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

Q2W3G8 (SYE2_MAGSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:amb2803
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

Protein attributes

Sequence length477 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 – 477477Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000237369

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif238 – 2425"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2W3G8 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 48CDC54BF366EBED

FASTA47752,538
        10         20         30         40         50         60 
MTVVTRFAPS PTGFLHIGGG RTALFNWLFA RHHGGKFLLR IEDTDRARST DAAVEAIFDG 

        70         80         90        100        110        120 
IKWLGLDWDG EAVMQFARAC RHAEVARQLL DEGKAYRCYC TQDELTAIRE EQKAKGQPMR 

       130        140        150        160        170        180 
YPGIWRDRPA TDAPEGAPFV VRLKAPAEGE TIIADLVQGD VRVANDQLDD MVLLRADGTP 

       190        200        210        220        230        240 
TYMLSVVVDD HDMGITHVIR GDDHLTNAFR QYQLYKACGW EVPTFAHIPL IHGPDGAKLS 

       250        260        270        280        290        300 
KRHGALGVDA YRDMGFLPEA MRNYLLRLGW SHGDDEIIST EQAVEWFTLD SVGRSPSRFD 

       310        320        330        340        350        360 
FVKLTNLNGH YMRGADDGRL TEVLVPLLEA KTGKALSGES VARLRTGMTG LKERAKTMVE 

       370        380        390        400        410        420 
LADSALFYVA ERPLALDEKA AKTMADETAT ADLAAYRTEV KELGAWTRDT LEDAARRLAE 

       430        440        450        460        470 
ARGQKLGKIA QPLRAALAGS SVSPPIFEVM EVLGREESLG RIEDALGGTR PTTSTAA 

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007255 Genomic DNA. Translation: BAE51607.1.
RefSeqYP_422166.1. NC_007626.1.

3D structure databases

ProteinModelPortalQ2W3G8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342108.amb2803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE51607; BAE51607; amb2803.
GeneID3804011.
KEGGmag:amb2803.
PATRIC22439864. VBIMagMag129836_2768.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMMAG342108:GJNU-2835-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_MAGSA
AccessionPrimary (citable) accession number: Q2W3G8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 10, 2006
Last modified: May 14, 2014
This is version 59 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