Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A7Z0L4 (SYE_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:RBAM_001170
OrganismBacillus amyloliquefaciens subsp. plantarum (strain DSM 23117 / BGSC 10A6 / FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length483 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 – 483483Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001871

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z0L4 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: F8CE741A129B45BC

FASTA48355,731
        10         20         30         40         50         60 
MGNEVRVRYA PSPTGHLHIG NARTALFNYL FARSQGGKFI IRIEDTDKKR NIEGGEQSQL 

        70         80         90        100        110        120 
NYLKWLGMDW DESVDIGGEY GPYRQSERND IYKKYYEELL EKGLAYKCFC TEEELEKERE 

       130        140        150        160        170        180 
EQIARGEMPR YSGKHRNLTQ EEQERFLAEG RQPSIRFRVP EGKIIAFNDI VKGEISFESD 

       190        200        210        220        230        240 
GIGDFVIVKK DGTPTYNFAV AIDDYLMKMT HVLRGEDHIS NTPKQIMIFQ AFGWDVPVFG 

       250        260        270        280        290        300 
HMTLIVNESR KKLSKRDESI IQFIEQYDEL GYLPEALFNF IGLLGWSPVG EEELFTREQF 

       310        320        330        340        350        360 
IEIFDVNRLS KSPALFDMHK LKWVNNQYVK ALDLDQVVEL TLPHLQKAGK VGTELSAEEQ 

       370        380        390        400        410        420 
EWVRKLISLY HEQLSYGAEI VELTDLFFKD EIEYNQEAKA VLEEEQVPEV LSVFAAKLEE 

       430        440        450        460        470        480 
LEEFTPELIK ASIKAVQKET GHKGKKLFMP IRVAVTGQTH GPELPQAIEL IGRETAVRRL 


KSI 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 23117 / BGSC 10A6 / FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS72540.1.
RefSeqYP_001419771.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z0L4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326423.RBAM_001170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS72540; ABS72540; RBAM_001170.
GeneID5460825.
KEGGbay:RBAM_001170.
PATRIC18745129. VBIBacAmy31356_0098.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycBAMY326423:GCM4-117-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_BACA2
AccessionPrimary (citable) accession number: A7Z0L4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 48 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