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O26157 (SYE_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:MTH_51
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter ›

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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 term3D-structure
Complete proteome
Reference 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 – 553553Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119721

Regions

Motif103 – 11311"HIGH" region HAMAP-Rule MF_00022

Secondary structure

1 ....................................................................................... 553
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O26157 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C6DB8AE92C2FEE6B

FASTA55363,090
        10         20         30         40         50         60 
MVPVEDLVYR YALLNAVKHR GRANPGAVMG AVMSNEPELR KMAPQVKEAV EAAVERVNSL 

        70         80         90        100        110        120 
SPEEQQQEME RLGLEITERK QKKRKGLREL AGVKGEVVLR FAPNPSGPLH IGHARAAILN 

       130        140        150        160        170        180 
HEYARKYDGR LILRIEDTDP RRVDPEAYDM IPADLEWLGV EWDETVIQSD RMETYYEYTE 

       190        200        210        220        230        240 
KLIERGGAYV CTCRPEEFRE LKNRGEACHC RSLGFRENLQ RWREMFEMKE GSAVVRVKTD 

       250        260        270        280        290        300 
LNHPNPAIRD WVSMRIVEAE HPRTGTRYRV YPMMNFSVAV DDHLLGVTHV LRGKDHLANR 

       310        320        330        340        350        360 
EKQEYLYRHL GWEPPEFIHY GRLKMDDVAL STSGAREGIL RGEYSGWDDP RLGTLRAIAR 

       370        380        390        400        410        420 
RGIRPEAIRK LMVEIGVKIA DSTMSWKKIY GLNRSILEEE ARRYFFAADP VKLEVVGLPG 

       430        440        450        460        470        480 
PVRVERPLHP DHPEIGNRVL ELRGEVYLPG DDLGEGPLRL IDAVNVIYSG GELRYHSEGI 

       490        500        510        520        530        540 
EEARELGASM IHWVPAESAL EAEVIMPDAS RVRGVIEADA SELEVDDVVQ LERFGFARLD 

       550 
SAGPGMVFYY AHK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000666 Genomic DNA. Translation: AAB84558.1.
PIRB69167.
RefSeqNP_275194.1. NC_000916.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AIIX-ray1.65A1-553[»]
ProteinModelPortalO26157.
ModBaseSearch...

Protein-protein interaction databases

STRING187420.MTH51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB84558; AAB84558; MTH_51.
GeneID1470013.
KEGGmth:MTH51.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAMRFAPNP.
ProtClustDBPRK04156.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-51-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_Ib_arc/euk.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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. Ribosomal_L25rel. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_METTH
AccessionPrimary (citable) accession number: O26157
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents