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Q03U68 (SYE1_LACBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:LVIS_0080
OrganismLactobacillus brevis (strain ATCC 367 / JCM 1170) [Complete proteome] [HAMAP]
Taxonomic identifier387344 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

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 termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367695

Regions

Motif17 – 2711"HIGH" region HAMAP-Rule MF_00022
Motif261 – 2655"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2641ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03U68 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: F4FED28A21F61247

FASTA50357,736
        10         20         30         40         50         60 
MSENSTVKKN VRVRYAPSPT GFLHIGNAQS ALFNYLFARH YHGTMVLRIE DTDVKRNVPH 

        70         80         90        100        110        120 
GEDSQIDNLH WLGIDWDEGP DKPNPKYAPY HQTERQDLYH RYITQLLDQG LAYKDYATED 

       130        140        150        160        170        180 
ELTTMRDQQR AAGEAPHYDG RWYGRSVADQ QAAEARGLKP SIRLHLPANH EYAWDDIIKG 

       190        200        210        220        230        240 
HVAFNSDNMG GDFIIEKSNG MPTYNFAVVI DDYLMDITDV LRGDDHIANT PKQIAVYEAL 

       250        260        270        280        290        300 
GLKHPNFGHI TLIYNPKTRK KLSKRDKETL QFISQYKNQG YLSEAIFNFI AFLGWSPEGE 

       310        320        330        340        350        360 
DELFSREELI ERYDPARMSK SPAYFDQSKL DWINAAYIKR LDLDDMTDRV LELVDEGQTD 

       370        380        390        400        410        420 
VARQVKALQL PDLRTLTSQV CKIYQTEIHQ LSEIMDKVLF YVTILQEPLD YDQLRQFDRT 

       430        440        450        460        470        480 
ATLAVLTAFR KHVQALPVDV ATPDFKKMIQ TVSQETGVTG RNLYFPLNVA FTGDHSAPQI 

       490        500 
DEVLRLFANS TIIELLTKAI AHV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000416 Genomic DNA. Translation: ABJ63254.1.
RefSeqYP_794285.1. NC_008497.1.

3D structure databases

ProteinModelPortalQ03U68.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387344.LVIS_0080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ63254; ABJ63254; LVIS_0080.
GeneID4412658.
KEGGlbr:LVIS_0080.
PATRIC22199128. VBILacBre134470_0079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAPANHEYA.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycLBRE387344:GJ8S-80-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.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_LACBA
AccessionPrimary (citable) accession number: Q03U68
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries