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B5R3U6 (SYE_SALEP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:SEN2399
OrganismSalmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP]
Taxonomic identifier550537 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length471 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090102

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B5R3U6 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: CA4A0E377511292F

FASTA47153,674
        10         20         30         40         50         60 
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RHHGGEFVLR IEDTDLERST PEAIEAIMDG 

        70         80         90        100        110        120 
MNWLNLEWDE GPYFQTKRFD RYNAVIDEML EAGTAYKCYC SKERLEQLRE EQMAKGEKPR 

       130        140        150        160        170        180 
YDGRCRHSYE HHADDEPCVV RFANPQDGSV IFDDQIRGPI EFSNQELDDL IIRRTDGSPT 

       190        200        210        220        230        240 
YNFCVVVDDW DMEITHVIRG EDHINNTPRQ INILKALNAP VPMYAHVSMI NGDDGKKLSK 

       250        260        270        280        290        300 
RHGAVSVMQY RDDGYLPEAL LNYLVRLGWS SGDQEIFTRE EMIKLFSLGA VSKSASAFNT 

       310        320        330        340        350        360 
DKLLWLNHHY INTLAPEYVA THLQWHIEQE NIDTRNGPQL AELVKLLGER CKTLKEMAQS 

       370        380        390        400        410        420 
CRYFYEDFSE FDADAAKKHL RPVARQPLEV VRDKLSAITD WSAENVHHAI QATADELEVG 

       430        440        450        460        470 
MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK TRSIERINKA LGFIAERESQ Q 

« Hide

References

[1]"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P125109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM933172 Genomic DNA. Translation: CAR33985.1.
RefSeqYP_002244483.1. NC_011294.1.

3D structure databases

ProteinModelPortalB5R3U6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING550537.SEN2399.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR33985; CAR33985; SEN2399.
PATRIC32335331. VBISalEnt14964_2436.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSENT550537:GJFI-2433-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_SALEP
AccessionPrimary (citable) accession number: B5R3U6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: June 11, 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