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O51345 (SYE_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:BB_0372
OrganismBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) [Reference proteome] [HAMAP]
Taxonomic identifier224326 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group ›

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119517

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif251 – 2555"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2541ATP By similarity

Secondary structure

1 ................................................................................... 490
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O51345 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: E7ED6AD2474934F4

FASTA49056,752
        10         20         30         40         50         60 
MSTRVRYAPS PTGLQHIGGI RTALFNYFFA KSCGGKFLLR IEDTDQSRYS PEAENDLYSS 

        70         80         90        100        110        120 
LKWLGISFDE GPVVGGDYAP YVQSQRSAIY KQYAKYLIES GHAYYCYCSP ERLERIKKIQ 

       130        140        150        160        170        180 
NINKMPPGYD RHCRNLSNEE VENALIKKIK PVVRFKIPLE GDTSFDDILL GRITWANKDI 

       190        200        210        220        230        240 
SPDPVILKSD GLPTYHLANV VDDYLMKITH VLRAQEWVSS GPLHVLLYKA FKWKPPIYCH 

       250        260        270        280        290        300 
LPMVMGNDGQ KLSKRHGSTA LRQFIEDGYL PEAIINYVTL LGWSYDDKRE FFSKNDLEQF 

       310        320        330        340        350        360 
FSIEKINKSP AIFDYHKLDF FNSYYIREKK DEDLFNLLLP FFQKKGYVSK PSTLEENQKL 

       370        380        390        400        410        420 
KLLIPLIKSR IKKLSDALNM TKFFYEDIKS WNLDEFLSRK KTAKEVCSIL ELIKPILEGF 

       430        440        450        460        470        480 
EKRSSEENDK IFYDFAESNG FKLGEILLPI RIAALGSKVS PPLFDSLKLI GKSKVFERIK 

       490 
LAQEFLRINE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000783 Genomic DNA. Translation: AAC66742.1.
PIRC70146.
RefSeqNP_212506.1. NC_001318.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GRIX-ray2.60A/B2-490[»]
ProteinModelPortalO51345.
ModBaseSearch...

Protein-protein interaction databases

STRING224326.BB0372.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC66742; AAC66742; BB_0372.
GeneID1195209.
KEGGbbu:BB_0372.
PATRIC20557354. VBIBorBur75917_0767.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMARYRDFKG.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBBUR224326:BB_0372-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR004527. Glu-tRNA-ligase_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]
PANTHERPTHR10119. PTHR10119. 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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_BORBU
AccessionPrimary (citable) accession number: O51345
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 91 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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