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P53662 (SYE_MYCPU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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
Ordered Locus Names:MYPU_6820
OrganismMycoplasma pulmonis (strain UAB CTIP) [Complete proteome] [HAMAP]
Taxonomic identifier272635 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length468 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 – 468468Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119609

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P53662 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 73026ACA2ED2941B

FASTA46855,066
        10         20         30         40         50         60 
MKKLRTRYAP SPTGYLHIGG ARTALFNYLL AKHYNGDFII RIEDTDVKRN IADGEASQIE 

        70         80         90        100        110        120 
NLKWLNIEAN ESPLKPNEKY GPYRQSQKLE KYLKIAHELI EKGYAYKAYD NSEELEEQKK 

       130        140        150        160        170        180 
HSEKLGVASF RYQRDFLKIS EEEKQKRDAS GAYSIRVICP KNTTYQWDDL VRGNIAVNSN 

       190        200        210        220        230        240 
DIGDWIIIKS DDYPTYNFAV VIDDIDMEIS HILRGEEHIT NTPKQMMIYD YLNAPKPLFG 

       250        260        270        280        290        300 
HLTIITNMEG KKLSKRDLSL KQFIHEYKEE GYNSQAIFNF LTLLGWTDEK ARELMDHDEI 

       310        320        330        340        350        360 
IKSFLYTRLS KSPSKFDITK MQWFSKQYWK NTPNEELIKI LNLNDYDNDW INLFLDLYKE 

       370        380        390        400        410        420 
NIYSLNQLKN YLKIYKQANL NQEKDLDLND AEKNVVKSFS SYIDYSNFSV NQIQEAINKT 

       430        440        450        460 
QEKLSIKGKN LFLPIRKATT FQEHGPELAK AIYLFGSEII EKRMKKWK 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of a restriction and modification system via DNA inversion in Mycoplasma pulmonis."
Dybvig K., Yu H.
Mol. Microbiol. 12:547-560(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: KD735-16.
[2]"The complete genome sequence of the murine respiratory pathogen Mycoplasma pulmonis."
Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F., Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.
Nucleic Acids Res. 29:2145-2153(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UAB CTIP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25415 Genomic DNA. Translation: AAA65629.1.
AL445565 Genomic DNA. Translation: CAC13855.1.
PIRS49391.
RefSeqNP_326513.1. NC_002771.1.

3D structure databases

ProteinModelPortalP53662.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272635.MYPU_6820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC13855; CAC13855; CAC13855.
GeneID911061.
KEGGmpu:MYPU_6820.
PATRIC20024318. VBIMycPul29704_0695.

Organism-specific databases

GenoListMYPU_6820.
CMRSearch...

Phylogenomic databases

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

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_MYCPU
AccessionPrimary (citable) accession number: P53662
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 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