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P15189 (SYE_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 106. 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:R02903
ORF Names:SMc03172
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length485 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 – 485485Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119633

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Experimental info

Sequence conflict4271Missing in AAC35209. Ref.1
Sequence conflict4851K → KQ Ref.2

Sequences

Sequence LengthMass (Da)Tools
P15189 [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: 01897C93708FE978

FASTA48554,300
        10         20         30         40         50         60 
MADSAVRVRI APSPTGEPHV GTAYIALFNY LFAKKHGGKF ILRIEDTDAT RSTPEFEKKV 

        70         80         90        100        110        120 
LDALKWCGLE WSEGPDIGGP YGPYRQSDRK DIYKPYVEKI VANGHGFRCF CTPERLEQMR 

       130        140        150        160        170        180 
EAQRAAGKPP KYDGLCLSLS AEEVTSRVDA GEPHVVRMKI PTEGSCKFRD GVYGDVEIPW 

       190        200        210        220        230        240 
EAVDMQVLLK ADGMPTYHMA NVVDDHLMKI THVARGEEWL ASVPKHILIY QYLGLEPPVF 

       250        260        270        280        290        300 
MHLSLMRNAD KSKLSKRKNP TSISYYTALG YLPEALMNFL GLFFIQIAEG EELLTMEELA 

       310        320        330        340        350        360 
EKFDPENLSK AGAIFDIQKL DWLNARWIRE KLSEEEFAAR VLAWAMDNER LKEGLKLSQT 

       370        380        390        400        410        420 
RISKLGELPD LAAFLFKSDL GLQPAAFAGV KASPEEMLKI LNTVQPDLEK ILEWNKDSIE 

       430        440        450        460        470        480 
TELRASAERM GKKLKAVVAP LFVACSGSQR SLPLFDSMEL LGRSVVRQRL KVAAQVVASM 


AGSGK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the gltX gene, encoding the glutamyl-tRNA synthetase of Rhizobium meliloti A2."
Laberge S., Gagnon Y., Bordeleau L.M., Lapointe J.
J. Bacteriol. 171:3926-3932(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A2.
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27221 Genomic DNA. Translation: AAC35209.1.
AL591688 Genomic DNA. Translation: CAC47482.1.
PIRSYRZET. A32888.
RefSeqNP_387009.1. NC_003047.1.

3D structure databases

ProteinModelPortalP15189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc03172.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC47482; CAC47482; SMc03172.
GeneID1234580.
KEGGsme:SMc03172.
PATRIC23635390. VBISinMel96828_4424.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-2972-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_RHIME
AccessionPrimary (citable) accession number: P15189
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 2, 2001
Last modified: February 19, 2014
This is version 106 of the entry and version 2 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