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Q5ZU96 (SYE_LEGPH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:lpg1911
OrganismLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]
Taxonomic identifier272624 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length470 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.

Sequence caution

The sequence AAU27981.1 differs from that shown. Reason: Erroneous initiation.

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 – 470470Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119587

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5ZU96 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 37B2F48A462D198D

FASTA47053,574
        10         20         30         40         50         60 
MTVRTRFAPS PTGFLHVGGV RTALFSWLYA KHHNGQFILR IEDTDRERST QESVQAILDG 

        70         80         90        100        110        120 
MAWLGLNFDE GPYYQTERYA RYQQVAQQLL EEGKAYRCQC SKERLEALRE AQLAAKEKPR 

       130        140        150        160        170        180 
YDGHCRNQSL PDSGIPYVIR FRNPDAGIVS FHDEVYGDIH VDNSELDDLI LVRSDGHPTY 

       190        200        210        220        230        240 
NFAVVIDDWD MKITHVIRGD DHINNTPRQI NLFKALDAPV PVFAHLPMIL GEDGKRLSKR 

       250        260        270        280        290        300 
HGAVSVLQFK ELGVLPHALL NYLVRLGWSH GDQEIFSVQE MITSFDLKNV SRGVSSFNYD 

       310        320        330        340        350        360 
KLYWLNQHYQ KSDSPESVAN ALQWHFEQAG IDLNQGPDLK DLVAVQAERC KSLAEMCQIS 

       370        380        390        400        410        420 
QYFYTDIIEY NEDAVKKHLR PVVLEPLMVL HERLKALDEW KNDKIQECIN DVSLQFDLNL 

       430        440        450        460        470 
GKIAQPLRVA VTGSGTSPSI DMTLALLGKN KSIKRLEDAL EKIRARASVV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017354 Genomic DNA. Translation: AAU27981.1. Different initiation.
RefSeqYP_007567822.1. NC_020521.1.
YP_095928.1. NC_002942.5.

3D structure databases

ProteinModelPortalQ5ZU96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272624.lpg1911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU27981; AAU27981; lpg1911.
GeneID14799971.
3078160.
KEGGlpn:lpg1911.
lpu:LPE509_01279.
PATRIC22330968. VBILegPne29832_1996.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycLPNE272624:GHDI-1910-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_LEGPH
AccessionPrimary (citable) accession number: Q5ZU96
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 71 of the entry and version 2 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