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A3NAZ3 (SYE_BURP6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:BURPS668_2487
OrganismBurkholderia pseudomallei (strain 668) [Complete proteome] [HAMAP]
Taxonomic identifier320373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length469 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 ABN84591.1 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 – 469469Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367630

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3NAZ3 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 358E1E438076C433

FASTA46952,147
        10         20         30         40         50         60 
MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDLER STEASVDAIL 

        70         80         90        100        110        120 
EGMAWLGLDY DEGPYYQMQR MDRYREVLAQ MLEKDLVYPC YMSTEELDAL RERQRAAGEK 

       130        140        150        160        170        180 
PRYDGTWRPE PGKVLPEPPA GVTPVLRFRN PLTGSVVWDD AVKGRVEISN EELDDLVIAR 

       190        200        210        220        230        240 
PDGTPTYNFC VVVDDLDMGI THVIRGDDHV NNTPRQINIL RALGGEVPVY AHLPTVLNEQ 

       250        260        270        280        290        300 
GEKMSKRHGA MSVMGYRDAG YLPEAVLNYL ARLGWSHGDA EIFSREQFVE WFDLEHLGKS 

       310        320        330        340        350        360 
PAQYDHNKLN WLNNHYIKEA DDARLAELAK PFFAALGIDA DAIARGPDLV GVMGLMKDRA 

       370        380        390        400        410        420 
STVKEIAENS TMFYRAPAPD AQALAQHVTD AVRPALAEFA AALKTAEWTK EAIAAALKAV 

       430        440        450        460 
LGAHKLKMPQ LAMPVRLLVA GTTHTPSIDA VLLLFGRDVV VSRLAAALA 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 668.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000570 Genomic DNA. Translation: ABN84591.1. Different initiation.
RefSeqYP_001059514.1. NC_009074.1.

3D structure databases

ProteinModelPortalA3NAZ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING320373.BURPS668_2487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN84591; ABN84591; BURPS668_2487.
GeneID4884470.
KEGGbpd:BURPS668_2487.
PATRIC19250741. VBIBurPse82117_2318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBPSE320373:GJ9C-2481-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_BURP6
AccessionPrimary (citable) accession number: A3NAZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 53 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