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A5UN79 (SYE_METS3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Msm_1452
OrganismMethanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [Complete proteome] [HAMAP]
Taxonomic identifier420247 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobrevibacter

Protein attributes

Sequence length555 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

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
Nucleotide-binding
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000331003

Regions

Motif103 – 11311"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
A5UN79 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 49F61D8B7532ECDF

FASTA55562,827
        10         20         30         40         50         60 
MNDLEEIVYK HALLNAAKHK GSANPGAVIG SIMSQEPDLR SRAKEIGPIA GKIVAQVNKL 

        70         80         90        100        110        120 
SEDEQSAQMA KYHVEVKENK QKKEEGLQEL PGSHDNVVMR FAPNPSGPLH IGHARAAVPN 

       130        140        150        160        170        180 
AEYVKRYGGK LILRIEDTDP KRVFEPAYDL IPQDLEWLGI KADEVYYQSD RFEIYYDYAR 

       190        200        210        220        230        240 
QLIEKGAAYM CTCDGATFKE LKDNCKPCPC RDNSVEKNLE LWDKFDQMHA GEAVLRVKTD 

       250        260        270        280        290        300 
INHKNPAIRD WVAMRIVEET HPRLGNKYRV YPMMNFSVAV DDHLMGMSHV LRGKDHLANS 

       310        320        330        340        350        360 
EKQKYLYDHM GWDVPEFIHY GRLKMEDIAL STSKALEGIS SGKYSGWDDP RLGTLKAIAR 

       370        380        390        400        410        420 
RGIQPQTIYN LITEIGVKMS DSAISWKKIY GLNRNFLEPI ANRYFFVENP VEITVDGYED 

       430        440        450        460        470        480 
GAVDIERPLH ADHEDRGNRI LPFAGKAYLA SEDVKDGISR LMDAVNVDID GDKITYNSTS 

       490        500        510        520        530        540 
FEQARDLKAK IIQWVPVEDN VNVSIVMDDA STKTGLGEGA LKDLKVGDVV QFERVGFARL 

       550 
DEIKDNELVF YYAHK 

« Hide

References

[1]"Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut."
Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PS / ATCC 35061 / DSM 861.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000678 Genomic DNA. Translation: ABQ87657.1.
RefSeqYP_001274025.1. NC_009515.1.

3D structure databases

ProteinModelPortalA5UN79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420247.Msm_1452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ87657; ABQ87657; Msm_1452.
GeneID5216855.
KEGGmsi:Msm_1452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAYLGWDDP.

Enzyme and pathway databases

BioCycMSMI420247:GHWZ-1490-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_A. Glu_tRNA_synth_A.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR022888. Glu_tRNA_synth_arc.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_METS3
AccessionPrimary (citable) accession number: A5UN79
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: July 10, 2007
Last modified: May 14, 2014
This is version 46 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