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Q661P7 (SYE_BORGA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:BG0371
OrganismBorrelia garinii (strain PBi) [Complete proteome] [HAMAP]
Taxonomic identifier290434 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length490 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 – 490490Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119518

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif251 – 2555"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2541ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q661P7 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 100D7D999A886175

FASTA49056,972
        10         20         30         40         50         60 
MSIRVRYAPS PTGLQHIGGI RTALFNYFFA KSCGGKFLLR IEDTDQSRYF PEAENDLYSS 

        70         80         90        100        110        120 
LKWLGISFDE GPIVGGDYAP YVQSQRSAIY KKYAKYLIES GHAYYCYCSP ERLERIKKIQ 

       130        140        150        160        170        180 
NINKMPPGYD RHCRNLSDDE VENALIKKIN PVVRFKIPLE GETSFDDILL GKITWSNKDI 

       190        200        210        220        230        240 
SPDPVILKSD GLPTYHLANV VDDYLMKITH VLRSQEWVSS GPLHILLYKA FEWKSPIYCH 

       250        260        270        280        290        300 
LPMVMGNDGQ KLSKRHGSTA LRQFIEDGYL PEAIINYVTL LGWSYDDKRE FFSKNDLEQF 

       310        320        330        340        350        360 
FSIEKINKSS AIFDYHKLDF FNSYYIKEKK DEDLYNLLLP FFQKKGYVSE LITLEESQKL 

       370        380        390        400        410        420 
KLLIPLIKNR IKKLSDALNM TKFFYEDIKS WNLDEFLNRK KTAKEVCYIL ELTKPILEGF 

       430        440        450        460        470        480 
EKRSSEENDK IFYDFAENNG FKLGEILLPI RIAALGSKVS PPLFDSLKLI GKSKVFKRIK 

       490 
LAQEFLRINE 

« Hide

References

[1]"Comparative analysis of the Borrelia garinii genome."
Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U., Schilhabel M., Wilske B., Suehnel J., Platzer M.
Nucleic Acids Res. 32:6038-6046(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PBi.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000013 Genomic DNA. Translation: AAU07224.1.
RefSeqYP_072816.1. NC_006156.1.

3D structure databases

ProteinModelPortalQ661P7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290434.BG0371.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU07224; AAU07224; BG0371.
GeneID2957485.
KEGGbga:BG0371.
PATRIC20566303. VBIBorGar102262_0477.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBGAR290434:BG0371-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_BORGA
AccessionPrimary (citable) accession number: Q661P7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 65 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