Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q82U77 (SYE_NITEU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 71. 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:NE1624
OrganismNitrosomonas europaea (strain ATCC 19718 / NBRC 14298) [Complete proteome] [HAMAP]
Taxonomic identifier228410 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length463 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 – 463463Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119614

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82U77 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B1E31A1E4D01F358

FASTA46352,887
        10         20         30         40         50         60 
MVKTRFAPSP TGYLHIGGAR TALFSWAFAR KQGGKFVLRI EDTDLERSTQ QSVQAILDGM 

        70         80         90        100        110        120 
AWLGLDYDEG PYYQMQRLNR YQEVAEQLLT QGLAYQCYAS REELDALREQ QRLAGLKPRY 

       130        140        150        160        170        180 
DGRWRDSRQT PPAGVKPVVR LKTPQHGYVV FDDLVKGKIS VANHELDDLV LLRSDGTPTY 

       190        200        210        220        230        240 
NFGVVLDDLD MGITHVIRGD DHVNNTPRQI NILKALGAAI PQYAHVPMIL GADGERLSKR 

       250        260        270        280        290        300 
HGAVSVMHYR DQGYLPEALI NYLARLGWSH GDEEIFSREQ LVEWFDLAAI SRSPAKFNPE 

       310        320        330        340        350        360 
KLTWLNQHYL KMADDARLVE LVMPFLLERN YPLPATENLL KIVNLLKDRA STIEELADAS 

       370        380        390        400        410        420 
AYFFRTIEPP EELRTQYFTA EIRPVLEYLV DRLAQIEWKR ETIHHEIKQT VSSHNLKFPS 

       430        440        450        460 
LAMPLRVMVT GEAQTPAIDA VLELLGKEET LHRLRGRMEI FPG 

« Hide

References

[1]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / NBRC 14298.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954747 Genomic DNA. Translation: CAD85535.1.
RefSeqNP_841659.1. NC_004757.1.

3D structure databases

ProteinModelPortalQ82U77.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228410.NE1624.

Proteomic databases

PRIDEQ82U77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD85535; CAD85535; NE1624.
GeneID1082576.
KEGGneu:NE1624.
PATRIC22714450. VBINitEur56163_1817.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.
PhylomeDBQ82U77.

Enzyme and pathway databases

BioCycNEUR228410:GJNO-1655-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
1.10.8.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
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 nameSYE_NITEU
AccessionPrimary (citable) accession number: Q82U77
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 71 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