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B2G868 (SYE_LACRJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:LAR_1134
OrganismLactobacillus reuteri (strain JCM 1112) [Complete proteome] [HAMAP]
Taxonomic identifier557433 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length501 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 – 501501Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090084

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif257 – 2615"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2601ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2G868 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 299495BBD03FBE6A

FASTA50158,350
        10         20         30         40         50         60 
MDQKVRVRYA PSPTGFLHIG NAQSALFNYL FARHFDGTMV LRIEDTDTKR NVEDGEASQR 

        70         80         90        100        110        120 
ENLHWLGIDW DEGPNKPNPK YAPYRQSERN KEGIYHKYIQ ELLDKGIAYK DYSTEEELAE 

       130        140        150        160        170        180 
MRERQKANNE PPHYDGRWYG KSEEEQKAAE AKGLKPTIRF HFPKDHDYEW DDIARGHVSF 

       190        200        210        220        230        240 
NSDNLGGDFI IEKSDGMPTY NFAVVVDDHT MDITHVLRGA DHISNTPKQI AIYEALGWEH 

       250        260        270        280        290        300 
PTFCHIPLIF NPKTRKKLSK RDKDTLQFIS EYKKHGYLHE AIFNFIAFLG WSPVGEREIY 

       310        320        330        340        350        360 
SKEELIKVYD PKRMSKAPAY FDQKKLDWMN AQYIKSMSID ELTDRTMELI KEGETEEAKR 

       370        380        390        400        410        420 
LQSIPEEQLT ELLKKTIKVH QRDVNKLLEV IQYAWSYYTV LDQSFNYDLL KDNEDFANED 

       430        440        450        460        470        480 
VLAVLKGLKA KLENGDDDLD YSQAIKEVGK DTGIKGRGLY FPLNLAFTGS TSAPQIYEIM 

       490        500 
DIYSRDTDIE LLDRMIKAFE N 

« Hide

References

[1]"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 1112.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007281 Genomic DNA. Translation: BAG25650.1.
RefSeqYP_001842130.1. NC_010609.1.

3D structure databases

ProteinModelPortalB2G868.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557433.LAR_1134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG25650; BAG25650; LAR_1134.
GeneID6231269.
KEGGlrf:LAR_1134.
PATRIC22259788. VBILacReu111271_1250.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMACDCTREA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLREU557433:GHNR-1195-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_LACRJ
AccessionPrimary (citable) accession number: B2G868
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 45 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