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B5BB76 (SYE_SALPK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:SSPA0415
OrganismSalmonella paratyphi A (strain AKU_12601) [Complete proteome] [HAMAP]
Taxonomic identifier554290 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length471 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 – 471471Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090105

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B5BB76 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 616B4CDBAADCC608

FASTA47153,650
        10         20         30         40         50         60 
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RHHGGEFVLR IEDTDLERST PEAIEAIMDG 

        70         80         90        100        110        120 
MNWLNLEWDE GPYFQTKRFD RYNAVIDEML EAGTAYKCYC SKERLEQLRE DQMAKGEKPR 

       130        140        150        160        170        180 
YDGRCRHSHE HHADDEPCVV RFANPQDGSV IFDDQIRGPI EFSNQELDDL IIRRTDGSPT 

       190        200        210        220        230        240 
YNFCVVVDDW DMEITHVIRG EDHINNTPRQ INILKALNAP VPMYAHVSMI NGDDGKKLSK 

       250        260        270        280        290        300 
RHGAVSVMQY RDDGYLPEAL LNYLVRLGWS SGDQEIFTRE EMIKLFSLGA VSKSASAFNT 

       310        320        330        340        350        360 
DKLLWLNHHY INTLAPEYVA THLQWHIEQE NIDTRNGPQL AELVKLLGER CKTLKEMSQS 

       370        380        390        400        410        420 
CRYFYEDFSE FDADAAKKHL RPVARQPLEV VRDKLSAITD WSAENVHHAI QATADELEVG 

       430        440        450        460        470 
MGKVGMPLRV AVTGAGQSPA LDVTVHAIGK TRSIERINKA LGFIAERESQ Q 

« Hide

References

[1]"Pseudogene accumulation in the evolutionary histories of Salmonella enterica serovars Paratyphi A and Typhi."
Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A., Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N., Mungall K., Dougan G., Parkhill J.
BMC Genomics 10:36-36(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AKU_12601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM200053 Genomic DNA. Translation: CAR58539.1.
RefSeqYP_002141260.1. NC_011147.1.

3D structure databases

ProteinModelPortalB5BB76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING554290.SSPA0415.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR58539; CAR58539; SSPA0415.
PATRIC32340437. VBISalEnt134303_0476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSENT554290:GJDA-441-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_SALPK
AccessionPrimary (citable) accession number: B5BB76
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 38 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