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Q01WJ8 (SYE_SOLUE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:Acid_5011
OrganismSolibacter usitatus (strain Ellin6076) [Complete proteome] [HAMAP]
Taxonomic identifier234267 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaSolibacteresSolibacteralesSolibacteraceaeCandidatus Solibacter

Protein attributes

Sequence length472 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 – 472472Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001967

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01WJ8 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 53566FFA7C67A6F8

FASTA47252,434
        10         20         30         40         50         60 
MHRVRFAPSP TGFLHIGSAR TYIFNWLFAR HHGGTMILRI DDTDVGRNSD ASETSIFDGL 

        70         80         90        100        110        120 
AWLGLDWDEQ YRQSERLPLH RAMADAILTK GMAYRDFTPA QAGDSEKSGA QGTWLFNAGM 

       130        140        150        160        170        180 
RELSREESDR RAAAGEPFAL RFRVPHDREG SVQFTDAVYG EQAKGYGDIE DFALLRSDGM 

       190        200        210        220        230        240 
PTYHLANCAD DADLRISHII RGQEHLSNAF KHKLIFDAAG AESPTFAHLP LLMAPDGMKL 

       250        260        270        280        290        300 
SKRVHGPVVS VTTYRDAGFL PQAFINFLSL LGWSPKNDRE KLSREEMVEL FTLEGINRAN 

       310        320        330        340        350        360 
AVVNFTEEEP FDAKALWLNA EHIRAMPAAD LARELLPFVP VDLEKMLQIT PLIQERIKLL 

       370        380        390        400        410        420 
RDVQSVADFF FVKQLPPYDS AELIPKKGDA AMAKNVLIKA CDVLATAEFT HDGLEVALRA 

       430        440        450        460        470 
ASAELGIKAG QMFEPVRVAV CGRKTAPPLF GTLEVLGREA CLARIGQAIE KL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000473 Genomic DNA. Translation: ABJ85967.1.
RefSeqYP_826252.1. NC_008536.1.

3D structure databases

ProteinModelPortalQ01WJ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234267.Acid_5011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ85967; ABJ85967; Acid_5011.
GeneID4426759.
KEGGsus:Acid_5011.
PATRIC32012564. VBICanSol30224_5243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHHAPVVR.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycSUSI234267:GHSK-5052-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_SOLUE
AccessionPrimary (citable) accession number: Q01WJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 54 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