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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Binding sitei246ATPUniRule annotation1

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

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:BTH_I1984
OrganismiBurkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Taxonomic identifieri271848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000001930 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002373491 – 469Glutamate--tRNA ligaseAdd BLAST469

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 9Combined sources4
Helixi19 – 34Combined sources16
Beta strandi38 – 43Combined sources6
Helixi48 – 50Combined sources3
Helixi53 – 65Combined sources13
Beta strandi71 – 76Combined sources6
Helixi77 – 79Combined sources3
Helixi81 – 93Combined sources13
Beta strandi96 – 100Combined sources5
Beta strandi145 – 148Combined sources4
Beta strandi153 – 160Combined sources8
Turni161 – 163Combined sources3
Beta strandi164 – 169Combined sources6
Helixi170 – 172Combined sources3
Beta strandi177 – 179Combined sources3
Helixi187 – 197Combined sources11
Beta strandi202 – 206Combined sources5
Helixi207 – 212Combined sources6
Helixi213 – 222Combined sources10
Beta strandi229 – 233Combined sources5
Beta strandi241 – 243Combined sources3
Turni246 – 249Combined sources4
Helixi253 – 258Combined sources6
Helixi263 – 271Combined sources9
Beta strandi273 – 275Combined sources3
Helixi285 – 291Combined sources7
Helixi294 – 296Combined sources3
Helixi306 – 319Combined sources14
Helixi322 – 334Combined sources13
Turni335 – 337Combined sources3
Helixi340 – 345Combined sources6
Helixi349 – 356Combined sources8
Helixi363 – 370Combined sources8
Helixi371 – 373Combined sources3
Helixi448 – 454Combined sources7
Helixi457 – 465Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G6ZX-ray2.05A1-469[»]
ProteinModelPortaliQ2SX36.
SMRiQ2SX36.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi11 – 21"HIGH" regionAdd BLAST11
Motifi243 – 247"KMSKS" region5

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000252722.
KOiK01885.
OMAiLKTVEWT.
OrthoDBiPOG091H021W.

Family and domain databases

CDDicd00808. GluRS_core. 1 hit.
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. 1 hit.
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.
IPR033910. GluRS_core.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
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.

Q2SX36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRPVRTRFA PSPTGFIHLG NIRSALYPWA FARKMKGTFV LRIEDTDVER
60 70 80 90 100
SSQEAVDAIL EGMAWLGLDY DEGPYYQMQR MDRYREVLAQ MQEKGLVYPC
110 120 130 140 150
YMSTEELDAL RERQRAAGEK PRYDGTWRPE PGKVLPEPPA GVAPVLRFRN
160 170 180 190 200
PLTGTVAWDD AVKGRVEISN EELDDLVVAR PDGTPMYNFC VVVDDLDMGI
210 220 230 240 250
THVIRGDDHV NNTPRQINIL RALGGEVPVY AHLPTVLNEQ GEKMSKRHGA
260 270 280 290 300
MSVMGYRDAG YLPEAVLNYL ARLGWSHGDA EIFTREQFVE WFDLEHLGKS
310 320 330 340 350
PAQYDHNKLN WLNNHYIKEA DDARLAGLAK PFFAALGIDA GAIEQGPDLV
360 370 380 390 400
SVMGLMKDRA STVKEIAENS AMFYRAPAPG ADALAQHVTD AVRPALVEFA
410 420 430 440 450
AALKTVEWTK EAIAAALKAV LGAHKLKMPQ LAMPVRLLVA GTTHTPSIDA
460
VLLLFGRDVV VSRIEAALA
Length:469
Mass (Da):52,046
Last modified:January 24, 2006 - v1
Checksum:iEEE0D68248D730E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000086 Genomic DNA. Translation: ABC37833.1.
RefSeqiWP_009890362.1. NZ_CM000438.1.

Genome annotation databases

EnsemblBacteriaiABC37833; ABC37833; BTH_I1984.
KEGGibte:BTH_I1984.
PATRICi19307002. VBIBurTha36512_4795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000086 Genomic DNA. Translation: ABC37833.1.
RefSeqiWP_009890362.1. NZ_CM000438.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G6ZX-ray2.05A1-469[»]
ProteinModelPortaliQ2SX36.
SMRiQ2SX36.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC37833; ABC37833; BTH_I1984.
KEGGibte:BTH_I1984.
PATRICi19307002. VBIBurTha36512_4795.

Phylogenomic databases

HOGENOMiHOG000252722.
KOiK01885.
OMAiLKTVEWT.
OrthoDBiPOG091H021W.

Family and domain databases

CDDicd00808. GluRS_core. 1 hit.
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. 1 hit.
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.
IPR033910. GluRS_core.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
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...

Entry informationi

Entry nameiSYE_BURTA
AccessioniPrimary (citable) accession number: Q2SX36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 73 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

3D-structure, Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.