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Q5L431 (SYE_GEOKA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:GK0083
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length490 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 – 490490Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119566

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif254 – 2585"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1081Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1361Zinc By similarity
Metal binding1381Zinc By similarity
Binding site2571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L431 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 3A61E17B17C03CD0

FASTA49056,438
        10         20         30         40         50         60 
MAKEVRVRYA PSPTGHLHIG GARTALFNYL FARHHGGKMI VRIEDTDIER NVEGGEKSQL 

        70         80         90        100        110        120 
ENLKWLGIDY DESIDQDGGY GPYRQTERLD IYRKYVNELL EQGHAYKCFC TPEELERERE 

       130        140        150        160        170        180 
AQRAAGIAAP QYSGKCRHLT PEQVAELEAQ GKPYTIRLKV PEGKTYEFYD LVRGKVVFES 

       190        200        210        220        230        240 
KDVGGDWVIV KANGIPTYNF AVVIDDHLME ISHVFRGEEH LSNTPKQLMV YEYFGWEPPQ 

       250        260        270        280        290        300 
FAHLTLIVNE QRKKLSKRDE SIIQFVSQYK ELGYLPEAMF NFFALLGWSP EGEEEIFTKD 

       310        320        330        340        350        360 
ELIRMFDVSR LSKSPSMFDT KKLTWMNNQY IKKLDLDRLV ELALPHLVKA GRLPADMTDE 

       370        380        390        400        410        420 
QRQWARDLIA LYQEQMSYGA EIVPLSELFF KEEIDYEDEA RQVLAEEQVP AVLSTFLESV 

       430        440        450        460        470        480 
RELEPFTADE IKAAIKAVQK ATGQKGKKLF MPIRAAVTGQ THGPELPFAI QLLGKEKVIE 

       490 
RLERALQEKF 

« Hide

References

[1]"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTA426.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000043 Genomic DNA. Translation: BAD74368.1.
RefSeqYP_145936.1. NC_006510.1.

3D structure databases

ProteinModelPortalQ5L431.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING235909.GK0083.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD74368; BAD74368; GK0083.
GeneID3185505.
KEGGgka:GK0083.
PATRIC21961225. VBIGeoKau81518_0136.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycGKAU235909:GJO7-107-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_GEOKA
AccessionPrimary (citable) accession number: Q5L431
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 62 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