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B2A4B3 (SYE_NATTJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:Nther_0168
OrganismNatranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF) [Complete proteome] [HAMAP]
Taxonomic identifier457570 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaNatranaerobialesNatranaerobiaceaeNatranaerobius

Protein attributes

Sequence length488 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 – 488488Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367717

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1081Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1351Zinc By similarity
Metal binding1371Zinc By similarity
Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2A4B3 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 83CFE1333CDD8F03

FASTA48855,984
        10         20         30         40         50         60 
MTNKARLRFA PSPTGQIHIG NIRTALFNWL YSRHIDGEFI LRVEDTDMNR SVEEYEQIIF 

        70         80         90        100        110        120 
RALSWLGLDW DEGPQKGGDF GPYRQSERKD IYHKYANKLL EAGKAYYCYC TEEELEEMRE 

       130        140        150        160        170        180 
AQRARGEMPR YSGKCADLSS EERAELENEG RKSVIRFKVP ENQTIRVNDL VKGEVDFESD 

       190        200        210        220        230        240 
GIGDFILIKS DDMASYNFAC VVDDYLMNIT HVLRGEDHLS NTPKQVMIYE ALGFETPEFG 

       250        260        270        280        290        300 
HLSLILGPDK AKLSKRHGDT FIGEYREKGY LPEAMVNFLA LLGWSPPGED ELFTQDELIR 

       310        320        330        340        350        360 
LFDIGRVSKS AAVFDVDKLN WMNSHYIKEA DTERLLNLSK EYLINSDLVS QEQLEHDWEW 

       370        380        390        400        410        420 
FVSAVDLVKE KIDMLSELPP QLKIFYGDDV DLKGEEVEFL EKDHVPELLS EVINQFNDLD 

       430        440        450        460        470        480 
SFEDPKAIKK AVNKAGKQVG VKGKQLFMPV RIAVSGQMHG PELDQLISLL GRERAINRVN 


STLSQIQS 

« Hide

References

[1]"Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-LF."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001034 Genomic DNA. Translation: ACB83767.1.
RefSeqYP_001916355.1. NC_010718.1.

3D structure databases

ProteinModelPortalB2A4B3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING457570.Nther_0168.

Proteomic databases

PRIDEB2A4B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB83767; ACB83767; Nther_0168.
GeneID6316550.
KEGGnth:Nther_0168.
PATRIC22668934. VBINatThe92436_0185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycNTHE457570:GHRL-185-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_NATTJ
AccessionPrimary (citable) accession number: B2A4B3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 42 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