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Q50543 (SYE_METTM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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:MTBMA_c05400
OrganismMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP]
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length552 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 – 552552Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119722

Regions

Motif102 – 11211"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
Q50543 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 882B6B97D2EF6576

FASTA55263,238
        10         20         30         40         50         60 
MMVEDLVYRY ALMNAVKHKG KANPGAVMGA VMSNEPELRK RAPEVKEAVQ AAVEKVNSLK 

        70         80         90        100        110        120 
PEEQQSEMER LGLEIRERKQ KKRQGLRNLP DVKGEVVLRF APNPSGPLHI GHARAAILNH 

       130        140        150        160        170        180 
EYARRYDGKL ILRIEDTDPR RVDPEAYDMI PSDLEWLGVE WDETIIQSDR MEIYYEYTER 

       190        200        210        220        230        240 
LIERGGAYVC TCTPEAFREF KNEGKACHCR DLGVRENLQR WREMFEMPEG SAVVRVKTDL 

       250        260        270        280        290        300 
QHPNPAIRDW VSMRIVEAEH PRTGTRYRVY PMMNFSVAVD DHLLGVTHVL RGKDHLANSE 

       310        320        330        340        350        360 
KQEYLYRHLG WEPPVFIHYG RLKMDDIALS TSGAREGIVE GKYSGWDDPR LGTIRAIARR 

       370        380        390        400        410        420 
GIRSDAIRKL MVEIGVKIAD STMSWKKIYG LNRNILEEEA RRYFFAADPV RFEIEGLPGP 

       430        440        450        460        470        480 
IRVERSLHPD KPELGNRILE LNGDVYLPRG DLREGPLRLI DAVNVIYSDG ELRYHSEGIE 

       490        500        510        520        530        540 
EARELQAAMI HWVPAESALK AVVVMPDASE IEGVIEGDAS ELEVDDVVQL ERFGFARVDS 

       550 
SGERLVFYYA HK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the gltX gene encoding glutamyl-tRNA synthetase from Methanobacterium thermoautotrophicum."
Moore J.A., Chen A., Yan M., Hurlburt A.P., Poulter C.D.
Biochim. Biophys. Acta 1305:113-116(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
[2]"Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37405 Genomic DNA. Translation: AAC43972.1.
CP001710 Genomic DNA. Translation: ADL58135.1.
RefSeqYP_003849448.1. NC_014408.1.

3D structure databases

ProteinModelPortalQ50543.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL58135; ADL58135; MTBMA_c05400.
GeneID9704248.
KEGGmmg:MTBMA_c05400.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000073585.
KOK01885.
OMAMRFAPNP.
ProtClustDBPRK04156.

Enzyme and pathway databases

BioCycMMAR79929:GH5J-543-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_METTM
AccessionPrimary (citable) accession number: Q50543
Secondary accession number(s): D9PV87
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 77 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