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Q728Q1 (SYE_DESVH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:DVU_2552
OrganismDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Reference proteome] [HAMAP]
Taxonomic identifier882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length463 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
Reference 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 – 463463Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119554

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q728Q1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 1DCC1DEF1214D4CF

FASTA46351,485
        10         20         30         40         50         60 
MSNVVTRFAP SPTGHLHIGG ARTAIFNWLL ARHFGGRFVL RIEDTDTERS KQEYTDSILA 

        70         80         90        100        110        120 
SMKWLGLDWD GDLIYQSERF DIYNSYIDRL LESGHAYWCE CPPDEVEKMR EEARAKGLKP 

       130        140        150        160        170        180 
RYNGRCRSRD LGPGDGRVVR LKAPAEGRIV FDDLVKGTVA FDVAELDDMV LRRSDGAPTY 

       190        200        210        220        230        240 
NLAVVVDDAT MGVTHVLRGD DHLSNTPKQI LLYQALGFDL PRFGHVPMIL GPDRKKLSKR 

       250        260        270        280        290        300 
HGAKAVIEYE QYGLLPQALV NYLVRLGWSH GDQEIFALEE LVEKFGTENL NSSAAGFDPD 

       310        320        330        340        350        360 
KLEWLNGHYL RETSPEELAR LVLPFVAAEG FDVDASRLAQ LVPLFRERAN NLVELARVMR 

       370        380        390        400        410        420 
FMLVPAAEVE YDAAAVAKAL TEEGRRHVAG VREALAALGT FDREGCEKAI HDYVEGNGLK 

       430        440        450        460 
FKQVAPAVRV AVVGAMGGPG LPDMMALLGR DDVLARLDRA VAL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017285 Genomic DNA. Translation: AAS97024.1.
RefSeqYP_011764.1. NC_002937.3.

3D structure databases

ProteinModelPortalQ728Q1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING882.DVU2552.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS97024; AAS97024; DVU_2552.
GeneID2796126.
KEGGdvu:DVU2552.
PATRIC32064704. VBIDesVul119526_2308.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAIQECIND.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycDVUL882:GJIL-2614-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_DESVH
AccessionPrimary (citable) accession number: Q728Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 69 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