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A1RI52 (SYE_SHESW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:Sputw3181_1509
OrganismShewanella sp. (strain W3-18-1) [Complete proteome] [HAMAP]
Taxonomic identifier351745 [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_1000001964

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
A1RI52 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0DB28570C88C4F7A

FASTA46952,671
        10         20         30         40         50         60 
MTTKTRFAPS PTGFLHVGGA RTALYSWLQA RANNGEFVLR IEDTDIERST QAACDAILEG 

        70         80         90        100        110        120 
MNWLGLTWDE GPYYQTKRFD RYNEIIAQML EKGTAYKCYC SRERIDALRE SQAANGEAQK 

       130        140        150        160        170        180 
YDGCCRDLPA RDTDEPFVVR FKNPIGGSVV FDDHVRGRIE FSNDALDDLI IARTDGVPTY 

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

       250        260        270        280        290        300 
HGAVSVMQYR DDGYLPEALL NYLVRLGWSH GDQEVFSLEE MKQYFKLDDI NKAPSAFNTD 

       310        320        330        340        350        360 
KLVWLNQHYI KTLDPEYVAT HLQWHMDDQK IDTSNGPALA EVVTALAERA KTLKELAASS 

       370        380        390        400        410        420 
RYFYEDFADF DAEQAKKHLR GVALEPLQLV QQKLAALTEW TVEAIHQAIE QTATELDVGM 

       430        440        450        460 
GKVGMPLRVS VTGAGQSPGL DITLFLIGRS RSEQRISKAI EFVADRINS 

« Hide

References

[1]"Complete sequence of Shewanella sp. W3-18-1."
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., Tiedje J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W3-18-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000503 Genomic DNA. Translation: ABM24347.1.
RefSeqYP_962901.1. NC_008750.1.

3D structure databases

ProteinModelPortalA1RI52.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351745.Sputw3181_1509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM24347; ABM24347; Sputw3181_1509.
GeneID4658801.
KEGGshw:Sputw3181_1509.
PATRIC23596589. VBISheSp103602_1570.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSSP351745:GCOY-1557-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_SHESW
AccessionPrimary (citable) accession number: A1RI52
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 56 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