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Q98MD0 (SYE1_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:mlr0628
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length474 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

Subunit structure

Monomer By similarity. 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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000119631

Regions

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

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98MD0 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 7A2F5D16AFF4DAFB

FASTA47451,492
        10         20         30         40         50         60 
MSDKVVTRFA PSPTGYLHIG GARTALFNWL YAKHTGGTML LRIEDTDRER STAAATAAIL 

        70         80         90        100        110        120 
DGLSWLGLGW DGDAVSQFER APRHREVAEE LVRMGKAYYS YETPAELEAM REAARAKGLP 

       130        140        150        160        170        180 
PRYNGQWRDR TPSEAPAGVK GAIRIKAPTE GETIVHDRVQ GEVRFPNKDL DDFIILRSDG 

       190        200        210        220        230        240 
NPTYMHAVVV DDHDMGVTHI IRGDDHLTNA ARQTVIYNAM GWDVPSMSHI PLIHGADGAK 

       250        260        270        280        290        300 
LSKRHGALGV EAYRAMGYLP EALLNYLARL GWSHGDDEIM SIKDMISWFD IGDVNKGAAR 

       310        320        330        340        350        360 
FDFAKLEAIN GAHMRRMADA QLLDIFIATL PYLEGGPAMA ARLNEHNKAQ LLAALPGLKE 

       370        380        390        400        410        420 
RAKTLVELVD GAAFLFATRP LPVDEKAALL LNDGARKILR GAHEALNALS GDWTAAAAEA 

       430        440        450        460        470 
AVRDYALAGG HKLGAVAQPL RAALTGKSTS PGVFDVLAVL GREESLARIA DQID 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB48183.1.
RefSeqNP_102397.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98MD0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mlr0628.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB48183; BAB48183; BAB48183.
GeneID1225060.
KEGGmlo:mlr0628.
PATRIC22475170. VBIMesLot2464_0505.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-509-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_RHILO
AccessionPrimary (citable) accession number: Q98MD0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 1, 2001
Last modified: February 19, 2014
This is version 67 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