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Q02W76 (SYE_LACLS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:LACR_2346
OrganismLactococcus lactis subsp. cremoris (strain SK11) [Complete proteome] [HAMAP]
Taxonomic identifier272622 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length483 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 – 483483Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001914

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif255 – 2595"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02W76 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: C720FE0FACA77DB6

FASTA48355,368
        10         20         30         40         50         60 
MNKKIRVRYA PSPTGLLHIG NARTALFNYL FARHHGGDFI IRIEDTDRER HVEDGERSQL 

        70         80         90        100        110        120 
ENLRWLGMDW DESPETHENY RQSERLPLYQ KYIDQLLAEG KAYYSYKTPE ELEADHAKQE 

       130        140        150        160        170        180 
AAGIPPHYIN EYAGMSDDEK AAYIAERKAQ NIEPVVRISV DEKAIYKWND IVKGEIEFEG 

       190        200        210        220        230        240 
GNIGGDWVIQ KRDGYPTYNF AVVVDDHDMQ ISHVIRGDDH IANTPKQLVV YDALGWEAPQ 

       250        260        270        280        290        300 
FGHMTLIINS ETGKKLSKRD TNTLQFIEDY RKKGYMSDAI FNFIALLGWN PGGEKEIFSR 

       310        320        330        340        350        360 
EELIELFDEN RLSKSPAAFD QKKLDWMDNE YIKNADFAKV FELTKPFLLA ANRFDERAQE 

       370        380        390        400        410        420 
LVKLYQPQMK SADEVVELTD LFYGDFPELT DEAREMLAAE TTPLALSTFR AKLAELPESD 

       430        440        450        460        470        480 
FTVENIFPLF KATQKETGVK GKMLWMPIRI AASGSMHGPE LPETIALLGK EKVLAHLDAA 


LNK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000425 Genomic DNA. Translation: ABJ73796.1.
RefSeqYP_811909.1. NC_008527.1.

3D structure databases

ProteinModelPortalQ02W76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272622.LACR_2346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ73796; ABJ73796; LACR_2346.
GeneID4433965.
KEGGllc:LACR_2346.
PATRIC22291563. VBILacLac38071_2512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLLAC272622:GJUG-2346-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_LACLS
AccessionPrimary (citable) accession number: Q02W76
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 57 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