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A5G3W1 (SYE_GEOUR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Gura_2300
OrganismGeobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens) [Complete proteome] [HAMAP]
Taxonomic identifier351605 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

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_1000074322

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
A5G3W1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 05707FF432C9649B

FASTA46752,510
        10         20         30         40         50         60 
MTEVRLRFAP SPTGYLHVGG ARTALFNWLL ARKQKGTFIL RIEDTDVARS TQESVDAILQ 

        70         80         90        100        110        120 
GMEWLGLDWD EGPYYQSDRF PVYKEFVQKL LDSGKAYKCY CTPEELEAKR EQALMDGRKP 

       130        140        150        160        170        180 
KYDGTCRELA GDVPGKPHVV RFRAPHEGVT AFDDLIKGRI AFNNDELDDL IIQRSDGTPT 

       190        200        210        220        230        240 
YNFVVVIDDA TMGITTVIRG DDHVNNTPRQ ILLYEALGYP VPHFAHVPMI LGADKARLSK 

       250        260        270        280        290        300 
RHGATGVMAY RDMGYLPEAL VNYLVRLGWS FGDEEIFSKE DLIEKFSIEQ VGRSAGVFNP 

       310        320        330        340        350        360 
DKLLWLNAHY IKTGDPSRLA GLLVPFLRER GVDPTGGPDL VAVVKTLQER SRTLLEMADG 

       370        380        390        400        410        420 
ALFYFRRDFS YDEKAVEKFL TPEVSPLYEL LIAKFASSAD FTHQSIEQIF KEICEEKGLK 

       430        440        450        460 
LGQVAQPARI ALCGGTVAPS IFEVMEVLGK EETNLRLEKA LAFVRRG 

« Hide

References

[1]"Complete sequence of Geobacter uraniireducens Rf4."
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., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M., Lovley D., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Rf4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000698 Genomic DNA. Translation: ABQ26479.1.
RefSeqYP_001231052.1. NC_009483.1.

3D structure databases

ProteinModelPortalA5G3W1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351605.Gura_2300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ26479; ABQ26479; Gura_2300.
GeneID5165291.
KEGGgur:Gura_2300.
PATRIC22034766. VBIGeoUra13052_2449.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycGURA351605:GI6A-2337-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_GEOUR
AccessionPrimary (citable) accession number: A5G3W1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 52 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