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Q3A413 (SYE_PELCD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:Pcar_1650
OrganismPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]
Taxonomic identifier338963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length466 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 – 466466Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237383

Regions

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

Sites

Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3A413 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: F6E58F0207DCC780

FASTA46652,033
        10         20         30         40         50         60 
MSKLRVRFAP SPTGYLHIGG ARTALFNFLL ARKEQGTFVL RIEDTDVARS TQESVDAILQ 

        70         80         90        100        110        120 
AMDWLGMSCD EGPIYQSDRF DLYRAKIDQL VEQGKAYRCY CTAEELEKKR EAAMQDGRKP 

       130        140        150        160        170        180 
KYDGTCRQLQ EVCDDKPYVI RFKAPQEGAT TFHDRIKGDI TFQNEELDDL IIQRTDGTPT 

       190        200        210        220        230        240 
YNFVVVVDDA EMGINLVLRG DDHINNTPRQ IMLYKALGYP VPDFAHVPMI LGADKSRLSK 

       250        260        270        280        290        300 
RHGATSVMAY KEMGYLPEAL VNYLVRLGWS HGDQEIFTQD ELTQLFSLDN IGKSASVFNP 

       310        320        330        340        350        360 
EKLIWLNSHY IKTGNPGRLA QLLAGHLAAD GIDVANIADL EPIVVALQDR SKTLVDMAQQ 

       370        380        390        400        410        420 
ARCFFADDIQ FDEKAAAKFL IEDNRFVFEA LSAALESCDD WKEDILDGVF KGVLEATGLK 

       430        440        450        460 
FGKLAQPARV ALVGGTTGPS ICLIMQILGR EKTLARLQGA MSRLGQ 

« Hide

References

[1]"Complete sequence of Pelobacter carbinolicus DSM 2380."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2380 / Gra Bd 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000142 Genomic DNA. Translation: ABA88894.1.
RefSeqYP_006717380.1. NC_007498.2.

3D structure databases

ProteinModelPortalQ3A413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338963.Pcar_1650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA88894; ABA88894; Pcar_1650.
GeneID3724352.
KEGGpca:Pcar_1650.
PATRIC22889472. VBIPelCar86875_1796.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADSHEHHA.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPCAR338963:GKDU-1829-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_PELCD
AccessionPrimary (citable) accession number: Q3A413
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 59 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