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

Q4AAJ3 (SYE_MYCHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:MHJ_0137
OrganismMycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110) [Complete proteome] [HAMAP]
Taxonomic identifier262719 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length467 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 – 467467Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237373

Regions

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

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4AAJ3 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: E85F512E16BAD9D2

FASTA46755,311
        10         20         30         40         50         60 
MKIRTRYAPS PTGFLHIGGA RTALFNYLFA KHHNGDFILR IEDSDNSRNI KDGEKSQIEN 

        70         80         90        100        110        120 
LLWLGIIPDE KPGSETKFGP YRQSEKLERY QKLAQELIKK GFAYYAFDNQ EELKLQKKEQ 

       130        140        150        160        170        180 
IAKGIFSFRY DQNWLKISDQ EKQKRLKNKH FVIRFKVDKA KNFCWNDLVR GQICFEGSAI 

       190        200        210        220        230        240 
SDWVIIKSDG FPTYNFAVVV DDFDMEISHI FRGEEHISNT PKQIGIYQAF NWKTPKFGHL 

       250        260        270        280        290        300 
TIITDKNGKK LSKRDKNLFQ FIEDYKNQGY HSEAFFNFLA LLGWTSPDSQ EFFDHKSLIK 

       310        320        330        340        350        360 
AFDYKRLSKA PSHFDIEKLN WFSKSYISKM PVDKILENLE LSDNQIWNRF FVETFQKSSI 

       370        380        390        400        410        420 
KYADFYKNFE FFHRPKQEMD EKMLEIFEKL DKKPVKIFAS KIDYQNWDYT KINDLIKEIG 

       430        440        450        460 
QKLEITGKNL LLPIRLATTF TNSGPELARA IWLLGKKIIE KRLLKWK 

« Hide

References

[1]"Swine and poultry pathogens: the complete genome sequences of two strains of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae."
Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R., Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M., Brocchi M., Burity H.A., Camargo A.A., Camargo S.S. expand/collapse author list , Carepo M.S., Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P., Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S., Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B., Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A., Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B., Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L., Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R., Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N., Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C., Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P., Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.
J. Bacteriol. 187:5568-5577(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J / ATCC 25934 / NCTC 10110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017243 Genomic DNA. Translation: AAZ44228.2.
RefSeqYP_278939.1. NC_007295.1.

3D structure databases

ProteinModelPortalQ4AAJ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262719.MHJ_0137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ44228; AAZ44228; MHJ_0137.
GeneID3563582.
KEGGmhj:MHJ_0137.
PATRIC20014024. VBIMycHyo90918_0148.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAWLPEEMG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMHYO262719:GJ59-151-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_MYCHJ
AccessionPrimary (citable) accession number: Q4AAJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 61 of the entry and version 2 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