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Q2NSC4 (SYE_SODGM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:SG1676
OrganismSodalis glossinidius (strain morsitans) [Complete proteome] [HAMAP]
Taxonomic identifier343509 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis

Protein attributes

Sequence length473 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 – 473473Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237402

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
Q2NSC4 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 756D0593D9FE2489

FASTA47352,969
        10         20         30         40         50         60 
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RHLGGEFLLR IEDTDLERST QPAIDAIMDG 

        70         80         90        100        110        120 
MNWLNLDWDE GPYFQTKRFD RYNAVIDDML SKGTAYHCYC SKERLETLRE AQMARGEKPR 

       130        140        150        160        170        180 
YDGRCRDSHE HHADDEPCVV RFRNPQDGSV VFNDLIRGPI EFSNQELDDL IIRRIDGSPT 

       190        200        210        220        230        240 
YNFCVVVDDF DMAITHVIRG EDHINNTPRQ INILKALGAP VPAYAHVSMI LGDDGKKLSK 

       250        260        270        280        290        300 
RHGAVGVMQY RDDGFLPEAL LNYLVRLGWS HGDQEIFSVD EMKQLFSFEA VSKSASAFNT 

       310        320        330        340        350        360 
EKLLWLNHHY INHLPADYVA THLVLHIEQQ GIDTRTGPQL AALVKLLGER CKTLKEIAAS 

       370        380        390        400        410        420 
CRYFYEDFSE FDADAAKKHL RPVAVLALEA VRANLAALSE WTPATVHAAI EQTAEALQVG 

       430        440        450        460        470 
MGKVGMPLRV AVTGTGQSPA LDVTVHAIGQ SRCLARIVKA LDFIACRTQE SAG 

« Hide

References

[1]"Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
Genome Res. 16:149-156(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: morsitans.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008232 Genomic DNA. Translation: BAE74951.1.
RefSeqYP_455356.1. NC_007712.1.

3D structure databases

ProteinModelPortalQ2NSC4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING343509.SG1676.

Proteomic databases

PRIDEQ2NSC4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE74951; BAE74951; SG1676.
GeneID3868540.
KEGGsgl:SG1676.
PATRIC23653428. VBISodGlo61428_4003.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSGLO343509:GJJC-1735-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_SODGM
AccessionPrimary (citable) accession number: Q2NSC4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 57 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