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Q03E40 (SYE_PEDPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:PEPE_1501
OrganismPediococcus pentosaceus (strain ATCC 25745 / 183-1w) [Complete proteome] [HAMAP]
Taxonomic identifier278197 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaePediococcus

Protein attributes

Sequence length495 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 – 495495Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001929

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03E40 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 07970F6C725D7F40

FASTA49556,726
        10         20         30         40         50         60 
MAKQKIRVRY APSPTGHLHI GNARTALFNY LFARHYKGKF ILRIEDTDQS RNIADGEKSQ 

        70         80         90        100        110        120 
IDNLKWLGMD WDEGPDKPGE YGPYRQSERK GIYQPLIDQL VAEGKAYESY MTEEELAAQR 

       130        140        150        160        170        180 
EEQKANGEMP HYVDEYAGLS PEQKEQKIAD AKAAGIEPVI RFKVPTNTTY EWDDLVKGHI 

       190        200        210        220        230        240 
SFESETIGGD FVIQKRDGMP TYNFAVVVDD HMMEISHVFR GDDHVANTPK QLMIYEALGW 

       250        260        270        280        290        300 
DAPQFGHMSL IINTETGKKL SKRDESILQF IEQYRSLGYL PEAMLNFIIL LGWSPVGESE 

       310        320        330        340        350        360 
IFTLREFVKM YDEKRLSKSP AAFDAKKLEW INNQYVKAAD EDRIMHSALL QLINAGKIEK 

       370        380        390        400        410        420 
NPAPMKVEWA RKLINLFKRQ MSYTAQIVEF TELFFNGPEN IDEEAKEELA TDDALPVLKA 

       430        440        450        460        470        480 
LEKQFSDLPV FDTVNILAAI KAVQKETGIK GRKLWMPIRI AITHEMHGPE LPESLELLGY 

       490 
ELSMQHLRAM IEELS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000422 Genomic DNA. Translation: ABJ68532.1.
RefSeqYP_804974.1. NC_008525.1.

3D structure databases

ProteinModelPortalQ03E40.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING278197.PEPE_1501.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ68532; ABJ68532; PEPE_1501.
GeneID4417226.
KEGGppe:PEPE_1501.
PATRIC22876312. VBIPedPen34213_1418.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAKHYDGDF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPPEN278197:GI4Y-1501-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_PEDPA
AccessionPrimary (citable) accession number: Q03E40
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: May 14, 2014
This is version 56 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