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A5FPX2 (SYE_DEHMB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:DehaBAV1_1176
OrganismDehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1) [Complete proteome] [HAMAP]
Taxonomic identifier216389 [NCBI]
Taxonomic lineageBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

Protein attributes

Sequence length487 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 – 487487Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000074319

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif245 – 2495"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1081Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1351Zinc By similarity
Metal binding1371Zinc By similarity
Binding site2481ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FPX2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 9C833C01EDFCC08A

FASTA48755,334
        10         20         30         40         50         60 
MTNEVRVRYA PSPTGYPHLG NIRTAMFNWL FARHNGGKFI VRIEDTDRER YVEGAVESIL 

        70         80         90        100        110        120 
ESLNWLGLDW DEGPDKGGDY GPYYQSERLP LYRKAAEKLV AEGKAYYCHC SSEKLDKMRE 

       130        140        150        160        170        180 
DQIARKEPPG YDRCCRDRGL GQKEGAVIRF KIPLDGQTAF TDLIRGEVTF DNAKQDDFVI 

       190        200        210        220        230        240 
LKSDGFPTYH LASVVDDHAM QISHVLRAEE WLPSTPKHLM LYKALGYTPP LYAHLPMILG 

       250        260        270        280        290        300 
PDRSKLSKRH GATSTIEYKQ AGYLPETMVN FLSLLGWAYD DKTELFSREQ LIEYFCLEKV 

       310        320        330        340        350        360 
SKTAAIFNYE KLDWMNGMYI RTLSAQDLAC RAMPFLEKDA RIAASGHLNL DYTVKVMPLI 

       370        380        390        400        410        420 
QERAKKLNEL AELCWFIYSD DISYDPALLI DKKLTKETSL SALKAANARL EALPNFDAAS 

       430        440        450        460        470        480 
MEEHIRPLAA ELELKPGQLF GMLRTASTGQ QVAPPLFQTM EVLGRQRCLG RIAMAIARLS 


EMPSQRS 

« Hide

References

[1]"Complete sequence of Dehalococcoides sp. BAV1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Ritalahti K.M., Loeffler F., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000688 Genomic DNA. Translation: ABQ17755.1.
RefSeqYP_001214633.1. NC_009455.1.

3D structure databases

ProteinModelPortalA5FPX2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216389.DehaBAV1_1176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ17755; ABQ17755; DehaBAV1_1176.
GeneID5131234.
KEGGdeb:DehaBAV1_1176.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycDSP216389:GH6D-1213-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_DEHMB
AccessionPrimary (citable) accession number: A5FPX2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 53 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