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B0V8Q3 (SYE_ACIBY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:ABAYE0277
OrganismAcinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]
Taxonomic identifier509173 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length502 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 – 502502Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367602

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0V8Q3 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 3BDF319E336E5E92

FASTA50257,491
        10         20         30         40         50         60 
MKVRTRIAPS PTGFPHVGTA YIALFNMCFA KQHGGEFILR IEDTDQLRST PESEKMILDS 

        70         80         90        100        110        120 
LRWLGLNWSE GPDVGGPHAP YRQSERMGIY KQYALELVEK GHAFYCFATA EELDQMRAEQ 

       130        140        150        160        170        180 
QARGETPKYD GRGLKLSQEE VARRLEAGEP HVIRMKVPEE GVCKFNDLLR GEVEIPWAQV 

       190        200        210        220        230        240 
DMQVLLKTDG LPTYHLANVV DDHLMEITHV LRGEEWLPSA PKHQLLYQYF GWEMPTLCHM 

       250        260        270        280        290        300 
PLLRNPDKSK LSKRKNPTSI NYYRDIGVLP EALLNYLGRM GWSMPDEREV FTLQDMMDNF 

       310        320        330        340        350        360 
DIQRVSLGGP IFDVEKLNWL NGQWIKGLTP GQLLDRLLTW KSDRSTLEDI AAAIQPRINL 

       370        380        390        400        410        420 
LSEAVNWAGF YFNHMPQITA EMFESKKLTQ EQVRQSLQFA IWRLESQFTW NNDTVSQTLM 

       430        440        450        460        470        480 
DLANQMGIKL RDFMPTFFIA IAGSTSSTPV MQSMVTLGPD LTFARLRHAL EIVGAPSKKE 

       490        500 
VKNWEKLNES LKLPKNEATS EA 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AYE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU459141 Genomic DNA. Translation: CAM85257.1.
RefSeqYP_001712262.1. NC_010410.1.

3D structure databases

ProteinModelPortalB0V8Q3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509173.ABAYE0277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM85257; CAM85257; ABAYE0277.
GeneID6002845.
KEGGaby:ABAYE0277.
PATRIC20724021. VBIAciBau69881_0364.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycABAU509173:GJXF-279-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_ACIBY
AccessionPrimary (citable) accession number: B0V8Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 38 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