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Q1BHL9 (SYE_BURCA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_1000001878

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022_B
Motif243 – 2475"KMSKS" region HAMAP MF_00022_B

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...

Protein-protein interaction databases

STRINGQ1BHL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4097027.
GenomeReviewsGene locus Bcen_6021 in contig CP000380_GR.
KEGGbcn:Bcen_6021.
PATRIC19056058. VBIBurCen11237_6222.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAANFNDES.
PhylomeDBQ1BHL9.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBCEN331271:BCEN_6021-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 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: January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families