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Reviewed, UniProtKB/Swiss-Prot B1LUJ9 (SYE1_METRJ)

Last modified November 3, 2009. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1
Gene names
Name: gltX1
Ordered Locus Names: Mrad2831_2022
OrganismMethylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831) [Complete proteome] [HAMAP]
Taxonomic identifier426355 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_1000090089

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022
Motif240 – 2445"KMSKS" region HAMAP MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LUJ9-1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 9F832F1406F04989

FASTA47551,722
        10         20         30         40         50         60 
MSSAVVTRFA PSPTGYLHIG GARTALFNWL YARHTGGKML LRIEDTDRER STKGAIDAIL 

        70         80         90        100        110        120 
DGLSWLGLDW DGDVVFQFAR AERHRAVAEE LLAAGRAYHC YATAEELAQM RETARAEGRA 

       130        140        150        160        170        180 
PRYDGRWRDR DPSEAPAGVK PVIRLRAPIE GETVVEDAVQ GRVTWANKDL DDLVLLRSDG 

       190        200        210        220        230        240 
TPTYMLAVVV DDHDMGVTQI IRGDDHLTNA ARQSQIFSAL GWDVPRMAHI PLIHGADGAK 

       250        260        270        280        290        300 
LSKRHGALGV EAYRDLGYLP AALRNYLVRL GWSHGDQEVF STEEMVAAFD LGAVGRSAAR 

       310        320        330        340        350        360 
FDFAKLANLN GLYIRTSADA DLVAAIETIL PNVGPERGLS APLQPDLKDK LIQAMPGLKE 

       370        380        390        400        410        420 
RAKTLIELLD SAYYLYAQRP LALDDKARAL LSDEGRGRLA GVRPVLEALP DWSAASTEGA 

       430        440        450        460        470 
VRQYAESAGC KLGQVAQPLR AALTGRTTSP PLFDVMAVLG REETLARLGD QAPQG 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium radiotolerans JCM 2831."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marx C.J., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001001 Genomic DNA. Translation: ACB24017.1.
RefSeqYP_001754700.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6138051.
GenomeReviewsGene locus Mrad2831_2022 in contig CP001001_GR.
KEGGmrd:Mrad2831_2022.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMAHIPLI.

Family and domain databases

HAMAPMF_00022.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_METRJ
AccessionPrimary (citable) accession number: B1LUJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: November 3, 2009
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents