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B3E399 (SYE_GEOLS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Glov_0584
OrganismGeobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) [Complete proteome] [HAMAP]
Taxonomic identifier398767 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length466 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 – 466466Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090078

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding991Zinc By similarity
Metal binding1011Zinc By similarity
Metal binding1261Zinc By similarity
Metal binding1281Zinc By similarity
Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3E399 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: A291BDBAB97E99B6

FASTA46652,155
        10         20         30         40         50         60 
MSDLRVRFAP SPTGYLHVGG ARTALFNWLY ARHFGGTFIL RIEDTDTERS TQQSVDAILQ 

        70         80         90        100        110        120 
GMEWLGLDWD EGPFYQTDNF PLYKQHVQKL LDEGKAYRCW CRPEELEAKR EAAMAEGRKP 

       130        140        150        160        170        180 
KYDGTCRHRQ DQPLDQPHVI RFKAPEEGET AFDDLIKGRI AFPNAELDDL IISRTDGTPT 

       190        200        210        220        230        240 
YNFCVVIDDA LMRISHVIRG DDHVNNTPRQ IQLYEALGYP VPIFAHVPMI LGSDKARLSK 

       250        260        270        280        290        300 
RHGATSVIAY RDMGYLPEAL NNYLVRLGWS NGDDEIFSRE EMVQKFDIAN VGRSPSVFNP 

       310        320        330        340        350        360 
DKLNWLNAHY IKTGNPARLA ELLQPHLAGR GVADCSTPDL AGVISTLQER AQTLEEMAER 

       370        380        390        400        410        420 
ALFYYQAPQQ YDEAALSKFD KPHLAAVFSA VAARLSATTA AAAPEFDTLL KEICAEGGWK 

       430        440        450        460 
MPHVGQPLRI ALSGSTQAPG IGEIITALGV NETIARIERA REFLAH 

« Hide

References

[1]"Complete sequence of chromosome of Geobacter lovleyi SZ."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1151 / DSM 17278 / SZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001089 Genomic DNA. Translation: ACD94311.1.
RefSeqYP_001950831.1. NC_010814.1.

3D structure databases

ProteinModelPortalB3E399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398767.Glov_0584.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD94311; ACD94311; Glov_0584.
GeneID6367962.
KEGGglo:Glov_0584.
PATRIC21992851. VBIGeoLov31523_0555.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGLOV398767:GH32-586-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_GEOLS
AccessionPrimary (citable) accession number: B3E399
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: February 19, 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