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A6L0E8 (SYE_BACV8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:BVU_1475
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

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_1000001872

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
A6L0E8 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: B2E721D705D60FD3

FASTA50557,874
        10         20         30         40         50         60 
MSERKVRVRF APSPTGALHI GGVRTALYNY LFARQHGGDL IFRIEDTDSN RFVPGAEEYI 

        70         80         90        100        110        120 
IESFKWLGIN FDEGVSFGGN YGPYRQSERR DIYKKYVQVL LDSGKAYIAF DTPAELDAKR 

       130        140        150        160        170        180 
QEISNFQYDA STRMSMRNSL TLPKEEVDAL IADGKQYVVR FKIEPNEDVH VHDIIRGEVV 

       190        200        210        220        230        240 
INSSILDDKV LYKSADELPT YHLANIVDDH LMEVSHVIRG EEWLPSAPLH VLLYRAFGWA 

       250        260        270        280        290        300 
DTMPEFAHLP LLLKPDGNGK LSKRDGDRLG FPVFPLEWHD PKTGEVSSGY RESGYLPEAV 

       310        320        330        340        350        360 
INFLALLGWN PGNDQELMSL DELVKLFDLH RCSKAGAKFD FEKGKWFNHE YILKKSNEEV 

       370        380        390        400        410        420 
AGLFMPILKE HGIEAPMDKV VTVVGLMKDR VSFIKDLWET CKFFFVAPTE YDEKTRKKRW 

       430        440        450        460        470        480 
KEDSPERMLE LADVLEALDD FSLENQEAVV MKWIEDKGYH LGNIMNAFRL TLVGEGKGPH 

       490        500 
MFDISAVLGK EETLRRIRRA VEVLK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000139 Genomic DNA. Translation: ABR39162.1.
RefSeqYP_001298784.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L0E8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING435590.BVU_1475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR39162; ABR39162; BVU_1475.
GeneID5302441.
KEGGbvu:BVU_1475.
PATRIC21067812. VBIBacVul85104_1537.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBVUL435590:GH96-1472-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_BACV8
AccessionPrimary (citable) accession number: A6L0E8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: May 14, 2014
This is version 53 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