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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Mycoplasma synoviae (strain 53)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei255 – 2551ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. tRNA binding Source: InterPro

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMSYN262723:GH37-109-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:MS53_0100
OrganismiMycoplasma synoviae (strain 53)
Taxonomic identifieri262723 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000000549: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Glutamate--tRNA ligasePRO_0000237374Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi262723.MS53_0100.

Structurei

3D structure databases

ProteinModelPortaliQ4A6V0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi10 – 2011"HIGH" regionAdd
BLAST
Motifi252 – 2565"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OMAiKLNWINS.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4A6V0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKIRTRYAP SPTGFLHIGG ARTALFCYLF AKHFNGDFIF RLEDTDVKRN
60 70 80 90 100
VEGGEASQLE NLAWLGIIPD ESPLKPNLKY GKYRQSEKLD RYKEVLDMLL
110 120 130 140 150
EKNLAYKAYD LPEELEAQKL ESEQKGFASF RYDPSWLKIS DEEKAKRDLN
160 170 180 190 200
NQFSYRIRMP KDKVFSWNDL VRGEISFSSN EISDWVIFKS DNYPTYNFAV
210 220 230 240 250
VVDDHDMQIS HVLRGEEHIG NTPKQLALYD YLNWSSPQYG HLTIITDMGG
260 270 280 290 300
KKLSKRDLSL KQFIEDYKNE GYIPHAIFNF LALLGWTSED AKEVMSKKEL
310 320 330 340 350
ISKFNPARLS KSPSKFDVNK MSWFSKIYMK NQSNEEVQSH LDFKDFNSNS
360 370 380 390 400
SWKEIFTSTF KESATTYLEL QKALNNYLNP MSSELVLNEE ELKVVKEFKA
410 420 430 440 450
NLKSFTVEEI QAAINLTASN LKLKGKALFM PIRKACTYLE HGPELAKAIY
460
LFGEKLITER LAKYEN
Length:466
Mass (Da):54,074
Last modified:September 13, 2005 - v1
Checksum:i2F1617956A8AC999
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017245 Genomic DNA. Translation: AAZ43521.1.
RefSeqiYP_278232.1. NC_007294.1.

Genome annotation databases

EnsemblBacteriaiAAZ43521; AAZ43521; MS53_0100.
GeneIDi3564379.
KEGGimsy:MS53_0100.
PATRICi20024753. VBIMycSyn118523_0106.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017245 Genomic DNA. Translation: AAZ43521.1.
RefSeqiYP_278232.1. NC_007294.1.

3D structure databases

ProteinModelPortaliQ4A6V0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262723.MS53_0100.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ43521; AAZ43521; MS53_0100.
GeneIDi3564379.
KEGGimsy:MS53_0100.
PATRICi20024753. VBIMycSyn118523_0106.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK01885.
OMAiKLNWINS.
OrthoDBiEOG6DRPF7.

Enzyme and pathway databases

BioCyciMSYN262723:GH37-109-MONOMER.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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: 53.

Entry informationi

Entry nameiSYE_MYCS5
AccessioniPrimary (citable) accession number: Q4A6V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: September 13, 2005
Last modified: March 4, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.