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

A0M6K0 (SYE_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:GFO_3302
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length505 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 – 505505Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330972

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif260 – 2645"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2631ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0M6K0 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: EB97044506B9F445

FASTA50558,397
        10         20         30         40         50         60 
MSSKVRVRFA PSPTGPLHIG GVRTALYNYL FAKKHGGDFV LRIEDTDQNR YVEGAEDYII 

        70         80         90        100        110        120 
EALNWCGIPY DEGPGKEKGF GPYRQSERKD QYREYAEKLI KSGNAYYAFD TSDELDGHRK 

       130        140        150        160        170        180 
DHEEKGKTFI YNWHNRQKLK NSLSLSQEEV QEKLDGEEDY VIRFKSPQDE TLHLKDVIRG 

       190        200        210        220        230        240 
DMEIDTNILD DKVLFKSDGM PTYHLANIVD DHLMEITHVI RGEEWLPSLA LHYMLYRAFG 

       250        260        270        280        290        300 
WNAPQFAHLP LILKPQGKGK LSKRDGEKMG FPVFPLEWKD PESGDISAGY KEEGYFPEAV 

       310        320        330        340        350        360 
VNMLAFLGWN PGTEEEFFGL EDLTKAFELE RVHKGGAKFD PEKTKWFQQH YIQLADNEFL 

       370        380        390        400        410        420 
ADEFEKRLEK KEIEADKIYI SEVVALIKER VVFVEDFWDQ GYFFFIAPTS FDPKDSKKAW 

       430        440        450        460        470        480 
KEGTSELMTE LNEYLKSIDN FEAEHLQETV KGWIKSKEIG FGKVMMPLRI ALVGALQGPD 

       490        500 
LYKIAEFIGK EATLKRIQKA VDTLK 

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207366 Genomic DNA. Translation: CAL68245.1.
RefSeqYP_863312.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M6K0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING411154.GFO_3302.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL68245; CAL68245; GFO_3302.
GeneID4651369.
KEGGgfo:GFO_3302.
PATRIC22075340. VBIGraFor5527_3185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAWINGYYL.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycGFOR411154:GI79-3302-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_GRAFK
AccessionPrimary (citable) accession number: A0M6K0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 12, 2006
Last modified: May 14, 2014
This is version 58 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