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A9VNA0 (SYE_BACWK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:BcerKBAB4_0082
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP]
Taxonomic identifier315730 [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.

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_1000090053

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
A9VNA0 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 5A0690BA708F3F51

FASTA48555,579
        10         20         30         40         50         60 
MEKQVRVRYA PSPTGHLHIG NARTALFNYL FARHQDGKFI IRIEDTDVKR NVAGGEESQL 

        70         80         90        100        110        120 
KYLKWLGMDW DEGVDVGGEF GPYRQTERLD IYKKLYKDLL ERDLAYKCYM TEEELEAERE 

       130        140        150        160        170        180 
GQIARGETPR YAGNHRDLTE EQIKGFEAEG RIPSIRFRVP ADSDYTFKDL VKDEVAFHSN 

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

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

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

       370        380        390        400        410        420 
AWVRDVIALY HDQMSFGAEI VELSEMFFKD HVDHEEEGQE VLKGEQVPEV LRAFADQLEA 

       430        440        450        460        470        480 
LEAMEPAAVK AAIKAVQKET GHKGKNLFMP IRVATTGQTH GPELPNAIAL LGKEKVLNRI 


QKVIG 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KBAB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000903 Genomic DNA. Translation: ABY41351.1.
RefSeqYP_001642979.1. NC_010184.1.

3D structure databases

ProteinModelPortalA9VNA0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315730.BcerKBAB4_0082.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY41351; ABY41351; BcerKBAB4_0082.
GeneID5840433.
KEGGbwe:BcerKBAB4_0082.
PATRIC19004478. VBIBacWei55973_0647.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBWEI315730:GHRU-111-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_BACWK
AccessionPrimary (citable) accession number: A9VNA0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 47 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