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A9KBJ3 (SYE1_COXBN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:CBUD_0531
OrganismCoxiella burnetii (strain Dugway 5J108-111) [Complete proteome] [HAMAP]
Taxonomic identifier434922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length465 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.

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 – 465465Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367659

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif249 – 2535"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KBJ3 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 393FE9F270B9F55B

FASTA46552,691
        10         20         30         40         50         60 
MMKSRFCPSP TGLMHLGNAR TALFNYLFAK SKDGIFLLRI EDTDVERSKE TFDLGLKEDL 

        70         80         90        100        110        120 
RWLNLEWQEG PGADEGNGPY HQSKRQAIYD DYYQRLEEAD QAYPCFCSEE QLRLSRKIQR 

       130        140        150        160        170        180 
SAGKPPRYAG TCRSLSAAEI EKKKAEGLQP ALRFRVPDDE VVVFADLVRG EQRFQTNDIG 

       190        200        210        220        230        240 
DFIIRRANGT SPFMFCNAID DALMGVSHVL RGEDHLTNTP RQLLILQALE LPVPTYAHIA 

       250        260        270        280        290        300 
LIVGPDGSPL SKRHGSRGIK ELRDNGYLPL ALTNYLARLG HYYASDELLS LAELAKGFNV 

       310        320        330        340        350        360 
ESLSKSPAKF NAQQLDYWQK QTVNQLPNDD FWEWAGSELQ SQIPTDKADL FLTTVKPNAS 

       370        380        390        400        410        420 
FPRDVAYWVN VCFGKTLNLE TAQSELLRAT GNRYFEEAFE AFKKFGKDLN SVVSHLKEKL 

       430        440        450        460 
NLKGKPLYQP LRIALTGAEH GPELAKLILI MDYETIQNRL QEACQ 

« 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: Dugway 5J108-111.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000733 Genomic DNA. Translation: ABS78423.1.
RefSeqYP_001423945.1. NC_009727.1.

3D structure databases

ProteinModelPortalA9KBJ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434922.CBUD_0531.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS78423; ABS78423; CBUD_0531.
GeneID5457444.
KEGGcbd:CBUD_0531.
PATRIC17920885. VBICoxBur32972_0561.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAFLYARHL.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCBUR434922:GJTP-568-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_COXBN
AccessionPrimary (citable) accession number: A9KBJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 48 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