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B5FGU2 (SYE_VIBFM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:VFMJ11_2020
OrganismVibrio fischeri (strain MJ11) [Complete proteome] [HAMAP]
Taxonomic identifier388396 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length474 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_1000090120

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022_B
Motif240 – 2445"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2431ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B5FGU2 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 66250A098E9D68E5

FASTA47453,263
        10         20         30         40         50         60 
MTVKTRFAPS PTGYLHVGGA RTALYSWLFA KNQGGEFVLR IEDTDLERNS QEAVDAIIEG 

        70         80         90        100        110        120 
MHWMGMEWDE GPYYQSKRFD RYNEVVDQLL AEDKAYKCYA SKELLDEIRA EQEANKEMAR 

       130        140        150        160        170        180 
YDANHPKIVA ANAAAKEGDA CVIRFRNPKE GSVVFDDQIR GRIEISNSQL DDLIIRRTDG 

       190        200        210        220        230        240 
APTYNFVVVV DDWDMGITQV IRGEDHINNT PRQINIYEAL GAPVPMFAHC AMILGDDGAK 

       250        260        270        280        290        300 
LSKRHGAVSV MQYRDEGYLP NALNNYLVRL GWSHGDQEIF SQEEMINLFS LSAVSKSASA 

       310        320        330        340        350        360 
FNTDKLLWLN NHYIKSSEPE YVAKYLQWHL DQKEISLDNG PAITEVIKLV GERCNTLIEL 

       370        380        390        400        410        420 
AEQSRYFYQD FEEFEAGAAK KHLRGVAKGP LELALAKVEA LEEWTTENLH NVIEEVCAEL 

       430        440        450        460        470 
EIGMGKIGMP LRVAVTGGGQ SPSVDAVMQL VGKERVVARI KMALAFIAER EANA 

« Hide

References

[1]"Complete sequence of Vibrio fischeri strain MJ11."
Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MJ11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001139 Genomic DNA. Translation: ACH66047.1.
RefSeqYP_002156714.1. NC_011184.1.

3D structure databases

ProteinModelPortalB5FGU2.
ModBaseSearch...

Protein-protein interaction databases

STRINGB5FGU2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6806693.
GenomeReviewsGene locus VFMJ11_2020 in contig CP001139_GR.
KEGGvfm:VFMJ11_2020.
PATRIC20122504. VBIVibFis37164_1942.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAWENVRVR.
ProtClustDBPRK01406.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_VIBFM
AccessionPrimary (citable) accession number: B5FGU2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: January 25, 2012
This is version 27 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

SIMILARITY comments

Index of protein domains and families