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Q492G6 (SYE_BLOPB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:BPEN_521
OrganismBlochmannia pennsylvanicus (strain BPEN) [Complete proteome] [HAMAP]
Taxonomic identifier291272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia

Protein attributes

Sequence length468 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 – 468468Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237341

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q492G6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 22F09C0C03E75B6D

FASTA46854,323
        10         20         30         40         50         60 
MNIKTRFAPS PTGSIHIGNI RTALYSWLFA RKQGGKFLLR IEDSDLQRSI DDTVELIVAG 

        70         80         90        100        110        120 
MRWLSLDWDE GPYFQTNRFS RYNSIISYMI QHDMAYKCYC SSERLESLRS NQIKNGEKPK 

       130        140        150        160        170        180 
YDGYCRFKST DIYSSSISSY VVRFCNPQDG VVIFHDQIRG TITFNNKELD DLIIRRADGS 

       190        200        210        220        230        240 
PTYNFCVVID DMDMQITHII RGEEHINNTP RQINILKALR APIPTYAHVS MILDNNLKKL 

       250        260        270        280        290        300 
SKRCGTLGIM QYRNDGFLPE AILNYLVRLG WSHGDQEIFS IEEMIKYFDL SRISKSPSIL 

       310        320        330        340        350        360 
NLEKLLWLNH YYINHLPIDY VASHLSWHMH QQKINIQNGP KLTDIIKLFA RRSRTLKEIV 

       370        380        390        400        410        420 
NNCLYFYIDF DLFDNKVAKD YLKPVAITPL KFLRKKFSNI VDWTPEIIKS IIIETVNEFN 

       430        440        450        460 
TSIDKIGMPL RVALTGTNCS PTLSITIHAI GQSRVLERID QAIRYIST 

« Hide

References

[1]"Genome sequence of Blochmannia pennsylvanicus indicates parallel evolutionary trends among bacterial mutualists of insects."
Degnan P.H., Lazarus A.B., Wernegreen J.J.
Genome Res. 15:1023-1033(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BPEN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000016 Genomic DNA. Translation: AAZ41133.1.
RefSeqYP_278010.1. NC_007292.1.

3D structure databases

ProteinModelPortalQ492G6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING291272.BPEN_521.

Proteomic databases

PRIDEQ492G6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ41133; AAZ41133; BPEN_521.
GeneID3562945.
KEGGbpn:BPEN_521.
PATRIC31965967. VBICanBlo110049_0509.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.

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_BLOPB
AccessionPrimary (citable) accession number: Q492G6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 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