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

Q2N5Q3 (SYE2_ERYLH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:ELI_14480
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter

Protein attributes

Sequence length452 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.

Sequence caution

The sequence ABC64988.1 differs from that shown. Reason: Erroneous initiation.

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 – 452452Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367669

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif246 – 2505"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2491ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2N5Q3 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 29E4636AC0CBE197

FASTA45250,361
        10         20         30         40         50         60 
MTTTRFAPSP TGRLHVGNIR TALHNWMLAK KHGGRFLLRI DDTDAERSKE EYVHAIRADL 

        70         80         90        100        110        120 
AWLGLEPDGE ERQSERLEHY EAAFEALKAA GRVYPAYETA QELELKRKIQ LGRGLPPIYD 

       130        140        150        160        170        180 
RAALKLSDDE RAAKEAQGIA PHWRFKLDHD VPITWEDRVR GPQKFDPAQL SDPVIRRADG 

       190        200        210        220        230        240 
SWLYMLPSAV DDIDMGITHV LRGEDHVSNT AVQIQMFTAL FAAQHDAQQS PPEFAHEALL 

       250        260        270        280        290        300 
VGKEGKLSKR LGSLGCDAFR ERGIEPEALV AMLARLGTSQ PVEPIADRQV LLDTFDLSTF 

       310        320        330        340        350        360 
GRAPAKFDDA ELERVNTAIV HAMDFEQVKQ RLPEGIDAAG WHAIQPNLAT VDEAGEWWRL 

       370        380        390        400        410        420 
VTGPIEQPEF SDEDRAYLAE AAETLAWDDD PWGTLTAKLK DSTGRKGKAL FLPLRQALTG 

       430        440        450 
MNHGPDMGEL LPLIGEEEAR ARLQSAADQR GG 

« Hide

References

[1]"Complete genome sequence of Erythrobacter litoralis HTCC2594."
Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC2594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000157 Genomic DNA. Translation: ABC64988.1. Different initiation.
RefSeqYP_459785.1. NC_007722.1.

3D structure databases

ProteinModelPortalQ2N5Q3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314225.ELI_14480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC64988; ABC64988; ELI_14480.
GeneID3871196.
KEGGeli:ELI_14480.
PATRIC21862973. VBIEryLit102657_2897.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycELIT314225:GHLE-2944-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 nameSYE2_ERYLH
AccessionPrimary (citable) accession number: Q2N5Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 60 of the entry and version 2 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