Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q21V06 (SYE_RHOFD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:Rfer_2681
OrganismRhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) [Complete proteome] [HAMAP]
Taxonomic identifier338969 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAlbidiferax

Protein attributes

Sequence length462 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 – 462462Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001948

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif243 – 2475"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21V06 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 7CFF949E19B04B2D

FASTA46251,700
        10         20         30         40         50         60 
MTQKTRTRFA PSPTGFIHLG NIRSALYPWA FARSTGGDFI LRIEDTDLDR STQAAVDVII 

        70         80         90        100        110        120 
ESMSWLGLDY DEGPFYQMQR MDRYKTVLAE LQAAGHVYPC YMSVAELDAL RDAQMAAKEK 

       130        140        150        160        170        180 
PRYDGTWRPA PGKTLPPIPE GVKPVLRFKN PLGGSVVWDD KVKGRIEISN DELDDLVIAR 

       190        200        210        220        230        240 
PDGTPTYNFC VVVDDLDMAI THVIRGDDHV NNTPRQINIF KALGQEPPVY AHLPTVLNEQ 

       250        260        270        280        290        300 
GEKMSKRNGA KPVTQYRDEG YLPDAMVNYL ARLGWSHGDD EIFSRAQFLQ WFNLDHLGRS 

       310        320        330        340        350        360 
AAQFDEAKLR WVNAQHLKIM SDDALAPLVQ AQLQKRGIQA DERLPRICAL FKDRCDTTVV 

       370        380        390        400        410        420 
LADWAAAFYA DITLNPAEVS QHVTDAIKPA LNLLSEKLAS CSWDKLSIAA AIKEVLVACA 

       430        440        450        460 
IKMPLLAMPV RVLVMGSAHT PSLDAVLELC EREKVLTRLR SE 

« Hide

References

[1]"Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15236 / ATCC BAA-621 / T118.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000267 Genomic DNA. Translation: ABD70397.1.
RefSeqYP_523928.1. NC_007908.1.

3D structure databases

ProteinModelPortalQ21V06.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338969.Rfer_2681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD70397; ABD70397; Rfer_2681.
GeneID3962014.
KEGGrfr:Rfer_2681.
PATRIC23238085. VBIRhoFer131161_3042.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycAFER338969:GHU9-2713-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_RHOFD
AccessionPrimary (citable) accession number: Q21V06
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 62 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