Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q88YY0 (SYE_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. 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:lp_0609
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length496 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
Reference 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 – 496496Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119585

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
Q88YY0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1A157B4045C06A45

FASTA49656,919
        10         20         30         40         50         60 
MAKSKIRVRY APSPTGHLHI GNARTALFNY LFARHNKGKF ILRIEDTDLK RNVKDGEKSQ 

        70         80         90        100        110        120 
MDNLTWLGID WDEGPDKGGD FGPYRQSERK SIYDPLIQQL IDEGKAYESY MTEDELSAQR 

       130        140        150        160        170        180 
EAQKARKEMP HYVYEFAGMT EDEKQAKIAA AKAAGIQPVI RFHVPENTTY AWDDMVKGKV 

       190        200        210        220        230        240 
SFESKTVGGD FVIKKRDGMP TYNFAVVVDD HMMEISHVFR GDDHVANTPK QLMIYEAFGW 

       250        260        270        280        290        300 
QPPKFGHMSL IINTETGKKL SKRDETVLQF IEQYRELGYL PEAMLNFIIL LGWSPVGESE 

       310        320        330        340        350        360 
LFSKREFIKM YDEKRLSKSP AAFDGKKLEW VNNQYIKKAD ENEVFAMSIR QLIKAGRLPQ 

       370        380        390        400        410        420 
RPDMSQIEWT RTLVSLFKNQ MSYTGQIVDL ADLFFNGPAD INDEAKAELD NDTALPVLKE 

       430        440        450        460        470        480 
FRQRIEDIDV FEATAIQKTI KSIQKDTKIK GRALYMPIRI AVSHEMHGPE LPETIELLGR 

       490 
ETTKKHLDAM IAELAK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL935263 Genomic DNA. Translation: CCC78089.1.
RefSeqYP_004888603.1. NC_004567.2.

3D structure databases

ProteinModelPortalQ88YY0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220668.lp_0609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC78089; CCC78089; lp_0609.
GeneID1061586.
KEGGlpl:lp_0609.
PATRIC22247665. VBILacPla27411_0509.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAKHYDGDF.

Enzyme and pathway databases

BioCycLPLA220668-WGS:GSPK-520-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_LACPL
AccessionPrimary (citable) accession number: Q88YY0
Secondary accession number(s): F9UL74
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 73 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