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B2GAB3 (SYE_LACF3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:LAF_0259
OrganismLactobacillus fermentum (strain NBRC 3956 / LMG 18251) [Complete proteome] [HAMAP]
Taxonomic identifier334390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length498 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 – 498498Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090083

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2GAB3 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 207FF7F3D3E922A3

FASTA49857,508
        10         20         30         40         50         60 
MSKNEIRVRY APSPTGHLHI GNARTALFNY LFARHNHGKF IIRIEDTDTK RNIADGERSQ 

        70         80         90        100        110        120 
LDNLKWMGLD WDEGPDKGGD FGPYRQSERK DIYAQYIQEL MDKGLAYKSY MTEEELEAQR 

       130        140        150        160        170        180 
EAQKAAHQMP HYEYEYAGMS DDQIKAAQEA AEEKGLKPVI RFRVPKDEVF EWEDLVKGPM 

       190        200        210        220        230        240 
SFEAQSIGGD FVIQKRDGMP TYNFAVVIDD HLMKISHVFR GDDHVSNTPK QMAIYQALGW 

       250        260        270        280        290        300 
KVPEFGHMSL IINNETGKKL SKRDESVLQF IEQYRDLGYL PEAMDNFIIL LGWSPVGEDE 

       310        320        330        340        350        360 
IFSLKEFVKM YDEKRLSKSP AAFDRKKLQW INNQYMKLSS ADEVFHVAMP QLLDAGLIEK 

       370        380        390        400        410        420 
NANPYKMEWM RRLVELFKRE ISYAREIVDY VKPFVNGPED ISEEAKAEMQ EDTALVVIKA 

       430        440        450        460        470        480 
FRDRVAAMDF MDATGVLAAI KDVQKSTKVK GRKLWMPLRI AVTHETHGPE LPESIELFGQ 

       490 
EKTLAHLDEM IAQLEENK 

« Hide

References

[1]"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 3956 / LMG 18251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008937 Genomic DNA. Translation: BAG26595.1.
RefSeqYP_001843075.1. NC_010610.1.

3D structure databases

ProteinModelPortalB2GAB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334390.LAF_0259.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG26595; BAG26595; LAF_0259.
GeneID6233363.
KEGGlfe:LAF_0259.
PATRIC22224554. VBILacFer15497_0290.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAKHYDGDF.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycLFER334390:GJ2S-279-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 nameSYE_LACF3
AccessionPrimary (citable) accession number: B2GAB3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 42 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