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A6LEA1 (SYE_PARD8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:BDI_2289
OrganismParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC 11152) [Complete proteome] [HAMAP]
Taxonomic identifier435591 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaeParabacteroides

Protein attributes

Sequence length505 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 – 505505Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001928

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif260 – 2645"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2631ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6LEA1 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 064BE993584ADCDF

FASTA50557,731
        10         20         30         40         50         60 
MTQRKVRVRF APSPTGALHI GGVRTALYNY LFAKQNGGDM ILRIEDTDSQ RFVPGAEDYI 

        70         80         90        100        110        120 
IEALTWLGIK FDEGVSFGGN YGPYRQSERR EIYKKYVDQL LNDGHAYIAF DTPAELEEKR 

       130        140        150        160        170        180 
KEIANFQYDA STRSQMRNSL TLSQEEVQSL IESGHQYVVR AKIEPNEDIH VNDLIRGEVV 

       190        200        210        220        230        240 
INSSILDDKV LYKSADQLPT YHLANIVDDH LMEVTHVIRG EEWLPSAPLH VLLYRFFGWE 

       250        260        270        280        290        300 
DTMPSFAHLS LLLKPEGNGK LSKRDGDRLG FPVFPLEWHD PKTGDVSSGY RESGYFPEAV 

       310        320        330        340        350        360 
VNFLALLGWN PGNDQEVMSM DDLIRLFDLS RCSKSGAKFD YEKGRWFNHH YLLEKSNAEI 

       370        380        390        400        410        420 
ADLFLPIVES HGIQTTHAYV EKVVGMMKGR VNFVSELWDL CSFFFIAPTE YDEKTRKKRW 

       430        440        450        460        470        480 
KEDSAVQLGE FIEQLRAREP FDVEGTENEC KAWIESKGYH LGNIMNAARL ALVGEGKGPG 

       490        500 
IFDITEALGK EESIRRIQRA IEILK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000140 Genomic DNA. Translation: ABR44015.1.
RefSeqYP_001303637.1. NC_009615.1.

3D structure databases

ProteinModelPortalA6LEA1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING435591.BDI_2289.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR44015; ABR44015; BDI_2289.
GeneID5307438.
KEGGpdi:BDI_2289.
PATRIC22847788. VBIParDis29947_2270.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPDIS435591:GCNH-2283-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_PARD8
AccessionPrimary (citable) accession number: A6LEA1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: February 19, 2014
This is version 51 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