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Q47SA6 (SYE_THEFY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:Tfu_0623
OrganismThermobifida fusca (strain YX) [Complete proteome] [HAMAP]
Taxonomic identifier269800 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

Protein attributes

Sequence length477 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 – 477477Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237415

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif238 – 2425"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1061Zinc By similarity
Metal binding1081Zinc By similarity
Metal binding1281Zinc By similarity
Metal binding1301Zinc By similarity
Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47SA6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 82327E88C794893F

FASTA47753,668
        10         20         30         40         50         60 
MTDKAIRTRF APSPTGMFHV GGARSALFNW ALALQQPEGK FVLRIEDTDA ARNRPEWTEG 

        70         80         90        100        110        120 
ILRALSALGI DERDPHFEGP YFQSAYADKH REVAEELYRK GRAYYCDCTR EQIQERRGNP 

       130        140        150        160        170        180 
HLGYDGYCRD RGLEPGPGRA LRFRVPEGGP TVVDDKIRGR VEFDHSAIED FVIARSDGSP 

       190        200        210        220        230        240 
LFVLANVVDD VEMAITHVVR GEEHLSNTPK QQLLWEALGQ TPPVWAHLPV IVNEKRQKLS 

       250        260        270        280        290        300 
KRRDKVALED YLAEGYLPEA MVNYLMLLGW GPGDDREIMP FSEMVPLFRL EDVNSSSAFF 

       310        320        330        340        350        360 
DEKKLRAFNG EYIRALDTTE FVERCAPWLG SEKAPWPAEN FDAQVFEAVA PLAQTRISVL 

       370        380        390        400        410        420 
SEIVSYVDFL FLDRPVEDEK SWAKAMKPGV GEEMLTAALE RFSDPNLEWR AEPLKAALEE 

       430        440        450        460        470 
VAAAQGLKLG KAQAPVRVAV TGRTVGLPLF ESLELLGRSR VQERLRAALE KLKAAGE 

« Hide

References

[1]"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX."
Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N.
J. Bacteriol. 189:2477-2486(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000088 Genomic DNA. Translation: AAZ54661.1.
RefSeqYP_288684.1. NC_007333.1.

3D structure databases

ProteinModelPortalQ47SA6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269800.Tfu_0623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ54661; AAZ54661; Tfu_0623.
GeneID3580652.
KEGGtfu:Tfu_0623.
PATRIC23901684. VBITheFus33945_0647.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycTFUS269800:GI42-636-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_THEFY
AccessionPrimary (citable) accession number: Q47SA6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 63 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