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Q3ZYP4 (SYE_DEHSC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:cbdbA1316
OrganismDehalococcoides sp. (strain CBDB1) [Complete proteome] [HAMAP]
Taxonomic identifier255470 [NCBI]
Taxonomic lineageBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

Protein attributes

Sequence length487 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237358

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif245 – 2495"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1081Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1351Zinc By similarity
Metal binding1371Zinc By similarity
Binding site2481ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ZYP4 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 3D04551A2A9DA0D4

FASTA48755,527
        10         20         30         40         50         60 
MTNEVRVRYA PSPTGYPHLG NIRTAMFNWL FARHNGGKFI VRIEDTDRER YVEGAVESIL 

        70         80         90        100        110        120 
ESLNWLGLDW DEGPDKGGDY GPYYQSERLP LYRKAAEKLV AEGKAYYCHC SSEKLDKMRE 

       130        140        150        160        170        180 
DQIARKEPPG YDRCCRDMGL GQKEGAVIRF KIPLDGQTAF TDLIRGEVTF DNAKQDDFVI 

       190        200        210        220        230        240 
LKSDGFPTYH LASVVDDHAM QISHVLRAEE WLPSTPKHLM LYKALGYTPP LYAHLPMILG 

       250        260        270        280        290        300 
PDRSKLSKRH GATSTIEYKQ AGYLPETMVN FLSLLGWAYD DKTELFSREQ LIEYFCLEKV 

       310        320        330        340        350        360 
SKTAAIFNYE KLDWMNGMYI RTLSAQDLAC RAMPFLEKDV RIAASGHLNL DYTVKVMPLI 

       370        380        390        400        410        420 
QERAKKLNEL AELCWFIYSD DISYDPALLI DKKLTKETSL SALKAANARL EALPNFDAAS 

       430        440        450        460        470        480 
MEEHIRPLAA ELELKPGQLF GMLRTASTGQ QVAPPLFQTM EVLGRQRCLW RIAMAIARLS 


EMPFQRS 

« Hide

References

[1]"Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1."
Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.
Nat. Biotechnol. 23:1269-1273(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CBDB1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ965256 Genomic DNA. Translation: CAI83372.1.
RefSeqYP_308288.1. NC_007356.1.

3D structure databases

ProteinModelPortalQ3ZYP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING255470.cbdb_A1316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI83372; CAI83372; cbdbA1316.
GeneID3623605.
KEGGdeh:cbdb_A1316.
PATRIC21612575. VBIDehSp125902_1104.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycDSP255470:GJXW-1130-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_DEHSC
AccessionPrimary (citable) accession number: Q3ZYP4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: September 27, 2005
Last modified: February 19, 2014
This is version 61 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