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Q82JR3 (SYE_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:SAV_2691
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length504 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
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 – 504504Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119662

Regions

Motif25 – 3511"HIGH" region HAMAP-Rule MF_00022
Motif270 – 2745"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1221Zinc By similarity
Metal binding1241Zinc By similarity
Metal binding1491Zinc By similarity
Metal binding1511Zinc By similarity
Binding site2731ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82JR3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A8FE29F9FF1128C9

FASTA50456,013
        10         20         30         40         50         60 
MANANSPKSS TPLGEGVPPR VRFCPSPTGN PHVGLVRTAL FNWAFARHTG GTFVFRIEDT 

        70         80         90        100        110        120 
DAARDSEESY EQLLDSLRWL GFDWDEGPGV GGPHAPYRQS QRMDLYKDVA QKLLDGGYAY 

       130        140        150        160        170        180 
HCYCSTEELD TRRDAARAAG KPSGYDGHCR ELSAEQKAAY EAEGRTPIVR FRMPDEPITF 

       190        200        210        220        230        240 
TDLVRGDITY LPENVPDYGI VRANGAPLYT LVNPVDDALM EITHVLRGED LLSSTPRQVA 

       250        260        270        280        290        300 
LYRALIELGI AKSVPEFGHL PYVMGEGNKK LSKRDPQASL NLYRERGFLP EGLLNYLSLL 

       310        320        330        340        350        360 
GWSLSADRDI FTIDEMVAAF DVKDVNPNPA RFDLKKCEAI NADHIRLLDV KDFTERCRPW 

       370        380        390        400        410        420 
LKAPFANWAP EDFDEAKWQV IAPYAQSRLK VLSEITDNVD FLFLPEPVFD EASWTKAMKE 

       430        440        450        460        470        480 
GSDALLRTAR EKLEAADWTS PESLKEAVLA AGEEHGLKLG KAQAPVRVAV TGRTVGLPLF 

       490        500 
ESLEILGKEK TLARVDAALA KLTA 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC70402.1.
RefSeqNP_823867.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82JR3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_2691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC70402; BAC70402; SAV_2691.
GeneID1210518.
KEGGsma:SAV_2691.
PATRIC23718943. VBIStrAve112782_2881.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPEGMLNY.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-2712-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.
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_STRAW
AccessionPrimary (citable) accession number: Q82JR3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 76 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