Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q4QNR5 (SYE_HAEI8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:NTHI0382
OrganismHaemophilus influenzae (strain 86-028NP) [Complete proteome] [HAMAP]
Taxonomic identifier281310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

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-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 – 480480Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119573

Regions

Motif21 – 3111"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1101Zinc By similarity
Metal binding1121Zinc By similarity
Metal binding1371Zinc By similarity
Metal binding1391Zinc By similarity
Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4QNR5 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: DB8806EE7266AA3A

FASTA48054,835
        10         20         30         40         50         60 
MKLDAPFNLD PNVKVRTRFA PSPTGYLHVG GARTALYSWL YAKHNNGEFV LRIEDTDLER 

        70         80         90        100        110        120 
STPEATAAII EGMEWLNLPW EHGPYYQTKR FDRYNQVIDE MIEQGLAYRC YCTKEHLEEL 

       130        140        150        160        170        180 
RHTQEQNKEK PRYDRHCLHD HNHSPDEPHV VRFKNPTEGS VVFDDAVRGR IEISNSELDD 

       190        200        210        220        230        240 
LIIRRTDGSP TYNFCVVVDD WDMGITHVVR GEDHINNTPR QINILKAIGA PIPTYAHVSM 

       250        260        270        280        290        300 
INGDDGQKLS KRHGAVSVMQ YRDDGYLPEA LINYLVRLGW GHGDQEIFSR EEMINYFELD 

       310        320        330        340        350        360 
HVSKSASAFN TEKLQWLNQH YIRELPPEYV AKHLEWHYKD QSIDTSNGPA LTDIVSMLAE 

       370        380        390        400        410        420 
RCKTLKEMAS SSRYFFEEFE TFDEAAAKKH FKGNAAEALA KVKEKLTALS SWNLHSIHEA 

       430        440        450        460        470        480 
IEQTAAELEV GMGKVGMPLR VAVTGSGQSP SMDVTLVGIG RDRVLVRIQR AIDFIHAQNA 

« Hide

References

[1]"Genomic sequence of an otitis media isolate of nontypeable Haemophilus influenzae: comparative study with H. influenzae serotype d, strain KW20."
Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., Munson R.S. Jr.
J. Bacteriol. 187:4627-4636(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 86-028NP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000057 Genomic DNA. Translation: AAX87332.1.
RefSeqYP_247992.1. NC_007146.2.

3D structure databases

ProteinModelPortalQ4QNR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281310.NTHI0382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX87332; AAX87332; NTHI0382.
GeneID3429707.
KEGGhit:NTHI0382.
PATRIC20180933. VBIHaeInf100748_0348.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycHINF281310:GJ89-359-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_HAEI8
AccessionPrimary (citable) accession number: Q4QNR5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: July 19, 2005
Last modified: February 19, 2014
This is version 58 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