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

Q7M7L9 (SYE1_WOLSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:WS2217
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 length465 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 – 465465Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000119699

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
Q7M7L9 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 3BD7947A4E04EA40

FASTA46552,651
        10         20         30         40         50         60 
MIVTRFAPSP TGNLHIGGLR TALFSYLYAR KTGGKFLLRI EDTDLARNSH DATKAIIEAF 

        70         80         90        100        110        120 
DWVGLSYDGE AIYQSERFPL YKEYIDRLIQ EGKAYYCYMS KEELDALREE QRSRGETPRY 

       130        140        150        160        170        180 
DNRYRDFTGT PPSGVAPVVR IKAPLEGYIE FEDGVKGEMK IGAKEMDDYI IARSDGTPTY 

       190        200        210        220        230        240 
NFVVSIDDAL MGVTDVIRGD DHLTNTPKQI IVYQALGFPI PKFYHVPMIL NPEGRKLSKR 

       250        260        270        280        290        300 
DGAMGVMDYK RAGYLPEAVL NFLVRLGWSH GDQEIFSMEE MLRFFDPKDL NSSASAYNQE 

       310        320        330        340        350        360 
KFLWLNHHYI TQTPNERLEE LLLEFGCQPL SLGVREILYP ALKERAKTLA ELAQMLQEIV 

       370        380        390        400        410        420 
QTPSELDTKM LEKVGNSENG EILENYALFL ESLESAGENP KILEEETQAF LDIHGLKSGK 

       430        440        450        460 
LFQSVRLALL GKGGGPGIFE IMAAIGKEES MARIQKASEI FKNRN 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571663 Genomic DNA. Translation: CAE11205.1.
RefSeqNP_908305.1. NC_005090.1.

3D structure databases

ProteinModelPortalQ7M7L9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273121.WS2217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE11205; CAE11205; WS2217.
GeneID2553615.
KEGGwsu:WS2217.
PATRIC24041352. VBIWolSuc63014_2086.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAIQECIND.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

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_WOLSU
AccessionPrimary (citable) accession number: Q7M7L9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 68 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