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A1AWC3 (SYE_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:Rmag_0474
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length454 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 – 454454Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330994

Regions

Motif7 – 1711"HIGH" region HAMAP-Rule MF_00022
Motif230 – 2345"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding961Zinc By similarity
Metal binding981Zinc By similarity
Metal binding1231Zinc By similarity
Metal binding1251Zinc By similarity
Binding site2331ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1AWC3 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: C7FE21E05A226755

FASTA45451,820
        10         20         30         40         50         60 
MKSRFAPSPT GCLHIGGART ALFAWVWAKK QHGKFVLRIE DTDLERSNQA SVDAILQGMN 

        70         80         90        100        110        120 
WLGLDYDEGP FYQTDRFNRY KQVVRQLLDE KKAYYCECSK ERLQILHEDL IKQGKKVRYD 

       130        140        150        160        170        180 
GCCRDKNLND GVVRFNNPED GLVIFNDVIK GQISINNKEL DDLIIVRSDG TPTYNLTVVV 

       190        200        210        220        230        240 
DDHDMQIDCV IRGDDHINNT PKQINLYQAL GWHLPEFAHL PMILSSDGAR LSKRHDAVSI 

       250        260        270        280        290        300 
MTYRDAGFLP EALLNYLARL GWSYGDQEIF SMDEIVKLFE LKSINKAPAS FNQDKLLWLN 

       310        320        330        340        350        360 
QKIIKNSSVE NLLNNLTWHL QNQAITITNA PNIEAVVQYL QNRCKTLVDM AGEVKMFYQD 

       370        380        390        400        410        420 
FDTFDEKLAK RYLKDKTPLK HLFAKLEALR IWKANNIKQA VKEVCFELNI SFGKVGQPFR 

       430        440        450 
LALSGNGNAG SIDIVAELVG KNKALSRLKM AIDS 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL02230.1.
RefSeqYP_903701.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AWC3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413404.Rmag_0474.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL02230; ABL02230; Rmag_0474.
GeneID4554799.
KEGGrma:Rmag_0474.
PATRIC32000621. VBICanRut45856_0529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHYIKELD.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCRUT413404:GHM7-494-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_RUTMC
AccessionPrimary (citable) accession number: A1AWC3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 60 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