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O86528 (SYE_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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:SCO5547
ORF Names:SC1C2.28
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length494 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119663

Regions

Motif15 – 2511"HIGH" region HAMAP-Rule MF_00022
Motif260 – 2645"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1121Zinc By similarity
Metal binding1141Zinc By similarity
Metal binding1391Zinc By similarity
Metal binding1411Zinc By similarity
Binding site2631ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O86528 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: AC3F4EF4D58D0FAB

FASTA49454,917
        10         20         30         40         50         60 
MASASGSPVR VRFCPSPTGN PHVGLVRTAL FNWAFARHHQ GTLVFRIEDT DAARDSEESY 

        70         80         90        100        110        120 
DQLLDSMRWL GFDWDEGPEV GGPHAPYRQS QRMDIYQDVA QKLLDAGHAY RCYCSQEELD 

       130        140        150        160        170        180 
TRREAARAAG KPSGYDGHCR ELTDAQVEEY TSQGREPIVR FRMPDEAITF TDLVRGEITY 

       190        200        210        220        230        240 
LPENVPDYGI VRANGAPLYT LVNPVDDALM EITHVLRGED LLSSTPRQIA LYKALIELGV 

       250        260        270        280        290        300 
AKEIPAFGHL PYVMGEGNKK LSKRDPQSSL NLYRERGFLP EGLLNYLSLL GWSLSADQDI 

       310        320        330        340        350        360 
FTIEEMVAAF DVSDVQPNPA RFDLKKCEAI NGDHIRLLEV KDFTERCRPW LKAPVAPWAP 

       370        380        390        400        410        420 
EDFDEAKWQA IAPHAQTRLK VLSEITDNVD FLFLPEPVFD EASWTKAMKE GSDALLTTAR 

       430        440        450        460        470        480 
EKLDAADWTS PEALKEAVLA AGEAHGLKLG KAQAPVRVAV TGRTVGLPLF ESLEVLGKEK 

       490 
ALARIDAALA RLAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939124 Genomic DNA. Translation: CAA19995.1.
PIRT29077.
RefSeqNP_629681.1. NC_003888.3.

3D structure databases

ProteinModelPortalO86528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO5547.

Proteomic databases

PRIDEO86528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA19995; CAA19995; CAA19995.
GeneID1100987.
KEGGsco:SCO5547.
PATRIC23740958. VBIStrCoe124346_5635.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
PhylomeDBO86528.
ProtClustDBPRK01406.

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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_STRCO
AccessionPrimary (citable) accession number: O86528
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 95 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