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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
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 sitei257 – 2571ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciCEFF196164:GJW8-1409-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:CE1389
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493Glutamate--tRNA ligasePRO_0000119548Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi196164.HMPREF0290_0760.

Structurei

3D structure databases

ProteinModelPortaliQ8FPU9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi10 – 2011"HIGH" regionAdd
BLAST
Motifi254 – 2585"KMSKS" region

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000252720.
KOiK01885.
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.
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.

Sequencei

Sequence statusi: Complete.

Q8FPU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDVRVRFCP SPTGTPHVGL VRTALFNWAY ARHTGGKLIF RIEDTDAARD
60 70 80 90 100
SEESYAALLD AMNWLGLNWD EGVEVGGPHE PYRQSQRSDI YQDVLKKLID
110 120 130 140 150
AGEVYPAYST AEEVEERHRA AGRDPKLGYD NYDRTLTEDE ITAFEAEGRK
160 170 180 190 200
PVWRLRMPEQ DWKWNDLVRG EVEFKSFTQP DFVVARSNGQ PLYTLVNPVD
210 220 230 240 250
DALMEITHVL RGEDLLPSTP RQIALYEALK RIGVAKQTPV FGHLPFVMGE
260 270 280 290 300
GNKKLSKRDP QSDLFQHRTN GIIPEGMLNY LGLLGWSLSA DQDIFTVEEF
310 320 330 340 350
VANFDIADVL GNPARFDQKK LEAINADHIR LLPAGEFEER LRAHLSEFTD
360 370 380 390 400
FPEDYPAEKF SFAAELVQTR IKTLAEGYDL LKFLVTADED LVLDEKAAKK
410 420 430 440 450
NLKEAAIEPL DAGINALEAV AEWTTPNIEA ALTRALIEEL GLKPRVAYGA
460 470 480 490
LRVAISGAAV SPPLFESMEL LGRESTLTRL RAARAATPYQ AAE
Length:493
Mass (Da):55,275
Last modified:April 30, 2003 - v2
Checksum:i760271536159CB99
GO

Sequence cautioni

The sequence BAC18199.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18199.1. Different initiation.
RefSeqiWP_035109516.1. NZ_GG700686.1.

Genome annotation databases

EnsemblBacteriaiBAC18199; BAC18199; BAC18199.
KEGGicef:CE1389.
PATRICi21488910. VBICorEff9312_1388.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC18199.1. Different initiation.
RefSeqiWP_035109516.1. NZ_GG700686.1.

3D structure databases

ProteinModelPortaliQ8FPU9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.HMPREF0290_0760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC18199; BAC18199; BAC18199.
KEGGicef:CE1389.
PATRICi21488910. VBICorEff9312_1388.

Phylogenomic databases

HOGENOMiHOG000252720.
KOiK01885.
OrthoDBiEOG6DRPF7.

Enzyme and pathway databases

BioCyciCEFF196164:GJW8-1409-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.
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.
ProtoNetiSearch...

Publicationsi

  1. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiSYE_COREF
AccessioniPrimary (citable) accession number: Q8FPU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: April 30, 2003
Last modified: July 22, 2015
This is version 83 of the entry and version 2 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.