Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q4AAJ3 (SYE_MYCHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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
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 lineageBacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

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 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 – 467467Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000237373

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022_B
Motif250 – 2545"KMSKS" region HAMAP MF_00022_B

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: 16077101] [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...

Protein-protein interaction databases

STRINGQ4AAJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3563582.
GenomeReviewsGene locus MHJ_0137 in contig AE017243_GR.
KEGGmhj:MHJ_0137.
PATRIC20014024. VBIMycHyo90918_0148.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADDFDMEI.
PhylomeDBQ4AAJ3.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycMHYO262719:MHJ_0137-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_MYCHJ
AccessionPrimary (citable) accession number: Q4AAJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 48 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents