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B3QYR1 (SYE_CHLT3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:Ctha_2685
OrganismChloroherpeton thalassium (strain ATCC 35110 / GB-78) [Complete proteome] [HAMAP]
Taxonomic identifier517418 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChloroherpeton

Protein attributes

Sequence length503 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 – 503503Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090064

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3QYR1 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: D620D74DFFFBC062

FASTA50357,584
        10         20         30         40         50         60 
MSEQTIRTRF APSPTGYLHV GGLRTALYNF LFAKKNGGQF LLRLEDTDRA RLVEGAVENL 

        70         80         90        100        110        120 
LSSLEWAGII PDESPKHGGD FGPYVQSERL DIYKQYVQQL LDEKKAYYCF ATPDELEESR 

       130        140        150        160        170        180 
QLQIKQGVQP KYNRKWLPED MGGSMPQSEI QKRLDAGEPC VIRMKIPDHT RIRHDDIIRG 

       190        200        210        220        230        240 
IVWFDSSTVD DQVLMKSDGF PTYHLASVVD DHLMNITHVI RGEEWLSSTP KHLLLYDFFG 

       250        260        270        280        290        300 
WEKPEFAHLP LLLNPDRSKL SKRQGDVAVE DYMAKGYSKD ALVNFVALLG WNEGEGVEQE 

       310        320        330        340        350        360 
VYSMNELIEK FTLEKVGKSG AVFNVEKLNW IQKQHLKLVS HEDLAKQAKA ILVEKLKERE 

       370        380        390        400        410        420 
SMMPSEKITD DAYLLNVVEL MHDRVNFVHE FVTFSEYFFF EPEAYEEAAI KKRWKENTND 

       430        440        450        460        470        480 
LLSEFKGILA GLDNFNSAAI EEALAKYAEL KGVKNAALIH PIRLAVSGVS FGPSLYHLME 

       490        500 
VIGKEACLRR IERAVDKLDY QEA 

« Hide

References

[1]"Complete sequence of Chloroherpeton thalassium ATCC 35110."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35110 / GB-78.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001100 Genomic DNA. Translation: ACF15134.1.
RefSeqYP_001997581.1. NC_011026.1.

3D structure databases

ProteinModelPortalB3QYR1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING517418.Ctha_2685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF15134; ACF15134; Ctha_2685.
GeneID6423775.
KEGGcts:Ctha_2685.
PATRIC21434675. VBIChlTha99257_3121.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCTHA517418:GHTO-2735-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_CHLT3
AccessionPrimary (citable) accession number: B3QYR1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 40 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