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Reviewed, UniProtKB/Swiss-Prot B0UQ09 (SYE1_METS4)

Last modified November 3, 2009. Version 12. 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: M446_0647
OrganismMethylobacterium sp. (strain 4-46) [Complete proteome] [HAMAP]
Taxonomic identifier426117 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length474 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 – 474474Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367713

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022
Motif239 – 2435"KMSKS" region HAMAP MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0UQ09-1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 9DA2B3F05E7413FD

FASTA47452,159
        10         20         30         40         50         60 
MSSVVTRFAP SPTGFLHIGG GRTALFNWLY ARKHGGRMLL RIEDTDRERS TEAAIEAILD 

        70         80         90        100        110        120 
GLSWLGLDWD GDVIYQFARA ARHREVAEGL LAAGRAYRCY ASPEELTEMR EAARREGRPL 

       130        140        150        160        170        180 
RYDGRWRDRN PSEAPPGVRP VIRLRAPVEG ETVVEDEVQG RVVWQNKDLD DLVLLRSDGT 

       190        200        210        220        230        240 
PTYMLAVVVD DHDMGVTHVI RGDDHLTNAA RQTQIYHALG WTVPSMSHIP LIHGPDGAKL 

       250        260        270        280        290        300 
SKRHGALGVD AYRGLGYLPA ALRNYLVRLG WSHGDQEVFS TEEMVAAFDL KQIGRSPARF 

       310        320        330        340        350        360 
DFAKLENLNG QYIRATSDAD LVAAIEAILP SQGPARGLPA RFDDALRARF LAAMPGLKER 

       370        380        390        400        410        420 
AKTLIELLDS AYYLYAPRPL ALDERAEGLL GNGGRERLAG VLPRLEALPD WSAASTEQAV 

       430        440        450        460        470 
RDFAEAAAVK LGHVAQPLRA ALTGRATSPG LFDVMAVLGR EESLGRLRDQ ARAA 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium sp. 4-46."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ivanova N., Marx C.J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000943 Genomic DNA. Translation: ACA15208.1.
RefSeqYP_001767642.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6135362.
GenomeReviewsGene locus M446_0647 in contig CP000943_GR.
KEGGmet:M446_0647.

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_METS4
AccessionPrimary (citable) accession number: B0UQ09
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: November 3, 2009
This is version 12 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