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A9NAJ6 (SYE1_COXBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:COXBURSA331_A0298
OrganismCoxiella burnetii (strain RSA 331 / Henzerling II) [Complete proteome] [HAMAP]
Taxonomic identifier360115 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length469 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 – 469469Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367661

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding991Zinc By similarity
Metal binding1011Zinc By similarity
Metal binding1261Zinc By similarity
Metal binding1281Zinc By similarity
Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9NAJ6 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 1C69A513E77FC99D

FASTA46953,696
        10         20         30         40         50         60 
MKHIRTRFAP SPTGYLHIGG VRTALFSWLF ARQNNGAFIL RIEDTDVARS TQASVDAILE 

        70         80         90        100        110        120 
GLRWLQIDWN EGPYYQSQRM DRYREVIEQL VKSDDAYRCY CSKERLIKLR NTQLKNKQKP 

       130        140        150        160        170        180 
RYDGFCRDKA PRQSNEPFVI RFRNPVEGAV VFDDLIRGTI SIDNRELDDL IIARSDGGPT 

       190        200        210        220        230        240 
YNLTVVVDDW DMKITHVIRG DDHINNTPRQ INILHALGAE LPHYGHVPMI LGPDGKRLSK 

       250        260        270        280        290        300 
RHGAVSVLQY RDEGYLPEAL MNYLIRLGWA HGDQEIFSRE EMVQLFDISA VSRSPAAFNP 

       310        320        330        340        350        360 
EKLLWLNQHY LKTVSPTIIA EAFATQLEKA GTDLRNGPSL EQVIALQAER TKTLKEMAQR 

       370        380        390        400        410        420 
SLYFYQEVRS YDEKAARKHL LATIVEPLQR VRERLASLPS WEKEAIHEVI VETAQLHQLK 

       430        440        450        460 
LGQLAQPIRV ALTGDTVSPP IDATLYLIGR DSALKRLDHA IRFIHQGMG 

« Hide

References

[1]"Genome sequencing of phylogenetically and phenotypically diverse Coxiella burnetii isolates."
Seshadri R., Samuel J.E.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RSA 331 / Henzerling II.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000890 Genomic DNA. Translation: ABX77265.1.
RefSeqYP_001596157.1. NC_010117.1.

3D structure databases

ProteinModelPortalA9NAJ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360115.COXBURSA331_A0298.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX77265; ABX77265; COXBURSA331_A0298.
GeneID5794566.
KEGGcbs:COXBURSA331_A0298.
PATRIC17924864. VBICoxBur33747_0332.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCBUR360115:GI0X-304-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 nameSYE1_COXBR
AccessionPrimary (citable) accession number: A9NAJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 46 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