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Q048S3 (SYE_LACDB) 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:LBUL_1560
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365) [Complete proteome] [HAMAP]
Taxonomic identifier321956 [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.

Sequence caution

The sequence ABJ59049.1 differs from that shown. Reason: Erroneous initiation.

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 – 500500Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367697

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
Q048S3 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: DDAF564685854CF7

FASTA50057,192
        10         20         30         40         50         60 
MANKKIRVRY APSPTGHLHI GNARTALFNY LFARHNKGTL VLRIEDTDTA RNVEGGAESQ 

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

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

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

       250        260        270        280        290        300 
EAPVFGHMTL IINSATGKKL SKRDESVLQF IEQYRELGFL PEAMFNFITL 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 FTAKKIMDAI MATRRETGIK GRKLFMPIRI ATTRSMVGPG IGEAMELMGK 

       490        500 
DTVMKHLDLT LKQLSEAGIE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000412 Genomic DNA. Translation: ABJ59049.1. Different initiation.
RefSeqYP_813487.1. NC_008529.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321956.LBUL_1560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ59049; ABJ59049; LBUL_1560.
GeneID4435078.
KEGGlbu:LBUL_1560.
PATRIC22222997. VBILacDel70259_1536.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLDEL321956:GI15-1555-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_LACDB
AccessionPrimary (citable) accession number: Q048S3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 54 of the entry and version 2 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