNA. Translation: ABX26588.1.
RefSeqYP_001576879.1. NC_010080.1.

3D structure databases

ProteinModelPortalA8YTD2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405566.lhv_0369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX26588; ABX26588; lhv_0369.
GeneID5772441.
KEGGlhe:lhv_0369.
PATRIC22232761. VBILacHel91643_0383.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLHEL405566:GJEN-330-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_LACH4
AccessionPrimary (citable) accession number: A8YTD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 41 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