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Q83GP4 (SYE_TROWT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. 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
Synonyms:gltS
Ordered Locus Names:TWT_209
OrganismTropheryma whipplei (strain Twist) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier203267 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length480 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119689

Regions

Motif12 – 2211"HIGH" region HAMAP MF_00022_B
Motif255 – 2595"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83GP4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 798470EDC1A71F42

FASTA48054,801
        10         20         30         40         50         60 
MRDPRVRVRF CPSPTGAPHL GLVRTALFNW VFARKHGGGF IFRIEDTDAT RNREESCSQL 

        70         80         90        100        110        120 
IDTLKWLGLD WDEGPDKGGQ FGPYYQSQRG DIYQEVLDKL LAADLAYESF STKEEIEKRN 

       130        140        150        160        170        180 
LEAGRPIQLG YDNYDRTLSE QTKAAMREAG RTPIIRLRMD DENIAFEDLV KGEVVFTDPI 

       190        200        210        220        230        240 
PDFALTRASG EPLYTLVNPV DDAFMKITHV LRGEDLLSST PRQIALYKAL ITIGITDYVP 

       250        260        270        280        290        300 
FFGHLPIVMG EGNRKLSKRN PESDFYFYKA RGFIREGLLN YLSLLGWSIS NSRDTFSLSE 

       310        320        330        340        350        360 
MIHAFDVRDV RGNPARFDYK KCLAINAYHL RELNVEDFFL RLVPFVEEML GIPLSFEQKN 

       370        380        390        400        410        420 
SLRAICPFVQ GRVQLLTEAA EMVRFLLVDN ISVDFAVTDK EIDVLRHCLA LLNLLDTWES 

       430        440        450        460        470        480 
AQIASCIKQA IEQFDLQPKR IFSILRLAIT GRRVSPPLFE SMQILGRSAS LNRVETFVTN 

« Hide

References

[1]"Tropheryma whipplei twist: a human pathogenic Actinobacteria with a reduced genome."
Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M., Claverie J.-M.
Genome Res. 13:1800-1809(2003) [PubMed: 12902375] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Twist.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014184 Genomic DNA. Translation: AAO44306.1.
RefSeqNP_787337.1. NC_004572.3.

3D structure databases

ProteinModelPortalQ83GP4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ83GP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1482479.
GenomeReviewsGene locus TWT_209 in contig AE014184_GR.
KEGGtwh:TWT209.
PATRIC23996903. VBITroWhi72342_0336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAIEWFNLD.
PhylomeDBQ83GP4.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycTWHI203267:TW209-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_TROWT
AccessionPrimary (citable) accession number: Q83GP4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families