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A0R8F9 (SYE_BACAH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:BALH_0087
OrganismBacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]
Taxonomic identifier412694 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

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.

Sequence caution

The sequence ABK83502.1 differs from that shown. Reason: Erroneous initiation.

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_0000330955

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
A0R8F9 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 506D96D48A9259A1

FASTA48555,616
        10         20         30         40         50         60 
MEKQVRVRYA PSPTGHLHIG NARTALFNYL FARHQDGKFI IRIEDTDVKR NVAGGEESQL 

        70         80         90        100        110        120 
KYLKWLGMDW DEGVDVGGEF GPYRQTERLD IYKKLYEDLL ERGLAYKCYM TEEELEAERE 

       130        140        150        160        170        180 
GQIARGETPR YAGNHRDLTE AQVKEFEAEG RIPSIRFRVP ADRDYTFKDI VKDEVAFHSN 

       190        200        210        220        230        240 
DFGDFVIVKK DGIPTYNFAV AVDDHLMEIT HVLRGDDHIS NTPKQMMIYE AFGWDIPQFG 

       250        260        270        280        290        300 
HMTLIVNESR KKLSKRDESI IQFIEQYKEL GYLPEAIFNF IALLGWSPVG EEEIFSQEEF 

       310        320        330        340        350        360 
IKMFDAARLS KSPALFDSQK LKWMNNQYMK KQDLDTVVEL SLPHLVKAGR IGETLSEQEQ 

       370        380        390        400        410        420 
AWIRDVIALY HEQMSFGAEI VELSEMFFKD HVDYEEEGQE VLKGEQVPEV LRAFAGQVEA 

       430        440        450        460        470        480 
LEAMEPAAIK AAIKAVQKET GHKGKNLFMP IRVATTGQTH GPELPNAIAL LGKEKVLNRL 


QKVIG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000485 Genomic DNA. Translation: ABK83502.1. Different initiation.
RefSeqYP_893009.1. NC_008600.1.

3D structure databases

ProteinModelPortalA0R8F9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412694.BALH_0087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK83502; ABK83502; BALH_0087.
GeneID4542656.
KEGGbtl:BALH_0087.
PATRIC18992159. VBIBacThu63319_0165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBTHU412694:GH1W-108-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_BACAH
AccessionPrimary (citable) accession number: A0R8F9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 55 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