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Q6NHM1 (SYE_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:DIP1115
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length497 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 – 497497Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119547

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif257 – 2615"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2601ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NHM1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B13C2F52CF212B0B

FASTA49755,744
        10         20         30         40         50         60 
MNIMSDVRVR FCPSPTGTPH VGMVRTALFN WAHARHTGGK LIFRIEDTDA ARDSEESYQA 

        70         80         90        100        110        120 
IIDSLKWLGM DWDEGVIVGG PHEPYRQSQR MDIYKDVLEK LKEAGFVYPA YSTAQEVEER 

       130        140        150        160        170        180 
HKAAGRDPKL GYDNYDRTLT DEQIAAFEAE GRQPVWRLRM PERDWKWNDL VRGEIEFKSS 

       190        200        210        220        230        240 
TQPDYVVARS NGAPLYTLVN PVDDALMGIT HVLRGEDLLP STPRQLALYE ALKVIGVAQQ 

       250        260        270        280        290        300 
TPEFGHLPFV MGEGNKKLSK RDPQSNLFNH RDAGIIPEGM LNYLALLGWS LAGEKDIFSV 

       310        320        330        340        350        360 
DELVENFDVT NVLANPARFD QKKLEAINAD HIRLLEPKDF EQRLRAYLTE YTDFPTDYPA 

       370        380        390        400        410        420 
EKFAIAAELV QTRIKMLGDA YGLLSFLAIA DEDLTLDEKS AKKNLKETAI PALDAGIAAL 

       430        440        450        460        470        480 
EGVEEWTTPA IEAALHKALI EDLDLKPRVA FGALRVGISG QAVSPPLFES MELLGKESTL 

       490 
TRLRATREVT PYQVAAE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248357 Genomic DNA. Translation: CAE49635.1.
RefSeqNP_939472.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NHM1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP1115.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE49635; CAE49635; DIP1115.
GeneID2650854.
KEGGcdi:DIP1115.
PATRIC21483411. VBICorDip47633_1098.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAPEGMLNY.
OrthoDBEOG6DRPF7.

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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_CORDI
AccessionPrimary (citable) accession number: Q6NHM1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 72 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