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Q1BHL9 (SYE_BURCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Bcen_6021
OrganismBurkholderia cenocepacia (strain AU 1054) [Complete proteome] [HAMAP]
Taxonomic identifier331271 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

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.

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_1000001878

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
Q1BHL9 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: C007AC4B7BE25261

FASTA46951,828
        10         20         30         40         50         60 
MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDVER SSQEAVDAIL 

        70         80         90        100        110        120 
EGMQWLGLDF DEGPIYQMQR MDRYREVLAQ MLEKGLAYPC YMSAEELDAL RERQREAGLK 

       130        140        150        160        170        180 
PRYDGTWRPE PGKVLPEPPA GVKPVLRFRN PLTGTVVWDD AVKGRVEISN EELDDLVIAR 

       190        200        210        220        230        240 
PDGTPIYNFC VVVDDMDMGI THVIRGDDHV NNTPRQINIL NALGGEPPVY AHLPTVLNEQ 

       250        260        270        280        290        300 
GEKMSKRHGA MSVMAYRDAG FLPEAVVNYL ARLGWSHGDA EIFSREQFVE WFDLEHLGKS 

       310        320        330        340        350        360 
PAQYDHSKLS WLNAHYIKEA DNARLAELAK PFLDALGIDD AAIATGPALD AVVGLMKDRA 

       370        380        390        400        410        420 
TTVKEIAEGA AMFYRVPAPD ADALAQHVTD AVRPALADLA AALKAADWTK EAVSAALKAT 

       430        440        450        460 
LATHKLKMPQ LAMSVRLLVA GTTHTPSIDA VLVLFGRDVV VTRIEAALA 

« Hide

References

[1]"Complete sequence of chromosome 3 of Burkholderia cenocepacia AU 1054."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AU 1054.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000380 Genomic DNA. Translation: ABF80886.1.
RefSeqYP_625859.1. NC_008062.1.

3D structure databases

ProteinModelPortalQ1BHL9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331271.Bcen_6021.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF80886; ABF80886; Bcen_6021.
GeneID4097027.
KEGGbcn:Bcen_6021.
PATRIC19056058. VBIBurCen11237_6222.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBCEN331271:GHKX-6108-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_BURCA
AccessionPrimary (citable) accession number: Q1BHL9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: February 19, 2014
This is version 59 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