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A3DD54 (SYE_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:Cthe_0648
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length546 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 – 546546Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367652

Regions

Motif42 – 5211"HIGH" region HAMAP-Rule MF_00022
Motif293 – 2975"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3DD54 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: C9413F90F7CCF186

FASTA54663,401
        10         20         30         40         50         60 
MDYKKLADML FPHITKSVSY YEDVVFPARN LSPGAKVTRL APSPTGFIHL GNLYGAFVDE 

        70         80         90        100        110        120 
RLAHQSNGVF ILRIEDTDDK RKVEGAVETI ISSLEFFNLK FDEGAGINGE TGNYGPYFQS 

       130        140        150        160        170        180 
NRAEIYQTVA KHLVEMGRAY PCFCSEEELE EIRKQQLAEN VNTGYYGKWA VHRNLTLEEV 

       190        200        210        220        230        240 
QKHLENNESF VIRFKSMGNP EETFEIDDAI RGRLSMQVNF QDIVLLKANG IPTYHFAHVV 

       250        260        270        280        290        300 
DDHLMRVTHV VRGEEWLSTL PIHYELFTTL GWDLPVYCHT AHLMKIDNGV KRKLSKRKDP 

       310        320        330        340        350        360 
ELGLEYYMQL GYHPAAVREY LMTILNSNFE EWRIQNPDSD INDFPFSLNK MSNSGALFDL 

       370        380        390        400        410        420 
DKLNDVSKNV LAKIPAEEIY EFLLKWAKEY KKEIVNLLEE HKDSVIKLLS VGRNSEKPRK 

       430        440        450        460        470        480 
DLIYCEQIFE FIKYFFDEYF AIVDKYPDNV DEEEAKKILK AYLETYDHND DQTQWFEKIK 

       490        500        510        520        530        540 
VIATENGYAA KPKDYKKNPD MYKGHVGDVS TVIRIAIVGR SSSPDLWEIQ QIMGEEKVRE 


RIQRLL 

« Hide

References

[1]"Complete sequence of Clostridium thermocellum ATCC 27405."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27405 / DSM 1237.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000568 Genomic DNA. Translation: ABN51883.1.
RefSeqYP_001037076.1. NC_009012.1.

3D structure databases

ProteinModelPortalA3DD54.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203119.Cthe_0648.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN51883; ABN51883; Cthe_0648.
GeneID4808177.
KEGGcth:Cthe_0648.
PATRIC19514971. VBICloThe47081_0677.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-669-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_CLOTH
AccessionPrimary (citable) accession number: A3DD54
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 20, 2007
Last modified: February 19, 2014
This is version 54 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