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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
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 sitei254ATPUniRule 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:BB_0372
OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Taxonomic identifieri224326 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorreliella
Proteomesi
  • UP000001807 Componenti: Chromosome

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_00001195171 – 490Glutamate--tRNA ligaseAdd BLAST490

Proteomic databases

PRIDEiO51345.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi224326.BB_0372.

Structurei

Secondary structure

1490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi11 – 13Combined sources3
Helixi17 – 32Combined sources16
Beta strandi36 – 39Combined sources4
Helixi51 – 64Combined sources14
Beta strandi69 – 71Combined sources3
Turni72 – 74Combined sources3
Helixi83 – 85Combined sources3
Helixi87 – 99Combined sources13
Beta strandi102 – 106Combined sources5
Helixi110 – 122Combined sources13
Turni132 – 135Combined sources4
Helixi138 – 146Combined sources9
Beta strandi152 – 155Combined sources4
Beta strandi162 – 167Combined sources6
Turni168 – 170Combined sources3
Beta strandi171 – 176Combined sources6
Helixi177 – 179Combined sources3
Beta strandi185 – 187Combined sources3
Helixi195 – 205Combined sources11
Beta strandi209 – 214Combined sources6
Helixi215 – 220Combined sources6
Helixi221 – 231Combined sources11
Beta strandi237 – 241Combined sources5
Beta strandi249 – 251Combined sources3
Turni254 – 256Combined sources3
Helixi261 – 267Combined sources7
Helixi271 – 280Combined sources10
Beta strandi281 – 283Combined sources3
Beta strandi285 – 288Combined sources4
Helixi294 – 300Combined sources7
Helixi303 – 305Combined sources3
Helixi315 – 328Combined sources14
Helixi331 – 344Combined sources14
Helixi354 – 368Combined sources15
Helixi376 – 380Combined sources5
Helixi382 – 385Combined sources4
Helixi393 – 395Combined sources3
Beta strandi398 – 400Combined sources3
Helixi405 – 417Combined sources13
Helixi420 – 422Combined sources3
Helixi425 – 438Combined sources14
Helixi444 – 454Combined sources11
Beta strandi455 – 459Combined sources5
Helixi463 – 470Combined sources8
Helixi472 – 486Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GRIX-ray2.60A/B2-490[»]
ProteinModelPortaliO51345.
SMRiO51345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi9 – 19"HIGH" regionAdd BLAST11
Motifi251 – 255"KMSKS" region5

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C20. Bacteria.
COG0008. LUCA.
KOiK01885.
OMAiQLCYMPL.

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.
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.

Sequencei

Sequence statusi: Complete.

O51345-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTRVRYAPS PTGLQHIGGI RTALFNYFFA KSCGGKFLLR IEDTDQSRYS
60 70 80 90 100
PEAENDLYSS LKWLGISFDE GPVVGGDYAP YVQSQRSAIY KQYAKYLIES
110 120 130 140 150
GHAYYCYCSP ERLERIKKIQ NINKMPPGYD RHCRNLSNEE VENALIKKIK
160 170 180 190 200
PVVRFKIPLE GDTSFDDILL GRITWANKDI SPDPVILKSD GLPTYHLANV
210 220 230 240 250
VDDYLMKITH VLRAQEWVSS GPLHVLLYKA FKWKPPIYCH LPMVMGNDGQ
260 270 280 290 300
KLSKRHGSTA LRQFIEDGYL PEAIINYVTL LGWSYDDKRE FFSKNDLEQF
310 320 330 340 350
FSIEKINKSP AIFDYHKLDF FNSYYIREKK DEDLFNLLLP FFQKKGYVSK
360 370 380 390 400
PSTLEENQKL KLLIPLIKSR IKKLSDALNM TKFFYEDIKS WNLDEFLSRK
410 420 430 440 450
KTAKEVCSIL ELIKPILEGF EKRSSEENDK IFYDFAESNG FKLGEILLPI
460 470 480 490
RIAALGSKVS PPLFDSLKLI GKSKVFERIK LAQEFLRINE
Length:490
Mass (Da):56,752
Last modified:June 1, 1998 - v1
Checksum:iE7ED6AD2474934F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000783 Genomic DNA. Translation: AAC66742.1.
PIRiC70146.
RefSeqiNP_212506.1. NC_001318.1.
WP_002665196.1. NC_001318.1.

Genome annotation databases

EnsemblBacteriaiAAC66742; AAC66742; BB_0372.
GeneIDi1195209.
KEGGibbu:BB_0372.
PATRICi20557354. VBIBorBur75917_0767.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000783 Genomic DNA. Translation: AAC66742.1.
PIRiC70146.
RefSeqiNP_212506.1. NC_001318.1.
WP_002665196.1. NC_001318.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GRIX-ray2.60A/B2-490[»]
ProteinModelPortaliO51345.
SMRiO51345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224326.BB_0372.

Proteomic databases

PRIDEiO51345.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC66742; AAC66742; BB_0372.
GeneIDi1195209.
KEGGibbu:BB_0372.
PATRICi20557354. VBIBorBur75917_0767.

Phylogenomic databases

eggNOGiENOG4105C20. Bacteria.
COG0008. LUCA.
KOiK01885.
OMAiQLCYMPL.

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.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiSYE_BORBU
AccessioniPrimary (citable) accession number: O51345
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 109 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, Reference 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.