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Q8EU94 (SYE_MYCPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. 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:MYPE10370
OrganismMycoplasma penetrans (strain HF-2) [Complete proteome] [HAMAP]
Taxonomic identifier272633 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length487 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119607

Regions

Motif13 – 2311"HIGH" region HAMAP MF_00022_B
Motif255 – 2595"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2581ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8EU94 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 90742E0CB5157E46

FASTA48755,636
        10         20         30         40         50         60 
MNKNKIIRTR YAPSPTGLFH IGGARTALFN YLFAKKNNGD FIVRIEDTDI DRNVENGIES 

        70         80         90        100        110        120 
QLLNLKWLKI FPDESPLNPG NYGPYIQTER LPIYKEKAEQ LLKEKKAYRC FCTPEQLEKN 

       130        140        150        160        170        180 
RKKALKDGKT PKYNRTCLSL SEDQISEKIK NNIPFSLRFK ITDNTEIKWN DIVRGEMCVP 

       190        200        210        220        230        240 
TSALTDPVIL KSNGIPTYNF AVVIDDNDML ISHIIRGEEH LSNTPYQIAI NEALDINKNI 

       250        260        270        280        290        300 
VFGHLSVIID ETGKKLSKRN MELKQFIEDY KNMGFSPEAI VNFMYLLGLS SSDNKEIFSL 

       310        320        330        340        350        360 
AEAVKNFDIK KVSKSPTTFD FKKMEWISSE HFKMMSDSAF ISFAKPFITI DLGFLKGNEN 

       370        380        390        400        410        420 
DVILLFKNQI AYAKQINDLI DETFFSPETF AAVCEKFPFL KQADTKELIK VFIKQLQELP 

       430        440        450        460        470        480 
NWNISEIATV IDAVKKQTGK SGKELFMPIR VYSSHNSHGP ELAKVIFILG KDKVIKNAKS 


FLDNKGA 

« Hide

References

[1]"The complete genomic sequence of Mycoplasma penetrans, an intracellular bacterial pathogen in humans."
Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K., Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.
Nucleic Acids Res. 30:5293-5300(2002) [PubMed: 12466555] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HF-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000026 Genomic DNA. Translation: BAC44822.1.
RefSeqNP_758418.1. NC_004432.1.

3D structure databases

ProteinModelPortalQ8EU94.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1041059.
GenomeReviewsGene locus MYPE10370 in contig BA000026_GR.
KEGGmpe:MYPE10370.
NMPDRfig|272633.1.peg.1032.
PATRIC20021262. VBIMycPen56664_1061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMASVKWLLN.
PhylomeDBQ8EU94.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycMPEN272633:MYPE10370-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_MYCPE
AccessionPrimary (citable) accession number: Q8EU94
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families