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Q8E284 (SYE_STRA5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:SAG0113
OrganismStreptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R) [Complete proteome] [HAMAP]
Taxonomic identifier208435 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length484 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 – 484484Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119661

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
Q8E284 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F052C57934672396

FASTA48455,555
        10         20         30         40         50         60 
MANKIRVRYA PSPTGLLHIG NARTALFNYL YARHHGGDFV IRIEDTDRKR HVEDGERSQL 

        70         80         90        100        110        120 
ENLRWLGMDW DESPETHENY RQSERLELYQ RYIDQLLAEG KAYKSYVTEE ELAAERERQE 

       130        140        150        160        170        180 
LAGETPRYIN EFIGMSETEK EAYIAEREAA GIIPTVRLAV NESGIYKWTD MVKGDIEFEG 

       190        200        210        220        230        240 
SNIGGDWVIQ KKDGYPTYNF AVVIDDHDMQ ISHVIRGDDH IANTPKQLMV YEALGWEAPQ 

       250        260        270        280        290        300 
FGHMTLIINS ETGKKLSKRD TNTLQFIEDY RKKGYMSEAV FNFIALLGWN PGGEEEIFSR 

       310        320        330        340        350        360 
EQLINLFDEN RLSKSPAAFD QKKMDWMSND YLKNADFESV FALCKPFLEE AGRLTDKAEK 

       370        380        390        400        410        420 
LVELYQPQLK SADEIVPLTD LFFADFPELT EAEKEVMAAE TVPTVLSAFK EKLVSLSDEE 

       430        440        450        460        470        480 
FTRDTIFPQI KAVQKETGIK GKNLFMPIRI AVSGEMHGPE LPDTIYLLGK EKSVQHIDNM 


LAKL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009948 Genomic DNA. Translation: AAM99021.1.
RefSeqNP_687149.1. NC_004116.1.

3D structure databases

ProteinModelPortalQ8E284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208435.SAG0113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM99021; AAM99021; SAG0113.
GeneID1012882.
KEGGsag:SAG0113.
PATRIC19626966. VBIStrAga72745_0112.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSAGA208435:GHVY-167-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_STRA5
AccessionPrimary (citable) accession number: Q8E284
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 70 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