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Q1QMM2 (SYE_NITHX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. 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
Ordered Locus Names:Nham_1709
OrganismNitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]
Taxonomic identifier323097 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length474 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.

Sequence caution

The sequence ABE62525.1 differs from that shown. Reason: Erroneous initiation.

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 – 474474Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330985

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif240 – 2445"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QMM2 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 4D1430BDAD4ECD54

FASTA47452,770
        10         20         30         40         50         60 
MIASVVTRFA PSPTGFLHIG GARTALFNWL YARKHGGKML LRIEDTDRAR STTAAIEAIL 

        70         80         90        100        110        120 
DGLKWLGIDW DDDVVYQFSR VARHRDIAEQ LLAEGKAYRC YATPEELAEM REKARAEGRA 

       130        140        150        160        170        180 
KLYDGRWRDR DPSEAPPDLK PTIRLKAPLS GETVIEDQVQ GRVVWQNENL DDLVLLRGDG 

       190        200        210        220        230        240 
TPTYMLAVVV DDHDMGVTHI IRGDDHLINA ARQKQIYDTL GWALPTMAHI PLIHGPDGSK 

       250        260        270        280        290        300 
LSKRHGALGV DAYRAMGYLP AALRNYLVRL GWSHGDQEIF STQEMIDAFD LSAIGRSAAR 

       310        320        330        340        350        360 
FDFAKLENLN GHYIRNCDDH VLVDLFQDAL DYVPRGADLK PKLNDATRAQ LLRAMPGLKE 

       370        380        390        400        410        420 
RAKTLIELID SARFIFADRP LTLDAKAIPL LTSETRALIG RLRTTLETVT SWSAQTTEAA 

       430        440        450        460        470 
MRTFAEQNNL KLGAIAQPLR IALTGRTTSP GIFDVLAVLG KETCLARLDD QSSP 

« Hide

References

[1]"Complete sequence of chromosome of Nitrobacter hamburgensis X14."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X14 / DSM 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000319 Genomic DNA. Translation: ABE62525.1. Different initiation.
RefSeqYP_576985.1. NC_007964.1.

3D structure databases

ProteinModelPortalQ1QMM2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323097.Nham_1709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE62525; ABE62525; Nham_1709.
GeneID4030309.
KEGGnha:Nham_1709.
PATRIC22691080. VBINitHam61822_2562.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycNHAM323097:GHP7-1736-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_NITHX
AccessionPrimary (citable) accession number: Q1QMM2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 60 of the entry and version 2 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