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A8FXE0 (SYE_SHESH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Ssed_2906
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

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

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 – 469469Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000074335

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FXE0 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: F546409068E927C1

FASTA46952,865
        10         20         30         40         50         60 
MTTKTRFAPS PTGFLHVGGA RTALYSWLYA RANQGEFVLR VEDTDIERST PEACEAILEG 

        70         80         90        100        110        120 
MQWLGLNWDE GPYYQTKRFD RYNEIIAQML EQGTAYKCYC SRERIETMRD EQAAKGEQQK 

       130        140        150        160        170        180 
YDGCCRDKAP RDTDEPFVIR FKNPTEGSVV FDDHVRGRIE ISNDLLDDLI IARTEGTPTY 

       190        200        210        220        230        240 
NFCVVVDDWD MGITCVVRGE DHINNTPRQI NILKALGAPI PEYAHVAMIL GDDGAKLSKR 

       250        260        270        280        290        300 
HGAVGVMQYR DDGYLPEALL NYLVRLGWSH GDQEVFSIDE MKQLFKLDDI NKAASAFNTE 

       310        320        330        340        350        360 
KLNWLNQHYI KELDPEYVAK HLEWHMADQK IDTSNGPALS AVVTALSERA KTLKELAASS 

       370        380        390        400        410        420 
RYFYEDFAEF DATAAKKHLR GVAMEPLELV QKKLAELSEW TLEGIHQAIE DTATELEVGM 

       430        440        450        460 
GKVGMPLRVA VTGAGMSPAV DLTLFLVGKA RCEQRISKAI EFVANRINS 

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000821 Genomic DNA. Translation: ABV37513.1.
RefSeqYP_001474641.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FXE0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING425104.Ssed_2906.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV37513; ABV37513; Ssed_2906.
GeneID5610569.
KEGGsse:Ssed_2906.
PATRIC23563529. VBISheSed62411_3091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHYIKELD.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSSED425104:GH7Q-3016-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_SHESH
AccessionPrimary (citable) accession number: A8FXE0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 50 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