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B6J5A0 (SYE1_COXB1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:CbuK_0394
OrganismCoxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)) [Complete proteome] [HAMAP]
Taxonomic identifier434924 [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.

Sequence caution

The sequence ACJ19684.1 differs from that shown. Reason: Erroneous initiation.

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_0000367657

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
B6J5A0 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: DE14304AEA0AB42A

FASTA46953,730
        10         20         30         40         50         60 
MKHIRTRFAP SPTGYLHIGG VRTALFSWLF ARQNNGAFIL RIEDTDVARS TQASVDAILE 

        70         80         90        100        110        120 
GLRWLQIDWN EGPYYQSQRM DRYREVIEQL VKSDDAYRCY CSKERLIELR 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 KAFATQLEKA GTDLRNGPSL EQVIALQAER TKTLKEMAQR 

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

       430        440        450        460 
LGQLAQPIRV ALTGDTVSPP IDATLYLIGR DSALKRLDHA IRFIHQGMG 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CbuK_Q154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001020 Genomic DNA. Translation: ACJ19684.1. Different initiation.
RefSeqYP_002304829.1. NC_011528.1.

3D structure databases

ProteinModelPortalB6J5A0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434924.CbuK_0394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ19684; ACJ19684; CbuK_0394.
GeneID7014907.
KEGGcbc:CbuK_0394.
PATRIC17916193. VBICoxBur77120_0418.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCBUR434924:GHWU-392-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_COXB1
AccessionPrimary (citable) accession number: B6J5A0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 37 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