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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. tRNA binding Source: InterPro

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-2021-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:lpl1875
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517 Componenti: Chromosome

Organism-specific databases

LegioListilpl1875.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Glutamate--tRNA ligasePRO_0000119588Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi297245.lpl1875.

Structurei

3D structure databases

ProteinModelPortaliQ5WVE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi9 – 1911"HIGH" regionAdd
BLAST
Motifi236 – 2405"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
OMAiIQECIND.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5WVE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVRTRFAPS PTGFLHVGGV RTALFSWLYA KHHNGQFILR IEDTDRERST
60 70 80 90 100
QESVQAILDG MAWLGLNFDE GPYYQTERYA RYQQVAQQLL EEGKAYRCQC
110 120 130 140 150
SKERLEALRE AQLAAKEKPR YDGHCRNQSL PDSGIPYVIR FRNPDGGIVS
160 170 180 190 200
FHDEVYGDIH VDNSELDDLI LVRSDGHPTY NFAVVIDDWD MKITHVIRGD
210 220 230 240 250
DHINNTPRQI NLFKALDAPV PVFAHLPMIL GEDGKRLSKR HGAVSVLQFK
260 270 280 290 300
ELGVLPHALL NYLVRLGWSH GDQEIFSVQE MITSFDLKNV SRGVSSFNYD
310 320 330 340 350
KLYWLNQHYQ KSDSPESVAN ALQWHFEQAG IDLNQGPDLK DLVAVQAERC
360 370 380 390 400
KSLAEMCQIS QYFYTDTIEY NEDAVKKHLR PVVLEPLMVL HERLKALDEW
410 420 430 440 450
KNDKIQECIN DVSLQFDLNL GKIAQPLRVA VTGSGTSPSI DMTLALLGKN
460 470
KSIKRLEDAL EKIRARASVV
Length:470
Mass (Da):53,548
Last modified:November 22, 2004 - v1
Checksum:iEACE7D81A3A3DBBC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH16114.1.
RefSeqiYP_127213.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH16114; CAH16114; lpl1875.
KEGGilpf:lpl1875.
PATRICi22317493. VBILegPne33733_2064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH16114.1.
RefSeqiYP_127213.1. NC_006369.1.

3D structure databases

ProteinModelPortaliQ5WVE0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi297245.lpl1875.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH16114; CAH16114; lpl1875.
KEGGilpf:lpl1875.
PATRICi22317493. VBILegPne33733_2064.

Organism-specific databases

LegioListilpl1875.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
OMAiIQECIND.
OrthoDBiEOG6DRPF7.

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-2021-MONOMER.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiSYE_LEGPL
AccessioniPrimary (citable) accession number: Q5WVE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2005
Last sequence update: November 22, 2004
Last modified: March 31, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.