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B1HNM5 (SYE_LYSSC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:Bsph_4644
OrganismLysinibacillus sphaericus (strain C3-41) [Complete proteome] [HAMAP]
Taxonomic identifier444177 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

Protein attributes

Sequence length486 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 – 486486Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090086

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1081Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1361Zinc By similarity
Metal binding1381Zinc By similarity
Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1HNM5 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 7CDABB981E3A5CB4

FASTA48655,274
        10         20         30         40         50         60 
MTKEVRVRYA PSPTGFLHIG GARTALFNYL YAKHHNGKFI VRIEDTDIER NVEGGEASQL 

        70         80         90        100        110        120 
DNLKWLGIEY DESIDIGGPY APYRQMERLD IYKEHAEKLL AQGAAYKCFC SSEKLEASRE 

       130        140        150        160        170        180 
EQKARGVAAP TYDGTCRHLS AEEVAAKEAA GEPYTIRMRV PENVTYDFED LVRGQVTFES 

       190        200        210        220        230        240 
KDIGDWVIVK ANGIPTYNYA VVLDDHFMEI SHVFRGEEHL SNTPKQMMIF DAFGWEYPRF 

       250        260        270        280        290        300 
GHMTLIINEN RKKLSKRDES IIQFVTQYKD LGYLPEAMFN FFALLGWSPE GEEEIFSKEE 

       310        320        330        340        350        360 
FIKIFDEKRL SKSPSMFDKQ KLTWMNNQYI KKLSLEEVVA LSLPHLQKAG LLPDELSAVQ 

       370        380        390        400        410        420 
HAWATDLIGL YHDQMSFGAE IVELSSLFFK DHIEYDEEAK AVLAGEQVPE VMAAFKAQLE 

       430        440        450        460        470        480 
ELEEFTPDAV KAAIKAVQKA TGHKGKNLFM PIRVVTTGET HGPELPNAIC LIGKEKAIDR 


VEKFAQ 

« Hide

References

[1]"Complete genome sequence of the mosquitocidal bacterium Bacillus sphaericus C3-41 and comparison with those of closely related Bacillus species."
Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M., Berry C., Yuan Z.
J. Bacteriol. 190:2892-2902(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C3-41.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000817 Genomic DNA. Translation: ACA42088.1.
RefSeqYP_001700218.1. NC_010382.1.

3D structure databases

ProteinModelPortalB1HNM5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444177.Bsph_4644.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA42088; ACA42088; Bsph_4644.
GeneID6024547.
KEGGlsp:Bsph_4644.
PATRIC22421807. VBILysSph89750_4721.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLSPH444177:GJEL-4643-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_LYSSC
AccessionPrimary (citable) accession number: B1HNM5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 42 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