Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6D206 (SYE_PECAS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. 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:ECA3291
OrganismPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica) [Complete proteome] [HAMAP]
Taxonomic identifier218491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length471 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 – 471471Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119563

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6D206 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: FBD5FFE58A6677DA

FASTA47153,367
        10         20         30         40         50         60 
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RHQDGEFVLR IEDTDLERST QDAIDAIMDG 

        70         80         90        100        110        120 
MNWLSLNWDE GPYYQTKRFD RYNAVIDQML ENGTAYKCYC SKERLEALRE QQMEKGDKPR 

       130        140        150        160        170        180 
YDGHCRGSHE HHADNEPHVV RFLNPQEGSV IFNDRIRGPI EFSNQELDDL IIRRTDGSPT 

       190        200        210        220        230        240 
YNFCVVIDDW DMEITHVIRG EDHINNTPRQ INILKALGAP VPEYAHVSMI LGDDGKKLSK 

       250        260        270        280        290        300 
RHGAVGVMQY RDDGYLPEAL LNYLVRLGWS SGDQEIFSID EMKSLFSLDA VNKSASAFNT 

       310        320        330        340        350        360 
EKLQWLNHHY INHLPAEYVA THLSWHIEQA GLDTRTGPQL SELVGLLGER CKTLKEMADS 

       370        380        390        400        410        420 
CRYFYEDFAE FDADAAKKHL RPVARQPLEL VREKLAAITS WTAENIHHAI QGTADELGQG 

       430        440        450        460        470 
MGKVGMPLRV AVTGAGQSPG VDVTVHAIGQ QRSLARIDKA LAFIAERETQ Q 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG76189.1.
RefSeqYP_051380.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6D206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218491.ECA3291.

Proteomic databases

PRIDEQ6D206.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG76189; CAG76189; ECA3291.
GeneID2882140.
KEGGeca:ECA3291.
PATRIC20481931. VBIPecAtr54885_3339.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPATR218491:GJNB-3343-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_PECAS
AccessionPrimary (citable) accession number: Q6D206
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 67 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