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

A3N1S5 (SYE_ACTP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:APL_1275
OrganismActinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]
Taxonomic identifier416269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length479 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 – 479479Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001866

Regions

Motif21 – 3111"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3N1S5 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 4773629B891ACF97

FASTA47954,190
        10         20         30         40         50         60 
MNIETLFPLD PNVKVRTRFA PSPTGYLHVG GARTALSSWL YAKHFNGEFV LRIEDTDLER 

        70         80         90        100        110        120 
STPEATAAIL EGMEWLNLAW EHGPYYQTKR FDRYNQVIDQ MIEQGLAYRC YCSKERLENL 

       130        140        150        160        170        180 
RHEQEANKEK PRYDRHCLAH HDQPTDAPHV VRFKNPQEGS VVFDDAVRGR IEISNSELDD 

       190        200        210        220        230        240 
LIIRRTDGSP TYNFCVVVDD WDMGITHVVR GEDHINNTPR QINILKALGA PIPTYAHVSM 

       250        260        270        280        290        300 
INGDDGQKLS KRHGAVSVMQ YRDDGYLPEA LINYLVRLGW GHGDQEIFSR EEMIELFDIH 

       310        320        330        340        350        360 
SVSKSASAFN TDKLQWLNQH YMRSLPAEHV AKYLAWHMND QAIDTSSGPA LEEIIPVLSE 

       370        380        390        400        410        420 
RAKTLKELAA ASRYFYQEFD GYDEKAAAKN FKAEAVAPLA KLLEKLTALT DWSVEAIHDA 

       430        440        450        460        470 
MNATAADLEI GMGKVGMPFR LAVTGSGQSP SMDITAKLVG RERTLARIQK AIEFIQAQA 

« Hide

References

[1]"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
J. Bacteriol. 190:1495-1496(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000569 Genomic DNA. Translation: ABN74361.1.
RefSeqYP_001053966.1. NC_009053.1.

3D structure databases

ProteinModelPortalA3N1S5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416269.APL_1275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN74361; ABN74361; APL_1275.
GeneID4849358.
KEGGapl:APL_1275.
PATRIC20747497. VBIActPle94089_1331.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycAPLE416269:GHV7-1294-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 nameSYE_ACTP2
AccessionPrimary (citable) accession number: A3N1S5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: May 14, 2014
This is version 53 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