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Q6F0G6 (SYE_MESFL) 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:Mfl651
OrganismMesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1) (Acholeplasma florum) [Reference proteome] [HAMAP]
Taxonomic identifier265311 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesEntomoplasmatalesEntomoplasmataceaeMesoplasma

Protein attributes

Sequence length482 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
Reference 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 – 482482Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119596

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6F0G6 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: E70EC7D196D1EF46

FASTA48255,805
        10         20         30         40         50         60 
MTKFRLRYAP SPTGFLHIGN TRTALMNYLF AKHYNGDFIV RIEDTDLERN VEGAIESQFE 

        70         80         90        100        110        120 
NLNWLGINAD ESFLKPGEEK YGKYMQSQKF GRYQELAEKL ISIKKAYRCF CTTEELEKDY 

       130        140        150        160        170        180 
EDQVAKGIVA TKYSGKCSRL SESEIESNLK SNKDFSIRFL VPETTLNIKD FIKGEITFDS 

       190        200        210        220        230        240 
KELGDFVILK TNKIATYNFA VVVDDFDMEI SHVLRGEEHI SNTPRQILIY QAFGWETPQF 

       250        260        270        280        290        300 
GHMSLIVDST GKKLSKRSGN ALFFIEQYKN QGYLPEAMFN YISLLGWSPI GEKELLTKQE 

       310        320        330        340        350        360 
LISMFDDKRF SKSPSTFDMT KMKWINSQYM KALSEEEYLE FTKKYINTEM FNTKEKSEDW 

       370        380        390        400        410        420 
LNQVLLLFKK ELEFADQINN HLNIFFNEVD VTSETIEILK TIEEHESVIK EFETQISTLN 

       430        440        450        460        470        480 
EWEIENIKSL IKLVSENTGK KGKDLFMPIR IASSSSEHGP SLADVIYLLG KDKVLANIAK 


VK 

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References

[1]Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S., Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33453 / NBRC 100688 / NCTC 11704 / L1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017263 Genomic DNA. Translation: AAT76007.1.
RefSeqYP_053891.1. NC_006055.1.

3D structure databases

ProteinModelPortalQ6F0G6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265311.Mfl651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT76007; AAT76007; Mfl651.
GeneID2898181.
KEGGmfl:Mfl651.
PATRIC22474081. VBIMesFlo3168_0653.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycMFLO265311:GHIB-669-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_MESFL
AccessionPrimary (citable) accession number: Q6F0G6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: August 16, 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