Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B1YSK3 (SYE_BURA4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:BamMC406_1958
OrganismBurkholderia ambifaria (strain MC40-6) [Complete proteome] [HAMAP]
Taxonomic identifier398577 [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_1000090055

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
B1YSK3 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 8FC7E30A175950E4

FASTA46951,865
        10         20         30         40         50         60 
MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDVER SSQEAVDAIL 

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

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

       190        200        210        220        230        240 
PDGTPIYNFC VVVDDMDMNI THVIRGDDHV NNTPRQINIL RALGGEPPVY AHLPTVLNEQ 

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

       310        320        330        340        350        360 
PAQYDHSKLS WLNAHYIKEA DNARLAALAK PFLDALGIED AAIATGPALD AVVGLMKDRA 

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

       430        440        450        460 
LGTHKLKMPQ LAMPVRLLVA GTTHTPSIDA VLVLFGRDVV VSRIEAALA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A. expand/collapse author list , Ramette A., Konstantinidis K., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC40-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001025 Genomic DNA. Translation: ACB64439.1.
RefSeqYP_001808655.1. NC_010551.1.

3D structure databases

ProteinModelPortalB1YSK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398577.BamMC406_1958.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB64439; ACB64439; BamMC406_1958.
GeneID6178543.
KEGGbac:BamMC406_1958.
PATRIC19033392. VBIBurAmb82852_2008.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAKHYDGDF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBAMB398577:GH38-2014-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_BURA4
AccessionPrimary (citable) accession number: B1YSK3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 42 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