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A4XVX2 (SYE_PSEMY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:Pmen_2733
OrganismPseudomonas mendocina (strain ymp) [Complete proteome] [HAMAP]
Taxonomic identifier399739 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length493 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001940

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif251 – 2555"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1071Zinc By similarity
Metal binding1091Zinc By similarity
Metal binding1341Zinc By similarity
Metal binding1361Zinc By similarity
Binding site2541ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XVX2 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: E2E686CBB1018F8D

FASTA49356,407
        10         20         30         40         50         60 
MTTVRTRIAP SPTGDPHVGT AYIALFNLCF ARQHGGQFIL RIEDTDQLRS TRESEQQIFD 

        70         80         90        100        110        120 
ALRWLGIEWD EGPDVGGPHG PYRQSERGEI YKQYSDELVA KGHAFPCFCS AERLDEVRAQ 

       130        140        150        160        170        180 
QMANKETPRY DGHCMHLDPA EAQRRIAAGE SHVVRMKVPS EGVCVVPDML RGDVEIPWDR 

       190        200        210        220        230        240 
MDMQVLMKAD GLPTYFLANV VDDHLMGITH VLRGEEWLPS APKLIKLYEY FGWEQPALCY 

       250        260        270        280        290        300 
MPLLRNPDKS KLSKRKNPTS ITFYERMGYL PQAMLNYLGR MGWSMPDERE KFSLNEMIEH 

       310        320        330        340        350        360 
FDINRVSLGG PIFDLEKLSW LNGQWLRELP VETFAAEVQK WALNPEYLMK IAPHVQGRVE 

       370        380        390        400        410        420 
TFSQIAPLAG FFFSGALNLD AKLFEHKKLS PDQVRQLMQL ILWKLESLRQ WEKERITGCI 

       430        440        450        460        470        480 
QAVVEHLELK LRDAMPLMFA AITGQASSVS VLDAMEILGP DLTRFRLRQA LELLGGTSKK 

       490 
ETKEWEKLLA SIA 

« Hide

References

[1]"Complete sequence of Pseudomonas mendocina ymp."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Hersman L., Dubois J., Maurice P., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ymp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000680 Genomic DNA. Translation: ABP85488.1.
RefSeqYP_001188220.1. NC_009439.1.

3D structure databases

ProteinModelPortalA4XVX2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399739.Pmen_2733.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP85488; ABP85488; Pmen_2733.
GeneID5107272.
KEGGpmy:Pmen_2733.
PATRIC19912030. VBIPseMen131592_2763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPMEN399739:GHR6-2784-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_PSEMY
AccessionPrimary (citable) accession number: A4XVX2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 55 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