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Q7MAG3 (SYE2_WOLSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:WS0274
OrganismWolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) [Complete proteome] [HAMAP]
Taxonomic identifier273121 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeWolinella

Protein attributes

Sequence length438 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 – 438438Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119700

Regions

Motif6 – 1611"HIGH" region HAMAP-Rule MF_00022
Motif231 – 2355"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2341ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7MAG3 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: A0F385B35ABA3FE7

FASTA43850,518
        10         20         30         40         50         60 
MLRFAPSPTG DMHTGNLRAA IFNYILAKQR GEKFLVRIED TDMERNIEGK DKEILSLLNL 

        70         80         90        100        110        120 
FGMVWDELVY QSHNFPRHAQ MAEYLLSQGR AFYCYCSKEF LDQKREEALA QKLPFRYHDA 

       130        140        150        160        170        180 
WAEIEKDSTQ KPVIRLRGAS EEICFKDEIK GIVSFKPHEV DSFVIVREDG IPTYNFACAI 

       190        200        210        220        230        240 
DDMLYDVSFI VRGEDHVSNT PKQMLIQRGV GYEKLLQYAH LPILLNEEGK KMSKRDNASS 

       250        260        270        280        290        300 
VKWLLEEGYL PQAIANYLIL MGNKTPTEVF ALKEAIEWFD ITHVAKAPAK FDLDKLRFLN 

       310        320        330        340        350        360 
REHFKRLSEQ DLAFLLDHKD PSVGGLAKLY LQESSTLNEL RPKIDALFAP KIAQGEFASA 

       370        380        390        400        410        420 
MILLYPHLRA MIEEFSPALK DFEAFKKEAM ERSGLKGKPF FKSLRLLLTG SENGPELSDL 

       430 
FEYARFFFND IIRLKEPS 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571657 Genomic DNA. Translation: CAE09427.1.
RefSeqNP_906527.1. NC_005090.1.

3D structure databases

ProteinModelPortalQ7MAG3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273121.WS0274.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE09427; CAE09427; WS0274.
GeneID2554836.
KEGGwsu:WS0274.
PATRIC24037644. VBIWolSuc63014_0264.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAYCSKEFL.
OrthoDBEOG6DRPF7.

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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE2_WOLSU
AccessionPrimary (citable) accession number: Q7MAG3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 15, 2003
Last modified: May 14, 2014
This is version 69 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