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Q5L6T4 (SYE_CHLAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:CAB179
OrganismChlamydophila abortus (strain DSM 27085 / S26/3) [Complete proteome] [HAMAP]
Taxonomic identifier218497 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length505 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 – 505505Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237352

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L6T4 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 310EEA1E40BF605B

FASTA50558,455
        10         20         30         40         50         60 
MAWENVRVRV APSPTGDPHV GTAYMALFNA IFAKRFNGKM ILRIEDTDQT RSRDDYEKNI 

        70         80         90        100        110        120 
FSALQWCGIQ WDEGPDIGGP YGPYRQSERT EIYRKYAELL LKTDYAYKCF ATPKELEEMR 

       130        140        150        160        170        180 
AVATTLGYRG GYDRRYRYLS SEEVDARTRE GQPYTIRLKV PLTGECVLDD YCKGRVVFPW 

       190        200        210        220        230        240 
ADVDDQVLIK SDGFPTYHFA NVVDDHLMGI THVLRGEEWL SSTPKHLLLY QAFGWKAPTF 

       250        260        270        280        290        300 
LHMPLLLNPD GTKLSKRKNP TSIFYYRDAG YIKEAFMNFL TLMGYSMEGD EEIYSLEKLI 

       310        320        330        340        350        360 
ANFDPRRIGK SGAVFDTRKL DWMNKHYLTH ERSSESLLAK LKDWLINDEF FLKILPLCQS 

       370        380        390        400        410        420 
RITTLAEFIG FTGFFFSVLP EYSKEELLPT TISQEKAAIL LYSYVKYLEK SDLWVKDQFY 

       430        440        450        460        470        480 
QGSKWLSSAF QVHHKKVVIP LLYVAITGKK QGLPLFDSME LLGKPRTRAR LVHAQNLLGG 

       490        500 
VPKKIQTTID KVLKEEDLES KIFEF 

« Hide

References

[1]"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation."
Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.
Genome Res. 15:629-640(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 27085 / S26/3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR848038 Genomic DNA. Translation: CAH63637.1.
RefSeqYP_219608.1. NC_004552.2.

3D structure databases

ProteinModelPortalQ5L6T4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218497.CAB179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH63637; CAH63637; CAB179.
GeneID3337734.
KEGGcab:CAB179.
PATRIC20201752. VBIChlAbo21869_0197.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPAHSYLW.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCABO218497:GJB0-192-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_CHLAB
AccessionPrimary (citable) accession number: Q5L6T4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 21, 2005
Last modified: February 19, 2014
This is version 55 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