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O86083 (SYE_LACDE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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
OrganismLactobacillus delbrueckii subsp. bulgaricus
Taxonomic identifier1585 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length500 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
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 – 500500Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119582

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O86083 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 30EAA09133AE6841

FASTA50056,945
        10         20         30         40         50         60 
MANKKIRVRY APSPTGHLHI GNARTALFNY LFARHNKGTL VLRIEDADTE RNVEGGAESQ 

        70         80         90        100        110        120 
IENLHWLGID WDEGPDIGGD YGPYKQSERK DIYQKYIDQL LEEGKAYYSF KTEEELEAQR 

       130        140        150        160        170        180 
EEQRAMGIAP HYVYEYEGMT TDEIKQAQAE ARAKGLKPVV RIHIPEGVTY EWDDIVKGHL 

       190        200        210        220        230        240 
SFESDTIGGD FVIQKRDGMP TYNFAVVIDD HLMEISHVLR GDDHISNTPK QLCVYEALGW 

       250        260        270        280        290        300 
EAPVFGHMTL IINSATGKKL SKRDESVLQF IEQYRELVSC QKPCSTSSSL LGWSPVGESE 

       310        320        330        340        350        360 
IFSKREFIKQ FDPARLSKSP AAFDQKKLDW VNNQYMKTAD RDELLDLALH NLQEAGLVEA 

       370        380        390        400        410        420 
NPAPGKMEWV RQLVNMYANQ MSYTKQIVDL SKIFFTEAKY LTDEEVEEIK KDEARPAIEE 

       430        440        450        460        470        480 
FKKQLDKLDN FTAKKIMGAI MATRRETGIK GRKLFMPIRI ATTRSMVGPG IGEAMELMGK 

       490        500 
DTVMKHLDLT LKQLSEAGIE 

« Hide

References

[1]Ishino Y., Kim S.I., Soell D.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084366 Genomic DNA. Translation: AAC32611.1.

3D structure databases

ProteinModelPortalO86083.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_LACDE
AccessionPrimary (citable) accession number: O86083
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: February 19, 2014
This is version 74 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