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

Q6MEN1 (SYE_PARUW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:pc0244
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia

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

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 – 502502Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119618

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1061Zinc By similarity
Metal binding1081Zinc By similarity
Metal binding1331Zinc By similarity
Metal binding1351Zinc By similarity
Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MEN1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 1903CD607A03A1A2

FASTA50258,420
        10         20         30         40         50         60 
MSVRVRIAPS PTGDPHVGTA YMALFNMIFA RHYNGTFILR IEDTDRARSR PEYEENIYSA 

        70         80         90        100        110        120 
LKWANIQWDE GPDIGGAYGP YRQSERFDIY KQYAEELLSK GKAYKCFCTA AELDEMRELS 

       130        140        150        160        170        180 
AKQGGRQGYD RRCRHLTPDE IIEREQAELS YVIRLKVPLN GECVYEDAIK KRMTFPWADI 

       190        200        210        220        230        240 
DDQVLLKSDG FPTYHLANVV DDYLMKISHV IRGDEWMSST PKHILLYESF GWTPPTFLHM 

       250        260        270        280        290        300 
PLLLGKDGKK LSKRKNPTSI FFYRDSGYLS EAFINFLTLM GYSMTGDQEI YSLDDIIREF 

       310        320        330        340        350        360 
DYKRIGVSGA IFDVQKLDWV NQQYLIKNIP VEQLWDRIKE WSFNDEFMQR LMPLCHSRIK 

       370        380        390        400        410        420 
TFGDFMDLFN FLFINHLHYN DAIFVVKDLS KEQICYLIQS LIWRLDELEN WNGTGVNQAS 

       430        440        450        460        470        480 
REIAEIFGVN HKKIVMPILF ASLMSKTQGP PLFDSVNLLG KDRTRARLLK AMEYLGGISN 

       490        500 
KKMASLKKAW QEKSGQPLMI KD 

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UWE25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX908798 Genomic DNA. Translation: CAF22968.1.
RefSeqYP_007243.1. NC_005861.1.

3D structure databases

ProteinModelPortalQ6MEN1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264201.pc0244.

Proteomic databases

PRIDEQ6MEN1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF22968; CAF22968; pc0244.
GeneID2781428.
KEGGpcu:pc0244.
PATRIC31995772. VBICanPro72727_0246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPAMO264201:GH0M-248-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_PARUW
AccessionPrimary (citable) accession number: Q6MEN1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 68 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