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

O33120 (SYE_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. 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
Synonyms:gltS
Ordered Locus Names:ML1688
ORF Names:MLCB637.29
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length502 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 – 502502Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119603

Regions

Motif21 – 3111"HIGH" region HAMAP-Rule MF_00022
Motif265 – 2695"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2681ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O33120 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F618C748C9F24A60

FASTA50255,305
        10         20         30         40         50         60 
MTAVTSDGTP QAAKVRVRFC PSPTGVPHVG MVRTALFNWA YARHTGGTFV LRIEDTDADR 

        70         80         90        100        110        120 
DSEESYLALL DALRWLGLNW DEGPEVGGPY GPYRQSQRTD IYREVVAKLL ATGEAYYAFS 

       130        140        150        160        170        180 
TPEEVENRHL AAGRNPKLGY DNFDRDLTDA QFSAYLAEGR KPVVRLRMPD EDISWDDLVR 

       190        200        210        220        230        240 
GTTTFAVGTV PDYVLTRASG DPLYTLVNPC DDALMKITHV LRGEDLLSST PRQVALYQAL 

       250        260        270        280        290        300 
IRIGMAERIP EFGHFPSVLG EGTKKLSKRE PQSNLFAHRD RGFIPEGLLN YLALLGWAIA 

       310        320        330        340        350        360 
DDHDLFSLDE MVAAFDVVDV NSNPARFDQK KADAVNAEHI RMLDSEDFAG RLRDYFTTHG 

       370        380        390        400        410        420 
YHIALDPANY EAGFVAAAQL VQTRIVVLGD AWDLLKFLND DEYSIDSKAA AKELDADAGP 

       430        440        450        460        470        480 
VLDVACAVLD SLVDWTTASI EDVLKVALIE GLGLKPRKVF GPIRVAATGA LVSPPLFESL 

       490        500 
ELLGRARSLQ RLSAARARVT SA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z99263 Genomic DNA. Translation: CAB16444.1.
AL583923 Genomic DNA. Translation: CAC30641.1.
PIRT45422.
RefSeqNP_302160.1. NC_002677.1.

3D structure databases

ProteinModelPortalO33120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML1688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC30641; CAC30641; CAC30641.
GeneID910058.
KEGGmle:ML1688.
PATRIC18056506. VBIMycLep78757_3182.

Organism-specific databases

LepromaML1688.
CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

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_MYCLE
AccessionPrimary (citable) accession number: O33120
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 91 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