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A8ZWA3 (SYE_DESOH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:Dole_2533
OrganismDesulfococcus oleovorans (strain DSM 6200 / Hxd3) [Complete proteome] [HAMAP]
Taxonomic identifier96561 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfococcus

Protein attributes

Sequence length467 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 – 467467Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367663

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding991Zinc By similarity
Metal binding1011Zinc By similarity
Metal binding1261Zinc By similarity
Metal binding1281Zinc By similarity
Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8ZWA3 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: EC2171A4F6E65327

FASTA46752,586
        10         20         30         40         50         60 
MKQIITRFPP SPTGHLHIGG ARTALFNWLY ARHTGGRFIL RIEDTDVERS TTQSAEGIIK 

        70         80         90        100        110        120 
SLEWLGIDWD EGPYFQSRRM EVYAEYIQRL LASGHAYYCT CSPERLKERR ERALAEGRNP 

       130        140        150        160        170        180 
TYDGTCREKA LPPSDDAVVR FRTPDTGKTV LDDRVKGGIA FDNAEIGDFI IQRSDQTPTY 

       190        200        210        220        230        240 
NFAVVVDDIT MGINTIIRGD DHVTNTPRQI LMYRALDSEL PLFAHVPMVL GRDRSRLSKR 

       250        260        270        280        290        300 
HGAMSVLEYR DTGYLPDGLI NALVRLGWSH GDQEFFTRKE LIELFSLEHI GTSAGVFDPD 

       310        320        330        340        350        360 
KLLAINAEHI KKSDPAALAP HLLPLLKEKG YAAENNDYLH NAIHTLLLRS KTLKEMADKA 

       370        380        390        400        410        420 
AFYYEDPLSY DPAATAKFLV PENMEILEML AEKLATLDSL TEKDQEPAFT AVMEKTGKKF 

       430        440        450        460 
GKIAQPVRVA LTGRTESPGI FETIEALGRR KTLERLADAV EMIKKST 

« Hide

References

[1]"Complete sequence of Desulfococcus oleovorans Hxd3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., 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., Wawrik B., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6200 / Hxd3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000859 Genomic DNA. Translation: ABW68337.1.
RefSeqYP_001530414.1. NC_009943.1.

3D structure databases

ProteinModelPortalA8ZWA3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING96561.Dole_2533.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW68337; ABW68337; Dole_2533.
GeneID5695383.
KEGGdol:Dole_2533.
PATRIC21695223. VBIDesOle35880_2607.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAMGWEVP.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycDOLE96561:GHF3-2569-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_DESOH
AccessionPrimary (citable) accession number: A8ZWA3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 44 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